CNRS Nantes University US2B US2B
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***  3vq1  ***

elNémo ID: 2403071644412055180

Job options:

ID        	=	 2403071644412055180
JOBID     	=	 3vq1
USERID    	=	 merhid
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3vq1

HEADER    IMMUNE SYSTEM                           17-MAR-12   3VQ1              
TITLE     CRYSTAL STRUCTURE OF MOUSE TLR4/MD-2/LIPID IVA COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOLL-LIKE RECEPTOR 4;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 22-627;                                       
COMPND   5 SYNONYM: TLR4;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: LYMPHOCYTE ANTIGEN 96;                                     
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 SYNONYM: LY-96, ESOP-1, PROTEIN MD-2;                                
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: TLR4;                                                          
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL: S2;                                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 GENE: MD2;                                                           
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL: S2                                           
KEYWDS    LEUCINE RICH REPEAT MD-2 RELATED LIPID RECOGNITION, RECEPTOR INNATE   
KEYWDS   2 IMMUNITY, LIPID BINDING, GLYCOSYLATION, SECRETED, IMMUNE SYSTEM      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.OHTO,T.SHIMIZU                                                      
REVDAT   4   08-NOV-23 3VQ1    1       REMARK HETSYN                            
REVDAT   3   29-JUL-20 3VQ1    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   17-JUL-13 3VQ1    1       JRNL                                     
REVDAT   1   09-MAY-12 3VQ1    0                                                
JRNL        AUTH   U.OHTO,K.FUKASE,K.MIYAKE,T.SHIMIZU                           
JRNL        TITL   STRUCTURAL BASIS OF SPECIES-SPECIFIC ENDOTOXIN SENSING BY    
JRNL        TITL 2 INNATE IMMUNE RECEPTOR TLR4/MD-2                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  7421 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22532668                                                     
JRNL        DOI    10.1073/PNAS.1201193109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 54275                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2877                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3678                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 200                          
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11682                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 298                                     
REMARK   3   SOLVENT ATOMS            : 37                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.76000                                             
REMARK   3    B22 (A**2) : -1.25000                                             
REMARK   3    B33 (A**2) : 3.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.947         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.364         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.268         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.394        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.880                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12396 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):    42 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16788 ; 1.424 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    72 ; 0.742 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1468 ; 6.306 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   554 ;38.677 ;24.982       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2096 ;19.569 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;22.476 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1949 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9099 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):     3 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A   625                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7453  18.1942  29.5376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0857 T22:   0.1255                                     
REMARK   3      T33:   0.1097 T12:  -0.0069                                     
REMARK   3      T13:   0.0031 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1650 L22:   0.2250                                     
REMARK   3      L33:   0.0154 L12:   0.1201                                     
REMARK   3      L13:   0.0366 L23:   0.0109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0273 S12:  -0.0440 S13:  -0.0171                       
REMARK   3      S21:   0.0132 S22:  -0.0222 S23:  -0.0006                       
REMARK   3      S31:  -0.0145 S32:  -0.0095 S33:  -0.0051                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    21        C   155                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2451  35.0950  20.3753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0690 T22:   0.1045                                     
REMARK   3      T33:   0.1431 T12:   0.0131                                     
REMARK   3      T13:   0.0138 T23:  -0.0584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5577 L22:   0.4034                                     
REMARK   3      L33:   0.2873 L12:   0.1973                                     
REMARK   3      L13:   0.2494 L23:   0.1127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0631 S12:  -0.0363 S13:   0.0566                       
REMARK   3      S21:   0.0080 S22:  -0.1623 S23:   0.0792                       
REMARK   3      S31:  -0.0268 S32:  -0.0104 S33:   0.0992                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    27        B   625                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2332  -4.4280 -13.5706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1107 T22:   0.1029                                     
REMARK   3      T33:   0.1211 T12:   0.0275                                     
REMARK   3      T13:  -0.0133 T23:   0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0811 L22:   0.1196                                     
REMARK   3      L33:   0.0904 L12:  -0.0341                                     
REMARK   3      L13:  -0.0651 L23:  -0.0125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0222 S12:  -0.0187 S13:  -0.0048                       
REMARK   3      S21:  -0.0898 S22:  -0.0292 S23:   0.0283                       
REMARK   3      S31:   0.0038 S32:  -0.0081 S33:   0.0070                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    21        D   155                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2528 -20.9925  -4.8714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1817 T22:   0.0319                                     
REMARK   3      T33:   0.1101 T12:   0.0059                                     
REMARK   3      T13:   0.0203 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4041 L22:   0.2083                                     
REMARK   3      L33:   0.7400 L12:  -0.1956                                     
REMARK   3      L13:   0.0984 L23:   0.0714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0614 S12:   0.0314 S13:  -0.0033                       
REMARK   3      S21:  -0.0141 S22:  -0.0775 S23:  -0.0326                       
REMARK   3      S31:   0.1727 S32:  -0.0275 S33:   0.0160                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3VQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000095357.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54275                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 116.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14700                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2Z64                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 0.2M NA ACETATE, 0.1M       
REMARK 280  TRIS-HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.58000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.92350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.25950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.92350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.58000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.25950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E, F, G                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     VAL A   610                                                      
REMARK 465     GLU A   611                                                      
REMARK 465     MET A   612                                                      
REMARK 465     TYR A   626                                                      
REMARK 465     MET A   627                                                      
REMARK 465     GLU C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     LYS C    20                                                      
REMARK 465     ARG C   156                                                      
REMARK 465     ARG C   157                                                      
REMARK 465     ASP C   158                                                      
REMARK 465     VAL C   159                                                      
REMARK 465     ASN C   160                                                      
REMARK 465     PRO B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     LEU B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     VAL B   610                                                      
REMARK 465     GLU B   611                                                      
REMARK 465     MET B   612                                                      
REMARK 465     TYR B   626                                                      
REMARK 465     MET B   627                                                      
REMARK 465     GLU D    17                                                      
REMARK 465     SER D    18                                                      
REMARK 465     GLU D    19                                                      
REMARK 465     LYS D    20                                                      
REMARK 465     ARG D   156                                                      
REMARK 465     ARG D   157                                                      
REMARK 465     ASP D   158                                                      
REMARK 465     VAL D   159                                                      
REMARK 465     ASN D   160                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     THR A  614   CB   OG1  CG2                                       
REMARK 480     THR B  614   CB   OG1  CG2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   204     O5   NAG E     1              1.47            
REMARK 500   ND2  ASN A   524     C2   NAG F     1              1.48            
REMARK 500   OD1  ASN A   524     C1   NAG F     1              1.49            
REMARK 500   CG   ASN A   524     C1   NAG F     1              1.58            
REMARK 500   O5   LP4 C   300     O6   LP5 C   301              1.90            
REMARK 500   O5   LP4 D   300     O6   LP5 D   301              1.94            
REMARK 500   NZ   LYS A   263     O46  LP4 C   300              2.04            
REMARK 500   ND2  ASN A   524     N2   NAG F     1              2.08            
REMARK 500   C2   LP4 D   300     O6   LP5 D   301              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  34       -3.16     68.80                                   
REMARK 500    ILE A  35      -52.02   -131.46                                   
REMARK 500    LYS A  43       41.74   -103.36                                   
REMARK 500    PRO A  52      122.75    -37.49                                   
REMARK 500    SER A  54      -11.44   -153.45                                   
REMARK 500    PRO A  64       71.65    -68.76                                   
REMARK 500    LYS A  66      -54.37     68.41                                   
REMARK 500    TYR A  71       -3.30     74.53                                   
REMARK 500    THR A 109      131.55    -35.93                                   
REMARK 500    ASN A 159     -158.84   -128.99                                   
REMARK 500    ASN A 184     -163.31   -122.68                                   
REMARK 500    ASN A 200       77.76   -113.71                                   
REMARK 500    PRO A 201        2.20    -69.08                                   
REMARK 500    PHE A 216      119.58   -162.56                                   
REMARK 500    GLU A 265       72.57   -165.20                                   
REMARK 500    ARG A 266      -97.48    -86.09                                   
REMARK 500    ASN A 267      -45.77     97.07                                   
REMARK 500    SER A 317        5.01    -67.76                                   
REMARK 500    GLU A 322      -17.92   -140.96                                   
REMARK 500    CYS A 338     -168.97   -104.87                                   
REMARK 500    LYS A 367      127.70    -31.19                                   
REMARK 500    SER A 413      -15.26   -143.47                                   
REMARK 500    GLU A 420        1.32    -68.82                                   
REMARK 500    GLN A 428      130.34    -36.74                                   
REMARK 500    ASN A 456       47.12     70.83                                   
REMARK 500    LEU A 468       52.69    -90.28                                   
REMARK 500    MET A 476       38.08   -141.01                                   
REMARK 500    ASN A 479     -140.53   -119.73                                   
REMARK 500    ASN A 484       26.68     46.77                                   
REMARK 500    ASN A 528     -165.24   -110.11                                   
REMARK 500    GLN A 540       -5.34     91.03                                   
REMARK 500    ASN A 552     -150.42   -101.60                                   
REMARK 500    ILE A 560      107.54     65.60                                   
REMARK 500    LEU A 568      101.77    -57.97                                   
REMARK 500    ASN A 576     -160.99   -106.61                                   
REMARK 500    CYS A 580       47.34    -93.54                                   
REMARK 500    GLN A 594       40.99    -88.32                                   
REMARK 500    THR A 608     -162.85   -121.61                                   
REMARK 500    SER A 615     -127.56   -109.96                                   
REMARK 500    LEU A 616      -56.59   -143.17                                   
REMARK 500    ASN A 622     -101.86   -133.12                                   
REMARK 500    THR A 624      -53.73     54.76                                   
REMARK 500    SER C  28       -9.95    -56.74                                   
REMARK 500    ASP C  29       14.47   -149.59                                   
REMARK 500    SER C  84       -8.26     67.75                                   
REMARK 500    LYS C 128       52.71     75.17                                   
REMARK 500    GLU C 143       18.67     58.99                                   
REMARK 500    CYS B  28     -144.07   -120.12                                   
REMARK 500    ASN B  34        5.09     59.30                                   
REMARK 500    ILE B  35      -54.96   -131.08                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A  323     VAL A  324                 -149.72                    
REMARK 500 THR A  608     PRO A  609                 -146.23                    
REMARK 500 THR B  608     PRO B  609                 -141.30                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  705                                                       
REMARK 610     LP4 C  300                                                       
REMARK 610     LP4 D  300                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VQ2   RELATED DB: PDB                                   
DBREF  3VQ1 A   22   627  UNP    Q9QUK6   TLR4_MOUSE      22    627             
DBREF  3VQ1 C   17   160  UNP    Q9JHF9   LY96_MOUSE      17    160             
DBREF  3VQ1 B   22   627  UNP    Q9QUK6   TLR4_MOUSE      22    627             
DBREF  3VQ1 D   17   160  UNP    Q9JHF9   LY96_MOUSE      17    160             
SEQRES   1 A  606  PRO GLY SER LEU ASN PRO CYS ILE GLU VAL VAL PRO ASN          
SEQRES   2 A  606  ILE THR TYR GLN CYS MET ASP GLN LYS LEU SER LYS VAL          
SEQRES   3 A  606  PRO ASP ASP ILE PRO SER SER THR LYS ASN ILE ASP LEU          
SEQRES   4 A  606  SER PHE ASN PRO LEU LYS ILE LEU LYS SER TYR SER PHE          
SEQRES   5 A  606  SER ASN PHE SER GLU LEU GLN TRP LEU ASP LEU SER ARG          
SEQRES   6 A  606  CYS GLU ILE GLU THR ILE GLU ASP LYS ALA TRP HIS GLY          
SEQRES   7 A  606  LEU HIS HIS LEU SER ASN LEU ILE LEU THR GLY ASN PRO          
SEQRES   8 A  606  ILE GLN SER PHE SER PRO GLY SER PHE SER GLY LEU THR          
SEQRES   9 A  606  SER LEU GLU ASN LEU VAL ALA VAL GLU THR LYS LEU ALA          
SEQRES  10 A  606  SER LEU GLU SER PHE PRO ILE GLY GLN LEU ILE THR LEU          
SEQRES  11 A  606  LYS LYS LEU ASN VAL ALA HIS ASN PHE ILE HIS SER CYS          
SEQRES  12 A  606  LYS LEU PRO ALA TYR PHE SER ASN LEU THR ASN LEU VAL          
SEQRES  13 A  606  HIS VAL ASP LEU SER TYR ASN TYR ILE GLN THR ILE THR          
SEQRES  14 A  606  VAL ASN ASP LEU GLN PHE LEU ARG GLU ASN PRO GLN VAL          
SEQRES  15 A  606  ASN LEU SER LEU ASP MET SER LEU ASN PRO ILE ASP PHE          
SEQRES  16 A  606  ILE GLN ASP GLN ALA PHE GLN GLY ILE LYS LEU HIS GLU          
SEQRES  17 A  606  LEU THR LEU ARG GLY ASN PHE ASN SER SER ASN ILE MET          
SEQRES  18 A  606  LYS THR CYS LEU GLN ASN LEU ALA GLY LEU HIS VAL HIS          
SEQRES  19 A  606  ARG LEU ILE LEU GLY GLU PHE LYS ASP GLU ARG ASN LEU          
SEQRES  20 A  606  GLU ILE PHE GLU PRO SER ILE MET GLU GLY LEU CYS ASP          
SEQRES  21 A  606  VAL THR ILE ASP GLU PHE ARG LEU THR TYR THR ASN ASP          
SEQRES  22 A  606  PHE SER ASP ASP ILE VAL LYS PHE HIS CYS LEU ALA ASN          
SEQRES  23 A  606  VAL SER ALA MET SER LEU ALA GLY VAL SER ILE LYS TYR          
SEQRES  24 A  606  LEU GLU ASP VAL PRO LYS HIS PHE LYS TRP GLN SER LEU          
SEQRES  25 A  606  SER ILE ILE ARG CYS GLN LEU LYS GLN PHE PRO THR LEU          
SEQRES  26 A  606  ASP LEU PRO PHE LEU LYS SER LEU THR LEU THR MET ASN          
SEQRES  27 A  606  LYS GLY SER ILE SER PHE LYS LYS VAL ALA LEU PRO SER          
SEQRES  28 A  606  LEU SER TYR LEU ASP LEU SER ARG ASN ALA LEU SER PHE          
SEQRES  29 A  606  SER GLY CYS CYS SER TYR SER ASP LEU GLY THR ASN SER          
SEQRES  30 A  606  LEU ARG HIS LEU ASP LEU SER PHE ASN GLY ALA ILE ILE          
SEQRES  31 A  606  MET SER ALA ASN PHE MET GLY LEU GLU GLU LEU GLN HIS          
SEQRES  32 A  606  LEU ASP PHE GLN HIS SER THR LEU LYS ARG VAL THR GLU          
SEQRES  33 A  606  PHE SER ALA PHE LEU SER LEU GLU LYS LEU LEU TYR LEU          
SEQRES  34 A  606  ASP ILE SER TYR THR ASN THR LYS ILE ASP PHE ASP GLY          
SEQRES  35 A  606  ILE PHE LEU GLY LEU THR SER LEU ASN THR LEU LYS MET          
SEQRES  36 A  606  ALA GLY ASN SER PHE LYS ASP ASN THR LEU SER ASN VAL          
SEQRES  37 A  606  PHE ALA ASN THR THR ASN LEU THR PHE LEU ASP LEU SER          
SEQRES  38 A  606  LYS CYS GLN LEU GLU GLN ILE SER TRP GLY VAL PHE ASP          
SEQRES  39 A  606  THR LEU HIS ARG LEU GLN LEU LEU ASN MET SER HIS ASN          
SEQRES  40 A  606  ASN LEU LEU PHE LEU ASP SER SER HIS TYR ASN GLN LEU          
SEQRES  41 A  606  TYR SER LEU SER THR LEU ASP CYS SER PHE ASN ARG ILE          
SEQRES  42 A  606  GLU THR SER LYS GLY ILE LEU GLN HIS PHE PRO LYS SER          
SEQRES  43 A  606  LEU ALA PHE PHE ASN LEU THR ASN ASN SER VAL ALA CYS          
SEQRES  44 A  606  ILE CYS GLU HIS GLN LYS PHE LEU GLN TRP VAL LYS GLU          
SEQRES  45 A  606  GLN LYS GLN PHE LEU VAL ASN VAL GLU GLN MET THR CYS          
SEQRES  46 A  606  ALA THR PRO VAL GLU MET ASN THR SER LEU VAL LEU ASP          
SEQRES  47 A  606  PHE ASN ASN SER THR CYS TYR MET                              
SEQRES   1 C  144  GLU SER GLU LYS GLN GLN TRP PHE CYS ASN SER SER ASP          
SEQRES   2 C  144  ALA ILE ILE SER TYR SER TYR CYS ASP HIS LEU LYS PHE          
SEQRES   3 C  144  PRO ILE SER ILE SER SER GLU PRO CYS ILE ARG LEU ARG          
SEQRES   4 C  144  GLY THR ASN GLY PHE VAL HIS VAL GLU PHE ILE PRO ARG          
SEQRES   5 C  144  GLY ASN LEU LYS TYR LEU TYR PHE ASN LEU PHE ILE SER          
SEQRES   6 C  144  VAL ASN SER ILE GLU LEU PRO LYS ARG LYS GLU VAL LEU          
SEQRES   7 C  144  CYS HIS GLY HIS ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 C  144  LEU LYS GLY GLU THR VAL ASN THR SER ILE PRO PHE SER          
SEQRES   9 C  144  PHE GLU GLY ILE LEU PHE PRO LYS GLY HIS TYR ARG CYS          
SEQRES  10 C  144  VAL ALA GLU ALA ILE ALA GLY ASP THR GLU GLU LYS LEU          
SEQRES  11 C  144  PHE CYS LEU ASN PHE THR ILE ILE HIS ARG ARG ASP VAL          
SEQRES  12 C  144  ASN                                                          
SEQRES   1 B  606  PRO GLY SER LEU ASN PRO CYS ILE GLU VAL VAL PRO ASN          
SEQRES   2 B  606  ILE THR TYR GLN CYS MET ASP GLN LYS LEU SER LYS VAL          
SEQRES   3 B  606  PRO ASP ASP ILE PRO SER SER THR LYS ASN ILE ASP LEU          
SEQRES   4 B  606  SER PHE ASN PRO LEU LYS ILE LEU LYS SER TYR SER PHE          
SEQRES   5 B  606  SER ASN PHE SER GLU LEU GLN TRP LEU ASP LEU SER ARG          
SEQRES   6 B  606  CYS GLU ILE GLU THR ILE GLU ASP LYS ALA TRP HIS GLY          
SEQRES   7 B  606  LEU HIS HIS LEU SER ASN LEU ILE LEU THR GLY ASN PRO          
SEQRES   8 B  606  ILE GLN SER PHE SER PRO GLY SER PHE SER GLY LEU THR          
SEQRES   9 B  606  SER LEU GLU ASN LEU VAL ALA VAL GLU THR LYS LEU ALA          
SEQRES  10 B  606  SER LEU GLU SER PHE PRO ILE GLY GLN LEU ILE THR LEU          
SEQRES  11 B  606  LYS LYS LEU ASN VAL ALA HIS ASN PHE ILE HIS SER CYS          
SEQRES  12 B  606  LYS LEU PRO ALA TYR PHE SER ASN LEU THR ASN LEU VAL          
SEQRES  13 B  606  HIS VAL ASP LEU SER TYR ASN TYR ILE GLN THR ILE THR          
SEQRES  14 B  606  VAL ASN ASP LEU GLN PHE LEU ARG GLU ASN PRO GLN VAL          
SEQRES  15 B  606  ASN LEU SER LEU ASP MET SER LEU ASN PRO ILE ASP PHE          
SEQRES  16 B  606  ILE GLN ASP GLN ALA PHE GLN GLY ILE LYS LEU HIS GLU          
SEQRES  17 B  606  LEU THR LEU ARG GLY ASN PHE ASN SER SER ASN ILE MET          
SEQRES  18 B  606  LYS THR CYS LEU GLN ASN LEU ALA GLY LEU HIS VAL HIS          
SEQRES  19 B  606  ARG LEU ILE LEU GLY GLU PHE LYS ASP GLU ARG ASN LEU          
SEQRES  20 B  606  GLU ILE PHE GLU PRO SER ILE MET GLU GLY LEU CYS ASP          
SEQRES  21 B  606  VAL THR ILE ASP GLU PHE ARG LEU THR TYR THR ASN ASP          
SEQRES  22 B  606  PHE SER ASP ASP ILE VAL LYS PHE HIS CYS LEU ALA ASN          
SEQRES  23 B  606  VAL SER ALA MET SER LEU ALA GLY VAL SER ILE LYS TYR          
SEQRES  24 B  606  LEU GLU ASP VAL PRO LYS HIS PHE LYS TRP GLN SER LEU          
SEQRES  25 B  606  SER ILE ILE ARG CYS GLN LEU LYS GLN PHE PRO THR LEU          
SEQRES  26 B  606  ASP LEU PRO PHE LEU LYS SER LEU THR LEU THR MET ASN          
SEQRES  27 B  606  LYS GLY SER ILE SER PHE LYS LYS VAL ALA LEU PRO SER          
SEQRES  28 B  606  LEU SER TYR LEU ASP LEU SER ARG ASN ALA LEU SER PHE          
SEQRES  29 B  606  SER GLY CYS CYS SER TYR SER ASP LEU GLY THR ASN SER          
SEQRES  30 B  606  LEU ARG HIS LEU ASP LEU SER PHE ASN GLY ALA ILE ILE          
SEQRES  31 B  606  MET SER ALA ASN PHE MET GLY LEU GLU GLU LEU GLN HIS          
SEQRES  32 B  606  LEU ASP PHE GLN HIS SER THR LEU LYS ARG VAL THR GLU          
SEQRES  33 B  606  PHE SER ALA PHE LEU SER LEU GLU LYS LEU LEU TYR LEU          
SEQRES  34 B  606  ASP ILE SER TYR THR ASN THR LYS ILE ASP PHE ASP GLY          
SEQRES  35 B  606  ILE PHE LEU GLY LEU THR SER LEU ASN THR LEU LYS MET          
SEQRES  36 B  606  ALA GLY ASN SER PHE LYS ASP ASN THR LEU SER ASN VAL          
SEQRES  37 B  606  PHE ALA ASN THR THR ASN LEU THR PHE LEU ASP LEU SER          
SEQRES  38 B  606  LYS CYS GLN LEU GLU GLN ILE SER TRP GLY VAL PHE ASP          
SEQRES  39 B  606  THR LEU HIS ARG LEU GLN LEU LEU ASN MET SER HIS ASN          
SEQRES  40 B  606  ASN LEU LEU PHE LEU ASP SER SER HIS TYR ASN GLN LEU          
SEQRES  41 B  606  TYR SER LEU SER THR LEU ASP CYS SER PHE ASN ARG ILE          
SEQRES  42 B  606  GLU THR SER LYS GLY ILE LEU GLN HIS PHE PRO LYS SER          
SEQRES  43 B  606  LEU ALA PHE PHE ASN LEU THR ASN ASN SER VAL ALA CYS          
SEQRES  44 B  606  ILE CYS GLU HIS GLN LYS PHE LEU GLN TRP VAL LYS GLU          
SEQRES  45 B  606  GLN LYS GLN PHE LEU VAL ASN VAL GLU GLN MET THR CYS          
SEQRES  46 B  606  ALA THR PRO VAL GLU MET ASN THR SER LEU VAL LEU ASP          
SEQRES  47 B  606  PHE ASN ASN SER THR CYS TYR MET                              
SEQRES   1 D  144  GLU SER GLU LYS GLN GLN TRP PHE CYS ASN SER SER ASP          
SEQRES   2 D  144  ALA ILE ILE SER TYR SER TYR CYS ASP HIS LEU LYS PHE          
SEQRES   3 D  144  PRO ILE SER ILE SER SER GLU PRO CYS ILE ARG LEU ARG          
SEQRES   4 D  144  GLY THR ASN GLY PHE VAL HIS VAL GLU PHE ILE PRO ARG          
SEQRES   5 D  144  GLY ASN LEU LYS TYR LEU TYR PHE ASN LEU PHE ILE SER          
SEQRES   6 D  144  VAL ASN SER ILE GLU LEU PRO LYS ARG LYS GLU VAL LEU          
SEQRES   7 D  144  CYS HIS GLY HIS ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 D  144  LEU LYS GLY GLU THR VAL ASN THR SER ILE PRO PHE SER          
SEQRES   9 D  144  PHE GLU GLY ILE LEU PHE PRO LYS GLY HIS TYR ARG CYS          
SEQRES  10 D  144  VAL ALA GLU ALA ILE ALA GLY ASP THR GLU GLU LYS LEU          
SEQRES  11 D  144  PHE CYS LEU ASN PHE THR ILE ILE HIS ARG ARG ASP VAL          
SEQRES  12 D  144  ASN                                                          
MODRES 3VQ1 ASN A  204  ASN  GLYCOSYLATION SITE                                 
MODRES 3VQ1 ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 3VQ1 ASN B  524  ASN  GLYCOSYLATION SITE                                 
MODRES 3VQ1 ASN B  572  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  A 705      14                                                       
HET    LP4  C 300      45                                                       
HET    LP5  C 301      48                                                       
HET    NAG  B 802      14                                                       
HET    LP4  D 300      45                                                       
HET    LP5  D 301      48                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     LP4 2-DEOXY-3-O-[(3R)-3-HYDROXYTETRADECANOYL]-2-{[(3R)-3-            
HETNAM   2 LP4  HYDROXYTETRADECANOYL]AMINO}-4-O-PHOSPHONO-BETA-D-               
HETNAM   3 LP4  GLUCOPYRANOSE                                                   
HETNAM     LP5 (R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-             
HETNAM   2 LP5  ((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)                 
HETNAM   3 LP5  TETRAHYDRO-2H-PYRAN-4-YL) 3-HYDROXYTETRADECANOATE               
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   5  NAG    8(C8 H15 N O6)                                               
FORMUL   9  LP4    2(C34 H66 N O12 P)                                           
FORMUL  10  LP5    2(C34 H66 N O12 P)                                           
FORMUL  14  HOH   *37(H2 O)                                                     
HELIX    1   1 PRO A  167  ASN A  172  5                                   6    
HELIX    2   2 LEU A  194  ASN A  200  1                                   7    
HELIX    3   3 SER A  238  GLN A  247  1                                  10    
HELIX    4   4 ASN A  248  ALA A  250  5                                   3    
HELIX    5   5 GLU A  272  ASP A  281  5                                  10    
HELIX    6   6 SER A  296  VAL A  300  5                                   5    
HELIX    7   7 PHE A  302  ALA A  306  5                                   5    
HELIX    8   8 SER A  390  GLY A  395  1                                   6    
HELIX    9   9 SER A  536  TYR A  538  5                                   3    
HELIX   10  10 ILE A  560  PHE A  564  5                                   5    
HELIX   11  11 ILE A  581  GLU A  583  5                                   3    
HELIX   12  12 HIS A  584  GLN A  594  1                                  11    
HELIX   13  13 ASN A  600  MET A  604  5                                   5    
HELIX   14  14 TYR C  102  ALA C  107  5                                   6    
HELIX   15  15 PRO B  167  ASN B  172  5                                   6    
HELIX   16  16 LEU B  194  GLU B  199  1                                   6    
HELIX   17  17 SER B  238  ASN B  248  1                                  11    
HELIX   18  18 GLU B  272  VAL B  282  5                                  11    
HELIX   19  19 SER B  296  VAL B  300  5                                   5    
HELIX   20  20 PHE B  302  ALA B  306  5                                   5    
HELIX   21  21 SER B  390  GLY B  395  1                                   6    
HELIX   22  22 SER B  536  ASN B  539  5                                   4    
HELIX   23  23 ILE B  560  PHE B  564  5                                   5    
HELIX   24  24 ILE B  581  GLU B  583  5                                   3    
HELIX   25  25 HIS B  584  GLN B  594  1                                  11    
HELIX   26  26 TYR D  102  ALA D  107  5                                   6    
SHEET    1   A25 ILE A  29  VAL A  32  0                                        
SHEET    2   A25 THR A  36  GLN A  38 -1  O  THR A  36   N  VAL A  32           
SHEET    3   A25 ASN A  57  ASP A  59  1  O  ASN A  57   N  TYR A  37           
SHEET    4   A25 TRP A  81  ASP A  83  1  O  TRP A  81   N  ILE A  58           
SHEET    5   A25 ASN A 105  ILE A 107  1  O  ILE A 107   N  LEU A  82           
SHEET    6   A25 ASN A 129  VAL A 131  1  O  VAL A 131   N  LEU A 106           
SHEET    7   A25 LYS A 153  ASN A 155  1  O  ASN A 155   N  LEU A 130           
SHEET    8   A25 HIS A 178  ASP A 180  1  O  ASP A 180   N  LEU A 154           
SHEET    9   A25 SER A 206  ASP A 208  1  O  SER A 206   N  VAL A 179           
SHEET   10   A25 LYS A 226  ARG A 233  1  O  GLU A 229   N  LEU A 207           
SHEET   11   A25 HIS A 253  GLY A 260  1  O  ILE A 258   N  LEU A 232           
SHEET   12   A25 THR A 283  LEU A 289  1  O  ARG A 288   N  LEU A 257           
SHEET   13   A25 ALA A 310  ALA A 314  1  O  ALA A 310   N  PHE A 287           
SHEET   14   A25 SER A 332  ILE A 336  1  O  ILE A 336   N  LEU A 313           
SHEET   15   A25 SER A 353  THR A 357  1  O  THR A 355   N  ILE A 335           
SHEET   16   A25 TYR A 375  ASP A 377  1  O  ASP A 377   N  LEU A 356           
SHEET   17   A25 HIS A 401  ASP A 403  1  O  ASP A 403   N  LEU A 376           
SHEET   18   A25 HIS A 424  ASP A 426  1  O  HIS A 424   N  LEU A 402           
SHEET   19   A25 TYR A 449  ASP A 451  1  O  TYR A 449   N  LEU A 425           
SHEET   20   A25 THR A 473  LYS A 475  1  O  THR A 473   N  LEU A 450           
SHEET   21   A25 PHE A 498  ASP A 500  1  O  ASP A 500   N  LEU A 474           
SHEET   22   A25 LEU A 522  ASN A 524  1  O  LEU A 522   N  LEU A 499           
SHEET   23   A25 THR A 546  ASP A 548  1  O  ASP A 548   N  LEU A 523           
SHEET   24   A25 PHE A 570  ASN A 572  1  O  PHE A 570   N  LEU A 547           
SHEET   25   A25 LEU A 598  VAL A 599  1  O  VAL A 599   N  PHE A 571           
SHEET    1   B 2 ILE A  67  LEU A  68  0                                        
SHEET    2   B 2 THR A  91  ILE A  92  1  O  THR A  91   N  LEU A  68           
SHEET    1   C 2 THR A 188  ILE A 189  0                                        
SHEET    2   C 2 PHE A 216  ILE A 217  1  O  PHE A 216   N  ILE A 189           
SHEET    1   D 3 PHE A 385  CYS A 388  0                                        
SHEET    2   D 3 ALA A 409  MET A 412  1  O  ALA A 409   N  PHE A 385           
SHEET    3   D 3 THR A 431  LYS A 433  1  O  THR A 431   N  ILE A 410           
SHEET    1   E 2 LYS A 458  ILE A 459  0                                        
SHEET    2   E 2 SER A 480  PHE A 481  1  O  SER A 480   N  ILE A 459           
SHEET    1   F 2 THR A 485  LEU A 486  0                                        
SHEET    2   F 2 GLN A 508  ILE A 509  1  O  GLN A 508   N  LEU A 486           
SHEET    1   G 2 LEU A 533  ASP A 534  0                                        
SHEET    2   G 2 SER A 557  LYS A 558  1  O  LYS A 558   N  LEU A 533           
SHEET    1   H 6 TRP C  23  SER C  27  0                                        
SHEET    2   H 6 ALA C  30  TYR C  36 -1  O  ALA C  30   N  SER C  27           
SHEET    3   H 6 GLU C 144  HIS C 155 -1  O  ASN C 150   N  SER C  35           
SHEET    4   H 6 GLY C 129  ALA C 139 -1  N  ALA C 137   O  LEU C 146           
SHEET    5   H 6 LEU C  74  VAL C  82 -1  N  TYR C  75   O  ILE C 138           
SHEET    6   H 6 ILE C  85  GLU C  86 -1  O  ILE C  85   N  VAL C  82           
SHEET    1   I 6 TRP C  23  SER C  27  0                                        
SHEET    2   I 6 ALA C  30  TYR C  36 -1  O  ALA C  30   N  SER C  27           
SHEET    3   I 6 GLU C 144  HIS C 155 -1  O  ASN C 150   N  SER C  35           
SHEET    4   I 6 GLY C 129  ALA C 139 -1  N  ALA C 137   O  LEU C 146           
SHEET    5   I 6 LEU C  74  VAL C  82 -1  N  TYR C  75   O  ILE C 138           
SHEET    6   I 6 ARG C  90  VAL C  93 -1  O  ARG C  90   N  LEU C  78           
SHEET    1   J 3 ILE C  44  GLU C  49  0                                        
SHEET    2   J 3 THR C  57  PHE C  65 -1  O  GLU C  64   N  SER C  45           
SHEET    3   J 3 VAL C 113  PHE C 121 -1  O  ILE C 117   N  VAL C  61           
SHEET    1   K24 ILE B  29  VAL B  32  0                                        
SHEET    2   K24 THR B  36  GLN B  38 -1  O  GLN B  38   N  ILE B  29           
SHEET    3   K24 ASN B  57  ASP B  59  1  O  ASN B  57   N  TYR B  37           
SHEET    4   K24 TRP B  81  ASP B  83  1  O  TRP B  81   N  ILE B  58           
SHEET    5   K24 ASN B 105  ILE B 107  1  O  ASN B 105   N  LEU B  82           
SHEET    6   K24 ASN B 129  VAL B 131  1  O  VAL B 131   N  LEU B 106           
SHEET    7   K24 LYS B 153  ASN B 155  1  O  ASN B 155   N  LEU B 130           
SHEET    8   K24 HIS B 178  ASP B 180  1  O  HIS B 178   N  LEU B 154           
SHEET    9   K24 SER B 206  ASP B 208  1  O  SER B 206   N  VAL B 179           
SHEET   10   K24 ILE B 225  ARG B 233  1  O  GLU B 229   N  LEU B 207           
SHEET   11   K24 LEU B 252  GLY B 260  1  O  ILE B 258   N  LEU B 232           
SHEET   12   K24 THR B 283  LEU B 289  1  O  ARG B 288   N  LEU B 259           
SHEET   13   K24 ALA B 310  ALA B 314  1  O  SER B 312   N  LEU B 289           
SHEET   14   K24 SER B 332  ILE B 336  1  O  SER B 334   N  LEU B 313           
SHEET   15   K24 SER B 353  THR B 357  1  O  THR B 355   N  ILE B 335           
SHEET   16   K24 TYR B 375  ASP B 377  1  O  ASP B 377   N  LEU B 356           
SHEET   17   K24 HIS B 401  ASP B 403  1  O  ASP B 403   N  LEU B 376           
SHEET   18   K24 HIS B 424  ASP B 426  1  O  HIS B 424   N  LEU B 402           
SHEET   19   K24 TYR B 449  ASP B 451  1  O  TYR B 449   N  LEU B 425           
SHEET   20   K24 THR B 473  LYS B 475  1  O  LYS B 475   N  LEU B 450           
SHEET   21   K24 PHE B 498  ASP B 500  1  O  PHE B 498   N  LEU B 474           
SHEET   22   K24 LEU B 522  ASN B 524  1  O  ASN B 524   N  LEU B 499           
SHEET   23   K24 THR B 546  ASP B 548  1  O  ASP B 548   N  LEU B 523           
SHEET   24   K24 PHE B 570  ASN B 572  1  O  ASN B 572   N  LEU B 547           
SHEET    1   L 2 ILE B  67  LEU B  68  0                                        
SHEET    2   L 2 THR B  91  ILE B  92  1  O  THR B  91   N  LEU B  68           
SHEET    1   M 2 THR B 188  ILE B 189  0                                        
SHEET    2   M 2 PHE B 216  ILE B 217  1  O  PHE B 216   N  ILE B 189           
SHEET    1   N 3 PHE B 385  CYS B 388  0                                        
SHEET    2   N 3 ALA B 409  MET B 412  1  O  ILE B 411   N  PHE B 385           
SHEET    3   N 3 THR B 431  LYS B 433  1  O  THR B 431   N  ILE B 410           
SHEET    1   O 2 LYS B 458  ILE B 459  0                                        
SHEET    2   O 2 SER B 480  PHE B 481  1  O  SER B 480   N  ILE B 459           
SHEET    1   P 2 THR B 485  LEU B 486  0                                        
SHEET    2   P 2 GLN B 508  ILE B 509  1  O  GLN B 508   N  LEU B 486           
SHEET    1   Q 2 LEU B 533  ASP B 534  0                                        
SHEET    2   Q 2 SER B 557  LYS B 558  1  O  LYS B 558   N  LEU B 533           
SHEET    1   R 6 TRP D  23  SER D  27  0                                        
SHEET    2   R 6 ALA D  30  TYR D  36 -1  O  ILE D  32   N  CYS D  25           
SHEET    3   R 6 GLU D 144  HIS D 155 -1  O  ASN D 150   N  SER D  35           
SHEET    4   R 6 GLY D 129  ALA D 139 -1  N  ALA D 137   O  LEU D 146           
SHEET    5   R 6 LEU D  74  VAL D  82 -1  N  TYR D  75   O  ILE D 138           
SHEET    6   R 6 ILE D  85  GLU D  86 -1  O  ILE D  85   N  VAL D  82           
SHEET    1   S 6 TRP D  23  SER D  27  0                                        
SHEET    2   S 6 ALA D  30  TYR D  36 -1  O  ILE D  32   N  CYS D  25           
SHEET    3   S 6 GLU D 144  HIS D 155 -1  O  ASN D 150   N  SER D  35           
SHEET    4   S 6 GLY D 129  ALA D 139 -1  N  ALA D 137   O  LEU D 146           
SHEET    5   S 6 LEU D  74  VAL D  82 -1  N  TYR D  75   O  ILE D 138           
SHEET    6   S 6 ARG D  90  VAL D  93 -1  O  GLU D  92   N  PHE D  76           
SHEET    1   T 3 ILE D  44  GLU D  49  0                                        
SHEET    2   T 3 THR D  57  PHE D  65 -1  O  HIS D  62   N  SER D  47           
SHEET    3   T 3 VAL D 113  PHE D 121 -1  O  ILE D 117   N  VAL D  61           
SSBOND   1 CYS A   28    CYS A   39                          1555   1555  2.04  
SSBOND   2 CYS A  280    CYS A  304                          1555   1555  2.03  
SSBOND   3 CYS A  388    CYS A  389                          1555   1555  2.07  
SSBOND   4 CYS A  580    CYS A  606                          1555   1555  2.05  
SSBOND   5 CYS A  582    CYS A  625                          1555   1555  2.05  
SSBOND   6 CYS C   25    CYS C   51                          1555   1555  2.03  
SSBOND   7 CYS C   37    CYS C  148                          1555   1555  2.06  
SSBOND   8 CYS C   95    CYS C  105                          1555   1555  2.07  
SSBOND   9 CYS B   28    CYS B   39                          1555   1555  2.04  
SSBOND  10 CYS B  280    CYS B  304                          1555   1555  2.05  
SSBOND  11 CYS B  388    CYS B  389                          1555   1555  2.02  
SSBOND  12 CYS B  580    CYS B  606                          1555   1555  2.05  
SSBOND  13 CYS B  582    CYS B  625                          1555   1555  2.05  
SSBOND  14 CYS D   25    CYS D   51                          1555   1555  2.05  
SSBOND  15 CYS D   37    CYS D  148                          1555   1555  2.05  
SSBOND  16 CYS D   95    CYS D  105                          1555   1555  2.04  
LINK         ND2 ASN A 204                 C1  NAG E   1     1555   1555  1.37  
LINK         ND2 ASN A 524                 C1  NAG F   1     1555   1555  1.40  
LINK         C1  LP4 C 300                 O6  LP5 C 301     1555   1555  1.44  
LINK         ND2 ASN B 524                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN B 572                 C1  NAG B 802     1555   1555  1.46  
LINK         C1  LP4 D 300                 O6  LP5 D 301     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
CISPEP   1 CYS A  388    CYS A  389          0       -17.57                     
CISPEP   2 THR A  614    SER A  615          0        -8.37                     
CISPEP   3 GLU C   49    PRO C   50          0        -0.80                     
CISPEP   4 PRO C  127    LYS C  128          0        23.58                     
CISPEP   5 CYS B  388    CYS B  389          0        -8.07                     
CISPEP   6 THR B  614    SER B  615          0        -6.24                     
CISPEP   7 GLU D   49    PRO D   50          0        -3.65                     
CRYST1   77.160  150.519  181.847  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012960  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006644  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005499        0.00000                         
ATOM      1  N   PRO A  27      -4.097  37.234  52.631  1.00 93.84           N  
ANISOU    1  N   PRO A  27    11585  12226  11840   -333    586   -297       N  
ATOM      2  CA  PRO A  27      -4.443  35.815  52.601  1.00 96.01           C  
ANISOU    2  CA  PRO A  27    11862  12514  12102   -339    578   -271       C  
ATOM      3  C   PRO A  27      -3.648  35.087  51.521  1.00 96.65           C  
ANISOU    3  C   PRO A  27    11950  12589  12182   -319    537   -231       C  
ATOM      4  O   PRO A  27      -3.946  35.222  50.333  1.00 95.20           O  
ANISOU    4  O   PRO A  27    11752  12383  12036   -290    521   -223       O  
ATOM      5  CB  PRO A  27      -5.939  35.830  52.267  1.00 97.08           C  
ANISOU    5  CB  PRO A  27    11970  12634  12281   -327    598   -289       C  
ATOM      6  CG  PRO A  27      -6.423  37.145  52.786  1.00 95.85           C  
ANISOU    6  CG  PRO A  27    11802  12469  12145   -331    629   -332       C  
ATOM      7  CD  PRO A  27      -5.288  38.100  52.551  1.00 95.32           C  
ANISOU    7  CD  PRO A  27    11748  12396  12074   -324    613   -332       C  
ATOM      8  N   CYS A  28      -2.644  34.321  51.942  1.00 97.30           N  
ANISOU    8  N   CYS A  28    12054  12691  12221   -335    521   -206       N  
ATOM      9  CA  CYS A  28      -1.690  33.701  51.020  1.00 97.46           C  
ANISOU    9  CA  CYS A  28    12084  12708  12239   -319    483   -169       C  
ATOM     10  C   CYS A  28      -1.982  32.234  50.704  1.00 96.97           C  
ANISOU   10  C   CYS A  28    12021  12652  12172   -318    468   -140       C  
ATOM     11  O   CYS A  28      -2.342  31.456  51.591  1.00 99.05           O  
ANISOU   11  O   CYS A  28    12289  12934  12411   -342    481   -138       O  
ATOM     12  CB  CYS A  28      -0.262  33.828  51.566  1.00102.92           C  
ANISOU   12  CB  CYS A  28    12800  13412  12891   -335    469   -158       C  
ATOM     13  SG  CYS A  28       0.449  35.490  51.480  1.00109.77           S  
ANISOU   13  SG  CYS A  28    13670  14267  13769   -326    471   -181       S  
ATOM     14  N   ILE A  29      -1.801  31.874  49.432  1.00 94.82           N  
ANISOU   14  N   ILE A  29    11742  12363  11922   -291    441   -118       N  
ATOM     15  CA  ILE A  29      -1.888  30.489  48.943  1.00 89.99           C  
ANISOU   15  CA  ILE A  29    11129  11754  11307   -287    421    -87       C  
ATOM     16  C   ILE A  29      -0.814  29.602  49.590  1.00 90.41           C  
ANISOU   16  C   ILE A  29    11204  11828  11318   -308    406    -62       C  
ATOM     17  O   ILE A  29       0.314  30.040  49.819  1.00 95.50           O  
ANISOU   17  O   ILE A  29    11864  12477  11943   -314    396    -59       O  
ATOM     18  CB  ILE A  29      -1.782  30.445  47.397  1.00 86.28           C  
ANISOU   18  CB  ILE A  29    10650  11261  10870   -254    395    -71       C  
ATOM     19  CG1 ILE A  29      -2.961  31.200  46.766  1.00 86.18           C  
ANISOU   19  CG1 ILE A  29    10616  11227  10901   -234    408    -93       C  
ATOM     20  CG2 ILE A  29      -1.717  29.010  46.881  1.00 81.70           C  
ANISOU   20  CG2 ILE A  29    10072  10685  10285   -250    373    -39       C  
ATOM     21  CD1 ILE A  29      -2.694  31.743  45.377  1.00 87.74           C  
ANISOU   21  CD1 ILE A  29    10807  11400  11129   -205    385    -85       C  
ATOM     22  N   GLU A  30      -1.173  28.356  49.880  1.00 88.97           N  
ANISOU   22  N   GLU A  30    11022  11658  11123   -319    403    -45       N  
ATOM     23  CA  GLU A  30      -0.297  27.449  50.609  1.00 87.48           C  
ANISOU   23  CA  GLU A  30    10852  11489  10895   -342    390    -21       C  
ATOM     24  C   GLU A  30       0.054  26.223  49.763  1.00 86.75           C  
ANISOU   24  C   GLU A  30    10759  11392  10809   -329    360     12       C  
ATOM     25  O   GLU A  30      -0.709  25.257  49.716  1.00 84.24           O  
ANISOU   25  O   GLU A  30    10432  11077  10496   -331    361     22       O  
ATOM     26  CB  GLU A  30      -0.993  27.036  51.905  1.00 85.42           C  
ANISOU   26  CB  GLU A  30    10595  11250  10610   -374    415    -31       C  
ATOM     27  CG  GLU A  30      -0.125  26.309  52.913  1.00 84.84           C  
ANISOU   27  CG  GLU A  30    10544  11199  10492   -405    405    -12       C  
ATOM     28  CD  GLU A  30      -0.843  26.122  54.234  1.00 84.05           C  
ANISOU   28  CD  GLU A  30    10449  11120  10366   -438    433    -26       C  
ATOM     29  OE1 GLU A  30      -1.158  27.137  54.892  1.00 82.11           O  
ANISOU   29  OE1 GLU A  30    10204  10878  10114   -450    461    -58       O  
ATOM     30  OE2 GLU A  30      -1.105  24.962  54.610  1.00 82.97           O  
ANISOU   30  OE2 GLU A  30    10314  10995  10213   -454    429     -7       O  
ATOM     31  N   VAL A  31       1.206  26.263  49.094  1.00 86.35           N  
ANISOU   31  N   VAL A  31    10715  11333  10757   -316    334     29       N  
ATOM     32  CA  VAL A  31       1.595  25.168  48.192  1.00 85.34           C  
ANISOU   32  CA  VAL A  31    10586  11199  10639   -302    306     59       C  
ATOM     33  C   VAL A  31       2.167  23.985  48.982  1.00 88.17           C  
ANISOU   33  C   VAL A  31    10957  11576  10967   -326    293     84       C  
ATOM     34  O   VAL A  31       1.833  22.831  48.704  1.00 91.39           O  
ANISOU   34  O   VAL A  31    11359  11984  11379   -324    282    103       O  
ATOM     35  CB  VAL A  31       2.516  25.622  47.017  1.00 80.77           C  
ANISOU   35  CB  VAL A  31    10008  10602  10077   -277    284     68       C  
ATOM     36  CG1 VAL A  31       2.588  27.141  46.925  1.00 78.13           C  
ANISOU   36  CG1 VAL A  31     9673  10259   9753   -269    297     42       C  
ATOM     37  CG2 VAL A  31       3.915  25.030  47.121  1.00 78.68           C  
ANISOU   37  CG2 VAL A  31     9758  10344   9792   -285    259     93       C  
ATOM     38  N   VAL A  32       3.025  24.277  49.959  1.00 87.12           N  
ANISOU   38  N   VAL A  32    10841  11457  10803   -349    293     84       N  
ATOM     39  CA  VAL A  32       3.462  23.284  50.939  1.00 89.93           C  
ANISOU   39  CA  VAL A  32    11209  11831  11127   -378    284    105       C  
ATOM     40  C   VAL A  32       3.332  23.905  52.331  1.00 96.52           C  
ANISOU   40  C   VAL A  32    12057  12685  11931   -409    307     86       C  
ATOM     41  O   VAL A  32       4.144  24.759  52.702  1.00100.19           O  
ANISOU   41  O   VAL A  32    12532  13152  12381   -416    307     77       O  
ATOM     42  CB  VAL A  32       4.917  22.801  50.714  1.00 88.43           C  
ANISOU   42  CB  VAL A  32    11031  11640  10929   -377    252    133       C  
ATOM     43  CG1 VAL A  32       5.294  21.746  51.748  1.00 86.86           C  
ANISOU   43  CG1 VAL A  32    10843  11459  10699   -408    240    155       C  
ATOM     44  CG2 VAL A  32       5.111  22.249  49.308  1.00 87.07           C  
ANISOU   44  CG2 VAL A  32    10846  11449  10786   -347    231    149       C  
ATOM     45  N   PRO A  33       2.292  23.500  53.094  1.00100.81           N  
ANISOU   45  N   PRO A  33    12598  13242  12464   -428    328     77       N  
ATOM     46  CA  PRO A  33       2.103  23.890  54.495  1.00 97.96           C  
ANISOU   46  CA  PRO A  33    12250  12901  12069   -462    352     60       C  
ATOM     47  C   PRO A  33       3.407  23.892  55.300  1.00 96.72           C  
ANISOU   47  C   PRO A  33    12115  12757  11877   -487    335     75       C  
ATOM     48  O   PRO A  33       4.182  22.932  55.225  1.00 97.06           O  
ANISOU   48  O   PRO A  33    12164  12801  11910   -491    306    107       O  
ATOM     49  CB  PRO A  33       1.157  22.809  55.025  1.00 97.10           C  
ANISOU   49  CB  PRO A  33    12136  12804  11950   -480    361     69       C  
ATOM     50  CG  PRO A  33       0.393  22.335  53.827  1.00 98.70           C  
ANISOU   50  CG  PRO A  33    12318  12990  12193   -449    357     74       C  
ATOM     51  CD  PRO A  33       1.117  22.769  52.579  1.00100.15           C  
ANISOU   51  CD  PRO A  33    12496  13152  12402   -416    335     80       C  
ATOM     52  N   ASN A  34       3.640  24.977  56.042  1.00 93.83           N  
ANISOU   52  N   ASN A  34    11760  12398  11492   -502    352     51       N  
ATOM     53  CA  ASN A  34       4.840  25.155  56.881  1.00 95.98           C  
ANISOU   53  CA  ASN A  34    12054  12683  11730   -527    338     61       C  
ATOM     54  C   ASN A  34       6.181  25.337  56.130  1.00 95.30           C  
ANISOU   54  C   ASN A  34    11971  12582  11654   -508    306     79       C  
ATOM     55  O   ASN A  34       7.217  25.563  56.765  1.00 93.89           O  
ANISOU   55  O   ASN A  34    11809  12412  11451   -526    293     86       O  
ATOM     56  CB  ASN A  34       4.961  24.031  57.939  1.00 95.13           C  
ANISOU   56  CB  ASN A  34    11962  12597  11586   -563    329     84       C  
ATOM     57  CG  ASN A  34       4.023  24.220  59.129  1.00 95.56           C  
ANISOU   57  CG  ASN A  34    12023  12670  11612   -596    363     61       C  
ATOM     58  OD1 ASN A  34       3.641  25.340  59.470  1.00 94.45           O  
ANISOU   58  OD1 ASN A  34    11882  12531  11470   -599    391     27       O  
ATOM     59  ND2 ASN A  34       3.664  23.115  59.780  1.00 95.02           N  
ANISOU   59  ND2 ASN A  34    11960  12617  11523   -621    361     79       N  
ATOM     60  N   ILE A  35       6.167  25.256  54.797  1.00 89.72           N  
ANISOU   60  N   ILE A  35    11248  11855  10984   -472    294     85       N  
ATOM     61  CA  ILE A  35       7.415  25.277  54.018  1.00 86.21           C  
ANISOU   61  CA  ILE A  35    10805  11397  10551   -454    264    104       C  
ATOM     62  C   ILE A  35       7.414  26.258  52.831  1.00 83.96           C  
ANISOU   62  C   ILE A  35    10508  11091  10301   -419    267     88       C  
ATOM     63  O   ILE A  35       8.333  27.074  52.701  1.00 85.80           O  
ANISOU   63  O   ILE A  35    10748  11318  10534   -414    260     84       O  
ATOM     64  CB  ILE A  35       7.854  23.847  53.596  1.00 88.31           C  
ANISOU   64  CB  ILE A  35    11069  11661  10822   -450    235    141       C  
ATOM     65  CG1 ILE A  35       8.400  23.082  54.810  1.00 89.03           C  
ANISOU   65  CG1 ILE A  35    11177  11772  10878   -487    222    161       C  
ATOM     66  CG2 ILE A  35       8.916  23.890  52.501  1.00 86.38           C  
ANISOU   66  CG2 ILE A  35    10820  11398  10600   -425    209    156       C  
ATOM     67  CD1 ILE A  35       8.302  21.575  54.704  1.00 88.99           C  
ANISOU   67  CD1 ILE A  35    11167  11768  10874   -491    202    192       C  
ATOM     68  N   THR A  36       6.400  26.180  51.970  1.00 77.47           N  
ANISOU   68  N   THR A  36     9668  10257   9508   -396    277     80       N  
ATOM     69  CA  THR A  36       6.324  27.062  50.800  1.00 70.26           C  
ANISOU   69  CA  THR A  36     8744   9323   8629   -364    279     67       C  
ATOM     70  C   THR A  36       4.994  27.808  50.750  1.00 69.08           C  
ANISOU   70  C   THR A  36     8581   9169   8497   -356    308     36       C  
ATOM     71  O   THR A  36       3.921  27.198  50.776  1.00 70.01           O  
ANISOU   71  O   THR A  36     8689   9289   8622   -357    320     35       O  
ATOM     72  CB  THR A  36       6.559  26.302  49.467  1.00 68.03           C  
ANISOU   72  CB  THR A  36     8451   9024   8372   -337    255     90       C  
ATOM     73  OG1 THR A  36       7.644  25.379  49.611  1.00 66.80           O  
ANISOU   73  OG1 THR A  36     8304   8873   8200   -346    229    119       O  
ATOM     74  CG2 THR A  36       6.882  27.273  48.328  1.00 64.01           C  
ANISOU   74  CG2 THR A  36     7935   8495   7889   -308    250     81       C  
ATOM     75  N   TYR A  37       5.080  29.133  50.682  1.00 70.34           N  
ANISOU   75  N   TYR A  37     8740   9320   8665   -349    320     12       N  
ATOM     76  CA  TYR A  37       3.897  29.990  50.599  1.00 73.75           C  
ANISOU   76  CA  TYR A  37     9158   9744   9119   -340    348    -18       C  
ATOM     77  C   TYR A  37       3.993  30.925  49.401  1.00 71.30           C  
ANISOU   77  C   TYR A  37     8837   9410   8842   -309    342    -26       C  
ATOM     78  O   TYR A  37       5.063  31.441  49.093  1.00 73.90           O  
ANISOU   78  O   TYR A  37     9174   9733   9169   -303    327    -20       O  
ATOM     79  CB  TYR A  37       3.693  30.773  51.907  1.00 75.64           C  
ANISOU   79  CB  TYR A  37     9405   9998   9335   -367    375    -46       C  
ATOM     80  CG  TYR A  37       3.297  29.886  53.065  1.00 76.72           C  
ANISOU   80  CG  TYR A  37     9550  10157   9440   -399    386    -41       C  
ATOM     81  CD1 TYR A  37       4.247  29.112  53.732  1.00 77.56           C  
ANISOU   81  CD1 TYR A  37     9676  10280   9512   -421    368    -16       C  
ATOM     82  CD2 TYR A  37       1.969  29.801  53.480  1.00 79.33           C  
ANISOU   82  CD2 TYR A  37     9871  10493   9777   -406    415    -61       C  
ATOM     83  CE1 TYR A  37       3.888  28.281  54.780  1.00 81.44           C  
ANISOU   83  CE1 TYR A  37    10176  10793   9974   -452    376    -10       C  
ATOM     84  CE2 TYR A  37       1.599  28.974  54.532  1.00 81.20           C  
ANISOU   84  CE2 TYR A  37    10116  10752   9985   -437    425    -56       C  
ATOM     85  CZ  TYR A  37       2.565  28.218  55.177  1.00 82.56           C  
ANISOU   85  CZ  TYR A  37    10307  10940  10120   -460    406    -30       C  
ATOM     86  OH  TYR A  37       2.217  27.394  56.219  1.00 86.14           O  
ANISOU   86  OH  TYR A  37    10771  11415  10543   -491    414    -23       O  
ATOM     87  N   GLN A  38       2.869  31.132  48.728  1.00 70.66           N  
ANISOU   87  N   GLN A  38     8738   9315   8794   -291    353    -39       N  
ATOM     88  CA  GLN A  38       2.838  31.920  47.511  1.00 76.16           C  
ANISOU   88  CA  GLN A  38     9423   9987   9524   -262    344    -44       C  
ATOM     89  C   GLN A  38       1.916  33.121  47.699  1.00 78.59           C  
ANISOU   89  C   GLN A  38     9719  10286   9855   -258    370    -78       C  
ATOM     90  O   GLN A  38       0.700  32.967  47.838  1.00 78.91           O  
ANISOU   90  O   GLN A  38     9746  10326   9911   -258    389    -92       O  
ATOM     91  CB  GLN A  38       2.375  31.042  46.344  1.00 80.61           C  
ANISOU   91  CB  GLN A  38     9976  10540  10112   -240    328    -24       C  
ATOM     92  CG  GLN A  38       3.281  31.080  45.120  1.00 84.43           C  
ANISOU   92  CG  GLN A  38    10462  11008  10607   -219    301     -5       C  
ATOM     93  CD  GLN A  38       2.829  32.080  44.072  1.00 87.23           C  
ANISOU   93  CD  GLN A  38    10805  11340  10998   -194    301    -18       C  
ATOM     94  OE1 GLN A  38       2.583  33.249  44.371  1.00 84.35           O  
ANISOU   94  OE1 GLN A  38    10436  10969  10642   -194    316    -42       O  
ATOM     95  NE2 GLN A  38       2.726  31.623  42.827  1.00 87.98           N  
ANISOU   95  NE2 GLN A  38    10894  11420  11112   -174    282     -1       N  
ATOM     96  N   CYS A  39       2.504  34.316  47.708  1.00 80.34           N  
ANISOU   96  N   CYS A  39     9944  10500  10079   -255    372    -93       N  
ATOM     97  CA  CYS A  39       1.762  35.548  47.983  1.00 80.60           C  
ANISOU   97  CA  CYS A  39     9966  10524  10133   -253    397   -127       C  
ATOM     98  C   CYS A  39       1.748  36.518  46.802  1.00 77.25           C  
ANISOU   98  C   CYS A  39     9530  10073   9746   -225    387   -132       C  
ATOM     99  O   CYS A  39       1.563  37.720  46.984  1.00 79.28           O  
ANISOU   99  O   CYS A  39     9782  10321  10019   -223    401   -158       O  
ATOM    100  CB  CYS A  39       2.331  36.236  49.224  1.00 84.87           C  
ANISOU  100  CB  CYS A  39    10521  11080  10645   -278    413   -146       C  
ATOM    101  SG  CYS A  39       2.313  35.198  50.702  1.00104.11           S  
ANISOU  101  SG  CYS A  39    12973  13549  13035   -315    426   -142       S  
ATOM    102  N   MET A  40       1.934  35.987  45.596  1.00 74.93           N  
ANISOU  102  N   MET A  40     9234   9768   9467   -205    362   -108       N  
ATOM    103  CA  MET A  40       1.926  36.791  44.371  1.00 74.53           C  
ANISOU  103  CA  MET A  40     9174   9693   9451   -179    349   -108       C  
ATOM    104  C   MET A  40       0.600  37.521  44.190  1.00 74.96           C  
ANISOU  104  C   MET A  40     9207   9729   9543   -169    366   -133       C  
ATOM    105  O   MET A  40      -0.451  37.006  44.567  1.00 81.90           O  
ANISOU  105  O   MET A  40    10075  10613  10429   -175    382   -141       O  
ATOM    106  CB  MET A  40       2.193  35.902  43.153  1.00 71.51           C  
ANISOU  106  CB  MET A  40     8793   9302   9075   -162    321    -78       C  
ATOM    107  CG  MET A  40       2.688  36.642  41.923  1.00 73.17           C  
ANISOU  107  CG  MET A  40     9001   9491   9306   -140    302    -71       C  
ATOM    108  SD  MET A  40       2.661  35.677  40.397  1.00 76.69           S  
ANISOU  108  SD  MET A  40     9446   9926   9767   -120    275    -41       S  
ATOM    109  CE  MET A  40       3.773  34.322  40.764  1.00 73.96           C  
ANISOU  109  CE  MET A  40     9117   9601   9382   -133    262    -14       C  
ATOM    110  N   ASP A  41       0.665  38.726  43.630  1.00 76.48           N  
ANISOU  110  N   ASP A  41     9394   9903   9762   -155    363   -146       N  
ATOM    111  CA  ASP A  41      -0.517  39.495  43.218  1.00 77.15           C  
ANISOU  111  CA  ASP A  41     9455   9965   9890   -141    373   -166       C  
ATOM    112  C   ASP A  41      -1.691  39.478  44.211  1.00 78.83           C  
ANISOU  112  C   ASP A  41     9656  10185  10111   -155    405   -193       C  
ATOM    113  O   ASP A  41      -2.850  39.305  43.829  1.00 80.21           O  
ANISOU  113  O   ASP A  41     9812  10347  10317   -145    410   -199       O  
ATOM    114  CB  ASP A  41      -0.967  39.069  41.810  1.00 77.41           C  
ANISOU  114  CB  ASP A  41     9480   9980   9952   -118    350   -146       C  
ATOM    115  CG  ASP A  41      -2.001  40.015  41.200  1.00 78.56           C  
ANISOU  115  CG  ASP A  41     9603  10098  10146   -102    353   -163       C  
ATOM    116  OD1 ASP A  41      -2.167  41.158  41.686  1.00 76.95           O  
ANISOU  116  OD1 ASP A  41     9392   9886   9957   -105    369   -190       O  
ATOM    117  OD2 ASP A  41      -2.654  39.604  40.219  1.00 80.49           O  
ANISOU  117  OD2 ASP A  41     9837  10328  10415    -87    338   -150       O  
ATOM    118  N   GLN A  42      -1.373  39.630  45.492  1.00 81.09           N  
ANISOU  118  N   GLN A  42     9952  10491  10367   -178    426   -209       N  
ATOM    119  CA  GLN A  42      -2.337  40.132  46.466  1.00 82.14           C  
ANISOU  119  CA  GLN A  42    10072  10626  10511   -191    460   -244       C  
ATOM    120  C   GLN A  42      -2.167  41.652  46.407  1.00 83.90           C  
ANISOU  120  C   GLN A  42    10289  10831  10758   -184    466   -268       C  
ATOM    121  O   GLN A  42      -1.361  42.154  45.609  1.00 90.46           O  
ANISOU  121  O   GLN A  42    11125  11649  11594   -170    443   -255       O  
ATOM    122  CB  GLN A  42      -2.039  39.598  47.870  1.00 81.15           C  
ANISOU  122  CB  GLN A  42     9962  10530  10339   -222    480   -250       C  
ATOM    123  CG  GLN A  42      -1.932  38.077  47.970  1.00 81.67           C  
ANISOU  123  CG  GLN A  42    10038  10614  10376   -231    469   -222       C  
ATOM    124  CD  GLN A  42      -3.279  37.371  47.968  1.00 81.08           C  
ANISOU  124  CD  GLN A  42     9946  10539  10321   -231    483   -226       C  
ATOM    125  OE1 GLN A  42      -3.609  36.644  47.030  1.00 72.43           O  
ANISOU  125  OE1 GLN A  42     8843   9433   9241   -214    464   -204       O  
ATOM    126  NE2 GLN A  42      -4.065  37.583  49.024  1.00 82.98           N  
ANISOU  126  NE2 GLN A  42    10180  10789  10559   -250    517   -255       N  
ATOM    127  N   LYS A  43      -2.904  42.402  47.214  1.00 77.67           N  
ANISOU  127  N   LYS A  43     9487  10040   9983   -194    497   -304       N  
ATOM    128  CA  LYS A  43      -2.684  43.845  47.211  1.00 79.41           C  
ANISOU  128  CA  LYS A  43     9702  10243  10226   -188    503   -328       C  
ATOM    129  C   LYS A  43      -1.886  44.278  48.439  1.00 80.57           C  
ANISOU  129  C   LYS A  43     9867  10410  10334   -213    520   -345       C  
ATOM    130  O   LYS A  43      -2.160  45.314  49.049  1.00 87.17           O  
ANISOU  130  O   LYS A  43    10695  11240  11184   -220    543   -379       O  
ATOM    131  CB  LYS A  43      -3.995  44.615  47.033  1.00 77.52           C  
ANISOU  131  CB  LYS A  43     9433   9980  10040   -177    521   -357       C  
ATOM    132  CG  LYS A  43      -4.649  44.363  45.683  1.00 76.58           C  
ANISOU  132  CG  LYS A  43     9297   9836   9961   -151    498   -338       C  
ATOM    133  CD  LYS A  43      -5.433  45.569  45.197  1.00 78.89           C  
ANISOU  133  CD  LYS A  43     9564  10097  10312   -134    502   -361       C  
ATOM    134  CE  LYS A  43      -5.989  45.324  43.803  1.00 79.68           C  
ANISOU  134  CE  LYS A  43     9651  10174  10450   -110    474   -339       C  
ATOM    135  NZ  LYS A  43      -6.698  46.521  43.274  1.00 79.34           N  
ANISOU  135  NZ  LYS A  43     9582  10097  10465    -93    473   -358       N  
ATOM    136  N   LEU A  44      -0.872  43.476  48.763  1.00 79.58           N  
ANISOU  136  N   LEU A  44     9766  10308  10163   -226    507   -321       N  
ATOM    137  CA  LEU A  44      -0.080  43.626  49.984  1.00 81.08           C  
ANISOU  137  CA  LEU A  44     9976  10520  10308   -253    520   -331       C  
ATOM    138  C   LEU A  44       0.796  44.878  50.040  1.00 83.53           C  
ANISOU  138  C   LEU A  44    10294  10823  10621   -252    516   -344       C  
ATOM    139  O   LEU A  44       1.294  45.351  49.013  1.00 80.61           O  
ANISOU  139  O   LEU A  44     9921  10434  10272   -230    492   -330       O  
ATOM    140  CB  LEU A  44       0.789  42.384  50.209  1.00 79.68           C  
ANISOU  140  CB  LEU A  44     9821  10366  10084   -267    502   -298       C  
ATOM    141  CG  LEU A  44       0.107  41.053  50.535  1.00 78.75           C  
ANISOU  141  CG  LEU A  44     9704  10266   9952   -278    508   -286       C  
ATOM    142  CD1 LEU A  44       1.162  39.988  50.787  1.00 78.21           C  
ANISOU  142  CD1 LEU A  44     9658  10218   9838   -291    488   -253       C  
ATOM    143  CD2 LEU A  44      -0.824  41.168  51.733  1.00 81.85           C  
ANISOU  143  CD2 LEU A  44    10091  10671  10338   -301    547   -319       C  
ATOM    144  N   SER A  45       0.973  45.393  51.259  1.00 87.79           N  
ANISOU  144  N   SER A  45    10842  11375  11136   -276    540   -371       N  
ATOM    145  CA  SER A  45       1.795  46.579  51.535  1.00 84.70           C  
ANISOU  145  CA  SER A  45    10459  10980  10743   -279    540   -387       C  
ATOM    146  C   SER A  45       3.100  46.209  52.239  1.00 84.20           C  
ANISOU  146  C   SER A  45    10424  10940  10627   -300    529   -371       C  
ATOM    147  O   SER A  45       4.100  46.916  52.109  1.00 84.16           O  
ANISOU  147  O   SER A  45    10428  10929  10617   -297    515   -368       O  
ATOM    148  CB  SER A  45       1.018  47.583  52.387  1.00 81.83           C  
ANISOU  148  CB  SER A  45    10082  10611  10396   -291    577   -433       C  
ATOM    149  OG  SER A  45      -0.263  47.832  51.837  1.00 85.02           O  
ANISOU  149  OG  SER A  45    10459  10993  10850   -273    589   -449       O  
ATOM    150  N   LYS A  46       3.071  45.112  52.994  1.00 82.58           N  
ANISOU  150  N   LYS A  46    10232  10759  10383   -323    535   -360       N  
ATOM    151  CA  LYS A  46       4.261  44.548  53.629  1.00 86.28           C  
ANISOU  151  CA  LYS A  46    10728  11252  10803   -344    520   -339       C  
ATOM    152  C   LYS A  46       4.106  43.043  53.773  1.00 85.09           C  
ANISOU  152  C   LYS A  46    10584  11119  10627   -354    513   -312       C  
ATOM    153  O   LYS A  46       3.072  42.477  53.410  1.00 82.29           O  
ANISOU  153  O   LYS A  46    10214  10760  10292   -345    520   -311       O  
ATOM    154  CB  LYS A  46       4.510  45.180  55.003  1.00 96.75           C  
ANISOU  154  CB  LYS A  46    12068  12593  12098   -375    544   -368       C  
ATOM    155  CG  LYS A  46       5.447  46.379  54.982  1.00104.66           C  
ANISOU  155  CG  LYS A  46    13076  13585  13104   -371    536   -379       C  
ATOM    156  CD  LYS A  46       5.220  47.275  56.191  1.00106.71           C  
ANISOU  156  CD  LYS A  46    13340  13852  13350   -396    568   -420       C  
ATOM    157  CE  LYS A  46       5.697  48.695  55.924  1.00107.50           C  
ANISOU  157  CE  LYS A  46    13436  13933  13475   -384    567   -439       C  
ATOM    158  NZ  LYS A  46       5.059  49.682  56.842  1.00107.82           N  
ANISOU  158  NZ  LYS A  46    13471  13973  13522   -400    603   -486       N  
ATOM    159  N   VAL A  47       5.144  42.402  54.299  1.00 85.55           N  
ANISOU  159  N   VAL A  47    10665  11196  10642   -373    496   -289       N  
ATOM    160  CA  VAL A  47       5.102  40.982  54.612  1.00 92.34           C  
ANISOU  160  CA  VAL A  47    11534  12076  11474   -388    489   -263       C  
ATOM    161  C   VAL A  47       4.129  40.752  55.770  1.00105.32           C  
ANISOU  161  C   VAL A  47    13178  13737  13099   -415    523   -288       C  
ATOM    162  O   VAL A  47       4.319  41.320  56.852  1.00110.05           O  
ANISOU  162  O   VAL A  47    13791  14349  13674   -441    541   -311       O  
ATOM    163  CB  VAL A  47       6.485  40.460  55.036  1.00 87.21           C  
ANISOU  163  CB  VAL A  47    10909  11442  10784   -405    464   -236       C  
ATOM    164  CG1 VAL A  47       6.551  38.950  54.874  1.00 87.96           C  
ANISOU  164  CG1 VAL A  47    11009  11548  10864   -408    445   -201       C  
ATOM    165  CG2 VAL A  47       7.586  41.143  54.241  1.00 83.79           C  
ANISOU  165  CG2 VAL A  47    10478  10993  10365   -385    439   -225       C  
ATOM    166  N   PRO A  48       3.076  39.937  55.547  1.00113.85           N  
ANISOU  166  N   PRO A  48    14246  14818  14193   -411    532   -284       N  
ATOM    167  CA  PRO A  48       2.136  39.610  56.625  1.00117.59           C  
ANISOU  167  CA  PRO A  48    14720  15309  14648   -438    564   -304       C  
ATOM    168  C   PRO A  48       2.773  38.712  57.686  1.00118.86           C  
ANISOU  168  C   PRO A  48    14907  15499  14754   -473    559   -286       C  
ATOM    169  O   PRO A  48       3.416  37.712  57.353  1.00115.12           O  
ANISOU  169  O   PRO A  48    14442  15031  14266   -471    529   -249       O  
ATOM    170  CB  PRO A  48       1.000  38.874  55.898  1.00117.08           C  
ANISOU  170  CB  PRO A  48    14634  15235  14614   -420    567   -297       C  
ATOM    171  CG  PRO A  48       1.142  39.258  54.463  1.00114.26           C  
ANISOU  171  CG  PRO A  48    14262  14851  14300   -382    544   -285       C  
ATOM    172  CD  PRO A  48       2.619  39.402  54.253  1.00114.18           C  
ANISOU  172  CD  PRO A  48    14270  14842  14270   -380    515   -263       C  
ATOM    173  N   ASP A  49       2.594  39.088  58.951  1.00123.27           N  
ANISOU  173  N   ASP A  49    15478  16076  15284   -506    587   -313       N  
ATOM    174  CA  ASP A  49       3.203  38.388  60.090  1.00125.02           C  
ANISOU  174  CA  ASP A  49    15726  16325  15450   -544    583   -299       C  
ATOM    175  C   ASP A  49       2.548  37.036  60.386  1.00119.56           C  
ANISOU  175  C   ASP A  49    15036  15650  14742   -559    586   -281       C  
ATOM    176  O   ASP A  49       3.145  36.175  61.044  1.00112.55           O  
ANISOU  176  O   ASP A  49    14169  14782  13813   -585    571   -256       O  
ATOM    177  CB  ASP A  49       3.175  39.278  61.341  1.00129.50           C  
ANISOU  177  CB  ASP A  49    16306  16905  15990   -576    613   -336       C  
ATOM    178  CG  ASP A  49       1.775  39.788  61.671  1.00133.78           C  
ANISOU  178  CG  ASP A  49    16831  17445  16554   -579    658   -378       C  
ATOM    179  OD1 ASP A  49       1.091  40.309  60.761  1.00135.09           O  
ANISOU  179  OD1 ASP A  49    16970  17586  16770   -547    664   -392       O  
ATOM    180  OD2 ASP A  49       1.364  39.676  62.846  1.00134.11           O  
ANISOU  180  OD2 ASP A  49    16884  17507  16562   -615    686   -398       O  
ATOM    181  N   ASP A  50       1.323  36.861  59.894  1.00114.37           N  
ANISOU  181  N   ASP A  50    14354  14981  14118   -542    603   -292       N  
ATOM    182  CA  ASP A  50       0.574  35.614  60.066  1.00108.52           C  
ANISOU  182  CA  ASP A  50    13610  14252  13368   -553    608   -276       C  
ATOM    183  C   ASP A  50       1.056  34.491  59.137  1.00101.77           C  
ANISOU  183  C   ASP A  50    12754  13392  12520   -533    569   -231       C  
ATOM    184  O   ASP A  50       0.389  33.466  58.989  1.00100.28           O  
ANISOU  184  O   ASP A  50    12558  13207  12334   -533    568   -216       O  
ATOM    185  CB  ASP A  50      -0.946  35.852  59.934  1.00109.44           C  
ANISOU  185  CB  ASP A  50    13701  14359  13520   -544    643   -306       C  
ATOM    186  CG  ASP A  50      -1.314  36.771  58.769  1.00108.65           C  
ANISOU  186  CG  ASP A  50    13576  14228  13476   -504    642   -321       C  
ATOM    187  OD1 ASP A  50      -0.743  37.882  58.658  1.00106.23           O  
ANISOU  187  OD1 ASP A  50    13271  13911  13178   -496    640   -337       O  
ATOM    188  OD2 ASP A  50      -2.202  36.387  57.977  1.00104.95           O  
ANISOU  188  OD2 ASP A  50    13086  13746  13044   -482    642   -317       O  
ATOM    189  N   ILE A  51       2.215  34.696  58.515  1.00 99.79           N  
ANISOU  189  N   ILE A  51    12510  13132  12272   -517    536   -210       N  
ATOM    190  CA  ILE A  51       2.896  33.641  57.768  1.00 99.63           C  
ANISOU  190  CA  ILE A  51    12493  13109  12252   -503    499   -168       C  
ATOM    191  C   ILE A  51       3.832  32.911  58.732  1.00 98.36           C  
ANISOU  191  C   ILE A  51    12358  12971  12042   -536    482   -144       C  
ATOM    192  O   ILE A  51       4.741  33.524  59.297  1.00 97.02           O  
ANISOU  192  O   ILE A  51    12206  12808  11849   -551    477   -149       O  
ATOM    193  CB  ILE A  51       3.689  34.185  56.549  1.00 98.05           C  
ANISOU  193  CB  ILE A  51    12286  12886  12082   -468    472   -157       C  
ATOM    194  CG1 ILE A  51       2.748  34.884  55.556  1.00 96.99           C  
ANISOU  194  CG1 ILE A  51    12126  12728  11997   -436    485   -177       C  
ATOM    195  CG2 ILE A  51       4.458  33.061  55.857  1.00 90.39           C  
ANISOU  195  CG2 ILE A  51    11319  11914  11109   -457    435   -114       C  
ATOM    196  CD1 ILE A  51       3.442  35.819  54.587  1.00 95.22           C  
ANISOU  196  CD1 ILE A  51    11897  12482  11800   -408    468   -178       C  
ATOM    197  N   PRO A  52       3.598  31.601  58.936  1.00 99.62           N  
ANISOU  197  N   PRO A  52    12521  13143  12186   -549    473   -119       N  
ATOM    198  CA  PRO A  52       4.422  30.770  59.809  1.00100.37           C  
ANISOU  198  CA  PRO A  52    12640  13259  12237   -581    454    -92       C  
ATOM    199  C   PRO A  52       5.915  31.101  59.754  1.00 97.26           C  
ANISOU  199  C   PRO A  52    12260  12862  11830   -581    424    -76       C  
ATOM    200  O   PRO A  52       6.520  31.077  58.683  1.00 97.38           O  
ANISOU  200  O   PRO A  52    12268  12860  11872   -551    399    -58       O  
ATOM    201  CB  PRO A  52       4.160  29.362  59.272  1.00100.49           C  
ANISOU  201  CB  PRO A  52    12646  13273  12261   -572    435    -59       C  
ATOM    202  CG  PRO A  52       2.738  29.419  58.813  1.00102.24           C  
ANISOU  202  CG  PRO A  52    12846  13486  12514   -555    461    -80       C  
ATOM    203  CD  PRO A  52       2.455  30.841  58.392  1.00 99.40           C  
ANISOU  203  CD  PRO A  52    12474  13110  12183   -535    481   -115       C  
ATOM    204  N   SER A  53       6.487  31.427  60.910  1.00 98.38           N  
ANISOU  204  N   SER A  53    12424  13021  11932   -615    428    -82       N  
ATOM    205  CA  SER A  53       7.919  31.683  61.036  1.00 98.69           C  
ANISOU  205  CA  SER A  53    12480  13060  11956   -620    399    -65       C  
ATOM    206  C   SER A  53       8.683  30.361  60.978  1.00100.91           C  
ANISOU  206  C   SER A  53    12769  13346  12224   -627    362    -20       C  
ATOM    207  O   SER A  53       9.390  29.988  61.922  1.00102.59           O  
ANISOU  207  O   SER A  53    13003  13575  12399   -660    347     -5       O  
ATOM    208  CB  SER A  53       8.219  32.436  62.338  1.00 99.92           C  
ANISOU  208  CB  SER A  53    12658  13233  12072   -657    415    -87       C  
ATOM    209  OG  SER A  53       7.736  31.726  63.467  1.00 98.37           O  
ANISOU  209  OG  SER A  53    12476  13061  11838   -696    427    -85       O  
ATOM    210  N   SER A  54       8.525  29.663  59.854  1.00 98.33           N  
ANISOU  210  N   SER A  54    12425  13005  11930   -597    346      0       N  
ATOM    211  CA  SER A  54       9.066  28.318  59.664  1.00 94.72           C  
ANISOU  211  CA  SER A  54    11970  12549  11468   -599    313     40       C  
ATOM    212  C   SER A  54       9.327  28.009  58.190  1.00 92.36           C  
ANISOU  212  C   SER A  54    11653  12228  11211   -558    293     57       C  
ATOM    213  O   SER A  54       9.980  27.010  57.867  1.00 87.70           O  
ANISOU  213  O   SER A  54    11063  11634  10622   -555    262     90       O  
ATOM    214  CB  SER A  54       8.094  27.288  60.229  1.00 92.99           C  
ANISOU  214  CB  SER A  54    11752  12346  11234   -620    325     46       C  
ATOM    215  OG  SER A  54       6.811  27.467  59.659  1.00 94.47           O  
ANISOU  215  OG  SER A  54    11919  12525  11449   -599    352     25       O  
ATOM    216  N   THR A  55       8.818  28.875  57.312  1.00 90.84           N  
ANISOU  216  N   THR A  55    11444  12019  11051   -528    308     33       N  
ATOM    217  CA  THR A  55       8.879  28.679  55.857  1.00 88.13           C  
ANISOU  217  CA  THR A  55    11083  11653  10747   -489    293     45       C  
ATOM    218  C   THR A  55      10.306  28.753  55.279  1.00 88.68           C  
ANISOU  218  C   THR A  55    11157  11711  10824   -476    262     66       C  
ATOM    219  O   THR A  55      11.196  29.389  55.864  1.00 90.10           O  
ANISOU  219  O   THR A  55    11351  11896  10986   -491    256     63       O  
ATOM    220  CB  THR A  55       7.954  29.664  55.104  1.00 83.99           C  
ANISOU  220  CB  THR A  55    10541  11114  10256   -462    318     15       C  
ATOM    221  OG1 THR A  55       8.636  30.901  54.885  1.00 84.17           O  
ANISOU  221  OG1 THR A  55    10566  11126  10286   -452    317      0       O  
ATOM    222  CG2 THR A  55       6.694  29.934  55.893  1.00 83.05           C  
ANISOU  222  CG2 THR A  55    10419  11006  10128   -479    353    -13       C  
ATOM    223  N   LYS A  56      10.503  28.099  54.132  1.00 83.68           N  
ANISOU  223  N   LYS A  56    10511  11063  10217   -450    242     87       N  
ATOM    224  CA  LYS A  56      11.805  28.049  53.463  1.00 79.61           C  
ANISOU  224  CA  LYS A  56     9998  10536   9714   -436    213    107       C  
ATOM    225  C   LYS A  56      11.807  28.826  52.146  1.00 78.85           C  
ANISOU  225  C   LYS A  56     9888  10418   9652   -400    215     96       C  
ATOM    226  O   LYS A  56      12.858  29.278  51.680  1.00 76.83           O  
ANISOU  226  O   LYS A  56     9634  10151   9404   -390    200    102       O  
ATOM    227  CB  LYS A  56      12.246  26.599  53.222  1.00 79.57           C  
ANISOU  227  CB  LYS A  56     9991  10531   9710   -437    186    142       C  
ATOM    228  CG  LYS A  56      12.318  25.755  54.487  1.00 80.97           C  
ANISOU  228  CG  LYS A  56    10182  10728   9853   -474    180    158       C  
ATOM    229  CD  LYS A  56      13.610  24.958  54.573  1.00 77.72           C  
ANISOU  229  CD  LYS A  56     9778  10316   9437   -482    145    191       C  
ATOM    230  CE  LYS A  56      13.844  24.492  56.002  1.00 76.72           C  
ANISOU  230  CE  LYS A  56     9668  10209   9271   -523    138    203       C  
ATOM    231  NZ  LYS A  56      15.287  24.516  56.370  1.00 77.93           N  
ANISOU  231  NZ  LYS A  56     9833  10361   9414   -536    110    221       N  
ATOM    232  N   ASN A  57      10.626  28.972  51.550  1.00 75.06           N  
ANISOU  232  N   ASN A  57     9394   9930   9193   -383    233     80       N  
ATOM    233  CA  ASN A  57      10.474  29.686  50.289  1.00 69.80           C  
ANISOU  233  CA  ASN A  57     8715   9244   8562   -350    235     70       C  
ATOM    234  C   ASN A  57       9.201  30.506  50.335  1.00 67.41           C  
ANISOU  234  C   ASN A  57     8402   8938   8271   -345    264     39       C  
ATOM    235  O   ASN A  57       8.176  30.034  50.816  1.00 71.22           O  
ANISOU  235  O   ASN A  57     8880   9430   8747   -355    280     33       O  
ATOM    236  CB  ASN A  57      10.425  28.708  49.100  1.00 68.34           C  
ANISOU  236  CB  ASN A  57     8518   9046   8400   -327    217     93       C  
ATOM    237  CG  ASN A  57      11.419  27.559  49.233  1.00 67.48           C  
ANISOU  237  CG  ASN A  57     8416   8942   8279   -337    191    124       C  
ATOM    238  OD1 ASN A  57      12.632  27.744  49.115  1.00 63.63           O  
ANISOU  238  OD1 ASN A  57     7935   8450   7788   -337    173    135       O  
ATOM    239  ND2 ASN A  57      10.901  26.359  49.483  1.00 67.63           N  
ANISOU  239  ND2 ASN A  57     8433   8970   8292   -347    187    139       N  
ATOM    240  N   ILE A  58       9.272  31.739  49.850  1.00 66.78           N  
ANISOU  240  N   ILE A  58     8319   8846   8209   -329    272     20       N  
ATOM    241  CA  ILE A  58       8.090  32.591  49.734  1.00 66.16           C  
ANISOU  241  CA  ILE A  58     8228   8760   8150   -320    298     -9       C  
ATOM    242  C   ILE A  58       8.179  33.481  48.502  1.00 64.58           C  
ANISOU  242  C   ILE A  58     8018   8537   7983   -290    292    -15       C  
ATOM    243  O   ILE A  58       9.228  34.058  48.215  1.00 65.42           O  
ANISOU  243  O   ILE A  58     8130   8635   8088   -284    279    -11       O  
ATOM    244  CB  ILE A  58       7.818  33.422  51.021  1.00 70.84           C  
ANISOU  244  CB  ILE A  58     8828   9366   8722   -344    323    -37       C  
ATOM    245  CG1 ILE A  58       6.873  34.596  50.734  1.00 75.50           C  
ANISOU  245  CG1 ILE A  58     9403   9941   9339   -330    347    -70       C  
ATOM    246  CG2 ILE A  58       9.107  33.934  51.641  1.00 69.83           C  
ANISOU  246  CG2 ILE A  58     8718   9244   8570   -360    313    -34       C  
ATOM    247  CD1 ILE A  58       6.033  35.018  51.923  1.00 81.19           C  
ANISOU  247  CD1 ILE A  58    10125  10675  10045   -354    379    -99       C  
ATOM    248  N   ASP A  59       7.075  33.563  47.768  1.00 63.52           N  
ANISOU  248  N   ASP A  59     7867   8389   7877   -271    301    -25       N  
ATOM    249  CA  ASP A  59       6.978  34.460  46.629  1.00 63.38           C  
ANISOU  249  CA  ASP A  59     7838   8349   7892   -244    298    -33       C  
ATOM    250  C   ASP A  59       6.059  35.624  46.973  1.00 63.02           C  
ANISOU  250  C   ASP A  59     7784   8298   7863   -244    324    -66       C  
ATOM    251  O   ASP A  59       4.852  35.446  47.122  1.00 63.90           O  
ANISOU  251  O   ASP A  59     7883   8408   7986   -244    341    -79       O  
ATOM    252  CB  ASP A  59       6.485  33.717  45.377  1.00 61.67           C  
ANISOU  252  CB  ASP A  59     7610   8119   7700   -222    284    -16       C  
ATOM    253  CG  ASP A  59       6.235  34.653  44.197  1.00 63.54           C  
ANISOU  253  CG  ASP A  59     7837   8333   7971   -196    281    -24       C  
ATOM    254  OD1 ASP A  59       7.047  35.577  43.966  1.00 63.56           O  
ANISOU  254  OD1 ASP A  59     7845   8328   7976   -191    275    -28       O  
ATOM    255  OD2 ASP A  59       5.219  34.468  43.496  1.00 65.02           O  
ANISOU  255  OD2 ASP A  59     8010   8509   8183   -182    283    -26       O  
ATOM    256  N   LEU A  60       6.646  36.812  47.095  1.00 62.19           N  
ANISOU  256  N   LEU A  60     7683   8186   7759   -243    326    -81       N  
ATOM    257  CA  LEU A  60       5.902  38.033  47.397  1.00 59.96           C  
ANISOU  257  CA  LEU A  60     7390   7895   7494   -242    350   -115       C  
ATOM    258  C   LEU A  60       5.783  38.977  46.203  1.00 61.81           C  
ANISOU  258  C   LEU A  60     7613   8104   7767   -215    342   -120       C  
ATOM    259  O   LEU A  60       5.435  40.148  46.374  1.00 65.01           O  
ANISOU  259  O   LEU A  60     8011   8500   8189   -213    357   -146       O  
ATOM    260  CB  LEU A  60       6.547  38.772  48.575  1.00 58.37           C  
ANISOU  260  CB  LEU A  60     7203   7707   7267   -265    361   -132       C  
ATOM    261  CG  LEU A  60       6.182  38.311  49.987  1.00 58.03           C  
ANISOU  261  CG  LEU A  60     7168   7687   7192   -296    382   -143       C  
ATOM    262  CD1 LEU A  60       7.263  38.694  50.990  1.00 56.50           C  
ANISOU  262  CD1 LEU A  60     6994   7507   6964   -319    381   -146       C  
ATOM    263  CD2 LEU A  60       4.832  38.880  50.396  1.00 57.66           C  
ANISOU  263  CD2 LEU A  60     7107   7637   7164   -298    413   -176       C  
ATOM    264  N   SER A  61       6.059  38.472  45.000  1.00 62.66           N  
ANISOU  264  N   SER A  61     7719   8201   7887   -196    319    -96       N  
ATOM    265  CA  SER A  61       6.049  39.302  43.785  1.00 62.23           C  
ANISOU  265  CA  SER A  61     7655   8122   7866   -171    308    -96       C  
ATOM    266  C   SER A  61       4.714  40.011  43.528  1.00 61.96           C  
ANISOU  266  C   SER A  61     7602   8072   7868   -160    323   -119       C  
ATOM    267  O   SER A  61       3.694  39.655  44.114  1.00 61.46           O  
ANISOU  267  O   SER A  61     7530   8015   7807   -169    342   -132       O  
ATOM    268  CB  SER A  61       6.475  38.490  42.554  1.00 62.66           C  
ANISOU  268  CB  SER A  61     7712   8169   7925   -155    282    -66       C  
ATOM    269  OG  SER A  61       5.695  37.319  42.392  1.00 63.72           O  
ANISOU  269  OG  SER A  61     7840   8308   8061   -154    281    -55       O  
ATOM    270  N   PHE A  62       4.745  41.021  42.660  1.00 63.44           N  
ANISOU  270  N   PHE A  62     7783   8238   8084   -143    315   -124       N  
ATOM    271  CA  PHE A  62       3.550  41.789  42.243  1.00 65.03           C  
ANISOU  271  CA  PHE A  62     7963   8418   8325   -129    325   -144       C  
ATOM    272  C   PHE A  62       2.702  42.351  43.390  1.00 66.71           C  
ANISOU  272  C   PHE A  62     8167   8636   8544   -143    356   -178       C  
ATOM    273  O   PHE A  62       1.469  42.300  43.352  1.00 68.70           O  
ANISOU  273  O   PHE A  62     8401   8879   8821   -139    368   -191       O  
ATOM    274  CB  PHE A  62       2.692  40.990  41.247  1.00 61.13           C  
ANISOU  274  CB  PHE A  62     7458   7914   7852   -114    313   -128       C  
ATOM    275  CG  PHE A  62       3.345  40.793  39.909  1.00 59.05           C  
ANISOU  275  CG  PHE A  62     7201   7638   7594    -97    285   -102       C  
ATOM    276  CD1 PHE A  62       4.217  39.728  39.693  1.00 57.79           C  
ANISOU  276  CD1 PHE A  62     7056   7493   7407   -101    270    -76       C  
ATOM    277  CD2 PHE A  62       3.095  41.676  38.864  1.00 56.83           C  
ANISOU  277  CD2 PHE A  62     6911   7333   7347    -79    273   -103       C  
ATOM    278  CE1 PHE A  62       4.822  39.549  38.459  1.00 55.80           C  
ANISOU  278  CE1 PHE A  62     6809   7230   7160    -86    246    -53       C  
ATOM    279  CE2 PHE A  62       3.699  41.500  37.629  1.00 56.33           C  
ANISOU  279  CE2 PHE A  62     6856   7260   7287    -66    248    -79       C  
ATOM    280  CZ  PHE A  62       4.562  40.435  37.426  1.00 55.37           C  
ANISOU  280  CZ  PHE A  62     6748   7152   7136    -70    236    -55       C  
ATOM    281  N   ASN A  63       3.386  42.884  44.402  1.00 69.61           N  
ANISOU  281  N   ASN A  63     8545   9015   8887   -160    368   -192       N  
ATOM    282  CA  ASN A  63       2.759  43.573  45.533  1.00 69.29           C  
ANISOU  282  CA  ASN A  63     8498   8979   8848   -175    398   -227       C  
ATOM    283  C   ASN A  63       3.305  44.995  45.687  1.00 70.81           C  
ANISOU  283  C   ASN A  63     8692   9161   9052   -174    402   -247       C  
ATOM    284  O   ASN A  63       4.507  45.205  45.534  1.00 69.83           O  
ANISOU  284  O   ASN A  63     8582   9039   8909   -175    385   -233       O  
ATOM    285  CB  ASN A  63       3.005  42.792  46.824  1.00 65.17           C  
ANISOU  285  CB  ASN A  63     7991   8486   8283   -203    413   -228       C  
ATOM    286  CG  ASN A  63       2.232  41.494  46.875  1.00 63.16           C  
ANISOU  286  CG  ASN A  63     7732   8242   8022   -207    416   -216       C  
ATOM    287  OD1 ASN A  63       1.033  41.469  46.614  1.00 63.48           O  
ANISOU  287  OD1 ASN A  63     7754   8272   8092   -199    427   -227       O  
ATOM    288  ND2 ASN A  63       2.911  40.411  47.223  1.00 58.73           N  
ANISOU  288  ND2 ASN A  63     7187   7701   7424   -220    405   -192       N  
ATOM    289  N   PRO A  64       2.431  45.978  45.985  1.00 72.58           N  
ANISOU  289  N   PRO A  64     8899   9371   9306   -173    423   -279       N  
ATOM    290  CA  PRO A  64       2.943  47.321  46.280  1.00 72.31           C  
ANISOU  290  CA  PRO A  64     8866   9328   9280   -174    429   -300       C  
ATOM    291  C   PRO A  64       3.714  47.381  47.608  1.00 69.83           C  
ANISOU  291  C   PRO A  64     8570   9037   8922   -201    443   -312       C  
ATOM    292  O   PRO A  64       3.223  47.953  48.582  1.00 70.51           O  
ANISOU  292  O   PRO A  64     8653   9128   9009   -216    471   -345       O  
ATOM    293  CB  PRO A  64       1.670  48.184  46.342  1.00 74.49           C  
ANISOU  293  CB  PRO A  64     9116   9584   9600   -168    450   -333       C  
ATOM    294  CG  PRO A  64       0.615  47.397  45.642  1.00 71.72           C  
ANISOU  294  CG  PRO A  64     8750   9225   9273   -155    446   -322       C  
ATOM    295  CD  PRO A  64       0.959  45.959  45.888  1.00 73.73           C  
ANISOU  295  CD  PRO A  64     9022   9505   9486   -166    440   -296       C  
ATOM    296  N   LEU A  65       4.910  46.793  47.633  1.00 68.36           N  
ANISOU  296  N   LEU A  65     8405   8866   8700   -208    424   -286       N  
ATOM    297  CA  LEU A  65       5.762  46.779  48.824  1.00 67.80           C  
ANISOU  297  CA  LEU A  65     8355   8819   8587   -234    432   -292       C  
ATOM    298  C   LEU A  65       6.452  48.121  49.046  1.00 71.60           C  
ANISOU  298  C   LEU A  65     8840   9291   9074   -235    433   -310       C  
ATOM    299  O   LEU A  65       6.605  48.562  50.186  1.00 76.03           O  
ANISOU  299  O   LEU A  65     9409   9864   9614   -257    453   -333       O  
ATOM    300  CB  LEU A  65       6.805  45.667  48.741  1.00 64.53           C  
ANISOU  300  CB  LEU A  65     7960   8421   8137   -240    408   -256       C  
ATOM    301  CG  LEU A  65       6.346  44.218  48.904  1.00 64.70           C  
ANISOU  301  CG  LEU A  65     7983   8459   8139   -248    408   -238       C  
ATOM    302  CD1 LEU A  65       7.549  43.289  48.877  1.00 62.62           C  
ANISOU  302  CD1 LEU A  65     7739   8210   7842   -255    384   -204       C  
ATOM    303  CD2 LEU A  65       5.551  44.012  50.185  1.00 63.48           C  
ANISOU  303  CD2 LEU A  65     7829   8321   7966   -273    439   -262       C  
ATOM    304  N   LYS A  66       6.881  48.745  47.951  1.00 71.50           N  
ANISOU  304  N   LYS A  66     8822   9257   9088   -213    413   -299       N  
ATOM    305  CA  LYS A  66       7.344  50.143  47.928  1.00 70.05           C  
ANISOU  305  CA  LYS A  66     8637   9058   8922   -208    413   -317       C  
ATOM    306  C   LYS A  66       8.670  50.425  48.666  1.00 69.11           C  
ANISOU  306  C   LYS A  66     8538   8952   8766   -225    408   -315       C  
ATOM    307  O   LYS A  66       9.596  50.988  48.082  1.00 71.18           O  
ANISOU  307  O   LYS A  66     8806   9204   9035   -215    389   -303       O  
ATOM    308  CB  LYS A  66       6.216  51.101  48.370  1.00 69.70           C  
ANISOU  308  CB  LYS A  66     8572   9000   8908   -209    441   -357       C  
ATOM    309  CG  LYS A  66       5.019  51.170  47.419  1.00 70.71           C  
ANISOU  309  CG  LYS A  66     8676   9105   9084   -186    441   -359       C  
ATOM    310  CD  LYS A  66       5.287  52.071  46.212  1.00 73.45           C  
ANISOU  310  CD  LYS A  66     9014   9423   9468   -162    419   -350       C  
ATOM    311  CE  LYS A  66       4.264  51.902  45.085  1.00 70.90           C  
ANISOU  311  CE  LYS A  66     8671   9080   9187   -140    409   -341       C  
ATOM    312  NZ  LYS A  66       3.061  52.783  45.165  1.00 69.51           N  
ANISOU  312  NZ  LYS A  66     8469   8882   9057   -133    428   -373       N  
ATOM    313  N   ILE A  67       8.749  50.044  49.940  1.00 68.44           N  
ANISOU  313  N   ILE A  67     8466   8891   8645   -252    425   -327       N  
ATOM    314  CA  ILE A  67       9.954  50.216  50.753  1.00 67.29           C  
ANISOU  314  CA  ILE A  67     8342   8760   8462   -272    419   -325       C  
ATOM    315  C   ILE A  67      10.230  48.900  51.465  1.00 65.44           C  
ANISOU  315  C   ILE A  67     8124   8553   8184   -294    417   -306       C  
ATOM    316  O   ILE A  67       9.304  48.221  51.906  1.00 67.89           O  
ANISOU  316  O   ILE A  67     8430   8875   8488   -303    434   -313       O  
ATOM    317  CB  ILE A  67       9.778  51.322  51.824  1.00 71.81           C  
ANISOU  317  CB  ILE A  67     8915   9335   9033   -290    445   -365       C  
ATOM    318  CG1 ILE A  67       9.243  52.617  51.203  1.00 71.72           C  
ANISOU  318  CG1 ILE A  67     8883   9294   9070   -269    452   -388       C  
ATOM    319  CG2 ILE A  67      11.092  51.592  52.555  1.00 70.66           C  
ANISOU  319  CG2 ILE A  67     8792   9202   8852   -309    436   -361       C  
ATOM    320  CD1 ILE A  67       8.160  53.291  52.020  1.00 72.67           C  
ANISOU  320  CD1 ILE A  67     8991   9413   9206   -280    487   -431       C  
ATOM    321  N   LEU A  68      11.501  48.536  51.576  1.00 65.74           N  
ANISOU  321  N   LEU A  68     8180   8602   8194   -302    395   -282       N  
ATOM    322  CA  LEU A  68      11.885  47.352  52.335  1.00 67.52           C  
ANISOU  322  CA  LEU A  68     8423   8853   8379   -325    390   -263       C  
ATOM    323  C   LEU A  68      12.333  47.741  53.735  1.00 69.64           C  
ANISOU  323  C   LEU A  68     8709   9139   8612   -356    403   -282       C  
ATOM    324  O   LEU A  68      13.527  47.774  54.041  1.00 68.23           O  
ANISOU  324  O   LEU A  68     8546   8966   8410   -367    385   -268       O  
ATOM    325  CB  LEU A  68      12.956  46.543  51.598  1.00 68.45           C  
ANISOU  325  CB  LEU A  68     8549   8971   8488   -315    357   -223       C  
ATOM    326  CG  LEU A  68      12.525  45.237  50.918  1.00 68.32           C  
ANISOU  326  CG  LEU A  68     8526   8956   8475   -305    347   -196       C  
ATOM    327  CD1 LEU A  68      11.067  45.249  50.475  1.00 66.61           C  
ANISOU  327  CD1 LEU A  68     8289   8729   8287   -291    365   -212       C  
ATOM    328  CD2 LEU A  68      13.443  44.924  49.747  1.00 68.70           C  
ANISOU  328  CD2 LEU A  68     8574   8992   8534   -285    318   -165       C  
ATOM    329  N   LYS A  69      11.338  48.039  54.568  1.00 72.94           N  
ANISOU  329  N   LYS A  69     9122   9563   9026   -371    434   -314       N  
ATOM    330  CA  LYS A  69      11.525  48.468  55.951  1.00 73.64           C  
ANISOU  330  CA  LYS A  69     9227   9669   9083   -403    452   -339       C  
ATOM    331  C   LYS A  69      12.517  47.568  56.685  1.00 73.21           C  
ANISOU  331  C   LYS A  69     9197   9637   8980   -429    434   -313       C  
ATOM    332  O   LYS A  69      12.540  46.353  56.477  1.00 74.09           O  
ANISOU  332  O   LYS A  69     9312   9759   9080   -430    420   -284       O  
ATOM    333  CB  LYS A  69      10.176  48.462  56.677  1.00 75.10           C  
ANISOU  333  CB  LYS A  69     9404   9861   9267   -417    488   -371       C  
ATOM    334  CG  LYS A  69       9.949  49.646  57.604  1.00 78.42           C  
ANISOU  334  CG  LYS A  69     9827  10283   9686   -435    517   -414       C  
ATOM    335  CD  LYS A  69       9.072  50.716  56.962  1.00 78.59           C  
ANISOU  335  CD  LYS A  69     9822  10277   9759   -410    534   -443       C  
ATOM    336  CE  LYS A  69       9.159  52.043  57.710  1.00 82.41           C  
ANISOU  336  CE  LYS A  69    10308  10757  10245   -423    555   -483       C  
ATOM    337  NZ  LYS A  69       8.721  51.977  59.137  1.00 81.52           N  
ANISOU  337  NZ  LYS A  69    10207  10667  10097   -459    587   -512       N  
ATOM    338  N   SER A  70      13.337  48.179  57.536  1.00 71.34           N  
ANISOU  338  N   SER A  70     8977   9409   8719   -450    433   -323       N  
ATOM    339  CA  SER A  70      14.354  47.461  58.292  1.00 69.82           C  
ANISOU  339  CA  SER A  70     8808   9236   8481   -477    414   -300       C  
ATOM    340  C   SER A  70      13.724  46.365  59.137  1.00 68.13           C  
ANISOU  340  C   SER A  70     8604   9046   8236   -503    426   -296       C  
ATOM    341  O   SER A  70      12.681  46.575  59.744  1.00 70.90           O  
ANISOU  341  O   SER A  70     8951   9404   8584   -515    458   -326       O  
ATOM    342  CB  SER A  70      15.122  48.432  59.185  1.00 70.57           C  
ANISOU  342  CB  SER A  70     8920   9336   8556   -498    417   -319       C  
ATOM    343  OG  SER A  70      16.385  47.903  59.533  1.00 74.44           O  
ANISOU  343  OG  SER A  70     9429   9837   9016   -514    387   -289       O  
ATOM    344  N   TYR A  71      14.358  45.194  59.159  1.00 70.21           N  
ANISOU  344  N   TYR A  71     8879   9321   8477   -511    400   -259       N  
ATOM    345  CA  TYR A  71      13.906  44.039  59.962  1.00 71.64           C  
ANISOU  345  CA  TYR A  71     9070   9525   8624   -538    406   -248       C  
ATOM    346  C   TYR A  71      12.673  43.290  59.429  1.00 71.76           C  
ANISOU  346  C   TYR A  71     9067   9537   8658   -523    419   -247       C  
ATOM    347  O   TYR A  71      12.283  42.267  60.001  1.00 68.45           O  
ANISOU  347  O   TYR A  71     8656   9137   8214   -544    423   -235       O  
ATOM    348  CB  TYR A  71      13.709  44.426  61.441  1.00 70.93           C  
ANISOU  348  CB  TYR A  71     8998   9455   8494   -578    429   -276       C  
ATOM    349  CG  TYR A  71      14.954  44.997  62.063  1.00 73.51           C  
ANISOU  349  CG  TYR A  71     9345   9786   8797   -596    413   -274       C  
ATOM    350  CD1 TYR A  71      15.107  46.374  62.237  1.00 73.02           C  
ANISOU  350  CD1 TYR A  71     9283   9715   8745   -594    427   -307       C  
ATOM    351  CD2 TYR A  71      15.999  44.162  62.453  1.00 75.52           C  
ANISOU  351  CD2 TYR A  71     9619  10053   9020   -615    382   -240       C  
ATOM    352  CE1 TYR A  71      16.262  46.899  62.792  1.00 72.22           C  
ANISOU  352  CE1 TYR A  71     9200   9617   8622   -611    410   -304       C  
ATOM    353  CE2 TYR A  71      17.161  44.676  63.007  1.00 75.37           C  
ANISOU  353  CE2 TYR A  71     9618  10037   8980   -632    364   -236       C  
ATOM    354  CZ  TYR A  71      17.289  46.041  63.174  1.00 74.05           C  
ANISOU  354  CZ  TYR A  71     9451   9862   8823   -630    379   -269       C  
ATOM    355  OH  TYR A  71      18.449  46.531  63.725  1.00 74.52           O  
ANISOU  355  OH  TYR A  71     9528   9924   8861   -647    361   -265       O  
ATOM    356  N   SER A  72      12.082  43.784  58.335  1.00 71.77           N  
ANISOU  356  N   SER A  72     9046   9518   8705   -489    426   -256       N  
ATOM    357  CA  SER A  72      10.879  43.182  57.729  1.00 70.80           C  
ANISOU  357  CA  SER A  72     8904   9389   8606   -473    438   -256       C  
ATOM    358  C   SER A  72      10.851  41.660  57.824  1.00 69.46           C  
ANISOU  358  C   SER A  72     8740   9234   8415   -483    423   -223       C  
ATOM    359  O   SER A  72       9.836  41.074  58.196  1.00 69.63           O  
ANISOU  359  O   SER A  72     8758   9267   8431   -493    443   -230       O  
ATOM    360  CB  SER A  72      10.735  43.594  56.256  1.00 71.13           C  
ANISOU  360  CB  SER A  72     8925   9404   8697   -432    427   -251       C  
ATOM    361  OG  SER A  72      10.037  44.821  56.105  1.00 69.59           O  
ANISOU  361  OG  SER A  72     8714   9193   8531   -420    451   -286       O  
ATOM    362  N   PHE A  73      11.981  41.037  57.503  1.00 69.42           N  
ANISOU  362  N   PHE A  73     8745   9230   8400   -480    390   -188       N  
ATOM    363  CA  PHE A  73      12.074  39.588  57.387  1.00 70.26           C  
ANISOU  363  CA  PHE A  73     8854   9346   8493   -485    371   -154       C  
ATOM    364  C   PHE A  73      12.805  38.936  58.554  1.00 72.94           C  
ANISOU  364  C   PHE A  73     9218   9708   8787   -521    359   -137       C  
ATOM    365  O   PHE A  73      13.110  37.745  58.503  1.00 77.23           O  
ANISOU  365  O   PHE A  73     9766  10259   9319   -527    338   -105       O  
ATOM    366  CB  PHE A  73      12.780  39.212  56.078  1.00 68.96           C  
ANISOU  366  CB  PHE A  73     8680   9164   8355   -454    341   -123       C  
ATOM    367  CG  PHE A  73      12.134  39.783  54.846  1.00 67.31           C  
ANISOU  367  CG  PHE A  73     8450   8932   8191   -418    348   -135       C  
ATOM    368  CD1 PHE A  73      11.097  39.105  54.210  1.00 65.47           C  
ANISOU  368  CD1 PHE A  73     8201   8694   7978   -403    354   -130       C  
ATOM    369  CD2 PHE A  73      12.568  40.991  54.314  1.00 66.38           C  
ANISOU  369  CD2 PHE A  73     8328   8798   8096   -401    346   -148       C  
ATOM    370  CE1 PHE A  73      10.501  39.626  53.072  1.00 65.40           C  
ANISOU  370  CE1 PHE A  73     8174   8665   8011   -372    358   -139       C  
ATOM    371  CE2 PHE A  73      11.972  41.517  53.176  1.00 68.43           C  
ANISOU  371  CE2 PHE A  73     8568   9036   8396   -370    350   -157       C  
ATOM    372  CZ  PHE A  73      10.936  40.834  52.556  1.00 65.34           C  
ANISOU  372  CZ  PHE A  73     8162   8639   8024   -355    356   -152       C  
ATOM    373  N   SER A  74      13.083  39.705  59.602  1.00 76.52           N  
ANISOU  373  N   SER A  74     9687  10172   9214   -548    371   -159       N  
ATOM    374  CA  SER A  74      13.849  39.200  60.748  1.00 79.38           C  
ANISOU  374  CA  SER A  74    10074  10555   9530   -585    358   -144       C  
ATOM    375  C   SER A  74      13.253  37.940  61.381  1.00 80.13           C  
ANISOU  375  C   SER A  74    10176  10670   9599   -609    361   -129       C  
ATOM    376  O   SER A  74      13.984  37.111  61.928  1.00 76.18           O  
ANISOU  376  O   SER A  74     9692  10183   9070   -631    337   -101       O  
ATOM    377  CB  SER A  74      14.015  40.286  61.809  1.00 81.20           C  
ANISOU  377  CB  SER A  74    10319  10795   9735   -611    376   -176       C  
ATOM    378  OG  SER A  74      14.889  39.848  62.831  1.00 85.23           O  
ANISOU  378  OG  SER A  74    10855  11323  10203   -646    358   -158       O  
ATOM    379  N   ASN A  75      11.928  37.811  61.297  1.00 85.77           N  
ANISOU  379  N   ASN A  75    10876  11386  10325   -604    389   -148       N  
ATOM    380  CA  ASN A  75      11.207  36.646  61.810  1.00 91.54           C  
ANISOU  380  CA  ASN A  75    11610  12133  11035   -624    396   -136       C  
ATOM    381  C   ASN A  75      11.618  35.335  61.124  1.00 94.73           C  
ANISOU  381  C   ASN A  75    12010  12534  11447   -611    363    -93       C  
ATOM    382  O   ASN A  75      12.162  34.437  61.776  1.00 94.82           O  
ANISOU  382  O   ASN A  75    12038  12560  11428   -637    343    -66       O  
ATOM    383  CB  ASN A  75       9.683  36.862  61.719  1.00 92.48           C  
ANISOU  383  CB  ASN A  75    11712  12251  11173   -616    434   -167       C  
ATOM    384  CG  ASN A  75       9.101  37.528  62.961  1.00 92.23           C  
ANISOU  384  CG  ASN A  75    11693  12236  11114   -649    470   -204       C  
ATOM    385  OD1 ASN A  75       9.502  37.233  64.088  1.00 91.89           O  
ANISOU  385  OD1 ASN A  75    11673  12214  11026   -688    468   -199       O  
ATOM    386  ND2 ASN A  75       8.134  38.417  62.758  1.00 89.14           N  
ANISOU  386  ND2 ASN A  75    11284  11833  10749   -636    503   -242       N  
ATOM    387  N   PHE A  76      11.371  35.245  59.813  1.00 94.43           N  
ANISOU  387  N   PHE A  76    11951  12476  11452   -572    356    -86       N  
ATOM    388  CA  PHE A  76      11.613  34.020  59.038  1.00 92.78           C  
ANISOU  388  CA  PHE A  76    11734  12261  11255   -557    329    -48       C  
ATOM    389  C   PHE A  76      13.105  33.781  58.839  1.00 93.68           C  
ANISOU  389  C   PHE A  76    11858  12371  11365   -556    292    -18       C  
ATOM    390  O   PHE A  76      13.689  34.246  57.861  1.00 94.97           O  
ANISOU  390  O   PHE A  76    12012  12516  11556   -528    279    -14       O  
ATOM    391  CB  PHE A  76      10.913  34.072  57.670  1.00 89.00           C  
ANISOU  391  CB  PHE A  76    11231  11762  10822   -517    334    -52       C  
ATOM    392  CG  PHE A  76       9.674  34.925  57.643  1.00 89.92           C  
ANISOU  392  CG  PHE A  76    11334  11874  10957   -509    370    -90       C  
ATOM    393  CD1 PHE A  76       8.479  34.469  58.197  1.00 89.92           C  
ANISOU  393  CD1 PHE A  76    11330  11885  10948   -524    395   -102       C  
ATOM    394  CD2 PHE A  76       9.698  36.184  57.048  1.00 89.15           C  
ANISOU  394  CD2 PHE A  76    11227  11759  10887   -486    378   -113       C  
ATOM    395  CE1 PHE A  76       7.336  35.258  58.167  1.00 90.02           C  
ANISOU  395  CE1 PHE A  76    11329  11892  10982   -516    429   -138       C  
ATOM    396  CE2 PHE A  76       8.559  36.976  57.013  1.00 88.02           C  
ANISOU  396  CE2 PHE A  76    11070  11609  10764   -479    410   -148       C  
ATOM    397  CZ  PHE A  76       7.376  36.511  57.572  1.00 91.55           C  
ANISOU  397  CZ  PHE A  76    11512  12067  11205   -493    436   -161       C  
ATOM    398  N   SER A  77      13.711  33.048  59.767  1.00 94.73           N  
ANISOU  398  N   SER A  77    12009  12520  11462   -588    275      2       N  
ATOM    399  CA  SER A  77      15.156  32.830  59.765  1.00 96.02           C  
ANISOU  399  CA  SER A  77    12183  12680  11619   -592    239     30       C  
ATOM    400  C   SER A  77      15.610  31.678  58.864  1.00 94.54           C  
ANISOU  400  C   SER A  77    11984  12482  11453   -573    209     66       C  
ATOM    401  O   SER A  77      16.768  31.635  58.445  1.00 93.49           O  
ANISOU  401  O   SER A  77    11853  12339  11330   -563    182     86       O  
ATOM    402  CB  SER A  77      15.651  32.594  61.192  1.00103.50           C  
ANISOU  402  CB  SER A  77    13155  13649  12520   -637    231     37       C  
ATOM    403  OG  SER A  77      15.097  31.403  61.727  1.00109.55           O  
ANISOU  403  OG  SER A  77    13926  14430  13267   -658    230     54       O  
ATOM    404  N   GLU A  78      14.698  30.753  58.571  1.00 95.22           N  
ANISOU  404  N   GLU A  78    12061  12571  11548   -567    216     74       N  
ATOM    405  CA  GLU A  78      15.035  29.532  57.829  1.00 93.01           C  
ANISOU  405  CA  GLU A  78    11770  12282  11284   -552    189    108       C  
ATOM    406  C   GLU A  78      14.783  29.677  56.328  1.00 88.58           C  
ANISOU  406  C   GLU A  78    11188  11699  10767   -510    190    105       C  
ATOM    407  O   GLU A  78      14.936  28.717  55.563  1.00 86.69           O  
ANISOU  407  O   GLU A  78    10940  11452  10547   -494    172    130       O  
ATOM    408  CB  GLU A  78      14.232  28.355  58.370  1.00 95.60           C  
ANISOU  408  CB  GLU A  78    12100  12625  11596   -572    192    121       C  
ATOM    409  CG  GLU A  78      14.072  28.358  59.876  1.00 97.83           C  
ANISOU  409  CG  GLU A  78    12403  12931  11834   -615    202    115       C  
ATOM    410  CD  GLU A  78      12.657  28.026  60.282  1.00103.25           C  
ANISOU  410  CD  GLU A  78    13087  13630  12511   -626    231    100       C  
ATOM    411  OE1 GLU A  78      12.093  28.762  61.117  1.00101.51           O  
ANISOU  411  OE1 GLU A  78    12876  13423  12268   -647    260     71       O  
ATOM    412  OE2 GLU A  78      12.103  27.041  59.748  1.00107.51           O  
ANISOU  412  OE2 GLU A  78    13615  14167  13067   -614    227    116       O  
ATOM    413  N   LEU A  79      14.400  30.886  55.926  1.00 81.79           N  
ANISOU  413  N   LEU A  79    10322  10831   9923   -493    211     76       N  
ATOM    414  CA  LEU A  79      14.110  31.216  54.538  1.00 74.07           C  
ANISOU  414  CA  LEU A  79     9325   9832   8984   -454    214     70       C  
ATOM    415  C   LEU A  79      15.316  30.976  53.636  1.00 72.40           C  
ANISOU  415  C   LEU A  79     9111   9605   8791   -436    185     94       C  
ATOM    416  O   LEU A  79      16.460  31.231  54.026  1.00 72.57           O  
ANISOU  416  O   LEU A  79     9143   9628   8801   -447    168    103       O  
ATOM    417  CB  LEU A  79      13.661  32.674  54.444  1.00 71.30           C  
ANISOU  417  CB  LEU A  79     8971   9474   8643   -444    239     35       C  
ATOM    418  CG  LEU A  79      12.575  33.063  53.446  1.00 69.72           C  
ANISOU  418  CG  LEU A  79     8751   9259   8477   -415    257     17       C  
ATOM    419  CD1 LEU A  79      11.383  32.132  53.567  1.00 72.50           C  
ANISOU  419  CD1 LEU A  79     9097   9620   8829   -419    270     19       C  
ATOM    420  CD2 LEU A  79      12.139  34.503  53.668  1.00 69.23           C  
ANISOU  420  CD2 LEU A  79     8688   9194   8421   -413    282    -18       C  
ATOM    421  N   GLN A  80      15.044  30.474  52.434  1.00 67.43           N  
ANISOU  421  N   GLN A  80     8467   8962   8192   -408    179    104       N  
ATOM    422  CA  GLN A  80      16.081  30.133  51.469  1.00 62.13           C  
ANISOU  422  CA  GLN A  80     7789   8275   7539   -389    153    126       C  
ATOM    423  C   GLN A  80      15.865  30.806  50.125  1.00 57.19           C  
ANISOU  423  C   GLN A  80     7150   7630   6947   -355    159    115       C  
ATOM    424  O   GLN A  80      16.826  31.051  49.409  1.00 54.66           O  
ANISOU  424  O   GLN A  80     6828   7297   6641   -341    144    124       O  
ATOM    425  CB  GLN A  80      16.124  28.629  51.257  1.00 64.10           C  
ANISOU  425  CB  GLN A  80     8035   8527   7792   -390    135    155       C  
ATOM    426  CG  GLN A  80      17.055  27.883  52.190  1.00 66.34           C  
ANISOU  426  CG  GLN A  80     8330   8821   8053   -417    113    179       C  
ATOM    427  CD  GLN A  80      17.321  26.467  51.712  1.00 68.98           C  
ANISOU  427  CD  GLN A  80     8657   9150   8400   -412     90    209       C  
ATOM    428  OE1 GLN A  80      16.395  25.731  51.341  1.00 68.70           O  
ANISOU  428  OE1 GLN A  80     8613   9115   8374   -404     97    212       O  
ATOM    429  NE2 GLN A  80      18.592  26.077  51.710  1.00 68.95           N  
ANISOU  429  NE2 GLN A  80     8656   9141   8399   -416     64    231       N  
ATOM    430  N   TRP A  81      14.604  31.107  49.809  1.00 56.24           N  
ANISOU  430  N   TRP A  81     7021   7507   6838   -344    181     96       N  
ATOM    431  CA  TRP A  81      14.192  31.604  48.495  1.00 55.94           C  
ANISOU  431  CA  TRP A  81     6970   7451   6833   -312    186     87       C  
ATOM    432  C   TRP A  81      13.137  32.660  48.645  1.00 54.38           C  
ANISOU  432  C   TRP A  81     6767   7252   6642   -309    212     56       C  
ATOM    433  O   TRP A  81      12.021  32.368  49.070  1.00 55.28           O  
ANISOU  433  O   TRP A  81     6877   7374   6752   -316    229     46       O  
ATOM    434  CB  TRP A  81      13.654  30.437  47.663  1.00 60.14           C  
ANISOU  434  CB  TRP A  81     7491   7978   7381   -298    178    104       C  
ATOM    435  CG  TRP A  81      13.325  30.737  46.213  1.00 61.42           C  
ANISOU  435  CG  TRP A  81     7640   8120   7575   -267    178    101       C  
ATOM    436  CD1 TRP A  81      14.167  30.616  45.112  1.00 61.32           C  
ANISOU  436  CD1 TRP A  81     7626   8094   7579   -249    160    116       C  
ATOM    437  CD2 TRP A  81      12.032  31.185  45.654  1.00 61.61           C  
ANISOU  437  CD2 TRP A  81     7653   8137   7619   -251    195     83       C  
ATOM    438  NE1 TRP A  81      13.516  30.963  43.956  1.00 61.38           N  
ANISOU  438  NE1 TRP A  81     7622   8085   7611   -225    165    108       N  
ATOM    439  CE2 TRP A  81      12.236  31.311  44.206  1.00 60.71           C  
ANISOU  439  CE2 TRP A  81     7531   8003   7531   -225    184     89       C  
ATOM    440  CE3 TRP A  81      10.782  31.493  46.190  1.00 62.29           C  
ANISOU  440  CE3 TRP A  81     7733   8228   7704   -257    218     62       C  
ATOM    441  CZ2 TRP A  81      11.221  31.726  43.351  1.00 62.35           C  
ANISOU  441  CZ2 TRP A  81     7728   8198   7763   -205    194     77       C  
ATOM    442  CZ3 TRP A  81       9.767  31.911  45.317  1.00 63.29           C  
ANISOU  442  CZ3 TRP A  81     7846   8340   7858   -236    228     49       C  
ATOM    443  CH2 TRP A  81       9.983  32.022  43.931  1.00 63.38           C  
ANISOU  443  CH2 TRP A  81     7851   8333   7894   -211    215     57       C  
ATOM    444  N   LEU A  82      13.478  33.900  48.298  1.00 53.28           N  
ANISOU  444  N   LEU A  82     6627   7101   6514   -298    216     40       N  
ATOM    445  CA  LEU A  82      12.554  35.030  48.423  1.00 52.83           C  
ANISOU  445  CA  LEU A  82     6564   7040   6467   -293    241      9       C  
ATOM    446  C   LEU A  82      12.431  35.779  47.107  1.00 52.47           C  
ANISOU  446  C   LEU A  82     6507   6972   6455   -264    239      3       C  
ATOM    447  O   LEU A  82      13.427  36.255  46.563  1.00 56.44           O  
ANISOU  447  O   LEU A  82     7013   7465   6964   -254    225     11       O  
ATOM    448  CB  LEU A  82      12.994  35.992  49.543  1.00 53.13           C  
ANISOU  448  CB  LEU A  82     6614   7087   6484   -314    251     -9       C  
ATOM    449  CG  LEU A  82      12.158  37.258  49.817  1.00 52.73           C  
ANISOU  449  CG  LEU A  82     6558   7032   6444   -313    278    -44       C  
ATOM    450  CD1 LEU A  82      10.781  36.950  50.388  1.00 51.93           C  
ANISOU  450  CD1 LEU A  82     6450   6940   6340   -323    302    -60       C  
ATOM    451  CD2 LEU A  82      12.900  38.198  50.746  1.00 53.84           C  
ANISOU  451  CD2 LEU A  82     6712   7179   6565   -331    282    -59       C  
ATOM    452  N   ASP A  83      11.199  35.897  46.617  1.00 51.98           N  
ANISOU  452  N   ASP A  83     6431   6902   6414   -250    252     -8       N  
ATOM    453  CA  ASP A  83      10.925  36.492  45.314  1.00 51.05           C  
ANISOU  453  CA  ASP A  83     6303   6763   6330   -223    249    -11       C  
ATOM    454  C   ASP A  83      10.100  37.772  45.449  1.00 50.49           C  
ANISOU  454  C   ASP A  83     6223   6683   6276   -218    269    -42       C  
ATOM    455  O   ASP A  83       8.897  37.735  45.721  1.00 49.27           O  
ANISOU  455  O   ASP A  83     6059   6530   6131   -220    287    -58       O  
ATOM    456  CB  ASP A  83      10.216  35.470  44.416  1.00 51.89           C  
ANISOU  456  CB  ASP A  83     6399   6863   6452   -208    242      3       C  
ATOM    457  CG  ASP A  83      10.123  35.905  42.962  1.00 50.60           C  
ANISOU  457  CG  ASP A  83     6227   6679   6319   -182    232      6       C  
ATOM    458  OD1 ASP A  83      10.190  37.113  42.652  1.00 50.17           O  
ANISOU  458  OD1 ASP A  83     6170   6611   6279   -173    236     -8       O  
ATOM    459  OD2 ASP A  83       9.966  35.010  42.112  1.00 53.48           O  
ANISOU  459  OD2 ASP A  83     6588   7039   6693   -170    220     24       O  
ATOM    460  N   LEU A  84      10.767  38.901  45.226  1.00 50.91           N  
ANISOU  460  N   LEU A  84     6279   6726   6338   -212    266    -51       N  
ATOM    461  CA  LEU A  84      10.153  40.214  45.343  1.00 50.72           C  
ANISOU  461  CA  LEU A  84     6247   6691   6332   -208    284    -80       C  
ATOM    462  C   LEU A  84      10.120  40.940  43.992  1.00 51.18           C  
ANISOU  462  C   LEU A  84     6296   6726   6424   -182    273    -79       C  
ATOM    463  O   LEU A  84      10.237  42.166  43.938  1.00 52.86           O  
ANISOU  463  O   LEU A  84     6506   6926   6651   -177    278    -96       O  
ATOM    464  CB  LEU A  84      10.896  41.052  46.399  1.00 51.30           C  
ANISOU  464  CB  LEU A  84     6332   6773   6386   -226    291    -96       C  
ATOM    465  CG  LEU A  84      11.207  40.401  47.761  1.00 54.31           C  
ANISOU  465  CG  LEU A  84     6727   7178   6728   -256    297    -94       C  
ATOM    466  CD1 LEU A  84      12.336  41.120  48.481  1.00 52.51           C  
ANISOU  466  CD1 LEU A  84     6514   6957   6480   -270    294    -99       C  
ATOM    467  CD2 LEU A  84       9.977  40.304  48.659  1.00 53.89           C  
ANISOU  467  CD2 LEU A  84     6669   7137   6670   -270    324   -116       C  
ATOM    468  N   SER A  85       9.955  40.186  42.906  1.00 49.89           N  
ANISOU  468  N   SER A  85     6128   6554   6273   -166    259    -58       N  
ATOM    469  CA  SER A  85       9.831  40.771  41.567  1.00 52.05           C  
ANISOU  469  CA  SER A  85     6393   6805   6577   -143    248    -55       C  
ATOM    470  C   SER A  85       8.645  41.724  41.470  1.00 52.22           C  
ANISOU  470  C   SER A  85     6399   6812   6628   -134    263    -79       C  
ATOM    471  O   SER A  85       7.594  41.470  42.052  1.00 56.76           O  
ANISOU  471  O   SER A  85     6965   7392   7206   -140    279    -93       O  
ATOM    472  CB  SER A  85       9.673  39.677  40.513  1.00 53.33           C  
ANISOU  472  CB  SER A  85     6553   6964   6746   -130    232    -30       C  
ATOM    473  OG  SER A  85      10.778  38.795  40.515  1.00 57.62           O  
ANISOU  473  OG  SER A  85     7108   7517   7267   -136    218     -8       O  
ATOM    474  N   ARG A  86       8.818  42.816  40.733  1.00 51.14           N  
ANISOU  474  N   ARG A  86     6258   6656   6514   -120    256    -85       N  
ATOM    475  CA  ARG A  86       7.752  43.798  40.509  1.00 52.83           C  
ANISOU  475  CA  ARG A  86     6457   6852   6762   -111    267   -107       C  
ATOM    476  C   ARG A  86       6.995  44.236  41.773  1.00 54.91           C  
ANISOU  476  C   ARG A  86     6714   7124   7026   -125    294   -137       C  
ATOM    477  O   ARG A  86       5.776  44.129  41.836  1.00 58.56           O  
ANISOU  477  O   ARG A  86     7161   7581   7507   -122    306   -150       O  
ATOM    478  CB  ARG A  86       6.752  43.262  39.483  1.00 51.07           C  
ANISOU  478  CB  ARG A  86     6222   6616   6564    -95    259    -97       C  
ATOM    479  CG  ARG A  86       6.238  44.328  38.537  1.00 48.88           C  
ANISOU  479  CG  ARG A  86     5932   6313   6325    -77    252   -104       C  
ATOM    480  CD  ARG A  86       7.318  44.633  37.525  1.00 48.85           C  
ANISOU  480  CD  ARG A  86     5940   6300   6321    -68    230    -84       C  
ATOM    481  NE  ARG A  86       7.251  46.003  37.062  1.00 49.58           N  
ANISOU  481  NE  ARG A  86     6024   6370   6441    -58    226    -95       N  
ATOM    482  CZ  ARG A  86       8.182  46.585  36.319  1.00 50.38           C  
ANISOU  482  CZ  ARG A  86     6134   6462   6544    -52    211    -84       C  
ATOM    483  NH1 ARG A  86       9.265  45.915  35.946  1.00 50.04           N  
ANISOU  483  NH1 ARG A  86     6106   6428   6475    -54    198    -61       N  
ATOM    484  NH2 ARG A  86       8.024  47.847  35.947  1.00 53.03           N  
ANISOU  484  NH2 ARG A  86     6462   6777   6907    -44    208    -95       N  
ATOM    485  N   CYS A  87       7.713  44.726  42.777  1.00 56.37           N  
ANISOU  485  N   CYS A  87     6908   7319   7188   -141    303   -149       N  
ATOM    486  CA  CYS A  87       7.081  45.143  44.027  1.00 55.43           C  
ANISOU  486  CA  CYS A  87     6785   7209   7065   -157    330   -180       C  
ATOM    487  C   CYS A  87       7.152  46.649  44.239  1.00 57.16           C  
ANISOU  487  C   CYS A  87     6999   7414   7302   -156    340   -206       C  
ATOM    488  O   CYS A  87       6.807  47.154  45.309  1.00 58.02           O  
ANISOU  488  O   CYS A  87     7107   7531   7407   -171    363   -233       O  
ATOM    489  CB  CYS A  87       7.689  44.399  45.210  1.00 54.03           C  
ANISOU  489  CB  CYS A  87     6624   7059   6844   -182    337   -176       C  
ATOM    490  SG  CYS A  87       7.231  42.657  45.265  1.00 52.82           S  
ANISOU  490  SG  CYS A  87     6473   6922   6671   -188    334   -153       S  
ATOM    491  N   GLU A  88       7.595  47.355  43.201  1.00 58.42           N  
ANISOU  491  N   GLU A  88     7157   7555   7485   -138    322   -197       N  
ATOM    492  CA  GLU A  88       7.684  48.817  43.197  1.00 59.65           C  
ANISOU  492  CA  GLU A  88     7306   7693   7664   -133    326   -218       C  
ATOM    493  C   GLU A  88       8.600  49.374  44.307  1.00 59.91           C  
ANISOU  493  C   GLU A  88     7353   7740   7670   -152    336   -232       C  
ATOM    494  O   GLU A  88       8.446  50.522  44.742  1.00 62.21           O  
ANISOU  494  O   GLU A  88     7637   8021   7977   -154    349   -259       O  
ATOM    495  CB  GLU A  88       6.283  49.439  43.249  1.00 61.97           C  
ANISOU  495  CB  GLU A  88     7577   7971   7996   -127    344   -245       C  
ATOM    496  CG  GLU A  88       5.266  48.746  42.352  1.00 65.60           C  
ANISOU  496  CG  GLU A  88     8024   8420   8479   -112    337   -232       C  
ATOM    497  CD  GLU A  88       3.835  49.142  42.664  1.00 68.37           C  
ANISOU  497  CD  GLU A  88     8353   8760   8864   -110    358   -260       C  
ATOM    498  OE1 GLU A  88       3.447  50.276  42.314  1.00 70.92           O  
ANISOU  498  OE1 GLU A  88     8661   9059   9224   -100    359   -277       O  
ATOM    499  OE2 GLU A  88       3.094  48.318  43.246  1.00 66.83           O  
ANISOU  499  OE2 GLU A  88     8153   8578   8658   -120    374   -266       O  
ATOM    500  N   ILE A  89       9.559  48.553  44.739  1.00 55.45           N  
ANISOU  500  N   ILE A  89     6805   7195   7066   -165    328   -214       N  
ATOM    501  CA  ILE A  89      10.548  48.931  45.750  1.00 53.48           C  
ANISOU  501  CA  ILE A  89     6571   6959   6787   -184    332   -222       C  
ATOM    502  C   ILE A  89      11.502  50.017  45.252  1.00 54.27           C  
ANISOU  502  C   ILE A  89     6675   7044   6900   -175    318   -220       C  
ATOM    503  O   ILE A  89      12.150  49.869  44.208  1.00 52.44           O  
ANISOU  503  O   ILE A  89     6446   6803   6674   -161    296   -195       O  
ATOM    504  CB  ILE A  89      11.363  47.711  46.222  1.00 50.60           C  
ANISOU  504  CB  ILE A  89     6225   6618   6382   -200    322   -198       C  
ATOM    505  CG1 ILE A  89      10.439  46.686  46.882  1.00 50.87           C  
ANISOU  505  CG1 ILE A  89     6256   6668   6401   -213    337   -201       C  
ATOM    506  CG2 ILE A  89      12.459  48.136  47.189  1.00 50.03           C  
ANISOU  506  CG2 ILE A  89     6169   6558   6281   -219    322   -203       C  
ATOM    507  CD1 ILE A  89      10.942  45.261  46.802  1.00 52.05           C  
ANISOU  507  CD1 ILE A  89     6417   6834   6525   -218    322   -170       C  
ATOM    508  N   GLU A  90      11.571  51.112  46.005  1.00 54.44           N  
ANISOU  508  N   GLU A  90     6696   7063   6925   -184    332   -248       N  
ATOM    509  CA  GLU A  90      12.502  52.189  45.701  1.00 56.37           C  
ANISOU  509  CA  GLU A  90     6944   7295   7178   -179    321   -249       C  
ATOM    510  C   GLU A  90      13.578  52.312  46.771  1.00 56.54           C  
ANISOU  510  C   GLU A  90     6984   7334   7165   -200    322   -252       C  
ATOM    511  O   GLU A  90      14.618  52.928  46.540  1.00 57.63           O  
ANISOU  511  O   GLU A  90     7129   7465   7302   -198    309   -246       O  
ATOM    512  CB  GLU A  90      11.772  53.521  45.529  1.00 57.06           C  
ANISOU  512  CB  GLU A  90     7014   7359   7305   -168    332   -277       C  
ATOM    513  CG  GLU A  90      11.044  53.666  44.201  1.00 62.14           C  
ANISOU  513  CG  GLU A  90     7641   7979   7988   -144    321   -267       C  
ATOM    514  CD  GLU A  90      10.646  55.102  43.888  1.00 67.87           C  
ANISOU  514  CD  GLU A  90     8352   8679   8756   -133    325   -289       C  
ATOM    515  OE1 GLU A  90       9.789  55.304  42.999  1.00 65.81           O  
ANISOU  515  OE1 GLU A  90     8075   8398   8531   -116    319   -287       O  
ATOM    516  OE2 GLU A  90      11.183  56.038  44.526  1.00 75.57           O  
ANISOU  516  OE2 GLU A  90     9331   9653   9728   -141    331   -308       O  
ATOM    517  N   THR A  91      13.332  51.720  47.935  1.00 55.29           N  
ANISOU  517  N   THR A  91     6833   7196   6976   -223    338   -263       N  
ATOM    518  CA  THR A  91      14.247  51.869  49.054  1.00 55.18           C  
ANISOU  518  CA  THR A  91     6838   7200   6929   -246    340   -269       C  
ATOM    519  C   THR A  91      14.476  50.565  49.800  1.00 55.78           C  
ANISOU  519  C   THR A  91     6928   7302   6964   -267    339   -253       C  
ATOM    520  O   THR A  91      13.528  49.885  50.175  1.00 57.92           O  
ANISOU  520  O   THR A  91     7194   7582   7229   -274    354   -259       O  
ATOM    521  CB  THR A  91      13.759  52.970  50.020  1.00 53.43           C  
ANISOU  521  CB  THR A  91     6612   6976   6711   -259    366   -309       C  
ATOM    522  OG1 THR A  91      13.779  54.227  49.338  1.00 52.64           O  
ANISOU  522  OG1 THR A  91     6500   6852   6649   -241    363   -321       O  
ATOM    523  CG2 THR A  91      14.645  53.070  51.258  1.00 50.80           C  
ANISOU  523  CG2 THR A  91     6299   6662   6339   -287    369   -316       C  
ATOM    524  N   ILE A  92      15.746  50.223  49.989  1.00 56.77           N  
ANISOU  524  N   ILE A  92     7069   7436   7064   -276    320   -231       N  
ATOM    525  CA  ILE A  92      16.133  49.132  50.867  1.00 59.28           C  
ANISOU  525  CA  ILE A  92     7402   7778   7342   -300    316   -217       C  
ATOM    526  C   ILE A  92      16.804  49.760  52.075  1.00 61.29           C  
ANISOU  526  C   ILE A  92     7673   8044   7570   -325    322   -234       C  
ATOM    527  O   ILE A  92      17.909  50.289  51.988  1.00 61.85           O  
ANISOU  527  O   ILE A  92     7750   8109   7638   -324    306   -226       O  
ATOM    528  CB  ILE A  92      17.073  48.112  50.181  1.00 59.16           C  
ANISOU  528  CB  ILE A  92     7393   7765   7319   -293    288   -178       C  
ATOM    529  CG1 ILE A  92      16.327  47.345  49.091  1.00 59.51           C  
ANISOU  529  CG1 ILE A  92     7424   7801   7384   -271    284   -162       C  
ATOM    530  CG2 ILE A  92      17.634  47.119  51.190  1.00 59.89           C  
ANISOU  530  CG2 ILE A  92     7503   7881   7371   -319    281   -163       C  
ATOM    531  CD1 ILE A  92      17.236  46.637  48.111  1.00 61.08           C  
ANISOU  531  CD1 ILE A  92     7625   7995   7587   -258    258   -128       C  
ATOM    532  N   GLU A  93      16.107  49.706  53.200  1.00 65.69           N  
ANISOU  532  N   GLU A  93     8235   8617   8107   -347    345   -257       N  
ATOM    533  CA  GLU A  93      16.586  50.253  54.454  1.00 68.33           C  
ANISOU  533  CA  GLU A  93     8585   8964   8412   -375    353   -276       C  
ATOM    534  C   GLU A  93      17.835  49.503  54.874  1.00 67.88           C  
ANISOU  534  C   GLU A  93     8547   8921   8321   -392    329   -246       C  
ATOM    535  O   GLU A  93      18.120  48.432  54.341  1.00 66.87           O  
ANISOU  535  O   GLU A  93     8420   8797   8191   -385    310   -215       O  
ATOM    536  CB  GLU A  93      15.499  50.070  55.509  1.00 72.46           C  
ANISOU  536  CB  GLU A  93     9110   9503   8918   -398    384   -302       C  
ATOM    537  CG  GLU A  93      15.435  51.158  56.562  1.00 79.53           C  
ANISOU  537  CG  GLU A  93    10012  10403   9802   -418    406   -340       C  
ATOM    538  CD  GLU A  93      14.056  51.269  57.180  1.00 81.05           C  
ANISOU  538  CD  GLU A  93    10196  10600   9997   -429    441   -374       C  
ATOM    539  OE1 GLU A  93      13.143  51.798  56.512  1.00 80.72           O  
ANISOU  539  OE1 GLU A  93    10133  10541   9996   -407    455   -391       O  
ATOM    540  OE2 GLU A  93      13.885  50.829  58.336  1.00 84.11           O  
ANISOU  540  OE2 GLU A  93    10599  11011  10347   -460    455   -383       O  
ATOM    541  N   ASP A  94      18.584  50.068  55.817  1.00 70.68           N  
ANISOU  541  N   ASP A  94     8918   9285   8653   -415    328   -257       N  
ATOM    542  CA  ASP A  94      19.666  49.333  56.467  1.00 74.06           C  
ANISOU  542  CA  ASP A  94     9366   9729   9045   -437    306   -232       C  
ATOM    543  C   ASP A  94      19.071  48.113  57.155  1.00 71.10           C  
ANISOU  543  C   ASP A  94     8998   9375   8640   -458    312   -223       C  
ATOM    544  O   ASP A  94      17.880  48.100  57.469  1.00 66.36           O  
ANISOU  544  O   ASP A  94     8391   8780   8040   -463    339   -246       O  
ATOM    545  CB  ASP A  94      20.388  50.207  57.498  1.00 81.00           C  
ANISOU  545  CB  ASP A  94    10261  10614   9901   -461    307   -250       C  
ATOM    546  CG  ASP A  94      21.370  51.183  56.865  1.00 89.01           C  
ANISOU  546  CG  ASP A  94    11271  11609  10938   -444    291   -247       C  
ATOM    547  OD1 ASP A  94      22.313  51.610  57.572  1.00 92.03           O  
ANISOU  547  OD1 ASP A  94    11670  11997  11301   -463    281   -248       O  
ATOM    548  OD2 ASP A  94      21.205  51.526  55.671  1.00 92.06           O  
ANISOU  548  OD2 ASP A  94    11641  11976  11362   -413    288   -243       O  
ATOM    549  N   LYS A  95      19.896  47.092  57.375  1.00 71.84           N  
ANISOU  549  N   LYS A  95     9104   9480   8710   -471    287   -191       N  
ATOM    550  CA  LYS A  95      19.470  45.873  58.066  1.00 73.91           C  
ANISOU  550  CA  LYS A  95     9374   9762   8943   -493    289   -178       C  
ATOM    551  C   LYS A  95      18.061  45.416  57.650  1.00 74.10           C  
ANISOU  551  C   LYS A  95     9383   9787   8983   -480    311   -187       C  
ATOM    552  O   LYS A  95      17.265  44.963  58.482  1.00 73.74           O  
ANISOU  552  O   LYS A  95     9344   9758   8915   -502    329   -198       O  
ATOM    553  CB  LYS A  95      19.586  46.057  59.588  1.00 73.88           C  
ANISOU  553  CB  LYS A  95     9393   9781   8897   -533    299   -194       C  
ATOM    554  CG  LYS A  95      20.889  45.530  60.182  1.00 77.14           C  
ANISOU  554  CG  LYS A  95     9825  10203   9279   -556    268   -166       C  
ATOM    555  CD  LYS A  95      21.348  46.327  61.399  1.00 76.63           C  
ANISOU  555  CD  LYS A  95     9781  10150   9184   -588    273   -187       C  
ATOM    556  CE  LYS A  95      22.313  47.437  60.999  1.00 76.91           C  
ANISOU  556  CE  LYS A  95     9815  10168   9239   -574    261   -192       C  
ATOM    557  NZ  LYS A  95      22.567  48.415  62.096  1.00 76.73           N  
ANISOU  557  NZ  LYS A  95     9809  10153   9192   -601    272   -220       N  
ATOM    558  N   ALA A  96      17.763  45.550  56.356  1.00 74.35           N  
ANISOU  558  N   ALA A  96     9395   9798   9054   -446    308   -182       N  
ATOM    559  CA  ALA A  96      16.474  45.129  55.797  1.00 74.54           C  
ANISOU  559  CA  ALA A  96     9403   9819   9099   -430    325   -188       C  
ATOM    560  C   ALA A  96      16.410  43.611  55.738  1.00 75.74           C  
ANISOU  560  C   ALA A  96     9557   9982   9236   -435    311   -157       C  
ATOM    561  O   ALA A  96      15.335  43.009  55.882  1.00 78.33           O  
ANISOU  561  O   ALA A  96     9879  10318   9563   -438    327   -163       O  
ATOM    562  CB  ALA A  96      16.263  45.723  54.413  1.00 69.78           C  
ANISOU  562  CB  ALA A  96     8781   9191   8541   -393    322   -190       C  
ATOM    563  N   TRP A  97      17.581  43.008  55.548  1.00 72.04           N  
ANISOU  563  N   TRP A  97     9097   9514   8758   -436    281   -125       N  
ATOM    564  CA  TRP A  97      17.720  41.571  55.424  1.00 69.37           C  
ANISOU  564  CA  TRP A  97     8761   9185   8410   -440    263    -93       C  
ATOM    565  C   TRP A  97      18.217  40.955  56.698  1.00 71.73           C  
ANISOU  565  C   TRP A  97     9080   9506   8667   -476    255    -82       C  
ATOM    566  O   TRP A  97      18.693  39.820  56.692  1.00 75.54           O  
ANISOU  566  O   TRP A  97     9567   9994   9139   -483    233    -51       O  
ATOM    567  CB  TRP A  97      18.700  41.242  54.301  1.00 66.16           C  
ANISOU  567  CB  TRP A  97     8349   8763   8025   -417    235    -64       C  
ATOM    568  CG  TRP A  97      18.485  41.975  52.992  1.00 61.41           C  
ANISOU  568  CG  TRP A  97     7730   8139   7464   -382    238    -71       C  
ATOM    569  CD1 TRP A  97      19.357  42.862  52.367  1.00 59.67           C  
ANISOU  569  CD1 TRP A  97     7507   7902   7260   -367    227    -71       C  
ATOM    570  CD2 TRP A  97      17.324  41.890  52.090  1.00 56.83           C  
ANISOU  570  CD2 TRP A  97     7132   7548   6910   -359    252    -79       C  
ATOM    571  NE1 TRP A  97      18.830  43.321  51.189  1.00 57.84           N  
ANISOU  571  NE1 TRP A  97     7260   7653   7064   -338    233    -77       N  
ATOM    572  CE2 TRP A  97      17.619  42.778  50.960  1.00 55.86           C  
ANISOU  572  CE2 TRP A  97     6998   7403   6820   -331    246    -82       C  
ATOM    573  CE3 TRP A  97      16.120  41.203  52.110  1.00 54.77           C  
ANISOU  573  CE3 TRP A  97     6864   7294   6652   -358    266    -83       C  
ATOM    574  CZ2 TRP A  97      16.733  42.951  49.912  1.00 55.27           C  
ANISOU  574  CZ2 TRP A  97     6908   7314   6777   -306    254    -88       C  
ATOM    575  CZ3 TRP A  97      15.232  41.389  51.048  1.00 54.73           C  
ANISOU  575  CZ3 TRP A  97     6841   7272   6679   -332    274    -89       C  
ATOM    576  CH2 TRP A  97      15.535  42.241  49.975  1.00 55.56           C  
ANISOU  576  CH2 TRP A  97     6938   7357   6815   -306    268    -91       C  
ATOM    577  N   HIS A  98      18.094  41.688  57.803  1.00 76.01           N  
ANISOU  577  N   HIS A  98     9635  10059   9185   -502    272   -108       N  
ATOM    578  CA  HIS A  98      18.732  41.337  59.081  1.00 80.08           C  
ANISOU  578  CA  HIS A  98    10173  10594   9658   -540    262   -100       C  
ATOM    579  C   HIS A  98      18.685  39.886  59.501  1.00 81.13           C  
ANISOU  579  C   HIS A  98    10313  10743   9768   -558    249    -71       C  
ATOM    580  O   HIS A  98      19.734  39.280  59.744  1.00 81.35           O  
ANISOU  580  O   HIS A  98    10352  10774   9781   -571    219    -42       O  
ATOM    581  CB  HIS A  98      18.214  42.245  60.201  1.00 86.77           C  
ANISOU  581  CB  HIS A  98    11032  11454  10482   -565    291   -137       C  
ATOM    582  CG  HIS A  98      18.590  41.784  61.598  1.00 91.31           C  
ANISOU  582  CG  HIS A  98    11631  12052  11008   -609    285   -131       C  
ATOM    583  ND1 HIS A  98      19.841  41.894  62.089  1.00 91.12           N  
ANISOU  583  ND1 HIS A  98    11624  12031  10965   -626    260   -115       N  
ATOM    584  CD2 HIS A  98      17.820  41.207  62.613  1.00 91.15           C  
ANISOU  584  CD2 HIS A  98    11623  12054  10955   -640    303   -138       C  
ATOM    585  CE1 HIS A  98      19.874  41.408  63.346  1.00 93.42           C  
ANISOU  585  CE1 HIS A  98    11937  12345  11212   -666    259   -112       C  
ATOM    586  NE2 HIS A  98      18.635  40.990  63.665  1.00 93.82           N  
ANISOU  586  NE2 HIS A  98    11985  12407  11253   -675    286   -126       N  
ATOM    587  N   GLY A  99      17.489  39.307  59.587  1.00 78.05           N  
ANISOU  587  N   GLY A  99     9917  10360   9376   -560    269    -78       N  
ATOM    588  CA  GLY A  99      17.333  37.983  60.197  1.00 78.14           C  
ANISOU  588  CA  GLY A  99     9938  10390   9361   -584    259    -54       C  
ATOM    589  C   GLY A  99      17.648  36.763  59.348  1.00 80.40           C  
ANISOU  589  C   GLY A  99    10214  10668   9664   -566    233    -17       C  
ATOM    590  O   GLY A  99      17.578  35.634  59.839  1.00 85.39           O  
ANISOU  590  O   GLY A  99    10854  11314  10277   -586    222      4       O  
ATOM    591  N   LEU A 100      18.019  36.984  58.089  1.00 79.23           N  
ANISOU  591  N   LEU A 100    10050  10499   9552   -531    221     -9       N  
ATOM    592  CA  LEU A 100      18.073  35.916  57.084  1.00 76.31           C  
ANISOU  592  CA  LEU A 100     9667  10120   9206   -509    203     18       C  
ATOM    593  C   LEU A 100      19.430  35.212  56.955  1.00 75.00           C  
ANISOU  593  C   LEU A 100     9507   9951   9038   -512    166     54       C  
ATOM    594  O   LEU A 100      20.190  35.469  56.023  1.00 72.52           O  
ANISOU  594  O   LEU A 100     9184   9619   8750   -488    152     63       O  
ATOM    595  CB  LEU A 100      17.610  36.460  55.731  1.00 74.37           C  
ANISOU  595  CB  LEU A 100     9401   9854   9001   -470    213      7       C  
ATOM    596  CG  LEU A 100      16.182  37.012  55.695  1.00 74.84           C  
ANISOU  596  CG  LEU A 100     9450   9913   9070   -463    247    -24       C  
ATOM    597  CD1 LEU A 100      16.033  38.127  54.673  1.00 74.44           C  
ANISOU  597  CD1 LEU A 100     9386   9842   9055   -432    256    -43       C  
ATOM    598  CD2 LEU A 100      15.194  35.896  55.418  1.00 76.00           C  
ANISOU  598  CD2 LEU A 100     9588  10065   9223   -458    252    -14       C  
ATOM    599  N   HIS A 101      19.712  34.312  57.894  1.00 79.00           N  
ANISOU  599  N   HIS A 101    10026  10473   9515   -542    152     73       N  
ATOM    600  CA  HIS A 101      20.966  33.557  57.921  1.00 81.45           C  
ANISOU  600  CA  HIS A 101    10342  10781   9825   -549    116    108       C  
ATOM    601  C   HIS A 101      21.166  32.748  56.673  1.00 79.79           C  
ANISOU  601  C   HIS A 101    10114  10554   9648   -520    100    131       C  
ATOM    602  O   HIS A 101      22.255  32.745  56.102  1.00 78.24           O  
ANISOU  602  O   HIS A 101     9914  10344   9470   -507     78    147       O  
ATOM    603  CB  HIS A 101      21.002  32.585  59.105  1.00 91.18           C  
ANISOU  603  CB  HIS A 101    11590  12032  11021   -587    103    127       C  
ATOM    604  CG  HIS A 101      20.965  33.243  60.467  1.00 98.91           C  
ANISOU  604  CG  HIS A 101    12591  13029  11960   -623    115    109       C  
ATOM    605  ND1 HIS A 101      21.990  33.154  61.339  1.00101.88           N  
ANISOU  605  ND1 HIS A 101    12984  13412  12311   -652     90    125       N  
ATOM    606  CD2 HIS A 101      19.967  33.979  61.106  1.00101.42           C  
ANISOU  606  CD2 HIS A 101    12915  13359  12259   -636    149     75       C  
ATOM    607  CE1 HIS A 101      21.674  33.813  62.470  1.00104.56           C  
ANISOU  607  CE1 HIS A 101    13343  13769  12616   -682    108    102       C  
ATOM    608  NE2 HIS A 101      20.437  34.318  62.326  1.00107.24           N  
ANISOU  608  NE2 HIS A 101    13675  14112  12959   -673    145     71       N  
ATOM    609  N   HIS A 102      20.113  32.050  56.243  1.00 78.88           N  
ANISOU  609  N   HIS A 102     9987  10440   9542   -509    112    131       N  
ATOM    610  CA  HIS A 102      20.263  30.934  55.304  1.00 75.10           C  
ANISOU  610  CA  HIS A 102     9495   9950   9087   -489     94    157       C  
ATOM    611  C   HIS A 102      19.890  31.208  53.872  1.00 68.20           C  
ANISOU  611  C   HIS A 102     8603   9058   8250   -451    103    149       C  
ATOM    612  O   HIS A 102      20.172  30.380  52.999  1.00 66.69           O  
ANISOU  612  O   HIS A 102     8400   8856   8080   -434     88    170       O  
ATOM    613  CB  HIS A 102      19.529  29.695  55.825  1.00 78.44           C  
ANISOU  613  CB  HIS A 102     9919  10387   9495   -507     94    172       C  
ATOM    614  CG  HIS A 102      20.081  29.162  57.129  1.00 84.18           C  
ANISOU  614  CG  HIS A 102    10665  11131  10188   -545     76    189       C  
ATOM    615  ND1 HIS A 102      21.332  28.672  57.241  1.00 85.76           N  
ANISOU  615  ND1 HIS A 102    10868  11325  10389   -553     43    217       N  
ATOM    616  CD2 HIS A 102      19.503  29.058  58.395  1.00 84.80           C  
ANISOU  616  CD2 HIS A 102    10759  11230  10229   -580     87    182       C  
ATOM    617  CE1 HIS A 102      21.547  28.278  58.512  1.00 86.56           C  
ANISOU  617  CE1 HIS A 102    10988  11443  10457   -591     32    229       C  
ATOM    618  NE2 HIS A 102      20.426  28.514  59.217  1.00 86.22           N  
ANISOU  618  NE2 HIS A 102    10952  11417  10387   -608     60    207       N  
ATOM    619  N   LEU A 103      19.275  32.365  53.614  1.00 59.72           N  
ANISOU  619  N   LEU A 103     7526   7981   7184   -439    128    119       N  
ATOM    620  CA  LEU A 103      18.824  32.742  52.267  1.00 54.96           C  
ANISOU  620  CA  LEU A 103     6907   7360   6615   -404    137    110       C  
ATOM    621  C   LEU A 103      19.891  32.510  51.184  1.00 53.56           C  
ANISOU  621  C   LEU A 103     6721   7165   6462   -382    114    130       C  
ATOM    622  O   LEU A 103      21.012  33.011  51.277  1.00 50.58           O  
ANISOU  622  O   LEU A 103     6350   6782   6084   -385    101    135       O  
ATOM    623  CB  LEU A 103      18.350  34.197  52.248  1.00 52.07           C  
ANISOU  623  CB  LEU A 103     6540   6990   6254   -396    161     77       C  
ATOM    624  CG  LEU A 103      17.575  34.692  51.024  1.00 52.68           C  
ANISOU  624  CG  LEU A 103     6601   7051   6364   -364    175     63       C  
ATOM    625  CD1 LEU A 103      16.143  34.176  51.015  1.00 52.99           C  
ANISOU  625  CD1 LEU A 103     6631   7095   6405   -362    193     54       C  
ATOM    626  CD2 LEU A 103      17.583  36.213  50.964  1.00 51.59           C  
ANISOU  626  CD2 LEU A 103     6463   6904   6233   -357    189     36       C  
ATOM    627  N   SER A 104      19.537  31.732  50.169  1.00 51.18           N  
ANISOU  627  N   SER A 104     6408   6855   6183   -361    110    142       N  
ATOM    628  CA  SER A 104      20.456  31.482  49.065  1.00 51.97           C  
ANISOU  628  CA  SER A 104     6499   6937   6307   -341     92    159       C  
ATOM    629  C   SER A 104      20.041  32.216  47.789  1.00 49.25           C  
ANISOU  629  C   SER A 104     6144   6577   5989   -311    104    145       C  
ATOM    630  O   SER A 104      20.876  32.476  46.919  1.00 48.91           O  
ANISOU  630  O   SER A 104     6097   6519   5965   -294     94    151       O  
ATOM    631  CB  SER A 104      20.606  29.980  48.808  1.00 53.85           C  
ANISOU  631  CB  SER A 104     6732   7175   6551   -341     74    186       C  
ATOM    632  OG  SER A 104      19.344  29.370  48.607  1.00 55.56           O  
ANISOU  632  OG  SER A 104     6942   7397   6771   -336     87    183       O  
ATOM    633  N   ASN A 105      18.758  32.562  47.703  1.00 45.91           N  
ANISOU  633  N   ASN A 105     5717   6157   5570   -304    125    125       N  
ATOM    634  CA  ASN A 105      18.187  33.165  46.511  1.00 46.10           C  
ANISOU  634  CA  ASN A 105     5730   6165   5620   -277    135    113       C  
ATOM    635  C   ASN A 105      17.358  34.415  46.789  1.00 46.63           C  
ANISOU  635  C   ASN A 105     5796   6232   5687   -276    158     83       C  
ATOM    636  O   ASN A 105      16.426  34.380  47.585  1.00 50.00           O  
ANISOU  636  O   ASN A 105     6224   6670   6101   -289    174     70       O  
ATOM    637  CB  ASN A 105      17.348  32.132  45.756  1.00 47.44           C  
ANISOU  637  CB  ASN A 105     5889   6332   5803   -264    135    123       C  
ATOM    638  CG  ASN A 105      18.195  31.220  44.885  1.00 49.42           C  
ANISOU  638  CG  ASN A 105     6135   6573   6066   -253    114    148       C  
ATOM    639  OD1 ASN A 105      18.251  31.387  43.666  1.00 49.32           O  
ANISOU  639  OD1 ASN A 105     6117   6546   6076   -231    112    148       O  
ATOM    640  ND2 ASN A 105      18.876  30.264  45.507  1.00 49.11           N  
ANISOU  640  ND2 ASN A 105     6101   6542   6015   -269     99    167       N  
ATOM    641  N   LEU A 106      17.701  35.516  46.124  1.00 44.99           N  
ANISOU  641  N   LEU A 106     5586   6010   5495   -261    160     72       N  
ATOM    642  CA  LEU A 106      16.960  36.766  46.254  1.00 43.20           C  
ANISOU  642  CA  LEU A 106     5358   5780   5276   -257    180     44       C  
ATOM    643  C   LEU A 106      16.642  37.360  44.879  1.00 43.20           C  
ANISOU  643  C   LEU A 106     5347   5760   5307   -229    181     39       C  
ATOM    644  O   LEU A 106      17.544  37.623  44.082  1.00 42.88           O  
ANISOU  644  O   LEU A 106     5307   5707   5278   -217    168     49       O  
ATOM    645  CB  LEU A 106      17.746  37.764  47.109  1.00 43.06           C  
ANISOU  645  CB  LEU A 106     5350   5766   5243   -272    182     32       C  
ATOM    646  CG  LEU A 106      17.158  39.166  47.304  1.00 42.84           C  
ANISOU  646  CG  LEU A 106     5321   5733   5224   -269    202      1       C  
ATOM    647  CD1 LEU A 106      15.886  39.131  48.143  1.00 41.44           C  
ANISOU  647  CD1 LEU A 106     5141   5567   5037   -282    224    -18       C  
ATOM    648  CD2 LEU A 106      18.203  40.076  47.929  1.00 42.48           C  
ANISOU  648  CD2 LEU A 106     5285   5688   5166   -281    197     -5       C  
ATOM    649  N   ILE A 107      15.359  37.574  44.606  1.00 42.53           N  
ANISOU  649  N   ILE A 107     5252   5671   5236   -219    196     24       N  
ATOM    650  CA  ILE A 107      14.942  38.021  43.281  1.00 44.64           C  
ANISOU  650  CA  ILE A 107     5509   5919   5532   -194    195     22       C  
ATOM    651  C   ILE A 107      14.338  39.424  43.357  1.00 45.38           C  
ANISOU  651  C   ILE A 107     5598   6004   5641   -189    211     -5       C  
ATOM    652  O   ILE A 107      13.316  39.622  44.010  1.00 47.30           O  
ANISOU  652  O   ILE A 107     5836   6252   5883   -196    229    -24       O  
ATOM    653  CB  ILE A 107      13.987  37.001  42.614  1.00 43.74           C  
ANISOU  653  CB  ILE A 107     5386   5803   5429   -184    194     31       C  
ATOM    654  CG1 ILE A 107      14.642  35.619  42.588  1.00 43.74           C  
ANISOU  654  CG1 ILE A 107     5390   5811   5416   -190    178     58       C  
ATOM    655  CG2 ILE A 107      13.632  37.434  41.196  1.00 42.85           C  
ANISOU  655  CG2 ILE A 107     5264   5670   5345   -159    190     32       C  
ATOM    656  CD1 ILE A 107      13.661  34.471  42.505  1.00 47.36           C  
ANISOU  656  CD1 ILE A 107     5842   6276   5877   -189    181     65       C  
ATOM    657  N   LEU A 108      14.984  40.382  42.686  1.00 44.29           N  
ANISOU  657  N   LEU A 108     5460   5851   5517   -177    204     -6       N  
ATOM    658  CA  LEU A 108      14.647  41.808  42.798  1.00 44.56           C  
ANISOU  658  CA  LEU A 108     5490   5875   5565   -174    216    -31       C  
ATOM    659  C   LEU A 108      14.241  42.442  41.470  1.00 45.42           C  
ANISOU  659  C   LEU A 108     5590   5962   5706   -150    212    -32       C  
ATOM    660  O   LEU A 108      14.003  43.650  41.390  1.00 44.98           O  
ANISOU  660  O   LEU A 108     5529   5894   5667   -145    219    -50       O  
ATOM    661  CB  LEU A 108      15.821  42.587  43.398  1.00 44.23           C  
ANISOU  661  CB  LEU A 108     5458   5835   5510   -184    213    -35       C  
ATOM    662  CG  LEU A 108      16.163  42.284  44.857  1.00 45.63           C  
ANISOU  662  CG  LEU A 108     5646   6033   5655   -211    219    -40       C  
ATOM    663  CD1 LEU A 108      17.513  42.882  45.230  1.00 43.32           C  
ANISOU  663  CD1 LEU A 108     5365   5741   5351   -219    209    -37       C  
ATOM    664  CD2 LEU A 108      15.058  42.781  45.781  1.00 44.54           C  
ANISOU  664  CD2 LEU A 108     5505   5901   5515   -222    243    -68       C  
ATOM    665  N   THR A 109      14.169  41.614  40.434  1.00 46.05           N  
ANISOU  665  N   THR A 109     5666   6036   5793   -137    199    -12       N  
ATOM    666  CA  THR A 109      13.786  42.033  39.094  1.00 43.62           C  
ANISOU  666  CA  THR A 109     5351   5709   5513   -117    192     -9       C  
ATOM    667  C   THR A 109      12.720  43.113  39.113  1.00 45.72           C  
ANISOU  667  C   THR A 109     5606   5963   5803   -111    205    -33       C  
ATOM    668  O   THR A 109      11.724  42.991  39.833  1.00 49.01           O  
ANISOU  668  O   THR A 109     6015   6384   6219   -117    220    -48       O  
ATOM    669  CB  THR A 109      13.230  40.831  38.330  1.00 41.94           C  
ANISOU  669  CB  THR A 109     5134   5496   5305   -109    185      7       C  
ATOM    670  OG1 THR A 109      14.081  39.703  38.560  1.00 41.24           O  
ANISOU  670  OG1 THR A 109     5054   5420   5194   -117    176     26       O  
ATOM    671  CG2 THR A 109      13.113  41.119  36.840  1.00 40.82           C  
ANISOU  671  CG2 THR A 109     4988   5334   5185    -89    173     16       C  
ATOM    672  N   GLY A 110      12.940  44.177  38.345  1.00 45.60           N  
ANISOU  672  N   GLY A 110     5588   5928   5807    -99    199    -36       N  
ATOM    673  CA  GLY A 110      11.882  45.146  38.052  1.00 46.91           C  
ANISOU  673  CA  GLY A 110     5741   6078   6003    -89    206    -54       C  
ATOM    674  C   GLY A 110      11.515  46.149  39.134  1.00 48.53           C  
ANISOU  674  C   GLY A 110     5942   6284   6213    -98    224    -83       C  
ATOM    675  O   GLY A 110      10.553  46.898  38.976  1.00 50.70           O  
ANISOU  675  O   GLY A 110     6203   6544   6515    -90    232   -100       O  
ATOM    676  N   ASN A 111      12.269  46.162  40.230  1.00 48.72           N  
ANISOU  676  N   ASN A 111     5976   6324   6211   -115    232    -89       N  
ATOM    677  CA  ASN A 111      12.125  47.185  41.266  1.00 48.80           C  
ANISOU  677  CA  ASN A 111     5984   6335   6221   -126    249   -117       C  
ATOM    678  C   ASN A 111      13.024  48.387  40.969  1.00 47.97           C  
ANISOU  678  C   ASN A 111     5882   6217   6126   -121    241   -120       C  
ATOM    679  O   ASN A 111      14.232  48.220  40.801  1.00 48.38           O  
ANISOU  679  O   ASN A 111     5947   6274   6162   -123    227   -103       O  
ATOM    680  CB  ASN A 111      12.489  46.606  42.636  1.00 50.33           C  
ANISOU  680  CB  ASN A 111     6189   6554   6380   -149    260   -122       C  
ATOM    681  CG  ASN A 111      11.531  45.520  43.092  1.00 50.03           C  
ANISOU  681  CG  ASN A 111     6146   6529   6333   -156    270   -122       C  
ATOM    682  OD1 ASN A 111      11.893  44.350  43.177  1.00 49.18           O  
ANISOU  682  OD1 ASN A 111     6047   6435   6203   -162    262   -102       O  
ATOM    683  ND2 ASN A 111      10.304  45.907  43.395  1.00 51.35           N  
ANISOU  683  ND2 ASN A 111     6300   6691   6518   -155    289   -146       N  
ATOM    684  N   PRO A 112      12.452  49.604  40.906  1.00 47.29           N  
ANISOU  684  N   PRO A 112     5785   6114   6068   -114    249   -142       N  
ATOM    685  CA  PRO A 112      13.296  50.768  40.598  1.00 47.23           C  
ANISOU  685  CA  PRO A 112     5780   6093   6070   -110    240   -145       C  
ATOM    686  C   PRO A 112      14.103  51.300  41.793  1.00 48.34           C  
ANISOU  686  C   PRO A 112     5931   6246   6189   -127    249   -160       C  
ATOM    687  O   PRO A 112      13.978  52.464  42.162  1.00 48.77           O  
ANISOU  687  O   PRO A 112     5980   6290   6259   -129    258   -183       O  
ATOM    688  CB  PRO A 112      12.293  51.806  40.083  1.00 46.70           C  
ANISOU  688  CB  PRO A 112     5697   6003   6044    -96    244   -162       C  
ATOM    689  CG  PRO A 112      11.000  51.437  40.721  1.00 47.17           C  
ANISOU  689  CG  PRO A 112     5744   6067   6109   -101    264   -181       C  
ATOM    690  CD  PRO A 112      11.022  49.954  40.984  1.00 47.18           C  
ANISOU  690  CD  PRO A 112     5753   6090   6080   -109    264   -164       C  
ATOM    691  N   ILE A 113      14.926  50.435  42.382  1.00 51.30           N  
ANISOU  691  N   ILE A 113     6320   6641   6530   -141    246   -146       N  
ATOM    692  CA  ILE A 113      15.880  50.805  43.431  1.00 51.39           C  
ANISOU  692  CA  ILE A 113     6343   6664   6517   -159    249   -154       C  
ATOM    693  C   ILE A 113      17.094  51.402  42.748  1.00 53.51           C  
ANISOU  693  C   ILE A 113     6618   6922   6791   -152    231   -140       C  
ATOM    694  O   ILE A 113      18.104  50.717  42.602  1.00 60.51           O  
ANISOU  694  O   ILE A 113     7514   7816   7658   -155    217   -117       O  
ATOM    695  CB  ILE A 113      16.382  49.552  44.179  1.00 50.38           C  
ANISOU  695  CB  ILE A 113     6228   6560   6352   -177    246   -140       C  
ATOM    696  CG1 ILE A 113      15.210  48.639  44.556  1.00 50.99           C  
ANISOU  696  CG1 ILE A 113     6300   6648   6424   -182    260   -144       C  
ATOM    697  CG2 ILE A 113      17.254  49.939  45.375  1.00 50.29           C  
ANISOU  697  CG2 ILE A 113     6231   6562   6315   -198    250   -150       C  
ATOM    698  CD1 ILE A 113      15.600  47.191  44.755  1.00 51.18           C  
ANISOU  698  CD1 ILE A 113     6333   6690   6420   -191    251   -120       C  
ATOM    699  N   GLN A 114      17.028  52.649  42.309  1.00 52.35           N  
ANISOU  699  N   GLN A 114     6464   6755   6671   -141    230   -153       N  
ATOM    700  CA  GLN A 114      18.085  53.114  41.414  1.00 56.81           C  
ANISOU  700  CA  GLN A 114     7033   7308   7243   -132    212   -135       C  
ATOM    701  C   GLN A 114      19.488  53.027  42.034  1.00 59.28           C  
ANISOU  701  C   GLN A 114     7360   7632   7530   -146    204   -126       C  
ATOM    702  O   GLN A 114      20.435  52.585  41.376  1.00 60.30           O  
ANISOU  702  O   GLN A 114     7495   7761   7652   -142    188   -102       O  
ATOM    703  CB  GLN A 114      17.798  54.503  40.859  1.00 59.74           C  
ANISOU  703  CB  GLN A 114     7394   7656   7649   -120    211   -149       C  
ATOM    704  CG  GLN A 114      18.374  54.713  39.468  1.00 57.75           C  
ANISOU  704  CG  GLN A 114     7142   7387   7411   -104    192   -126       C  
ATOM    705  CD  GLN A 114      18.358  56.165  39.040  1.00 60.12           C  
ANISOU  705  CD  GLN A 114     7435   7664   7741    -95    188   -137       C  
ATOM    706  OE1 GLN A 114      17.379  56.888  39.263  1.00 59.73           O  
ANISOU  706  OE1 GLN A 114     7374   7604   7716    -92    199   -160       O  
ATOM    707  NE2 GLN A 114      19.451  56.606  38.424  1.00 61.31           N  
ANISOU  707  NE2 GLN A 114     7593   7808   7894    -92    174   -122       N  
ATOM    708  N   SER A 115      19.610  53.425  43.298  1.00 58.10           N  
ANISOU  708  N   SER A 115     7216   7493   7364   -163    216   -147       N  
ATOM    709  CA  SER A 115      20.887  53.363  43.999  1.00 56.07           C  
ANISOU  709  CA  SER A 115     6973   7248   7083   -178    208   -140       C  
ATOM    710  C   SER A 115      20.886  52.318  45.091  1.00 54.69           C  
ANISOU  710  C   SER A 115     6807   7097   6874   -198    214   -138       C  
ATOM    711  O   SER A 115      19.892  52.130  45.786  1.00 53.58           O  
ANISOU  711  O   SER A 115     6664   6966   6728   -207    231   -156       O  
ATOM    712  CB  SER A 115      21.242  54.715  44.608  1.00 58.70           C  
ANISOU  712  CB  SER A 115     7307   7574   7421   -185    214   -163       C  
ATOM    713  OG  SER A 115      22.012  55.480  43.709  1.00 63.31           O  
ANISOU  713  OG  SER A 115     7889   8140   8023   -172    200   -153       O  
ATOM    714  N   PHE A 116      22.023  51.650  45.230  1.00 56.67           N  
ANISOU  714  N   PHE A 116     7069   7357   7104   -207    199   -116       N  
ATOM    715  CA  PHE A 116      22.250  50.700  46.301  1.00 60.99           C  
ANISOU  715  CA  PHE A 116     7627   7926   7619   -228    199   -111       C  
ATOM    716  C   PHE A 116      23.382  51.229  47.180  1.00 62.29           C  
ANISOU  716  C   PHE A 116     7803   8096   7765   -246    192   -114       C  
ATOM    717  O   PHE A 116      24.526  51.364  46.726  1.00 63.60           O  
ANISOU  717  O   PHE A 116     7973   8256   7936   -242    175    -97       O  
ATOM    718  CB  PHE A 116      22.614  49.328  45.726  1.00 61.61           C  
ANISOU  718  CB  PHE A 116     7707   8011   7690   -224    184    -80       C  
ATOM    719  CG  PHE A 116      21.477  48.635  45.029  1.00 61.67           C  
ANISOU  719  CG  PHE A 116     7704   8015   7709   -211    190    -76       C  
ATOM    720  CD1 PHE A 116      21.166  48.931  43.701  1.00 61.10           C  
ANISOU  720  CD1 PHE A 116     7622   7926   7665   -188    186    -70       C  
ATOM    721  CD2 PHE A 116      20.725  47.671  45.692  1.00 62.34           C  
ANISOU  721  CD2 PHE A 116     7790   8117   7777   -222    199    -77       C  
ATOM    722  CE1 PHE A 116      20.122  48.287  43.055  1.00 60.69           C  
ANISOU  722  CE1 PHE A 116     7562   7872   7625   -176    191    -66       C  
ATOM    723  CE2 PHE A 116      19.677  47.022  45.048  1.00 64.23           C  
ANISOU  723  CE2 PHE A 116     8020   8354   8028   -210    204    -73       C  
ATOM    724  CZ  PHE A 116      19.374  47.332  43.730  1.00 62.02           C  
ANISOU  724  CZ  PHE A 116     7730   8055   7777   -187    199    -68       C  
ATOM    725  N   SER A 117      23.058  51.537  48.432  1.00 61.81           N  
ANISOU  725  N   SER A 117     7749   8047   7685   -266    206   -136       N  
ATOM    726  CA  SER A 117      24.044  52.086  49.363  1.00 62.96           C  
ANISOU  726  CA  SER A 117     7908   8200   7813   -285    201   -142       C  
ATOM    727  C   SER A 117      24.830  50.967  50.063  1.00 63.10           C  
ANISOU  727  C   SER A 117     7939   8235   7799   -305    186   -120       C  
ATOM    728  O   SER A 117      24.332  49.844  50.183  1.00 59.88           O  
ANISOU  728  O   SER A 117     7532   7840   7380   -310    187   -109       O  
ATOM    729  CB  SER A 117      23.356  52.988  50.394  1.00 62.12           C  
ANISOU  729  CB  SER A 117     7804   8098   7700   -300    223   -178       C  
ATOM    730  OG  SER A 117      22.413  52.256  51.159  1.00 59.69           O  
ANISOU  730  OG  SER A 117     7498   7806   7372   -315    239   -187       O  
ATOM    731  N   PRO A 118      26.068  51.264  50.517  1.00 63.52           N  
ANISOU  731  N   PRO A 118     8003   8289   7841   -318    171   -113       N  
ATOM    732  CA  PRO A 118      26.812  50.284  51.313  1.00 63.53           C  
ANISOU  732  CA  PRO A 118     8017   8307   7814   -340    156    -93       C  
ATOM    733  C   PRO A 118      25.933  49.672  52.405  1.00 65.62           C  
ANISOU  733  C   PRO A 118     8290   8592   8049   -362    170   -104       C  
ATOM    734  O   PRO A 118      25.158  50.390  53.047  1.00 68.27           O  
ANISOU  734  O   PRO A 118     8626   8931   8379   -371    191   -134       O  
ATOM    735  CB  PRO A 118      27.943  51.117  51.945  1.00 61.40           C  
ANISOU  735  CB  PRO A 118     7758   8036   7535   -354    145    -97       C  
ATOM    736  CG  PRO A 118      27.784  52.519  51.437  1.00 59.70           C  
ANISOU  736  CG  PRO A 118     7534   7802   7345   -338    155   -119       C  
ATOM    737  CD  PRO A 118      26.876  52.467  50.248  1.00 61.46           C  
ANISOU  737  CD  PRO A 118     7741   8013   7596   -311    165   -120       C  
ATOM    738  N   GLY A 119      26.035  48.358  52.595  1.00 63.79           N  
ANISOU  738  N   GLY A 119     8062   8373   7801   -371    159    -81       N  
ATOM    739  CA  GLY A 119      25.230  47.663  53.603  1.00 63.51           C  
ANISOU  739  CA  GLY A 119     8034   8357   7736   -394    171    -88       C  
ATOM    740  C   GLY A 119      23.801  47.350  53.179  1.00 64.10           C  
ANISOU  740  C   GLY A 119     8098   8433   7823   -381    192    -99       C  
ATOM    741  O   GLY A 119      22.996  46.915  54.006  1.00 63.68           O  
ANISOU  741  O   GLY A 119     8049   8395   7748   -399    206   -109       O  
ATOM    742  N   SER A 120      23.492  47.570  51.896  1.00 64.52           N  
ANISOU  742  N   SER A 120     8135   8468   7909   -351    193    -96       N  
ATOM    743  CA  SER A 120      22.185  47.227  51.300  1.00 65.14           C  
ANISOU  743  CA  SER A 120     8201   8544   8004   -335    209   -103       C  
ATOM    744  C   SER A 120      21.879  45.734  51.386  1.00 64.98           C  
ANISOU  744  C   SER A 120     8181   8536   7968   -342    203    -81       C  
ATOM    745  O   SER A 120      20.721  45.338  51.527  1.00 65.76           O  
ANISOU  745  O   SER A 120     8275   8642   8066   -343    220    -91       O  
ATOM    746  CB  SER A 120      22.113  47.653  49.823  1.00 63.49           C  
ANISOU  746  CB  SER A 120     7977   8313   7832   -303    205    -98       C  
ATOM    747  OG  SER A 120      21.969  49.056  49.670  1.00 64.92           O  
ANISOU  747  OG  SER A 120     8153   8481   8032   -295    215   -122       O  
ATOM    748  N   PHE A 121      22.926  44.917  51.290  1.00 62.03           N  
ANISOU  748  N   PHE A 121     7814   8166   7587   -346    179    -52       N  
ATOM    749  CA  PHE A 121      22.797  43.468  51.292  1.00 58.25           C  
ANISOU  749  CA  PHE A 121     7336   7698   7098   -351    170    -28       C  
ATOM    750  C   PHE A 121      23.440  42.853  52.527  1.00 60.19           C  
ANISOU  750  C   PHE A 121     7597   7961   7309   -382    158    -16       C  
ATOM    751  O   PHE A 121      23.897  41.715  52.489  1.00 61.14           O  
ANISOU  751  O   PHE A 121     7719   8086   7423   -387    139     10       O  
ATOM    752  CB  PHE A 121      23.427  42.884  50.021  1.00 54.54           C  
ANISOU  752  CB  PHE A 121     6856   7214   6651   -328    151     -1       C  
ATOM    753  CG  PHE A 121      22.743  43.313  48.759  1.00 51.20           C  
ANISOU  753  CG  PHE A 121     6419   6775   6259   -299    160     -9       C  
ATOM    754  CD1 PHE A 121      21.520  42.760  48.391  1.00 51.49           C  
ANISOU  754  CD1 PHE A 121     6447   6812   6303   -290    172    -12       C  
ATOM    755  CD2 PHE A 121      23.311  44.278  47.943  1.00 50.37           C  
ANISOU  755  CD2 PHE A 121     6309   6651   6175   -282    156    -12       C  
ATOM    756  CE1 PHE A 121      20.872  43.165  47.227  1.00 51.79           C  
ANISOU  756  CE1 PHE A 121     6472   6834   6369   -265    179    -18       C  
ATOM    757  CE2 PHE A 121      22.674  44.682  46.775  1.00 51.47           C  
ANISOU  757  CE2 PHE A 121     6437   6776   6343   -257    163    -17       C  
ATOM    758  CZ  PHE A 121      21.451  44.128  46.416  1.00 50.51           C  
ANISOU  758  CZ  PHE A 121     6306   6655   6228   -249    174    -20       C  
ATOM    759  N   SER A 122      23.476  43.611  53.620  1.00 63.14           N  
ANISOU  759  N   SER A 122     7984   8345   7662   -405    167    -37       N  
ATOM    760  CA  SER A 122      24.098  43.151  54.860  1.00 62.56           C  
ANISOU  760  CA  SER A 122     7927   8288   7554   -437    155    -27       C  
ATOM    761  C   SER A 122      23.190  42.148  55.563  1.00 61.75           C  
ANISOU  761  C   SER A 122     7830   8204   7427   -456    164    -25       C  
ATOM    762  O   SER A 122      21.987  42.390  55.716  1.00 61.93           O  
ANISOU  762  O   SER A 122     7849   8232   7450   -456    191    -48       O  
ATOM    763  CB  SER A 122      24.413  44.342  55.771  1.00 65.58           C  
ANISOU  763  CB  SER A 122     8323   8674   7920   -456    163    -52       C  
ATOM    764  OG  SER A 122      24.978  43.922  57.002  1.00 66.25           O  
ANISOU  764  OG  SER A 122     8426   8776   7969   -490    151    -43       O  
ATOM    765  N   GLY A 123      23.766  41.020  55.972  1.00 59.97           N  
ANISOU  765  N   GLY A 123     7612   7988   7185   -473    142      3       N  
ATOM    766  CA  GLY A 123      23.008  39.956  56.631  1.00 61.44           C  
ANISOU  766  CA  GLY A 123     7804   8192   7348   -492    147     10       C  
ATOM    767  C   GLY A 123      22.893  38.679  55.811  1.00 63.99           C  
ANISOU  767  C   GLY A 123     8114   8510   7687   -476    134     38       C  
ATOM    768  O   GLY A 123      22.828  37.574  56.375  1.00 62.81           O  
ANISOU  768  O   GLY A 123     7971   8373   7518   -495    124     57       O  
ATOM    769  N   LEU A 124      22.862  38.829  54.483  1.00 61.40           N  
ANISOU  769  N   LEU A 124     7770   8164   7394   -442    134     40       N  
ATOM    770  CA  LEU A 124      22.781  37.691  53.560  1.00 58.51           C  
ANISOU  770  CA  LEU A 124     7391   7791   7046   -425    122     64       C  
ATOM    771  C   LEU A 124      24.091  36.912  53.500  1.00 58.63           C  
ANISOU  771  C   LEU A 124     7410   7803   7063   -430     90     97       C  
ATOM    772  O   LEU A 124      24.789  36.924  52.480  1.00 57.76           O  
ANISOU  772  O   LEU A 124     7289   7676   6979   -408     78    109       O  
ATOM    773  CB  LEU A 124      22.398  38.139  52.147  1.00 56.37           C  
ANISOU  773  CB  LEU A 124     7104   7501   6811   -389    131     57       C  
ATOM    774  CG  LEU A 124      20.994  38.620  51.780  1.00 55.33           C  
ANISOU  774  CG  LEU A 124     6963   7368   6692   -375    158     32       C  
ATOM    775  CD1 LEU A 124      19.959  38.252  52.835  1.00 54.17           C  
ANISOU  775  CD1 LEU A 124     6822   7240   6520   -398    176     19       C  
ATOM    776  CD2 LEU A 124      21.005  40.112  51.511  1.00 53.32           C  
ANISOU  776  CD2 LEU A 124     6705   7101   6451   -363    171      6       C  
ATOM    777  N   THR A 125      24.402  36.218  54.591  1.00 58.51           N  
ANISOU  777  N   THR A 125     7408   7803   7021   -460     77    111       N  
ATOM    778  CA  THR A 125      25.679  35.517  54.733  1.00 59.48           C  
ANISOU  778  CA  THR A 125     7533   7922   7143   -469     45    141       C  
ATOM    779  C   THR A 125      25.691  34.141  54.051  1.00 56.01           C  
ANISOU  779  C   THR A 125     7082   7477   6720   -458     30    168       C  
ATOM    780  O   THR A 125      26.661  33.384  54.176  1.00 53.50           O  
ANISOU  780  O   THR A 125     6764   7156   6405   -466      3    195       O  
ATOM    781  CB  THR A 125      26.088  35.396  56.220  1.00 60.96           C  
ANISOU  781  CB  THR A 125     7741   8127   7294   -508     33    147       C  
ATOM    782  OG1 THR A 125      25.001  34.844  56.976  1.00 60.80           O  
ANISOU  782  OG1 THR A 125     7727   8125   7248   -528     48    141       O  
ATOM    783  CG2 THR A 125      26.445  36.773  56.788  1.00 61.93           C  
ANISOU  783  CG2 THR A 125     7875   8250   7404   -518     42    123       C  
ATOM    784  N   SER A 126      24.615  33.833  53.329  1.00 54.45           N  
ANISOU  784  N   SER A 126     6874   7278   6536   -439     47    161       N  
ATOM    785  CA  SER A 126      24.487  32.552  52.632  1.00 55.99           C  
ANISOU  785  CA  SER A 126     7057   7468   6748   -427     36    184       C  
ATOM    786  C   SER A 126      24.101  32.688  51.166  1.00 53.45           C  
ANISOU  786  C   SER A 126     6719   7130   6459   -391     46    178       C  
ATOM    787  O   SER A 126      23.891  31.678  50.493  1.00 55.06           O  
ANISOU  787  O   SER A 126     6912   7329   6677   -380     40    193       O  
ATOM    788  CB  SER A 126      23.451  31.670  53.330  1.00 56.22           C  
ANISOU  788  CB  SER A 126     7089   7513   6755   -444     43    187       C  
ATOM    789  OG  SER A 126      23.916  31.252  54.593  1.00 58.19           O  
ANISOU  789  OG  SER A 126     7354   7777   6976   -478     28    200       O  
ATOM    790  N   LEU A 127      24.009  33.926  50.679  1.00 51.53           N  
ANISOU  790  N   LEU A 127     6474   6879   6226   -376     61    156       N  
ATOM    791  CA  LEU A 127      23.422  34.203  49.368  1.00 50.96           C  
ANISOU  791  CA  LEU A 127     6387   6792   6180   -345     74    146       C  
ATOM    792  C   LEU A 127      24.250  33.604  48.239  1.00 52.00           C  
ANISOU  792  C   LEU A 127     6509   6908   6338   -326     56    167       C  
ATOM    793  O   LEU A 127      25.442  33.886  48.109  1.00 52.37           O  
ANISOU  793  O   LEU A 127     6558   6947   6393   -326     42    176       O  
ATOM    794  CB  LEU A 127      23.217  35.710  49.162  1.00 49.58           C  
ANISOU  794  CB  LEU A 127     6214   6611   6012   -335     91    120       C  
ATOM    795  CG  LEU A 127      22.416  36.187  47.941  1.00 48.51           C  
ANISOU  795  CG  LEU A 127     6066   6462   5901   -306    106    106       C  
ATOM    796  CD1 LEU A 127      20.921  35.966  48.118  1.00 49.22           C  
ANISOU  796  CD1 LEU A 127     6152   6560   5987   -307    126     92       C  
ATOM    797  CD2 LEU A 127      22.698  37.651  47.650  1.00 46.28           C  
ANISOU  797  CD2 LEU A 127     5785   6170   5630   -297    114     87       C  
ATOM    798  N   GLU A 128      23.608  32.765  47.435  1.00 52.22           N  
ANISOU  798  N   GLU A 128     6528   6933   6381   -311     58    175       N  
ATOM    799  CA  GLU A 128      24.281  32.116  46.315  1.00 53.07           C  
ANISOU  799  CA  GLU A 128     6625   7026   6513   -293     44    193       C  
ATOM    800  C   GLU A 128      23.897  32.747  44.978  1.00 48.30           C  
ANISOU  800  C   GLU A 128     6012   6406   5930   -265     57    180       C  
ATOM    801  O   GLU A 128      24.683  32.714  44.034  1.00 46.46           O  
ANISOU  801  O   GLU A 128     5774   6160   5718   -251     48    189       O  
ATOM    802  CB  GLU A 128      23.972  30.618  46.290  1.00 57.54           C  
ANISOU  802  CB  GLU A 128     7186   7596   7080   -296     35    212       C  
ATOM    803  CG  GLU A 128      24.610  29.796  47.402  1.00 61.23           C  
ANISOU  803  CG  GLU A 128     7659   8072   7530   -322     16    231       C  
ATOM    804  CD  GLU A 128      24.129  28.355  47.385  1.00 65.70           C  
ANISOU  804  CD  GLU A 128     8219   8643   8098   -325      8    249       C  
ATOM    805  OE1 GLU A 128      24.435  27.624  46.419  1.00 66.41           O  
ANISOU  805  OE1 GLU A 128     8298   8720   8212   -309      0    262       O  
ATOM    806  OE2 GLU A 128      23.431  27.951  48.336  1.00 71.36           O  
ANISOU  806  OE2 GLU A 128     8943   9376   8794   -345     11    250       O  
ATOM    807  N   ASN A 129      22.691  33.310  44.908  1.00 44.95           N  
ANISOU  807  N   ASN A 129     5587   5985   5504   -259     76    161       N  
ATOM    808  CA  ASN A 129      22.168  33.888  43.672  1.00 43.98           C  
ANISOU  808  CA  ASN A 129     5457   5850   5404   -234     87    150       C  
ATOM    809  C   ASN A 129      21.439  35.218  43.879  1.00 42.55           C  
ANISOU  809  C   ASN A 129     5278   5668   5220   -232    105    124       C  
ATOM    810  O   ASN A 129      20.388  35.270  44.521  1.00 43.40           O  
ANISOU  810  O   ASN A 129     5386   5786   5318   -240    119    110       O  
ATOM    811  CB  ASN A 129      21.270  32.874  42.939  1.00 44.28           C  
ANISOU  811  CB  ASN A 129     5486   5885   5451   -222     89    157       C  
ATOM    812  CG  ASN A 129      20.541  33.475  41.739  1.00 45.97           C  
ANISOU  812  CG  ASN A 129     5693   6087   5685   -199     99    145       C  
ATOM    813  OD1 ASN A 129      19.382  33.149  41.491  1.00 47.20           O  
ANISOU  813  OD1 ASN A 129     5844   6244   5845   -193    108    140       O  
ATOM    814  ND2 ASN A 129      21.212  34.354  40.990  1.00 47.05           N  
ANISOU  814  ND2 ASN A 129     5830   6210   5834   -187     97    142       N  
ATOM    815  N   LEU A 130      22.006  36.286  43.322  1.00 39.81           N  
ANISOU  815  N   LEU A 130     4931   5309   4886   -221    105    116       N  
ATOM    816  CA  LEU A 130      21.387  37.599  43.368  1.00 39.23           C  
ANISOU  816  CA  LEU A 130     4857   5231   4815   -216    121     92       C  
ATOM    817  C   LEU A 130      20.858  38.013  41.993  1.00 40.08           C  
ANISOU  817  C   LEU A 130     4956   5322   4948   -192    126     87       C  
ATOM    818  O   LEU A 130      21.610  38.092  41.013  1.00 40.33           O  
ANISOU  818  O   LEU A 130     4986   5342   4994   -179    116     98       O  
ATOM    819  CB  LEU A 130      22.359  38.651  43.924  1.00 38.86           C  
ANISOU  819  CB  LEU A 130     4818   5183   4763   -225    119     84       C  
ATOM    820  CG  LEU A 130      21.846  40.085  44.143  1.00 37.71           C  
ANISOU  820  CG  LEU A 130     4672   5033   4620   -223    134     58       C  
ATOM    821  CD1 LEU A 130      20.467  40.119  44.780  1.00 38.78           C  
ANISOU  821  CD1 LEU A 130     4807   5179   4749   -230    153     39       C  
ATOM    822  CD2 LEU A 130      22.814  40.886  44.987  1.00 37.32           C  
ANISOU  822  CD2 LEU A 130     4633   4986   4558   -238    130     52       C  
ATOM    823  N   VAL A 131      19.560  38.287  41.936  1.00 38.43           N  
ANISOU  823  N   VAL A 131     4742   5114   4745   -186    140     72       N  
ATOM    824  CA  VAL A 131      18.922  38.658  40.695  1.00 38.59           C  
ANISOU  824  CA  VAL A 131     4754   5119   4789   -165    143     68       C  
ATOM    825  C   VAL A 131      18.429  40.093  40.825  1.00 40.85           C  
ANISOU  825  C   VAL A 131     5038   5397   5084   -161    156     44       C  
ATOM    826  O   VAL A 131      17.432  40.366  41.501  1.00 43.59           O  
ANISOU  826  O   VAL A 131     5382   5750   5428   -167    171     26       O  
ATOM    827  CB  VAL A 131      17.783  37.684  40.336  1.00 38.58           C  
ANISOU  827  CB  VAL A 131     4745   5119   4792   -159    147     72       C  
ATOM    828  CG1 VAL A 131      17.043  38.140  39.086  1.00 38.39           C  
ANISOU  828  CG1 VAL A 131     4714   5080   4793   -138    149     67       C  
ATOM    829  CG2 VAL A 131      18.335  36.278  40.140  1.00 38.17           C  
ANISOU  829  CG2 VAL A 131     4694   5072   4733   -161    133     96       C  
ATOM    830  N   ALA A 132      19.155  41.003  40.183  1.00 39.09           N  
ANISOU  830  N   ALA A 132     4817   5162   4873   -152    150     43       N  
ATOM    831  CA  ALA A 132      18.884  42.425  40.272  1.00 37.62           C  
ANISOU  831  CA  ALA A 132     4629   4966   4698   -148    160     22       C  
ATOM    832  C   ALA A 132      18.644  42.970  38.875  1.00 38.31           C  
ANISOU  832  C   ALA A 132     4710   5034   4810   -128    155     25       C  
ATOM    833  O   ALA A 132      19.200  43.999  38.470  1.00 37.81           O  
ANISOU  833  O   ALA A 132     4648   4959   4757   -122    152     21       O  
ATOM    834  CB  ALA A 132      20.037  43.137  40.950  1.00 37.48           C  
ANISOU  834  CB  ALA A 132     4620   4951   4670   -160    156     19       C  
ATOM    835  N   VAL A 133      17.797  42.248  38.149  1.00 38.66           N  
ANISOU  835  N   VAL A 133     4748   5075   4864   -118    155     31       N  
ATOM    836  CA  VAL A 133      17.414  42.581  36.787  1.00 37.92           C  
ANISOU  836  CA  VAL A 133     4650   4964   4793   -100    149     36       C  
ATOM    837  C   VAL A 133      16.461  43.758  36.815  1.00 38.07           C  
ANISOU  837  C   VAL A 133     4661   4972   4830    -94    159     14       C  
ATOM    838  O   VAL A 133      15.619  43.852  37.700  1.00 38.72           O  
ANISOU  838  O   VAL A 133     4738   5061   4911   -101    172     -1       O  
ATOM    839  CB  VAL A 133      16.775  41.352  36.092  1.00 37.22           C  
ANISOU  839  CB  VAL A 133     4557   4877   4706    -93    144     49       C  
ATOM    840  CG1 VAL A 133      16.151  41.708  34.749  1.00 36.26           C  
ANISOU  840  CG1 VAL A 133     4431   4737   4607    -76    139     52       C  
ATOM    841  CG2 VAL A 133      17.820  40.259  35.920  1.00 37.01           C  
ANISOU  841  CG2 VAL A 133     4537   4858   4666    -97    134     70       C  
ATOM    842  N   GLU A 134      16.616  44.658  35.850  1.00 39.47           N  
ANISOU  842  N   GLU A 134     4837   5132   5026    -82    152     15       N  
ATOM    843  CA  GLU A 134      15.780  45.854  35.736  1.00 43.30           C  
ANISOU  843  CA  GLU A 134     5313   5602   5534    -75    158     -2       C  
ATOM    844  C   GLU A 134      15.602  46.571  37.079  1.00 44.63           C  
ANISOU  844  C   GLU A 134     5480   5777   5698    -87    173    -26       C  
ATOM    845  O   GLU A 134      14.482  46.838  37.517  1.00 45.30           O  
ANISOU  845  O   GLU A 134     5555   5861   5794    -87    186    -44       O  
ATOM    846  CB  GLU A 134      14.429  45.539  35.085  1.00 43.80           C  
ANISOU  846  CB  GLU A 134     5366   5657   5616    -65    159     -3       C  
ATOM    847  CG  GLU A 134      13.819  46.737  34.368  1.00 47.14           C  
ANISOU  847  CG  GLU A 134     5782   6059   6070    -53    156    -12       C  
ATOM    848  CD  GLU A 134      12.341  46.572  34.042  1.00 51.76           C  
ANISOU  848  CD  GLU A 134     6354   6635   6676    -45    158    -19       C  
ATOM    849  OE1 GLU A 134      11.739  47.539  33.526  1.00 55.08           O  
ANISOU  849  OE1 GLU A 134     6766   7036   7124    -36    155    -27       O  
ATOM    850  OE2 GLU A 134      11.767  45.490  34.300  1.00 54.37           O  
ANISOU  850  OE2 GLU A 134     6682   6976   6997    -48    163    -15       O  
ATOM    851  N   THR A 135      16.723  46.863  37.728  1.00 43.66           N  
ANISOU  851  N   THR A 135     5367   5663   5559    -98    172    -27       N  
ATOM    852  CA  THR A 135      16.714  47.610  38.974  1.00 45.18           C  
ANISOU  852  CA  THR A 135     5560   5862   5745   -111    186    -49       C  
ATOM    853  C   THR A 135      17.228  49.037  38.738  1.00 46.63           C  
ANISOU  853  C   THR A 135     5743   6030   5944   -106    183    -59       C  
ATOM    854  O   THR A 135      17.368  49.826  39.678  1.00 46.53           O  
ANISOU  854  O   THR A 135     5731   6020   5927   -116    193    -78       O  
ATOM    855  CB  THR A 135      17.508  46.891  40.096  1.00 45.22           C  
ANISOU  855  CB  THR A 135     5575   5888   5717   -129    187    -45       C  
ATOM    856  OG1 THR A 135      18.787  46.470  39.607  1.00 47.37           O  
ANISOU  856  OG1 THR A 135     5856   6161   5981   -129    171    -22       O  
ATOM    857  CG2 THR A 135      16.758  45.677  40.593  1.00 43.94           C  
ANISOU  857  CG2 THR A 135     5411   5740   5541   -137    194    -42       C  
ATOM    858  N   LYS A 136      17.472  49.369  37.470  1.00 46.97           N  
ANISOU  858  N   LYS A 136     5784   6056   6004    -92    170    -46       N  
ATOM    859  CA  LYS A 136      18.001  50.681  37.071  1.00 46.37           C  
ANISOU  859  CA  LYS A 136     5708   5964   5945    -86    165    -51       C  
ATOM    860  C   LYS A 136      19.462  50.897  37.486  1.00 44.50           C  
ANISOU  860  C   LYS A 136     5482   5733   5690    -96    159    -45       C  
ATOM    861  O   LYS A 136      19.982  52.010  37.363  1.00 44.97           O  
ANISOU  861  O   LYS A 136     5543   5782   5761    -94    156    -51       O  
ATOM    862  CB  LYS A 136      17.128  51.835  37.590  1.00 48.41           C  
ANISOU  862  CB  LYS A 136     5956   6212   6224    -86    177    -79       C  
ATOM    863  CG  LYS A 136      15.798  52.027  36.884  1.00 51.27           C  
ANISOU  863  CG  LYS A 136     6305   6559   6615    -73    178    -84       C  
ATOM    864  CD  LYS A 136      15.133  53.327  37.322  1.00 54.21           C  
ANISOU  864  CD  LYS A 136     6666   6918   7013    -71    189   -111       C  
ATOM    865  CE  LYS A 136      13.732  53.485  36.744  1.00 56.50           C  
ANISOU  865  CE  LYS A 136     6940   7191   7333    -59    190   -118       C  
ATOM    866  NZ  LYS A 136      13.722  53.632  35.258  1.00 60.62           N  
ANISOU  866  NZ  LYS A 136     7461   7695   7875    -45    170    -97       N  
ATOM    867  N   LEU A 137      20.122  49.839  37.954  1.00 42.71           N  
ANISOU  867  N   LEU A 137     5264   5524   5438   -106    157    -32       N  
ATOM    868  CA  LEU A 137      21.549  49.895  38.307  1.00 44.45           C  
ANISOU  868  CA  LEU A 137     5494   5750   5643   -115    149    -23       C  
ATOM    869  C   LEU A 137      22.406  50.569  37.219  1.00 42.51           C  
ANISOU  869  C   LEU A 137     5250   5488   5412   -105    137    -11       C  
ATOM    870  O   LEU A 137      22.229  50.301  36.042  1.00 42.24           O  
ANISOU  870  O   LEU A 137     5214   5445   5389    -93    130      1       O  
ATOM    871  CB  LEU A 137      22.076  48.485  38.573  1.00 44.75           C  
ANISOU  871  CB  LEU A 137     5538   5804   5659   -123    144     -5       C  
ATOM    872  CG  LEU A 137      23.010  48.240  39.763  1.00 47.36           C  
ANISOU  872  CG  LEU A 137     5877   6149   5966   -141    143     -5       C  
ATOM    873  CD1 LEU A 137      23.536  46.814  39.700  1.00 49.01           C  
ANISOU  873  CD1 LEU A 137     6090   6370   6161   -146    133     17       C  
ATOM    874  CD2 LEU A 137      24.172  49.215  39.836  1.00 47.88           C  
ANISOU  874  CD2 LEU A 137     5948   6209   6035   -144    136     -6       C  
ATOM    875  N   ALA A 138      23.334  51.434  37.619  1.00 43.20           N  
ANISOU  875  N   ALA A 138     5342   5573   5498   -111    135    -17       N  
ATOM    876  CA  ALA A 138      24.168  52.170  36.655  1.00 45.17           C  
ANISOU  876  CA  ALA A 138     5593   5807   5762   -102    125     -7       C  
ATOM    877  C   ALA A 138      25.605  51.643  36.531  1.00 46.25           C  
ANISOU  877  C   ALA A 138     5737   5948   5886   -108    115     11       C  
ATOM    878  O   ALA A 138      26.263  51.863  35.502  1.00 45.12           O  
ANISOU  878  O   ALA A 138     5595   5794   5752   -100    107     25       O  
ATOM    879  CB  ALA A 138      24.174  53.660  36.976  1.00 43.17           C  
ANISOU  879  CB  ALA A 138     5336   5541   5523   -103    128    -25       C  
ATOM    880  N   SER A 139      26.077  50.947  37.569  1.00 47.59           N  
ANISOU  880  N   SER A 139     5911   6134   6035   -121    116     13       N  
ATOM    881  CA  SER A 139      27.475  50.506  37.649  1.00 48.98           C  
ANISOU  881  CA  SER A 139     6094   6315   6201   -128    106     29       C  
ATOM    882  C   SER A 139      27.690  49.313  38.595  1.00 48.89           C  
ANISOU  882  C   SER A 139     6085   6321   6167   -142    104     35       C  
ATOM    883  O   SER A 139      27.119  49.270  39.681  1.00 48.48           O  
ANISOU  883  O   SER A 139     6035   6280   6103   -153    111     22       O  
ATOM    884  CB  SER A 139      28.361  51.696  38.065  1.00 48.99           C  
ANISOU  884  CB  SER A 139     6098   6310   6207   -134    103     21       C  
ATOM    885  OG  SER A 139      29.367  51.333  39.001  1.00 50.51           O  
ANISOU  885  OG  SER A 139     6295   6512   6382   -149     97     26       O  
ATOM    886  N   LEU A 140      28.521  48.356  38.180  1.00 48.67           N  
ANISOU  886  N   LEU A 140     6059   6296   6137   -142     95     56       N  
ATOM    887  CA  LEU A 140      28.969  47.289  39.082  1.00 48.81           C  
ANISOU  887  CA  LEU A 140     6080   6328   6136   -157     89     65       C  
ATOM    888  C   LEU A 140      29.848  47.837  40.207  1.00 50.23           C  
ANISOU  888  C   LEU A 140     6266   6513   6306   -172     85     60       C  
ATOM    889  O   LEU A 140      29.669  47.471  41.367  1.00 50.78           O  
ANISOU  889  O   LEU A 140     6340   6597   6357   -188     85     55       O  
ATOM    890  CB  LEU A 140      29.741  46.201  38.325  1.00 47.48           C  
ANISOU  890  CB  LEU A 140     5909   6158   5971   -153     80     88       C  
ATOM    891  CG  LEU A 140      29.010  45.152  37.486  1.00 46.26           C  
ANISOU  891  CG  LEU A 140     5751   6005   5821   -143     82     97       C  
ATOM    892  CD1 LEU A 140      30.010  44.331  36.693  1.00 45.66           C  
ANISOU  892  CD1 LEU A 140     5673   5923   5751   -139     73    117       C  
ATOM    893  CD2 LEU A 140      28.168  44.241  38.358  1.00 46.76           C  
ANISOU  893  CD2 LEU A 140     5814   6082   5868   -151     85     95       C  
ATOM    894  N   GLU A 141      30.784  48.719  39.854  1.00 53.17           N  
ANISOU  894  N   GLU A 141     6638   6873   6689   -169     80     61       N  
ATOM    895  CA  GLU A 141      31.780  49.275  40.787  1.00 57.09           C  
ANISOU  895  CA  GLU A 141     7141   7372   7179   -184     73     58       C  
ATOM    896  C   GLU A 141      31.190  49.847  42.085  1.00 55.71           C  
ANISOU  896  C   GLU A 141     6971   7207   6988   -198     80     37       C  
ATOM    897  O   GLU A 141      31.814  49.763  43.144  1.00 51.58           O  
ANISOU  897  O   GLU A 141     6454   6692   6448   -215     73     37       O  
ATOM    898  CB  GLU A 141      32.641  50.331  40.081  1.00 61.54           C  
ANISOU  898  CB  GLU A 141     7703   7919   7760   -176     69     59       C  
ATOM    899  CG  GLU A 141      33.475  49.799  38.914  1.00 69.52           C  
ANISOU  899  CG  GLU A 141     8709   8920   8783   -166     62     79       C  
ATOM    900  CD  GLU A 141      34.958  49.637  39.246  1.00 76.47           C  
ANISOU  900  CD  GLU A 141     9590   9799   9664   -176     49     92       C  
ATOM    901  OE1 GLU A 141      35.793  50.229  38.524  1.00 77.47           O  
ANISOU  901  OE1 GLU A 141     9714   9913   9806   -170     46     97       O  
ATOM    902  OE2 GLU A 141      35.297  48.927  40.222  1.00 78.99           O  
ANISOU  902  OE2 GLU A 141     9912  10129   9970   -190     41     97       O  
ATOM    903  N   SER A 142      29.984  50.405  41.992  1.00 56.30           N  
ANISOU  903  N   SER A 142     7043   7280   7067   -191     94     18       N  
ATOM    904  CA  SER A 142      29.287  50.978  43.146  1.00 57.66           C  
ANISOU  904  CA  SER A 142     7219   7461   7227   -203    105     -4       C  
ATOM    905  C   SER A 142      28.193  50.064  43.737  1.00 57.24           C  
ANISOU  905  C   SER A 142     7166   7423   7158   -210    114     -9       C  
ATOM    906  O   SER A 142      27.424  50.481  44.612  1.00 58.01           O  
ANISOU  906  O   SER A 142     7266   7528   7246   -220    127    -30       O  
ATOM    907  CB  SER A 142      28.691  52.340  42.772  1.00 60.20           C  
ANISOU  907  CB  SER A 142     7535   7768   7567   -192    115    -25       C  
ATOM    908  OG  SER A 142      27.707  52.210  41.757  1.00 61.49           O  
ANISOU  908  OG  SER A 142     7691   7924   7748   -175    121    -24       O  
ATOM    909  N   PHE A 143      28.137  48.824  43.261  1.00 54.11           N  
ANISOU  909  N   PHE A 143     6768   7031   6759   -206    109     10       N  
ATOM    910  CA  PHE A 143      27.178  47.838  43.747  1.00 53.52           C  
ANISOU  910  CA  PHE A 143     6693   6971   6670   -213    116      9       C  
ATOM    911  C   PHE A 143      27.794  47.132  44.954  1.00 52.20           C  
ANISOU  911  C   PHE A 143     6535   6820   6477   -236    107     17       C  
ATOM    912  O   PHE A 143      28.871  46.549  44.829  1.00 54.92           O  
ANISOU  912  O   PHE A 143     6882   7164   6820   -239     91     37       O  
ATOM    913  CB  PHE A 143      26.861  46.843  42.619  1.00 53.30           C  
ANISOU  913  CB  PHE A 143     6658   6939   6653   -197    112     27       C  
ATOM    914  CG  PHE A 143      25.552  46.119  42.769  1.00 51.72           C  
ANISOU  914  CG  PHE A 143     6454   6747   6447   -197    123     22       C  
ATOM    915  CD1 PHE A 143      24.415  46.765  43.250  1.00 52.49           C  
ANISOU  915  CD1 PHE A 143     6550   6847   6545   -198    139     -1       C  
ATOM    916  CD2 PHE A 143      25.444  44.792  42.375  1.00 51.72           C  
ANISOU  916  CD2 PHE A 143     6452   6753   6445   -194    117     41       C  
ATOM    917  CE1 PHE A 143      23.207  46.086  43.371  1.00 52.22           C  
ANISOU  917  CE1 PHE A 143     6511   6821   6507   -198    150     -6       C  
ATOM    918  CE2 PHE A 143      24.237  44.111  42.487  1.00 51.98           C  
ANISOU  918  CE2 PHE A 143     6481   6793   6473   -193    126     37       C  
ATOM    919  CZ  PHE A 143      23.116  44.759  42.986  1.00 51.52           C  
ANISOU  919  CZ  PHE A 143     6420   6737   6414   -195    143     13       C  
ATOM    920  N   PRO A 144      27.121  47.185  46.126  1.00 51.16           N  
ANISOU  920  N   PRO A 144     6410   6703   6326   -253    118      0       N  
ATOM    921  CA  PRO A 144      27.670  46.714  47.403  1.00 50.14           C  
ANISOU  921  CA  PRO A 144     6292   6589   6169   -279    110      5       C  
ATOM    922  C   PRO A 144      27.528  45.204  47.629  1.00 50.24           C  
ANISOU  922  C   PRO A 144     6305   6614   6167   -287    103     25       C  
ATOM    923  O   PRO A 144      26.897  44.777  48.600  1.00 50.18           O  
ANISOU  923  O   PRO A 144     6304   6622   6137   -304    110     18       O  
ATOM    924  CB  PRO A 144      26.828  47.474  48.422  1.00 51.39           C  
ANISOU  924  CB  PRO A 144     6455   6756   6313   -292    129    -23       C  
ATOM    925  CG  PRO A 144      25.487  47.554  47.771  1.00 51.18           C  
ANISOU  925  CG  PRO A 144     6418   6724   6302   -275    146    -36       C  
ATOM    926  CD  PRO A 144      25.758  47.724  46.298  1.00 51.92           C  
ANISOU  926  CD  PRO A 144     6501   6799   6424   -250    139    -24       C  
ATOM    927  N   ILE A 145      28.123  44.410  46.742  1.00 49.57           N  
ANISOU  927  N   ILE A 145     6215   6522   6096   -275     89     49       N  
ATOM    928  CA  ILE A 145      28.068  42.948  46.846  1.00 49.03           C  
ANISOU  928  CA  ILE A 145     6146   6463   6019   -281     80     69       C  
ATOM    929  C   ILE A 145      29.425  42.330  47.223  1.00 49.26           C  
ANISOU  929  C   ILE A 145     6179   6493   6043   -294     57     92       C  
ATOM    930  O   ILE A 145      29.535  41.110  47.404  1.00 47.55           O  
ANISOU  930  O   ILE A 145     5962   6284   5820   -301     46    111       O  
ATOM    931  CB  ILE A 145      27.470  42.295  45.569  1.00 48.96           C  
ANISOU  931  CB  ILE A 145     6126   6446   6030   -258     83     78       C  
ATOM    932  CG1 ILE A 145      28.343  42.572  44.335  1.00 49.50           C  
ANISOU  932  CG1 ILE A 145     6188   6497   6123   -240     75     89       C  
ATOM    933  CG2 ILE A 145      26.045  42.786  45.347  1.00 47.42           C  
ANISOU  933  CG2 ILE A 145     5926   6250   5839   -249    104     57       C  
ATOM    934  CD1 ILE A 145      28.070  41.675  43.146  1.00 47.78           C  
ANISOU  934  CD1 ILE A 145     5961   6272   5920   -222     73    103       C  
ATOM    935  N   GLY A 146      30.440  43.188  47.363  1.00 49.68           N  
ANISOU  935  N   GLY A 146     6236   6539   6100   -297     49     90       N  
ATOM    936  CA  GLY A 146      31.803  42.772  47.696  1.00 49.78           C  
ANISOU  936  CA  GLY A 146     6251   6549   6111   -309     26    111       C  
ATOM    937  C   GLY A 146      31.934  42.017  49.008  1.00 51.08           C  
ANISOU  937  C   GLY A 146     6426   6730   6250   -336     15    120       C  
ATOM    938  O   GLY A 146      32.980  41.432  49.281  1.00 47.79           O  
ANISOU  938  O   GLY A 146     6011   6313   5835   -347     -6    140       O  
ATOM    939  N   GLN A 147      30.870  42.036  49.812  1.00 55.88           N  
ANISOU  939  N   GLN A 147     7042   7354   6836   -349     29    104       N  
ATOM    940  CA  GLN A 147      30.825  41.338  51.097  1.00 62.10           C  
ANISOU  940  CA  GLN A 147     7841   8158   7593   -378     20    112       C  
ATOM    941  C   GLN A 147      30.288  39.906  50.926  1.00 64.06           C  
ANISOU  941  C   GLN A 147     8084   8414   7841   -378     16    129       C  
ATOM    942  O   GLN A 147      30.635  39.014  51.697  1.00 65.30           O  
ANISOU  942  O   GLN A 147     8248   8580   7982   -398      0    147       O  
ATOM    943  CB  GLN A 147      29.939  42.106  52.097  1.00 68.62           C  
ANISOU  943  CB  GLN A 147     8678   8998   8394   -395     39     84       C  
ATOM    944  CG  GLN A 147      30.158  41.733  53.568  1.00 76.53           C  
ANISOU  944  CG  GLN A 147     9697  10018   9362   -430     29     89       C  
ATOM    945  CD  GLN A 147      28.885  41.279  54.308  1.00 81.65           C  
ANISOU  945  CD  GLN A 147    10352  10685   9985   -445     47     77       C  
ATOM    946  OE1 GLN A 147      27.849  40.986  53.692  1.00 80.05           O  
ANISOU  946  OE1 GLN A 147    10139  10482   9792   -429     63     71       O  
ATOM    947  NE2 GLN A 147      28.973  41.197  55.640  1.00 75.12           N  
ANISOU  947  NE2 GLN A 147     9541   9874   9124   -478     42     76       N  
ATOM    948  N   LEU A 148      29.449  39.700  49.913  1.00 62.10           N  
ANISOU  948  N   LEU A 148     7825   8160   7609   -355     30    125       N  
ATOM    949  CA  LEU A 148      28.699  38.450  49.735  1.00 59.38           C  
ANISOU  949  CA  LEU A 148     7475   7822   7263   -353     31    137       C  
ATOM    950  C   LEU A 148      29.558  37.300  49.194  1.00 57.53           C  
ANISOU  950  C   LEU A 148     7233   7579   7045   -348      9    166       C  
ATOM    951  O   LEU A 148      29.419  36.903  48.038  1.00 55.40           O  
ANISOU  951  O   LEU A 148     6951   7298   6797   -326     12    172       O  
ATOM    952  CB  LEU A 148      27.497  38.700  48.814  1.00 57.53           C  
ANISOU  952  CB  LEU A 148     7231   7583   7043   -330     53    121       C  
ATOM    953  CG  LEU A 148      26.278  39.488  49.313  1.00 58.33           C  
ANISOU  953  CG  LEU A 148     7337   7693   7132   -334     78     93       C  
ATOM    954  CD1 LEU A 148      26.631  40.558  50.336  1.00 62.12           C  
ANISOU  954  CD1 LEU A 148     7829   8179   7595   -352     82     75       C  
ATOM    955  CD2 LEU A 148      25.549  40.117  48.132  1.00 59.05           C  
ANISOU  955  CD2 LEU A 148     7417   7770   7248   -306     94     79       C  
ATOM    956  N   ILE A 149      30.420  36.756  50.050  1.00 56.57           N  
ANISOU  956  N   ILE A 149     7118   7464   6912   -370    -11    184       N  
ATOM    957  CA  ILE A 149      31.454  35.801  49.638  1.00 56.91           C  
ANISOU  957  CA  ILE A 149     7153   7496   6974   -367    -35    211       C  
ATOM    958  C   ILE A 149      30.891  34.465  49.130  1.00 57.03           C  
ANISOU  958  C   ILE A 149     7158   7512   6997   -359    -36    226       C  
ATOM    959  O   ILE A 149      31.543  33.756  48.357  1.00 57.67           O  
ANISOU  959  O   ILE A 149     7228   7581   7103   -347    -49    243       O  
ATOM    960  CB  ILE A 149      32.502  35.592  50.757  1.00 58.67           C  
ANISOU  960  CB  ILE A 149     7384   7723   7183   -394    -60    227       C  
ATOM    961  CG1 ILE A 149      33.088  36.947  51.189  1.00 59.78           C  
ANISOU  961  CG1 ILE A 149     7533   7861   7316   -401    -58    212       C  
ATOM    962  CG2 ILE A 149      33.627  34.680  50.283  1.00 59.94           C  
ANISOU  962  CG2 ILE A 149     7534   7870   7369   -390    -84    254       C  
ATOM    963  CD1 ILE A 149      33.800  36.946  52.530  1.00 61.60           C  
ANISOU  963  CD1 ILE A 149     7779   8102   7525   -432    -78    221       C  
ATOM    964  N   THR A 150      29.671  34.140  49.543  1.00 56.83           N  
ANISOU  964  N   THR A 150     7137   7501   6954   -365    -23    218       N  
ATOM    965  CA  THR A 150      29.005  32.918  49.093  1.00 55.36           C  
ANISOU  965  CA  THR A 150     6942   7316   6775   -358    -23    230       C  
ATOM    966  C   THR A 150      28.414  33.035  47.685  1.00 53.98           C  
ANISOU  966  C   THR A 150     6755   7129   6623   -328     -7    221       C  
ATOM    967  O   THR A 150      28.008  32.030  47.097  1.00 56.08           O  
ANISOU  967  O   THR A 150     7013   7393   6900   -318     -8    231       O  
ATOM    968  CB  THR A 150      27.877  32.492  50.059  1.00 56.68           C  
ANISOU  968  CB  THR A 150     7118   7502   6913   -377    -14    225       C  
ATOM    969  OG1 THR A 150      27.025  33.613  50.337  1.00 56.82           O  
ANISOU  969  OG1 THR A 150     7143   7527   6918   -377     10    197       O  
ATOM    970  CG2 THR A 150      28.450  31.932  51.357  1.00 57.13           C  
ANISOU  970  CG2 THR A 150     7187   7571   6948   -409    -34    242       C  
ATOM    971  N   LEU A 151      28.372  34.256  47.153  1.00 51.43           N  
ANISOU  971  N   LEU A 151     6433   6799   6308   -313      6    202       N  
ATOM    972  CA  LEU A 151      27.701  34.549  45.887  1.00 47.54           C  
ANISOU  972  CA  LEU A 151     5931   6297   5835   -287     22    191       C  
ATOM    973  C   LEU A 151      28.281  33.753  44.738  1.00 47.48           C  
ANISOU  973  C   LEU A 151     5911   6274   5852   -270     12    208       C  
ATOM    974  O   LEU A 151      29.499  33.588  44.637  1.00 48.91           O  
ANISOU  974  O   LEU A 151     6090   6447   6044   -272     -3    222       O  
ATOM    975  CB  LEU A 151      27.775  36.041  45.572  1.00 46.31           C  
ANISOU  975  CB  LEU A 151     5778   6134   5684   -277     34    171       C  
ATOM    976  CG  LEU A 151      26.861  36.588  44.476  1.00 45.79           C  
ANISOU  976  CG  LEU A 151     5704   6058   5632   -254     51    156       C  
ATOM    977  CD1 LEU A 151      25.384  36.475  44.846  1.00 45.19           C  
ANISOU  977  CD1 LEU A 151     5629   5994   5545   -256     68    142       C  
ATOM    978  CD2 LEU A 151      27.237  38.024  44.158  1.00 43.86           C  
ANISOU  978  CD2 LEU A 151     5462   5804   5396   -246     58    140       C  
ATOM    979  N   LYS A 152      27.393  33.264  43.878  1.00 47.94           N  
ANISOU  979  N   LYS A 152     5963   6331   5921   -254     21    207       N  
ATOM    980  CA  LYS A 152      27.770  32.400  42.766  1.00 48.67           C  
ANISOU  980  CA  LYS A 152     6045   6411   6036   -239     14    221       C  
ATOM    981  C   LYS A 152      27.271  32.954  41.438  1.00 46.93           C  
ANISOU  981  C   LYS A 152     5820   6180   5831   -215     28    209       C  
ATOM    982  O   LYS A 152      28.014  33.006  40.457  1.00 44.66           O  
ANISOU  982  O   LYS A 152     5527   5878   5562   -202     25    214       O  
ATOM    983  CB  LYS A 152      27.222  30.981  42.985  1.00 50.21           C  
ANISOU  983  CB  LYS A 152     6236   6613   6227   -244      8    235       C  
ATOM    984  CG  LYS A 152      27.855  30.254  44.158  1.00 52.15           C  
ANISOU  984  CG  LYS A 152     6484   6867   6460   -268    -10    252       C  
ATOM    985  CD  LYS A 152      27.520  28.774  44.186  1.00 52.55           C  
ANISOU  985  CD  LYS A 152     6529   6921   6515   -272    -19    269       C  
ATOM    986  CE  LYS A 152      28.316  28.113  45.301  1.00 54.92           C  
ANISOU  986  CE  LYS A 152     6833   7227   6806   -296    -41    288       C  
ATOM    987  NZ  LYS A 152      28.379  26.634  45.171  1.00 57.24           N  
ANISOU  987  NZ  LYS A 152     7118   7518   7113   -298    -55    309       N  
ATOM    988  N   LYS A 153      26.006  33.359  41.425  1.00 46.04           N  
ANISOU  988  N   LYS A 153     5709   6073   5711   -210     44    194       N  
ATOM    989  CA  LYS A 153      25.348  33.833  40.225  1.00 45.45           C  
ANISOU  989  CA  LYS A 153     5629   5987   5650   -189     55    184       C  
ATOM    990  C   LYS A 153      24.908  35.269  40.442  1.00 44.13           C  
ANISOU  990  C   LYS A 153     5468   5821   5479   -188     68    163       C  
ATOM    991  O   LYS A 153      24.135  35.551  41.348  1.00 45.21           O  
ANISOU  991  O   LYS A 153     5608   5968   5601   -198     77    151       O  
ATOM    992  CB  LYS A 153      24.126  32.965  39.901  1.00 47.56           C  
ANISOU  992  CB  LYS A 153     5892   6259   5919   -183     61    185       C  
ATOM    993  CG  LYS A 153      24.407  31.482  39.723  1.00 50.85           C  
ANISOU  993  CG  LYS A 153     6303   6676   6340   -185     49    204       C  
ATOM    994  CD  LYS A 153      23.109  30.702  39.564  1.00 54.55           C  
ANISOU  994  CD  LYS A 153     6767   7150   6807   -181     56    204       C  
ATOM    995  CE  LYS A 153      23.354  29.199  39.523  1.00 57.07           C  
ANISOU  995  CE  LYS A 153     7081   7471   7132   -185     43    223       C  
ATOM    996  NZ  LYS A 153      22.077  28.425  39.547  1.00 57.49           N  
ANISOU  996  NZ  LYS A 153     7131   7531   7181   -183     49    223       N  
ATOM    997  N   LEU A 154      25.411  36.171  39.606  1.00 41.97           N  
ANISOU  997  N   LEU A 154     5193   5533   5218   -176     70    158       N  
ATOM    998  CA  LEU A 154      25.033  37.565  39.655  1.00 40.23           C  
ANISOU  998  CA  LEU A 154     4975   5309   4998   -172     81    138       C  
ATOM    999  C   LEU A 154      24.331  37.935  38.356  1.00 40.93           C  
ANISOU  999  C   LEU A 154     5059   5386   5104   -152     88    133       C  
ATOM   1000  O   LEU A 154      24.901  37.847  37.269  1.00 41.44           O  
ANISOU 1000  O   LEU A 154     5122   5439   5182   -141     83    142       O  
ATOM   1001  CB  LEU A 154      26.265  38.439  39.914  1.00 41.31           C  
ANISOU 1001  CB  LEU A 154     5117   5441   5136   -177     75    138       C  
ATOM   1002  CG  LEU A 154      26.169  39.924  40.298  1.00 42.15           C  
ANISOU 1002  CG  LEU A 154     5228   5545   5240   -179     83    118       C  
ATOM   1003  CD1 LEU A 154      26.283  40.805  39.071  1.00 43.94           C  
ANISOU 1003  CD1 LEU A 154     5452   5756   5487   -161     86    114       C  
ATOM   1004  CD2 LEU A 154      24.912  40.278  41.078  1.00 42.13           C  
ANISOU 1004  CD2 LEU A 154     5227   5553   5227   -185     97    100       C  
ATOM   1005  N   ASN A 155      23.073  38.330  38.482  1.00 41.61           N  
ANISOU 1005  N   ASN A 155     5144   5475   5190   -149    100    118       N  
ATOM   1006  CA  ASN A 155      22.258  38.676  37.336  1.00 40.29           C  
ANISOU 1006  CA  ASN A 155     4972   5296   5039   -131    105    113       C  
ATOM   1007  C   ASN A 155      21.904  40.161  37.381  1.00 41.39           C  
ANISOU 1007  C   ASN A 155     5112   5428   5185   -127    114     94       C  
ATOM   1008  O   ASN A 155      21.039  40.579  38.162  1.00 42.94           O  
ANISOU 1008  O   ASN A 155     5307   5629   5376   -133    124     78       O  
ATOM   1009  CB  ASN A 155      20.994  37.804  37.311  1.00 39.12           C  
ANISOU 1009  CB  ASN A 155     4819   5153   4890   -129    110    113       C  
ATOM   1010  CG  ASN A 155      20.289  37.812  35.964  1.00 39.61           C  
ANISOU 1010  CG  ASN A 155     4876   5202   4969   -111    111    114       C  
ATOM   1011  OD1 ASN A 155      19.397  37.005  35.733  1.00 41.29           O  
ANISOU 1011  OD1 ASN A 155     5085   5418   5184   -107    112    117       O  
ATOM   1012  ND2 ASN A 155      20.676  38.720  35.072  1.00 39.16           N  
ANISOU 1012  ND2 ASN A 155     4822   5133   4925   -101    109    112       N  
ATOM   1013  N   VAL A 156      22.580  40.949  36.546  1.00 39.82           N  
ANISOU 1013  N   VAL A 156     4915   5216   4998   -118    110     95       N  
ATOM   1014  CA  VAL A 156      22.287  42.375  36.420  1.00 39.35           C  
ANISOU 1014  CA  VAL A 156     4854   5145   4948   -113    116     79       C  
ATOM   1015  C   VAL A 156      21.857  42.775  35.003  1.00 39.46           C  
ANISOU 1015  C   VAL A 156     4865   5143   4981    -96    114     81       C  
ATOM   1016  O   VAL A 156      22.128  43.894  34.549  1.00 40.73           O  
ANISOU 1016  O   VAL A 156     5028   5293   5154    -91    113     76       O  
ATOM   1017  CB  VAL A 156      23.469  43.261  36.890  1.00 39.14           C  
ANISOU 1017  CB  VAL A 156     4833   5117   4919   -120    112     76       C  
ATOM   1018  CG1 VAL A 156      23.592  43.239  38.409  1.00 37.53           C  
ANISOU 1018  CG1 VAL A 156     4633   4928   4696   -138    116     68       C  
ATOM   1019  CG2 VAL A 156      24.766  42.835  36.221  1.00 37.63           C  
ANISOU 1019  CG2 VAL A 156     4645   4921   4730   -119    101     95       C  
ATOM   1020  N   ALA A 157      21.183  41.867  34.306  1.00 38.11           N  
ANISOU 1020  N   ALA A 157     4692   4972   4814    -89    112     90       N  
ATOM   1021  CA  ALA A 157      20.627  42.190  32.998  1.00 38.08           C  
ANISOU 1021  CA  ALA A 157     4686   4954   4827    -75    109     92       C  
ATOM   1022  C   ALA A 157      19.606  43.331  33.087  1.00 39.15           C  
ANISOU 1022  C   ALA A 157     4816   5081   4976    -70    116     74       C  
ATOM   1023  O   ALA A 157      18.984  43.545  34.137  1.00 37.53           O  
ANISOU 1023  O   ALA A 157     4607   4883   4767    -77    125     60       O  
ATOM   1024  CB  ALA A 157      19.990  40.963  32.379  1.00 36.80           C  
ANISOU 1024  CB  ALA A 157     4522   4795   4665    -70    107    103       C  
ATOM   1025  N   HIS A 158      19.443  44.061  31.983  1.00 38.36           N  
ANISOU 1025  N   HIS A 158     4716   4965   4892    -60    111     76       N  
ATOM   1026  CA  HIS A 158      18.379  45.052  31.866  1.00 39.46           C  
ANISOU 1026  CA  HIS A 158     4849   5093   5050    -53    114     62       C  
ATOM   1027  C   HIS A 158      18.571  46.178  32.857  1.00 39.90           C  
ANISOU 1027  C   HIS A 158     4903   5148   5107    -59    121     44       C  
ATOM   1028  O   HIS A 158      17.665  46.513  33.616  1.00 42.27           O  
ANISOU 1028  O   HIS A 158     5197   5451   5414    -61    131     27       O  
ATOM   1029  CB  HIS A 158      16.996  44.388  32.025  1.00 38.58           C  
ANISOU 1029  CB  HIS A 158     4729   4984   4943    -50    119     57       C  
ATOM   1030  CG  HIS A 158      15.853  45.173  31.404  1.00 39.78           C  
ANISOU 1030  CG  HIS A 158     4873   5120   5120    -40    117     48       C  
ATOM   1031  ND1 HIS A 158      14.735  44.579  30.943  1.00 40.62           N  
ANISOU 1031  ND1 HIS A 158     4974   5223   5235    -34    116     51       N  
ATOM   1032  CD2 HIS A 158      15.698  46.539  31.161  1.00 38.94           C  
ANISOU 1032  CD2 HIS A 158     4763   4997   5032    -35    116     39       C  
ATOM   1033  CE1 HIS A 158      13.904  45.512  30.437  1.00 40.03           C  
ANISOU 1033  CE1 HIS A 158     4892   5131   5185    -26    113     43       C  
ATOM   1034  NE2 HIS A 158      14.495  46.710  30.568  1.00 40.15           N  
ANISOU 1034  NE2 HIS A 158     4909   5139   5207    -27    112     36       N  
ATOM   1035  N   ASN A 159      19.760  46.766  32.867  1.00 39.19           N  
ANISOU 1035  N   ASN A 159     4819   5055   5013    -63    117     47       N  
ATOM   1036  CA  ASN A 159      20.036  47.924  33.716  1.00 39.21           C  
ANISOU 1036  CA  ASN A 159     4821   5057   5019    -68    123     30       C  
ATOM   1037  C   ASN A 159      20.658  49.064  32.881  1.00 39.18           C  
ANISOU 1037  C   ASN A 159     4820   5036   5030    -62    115     33       C  
ATOM   1038  O   ASN A 159      20.488  49.085  31.660  1.00 37.09           O  
ANISOU 1038  O   ASN A 159     4556   4760   4776    -53    107     45       O  
ATOM   1039  CB  ASN A 159      20.903  47.510  34.916  1.00 38.51           C  
ANISOU 1039  CB  ASN A 159     4738   4985   4908    -83    127     29       C  
ATOM   1040  CG  ASN A 159      20.158  46.610  35.897  1.00 38.93           C  
ANISOU 1040  CG  ASN A 159     4788   5054   4947    -91    136     23       C  
ATOM   1041  OD1 ASN A 159      19.001  46.862  36.232  1.00 39.81           O  
ANISOU 1041  OD1 ASN A 159     4893   5165   5067    -90    145      8       O  
ATOM   1042  ND2 ASN A 159      20.827  45.563  36.373  1.00 37.96           N  
ANISOU 1042  ND2 ASN A 159     4671   4945   4804   -101    133     35       N  
ATOM   1043  N   PHE A 160      21.357  50.003  33.523  1.00 40.37           N  
ANISOU 1043  N   PHE A 160     4973   5186   5180    -68    117     23       N  
ATOM   1044  CA  PHE A 160      21.983  51.127  32.811  1.00 41.57           C  
ANISOU 1044  CA  PHE A 160     5127   5321   5346    -63    110     26       C  
ATOM   1045  C   PHE A 160      23.503  51.106  32.835  1.00 40.11           C  
ANISOU 1045  C   PHE A 160     4950   5140   5149    -70    105     37       C  
ATOM   1046  O   PHE A 160      24.147  52.152  32.822  1.00 41.65           O  
ANISOU 1046  O   PHE A 160     5146   5325   5351    -70    102     33       O  
ATOM   1047  CB  PHE A 160      21.440  52.470  33.308  1.00 43.81           C  
ANISOU 1047  CB  PHE A 160     5403   5594   5646    -62    115      5       C  
ATOM   1048  CG  PHE A 160      19.978  52.650  33.043  1.00 48.61           C  
ANISOU 1048  CG  PHE A 160     6001   6192   6274    -54    118     -4       C  
ATOM   1049  CD1 PHE A 160      19.490  52.666  31.731  1.00 51.21           C  
ANISOU 1049  CD1 PHE A 160     6329   6508   6619    -43    108      7       C  
ATOM   1050  CD2 PHE A 160      19.081  52.790  34.092  1.00 50.85           C  
ANISOU 1050  CD2 PHE A 160     6277   6482   6561    -58    132    -26       C  
ATOM   1051  CE1 PHE A 160      18.135  52.820  31.473  1.00 52.47           C  
ANISOU 1051  CE1 PHE A 160     6478   6657   6798    -36    109      0       C  
ATOM   1052  CE2 PHE A 160      17.722  52.950  33.842  1.00 54.48           C  
ANISOU 1052  CE2 PHE A 160     6726   6932   7042    -51    135    -35       C  
ATOM   1053  CZ  PHE A 160      17.249  52.961  32.533  1.00 54.75           C  
ANISOU 1053  CZ  PHE A 160     6758   6951   7094    -39    122    -22       C  
ATOM   1054  N   ILE A 161      24.059  49.902  32.835  1.00 39.12           N  
ANISOU 1054  N   ILE A 161     4828   5026   5007    -74    103     51       N  
ATOM   1055  CA  ILE A 161      25.499  49.692  32.847  1.00 38.72           C  
ANISOU 1055  CA  ILE A 161     4784   4979   4947    -80     98     63       C  
ATOM   1056  C   ILE A 161      26.146  49.998  31.483  1.00 40.58           C  
ANISOU 1056  C   ILE A 161     5023   5201   5192    -73     91     77       C  
ATOM   1057  O   ILE A 161      25.746  49.450  30.449  1.00 40.25           O  
ANISOU 1057  O   ILE A 161     4982   5155   5154    -66     88     87       O  
ATOM   1058  CB  ILE A 161      25.820  48.268  33.340  1.00 37.29           C  
ANISOU 1058  CB  ILE A 161     4604   4814   4748    -87     98     73       C  
ATOM   1059  CG1 ILE A 161      25.474  48.154  34.826  1.00 36.83           C  
ANISOU 1059  CG1 ILE A 161     4545   4769   4677    -98    105     59       C  
ATOM   1060  CG2 ILE A 161      27.290  47.942  33.125  1.00 38.15           C  
ANISOU 1060  CG2 ILE A 161     4718   4924   4853    -91     92     87       C  
ATOM   1061  CD1 ILE A 161      25.075  46.766  35.288  1.00 37.52           C  
ANISOU 1061  CD1 ILE A 161     4632   4872   4751   -103    106     65       C  
ATOM   1062  N   HIS A 162      27.137  50.888  31.500  1.00 43.41           N  
ANISOU 1062  N   HIS A 162     5384   5553   5555    -76     88     77       N  
ATOM   1063  CA  HIS A 162      27.829  51.325  30.293  1.00 44.95           C  
ANISOU 1063  CA  HIS A 162     5583   5735   5759    -71     82     89       C  
ATOM   1064  C   HIS A 162      29.205  50.736  30.251  1.00 45.25           C  
ANISOU 1064  C   HIS A 162     5625   5777   5789    -77     80    101       C  
ATOM   1065  O   HIS A 162      29.902  50.834  29.240  1.00 46.27           O  
ANISOU 1065  O   HIS A 162     5758   5899   5923    -75     78    113       O  
ATOM   1066  CB  HIS A 162      27.933  52.850  30.246  1.00 49.81           C  
ANISOU 1066  CB  HIS A 162     6199   6337   6390    -70     80     80       C  
ATOM   1067  CG  HIS A 162      26.601  53.571  30.360  1.00 60.41           C  
ANISOU 1067  CG  HIS A 162     7535   7672   7745    -64     82     65       C  
ATOM   1068  ND1 HIS A 162      25.804  53.815  29.288  1.00 63.55           N  
ANISOU 1068  ND1 HIS A 162     7932   8057   8156    -55     77     70       N  
ATOM   1069  CD2 HIS A 162      25.949  54.127  31.468  1.00 65.22           C  
ANISOU 1069  CD2 HIS A 162     8138   8283   8357    -66     88     45       C  
ATOM   1070  CE1 HIS A 162      24.696  54.481  29.690  1.00 63.85           C  
ANISOU 1070  CE1 HIS A 162     7962   8089   8208    -52     79     54       C  
ATOM   1071  NE2 HIS A 162      24.784  54.671  31.023  1.00 68.97           N  
ANISOU 1071  NE2 HIS A 162     8608   8747   8851    -58     87     38       N  
ATOM   1072  N   SER A 163      29.611  50.108  31.351  1.00 45.61           N  
ANISOU 1072  N   SER A 163     5669   5836   5822    -85     82     99       N  
ATOM   1073  CA  SER A 163      30.984  49.642  31.505  1.00 44.98           C  
ANISOU 1073  CA  SER A 163     5591   5760   5739    -92     78    110       C  
ATOM   1074  C   SER A 163      31.100  48.136  31.653  1.00 45.47           C  
ANISOU 1074  C   SER A 163     5651   5833   5790    -95     78    120       C  
ATOM   1075  O   SER A 163      30.382  47.506  32.438  1.00 45.48           O  
ANISOU 1075  O   SER A 163     5651   5846   5782    -99     80    115       O  
ATOM   1076  CB  SER A 163      31.651  50.319  32.700  1.00 45.04           C  
ANISOU 1076  CB  SER A 163     5598   5770   5742   -102     77    101       C  
ATOM   1077  OG  SER A 163      32.964  49.819  32.882  1.00 46.37           O  
ANISOU 1077  OG  SER A 163     5768   5942   5909   -109     72    112       O  
ATOM   1078  N   CYS A 164      32.037  47.567  30.907  1.00 45.39           N  
ANISOU 1078  N   CYS A 164     5641   5819   5783    -95     76    134       N  
ATOM   1079  CA  CYS A 164      32.279  46.138  30.964  1.00 44.68           C  
ANISOU 1079  CA  CYS A 164     5549   5738   5687    -98     75    144       C  
ATOM   1080  C   CYS A 164      33.293  45.795  32.055  1.00 43.24           C  
ANISOU 1080  C   CYS A 164     5364   5562   5501   -109     69    147       C  
ATOM   1081  O   CYS A 164      33.630  44.628  32.253  1.00 42.96           O  
ANISOU 1081  O   CYS A 164     5325   5533   5463   -113     66    156       O  
ATOM   1082  CB  CYS A 164      32.752  45.632  29.601  1.00 45.49           C  
ANISOU 1082  CB  CYS A 164     5652   5833   5797    -92     77    155       C  
ATOM   1083  SG  CYS A 164      32.700  43.838  29.415  1.00 45.79           S  
ANISOU 1083  SG  CYS A 164     5686   5879   5832    -93     77    166       S  
ATOM   1084  N   LYS A 165      33.766  46.808  32.774  1.00 41.88           N  
ANISOU 1084  N   LYS A 165     5193   5388   5329   -115     67    140       N  
ATOM   1085  CA  LYS A 165      34.749  46.594  33.832  1.00 42.03           C  
ANISOU 1085  CA  LYS A 165     5211   5413   5345   -127     60    143       C  
ATOM   1086  C   LYS A 165      34.269  45.567  34.861  1.00 41.23           C  
ANISOU 1086  C   LYS A 165     5109   5326   5229   -135     56    144       C  
ATOM   1087  O   LYS A 165      33.178  45.679  35.415  1.00 41.94           O  
ANISOU 1087  O   LYS A 165     5201   5423   5308   -136     61    133       O  
ATOM   1088  CB  LYS A 165      35.133  47.923  34.498  1.00 42.14           C  
ANISOU 1088  CB  LYS A 165     5228   5422   5359   -132     58    132       C  
ATOM   1089  CG  LYS A 165      36.010  47.814  35.739  1.00 40.94           C  
ANISOU 1089  CG  LYS A 165     5076   5276   5200   -146     49    134       C  
ATOM   1090  CD  LYS A 165      37.452  47.460  35.416  1.00 41.80           C  
ANISOU 1090  CD  LYS A 165     5180   5378   5321   -149     41    148       C  
ATOM   1091  CE  LYS A 165      38.352  47.743  36.616  1.00 42.50           C  
ANISOU 1091  CE  LYS A 165     5270   5470   5406   -163     31    148       C  
ATOM   1092  NZ  LYS A 165      39.784  47.407  36.392  1.00 40.28           N  
ANISOU 1092  NZ  LYS A 165     4984   5181   5140   -167     22    162       N  
ATOM   1093  N   LEU A 166      35.088  44.543  35.056  1.00 41.64           N  
ANISOU 1093  N   LEU A 166     5157   5380   5282   -141     49    157       N  
ATOM   1094  CA  LEU A 166      34.927  43.566  36.120  1.00 41.03           C  
ANISOU 1094  CA  LEU A 166     5079   5315   5192   -152     42    162       C  
ATOM   1095  C   LEU A 166      35.713  44.058  37.349  1.00 40.68           C  
ANISOU 1095  C   LEU A 166     5038   5275   5142   -166     33    160       C  
ATOM   1096  O   LEU A 166      36.945  44.092  37.326  1.00 40.39           O  
ANISOU 1096  O   LEU A 166     4998   5231   5116   -170     25    168       O  
ATOM   1097  CB  LEU A 166      35.439  42.210  35.634  1.00 41.45           C  
ANISOU 1097  CB  LEU A 166     5126   5368   5255   -151     38    178       C  
ATOM   1098  CG  LEU A 166      34.415  41.220  35.057  1.00 43.68           C  
ANISOU 1098  CG  LEU A 166     5406   5654   5534   -143     43    180       C  
ATOM   1099  CD1 LEU A 166      33.491  41.822  34.013  1.00 43.43           C  
ANISOU 1099  CD1 LEU A 166     5377   5617   5505   -129     54    171       C  
ATOM   1100  CD2 LEU A 166      35.143  40.017  34.485  1.00 45.39           C  
ANISOU 1100  CD2 LEU A 166     5615   5866   5763   -142     39    195       C  
ATOM   1101  N   PRO A 167      35.001  44.458  38.417  1.00 40.64           N  
ANISOU 1101  N   PRO A 167     5039   5280   5120   -175     35    148       N  
ATOM   1102  CA  PRO A 167      35.606  45.185  39.552  1.00 41.92           C  
ANISOU 1102  CA  PRO A 167     5206   5445   5274   -190     28    142       C  
ATOM   1103  C   PRO A 167      36.728  44.475  40.325  1.00 43.70           C  
ANISOU 1103  C   PRO A 167     5431   5674   5498   -204     11    157       C  
ATOM   1104  O   PRO A 167      36.926  43.266  40.194  1.00 45.15           O  
ANISOU 1104  O   PRO A 167     5609   5860   5685   -206      4    172       O  
ATOM   1105  CB  PRO A 167      34.415  45.476  40.478  1.00 41.83           C  
ANISOU 1105  CB  PRO A 167     5201   5447   5244   -197     35    126       C  
ATOM   1106  CG  PRO A 167      33.289  44.634  39.989  1.00 41.64           C  
ANISOU 1106  CG  PRO A 167     5173   5428   5217   -188     43    127       C  
ATOM   1107  CD  PRO A 167      33.539  44.332  38.544  1.00 40.97           C  
ANISOU 1107  CD  PRO A 167     5082   5331   5151   -172     45    137       C  
ATOM   1108  N   ALA A 168      37.459  45.247  41.123  1.00 45.55           N  
ANISOU 1108  N   ALA A 168     5670   5908   5729   -216      3    153       N  
ATOM   1109  CA  ALA A 168      38.546  44.719  41.943  1.00 44.41           C  
ANISOU 1109  CA  ALA A 168     5524   5765   5583   -232    -14    167       C  
ATOM   1110  C   ALA A 168      38.007  43.787  43.018  1.00 44.81           C  
ANISOU 1110  C   ALA A 168     5580   5831   5613   -248    -20    171       C  
ATOM   1111  O   ALA A 168      38.662  42.809  43.382  1.00 44.53           O  
ANISOU 1111  O   ALA A 168     5542   5797   5580   -257    -36    188       O  
ATOM   1112  CB  ALA A 168      39.335  45.855  42.573  1.00 42.35           C  
ANISOU 1112  CB  ALA A 168     5268   5499   5322   -241    -20    160       C  
ATOM   1113  N   TYR A 169      36.800  44.081  43.501  1.00 45.99           N  
ANISOU 1113  N   TYR A 169     5737   5993   5744   -250     -9    155       N  
ATOM   1114  CA  TYR A 169      36.211  43.334  44.612  1.00 48.16           C  
ANISOU 1114  CA  TYR A 169     6019   6285   5995   -267    -13    157       C  
ATOM   1115  C   TYR A 169      35.758  41.926  44.225  1.00 49.00           C  
ANISOU 1115  C   TYR A 169     6119   6395   6104   -263    -14    171       C  
ATOM   1116  O   TYR A 169      35.352  41.133  45.087  1.00 49.70           O  
ANISOU 1116  O   TYR A 169     6212   6497   6175   -278    -20    176       O  
ATOM   1117  CB  TYR A 169      35.076  44.125  45.284  1.00 47.22           C  
ANISOU 1117  CB  TYR A 169     5908   6176   5855   -273      1    134       C  
ATOM   1118  CG  TYR A 169      33.818  44.292  44.458  1.00 48.42           C  
ANISOU 1118  CG  TYR A 169     6056   6326   6012   -255     21    121       C  
ATOM   1119  CD1 TYR A 169      32.999  43.203  44.156  1.00 47.40           C  
ANISOU 1119  CD1 TYR A 169     5923   6204   5882   -250     25    128       C  
ATOM   1120  CD2 TYR A 169      33.428  45.551  44.007  1.00 49.31           C  
ANISOU 1120  CD2 TYR A 169     6169   6432   6134   -243     34    102       C  
ATOM   1121  CE1 TYR A 169      31.848  43.362  43.412  1.00 46.85           C  
ANISOU 1121  CE1 TYR A 169     5850   6133   5818   -234     41    117       C  
ATOM   1122  CE2 TYR A 169      32.271  45.720  43.267  1.00 47.07           C  
ANISOU 1122  CE2 TYR A 169     5881   6146   5857   -228     50     92       C  
ATOM   1123  CZ  TYR A 169      31.490  44.624  42.973  1.00 47.48           C  
ANISOU 1123  CZ  TYR A 169     5929   6203   5906   -223     53     99       C  
ATOM   1124  OH  TYR A 169      30.345  44.792  42.232  1.00 49.05           O  
ANISOU 1124  OH  TYR A 169     6123   6399   6112   -208     67     89       O  
ATOM   1125  N   PHE A 170      35.833  41.618  42.933  1.00 47.85           N  
ANISOU 1125  N   PHE A 170     5963   6237   5979   -244     -9    177       N  
ATOM   1126  CA  PHE A 170      35.542  40.268  42.454  1.00 48.02           C  
ANISOU 1126  CA  PHE A 170     5977   6260   6006   -239    -12    191       C  
ATOM   1127  C   PHE A 170      36.468  39.229  43.077  1.00 48.57           C  
ANISOU 1127  C   PHE A 170     6044   6331   6078   -253    -32    212       C  
ATOM   1128  O   PHE A 170      36.095  38.061  43.196  1.00 48.44           O  
ANISOU 1128  O   PHE A 170     6024   6320   6059   -256    -37    223       O  
ATOM   1129  CB  PHE A 170      35.621  40.198  40.925  1.00 44.41           C  
ANISOU 1129  CB  PHE A 170     5511   5789   5572   -217     -3    193       C  
ATOM   1130  CG  PHE A 170      34.302  40.398  40.233  1.00 42.65           C  
ANISOU 1130  CG  PHE A 170     5289   5569   5346   -203     13    181       C  
ATOM   1131  CD1 PHE A 170      33.258  41.084  40.854  1.00 42.71           C  
ANISOU 1131  CD1 PHE A 170     5304   5586   5337   -207     23    164       C  
ATOM   1132  CD2 PHE A 170      34.114  39.929  38.942  1.00 41.77           C  
ANISOU 1132  CD2 PHE A 170     5171   5449   5250   -187     19    186       C  
ATOM   1133  CE1 PHE A 170      32.047  41.278  40.207  1.00 40.82           C  
ANISOU 1133  CE1 PHE A 170     5064   5346   5098   -194     38    153       C  
ATOM   1134  CE2 PHE A 170      32.911  40.125  38.287  1.00 40.91           C  
ANISOU 1134  CE2 PHE A 170     5062   5340   5138   -174     33    175       C  
ATOM   1135  CZ  PHE A 170      31.877  40.797  38.921  1.00 41.32           C  
ANISOU 1135  CZ  PHE A 170     5120   5401   5176   -177     41    159       C  
ATOM   1136  N   SER A 171      37.665  39.656  43.479  1.00 49.85           N  
ANISOU 1136  N   SER A 171     6206   6486   6246   -262    -46    217       N  
ATOM   1137  CA  SER A 171      38.651  38.739  44.052  1.00 51.46           C  
ANISOU 1137  CA  SER A 171     6406   6689   6458   -276    -68    238       C  
ATOM   1138  C   SER A 171      38.285  38.310  45.473  1.00 51.35           C  
ANISOU 1138  C   SER A 171     6402   6691   6417   -300    -80    242       C  
ATOM   1139  O   SER A 171      38.923  37.432  46.043  1.00 49.01           O  
ANISOU 1139  O   SER A 171     6103   6394   6123   -314   -100    261       O  
ATOM   1140  CB  SER A 171      40.053  39.340  43.998  1.00 53.39           C  
ANISOU 1140  CB  SER A 171     6645   6918   6719   -278    -79    243       C  
ATOM   1141  OG  SER A 171      40.130  40.524  44.767  1.00 56.81           O  
ANISOU 1141  OG  SER A 171     7090   7356   7137   -289    -79    230       O  
ATOM   1142  N   ASN A 172      37.252  38.936  46.029  1.00 52.75           N  
ANISOU 1142  N   ASN A 172     6591   6881   6569   -305    -66    224       N  
ATOM   1143  CA  ASN A 172      36.684  38.520  47.299  1.00 55.33           C  
ANISOU 1143  CA  ASN A 172     6928   7225   6867   -328    -72    225       C  
ATOM   1144  C   ASN A 172      35.514  37.579  47.086  1.00 54.40           C  
ANISOU 1144  C   ASN A 172     6808   7116   6742   -323    -62    227       C  
ATOM   1145  O   ASN A 172      35.239  36.713  47.918  1.00 55.15           O  
ANISOU 1145  O   ASN A 172     6908   7223   6821   -340    -72    237       O  
ATOM   1146  CB  ASN A 172      36.324  39.742  48.164  1.00 61.08           C  
ANISOU 1146  CB  ASN A 172     7671   7963   7572   -340    -63    204       C  
ATOM   1147  CG  ASN A 172      37.519  40.237  48.958  1.00 68.39           C  
ANISOU 1147  CG  ASN A 172     8603   8885   8495   -357    -82    210       C  
ATOM   1148  OD1 ASN A 172      38.576  39.610  48.906  1.00 67.12           O  
ANISOU 1148  OD1 ASN A 172     8435   8716   8350   -361   -103    231       O  
ATOM   1149  ND2 ASN A 172      37.382  41.343  49.691  1.00 85.49           N  
ANISOU 1149  ND2 ASN A 172    10781  11058  10643   -368    -76    192       N  
ATOM   1150  N   LEU A 173      34.854  37.743  45.943  1.00 54.66           N  
ANISOU 1150  N   LEU A 173     6835   7144   6789   -299    -44    217       N  
ATOM   1151  CA  LEU A 173      33.769  36.873  45.499  1.00 51.94           C  
ANISOU 1151  CA  LEU A 173     6485   6804   6442   -291    -34    218       C  
ATOM   1152  C   LEU A 173      34.378  35.649  44.845  1.00 51.44           C  
ANISOU 1152  C   LEU A 173     6411   6732   6401   -284    -47    239       C  
ATOM   1153  O   LEU A 173      34.310  35.467  43.636  1.00 53.83           O  
ANISOU 1153  O   LEU A 173     6704   7024   6724   -264    -39    239       O  
ATOM   1154  CB  LEU A 173      32.879  37.616  44.508  1.00 48.76           C  
ANISOU 1154  CB  LEU A 173     6081   6398   6047   -269    -12    199       C  
ATOM   1155  CG  LEU A 173      31.734  38.481  45.028  1.00 49.56           C  
ANISOU 1155  CG  LEU A 173     6190   6509   6129   -272      5    176       C  
ATOM   1156  CD1 LEU A 173      31.886  38.853  46.498  1.00 49.03           C  
ANISOU 1156  CD1 LEU A 173     6136   6455   6037   -298      0    171       C  
ATOM   1157  CD2 LEU A 173      31.600  39.720  44.152  1.00 48.69           C  
ANISOU 1157  CD2 LEU A 173     6078   6388   6032   -254     19    160       C  
ATOM   1158  N   THR A 174      34.978  34.803  45.665  1.00 52.40           N  
ANISOU 1158  N   THR A 174     6532   6857   6519   -302    -68    258       N  
ATOM   1159  CA  THR A 174      35.791  33.716  45.168  1.00 51.77           C  
ANISOU 1159  CA  THR A 174     6440   6766   6464   -298    -83    279       C  
ATOM   1160  C   THR A 174      34.970  32.530  44.648  1.00 49.89           C  
ANISOU 1160  C   THR A 174     6194   6530   6231   -290    -79    285       C  
ATOM   1161  O   THR A 174      35.518  31.619  44.029  1.00 47.72           O  
ANISOU 1161  O   THR A 174     5907   6243   5979   -283    -88    299       O  
ATOM   1162  CB  THR A 174      36.808  33.282  46.237  1.00 54.43           C  
ANISOU 1162  CB  THR A 174     6778   7103   6799   -321   -110    297       C  
ATOM   1163  OG1 THR A 174      37.898  32.614  45.597  1.00 59.24           O  
ANISOU 1163  OG1 THR A 174     7371   7694   7440   -314   -124    314       O  
ATOM   1164  CG2 THR A 174      36.164  32.368  47.278  1.00 54.95           C  
ANISOU 1164  CG2 THR A 174     6851   7184   6842   -342   -120    307       C  
ATOM   1165  N   ASN A 175      33.659  32.562  44.887  1.00 49.90           N  
ANISOU 1165  N   ASN A 175     6203   6545   6212   -290    -64    274       N  
ATOM   1166  CA  ASN A 175      32.743  31.514  44.436  1.00 48.08           C  
ANISOU 1166  CA  ASN A 175     5967   6318   5984   -283    -59    278       C  
ATOM   1167  C   ASN A 175      31.856  31.940  43.281  1.00 47.55           C  
ANISOU 1167  C   ASN A 175     5896   6247   5923   -260    -37    262       C  
ATOM   1168  O   ASN A 175      30.898  31.250  42.935  1.00 49.38           O  
ANISOU 1168  O   ASN A 175     6124   6482   6153   -253    -29    262       O  
ATOM   1169  CB  ASN A 175      31.871  31.052  45.600  1.00 50.49           C  
ANISOU 1169  CB  ASN A 175     6280   6641   6260   -302    -61    280       C  
ATOM   1170  CG  ASN A 175      32.620  30.149  46.550  1.00 51.40           C  
ANISOU 1170  CG  ASN A 175     6397   6760   6373   -325    -86    303       C  
ATOM   1171  OD1 ASN A 175      33.237  30.617  47.508  1.00 54.70           O  
ANISOU 1171  OD1 ASN A 175     6823   7181   6777   -344    -98    305       O  
ATOM   1172  ND2 ASN A 175      32.604  28.850  46.271  1.00 50.33           N  
ANISOU 1172  ND2 ASN A 175     6251   6620   6251   -323    -97    320       N  
ATOM   1173  N   LEU A 176      32.172  33.085  42.690  1.00 48.56           N  
ANISOU 1173  N   LEU A 176     6026   6367   6058   -248    -27    249       N  
ATOM   1174  CA  LEU A 176      31.374  33.639  41.600  1.00 46.35           C  
ANISOU 1174  CA  LEU A 176     5744   6081   5784   -228     -8    234       C  
ATOM   1175  C   LEU A 176      31.767  32.973  40.273  1.00 44.45           C  
ANISOU 1175  C   LEU A 176     5492   5827   5569   -211     -8    243       C  
ATOM   1176  O   LEU A 176      32.944  32.983  39.885  1.00 44.98           O  
ANISOU 1176  O   LEU A 176     5554   5882   5654   -208    -16    251       O  
ATOM   1177  CB  LEU A 176      31.529  35.163  41.554  1.00 43.69           C  
ANISOU 1177  CB  LEU A 176     5413   5742   5445   -224      1    217       C  
ATOM   1178  CG  LEU A 176      30.716  35.954  40.530  1.00 44.41           C  
ANISOU 1178  CG  LEU A 176     5504   5826   5542   -205     19    201       C  
ATOM   1179  CD1 LEU A 176      29.237  35.998  40.888  1.00 42.43           C  
ANISOU 1179  CD1 LEU A 176     5257   5587   5276   -205     31    189       C  
ATOM   1180  CD2 LEU A 176      31.282  37.360  40.418  1.00 44.23           C  
ANISOU 1180  CD2 LEU A 176     5485   5796   5523   -202     22    190       C  
ATOM   1181  N   VAL A 177      30.779  32.378  39.605  1.00 40.90           N  
ANISOU 1181  N   VAL A 177     5039   5379   5122   -199      0    241       N  
ATOM   1182  CA  VAL A 177      31.016  31.568  38.400  1.00 39.20           C  
ANISOU 1182  CA  VAL A 177     4814   5152   4927   -185      0    249       C  
ATOM   1183  C   VAL A 177      30.220  32.029  37.180  1.00 38.02           C  
ANISOU 1183  C   VAL A 177     4665   4997   4783   -167     16    237       C  
ATOM   1184  O   VAL A 177      30.529  31.637  36.051  1.00 37.84           O  
ANISOU 1184  O   VAL A 177     4637   4964   4777   -155     18    240       O  
ATOM   1185  CB  VAL A 177      30.764  30.052  38.639  1.00 38.13           C  
ANISOU 1185  CB  VAL A 177     4672   5020   4794   -191     -9    264       C  
ATOM   1186  CG1 VAL A 177      31.856  29.449  39.511  1.00 36.85           C  
ANISOU 1186  CG1 VAL A 177     4506   4857   4636   -207    -29    280       C  
ATOM   1187  CG2 VAL A 177      29.380  29.799  39.226  1.00 36.57           C  
ANISOU 1187  CG2 VAL A 177     4480   4838   4577   -196     -3    259       C  
ATOM   1188  N   HIS A 178      29.197  32.848  37.418  1.00 38.86           N  
ANISOU 1188  N   HIS A 178     4778   5110   4874   -165     27    223       N  
ATOM   1189  CA  HIS A 178      28.370  33.403  36.349  1.00 39.87           C  
ANISOU 1189  CA  HIS A 178     4907   5232   5007   -149     40    211       C  
ATOM   1190  C   HIS A 178      27.893  34.817  36.595  1.00 39.95           C  
ANISOU 1190  C   HIS A 178     4924   5244   5009   -148     50    194       C  
ATOM   1191  O   HIS A 178      27.241  35.097  37.605  1.00 38.39           O  
ANISOU 1191  O   HIS A 178     4730   5057   4797   -157     53    186       O  
ATOM   1192  CB  HIS A 178      27.172  32.500  36.083  1.00 41.03           C  
ANISOU 1192  CB  HIS A 178     5051   5385   5152   -144     44    212       C  
ATOM   1193  CG  HIS A 178      26.347  32.938  34.899  1.00 44.73           C  
ANISOU 1193  CG  HIS A 178     5520   5845   5627   -128     55    203       C  
ATOM   1194  ND1 HIS A 178      25.139  33.522  35.032  1.00 44.89           N  
ANISOU 1194  ND1 HIS A 178     5544   5871   5641   -125     64    191       N  
ATOM   1195  CD2 HIS A 178      26.615  32.888  33.526  1.00 45.20           C  
ANISOU 1195  CD2 HIS A 178     5578   5893   5701   -115     57    205       C  
ATOM   1196  CE1 HIS A 178      24.647  33.809  33.810  1.00 46.19           C  
ANISOU 1196  CE1 HIS A 178     5708   6025   5815   -110     69    186       C  
ATOM   1197  NE2 HIS A 178      25.555  33.421  32.890  1.00 45.28           N  
ANISOU 1197  NE2 HIS A 178     5591   5901   5711   -105     65    196       N  
ATOM   1198  N   VAL A 179      28.199  35.711  35.652  1.00 40.38           N  
ANISOU 1198  N   VAL A 179     4980   5287   5074   -137     55    189       N  
ATOM   1199  CA  VAL A 179      27.691  37.089  35.667  1.00 39.72           C  
ANISOU 1199  CA  VAL A 179     4901   5201   4987   -133     63    172       C  
ATOM   1200  C   VAL A 179      26.897  37.400  34.393  1.00 40.34           C  
ANISOU 1200  C   VAL A 179     4979   5271   5076   -117     71    167       C  
ATOM   1201  O   VAL A 179      27.423  37.321  33.277  1.00 40.91           O  
ANISOU 1201  O   VAL A 179     5051   5333   5160   -109     70    173       O  
ATOM   1202  CB  VAL A 179      28.832  38.118  35.821  1.00 40.13           C  
ANISOU 1202  CB  VAL A 179     4955   5246   5043   -137     61    170       C  
ATOM   1203  CG1 VAL A 179      28.306  39.544  35.670  1.00 38.60           C  
ANISOU 1203  CG1 VAL A 179     4766   5048   4850   -131     69    154       C  
ATOM   1204  CG2 VAL A 179      29.545  37.932  37.157  1.00 39.64           C  
ANISOU 1204  CG2 VAL A 179     4896   5194   4971   -154     51    174       C  
ATOM   1205  N   ASP A 180      25.633  37.763  34.569  1.00 39.53           N  
ANISOU 1205  N   ASP A 180     4876   5171   4969   -114     79    156       N  
ATOM   1206  CA  ASP A 180      24.775  38.141  33.454  1.00 38.26           C  
ANISOU 1206  CA  ASP A 180     4715   5001   4818   -100     84    151       C  
ATOM   1207  C   ASP A 180      24.703  39.671  33.286  1.00 36.55           C  
ANISOU 1207  C   ASP A 180     4502   4776   4607    -96     88    138       C  
ATOM   1208  O   ASP A 180      24.131  40.374  34.126  1.00 35.79           O  
ANISOU 1208  O   ASP A 180     4406   4685   4507   -100     94    124       O  
ATOM   1209  CB  ASP A 180      23.379  37.531  33.650  1.00 39.62           C  
ANISOU 1209  CB  ASP A 180     4885   5181   4988    -98     88    147       C  
ATOM   1210  CG  ASP A 180      22.489  37.652  32.411  1.00 41.12           C  
ANISOU 1210  CG  ASP A 180     5073   5360   5188    -84     91    145       C  
ATOM   1211  OD1 ASP A 180      22.526  38.682  31.704  1.00 40.44           O  
ANISOU 1211  OD1 ASP A 180     4989   5263   5111    -77     92    140       O  
ATOM   1212  OD2 ASP A 180      21.722  36.704  32.157  1.00 43.90           O  
ANISOU 1212  OD2 ASP A 180     5422   5716   5541    -81     90    150       O  
ATOM   1213  N   LEU A 181      25.277  40.167  32.188  1.00 35.22           N  
ANISOU 1213  N   LEU A 181     4335   4595   4449    -88     86    142       N  
ATOM   1214  CA  LEU A 181      25.346  41.599  31.908  1.00 34.49           C  
ANISOU 1214  CA  LEU A 181     4246   4493   4364    -84     89    132       C  
ATOM   1215  C   LEU A 181      24.535  41.988  30.675  1.00 35.93           C  
ANISOU 1215  C   LEU A 181     4429   4664   4558    -72     89    131       C  
ATOM   1216  O   LEU A 181      24.774  43.039  30.066  1.00 36.25           O  
ANISOU 1216  O   LEU A 181     4472   4692   4606    -68     89    129       O  
ATOM   1217  CB  LEU A 181      26.804  42.036  31.743  1.00 33.28           C  
ANISOU 1217  CB  LEU A 181     4095   4334   4213    -88     85    138       C  
ATOM   1218  CG  LEU A 181      27.647  42.174  33.011  1.00 32.10           C  
ANISOU 1218  CG  LEU A 181     3946   4192   4056   -100     82    136       C  
ATOM   1219  CD1 LEU A 181      29.131  42.119  32.704  1.00 31.42           C  
ANISOU 1219  CD1 LEU A 181     3861   4101   3975   -103     77    147       C  
ATOM   1220  CD2 LEU A 181      27.310  43.475  33.711  1.00 33.08           C  
ANISOU 1220  CD2 LEU A 181     4072   4315   4179   -103     86    120       C  
ATOM   1221  N   SER A 182      23.564  41.143  30.330  1.00 37.61           N  
ANISOU 1221  N   SER A 182     4639   4879   4770    -68     90    134       N  
ATOM   1222  CA  SER A 182      22.749  41.301  29.118  1.00 38.82           C  
ANISOU 1222  CA  SER A 182     4794   5022   4934    -57     88    135       C  
ATOM   1223  C   SER A 182      21.915  42.561  29.119  1.00 40.40           C  
ANISOU 1223  C   SER A 182     4991   5213   5144    -53     90    123       C  
ATOM   1224  O   SER A 182      21.574  43.094  30.184  1.00 42.23           O  
ANISOU 1224  O   SER A 182     5220   5450   5375    -57     95    110       O  
ATOM   1225  CB  SER A 182      21.775  40.133  28.962  1.00 38.39           C  
ANISOU 1225  CB  SER A 182     4735   4973   4877    -54     88    139       C  
ATOM   1226  OG  SER A 182      22.414  38.904  29.174  1.00 40.38           O  
ANISOU 1226  OG  SER A 182     4987   5234   5121    -59     87    149       O  
ATOM   1227  N   TYR A 183      21.552  42.997  27.913  1.00 40.59           N  
ANISOU 1227  N   TYR A 183     5019   5224   5179    -45     85    127       N  
ATOM   1228  CA  TYR A 183      20.605  44.089  27.707  1.00 40.83           C  
ANISOU 1228  CA  TYR A 183     5046   5243   5223    -39     84    117       C  
ATOM   1229  C   TYR A 183      20.959  45.299  28.578  1.00 39.62           C  
ANISOU 1229  C   TYR A 183     4891   5088   5074    -43     88    104       C  
ATOM   1230  O   TYR A 183      20.146  45.807  29.354  1.00 39.32           O  
ANISOU 1230  O   TYR A 183     4846   5050   5041    -43     93     89       O  
ATOM   1231  CB  TYR A 183      19.149  43.609  27.891  1.00 42.32           C  
ANISOU 1231  CB  TYR A 183     5227   5433   5417    -35     86    111       C  
ATOM   1232  CG  TYR A 183      18.112  44.592  27.379  1.00 45.92           C  
ANISOU 1232  CG  TYR A 183     5679   5874   5892    -27     82    105       C  
ATOM   1233  CD1 TYR A 183      18.338  45.341  26.218  1.00 48.57           C  
ANISOU 1233  CD1 TYR A 183     6021   6195   6238    -23     73    112       C  
ATOM   1234  CD2 TYR A 183      16.904  44.772  28.046  1.00 47.78           C  
ANISOU 1234  CD2 TYR A 183     5904   6110   6138    -25     87     91       C  
ATOM   1235  CE1 TYR A 183      17.397  46.244  25.752  1.00 49.03           C  
ANISOU 1235  CE1 TYR A 183     6075   6238   6316    -17     66    107       C  
ATOM   1236  CE2 TYR A 183      15.954  45.671  27.581  1.00 48.11           C  
ANISOU 1236  CE2 TYR A 183     5940   6136   6202    -19     82     85       C  
ATOM   1237  CZ  TYR A 183      16.210  46.402  26.439  1.00 49.19           C  
ANISOU 1237  CZ  TYR A 183     6083   6257   6348    -14     71     93       C  
ATOM   1238  OH  TYR A 183      15.278  47.295  25.979  1.00 54.62           O  
ANISOU 1238  OH  TYR A 183     6764   6927   7059     -8     64     89       O  
ATOM   1239  N   ASN A 184      22.214  45.716  28.452  1.00 38.61           N  
ANISOU 1239  N   ASN A 184     4769   4958   4942    -46     86    109       N  
ATOM   1240  CA  ASN A 184      22.717  46.929  29.070  1.00 37.88           C  
ANISOU 1240  CA  ASN A 184     4676   4862   4855    -50     88     99       C  
ATOM   1241  C   ASN A 184      23.269  47.805  27.959  1.00 37.85           C  
ANISOU 1241  C   ASN A 184     4677   4843   4860    -46     81    106       C  
ATOM   1242  O   ASN A 184      22.950  47.570  26.792  1.00 38.15           O  
ANISOU 1242  O   ASN A 184     4718   4872   4902    -41     76    116       O  
ATOM   1243  CB  ASN A 184      23.760  46.599  30.136  1.00 37.19           C  
ANISOU 1243  CB  ASN A 184     4590   4787   4753    -60     92     98       C  
ATOM   1244  CG  ASN A 184      23.125  46.139  31.438  1.00 37.74           C  
ANISOU 1244  CG  ASN A 184     4655   4870   4814    -66     98     87       C  
ATOM   1245  OD1 ASN A 184      22.481  46.922  32.122  1.00 37.30           O  
ANISOU 1245  OD1 ASN A 184     4595   4814   4763    -67    104     71       O  
ATOM   1246  ND2 ASN A 184      23.299  44.866  31.781  1.00 37.37           N  
ANISOU 1246  ND2 ASN A 184     4608   4836   4754    -71     99     96       N  
ATOM   1247  N   TYR A 185      24.080  48.804  28.297  1.00 38.92           N  
ANISOU 1247  N   TYR A 185     4814   4973   4999    -50     82    101       N  
ATOM   1248  CA  TYR A 185      24.533  49.797  27.302  1.00 38.51           C  
ANISOU 1248  CA  TYR A 185     4767   4906   4958    -47     75    107       C  
ATOM   1249  C   TYR A 185      26.045  49.767  27.060  1.00 37.52           C  
ANISOU 1249  C   TYR A 185     4647   4781   4825    -52     75    117       C  
ATOM   1250  O   TYR A 185      26.651  50.779  26.714  1.00 37.49           O  
ANISOU 1250  O   TYR A 185     4647   4767   4829    -53     72    118       O  
ATOM   1251  CB  TYR A 185      24.079  51.201  27.711  1.00 39.88           C  
ANISOU 1251  CB  TYR A 185     4936   5069   5147    -45     74     93       C  
ATOM   1252  CG  TYR A 185      22.575  51.376  27.699  1.00 43.33           C  
ANISOU 1252  CG  TYR A 185     5366   5500   5597    -39     74     84       C  
ATOM   1253  CD1 TYR A 185      21.776  50.848  28.725  1.00 42.46           C  
ANISOU 1253  CD1 TYR A 185     5248   5401   5483    -40     82     71       C  
ATOM   1254  CD2 TYR A 185      21.947  52.069  26.663  1.00 44.85           C  
ANISOU 1254  CD2 TYR A 185     5557   5675   5806    -32     65     88       C  
ATOM   1255  CE1 TYR A 185      20.399  50.998  28.712  1.00 44.39           C  
ANISOU 1255  CE1 TYR A 185     5483   5638   5741    -34     83     62       C  
ATOM   1256  CE2 TYR A 185      20.567  52.230  26.644  1.00 46.96           C  
ANISOU 1256  CE2 TYR A 185     5816   5935   6089    -26     63     80       C  
ATOM   1257  CZ  TYR A 185      19.795  51.694  27.667  1.00 47.17           C  
ANISOU 1257  CZ  TYR A 185     5834   5972   6114    -27     73     66       C  
ATOM   1258  OH  TYR A 185      18.421  51.857  27.644  1.00 47.10           O  
ANISOU 1258  OH  TYR A 185     5815   5955   6122    -21     72     58       O  
ATOM   1259  N   ILE A 186      26.644  48.596  27.244  1.00 35.60           N  
ANISOU 1259  N   ILE A 186     4405   4550   4569    -56     78    124       N  
ATOM   1260  CA  ILE A 186      28.069  48.426  27.049  1.00 33.77           C  
ANISOU 1260  CA  ILE A 186     4178   4319   4333    -62     78    133       C  
ATOM   1261  C   ILE A 186      28.364  48.520  25.563  1.00 34.01           C  
ANISOU 1261  C   ILE A 186     4215   4339   4368    -59     75    145       C  
ATOM   1262  O   ILE A 186      27.776  47.804  24.751  1.00 34.47           O  
ANISOU 1262  O   ILE A 186     4275   4397   4422    -56     75    151       O  
ATOM   1263  CB  ILE A 186      28.567  47.082  27.623  1.00 32.46           C  
ANISOU 1263  CB  ILE A 186     4009   4166   4155    -67     81    138       C  
ATOM   1264  CG1 ILE A 186      28.176  46.976  29.104  1.00 32.29           C  
ANISOU 1264  CG1 ILE A 186     3982   4156   4128    -71     83    127       C  
ATOM   1265  CG2 ILE A 186      30.073  46.948  27.428  1.00 31.23           C  
ANISOU 1265  CG2 ILE A 186     3855   4009   3999    -72     81    147       C  
ATOM   1266  CD1 ILE A 186      28.239  45.585  29.694  1.00 31.84           C  
ANISOU 1266  CD1 ILE A 186     3923   4113   4060    -76     83    132       C  
ATOM   1267  N   GLN A 187      29.266  49.420  25.210  1.00 33.73           N  
ANISOU 1267  N   GLN A 187     4182   4294   4337    -62     74    147       N  
ATOM   1268  CA  GLN A 187      29.635  49.581  23.824  1.00 35.13           C  
ANISOU 1268  CA  GLN A 187     4368   4462   4516    -62     73    158       C  
ATOM   1269  C   GLN A 187      31.041  49.099  23.560  1.00 34.99           C  
ANISOU 1269  C   GLN A 187     4353   4447   4495    -68     78    166       C  
ATOM   1270  O   GLN A 187      31.415  48.872  22.407  1.00 35.07           O  
ANISOU 1270  O   GLN A 187     4368   4451   4502    -69     80    175       O  
ATOM   1271  CB  GLN A 187      29.482  51.033  23.395  1.00 36.84           C  
ANISOU 1271  CB  GLN A 187     4588   4665   4744    -61     67    157       C  
ATOM   1272  CG  GLN A 187      28.068  51.555  23.554  1.00 38.99           C  
ANISOU 1272  CG  GLN A 187     4857   4932   5025    -54     62    149       C  
ATOM   1273  CD  GLN A 187      27.950  52.982  23.097  1.00 41.07           C  
ANISOU 1273  CD  GLN A 187     5122   5179   5302    -53     54    148       C  
ATOM   1274  OE1 GLN A 187      28.014  53.264  21.895  1.00 42.06           O  
ANISOU 1274  OE1 GLN A 187     5255   5295   5430    -55     49    159       O  
ATOM   1275  NE2 GLN A 187      27.789  53.901  24.053  1.00 40.82           N  
ANISOU 1275  NE2 GLN A 187     5083   5145   5281    -52     54    135       N  
ATOM   1276  N   THR A 188      31.820  48.948  24.627  1.00 35.46           N  
ANISOU 1276  N   THR A 188     4406   4513   4553    -72     80    163       N  
ATOM   1277  CA  THR A 188      33.229  48.618  24.479  1.00 36.73           C  
ANISOU 1277  CA  THR A 188     4566   4674   4715    -77     84    169       C  
ATOM   1278  C   THR A 188      33.734  47.633  25.532  1.00 36.79           C  
ANISOU 1278  C   THR A 188     4567   4693   4719    -81     85    169       C  
ATOM   1279  O   THR A 188      33.276  47.626  26.677  1.00 37.04           O  
ANISOU 1279  O   THR A 188     4594   4731   4746    -82     82    161       O  
ATOM   1280  CB  THR A 188      34.130  49.876  24.508  1.00 37.39           C  
ANISOU 1280  CB  THR A 188     4651   4748   4807    -81     83    168       C  
ATOM   1281  OG1 THR A 188      34.471  50.179  25.863  1.00 40.25           O  
ANISOU 1281  OG1 THR A 188     5007   5115   5170    -84     80    161       O  
ATOM   1282  CG2 THR A 188      33.458  51.105  23.850  1.00 35.29           C  
ANISOU 1282  CG2 THR A 188     4390   4470   4546    -78     78    167       C  
ATOM   1283  N   ILE A 189      34.683  46.798  25.119  1.00 36.76           N  
ANISOU 1283  N   ILE A 189     4560   4688   4716    -85     89    177       N  
ATOM   1284  CA  ILE A 189      35.409  45.928  26.036  1.00 35.45           C  
ANISOU 1284  CA  ILE A 189     4387   4530   4551    -90     88    179       C  
ATOM   1285  C   ILE A 189      36.892  46.282  25.900  1.00 34.76           C  
ANISOU 1285  C   ILE A 189     4297   4436   4473    -95     89    183       C  
ATOM   1286  O   ILE A 189      37.476  46.117  24.827  1.00 32.80           O  
ANISOU 1286  O   ILE A 189     4051   4181   4231    -95     96    188       O  
ATOM   1287  CB  ILE A 189      35.154  44.439  25.720  1.00 35.08           C  
ANISOU 1287  CB  ILE A 189     4337   4490   4501    -88     90    184       C  
ATOM   1288  CG1 ILE A 189      33.650  44.139  25.782  1.00 34.16           C  
ANISOU 1288  CG1 ILE A 189     4224   4380   4376    -83     89    180       C  
ATOM   1289  CG2 ILE A 189      35.939  43.546  26.679  1.00 34.43           C  
ANISOU 1289  CG2 ILE A 189     4245   4413   4421    -94     87    188       C  
ATOM   1290  CD1 ILE A 189      33.247  42.819  25.159  1.00 33.53           C  
ANISOU 1290  CD1 ILE A 189     4143   4303   4293    -80     91    185       C  
ATOM   1291  N   THR A 190      37.477  46.785  26.987  1.00 34.76           N  
ANISOU 1291  N   THR A 190     4293   4437   4477   -100     84    180       N  
ATOM   1292  CA  THR A 190      38.848  47.313  26.987  1.00 35.97           C  
ANISOU 1292  CA  THR A 190     4443   4582   4640   -105     84    183       C  
ATOM   1293  C   THR A 190      39.785  46.310  27.653  1.00 36.76           C  
ANISOU 1293  C   THR A 190     4534   4685   4747   -111     80    189       C  
ATOM   1294  O   THR A 190      39.309  45.393  28.322  1.00 36.46           O  
ANISOU 1294  O   THR A 190     4492   4657   4702   -112     76    189       O  
ATOM   1295  CB  THR A 190      38.930  48.635  27.777  1.00 35.90           C  
ANISOU 1295  CB  THR A 190     4435   4570   4632   -107     78    176       C  
ATOM   1296  OG1 THR A 190      38.858  48.345  29.174  1.00 37.07           O  
ANISOU 1296  OG1 THR A 190     4580   4729   4775   -112     71    172       O  
ATOM   1297  CG2 THR A 190      37.792  49.583  27.418  1.00 35.95           C  
ANISOU 1297  CG2 THR A 190     4450   4575   4635   -101     79    168       C  
ATOM   1298  N   VAL A 191      41.105  46.476  27.504  1.00 38.02           N  
ANISOU 1298  N   VAL A 191     4687   4836   4919   -116     81    193       N  
ATOM   1299  CA  VAL A 191      42.030  45.568  28.212  1.00 39.35           C  
ANISOU 1299  CA  VAL A 191     4846   5007   5098   -122     76    199       C  
ATOM   1300  C   VAL A 191      41.983  45.750  29.734  1.00 41.05           C  
ANISOU 1300  C   VAL A 191     5060   5230   5307   -128     62    197       C  
ATOM   1301  O   VAL A 191      42.178  44.784  30.472  1.00 43.38           O  
ANISOU 1301  O   VAL A 191     5348   5529   5602   -133     55    202       O  
ATOM   1302  CB  VAL A 191      43.503  45.516  27.677  1.00 38.16           C  
ANISOU 1302  CB  VAL A 191     4687   4844   4967   -126     80    205       C  
ATOM   1303  CG1 VAL A 191      43.647  46.130  26.290  1.00 37.24           C  
ANISOU 1303  CG1 VAL A 191     4576   4719   4854   -123     93    204       C  
ATOM   1304  CG2 VAL A 191      44.492  46.120  28.661  1.00 36.63           C  
ANISOU 1304  CG2 VAL A 191     4488   4646   4782   -133     70    206       C  
ATOM   1305  N   ASN A 192      41.706  46.961  30.211  1.00 42.85           N  
ANISOU 1305  N   ASN A 192     5294   5457   5528   -129     59    189       N  
ATOM   1306  CA  ASN A 192      41.551  47.137  31.658  1.00 46.13           C  
ANISOU 1306  CA  ASN A 192     5710   5881   5935   -136     48    185       C  
ATOM   1307  C   ASN A 192      40.170  46.750  32.206  1.00 46.44           C  
ANISOU 1307  C   ASN A 192     5755   5934   5957   -135     48    179       C  
ATOM   1308  O   ASN A 192      40.015  46.592  33.424  1.00 46.67           O  
ANISOU 1308  O   ASN A 192     5784   5972   5976   -143     40    177       O  
ATOM   1309  CB  ASN A 192      42.015  48.524  32.141  1.00 49.91           C  
ANISOU 1309  CB  ASN A 192     6191   6354   6415   -140     44    178       C  
ATOM   1310  CG  ASN A 192      43.543  48.611  32.299  1.00 56.51           C  
ANISOU 1310  CG  ASN A 192     7020   7181   7267   -147     38    186       C  
ATOM   1311  OD1 ASN A 192      44.157  47.826  33.043  1.00 56.56           O  
ANISOU 1311  OD1 ASN A 192     7021   7191   7278   -155     29    193       O  
ATOM   1312  ND2 ASN A 192      44.165  49.567  31.593  1.00 55.46           N  
ANISOU 1312  ND2 ASN A 192     6887   7036   7146   -145     43    185       N  
ATOM   1313  N   ASP A 193      39.189  46.563  31.312  1.00 44.71           N  
ANISOU 1313  N   ASP A 193     5538   5715   5733   -126     57    177       N  
ATOM   1314  CA  ASP A 193      37.875  46.013  31.698  1.00 45.38           C  
ANISOU 1314  CA  ASP A 193     5626   5812   5804   -124     57    172       C  
ATOM   1315  C   ASP A 193      38.011  44.569  32.176  1.00 44.10           C  
ANISOU 1315  C   ASP A 193     5459   5658   5640   -128     52    181       C  
ATOM   1316  O   ASP A 193      37.306  44.137  33.088  1.00 44.88           O  
ANISOU 1316  O   ASP A 193     5558   5767   5725   -133     48    178       O  
ATOM   1317  CB  ASP A 193      36.862  46.063  30.540  1.00 45.19           C  
ANISOU 1317  CB  ASP A 193     5606   5784   5778   -113     66    170       C  
ATOM   1318  CG  ASP A 193      36.202  47.426  30.379  1.00 45.36           C  
ANISOU 1318  CG  ASP A 193     5633   5801   5799   -108     69    159       C  
ATOM   1319  OD1 ASP A 193      36.280  48.258  31.309  1.00 45.76           O  
ANISOU 1319  OD1 ASP A 193     5684   5852   5847   -113     65    151       O  
ATOM   1320  OD2 ASP A 193      35.604  47.667  29.306  1.00 45.84           O  
ANISOU 1320  OD2 ASP A 193     5697   5855   5862   -101     74    159       O  
ATOM   1321  N   LEU A 194      38.925  43.833  31.554  1.00 41.04           N  
ANISOU 1321  N   LEU A 194     5065   5263   5265   -128     53    191       N  
ATOM   1322  CA  LEU A 194      39.116  42.426  31.862  1.00 42.08           C  
ANISOU 1322  CA  LEU A 194     5188   5399   5398   -132     47    200       C  
ATOM   1323  C   LEU A 194      40.356  42.122  32.720  1.00 44.41           C  
ANISOU 1323  C   LEU A 194     5477   5693   5704   -143     35    209       C  
ATOM   1324  O   LEU A 194      40.761  40.966  32.834  1.00 45.05           O  
ANISOU 1324  O   LEU A 194     5550   5774   5793   -146     30    218       O  
ATOM   1325  CB  LEU A 194      39.127  41.613  30.564  1.00 39.53           C  
ANISOU 1325  CB  LEU A 194     4862   5071   5085   -124     56    205       C  
ATOM   1326  CG  LEU A 194      37.836  41.634  29.740  1.00 37.65           C  
ANISOU 1326  CG  LEU A 194     4631   4835   4837   -115     65    200       C  
ATOM   1327  CD1 LEU A 194      37.971  40.695  28.561  1.00 36.25           C  
ANISOU 1327  CD1 LEU A 194     4451   4653   4668   -110     73    205       C  
ATOM   1328  CD2 LEU A 194      36.607  41.267  30.564  1.00 37.86           C  
ANISOU 1328  CD2 LEU A 194     4660   4874   4848   -116     61    196       C  
ATOM   1329  N   GLN A 195      40.930  43.156  33.336  1.00 46.85           N  
ANISOU 1329  N   GLN A 195     5788   5998   6013   -149     30    205       N  
ATOM   1330  CA  GLN A 195      42.149  43.031  34.133  1.00 48.58           C  
ANISOU 1330  CA  GLN A 195     6000   6214   6242   -160     17    213       C  
ATOM   1331  C   GLN A 195      42.002  42.031  35.279  1.00 48.35           C  
ANISOU 1331  C   GLN A 195     5969   6195   6205   -170      3    220       C  
ATOM   1332  O   GLN A 195      42.926  41.265  35.549  1.00 47.68           O  
ANISOU 1332  O   GLN A 195     5875   6105   6134   -177     -6    232       O  
ATOM   1333  CB  GLN A 195      42.575  44.395  34.686  1.00 55.64           C  
ANISOU 1333  CB  GLN A 195     6900   7105   7134   -165     13    206       C  
ATOM   1334  CG  GLN A 195      44.027  44.467  35.149  1.00 64.33           C  
ANISOU 1334  CG  GLN A 195     7993   8197   8251   -174      1    214       C  
ATOM   1335  CD  GLN A 195      44.317  45.690  36.015  1.00 74.69           C  
ANISOU 1335  CD  GLN A 195     9311   9509   9556   -181     -5    207       C  
ATOM   1336  OE1 GLN A 195      43.978  45.728  37.206  1.00 77.15           O  
ANISOU 1336  OE1 GLN A 195     9629   9831   9852   -192    -15    204       O  
ATOM   1337  NE2 GLN A 195      44.965  46.694  35.420  1.00 74.54           N  
ANISOU 1337  NE2 GLN A 195     9291   9479   9550   -177      0    204       N  
ATOM   1338  N   PHE A 196      40.852  42.031  35.952  1.00 46.95           N  
ANISOU 1338  N   PHE A 196     5800   6031   6006   -173      3    214       N  
ATOM   1339  CA  PHE A 196      40.627  41.074  37.029  1.00 45.41           C  
ANISOU 1339  CA  PHE A 196     5604   5847   5801   -184     -8    221       C  
ATOM   1340  C   PHE A 196      40.902  39.637  36.581  1.00 46.58           C  
ANISOU 1340  C   PHE A 196     5742   5991   5963   -182    -12    234       C  
ATOM   1341  O   PHE A 196      41.639  38.911  37.255  1.00 48.30           O  
ANISOU 1341  O   PHE A 196     5954   6208   6189   -193    -27    246       O  
ATOM   1342  CB  PHE A 196      39.227  41.202  37.624  1.00 44.42           C  
ANISOU 1342  CB  PHE A 196     5489   5737   5651   -186     -3    211       C  
ATOM   1343  CG  PHE A 196      38.821  40.022  38.462  1.00 45.39           C  
ANISOU 1343  CG  PHE A 196     5611   5870   5762   -196    -13    219       C  
ATOM   1344  CD1 PHE A 196      39.440  39.770  39.679  1.00 45.78           C  
ANISOU 1344  CD1 PHE A 196     5662   5925   5807   -213    -30    227       C  
ATOM   1345  CD2 PHE A 196      37.820  39.153  38.027  1.00 46.28           C  
ANISOU 1345  CD2 PHE A 196     5723   5989   5871   -189     -6    220       C  
ATOM   1346  CE1 PHE A 196      39.074  38.669  40.443  1.00 46.68           C  
ANISOU 1346  CE1 PHE A 196     5775   6049   5910   -224    -40    237       C  
ATOM   1347  CE2 PHE A 196      37.442  38.057  38.789  1.00 44.80           C  
ANISOU 1347  CE2 PHE A 196     5534   5812   5674   -198    -15    229       C  
ATOM   1348  CZ  PHE A 196      38.074  37.815  40.002  1.00 45.52           C  
ANISOU 1348  CZ  PHE A 196     5627   5908   5759   -216    -32    237       C  
ATOM   1349  N   LEU A 197      40.320  39.235  35.449  1.00 46.12           N  
ANISOU 1349  N   LEU A 197     5682   5931   5909   -169      1    232       N  
ATOM   1350  CA  LEU A 197      40.537  37.891  34.886  1.00 44.02           C  
ANISOU 1350  CA  LEU A 197     5405   5660   5657   -166      0    242       C  
ATOM   1351  C   LEU A 197      41.981  37.633  34.483  1.00 43.66           C  
ANISOU 1351  C   LEU A 197     5348   5600   5639   -167     -3    250       C  
ATOM   1352  O   LEU A 197      42.482  36.529  34.669  1.00 44.24           O  
ANISOU 1352  O   LEU A 197     5410   5669   5727   -171    -13    262       O  
ATOM   1353  CB  LEU A 197      39.624  37.639  33.686  1.00 42.97           C  
ANISOU 1353  CB  LEU A 197     5275   5528   5523   -152     16    236       C  
ATOM   1354  CG  LEU A 197      38.350  36.809  33.817  1.00 41.19           C  
ANISOU 1354  CG  LEU A 197     5052   5313   5283   -150     17    236       C  
ATOM   1355  CD1 LEU A 197      37.702  36.917  35.186  1.00 41.17           C  
ANISOU 1355  CD1 LEU A 197     5057   5326   5261   -161      8    235       C  
ATOM   1356  CD2 LEU A 197      37.390  37.269  32.740  1.00 41.33           C  
ANISOU 1356  CD2 LEU A 197     5077   5331   5295   -137     33    226       C  
ATOM   1357  N   ARG A 198      42.639  38.646  33.927  1.00 43.66           N  
ANISOU 1357  N   ARG A 198     5349   5591   5648   -163      3    245       N  
ATOM   1358  CA  ARG A 198      44.047  38.537  33.559  1.00 46.66           C  
ANISOU 1358  CA  ARG A 198     5716   5955   6055   -165      1    252       C  
ATOM   1359  C   ARG A 198      44.895  38.275  34.800  1.00 49.12           C  
ANISOU 1359  C   ARG A 198     6022   6266   6374   -179    -20    262       C  
ATOM   1360  O   ARG A 198      45.814  37.459  34.771  1.00 49.76           O  
ANISOU 1360  O   ARG A 198     6089   6337   6480   -182    -27    272       O  
ATOM   1361  CB  ARG A 198      44.522  39.809  32.858  1.00 44.26           C  
ANISOU 1361  CB  ARG A 198     5416   5643   5756   -160     12    244       C  
ATOM   1362  CG  ARG A 198      45.818  39.641  32.077  1.00 43.26           C  
ANISOU 1362  CG  ARG A 198     5278   5501   5659   -159     17    248       C  
ATOM   1363  CD  ARG A 198      46.046  40.784  31.100  1.00 42.69           C  
ANISOU 1363  CD  ARG A 198     5211   5421   5588   -153     32    240       C  
ATOM   1364  NE  ARG A 198      44.983  40.868  30.102  1.00 43.62           N  
ANISOU 1364  NE  ARG A 198     5337   5543   5691   -143     48    232       N  
ATOM   1365  CZ  ARG A 198      43.993  41.757  30.126  1.00 42.45           C  
ANISOU 1365  CZ  ARG A 198     5203   5403   5523   -139     51    224       C  
ATOM   1366  NH1 ARG A 198      43.922  42.665  31.096  1.00 41.95           N  
ANISOU 1366  NH1 ARG A 198     5145   5344   5449   -144     42    221       N  
ATOM   1367  NH2 ARG A 198      43.074  41.736  29.174  1.00 41.51           N  
ANISOU 1367  NH2 ARG A 198     5091   5286   5393   -131     63    219       N  
ATOM   1368  N   GLU A 199      44.549  38.974  35.879  1.00 53.53           N  
ANISOU 1368  N   GLU A 199     6591   6834   6912   -188    -29    259       N  
ATOM   1369  CA  GLU A 199      45.215  38.902  37.175  1.00 56.56           C  
ANISOU 1369  CA  GLU A 199     6973   7220   7297   -203    -51    268       C  
ATOM   1370  C   GLU A 199      45.082  37.515  37.790  1.00 57.87           C  
ANISOU 1370  C   GLU A 199     7132   7389   7464   -211    -65    281       C  
ATOM   1371  O   GLU A 199      46.070  36.938  38.229  1.00 58.48           O  
ANISOU 1371  O   GLU A 199     7198   7458   7561   -220    -82    294       O  
ATOM   1372  CB  GLU A 199      44.550  39.895  38.122  1.00 62.12           C  
ANISOU 1372  CB  GLU A 199     7692   7936   7972   -211    -53    259       C  
ATOM   1373  CG  GLU A 199      45.481  40.691  39.006  1.00 66.97           C  
ANISOU 1373  CG  GLU A 199     8308   8547   8588   -223    -68    261       C  
ATOM   1374  CD  GLU A 199      45.768  42.056  38.423  1.00 69.01           C  
ANISOU 1374  CD  GLU A 199     8571   8798   8851   -216    -56    249       C  
ATOM   1375  OE1 GLU A 199      45.349  43.060  39.046  1.00 68.38           O  
ANISOU 1375  OE1 GLU A 199     8502   8725   8752   -220    -56    239       O  
ATOM   1376  OE2 GLU A 199      46.393  42.114  37.337  1.00 67.57           O  
ANISOU 1376  OE2 GLU A 199     8379   8602   8690   -206    -46    250       O  
ATOM   1377  N   ASN A 200      43.848  37.002  37.819  1.00 57.78           N  
ANISOU 1377  N   ASN A 200     7128   7391   7433   -208    -59    278       N  
ATOM   1378  CA  ASN A 200      43.513  35.743  38.481  1.00 54.68           C  
ANISOU 1378  CA  ASN A 200     6732   7005   7037   -217    -73    290       C  
ATOM   1379  C   ASN A 200      43.076  34.660  37.487  1.00 54.93           C  
ANISOU 1379  C   ASN A 200     6756   7034   7081   -205    -62    292       C  
ATOM   1380  O   ASN A 200      41.877  34.371  37.370  1.00 53.78           O  
ANISOU 1380  O   ASN A 200     6617   6900   6917   -200    -54    287       O  
ATOM   1381  CB  ASN A 200      42.394  35.954  39.507  1.00 54.19           C  
ANISOU 1381  CB  ASN A 200     6685   6963   6941   -226    -75    285       C  
ATOM   1382  CG  ASN A 200      42.691  37.071  40.495  1.00 57.79           C  
ANISOU 1382  CG  ASN A 200     7151   7423   7381   -239    -83    280       C  
ATOM   1383  OD1 ASN A 200      43.060  36.813  41.642  1.00 57.31           O  
ANISOU 1383  OD1 ASN A 200     7093   7366   7314   -256   -103    290       O  
ATOM   1384  ND2 ASN A 200      42.508  38.321  40.061  1.00 55.53           N  
ANISOU 1384  ND2 ASN A 200     6872   7136   7090   -230    -69    265       N  
ATOM   1385  N   PRO A 201      44.043  34.033  36.787  1.00 54.32           N  
ANISOU 1385  N   PRO A 201     6662   6941   7035   -201    -63    299       N  
ATOM   1386  CA  PRO A 201      43.691  33.057  35.744  1.00 55.03           C  
ANISOU 1386  CA  PRO A 201     6744   7026   7137   -189    -51    299       C  
ATOM   1387  C   PRO A 201      43.078  31.757  36.279  1.00 54.52           C  
ANISOU 1387  C   PRO A 201     6676   6969   7069   -195    -63    309       C  
ATOM   1388  O   PRO A 201      42.766  30.858  35.502  1.00 56.66           O  
ANISOU 1388  O   PRO A 201     6940   7237   7351   -186    -55    309       O  
ATOM   1389  CB  PRO A 201      45.037  32.775  35.042  1.00 53.80           C  
ANISOU 1389  CB  PRO A 201     6571   6850   7018   -186    -50    303       C  
ATOM   1390  CG  PRO A 201      46.005  33.788  35.575  1.00 53.94           C  
ANISOU 1390  CG  PRO A 201     6589   6862   7041   -194    -58    304       C  
ATOM   1391  CD  PRO A 201      45.503  34.155  36.940  1.00 53.96           C  
ANISOU 1391  CD  PRO A 201     6605   6880   7017   -207    -74    307       C  
ATOM   1392  N   GLN A 202      42.891  31.668  37.590  1.00 57.08           N  
ANISOU 1392  N   GLN A 202     7006   7303   7377   -209    -81    317       N  
ATOM   1393  CA  GLN A 202      42.334  30.465  38.215  1.00 58.25           C  
ANISOU 1393  CA  GLN A 202     7152   7459   7521   -217    -94    329       C  
ATOM   1394  C   GLN A 202      40.810  30.536  38.406  1.00 57.09           C  
ANISOU 1394  C   GLN A 202     7019   7330   7340   -215    -84    321       C  
ATOM   1395  O   GLN A 202      40.205  29.620  38.966  1.00 59.30           O  
ANISOU 1395  O   GLN A 202     7299   7619   7612   -222    -93    329       O  
ATOM   1396  CB  GLN A 202      43.027  30.200  39.560  1.00 59.94           C  
ANISOU 1396  CB  GLN A 202     7363   7672   7735   -237   -122    345       C  
ATOM   1397  CG  GLN A 202      42.476  31.008  40.743  1.00 62.30           C  
ANISOU 1397  CG  GLN A 202     7682   7990   8000   -251   -128    342       C  
ATOM   1398  CD  GLN A 202      42.975  32.449  40.819  1.00 61.17           C  
ANISOU 1398  CD  GLN A 202     7546   7845   7851   -251   -123    331       C  
ATOM   1399  OE1 GLN A 202      43.792  32.894  40.009  1.00 59.74           O  
ANISOU 1399  OE1 GLN A 202     7357   7649   7692   -241   -115    327       O  
ATOM   1400  NE2 GLN A 202      42.486  33.183  41.815  1.00 60.22           N  
ANISOU 1400  NE2 GLN A 202     7441   7738   7699   -263   -126    326       N  
ATOM   1401  N   VAL A 203      40.194  31.617  37.937  1.00 54.92           N  
ANISOU 1401  N   VAL A 203     6756   7061   7050   -206    -66    304       N  
ATOM   1402  CA  VAL A 203      38.766  31.855  38.174  1.00 51.44           C  
ANISOU 1402  CA  VAL A 203     6327   6636   6579   -204    -56    295       C  
ATOM   1403  C   VAL A 203      37.875  31.270  37.081  1.00 47.20           C  
ANISOU 1403  C   VAL A 203     5788   6099   6045   -189    -41    290       C  
ATOM   1404  O   VAL A 203      38.082  31.523  35.896  1.00 45.16           O  
ANISOU 1404  O   VAL A 203     5527   5831   5800   -176    -27    283       O  
ATOM   1405  CB  VAL A 203      38.467  33.363  38.366  1.00 50.84           C  
ANISOU 1405  CB  VAL A 203     6264   6566   6484   -204    -46    280       C  
ATOM   1406  CG1 VAL A 203      36.990  33.606  38.637  1.00 49.62           C  
ANISOU 1406  CG1 VAL A 203     6122   6428   6304   -202    -36    269       C  
ATOM   1407  CG2 VAL A 203      39.298  33.920  39.507  1.00 51.64           C  
ANISOU 1407  CG2 VAL A 203     6369   6669   6581   -220    -62    284       C  
ATOM   1408  N   ASN A 204      36.888  30.482  37.502  1.00 46.01           N  
ANISOU 1408  N   ASN A 204     5640   5960   5881   -193    -43    293       N  
ATOM   1409  CA  ASN A 204      35.874  29.964  36.600  1.00 45.62           C  
ANISOU 1409  CA  ASN A 204     5589   5912   5830   -180    -30    288       C  
ATOM   1410  C   ASN A 204      34.763  30.994  36.433  1.00 44.60           C  
ANISOU 1410  C   ASN A 204     5473   5792   5679   -173    -15    272       C  
ATOM   1411  O   ASN A 204      33.876  31.098  37.281  1.00 46.83           O  
ANISOU 1411  O   ASN A 204     5763   6088   5941   -180    -15    269       O  
ATOM   1412  CB  ASN A 204      35.274  28.656  37.134  1.00 47.63           C  
ANISOU 1412  CB  ASN A 204     5840   6174   6081   -186    -40    299       C  
ATOM   1413  CG  ASN A 204      34.648  27.820  36.039  1.00 48.47           C  
ANISOU 1413  CG  ASN A 204     5941   6277   6198   -173    -30    297       C  
ATOM   1414  OD1 ASN A 204      34.722  28.184  34.871  1.00 49.50           O  
ANISOU 1414  OD1 ASN A 204     6071   6399   6338   -159    -16    288       O  
ATOM   1415  ND2 ASN A 204      34.025  26.702  36.402  1.00 52.51           N  
ANISOU 1415  ND2 ASN A 204     6449   6794   6706   -177    -37    306       N  
ATOM   1416  N   LEU A 205      34.804  31.765  35.353  1.00 40.63           N  
ANISOU 1416  N   LEU A 205     4972   5282   5183   -160     -1    261       N  
ATOM   1417  CA  LEU A 205      33.750  32.747  35.122  1.00 37.88           C  
ANISOU 1417  CA  LEU A 205     4634   4940   4818   -153     11    247       C  
ATOM   1418  C   LEU A 205      33.045  32.571  33.779  1.00 36.74           C  
ANISOU 1418  C   LEU A 205     4490   4790   4679   -138     24    241       C  
ATOM   1419  O   LEU A 205      33.680  32.316  32.748  1.00 35.06           O  
ANISOU 1419  O   LEU A 205     4271   4565   4482   -130     28    243       O  
ATOM   1420  CB  LEU A 205      34.273  34.182  35.300  1.00 35.82           C  
ANISOU 1420  CB  LEU A 205     4380   4676   4554   -154     14    238       C  
ATOM   1421  CG  LEU A 205      33.260  35.332  35.385  1.00 33.62           C  
ANISOU 1421  CG  LEU A 205     4111   4403   4259   -151     25    223       C  
ATOM   1422  CD1 LEU A 205      32.269  35.156  36.517  1.00 33.77           C  
ANISOU 1422  CD1 LEU A 205     4135   4437   4258   -160     23    219       C  
ATOM   1423  CD2 LEU A 205      33.977  36.654  35.541  1.00 34.28           C  
ANISOU 1423  CD2 LEU A 205     4199   4481   4344   -153     25    216       C  
ATOM   1424  N   SER A 206      31.720  32.679  33.829  1.00 36.34           N  
ANISOU 1424  N   SER A 206     4445   4748   4614   -134     31    234       N  
ATOM   1425  CA  SER A 206      30.903  32.785  32.635  1.00 38.27           C  
ANISOU 1425  CA  SER A 206     4692   4989   4860   -120     42    227       C  
ATOM   1426  C   SER A 206      30.310  34.182  32.560  1.00 38.81           C  
ANISOU 1426  C   SER A 206     4768   5057   4919   -116     50    214       C  
ATOM   1427  O   SER A 206      29.865  34.750  33.572  1.00 39.97           O  
ANISOU 1427  O   SER A 206     4919   5213   5053   -123     50    207       O  
ATOM   1428  CB  SER A 206      29.799  31.728  32.614  1.00 38.95           C  
ANISOU 1428  CB  SER A 206     4776   5082   4941   -118     42    230       C  
ATOM   1429  OG  SER A 206      30.337  30.480  32.240  1.00 39.64           O  
ANISOU 1429  OG  SER A 206     4854   5164   5042   -118     37    240       O  
ATOM   1430  N   LEU A 207      30.291  34.718  31.348  1.00 37.72           N  
ANISOU 1430  N   LEU A 207     4633   4910   4788   -105     58    209       N  
ATOM   1431  CA  LEU A 207      29.920  36.101  31.123  1.00 37.24           C  
ANISOU 1431  CA  LEU A 207     4580   4846   4724   -101     64    198       C  
ATOM   1432  C   LEU A 207      28.874  36.133  30.021  1.00 34.98           C  
ANISOU 1432  C   LEU A 207     4296   4556   4438    -90     71    194       C  
ATOM   1433  O   LEU A 207      29.145  35.699  28.911  1.00 34.30           O  
ANISOU 1433  O   LEU A 207     4210   4462   4360    -84     73    198       O  
ATOM   1434  CB  LEU A 207      31.178  36.866  30.703  1.00 38.29           C  
ANISOU 1434  CB  LEU A 207     4713   4969   4866   -101     65    199       C  
ATOM   1435  CG  LEU A 207      31.593  38.224  31.270  1.00 38.50           C  
ANISOU 1435  CG  LEU A 207     4744   4994   4890   -105     64    191       C  
ATOM   1436  CD1 LEU A 207      31.531  38.283  32.793  1.00 39.24           C  
ANISOU 1436  CD1 LEU A 207     4838   5099   4973   -117     58    189       C  
ATOM   1437  CD2 LEU A 207      32.993  38.541  30.760  1.00 36.94           C  
ANISOU 1437  CD2 LEU A 207     4545   4786   4704   -106     64    196       C  
ATOM   1438  N   ASP A 208      27.668  36.597  30.340  1.00 35.02           N  
ANISOU 1438  N   ASP A 208     4303   4565   4435    -87     73    185       N  
ATOM   1439  CA  ASP A 208      26.632  36.771  29.327  1.00 35.24           C  
ANISOU 1439  CA  ASP A 208     4334   4588   4465    -77     78    181       C  
ATOM   1440  C   ASP A 208      26.570  38.234  28.911  1.00 35.10           C  
ANISOU 1440  C   ASP A 208     4322   4561   4451    -73     80    173       C  
ATOM   1441  O   ASP A 208      26.176  39.106  29.690  1.00 34.53           O  
ANISOU 1441  O   ASP A 208     4250   4492   4376    -75     82    164       O  
ATOM   1442  CB  ASP A 208      25.266  36.265  29.812  1.00 36.10           C  
ANISOU 1442  CB  ASP A 208     4441   4705   4568    -76     78    178       C  
ATOM   1443  CG  ASP A 208      24.197  36.256  28.699  1.00 37.49           C  
ANISOU 1443  CG  ASP A 208     4619   4875   4749    -66     80    176       C  
ATOM   1444  OD1 ASP A 208      24.407  36.862  27.615  1.00 36.55           O  
ANISOU 1444  OD1 ASP A 208     4505   4746   4636    -60     81    176       O  
ATOM   1445  OD2 ASP A 208      23.124  35.643  28.917  1.00 37.73           O  
ANISOU 1445  OD2 ASP A 208     4646   4911   4778    -64     81    175       O  
ATOM   1446  N   MET A 209      26.965  38.478  27.667  1.00 35.91           N  
ANISOU 1446  N   MET A 209     4429   4654   4561    -68     82    177       N  
ATOM   1447  CA  MET A 209      27.150  39.820  27.144  1.00 37.45           C  
ANISOU 1447  CA  MET A 209     4630   4839   4760    -65     83    172       C  
ATOM   1448  C   MET A 209      26.114  40.171  26.082  1.00 36.73           C  
ANISOU 1448  C   MET A 209     4543   4740   4672    -57     83    170       C  
ATOM   1449  O   MET A 209      26.273  41.157  25.363  1.00 39.81           O  
ANISOU 1449  O   MET A 209     4938   5120   5066    -55     82    170       O  
ATOM   1450  CB  MET A 209      28.561  39.938  26.546  1.00 40.22           C  
ANISOU 1450  CB  MET A 209     4982   5183   5115    -68     84    178       C  
ATOM   1451  CG  MET A 209      29.282  41.229  26.902  1.00 45.64           C  
ANISOU 1451  CG  MET A 209     5671   5865   5805    -71     84    174       C  
ATOM   1452  SD  MET A 209      29.617  41.256  28.674  1.00 48.85           S  
ANISOU 1452  SD  MET A 209     6072   6282   6206    -80     81    169       S  
ATOM   1453  CE  MET A 209      30.294  39.610  28.802  1.00 46.10           C  
ANISOU 1453  CE  MET A 209     5717   5939   5857    -84     78    181       C  
ATOM   1454  N   SER A 210      25.057  39.371  25.987  1.00 34.90           N  
ANISOU 1454  N   SER A 210     4308   4512   4438    -54     82    171       N  
ATOM   1455  CA  SER A 210      24.014  39.547  24.972  1.00 33.84           C  
ANISOU 1455  CA  SER A 210     4178   4371   4307    -47     80    171       C  
ATOM   1456  C   SER A 210      23.329  40.900  24.997  1.00 33.42           C  
ANISOU 1456  C   SER A 210     4126   4309   4260    -43     78    163       C  
ATOM   1457  O   SER A 210      23.288  41.566  26.025  1.00 34.84           O  
ANISOU 1457  O   SER A 210     4302   4493   4442    -45     80    154       O  
ATOM   1458  CB  SER A 210      22.939  38.477  25.131  1.00 32.56           C  
ANISOU 1458  CB  SER A 210     4011   4215   4142    -44     79    172       C  
ATOM   1459  OG  SER A 210      23.504  37.201  24.981  1.00 32.17           O  
ANISOU 1459  OG  SER A 210     3961   4171   4089    -47     79    180       O  
ATOM   1460  N   LEU A 211      22.773  41.282  23.851  1.00 33.14           N  
ANISOU 1460  N   LEU A 211     4096   4263   4230    -38     73    166       N  
ATOM   1461  CA  LEU A 211      21.940  42.471  23.729  1.00 32.12           C  
ANISOU 1461  CA  LEU A 211     3967   4125   4111    -34     69    159       C  
ATOM   1462  C   LEU A 211      22.645  43.718  24.258  1.00 32.06           C  
ANISOU 1462  C   LEU A 211     3959   4113   4108    -37     71    153       C  
ATOM   1463  O   LEU A 211      22.034  44.593  24.856  1.00 34.07           O  
ANISOU 1463  O   LEU A 211     4208   4364   4370    -35     71    143       O  
ATOM   1464  CB  LEU A 211      20.572  42.261  24.401  1.00 32.06           C  
ANISOU 1464  CB  LEU A 211     3950   4120   4108    -30     69    151       C  
ATOM   1465  CG  LEU A 211      19.353  41.587  23.723  1.00 31.19           C  
ANISOU 1465  CG  LEU A 211     3839   4007   4002    -25     64    155       C  
ATOM   1466  CD1 LEU A 211      19.310  41.759  22.215  1.00 30.79           C  
ANISOU 1466  CD1 LEU A 211     3798   3945   3954    -23     56    165       C  
ATOM   1467  CD2 LEU A 211      19.239  40.122  24.084  1.00 30.70           C  
ANISOU 1467  CD2 LEU A 211     3774   3958   3931    -26     68    158       C  
ATOM   1468  N   ASN A 212      23.948  43.773  24.034  1.00 31.90           N  
ANISOU 1468  N   ASN A 212     3944   4093   4083    -42     73    158       N  
ATOM   1469  CA  ASN A 212      24.742  44.961  24.299  1.00 31.80           C  
ANISOU 1469  CA  ASN A 212     3932   4074   4075    -44     73    155       C  
ATOM   1470  C   ASN A 212      25.275  45.529  22.979  1.00 30.97           C  
ANISOU 1470  C   ASN A 212     3836   3957   3972    -45     70    163       C  
ATOM   1471  O   ASN A 212      25.845  44.795  22.174  1.00 29.73           O  
ANISOU 1471  O   ASN A 212     3685   3801   3809    -47     72    173       O  
ATOM   1472  CB  ASN A 212      25.886  44.625  25.260  1.00 31.88           C  
ANISOU 1472  CB  ASN A 212     3939   4094   4078    -51     78    154       C  
ATOM   1473  CG  ASN A 212      25.487  44.777  26.719  1.00 31.53           C  
ANISOU 1473  CG  ASN A 212     3888   4059   4032    -53     81    142       C  
ATOM   1474  OD1 ASN A 212      25.456  45.881  27.253  1.00 31.71           O  
ANISOU 1474  OD1 ASN A 212     3909   4077   4060    -54     81    133       O  
ATOM   1475  ND2 ASN A 212      25.196  43.665  27.371  1.00 31.75           N  
ANISOU 1475  ND2 ASN A 212     3912   4099   4052    -56     83    143       N  
ATOM   1476  N   PRO A 213      25.082  46.839  22.741  1.00 31.51           N  
ANISOU 1476  N   PRO A 213     3907   4014   4051    -44     65    160       N  
ATOM   1477  CA  PRO A 213      25.501  47.416  21.459  1.00 31.57           C  
ANISOU 1477  CA  PRO A 213     3925   4010   4060    -46     60    170       C  
ATOM   1478  C   PRO A 213      27.031  47.561  21.365  1.00 32.46           C  
ANISOU 1478  C   PRO A 213     4041   4123   4168    -52     66    174       C  
ATOM   1479  O   PRO A 213      27.559  48.670  21.419  1.00 34.10           O  
ANISOU 1479  O   PRO A 213     4250   4323   4383    -54     65    173       O  
ATOM   1480  CB  PRO A 213      24.807  48.775  21.454  1.00 30.26           C  
ANISOU 1480  CB  PRO A 213     3757   3831   3909    -42     53    165       C  
ATOM   1481  CG  PRO A 213      24.711  49.143  22.886  1.00 30.88           C  
ANISOU 1481  CG  PRO A 213     3824   3915   3991    -41     57    151       C  
ATOM   1482  CD  PRO A 213      24.562  47.866  23.665  1.00 31.44           C  
ANISOU 1482  CD  PRO A 213     3890   4001   4052    -41     64    148       C  
ATOM   1483  N   ILE A 214      27.729  46.440  21.241  1.00 32.66           N  
ANISOU 1483  N   ILE A 214     4067   4156   4184    -55     73    179       N  
ATOM   1484  CA  ILE A 214      29.182  46.444  21.259  1.00 34.75           C  
ANISOU 1484  CA  ILE A 214     4332   4422   4448    -61     79    182       C  
ATOM   1485  C   ILE A 214      29.647  46.861  19.881  1.00 36.12           C  
ANISOU 1485  C   ILE A 214     4516   4585   4620    -65     79    191       C  
ATOM   1486  O   ILE A 214      29.235  46.274  18.877  1.00 37.69           O  
ANISOU 1486  O   ILE A 214     4723   4784   4814    -66     79    196       O  
ATOM   1487  CB  ILE A 214      29.769  45.053  21.617  1.00 34.48           C  
ANISOU 1487  CB  ILE A 214     4293   4399   4408    -63     86    184       C  
ATOM   1488  CG1 ILE A 214      29.366  44.633  23.025  1.00 33.96           C  
ANISOU 1488  CG1 ILE A 214     4218   4343   4341    -62     84    177       C  
ATOM   1489  CG2 ILE A 214      31.289  45.063  21.545  1.00 34.16           C  
ANISOU 1489  CG2 ILE A 214     4253   4357   4370    -70     92    188       C  
ATOM   1490  CD1 ILE A 214      29.845  43.243  23.379  1.00 35.32           C  
ANISOU 1490  CD1 ILE A 214     4385   4525   4510    -64     88    181       C  
ATOM   1491  N   ASP A 215      30.490  47.882  19.823  1.00 36.53           N  
ANISOU 1491  N   ASP A 215     4571   4631   4678    -69     80    191       N  
ATOM   1492  CA  ASP A 215      30.989  48.328  18.538  1.00 38.40           C  
ANISOU 1492  CA  ASP A 215     4818   4858   4912    -75     81    200       C  
ATOM   1493  C   ASP A 215      32.513  48.385  18.511  1.00 38.72           C  
ANISOU 1493  C   ASP A 215     4858   4898   4954    -82     90    202       C  
ATOM   1494  O   ASP A 215      33.101  48.736  17.489  1.00 39.75           O  
ANISOU 1494  O   ASP A 215     4997   5021   5082    -88     94    208       O  
ATOM   1495  CB  ASP A 215      30.344  49.663  18.137  1.00 40.67           C  
ANISOU 1495  CB  ASP A 215     5112   5134   5207    -74     70    201       C  
ATOM   1496  CG  ASP A 215      30.868  50.847  18.939  1.00 42.12           C  
ANISOU 1496  CG  ASP A 215     5289   5312   5401    -74     68    196       C  
ATOM   1497  OD1 ASP A 215      32.100  51.031  18.996  1.00 41.50           O  
ANISOU 1497  OD1 ASP A 215     5210   5233   5322    -79     75    197       O  
ATOM   1498  OD2 ASP A 215      30.043  51.613  19.491  1.00 44.40           O  
ANISOU 1498  OD2 ASP A 215     5573   5596   5698    -69     60    189       O  
ATOM   1499  N   PHE A 216      33.139  48.012  19.629  1.00 37.31           N  
ANISOU 1499  N   PHE A 216     4669   4727   4779    -81     94    196       N  
ATOM   1500  CA  PHE A 216      34.583  48.134  19.787  1.00 35.75           C  
ANISOU 1500  CA  PHE A 216     4469   4528   4587    -87    101    198       C  
ATOM   1501  C   PHE A 216      35.129  47.275  20.939  1.00 34.55           C  
ANISOU 1501  C   PHE A 216     4304   4384   4436    -86    103    194       C  
ATOM   1502  O   PHE A 216      34.744  47.442  22.095  1.00 33.32           O  
ANISOU 1502  O   PHE A 216     4143   4234   4283    -84     97    188       O  
ATOM   1503  CB  PHE A 216      34.942  49.624  19.941  1.00 35.15           C  
ANISOU 1503  CB  PHE A 216     4393   4442   4517    -88     96    197       C  
ATOM   1504  CG  PHE A 216      36.317  49.891  20.497  1.00 34.88           C  
ANISOU 1504  CG  PHE A 216     4354   4407   4492    -93    101    196       C  
ATOM   1505  CD1 PHE A 216      37.448  49.312  19.934  1.00 34.37           C  
ANISOU 1505  CD1 PHE A 216     4288   4341   4429    -99    111    201       C  
ATOM   1506  CD2 PHE A 216      36.477  50.766  21.566  1.00 33.85           C  
ANISOU 1506  CD2 PHE A 216     4217   4275   4368    -92     95    190       C  
ATOM   1507  CE1 PHE A 216      38.706  49.585  20.443  1.00 34.44           C  
ANISOU 1507  CE1 PHE A 216     4290   4348   4448   -103    114    200       C  
ATOM   1508  CE2 PHE A 216      37.729  51.038  22.080  1.00 33.79           C  
ANISOU 1508  CE2 PHE A 216     4204   4266   4368    -97     97    190       C  
ATOM   1509  CZ  PHE A 216      38.847  50.451  21.515  1.00 34.62           C  
ANISOU 1509  CZ  PHE A 216     4307   4369   4476   -102    106    195       C  
ATOM   1510  N   ILE A 217      36.021  46.351  20.587  1.00 34.75           N  
ANISOU 1510  N   ILE A 217     4327   4412   4464    -90    112    198       N  
ATOM   1511  CA  ILE A 217      36.824  45.575  21.542  1.00 34.57           C  
ANISOU 1511  CA  ILE A 217     4293   4394   4447    -92    113    197       C  
ATOM   1512  C   ILE A 217      38.305  45.934  21.364  1.00 35.07           C  
ANISOU 1512  C   ILE A 217     4353   4450   4522    -99    119    199       C  
ATOM   1513  O   ILE A 217      38.885  45.712  20.295  1.00 35.58           O  
ANISOU 1513  O   ILE A 217     4420   4509   4588   -103    129    203       O  
ATOM   1514  CB  ILE A 217      36.639  44.050  21.354  1.00 33.90           C  
ANISOU 1514  CB  ILE A 217     4204   4316   4360    -91    117    199       C  
ATOM   1515  CG1 ILE A 217      35.166  43.661  21.536  1.00 33.73           C  
ANISOU 1515  CG1 ILE A 217     4184   4301   4328    -85    111    197       C  
ATOM   1516  CG2 ILE A 217      37.548  43.279  22.310  1.00 33.65           C  
ANISOU 1516  CG2 ILE A 217     4159   4287   4337    -94    116    200       C  
ATOM   1517  CD1 ILE A 217      34.882  42.182  21.370  1.00 33.49           C  
ANISOU 1517  CD1 ILE A 217     4151   4277   4296    -84    114    199       C  
ATOM   1518  N   GLN A 218      38.913  46.484  22.411  1.00 35.51           N  
ANISOU 1518  N   GLN A 218     4402   4506   4584   -100    114    197       N  
ATOM   1519  CA  GLN A 218      40.289  46.973  22.341  1.00 36.41           C  
ANISOU 1519  CA  GLN A 218     4512   4612   4711   -106    118    199       C  
ATOM   1520  C   GLN A 218      41.292  45.892  21.942  1.00 37.53           C  
ANISOU 1520  C   GLN A 218     4645   4751   4861   -110    127    203       C  
ATOM   1521  O   GLN A 218      41.069  44.707  22.161  1.00 36.18           O  
ANISOU 1521  O   GLN A 218     4469   4587   4691   -109    127    203       O  
ATOM   1522  CB  GLN A 218      40.697  47.632  23.660  1.00 37.31           C  
ANISOU 1522  CB  GLN A 218     4619   4726   4829   -108    108    196       C  
ATOM   1523  CG  GLN A 218      42.111  48.204  23.638  1.00 39.53           C  
ANISOU 1523  CG  GLN A 218     4896   4999   5125   -114    111    199       C  
ATOM   1524  CD  GLN A 218      42.447  49.087  24.830  1.00 39.27           C  
ANISOU 1524  CD  GLN A 218     4858   4965   5095   -116    100    195       C  
ATOM   1525  OE1 GLN A 218      41.783  49.050  25.874  1.00 41.95           O  
ANISOU 1525  OE1 GLN A 218     5197   5312   5427   -114     91    191       O  
ATOM   1526  NE2 GLN A 218      43.494  49.884  24.680  1.00 37.92           N  
ANISOU 1526  NE2 GLN A 218     4686   4785   4936   -120    102    197       N  
ATOM   1527  N   ASP A 219      42.398  46.318  21.345  1.00 41.03           N  
ANISOU 1527  N   ASP A 219     5088   5186   5316   -116    136    205       N  
ATOM   1528  CA  ASP A 219      43.417  45.394  20.886  1.00 43.71           C  
ANISOU 1528  CA  ASP A 219     5418   5521   5668   -120    147    207       C  
ATOM   1529  C   ASP A 219      44.047  44.720  22.093  1.00 44.54           C  
ANISOU 1529  C   ASP A 219     5508   5628   5786   -121    139    208       C  
ATOM   1530  O   ASP A 219      44.344  45.380  23.088  1.00 46.36           O  
ANISOU 1530  O   ASP A 219     5735   5859   6020   -122    128    208       O  
ATOM   1531  CB  ASP A 219      44.475  46.133  20.072  1.00 45.44           C  
ANISOU 1531  CB  ASP A 219     5638   5729   5895   -126    158    208       C  
ATOM   1532  CG  ASP A 219      45.305  45.204  19.221  1.00 47.94           C  
ANISOU 1532  CG  ASP A 219     5950   6041   6223   -131    174    207       C  
ATOM   1533  OD1 ASP A 219      46.427  44.846  19.641  1.00 49.66           O  
ANISOU 1533  OD1 ASP A 219     6153   6254   6461   -134    177    208       O  
ATOM   1534  OD2 ASP A 219      44.826  44.821  18.134  1.00 50.78           O  
ANISOU 1534  OD2 ASP A 219     6319   6403   6573   -133    185    206       O  
ATOM   1535  N   GLN A 220      44.221  43.404  22.004  1.00 44.96           N  
ANISOU 1535  N   GLN A 220     5553   5683   5846   -121    143    209       N  
ATOM   1536  CA  GLN A 220      44.793  42.597  23.088  1.00 46.58           C  
ANISOU 1536  CA  GLN A 220     5743   5889   6065   -122    133    212       C  
ATOM   1537  C   GLN A 220      43.919  42.507  24.351  1.00 43.23           C  
ANISOU 1537  C   GLN A 220     5320   5476   5629   -120    117    212       C  
ATOM   1538  O   GLN A 220      44.400  42.090  25.402  1.00 43.39           O  
ANISOU 1538  O   GLN A 220     5330   5497   5658   -123    106    216       O  
ATOM   1539  CB  GLN A 220      46.213  43.075  23.453  1.00 51.13           C  
ANISOU 1539  CB  GLN A 220     6308   6455   6661   -128    132    214       C  
ATOM   1540  CG  GLN A 220      47.307  42.674  22.471  1.00 57.25           C  
ANISOU 1540  CG  GLN A 220     7076   7219   7456   -132    149    213       C  
ATOM   1541  CD  GLN A 220      48.637  42.398  23.169  1.00 64.21           C  
ANISOU 1541  CD  GLN A 220     7940   8092   8365   -137    144    217       C  
ATOM   1542  OE1 GLN A 220      49.464  43.295  23.348  1.00 68.45           O  
ANISOU 1542  OE1 GLN A 220     8473   8621   8911   -141    143    218       O  
ATOM   1543  NE2 GLN A 220      48.839  41.153  23.583  1.00 66.97           N  
ANISOU 1543  NE2 GLN A 220     8276   8441   8728   -137    139    219       N  
ATOM   1544  N   ALA A 221      42.640  42.869  24.244  1.00 41.20           N  
ANISOU 1544  N   ALA A 221     5074   5226   5352   -115    115    209       N  
ATOM   1545  CA  ALA A 221      41.736  42.919  25.413  1.00 39.95           C  
ANISOU 1545  CA  ALA A 221     4918   5078   5182   -113    102    208       C  
ATOM   1546  C   ALA A 221      41.455  41.562  26.052  1.00 39.03           C  
ANISOU 1546  C   ALA A 221     4793   4969   5065   -113     96    211       C  
ATOM   1547  O   ALA A 221      41.224  41.482  27.253  1.00 39.03           O  
ANISOU 1547  O   ALA A 221     4791   4976   5060   -116     84    212       O  
ATOM   1548  CB  ALA A 221      40.430  43.620  25.065  1.00 36.67           C  
ANISOU 1548  CB  ALA A 221     4515   4667   4748   -107    103    203       C  
ATOM   1549  N   PHE A 222      41.477  40.507  25.239  1.00 39.95           N  
ANISOU 1549  N   PHE A 222     4907   5084   5188   -112    104    213       N  
ATOM   1550  CA  PHE A 222      41.230  39.133  25.697  1.00 41.34           C  
ANISOU 1550  CA  PHE A 222     5074   5265   5366   -112     98    217       C  
ATOM   1551  C   PHE A 222      42.512  38.296  25.780  1.00 43.07           C  
ANISOU 1551  C   PHE A 222     5279   5476   5610   -117     98    222       C  
ATOM   1552  O   PHE A 222      42.468  37.068  26.003  1.00 43.19           O  
ANISOU 1552  O   PHE A 222     5284   5492   5632   -117     94    226       O  
ATOM   1553  CB  PHE A 222      40.211  38.439  24.782  1.00 39.81           C  
ANISOU 1553  CB  PHE A 222     4886   5074   5162   -106    106    215       C  
ATOM   1554  CG  PHE A 222      38.794  38.723  25.144  1.00 37.60           C  
ANISOU 1554  CG  PHE A 222     4616   4805   4863   -101    101    212       C  
ATOM   1555  CD1 PHE A 222      38.146  39.827  24.633  1.00 37.70           C  
ANISOU 1555  CD1 PHE A 222     4641   4818   4865    -98    104    207       C  
ATOM   1556  CD2 PHE A 222      38.106  37.880  26.004  1.00 38.77           C  
ANISOU 1556  CD2 PHE A 222     4760   4963   5005   -101     92    214       C  
ATOM   1557  CE1 PHE A 222      36.826  40.090  24.970  1.00 39.07           C  
ANISOU 1557  CE1 PHE A 222     4822   5000   5024    -94     99    204       C  
ATOM   1558  CE2 PHE A 222      36.790  38.130  26.350  1.00 38.90           C  
ANISOU 1558  CE2 PHE A 222     4784   4988   5005    -98     88    211       C  
ATOM   1559  CZ  PHE A 222      36.146  39.241  25.828  1.00 39.42           C  
ANISOU 1559  CZ  PHE A 222     4861   5053   5062    -94     92    205       C  
ATOM   1560  N   GLN A 223      43.649  38.968  25.600  1.00 43.24           N  
ANISOU 1560  N   GLN A 223     5295   5487   5644   -120    102    222       N  
ATOM   1561  CA  GLN A 223      44.939  38.315  25.683  1.00 42.48           C  
ANISOU 1561  CA  GLN A 223     5184   5381   5575   -125    102    226       C  
ATOM   1562  C   GLN A 223      45.144  37.834  27.106  1.00 41.01           C  
ANISOU 1562  C   GLN A 223     4989   5199   5395   -130     82    234       C  
ATOM   1563  O   GLN A 223      44.992  38.604  28.064  1.00 39.07           O  
ANISOU 1563  O   GLN A 223     4748   4958   5137   -133     70    235       O  
ATOM   1564  CB  GLN A 223      46.064  39.252  25.256  1.00 44.29           C  
ANISOU 1564  CB  GLN A 223     5410   5599   5818   -128    110    225       C  
ATOM   1565  CG  GLN A 223      47.183  38.536  24.520  1.00 46.93           C  
ANISOU 1565  CG  GLN A 223     5731   5920   6179   -131    122    225       C  
ATOM   1566  CD  GLN A 223      46.838  38.242  23.067  1.00 47.55           C  
ANISOU 1566  CD  GLN A 223     5816   5997   6253   -128    142    218       C  
ATOM   1567  OE1 GLN A 223      46.851  37.090  22.636  1.00 45.50           O  
ANISOU 1567  OE1 GLN A 223     5549   5735   6003   -127    149    217       O  
ATOM   1568  NE2 GLN A 223      46.534  39.291  22.303  1.00 50.85           N  
ANISOU 1568  NE2 GLN A 223     6249   6416   6655   -127    152    214       N  
ATOM   1569  N   GLY A 224      45.431  36.538  27.219  1.00 40.70           N  
ANISOU 1569  N   GLY A 224     4937   5156   5372   -132     78    239       N  
ATOM   1570  CA  GLY A 224      45.622  35.868  28.496  1.00 39.32           C  
ANISOU 1570  CA  GLY A 224     4752   4984   5203   -138     58    248       C  
ATOM   1571  C   GLY A 224      44.380  35.748  29.356  1.00 39.62           C  
ANISOU 1571  C   GLY A 224     4800   5037   5215   -138     47    250       C  
ATOM   1572  O   GLY A 224      44.498  35.629  30.566  1.00 41.87           O  
ANISOU 1572  O   GLY A 224     5083   5327   5498   -146     30    257       O  
ATOM   1573  N   ILE A 225      43.184  35.780  28.765  1.00 39.24           N  
ANISOU 1573  N   ILE A 225     4763   4997   5146   -131     57    244       N  
ATOM   1574  CA  ILE A 225      41.977  35.602  29.587  1.00 38.43           C  
ANISOU 1574  CA  ILE A 225     4669   4910   5022   -131     48    244       C  
ATOM   1575  C   ILE A 225      41.205  34.322  29.260  1.00 37.91           C  
ANISOU 1575  C   ILE A 225     4599   4848   4954   -127     50    247       C  
ATOM   1576  O   ILE A 225      41.065  33.931  28.094  1.00 36.91           O  
ANISOU 1576  O   ILE A 225     4472   4716   4833   -121     63    242       O  
ATOM   1577  CB  ILE A 225      41.045  36.857  29.675  1.00 38.43           C  
ANISOU 1577  CB  ILE A 225     4685   4919   4998   -128     52    236       C  
ATOM   1578  CG1 ILE A 225      39.867  36.754  28.720  1.00 38.62           C  
ANISOU 1578  CG1 ILE A 225     4717   4947   5008   -119     64    230       C  
ATOM   1579  CG2 ILE A 225      41.792  38.178  29.519  1.00 37.86           C  
ANISOU 1579  CG2 ILE A 225     4616   4839   4929   -129     55    232       C  
ATOM   1580  CD1 ILE A 225      38.646  36.143  29.369  1.00 38.73           C  
ANISOU 1580  CD1 ILE A 225     4734   4973   5006   -119     57    230       C  
ATOM   1581  N   LYS A 226      40.733  33.673  30.322  1.00 38.06           N  
ANISOU 1581  N   LYS A 226     4617   4876   4966   -133     35    253       N  
ATOM   1582  CA  LYS A 226      40.076  32.376  30.254  1.00 37.11           C  
ANISOU 1582  CA  LYS A 226     4493   4760   4847   -131     33    257       C  
ATOM   1583  C   LYS A 226      38.618  32.556  30.643  1.00 35.54           C  
ANISOU 1583  C   LYS A 226     4306   4576   4621   -129     33    254       C  
ATOM   1584  O   LYS A 226      38.308  33.281  31.585  1.00 35.00           O  
ANISOU 1584  O   LYS A 226     4245   4517   4537   -134     26    252       O  
ATOM   1585  CB  LYS A 226      40.754  31.412  31.225  1.00 39.87           C  
ANISOU 1585  CB  LYS A 226     4829   5107   5212   -141     15    270       C  
ATOM   1586  CG  LYS A 226      40.613  29.934  30.893  1.00 44.99           C  
ANISOU 1586  CG  LYS A 226     5466   5752   5875   -139     14    276       C  
ATOM   1587  CD  LYS A 226      40.862  29.076  32.134  1.00 48.48           C  
ANISOU 1587  CD  LYS A 226     5899   6196   6323   -150     -7    290       C  
ATOM   1588  CE  LYS A 226      41.763  27.873  31.855  1.00 51.36           C  
ANISOU 1588  CE  LYS A 226     6244   6546   6722   -151    -12    298       C  
ATOM   1589  NZ  LYS A 226      41.216  26.910  30.853  1.00 52.35           N  
ANISOU 1589  NZ  LYS A 226     6366   6669   6855   -142      0    294       N  
ATOM   1590  N   LEU A 227      37.719  31.925  29.897  1.00 34.62           N  
ANISOU 1590  N   LEU A 227     4191   4462   4499   -121     41    251       N  
ATOM   1591  CA  LEU A 227      36.302  31.923  30.250  1.00 33.07           C  
ANISOU 1591  CA  LEU A 227     4004   4279   4282   -119     41    248       C  
ATOM   1592  C   LEU A 227      35.696  30.540  30.038  1.00 32.39           C  
ANISOU 1592  C   LEU A 227     3911   4195   4198   -117     39    252       C  
ATOM   1593  O   LEU A 227      36.113  29.794  29.156  1.00 31.95           O  
ANISOU 1593  O   LEU A 227     3849   4131   4160   -113     44    254       O  
ATOM   1594  CB  LEU A 227      35.531  32.976  29.451  1.00 32.84           C  
ANISOU 1594  CB  LEU A 227     3987   4251   4239   -111     53    236       C  
ATOM   1595  CG  LEU A 227      35.616  34.468  29.798  1.00 33.74           C  
ANISOU 1595  CG  LEU A 227     4109   4366   4344   -112     54    230       C  
ATOM   1596  CD1 LEU A 227      34.918  35.313  28.739  1.00 32.88           C  
ANISOU 1596  CD1 LEU A 227     4010   4255   4228   -103     66    221       C  
ATOM   1597  CD2 LEU A 227      35.036  34.779  31.169  1.00 34.07           C  
ANISOU 1597  CD2 LEU A 227     4154   4420   4370   -119     45    229       C  
ATOM   1598  N   HIS A 228      34.723  30.192  30.870  1.00 32.72           N  
ANISOU 1598  N   HIS A 228     3956   4249   4226   -120     32    255       N  
ATOM   1599  CA  HIS A 228      33.973  28.969  30.668  1.00 32.55           C  
ANISOU 1599  CA  HIS A 228     3930   4231   4205   -118     31    259       C  
ATOM   1600  C   HIS A 228      33.035  29.131  29.501  1.00 32.47           C  
ANISOU 1600  C   HIS A 228     3927   4220   4188   -106     44    250       C  
ATOM   1601  O   HIS A 228      33.226  28.512  28.460  1.00 33.31           O  
ANISOU 1601  O   HIS A 228     4030   4318   4307   -100     51    249       O  
ATOM   1602  CB  HIS A 228      33.214  28.560  31.934  1.00 32.71           C  
ANISOU 1602  CB  HIS A 228     3951   4264   4210   -126     20    265       C  
ATOM   1603  CG  HIS A 228      32.419  27.282  31.772  1.00 32.29           C  
ANISOU 1603  CG  HIS A 228     3894   4214   4159   -124     18    270       C  
ATOM   1604  ND1 HIS A 228      33.006  26.073  31.670  1.00 32.22           N  
ANISOU 1604  ND1 HIS A 228     3873   4199   4170   -126     10    279       N  
ATOM   1605  CD2 HIS A 228      31.048  27.063  31.661  1.00 31.91           C  
ANISOU 1605  CD2 HIS A 228     3851   4175   4097   -119     22    266       C  
ATOM   1606  CE1 HIS A 228      32.062  25.129  31.509  1.00 31.69           C  
ANISOU 1606  CE1 HIS A 228     3804   4136   4100   -123     10    282       C  
ATOM   1607  NE2 HIS A 228      30.864  25.735  31.504  1.00 31.72           N  
ANISOU 1607  NE2 HIS A 228     3818   4149   4082   -119     17    273       N  
ATOM   1608  N   GLU A 229      32.027  29.979  29.667  1.00 31.77           N  
ANISOU 1608  N   GLU A 229     3850   4140   4082   -103     48    243       N  
ATOM   1609  CA  GLU A 229      31.012  30.207  28.654  1.00 31.44           C  
ANISOU 1609  CA  GLU A 229     3815   4098   4033    -94     58    235       C  
ATOM   1610  C   GLU A 229      30.949  31.710  28.395  1.00 31.10           C  
ANISOU 1610  C   GLU A 229     3781   4052   3981    -91     64    226       C  
ATOM   1611  O   GLU A 229      30.928  32.504  29.339  1.00 31.99           O  
ANISOU 1611  O   GLU A 229     3896   4170   4086    -96     60    223       O  
ATOM   1612  CB  GLU A 229      29.668  29.656  29.142  1.00 32.59           C  
ANISOU 1612  CB  GLU A 229     3961   4253   4167    -93     55    235       C  
ATOM   1613  CG  GLU A 229      28.446  30.009  28.304  1.00 35.21           C  
ANISOU 1613  CG  GLU A 229     4301   4586   4491    -84     62    228       C  
ATOM   1614  CD  GLU A 229      27.185  29.242  28.724  1.00 37.85           C  
ANISOU 1614  CD  GLU A 229     4633   4929   4818    -83     59    229       C  
ATOM   1615  OE1 GLU A 229      27.060  28.024  28.401  1.00 37.98           O  
ANISOU 1615  OE1 GLU A 229     4644   4944   4841    -82     57    235       O  
ATOM   1616  OE2 GLU A 229      26.302  29.864  29.366  1.00 38.03           O  
ANISOU 1616  OE2 GLU A 229     4660   4960   4829    -84     60    223       O  
ATOM   1617  N   LEU A 230      30.965  32.098  27.122  1.00 29.95           N  
ANISOU 1617  N   LEU A 230     3641   3898   3839    -84     73    222       N  
ATOM   1618  CA  LEU A 230      30.815  33.496  26.732  1.00 29.42           C  
ANISOU 1618  CA  LEU A 230     3583   3828   3767    -81     78    214       C  
ATOM   1619  C   LEU A 230      29.700  33.616  25.708  1.00 29.73           C  
ANISOU 1619  C   LEU A 230     3630   3865   3800    -73     83    210       C  
ATOM   1620  O   LEU A 230      29.765  33.004  24.643  1.00 30.60           O  
ANISOU 1620  O   LEU A 230     3741   3970   3914    -70     87    212       O  
ATOM   1621  CB  LEU A 230      32.115  34.057  26.158  1.00 29.52           C  
ANISOU 1621  CB  LEU A 230     3596   3830   3789    -82     83    214       C  
ATOM   1622  CG  LEU A 230      32.033  35.444  25.484  1.00 30.03           C  
ANISOU 1622  CG  LEU A 230     3670   3889   3849    -79     88    208       C  
ATOM   1623  CD1 LEU A 230      31.543  36.525  26.437  1.00 29.04           C  
ANISOU 1623  CD1 LEU A 230     3549   3769   3715    -80     84    203       C  
ATOM   1624  CD2 LEU A 230      33.369  35.847  24.871  1.00 29.56           C  
ANISOU 1624  CD2 LEU A 230     3611   3820   3800    -82     94    209       C  
ATOM   1625  N   THR A 231      28.669  34.390  26.038  1.00 29.73           N  
ANISOU 1625  N   THR A 231     3635   3870   3791    -70     82    204       N  
ATOM   1626  CA  THR A 231      27.523  34.539  25.150  1.00 29.73           C  
ANISOU 1626  CA  THR A 231     3641   3867   3787    -63     84    201       C  
ATOM   1627  C   THR A 231      27.511  35.914  24.500  1.00 29.54           C  
ANISOU 1627  C   THR A 231     3625   3835   3762    -60     86    196       C  
ATOM   1628  O   THR A 231      27.480  36.940  25.186  1.00 28.48           O  
ANISOU 1628  O   THR A 231     3492   3701   3626    -61     85    191       O  
ATOM   1629  CB  THR A 231      26.180  34.266  25.862  1.00 29.84           C  
ANISOU 1629  CB  THR A 231     3653   3890   3795    -61     80    198       C  
ATOM   1630  OG1 THR A 231      26.180  32.930  26.386  1.00 31.00           O  
ANISOU 1630  OG1 THR A 231     3791   4043   3941    -64     77    204       O  
ATOM   1631  CG2 THR A 231      25.031  34.400  24.882  1.00 28.74           C  
ANISOU 1631  CG2 THR A 231     3519   3745   3654    -54     81    196       C  
ATOM   1632  N   LEU A 232      27.559  35.907  23.171  1.00 29.11           N  
ANISOU 1632  N   LEU A 232     3578   3772   3709    -58     89    198       N  
ATOM   1633  CA  LEU A 232      27.461  37.119  22.381  1.00 29.61           C  
ANISOU 1633  CA  LEU A 232     3650   3826   3771    -56     90    196       C  
ATOM   1634  C   LEU A 232      26.338  36.969  21.358  1.00 29.39           C  
ANISOU 1634  C   LEU A 232     3629   3795   3740    -51     88    197       C  
ATOM   1635  O   LEU A 232      26.583  36.638  20.199  1.00 30.78           O  
ANISOU 1635  O   LEU A 232     3813   3966   3915    -52     91    200       O  
ATOM   1636  CB  LEU A 232      28.794  37.419  21.677  1.00 29.54           C  
ANISOU 1636  CB  LEU A 232     3645   3811   3766    -60     96    198       C  
ATOM   1637  CG  LEU A 232      30.017  37.828  22.507  1.00 29.37           C  
ANISOU 1637  CG  LEU A 232     3618   3790   3750    -65     97    198       C  
ATOM   1638  CD1 LEU A 232      31.270  37.745  21.643  1.00 29.92           C  
ANISOU 1638  CD1 LEU A 232     3690   3852   3826    -69    105    201       C  
ATOM   1639  CD2 LEU A 232      29.876  39.218  23.106  1.00 29.06           C  
ANISOU 1639  CD2 LEU A 232     3581   3749   3710    -65     94    193       C  
ATOM   1640  N   ARG A 233      25.105  37.189  21.798  1.00 28.57           N  
ANISOU 1640  N   ARG A 233     3524   3694   3636    -47     83    193       N  
ATOM   1641  CA  ARG A 233      23.960  37.159  20.900  1.00 28.47           C  
ANISOU 1641  CA  ARG A 233     3517   3676   3622    -42     78    194       C  
ATOM   1642  C   ARG A 233      23.362  38.539  20.814  1.00 28.98           C  
ANISOU 1642  C   ARG A 233     3585   3734   3690    -40     73    190       C  
ATOM   1643  O   ARG A 233      23.215  39.211  21.828  1.00 29.26           O  
ANISOU 1643  O   ARG A 233     3615   3772   3729    -39     73    184       O  
ATOM   1644  CB  ARG A 233      22.898  36.168  21.374  1.00 28.18           C  
ANISOU 1644  CB  ARG A 233     3474   3647   3585    -39     75    194       C  
ATOM   1645  CG  ARG A 233      23.347  34.716  21.330  1.00 28.08           C  
ANISOU 1645  CG  ARG A 233     3457   3640   3570    -41     78    198       C  
ATOM   1646  CD  ARG A 233      22.196  33.765  21.595  1.00 27.33           C  
ANISOU 1646  CD  ARG A 233     3357   3551   3476    -37     75    199       C  
ATOM   1647  NE  ARG A 233      21.198  33.830  20.539  1.00 27.28           N  
ANISOU 1647  NE  ARG A 233     3357   3537   3468    -33     70    200       N  
ATOM   1648  CZ  ARG A 233      20.016  33.225  20.585  1.00 27.73           C  
ANISOU 1648  CZ  ARG A 233     3410   3597   3527    -29     65    200       C  
ATOM   1649  NH1 ARG A 233      19.684  32.499  21.644  1.00 27.27           N  
ANISOU 1649  NH1 ARG A 233     3342   3548   3470    -29     66    199       N  
ATOM   1650  NH2 ARG A 233      19.167  33.344  19.567  1.00 27.13           N  
ANISOU 1650  NH2 ARG A 233     3342   3514   3452    -27     59    202       N  
ATOM   1651  N   GLY A 234      23.017  38.959  19.602  1.00 29.99           N  
ANISOU 1651  N   GLY A 234     3723   3852   3818    -39     69    194       N  
ATOM   1652  CA  GLY A 234      22.391  40.266  19.388  1.00 31.51           C  
ANISOU 1652  CA  GLY A 234     3919   4035   4017    -37     61    192       C  
ATOM   1653  C   GLY A 234      23.244  41.425  19.869  1.00 32.12           C  
ANISOU 1653  C   GLY A 234     3995   4108   4098    -39     64    189       C  
ATOM   1654  O   GLY A 234      22.764  42.310  20.573  1.00 33.97           O  
ANISOU 1654  O   GLY A 234     4224   4341   4340    -37     61    182       O  
ATOM   1655  N   ASN A 235      24.516  41.408  19.487  1.00 32.07           N  
ANISOU 1655  N   ASN A 235     3994   4102   4087    -45     70    193       N  
ATOM   1656  CA  ASN A 235      25.483  42.413  19.912  1.00 31.59           C  
ANISOU 1656  CA  ASN A 235     3933   4039   4030    -48     73    190       C  
ATOM   1657  C   ASN A 235      25.848  43.417  18.827  1.00 31.60           C  
ANISOU 1657  C   ASN A 235     3945   4028   4032    -52     70    195       C  
ATOM   1658  O   ASN A 235      26.199  44.548  19.127  1.00 31.49           O  
ANISOU 1658  O   ASN A 235     3931   4008   4024    -52     68    193       O  
ATOM   1659  CB  ASN A 235      26.774  41.728  20.388  1.00 31.15           C  
ANISOU 1659  CB  ASN A 235     3872   3989   3971    -53     81    191       C  
ATOM   1660  CG  ASN A 235      26.696  41.251  21.829  1.00 30.69           C  
ANISOU 1660  CG  ASN A 235     3803   3942   3913    -52     82    185       C  
ATOM   1661  OD1 ASN A 235      26.595  42.046  22.759  1.00 31.32           O  
ANISOU 1661  OD1 ASN A 235     3878   4023   3996    -51     81    179       O  
ATOM   1662  ND2 ASN A 235      26.762  39.948  22.018  1.00 30.15           N  
ANISOU 1662  ND2 ASN A 235     3730   3882   3841    -52     85    188       N  
ATOM   1663  N   PHE A 236      25.780  42.998  17.570  1.00 32.83           N  
ANISOU 1663  N   PHE A 236     4111   4179   4181    -55     69    202       N  
ATOM   1664  CA  PHE A 236      26.461  43.721  16.512  1.00 34.82           C  
ANISOU 1664  CA  PHE A 236     4375   4422   4430    -62     70    208       C  
ATOM   1665  C   PHE A 236      25.513  44.267  15.446  1.00 37.64           C  
ANISOU 1665  C   PHE A 236     4744   4770   4787    -63     58    215       C  
ATOM   1666  O   PHE A 236      24.778  43.504  14.826  1.00 39.81           O  
ANISOU 1666  O   PHE A 236     5024   5046   5057    -63     54    218       O  
ATOM   1667  CB  PHE A 236      27.550  42.830  15.916  1.00 33.06           C  
ANISOU 1667  CB  PHE A 236     4157   4204   4200    -68     82    211       C  
ATOM   1668  CG  PHE A 236      28.532  42.308  16.935  1.00 32.87           C  
ANISOU 1668  CG  PHE A 236     4121   4187   4179    -68     91    207       C  
ATOM   1669  CD1 PHE A 236      28.662  40.948  17.163  1.00 32.61           C  
ANISOU 1669  CD1 PHE A 236     4081   4162   4144    -67     96    206       C  
ATOM   1670  CD2 PHE A 236      29.334  43.177  17.670  1.00 33.56           C  
ANISOU 1670  CD2 PHE A 236     4203   4273   4273    -69     92    204       C  
ATOM   1671  CE1 PHE A 236      29.573  40.457  18.091  1.00 31.59           C  
ANISOU 1671  CE1 PHE A 236     3942   4040   4021    -68    102    203       C  
ATOM   1672  CE2 PHE A 236      30.246  42.693  18.604  1.00 33.38           C  
ANISOU 1672  CE2 PHE A 236     4170   4257   4254    -70     99    201       C  
ATOM   1673  CZ  PHE A 236      30.364  41.329  18.815  1.00 32.20           C  
ANISOU 1673  CZ  PHE A 236     4014   4115   4103    -70    103    201       C  
ATOM   1674  N   ASN A 237      25.533  45.590  15.253  1.00 40.71           N  
ANISOU 1674  N   ASN A 237     5136   5148   5182    -64     51    217       N  
ATOM   1675  CA  ASN A 237      24.623  46.292  14.324  1.00 43.15           C  
ANISOU 1675  CA  ASN A 237     5454   5444   5493    -66     36    224       C  
ATOM   1676  C   ASN A 237      24.870  45.984  12.858  1.00 42.30           C  
ANISOU 1676  C   ASN A 237     5364   5334   5372    -76     36    235       C  
ATOM   1677  O   ASN A 237      24.012  46.252  12.011  1.00 42.89           O  
ANISOU 1677  O   ASN A 237     5448   5400   5446    -79     22    242       O  
ATOM   1678  CB  ASN A 237      24.682  47.816  14.531  1.00 45.85           C  
ANISOU 1678  CB  ASN A 237     5795   5776   5848    -66     28    224       C  
ATOM   1679  CG  ASN A 237      23.483  48.356  15.296  1.00 48.88           C  
ANISOU 1679  CG  ASN A 237     6167   6154   6249    -56     18    217       C  
ATOM   1680  OD1 ASN A 237      22.330  48.160  14.896  1.00 48.49           O  
ANISOU 1680  OD1 ASN A 237     6118   6100   6203    -53      7    220       O  
ATOM   1681  ND2 ASN A 237      23.750  49.061  16.395  1.00 52.46           N  
ANISOU 1681  ND2 ASN A 237     6610   6608   6713    -52     22    208       N  
ATOM   1682  N   SER A 238      26.043  45.421  12.577  1.00 41.69           N  
ANISOU 1682  N   SER A 238     5291   5263   5284    -83     50    234       N  
ATOM   1683  CA  SER A 238      26.517  45.182  11.214  1.00 40.52           C  
ANISOU 1683  CA  SER A 238     5160   5112   5121    -95     54    242       C  
ATOM   1684  C   SER A 238      27.486  43.995  11.114  1.00 40.37           C  
ANISOU 1684  C   SER A 238     5140   5103   5093    -99     73    238       C  
ATOM   1685  O   SER A 238      28.165  43.644  12.084  1.00 40.54           O  
ANISOU 1685  O   SER A 238     5149   5131   5122    -94     83    231       O  
ATOM   1686  CB  SER A 238      27.176  46.449  10.684  1.00 39.16           C  
ANISOU 1686  CB  SER A 238     4998   4931   4950   -104     52    248       C  
ATOM   1687  OG  SER A 238      28.500  46.203  10.265  1.00 40.51           O  
ANISOU 1687  OG  SER A 238     5173   5105   5111   -113     69    248       O  
ATOM   1688  N   SER A 239      27.552  43.394   9.929  1.00 40.02           N  
ANISOU 1688  N   SER A 239     5111   5059   5035   -109     77    242       N  
ATOM   1689  CA  SER A 239      28.433  42.259   9.690  1.00 39.69           C  
ANISOU 1689  CA  SER A 239     5067   5024   4986   -114     95    236       C  
ATOM   1690  C   SER A 239      29.911  42.638   9.808  1.00 37.77           C  
ANISOU 1690  C   SER A 239     4822   4781   4747   -120    110    234       C  
ATOM   1691  O   SER A 239      30.716  41.841  10.293  1.00 34.70           O  
ANISOU 1691  O   SER A 239     4423   4398   4363   -118    124    227       O  
ATOM   1692  CB  SER A 239      28.151  41.636   8.320  1.00 42.98           C  
ANISOU 1692  CB  SER A 239     5502   5440   5386   -125     97    240       C  
ATOM   1693  OG  SER A 239      28.737  42.401   7.274  1.00 47.42           O  
ANISOU 1693  OG  SER A 239     6082   5997   5938   -139    100    246       O  
ATOM   1694  N   ASN A 240      30.266  43.844   9.358  1.00 38.08           N  
ANISOU 1694  N   ASN A 240     4871   4813   4784   -127    107    240       N  
ATOM   1695  CA  ASN A 240      31.646  44.325   9.514  1.00 38.68           C  
ANISOU 1695  CA  ASN A 240     4943   4887   4865   -132    121    237       C  
ATOM   1696  C   ASN A 240      32.017  44.543  10.976  1.00 37.33           C  
ANISOU 1696  C   ASN A 240     4753   4719   4711   -121    120    232       C  
ATOM   1697  O   ASN A 240      33.127  44.196  11.404  1.00 37.70           O  
ANISOU 1697  O   ASN A 240     4791   4769   4765   -122    134    227       O  
ATOM   1698  CB  ASN A 240      31.922  45.599   8.711  1.00 39.79           C  
ANISOU 1698  CB  ASN A 240     5098   5018   5000   -143    117    246       C  
ATOM   1699  CG  ASN A 240      33.396  45.999   8.746  1.00 41.58           C  
ANISOU 1699  CG  ASN A 240     5321   5243   5231   -150    132    244       C  
ATOM   1700  OD1 ASN A 240      34.252  45.306   8.195  1.00 43.00           O  
ANISOU 1700  OD1 ASN A 240     5505   5426   5406   -158    151    240       O  
ATOM   1701  ND2 ASN A 240      33.695  47.116   9.405  1.00 41.48           N  
ANISOU 1701  ND2 ASN A 240     5302   5225   5230   -146    126    245       N  
ATOM   1702  N   ILE A 241      31.083  45.114  11.732  1.00 36.20           N  
ANISOU 1702  N   ILE A 241     4604   4574   4575   -111    105    232       N  
ATOM   1703  CA  ILE A 241      31.261  45.319  13.160  1.00 35.90           C  
ANISOU 1703  CA  ILE A 241     4549   4540   4551   -102    103    226       C  
ATOM   1704  C   ILE A 241      31.516  43.995  13.865  1.00 36.98           C  
ANISOU 1704  C   ILE A 241     4673   4686   4689    -97    112    220       C  
ATOM   1705  O   ILE A 241      32.380  43.901  14.739  1.00 37.44           O  
ANISOU 1705  O   ILE A 241     4720   4748   4756    -95    118    215       O  
ATOM   1706  CB  ILE A 241      30.052  46.024  13.783  1.00 35.59           C  
ANISOU 1706  CB  ILE A 241     4506   4498   4518    -93     87    225       C  
ATOM   1707  CG1 ILE A 241      29.953  47.453  13.210  1.00 34.67           C  
ANISOU 1707  CG1 ILE A 241     4399   4369   4403    -98     78    232       C  
ATOM   1708  CG2 ILE A 241      30.141  45.981  15.312  1.00 35.04           C  
ANISOU 1708  CG2 ILE A 241     4419   4434   4458    -84     87    217       C  
ATOM   1709  CD1 ILE A 241      28.878  48.337  13.809  1.00 33.28           C  
ANISOU 1709  CD1 ILE A 241     4218   4188   4239    -89     62    230       C  
ATOM   1710  N   MET A 242      30.791  42.959  13.465  1.00 36.62           N  
ANISOU 1710  N   MET A 242     4630   4645   4636    -95    111    220       N  
ATOM   1711  CA  MET A 242      31.032  41.647  14.037  1.00 37.18           C  
ANISOU 1711  CA  MET A 242     4690   4724   4711    -92    119    215       C  
ATOM   1712  C   MET A 242      32.424  41.095  13.692  1.00 37.70           C  
ANISOU 1712  C   MET A 242     4753   4790   4778    -99    135    213       C  
ATOM   1713  O   MET A 242      33.157  40.658  14.588  1.00 38.38           O  
ANISOU 1713  O   MET A 242     4827   4880   4876    -97    140    209       O  
ATOM   1714  CB  MET A 242      29.938  40.668  13.648  1.00 36.79           C  
ANISOU 1714  CB  MET A 242     4644   4678   4654    -89    114    215       C  
ATOM   1715  CG  MET A 242      30.033  39.362  14.398  1.00 38.24           C  
ANISOU 1715  CG  MET A 242     4815   4871   4844    -84    119    211       C  
ATOM   1716  SD  MET A 242      28.712  38.256  13.916  1.00 40.40           S  
ANISOU 1716  SD  MET A 242     5092   5148   5110    -80    113    212       S  
ATOM   1717  CE  MET A 242      29.174  36.795  14.835  1.00 42.16           C  
ANISOU 1717  CE  MET A 242     5298   5379   5341    -77    120    208       C  
ATOM   1718  N   LYS A 243      32.784  41.131  12.408  1.00 37.58           N  
ANISOU 1718  N   LYS A 243     4752   4770   4754   -109    144    215       N  
ATOM   1719  CA  LYS A 243      34.065  40.607  11.930  1.00 37.98           C  
ANISOU 1719  CA  LYS A 243     4801   4820   4809   -117    162    211       C  
ATOM   1720  C   LYS A 243      35.171  41.285  12.704  1.00 38.23           C  
ANISOU 1720  C   LYS A 243     4822   4848   4853   -117    166    210       C  
ATOM   1721  O   LYS A 243      36.123  40.657  13.177  1.00 37.88           O  
ANISOU 1721  O   LYS A 243     4765   4805   4821   -117    175    206       O  
ATOM   1722  CB  LYS A 243      34.220  40.886  10.430  1.00 38.82           C  
ANISOU 1722  CB  LYS A 243     4927   4921   4901   -130    170    214       C  
ATOM   1723  CG  LYS A 243      35.568  40.543   9.801  1.00 38.93           C  
ANISOU 1723  CG  LYS A 243     4941   4933   4917   -141    191    209       C  
ATOM   1724  CD  LYS A 243      35.464  40.712   8.288  1.00 41.35           C  
ANISOU 1724  CD  LYS A 243     5269   5237   5205   -155    198    211       C  
ATOM   1725  CE  LYS A 243      36.809  40.818   7.582  1.00 41.78           C  
ANISOU 1725  CE  LYS A 243     5326   5287   5261   -168    220    207       C  
ATOM   1726  NZ  LYS A 243      37.434  39.488   7.331  1.00 43.58           N  
ANISOU 1726  NZ  LYS A 243     5546   5517   5495   -171    239    197       N  
ATOM   1727  N   THR A 244      34.997  42.582  12.867  1.00 38.97           N  
ANISOU 1727  N   THR A 244     4920   4938   4946   -117    156    214       N  
ATOM   1728  CA  THR A 244      36.039  43.416  13.413  1.00 40.34           C  
ANISOU 1728  CA  THR A 244     5087   5107   5130   -118    159    214       C  
ATOM   1729  C   THR A 244      36.143  43.306  14.951  1.00 40.22           C  
ANISOU 1729  C   THR A 244     5056   5098   5128   -109    152    211       C  
ATOM   1730  O   THR A 244      37.213  43.508  15.530  1.00 40.38           O  
ANISOU 1730  O   THR A 244     5066   5116   5160   -111    157    209       O  
ATOM   1731  CB  THR A 244      35.872  44.856  12.874  1.00 39.22           C  
ANISOU 1731  CB  THR A 244     4958   4959   4984   -123    153    220       C  
ATOM   1732  OG1 THR A 244      37.140  45.502  12.839  1.00 40.08           O  
ANISOU 1732  OG1 THR A 244     5065   5063   5101   -130    162    220       O  
ATOM   1733  CG2 THR A 244      34.890  45.661  13.695  1.00 39.25           C  
ANISOU 1733  CG2 THR A 244     4959   4962   4990   -114    135    221       C  
ATOM   1734  N   CYS A 245      35.035  42.954  15.597  1.00 40.40           N  
ANISOU 1734  N   CYS A 245     5075   5126   5148   -101    141    210       N  
ATOM   1735  CA  CYS A 245      35.031  42.711  17.034  1.00 39.59           C  
ANISOU 1735  CA  CYS A 245     4958   5030   5054    -95    135    206       C  
ATOM   1736  C   CYS A 245      35.489  41.301  17.371  1.00 38.27           C  
ANISOU 1736  C   CYS A 245     4779   4867   4892    -94    141    205       C  
ATOM   1737  O   CYS A 245      36.137  41.095  18.393  1.00 39.27           O  
ANISOU 1737  O   CYS A 245     4893   4996   5029    -93    140    204       O  
ATOM   1738  CB  CYS A 245      33.646  42.953  17.626  1.00 41.69           C  
ANISOU 1738  CB  CYS A 245     5225   5300   5315    -87    122    205       C  
ATOM   1739  SG  CYS A 245      33.201  44.695  17.768  1.00 42.41           S  
ANISOU 1739  SG  CYS A 245     5321   5384   5407    -85    112    205       S  
ATOM   1740  N   LEU A 246      35.156  40.328  16.526  1.00 36.10           N  
ANISOU 1740  N   LEU A 246     4509   4594   4612    -95    147    205       N  
ATOM   1741  CA  LEU A 246      35.584  38.955  16.784  1.00 35.61           C  
ANISOU 1741  CA  LEU A 246     4435   4534   4558    -95    153    203       C  
ATOM   1742  C   LEU A 246      37.106  38.817  16.705  1.00 36.12           C  
ANISOU 1742  C   LEU A 246     4492   4594   4637   -101    165    201       C  
ATOM   1743  O   LEU A 246      37.692  37.951  17.360  1.00 36.68           O  
ANISOU 1743  O   LEU A 246     4549   4666   4721   -100    166    201       O  
ATOM   1744  CB  LEU A 246      34.896  37.954  15.848  1.00 34.09           C  
ANISOU 1744  CB  LEU A 246     4249   4344   4357    -95    157    202       C  
ATOM   1745  CG  LEU A 246      33.377  37.762  15.953  1.00 33.62           C  
ANISOU 1745  CG  LEU A 246     4195   4290   4287    -89    146    203       C  
ATOM   1746  CD1 LEU A 246      32.913  36.640  15.040  1.00 33.46           C  
ANISOU 1746  CD1 LEU A 246     4180   4271   4261    -90    151    202       C  
ATOM   1747  CD2 LEU A 246      32.927  37.502  17.379  1.00 33.24           C  
ANISOU 1747  CD2 LEU A 246     4135   4249   4244    -82    135    203       C  
ATOM   1748  N   GLN A 247      37.732  39.680  15.909  1.00 35.85           N  
ANISOU 1748  N   GLN A 247     4466   4552   4601   -108    173    201       N  
ATOM   1749  CA  GLN A 247      39.172  39.662  15.715  1.00 35.37           C  
ANISOU 1749  CA  GLN A 247     4398   4485   4555   -114    186    200       C  
ATOM   1750  C   GLN A 247      39.907  40.028  16.977  1.00 36.35           C  
ANISOU 1750  C   GLN A 247     4508   4609   4694   -112    179    201       C  
ATOM   1751  O   GLN A 247      41.039  39.591  17.183  1.00 37.03           O  
ANISOU 1751  O   GLN A 247     4582   4690   4797   -116    186    200       O  
ATOM   1752  CB  GLN A 247      39.587  40.596  14.583  1.00 35.95           C  
ANISOU 1752  CB  GLN A 247     4485   4552   4621   -123    196    200       C  
ATOM   1753  CG  GLN A 247      39.473  39.937  13.222  1.00 38.29           C  
ANISOU 1753  CG  GLN A 247     4793   4848   4908   -130    210    197       C  
ATOM   1754  CD  GLN A 247      39.517  40.912  12.071  1.00 40.02           C  
ANISOU 1754  CD  GLN A 247     5029   5062   5113   -139    217    199       C  
ATOM   1755  OE1 GLN A 247      39.685  40.512  10.921  1.00 40.56           O  
ANISOU 1755  OE1 GLN A 247     5107   5129   5173   -149    231    196       O  
ATOM   1756  NE2 GLN A 247      39.357  42.197  12.368  1.00 43.50           N  
ANISOU 1756  NE2 GLN A 247     5475   5501   5551   -138    206    205       N  
ATOM   1757  N   ASN A 248      39.266  40.820  17.831  1.00 36.02           N  
ANISOU 1757  N   ASN A 248     4468   4570   4645   -107    165    203       N  
ATOM   1758  CA  ASN A 248      39.915  41.245  19.060  1.00 35.60           C  
ANISOU 1758  CA  ASN A 248     4403   4517   4603   -107    157    204       C  
ATOM   1759  C   ASN A 248      39.569  40.395  20.274  1.00 36.00           C  
ANISOU 1759  C   ASN A 248     4444   4576   4658   -103    146    205       C  
ATOM   1760  O   ASN A 248      39.921  40.713  21.414  1.00 36.54           O  
ANISOU 1760  O   ASN A 248     4505   4646   4733   -103    137    206       O  
ATOM   1761  CB  ASN A 248      39.713  42.732  19.277  1.00 35.66           C  
ANISOU 1761  CB  ASN A 248     4419   4522   4605   -106    150    204       C  
ATOM   1762  CG  ASN A 248      40.648  43.563  18.419  1.00 36.39           C  
ANISOU 1762  CG  ASN A 248     4516   4605   4702   -113    160    205       C  
ATOM   1763  OD1 ASN A 248      41.756  43.138  18.107  1.00 36.25           O  
ANISOU 1763  OD1 ASN A 248     4492   4583   4697   -118    171    205       O  
ATOM   1764  ND2 ASN A 248      40.211  44.750  18.041  1.00 37.13           N  
ANISOU 1764  ND2 ASN A 248     4622   4696   4788   -114    156    206       N  
ATOM   1765  N   LEU A 249      38.898  39.285  19.987  1.00 35.58           N  
ANISOU 1765  N   LEU A 249     4390   4527   4601   -100    147    204       N  
ATOM   1766  CA  LEU A 249      38.783  38.161  20.900  1.00 34.83           C  
ANISOU 1766  CA  LEU A 249     4283   4438   4512    -98    140    206       C  
ATOM   1767  C   LEU A 249      40.080  37.340  20.937  1.00 35.30           C  
ANISOU 1767  C   LEU A 249     4328   4490   4592   -102    146    207       C  
ATOM   1768  O   LEU A 249      40.207  36.438  21.760  1.00 36.39           O  
ANISOU 1768  O   LEU A 249     4454   4631   4739   -102    138    210       O  
ATOM   1769  CB  LEU A 249      37.619  37.263  20.472  1.00 33.12           C  
ANISOU 1769  CB  LEU A 249     4071   4227   4284    -93    140    205       C  
ATOM   1770  CG  LEU A 249      36.275  37.247  21.200  1.00 31.77           C  
ANISOU 1770  CG  LEU A 249     3904   4066   4101    -88    128    206       C  
ATOM   1771  CD1 LEU A 249      35.884  38.568  21.834  1.00 31.19           C  
ANISOU 1771  CD1 LEU A 249     3836   3995   4020    -87    120    205       C  
ATOM   1772  CD2 LEU A 249      35.204  36.769  20.240  1.00 31.85           C  
ANISOU 1772  CD2 LEU A 249     3923   4078   4101    -84    131    205       C  
ATOM   1773  N   ALA A 250      41.027  37.641  20.043  1.00 35.60           N  
ANISOU 1773  N   ALA A 250     4366   4519   4639   -107    159    205       N  
ATOM   1774  CA  ALA A 250      42.350  36.967  20.010  1.00 35.84           C  
ANISOU 1774  CA  ALA A 250     4381   4540   4693   -111    167    204       C  
ATOM   1775  C   ALA A 250      42.923  36.761  21.407  1.00 35.65           C  
ANISOU 1775  C   ALA A 250     4343   4517   4685   -112    152    210       C  
ATOM   1776  O   ALA A 250      42.916  37.683  22.224  1.00 38.89           O  
ANISOU 1776  O   ALA A 250     4756   4930   5090   -113    142    212       O  
ATOM   1777  CB  ALA A 250      43.342  37.746  19.155  1.00 33.26           C  
ANISOU 1777  CB  ALA A 250     4057   4204   4373   -117    182    201       C  
ATOM   1778  N   GLY A 251      43.399  35.552  21.678  1.00 34.57           N  
ANISOU 1778  N   GLY A 251     4191   4376   4566   -113    151    212       N  
ATOM   1779  CA  GLY A 251      43.926  35.210  22.993  1.00 35.23           C  
ANISOU 1779  CA  GLY A 251     4260   4459   4664   -116    135    219       C  
ATOM   1780  C   GLY A 251      42.971  34.427  23.874  1.00 35.84           C  
ANISOU 1780  C   GLY A 251     4337   4547   4732   -113    120    223       C  
ATOM   1781  O   GLY A 251      43.393  33.575  24.637  1.00 37.32           O  
ANISOU 1781  O   GLY A 251     4510   4732   4935   -116    109    230       O  
ATOM   1782  N   LEU A 252      41.681  34.716  23.766  1.00 36.16           N  
ANISOU 1782  N   LEU A 252     4391   4598   4748   -109    119    221       N  
ATOM   1783  CA  LEU A 252      40.661  34.089  24.590  1.00 35.85           C  
ANISOU 1783  CA  LEU A 252     4352   4570   4697   -107    106    225       C  
ATOM   1784  C   LEU A 252      40.744  32.566  24.571  1.00 36.90           C  
ANISOU 1784  C   LEU A 252     4473   4701   4845   -107    104    229       C  
ATOM   1785  O   LEU A 252      40.971  31.952  23.530  1.00 37.45           O  
ANISOU 1785  O   LEU A 252     4539   4763   4924   -105    117    224       O  
ATOM   1786  CB  LEU A 252      39.281  34.558  24.127  1.00 34.97           C  
ANISOU 1786  CB  LEU A 252     4256   4467   4561   -101    109    221       C  
ATOM   1787  CG  LEU A 252      37.955  34.018  24.660  1.00 34.72           C  
ANISOU 1787  CG  LEU A 252     4229   4447   4515    -97    101    222       C  
ATOM   1788  CD1 LEU A 252      37.831  34.120  26.174  1.00 35.33           C  
ANISOU 1788  CD1 LEU A 252     4303   4533   4588   -102     86    227       C  
ATOM   1789  CD2 LEU A 252      36.827  34.787  23.992  1.00 34.65           C  
ANISOU 1789  CD2 LEU A 252     4235   4443   4487    -92    106    216       C  
ATOM   1790  N   HIS A 253      40.580  31.974  25.748  1.00 38.55           N  
ANISOU 1790  N   HIS A 253     4674   4915   5055   -110     88    236       N  
ATOM   1791  CA  HIS A 253      40.368  30.539  25.888  1.00 39.21           C  
ANISOU 1791  CA  HIS A 253     4748   4999   5150   -109     83    241       C  
ATOM   1792  C   HIS A 253      38.973  30.380  26.438  1.00 36.29           C  
ANISOU 1792  C   HIS A 253     4387   4643   4756   -107     75    243       C  
ATOM   1793  O   HIS A 253      38.713  30.728  27.592  1.00 35.55           O  
ANISOU 1793  O   HIS A 253     4295   4558   4652   -112     62    247       O  
ATOM   1794  CB  HIS A 253      41.433  29.937  26.812  1.00 43.65           C  
ANISOU 1794  CB  HIS A 253     5293   5554   5736   -117     69    250       C  
ATOM   1795  CG  HIS A 253      41.270  28.450  27.076  1.00 49.15           C  
ANISOU 1795  CG  HIS A 253     5977   6249   6446   -118     61    257       C  
ATOM   1796  ND1 HIS A 253      42.016  27.515  26.451  1.00 52.04           N  
ANISOU 1796  ND1 HIS A 253     6328   6602   6840   -117     67    256       N  
ATOM   1797  CD2 HIS A 253      40.434  27.757  27.959  1.00 52.93           C  
ANISOU 1797  CD2 HIS A 253     6456   6739   6915   -120     46    265       C  
ATOM   1798  CE1 HIS A 253      41.670  26.287  26.895  1.00 52.16           C  
ANISOU 1798  CE1 HIS A 253     6335   6619   6864   -118     56    264       C  
ATOM   1799  NE2 HIS A 253      40.700  26.436  27.816  1.00 55.22           N  
ANISOU 1799  NE2 HIS A 253     6731   7020   7227   -120     43    270       N  
ATOM   1800  N   VAL A 254      38.055  29.903  25.598  1.00 32.46           N  
ANISOU 1800  N   VAL A 254     3908   4161   4263   -101     84    238       N  
ATOM   1801  CA  VAL A 254      36.679  29.637  26.014  1.00 31.75           C  
ANISOU 1801  CA  VAL A 254     3825   4083   4154    -98     77    239       C  
ATOM   1802  C   VAL A 254      36.298  28.181  25.863  1.00 30.63           C  
ANISOU 1802  C   VAL A 254     3674   3941   4020    -97     75    243       C  
ATOM   1803  O   VAL A 254      36.605  27.540  24.856  1.00 30.75           O  
ANISOU 1803  O   VAL A 254     3686   3949   4049    -94     85    239       O  
ATOM   1804  CB  VAL A 254      35.611  30.452  25.230  1.00 32.60           C  
ANISOU 1804  CB  VAL A 254     3948   4196   4241    -92     86    231       C  
ATOM   1805  CG1 VAL A 254      34.892  31.433  26.142  1.00 33.40           C  
ANISOU 1805  CG1 VAL A 254     4058   4307   4324    -93     79    230       C  
ATOM   1806  CG2 VAL A 254      36.182  31.118  23.986  1.00 32.45           C  
ANISOU 1806  CG2 VAL A 254     3936   4168   4226    -90    101    225       C  
ATOM   1807  N   HIS A 255      35.592  27.670  26.855  1.00 30.35           N  
ANISOU 1807  N   HIS A 255     3637   3915   3976    -99     62    250       N  
ATOM   1808  CA  HIS A 255      35.041  26.335  26.750  1.00 31.74           C  
ANISOU 1808  CA  HIS A 255     3806   4092   4158    -98     59    253       C  
ATOM   1809  C   HIS A 255      33.798  26.371  25.905  1.00 30.57           C  
ANISOU 1809  C   HIS A 255     3670   3950   3995    -90     68    246       C  
ATOM   1810  O   HIS A 255      33.573  25.476  25.102  1.00 31.20           O  
ANISOU 1810  O   HIS A 255     3747   4025   4082    -86     73    245       O  
ATOM   1811  CB  HIS A 255      34.788  25.721  28.136  1.00 33.10           C  
ANISOU 1811  CB  HIS A 255     3973   4274   4330   -105     41    265       C  
ATOM   1812  CG  HIS A 255      34.146  24.352  28.092  1.00 34.71           C  
ANISOU 1812  CG  HIS A 255     4170   4478   4538   -103     37    270       C  
ATOM   1813  ND1 HIS A 255      32.855  24.144  28.434  1.00 36.53           N  
ANISOU 1813  ND1 HIS A 255     4406   4720   4750   -102     34    270       N  
ATOM   1814  CD2 HIS A 255      34.651  23.115  27.706  1.00 35.32           C  
ANISOU 1814  CD2 HIS A 255     4233   4545   4639   -103     35    273       C  
ATOM   1815  CE1 HIS A 255      32.554  22.837  28.284  1.00 36.05           C  
ANISOU 1815  CE1 HIS A 255     4337   4658   4701   -101     30    275       C  
ATOM   1816  NE2 HIS A 255      33.651  22.210  27.836  1.00 35.78           N  
ANISOU 1816  NE2 HIS A 255     4291   4611   4693   -102     30    277       N  
ATOM   1817  N   ARG A 256      32.983  27.406  26.052  1.00 29.93           N  
ANISOU 1817  N   ARG A 256     3602   3877   3893    -88     69    242       N  
ATOM   1818  CA  ARG A 256      31.758  27.476  25.275  1.00 30.55           C  
ANISOU 1818  CA  ARG A 256     3690   3959   3958    -80     75    236       C  
ATOM   1819  C   ARG A 256      31.495  28.873  24.737  1.00 30.61           C  
ANISOU 1819  C   ARG A 256     3710   3966   3952    -77     83    229       C  
ATOM   1820  O   ARG A 256      31.310  29.809  25.510  1.00 30.96           O  
ANISOU 1820  O   ARG A 256     3758   4015   3987    -79     79    228       O  
ATOM   1821  CB  ARG A 256      30.565  26.981  26.088  1.00 30.88           C  
ANISOU 1821  CB  ARG A 256     3732   4012   3989    -81     67    240       C  
ATOM   1822  CG  ARG A 256      29.362  26.654  25.225  1.00 32.93           C  
ANISOU 1822  CG  ARG A 256     3998   4273   4241    -73     71    236       C  
ATOM   1823  CD  ARG A 256      28.252  25.930  25.978  1.00 34.95           C  
ANISOU 1823  CD  ARG A 256     4250   4539   4489    -74     63    240       C  
ATOM   1824  NE  ARG A 256      28.767  24.833  26.798  1.00 37.04           N  
ANISOU 1824  NE  ARG A 256     4503   4805   4766    -80     54    250       N  
ATOM   1825  CZ  ARG A 256      28.669  24.777  28.127  1.00 36.71           C  
ANISOU 1825  CZ  ARG A 256     4457   4772   4718    -88     44    256       C  
ATOM   1826  NH1 ARG A 256      28.049  25.747  28.798  1.00 35.06           N  
ANISOU 1826  NH1 ARG A 256     4257   4572   4492    -89     45    252       N  
ATOM   1827  NH2 ARG A 256      29.179  23.741  28.779  1.00 35.95           N  
ANISOU 1827  NH2 ARG A 256     4350   4675   4633    -94     34    267       N  
ATOM   1828  N   LEU A 257      31.488  29.011  23.409  1.00 29.60           N  
ANISOU 1828  N   LEU A 257     3590   3832   3825    -73     93    224       N  
ATOM   1829  CA  LEU A 257      31.143  30.287  22.793  1.00 28.85           C  
ANISOU 1829  CA  LEU A 257     3507   3734   3717    -71     98    218       C  
ATOM   1830  C   LEU A 257      29.805  30.188  22.076  1.00 28.66           C  
ANISOU 1830  C   LEU A 257     3493   3713   3683    -65     99    215       C  
ATOM   1831  O   LEU A 257      29.616  29.333  21.210  1.00 27.98           O  
ANISOU 1831  O   LEU A 257     3407   3624   3599    -64    103    215       O  
ATOM   1832  CB  LEU A 257      32.242  30.754  21.834  1.00 28.84           C  
ANISOU 1832  CB  LEU A 257     3509   3723   3724    -73    109    215       C  
ATOM   1833  CG  LEU A 257      32.197  32.178  21.251  1.00 28.21           C  
ANISOU 1833  CG  LEU A 257     3443   3641   3635    -72    114    211       C  
ATOM   1834  CD1 LEU A 257      32.336  33.252  22.313  1.00 26.79           C  
ANISOU 1834  CD1 LEU A 257     3262   3464   3452    -74    107    211       C  
ATOM   1835  CD2 LEU A 257      33.281  32.328  20.202  1.00 27.48           C  
ANISOU 1835  CD2 LEU A 257     3353   3539   3550    -76    126    208       C  
ATOM   1836  N   ILE A 258      28.884  31.065  22.463  1.00 28.21           N  
ANISOU 1836  N   ILE A 258     3442   3661   3615    -62     94    213       N  
ATOM   1837  CA  ILE A 258      27.553  31.138  21.857  1.00 28.93           C  
ANISOU 1837  CA  ILE A 258     3541   3753   3696    -57     93    211       C  
ATOM   1838  C   ILE A 258      27.387  32.447  21.067  1.00 28.71           C  
ANISOU 1838  C   ILE A 258     3525   3719   3662    -56     96    208       C  
ATOM   1839  O   ILE A 258      27.483  33.544  21.625  1.00 27.72           O  
ANISOU 1839  O   ILE A 258     3400   3594   3535    -56     94    205       O  
ATOM   1840  CB  ILE A 258      26.440  30.996  22.920  1.00 28.76           C  
ANISOU 1840  CB  ILE A 258     3515   3741   3670    -55     86    211       C  
ATOM   1841  CG1 ILE A 258      26.604  29.681  23.687  1.00 28.19           C  
ANISOU 1841  CG1 ILE A 258     3431   3675   3603    -58     82    217       C  
ATOM   1842  CG2 ILE A 258      25.070  31.072  22.265  1.00 28.26           C  
ANISOU 1842  CG2 ILE A 258     3458   3677   3600    -49     84    209       C  
ATOM   1843  CD1 ILE A 258      26.236  29.776  25.149  1.00 29.13           C  
ANISOU 1843  CD1 ILE A 258     3545   3803   3717    -61     76    218       C  
ATOM   1844  N   LEU A 259      27.116  32.297  19.771  1.00 29.62           N  
ANISOU 1844  N   LEU A 259     3650   3829   3775    -55     99    207       N  
ATOM   1845  CA  LEU A 259      27.184  33.376  18.790  1.00 29.78           C  
ANISOU 1845  CA  LEU A 259     3682   3841   3790    -56    102    206       C  
ATOM   1846  C   LEU A 259      25.876  33.455  18.004  1.00 29.99           C  
ANISOU 1846  C   LEU A 259     3718   3866   3809    -52     96    206       C  
ATOM   1847  O   LEU A 259      25.297  32.423  17.662  1.00 30.89           O  
ANISOU 1847  O   LEU A 259     3832   3982   3922    -51     95    207       O  
ATOM   1848  CB  LEU A 259      28.326  33.058  17.833  1.00 30.13           C  
ANISOU 1848  CB  LEU A 259     3731   3880   3837    -62    112    205       C  
ATOM   1849  CG  LEU A 259      29.341  34.139  17.497  1.00 31.57           C  
ANISOU 1849  CG  LEU A 259     3918   4056   4020    -66    118    205       C  
ATOM   1850  CD1 LEU A 259      29.934  34.747  18.761  1.00 32.12           C  
ANISOU 1850  CD1 LEU A 259     3978   4128   4096    -66    115    205       C  
ATOM   1851  CD2 LEU A 259      30.443  33.558  16.620  1.00 31.69           C  
ANISOU 1851  CD2 LEU A 259     3934   4066   4040    -73    131    203       C  
ATOM   1852  N   GLY A 260      25.401  34.666  17.721  1.00 29.65           N  
ANISOU 1852  N   GLY A 260     3683   3818   3762    -51     91    206       N  
ATOM   1853  CA  GLY A 260      24.200  34.828  16.900  1.00 29.40           C  
ANISOU 1853  CA  GLY A 260     3661   3783   3727    -49     84    208       C  
ATOM   1854  C   GLY A 260      23.336  36.030  17.216  1.00 29.69           C  
ANISOU 1854  C   GLY A 260     3699   3816   3766    -45     75    207       C  
ATOM   1855  O   GLY A 260      23.754  36.928  17.928  1.00 29.58           O  
ANISOU 1855  O   GLY A 260     3681   3802   3756    -45     76    204       O  
ATOM   1856  N   GLU A 261      22.124  36.044  16.671  1.00 30.89           N  
ANISOU 1856  N   GLU A 261     3855   3964   3916    -42     66    208       N  
ATOM   1857  CA  GLU A 261      21.174  37.137  16.904  1.00 31.28           C  
ANISOU 1857  CA  GLU A 261     3904   4008   3972    -38     56    207       C  
ATOM   1858  C   GLU A 261      19.758  36.606  17.174  1.00 30.65           C  
ANISOU 1858  C   GLU A 261     3818   3930   3897    -32     49    206       C  
ATOM   1859  O   GLU A 261      19.590  35.427  17.482  1.00 30.01           O  
ANISOU 1859  O   GLU A 261     3731   3856   3814    -30     52    206       O  
ATOM   1860  CB  GLU A 261      21.207  38.154  15.754  1.00 32.55           C  
ANISOU 1860  CB  GLU A 261     4079   4157   4131    -42     50    212       C  
ATOM   1861  CG  GLU A 261      21.339  37.534  14.374  1.00 34.07           C  
ANISOU 1861  CG  GLU A 261     4285   4346   4313    -48     50    218       C  
ATOM   1862  CD  GLU A 261      21.557  38.556  13.269  1.00 36.21           C  
ANISOU 1862  CD  GLU A 261     4571   4606   4579    -56     45    224       C  
ATOM   1863  OE1 GLU A 261      21.156  38.274  12.114  1.00 37.84           O  
ANISOU 1863  OE1 GLU A 261     4791   4808   4778    -61     39    229       O  
ATOM   1864  OE2 GLU A 261      22.124  39.636  13.537  1.00 35.70           O  
ANISOU 1864  OE2 GLU A 261     4507   4539   4519    -57     46    223       O  
ATOM   1865  N   PHE A 262      18.754  37.479  17.089  1.00 30.84           N  
ANISOU 1865  N   PHE A 262     3841   3945   3929    -28     39    205       N  
ATOM   1866  CA  PHE A 262      17.386  37.136  17.474  1.00 30.11           C  
ANISOU 1866  CA  PHE A 262     3741   3854   3845    -22     33    203       C  
ATOM   1867  C   PHE A 262      16.424  37.536  16.389  1.00 30.81           C  
ANISOU 1867  C   PHE A 262     3838   3930   3939    -21     19    209       C  
ATOM   1868  O   PHE A 262      16.691  38.470  15.653  1.00 32.18           O  
ANISOU 1868  O   PHE A 262     4020   4093   4112    -25     13    213       O  
ATOM   1869  CB  PHE A 262      16.999  37.857  18.757  1.00 29.57           C  
ANISOU 1869  CB  PHE A 262     3660   3788   3787    -18     35    194       C  
ATOM   1870  CG  PHE A 262      17.819  37.461  19.953  1.00 29.19           C  
ANISOU 1870  CG  PHE A 262     3604   3752   3733    -20     47    189       C  
ATOM   1871  CD1 PHE A 262      18.894  38.242  20.362  1.00 28.71           C  
ANISOU 1871  CD1 PHE A 262     3545   3692   3671    -23     52    186       C  
ATOM   1872  CD2 PHE A 262      17.514  36.312  20.675  1.00 28.56           C  
ANISOU 1872  CD2 PHE A 262     3515   3683   3651    -19     51    188       C  
ATOM   1873  CE1 PHE A 262      19.646  37.880  21.470  1.00 28.75           C  
ANISOU 1873  CE1 PHE A 262     3543   3708   3672    -26     61    183       C  
ATOM   1874  CE2 PHE A 262      18.261  35.949  21.784  1.00 28.06           C  
ANISOU 1874  CE2 PHE A 262     3446   3632   3583    -22     59    185       C  
ATOM   1875  CZ  PHE A 262      19.329  36.734  22.182  1.00 28.05           C  
ANISOU 1875  CZ  PHE A 262     3447   3630   3580    -26     63    182       C  
ATOM   1876  N   LYS A 263      15.300  36.835  16.296  1.00 32.47           N  
ANISOU 1876  N   LYS A 263     4043   4140   4153    -17     12    210       N  
ATOM   1877  CA  LYS A 263      14.287  37.123  15.288  1.00 34.65           C  
ANISOU 1877  CA  LYS A 263     4326   4404   4436    -17     -2    216       C  
ATOM   1878  C   LYS A 263      13.798  38.546  15.423  1.00 35.27           C  
ANISOU 1878  C   LYS A 263     4400   4469   4529    -14    -11    214       C  
ATOM   1879  O   LYS A 263      13.600  39.252  14.428  1.00 35.43           O  
ANISOU 1879  O   LYS A 263     4432   4478   4552    -18    -24    221       O  
ATOM   1880  CB  LYS A 263      13.102  36.166  15.419  1.00 36.05           C  
ANISOU 1880  CB  LYS A 263     4495   4583   4619    -12     -7    216       C  
ATOM   1881  CG  LYS A 263      13.325  34.816  14.758  1.00 37.89           C  
ANISOU 1881  CG  LYS A 263     4735   4821   4838    -15     -5    221       C  
ATOM   1882  CD  LYS A 263      12.899  34.815  13.303  1.00 37.00           C  
ANISOU 1882  CD  LYS A 263     4637   4698   4721    -20    -20    230       C  
ATOM   1883  CE  LYS A 263      12.907  33.387  12.786  1.00 38.94           C  
ANISOU 1883  CE  LYS A 263     4888   4950   4956    -23    -17    232       C  
ATOM   1884  NZ  LYS A 263      11.710  33.052  11.961  1.00 39.16           N  
ANISOU 1884  NZ  LYS A 263     4920   4969   4988    -23    -34    238       N  
ATOM   1885  N   ASP A 264      13.629  38.954  16.673  1.00 36.07           N  
ANISOU 1885  N   ASP A 264     4488   4575   4641     -9     -3    204       N  
ATOM   1886  CA  ASP A 264      13.100  40.262  17.013  1.00 38.91           C  
ANISOU 1886  CA  ASP A 264     4840   4923   5019     -6     -9    199       C  
ATOM   1887  C   ASP A 264      14.183  41.320  17.229  1.00 39.97           C  
ANISOU 1887  C   ASP A 264     4979   5057   5151     -9     -4    196       C  
ATOM   1888  O   ASP A 264      13.897  42.390  17.751  1.00 41.09           O  
ANISOU 1888  O   ASP A 264     5113   5191   5308     -6     -6    189       O  
ATOM   1889  CB  ASP A 264      12.218  40.144  18.260  1.00 40.23           C  
ANISOU 1889  CB  ASP A 264     4989   5095   5199      0     -3    187       C  
ATOM   1890  CG  ASP A 264      12.877  39.354  19.383  1.00 39.60           C  
ANISOU 1890  CG  ASP A 264     4904   5034   5107      0     13    180       C  
ATOM   1891  OD1 ASP A 264      12.513  39.589  20.553  1.00 41.23           O  
ANISOU 1891  OD1 ASP A 264     5097   5245   5321      1     21    169       O  
ATOM   1892  OD2 ASP A 264      13.740  38.495  19.105  1.00 38.06           O  
ANISOU 1892  OD2 ASP A 264     4717   4848   4896     -5     18    186       O  
ATOM   1893  N   GLU A 265      15.411  41.019  16.804  1.00 41.74           N  
ANISOU 1893  N   GLU A 265     5213   5286   5357    -15      1    202       N  
ATOM   1894  CA  GLU A 265      16.577  41.875  17.011  1.00 43.82           C  
ANISOU 1894  CA  GLU A 265     5482   5550   5618    -19      8    200       C  
ATOM   1895  C   GLU A 265      17.701  41.398  16.086  1.00 45.69           C  
ANISOU 1895  C   GLU A 265     5732   5789   5836    -27     12    208       C  
ATOM   1896  O   GLU A 265      18.690  40.798  16.533  1.00 45.11           O  
ANISOU 1896  O   GLU A 265     5658   5727   5752    -29     24    206       O  
ATOM   1897  CB  GLU A 265      17.016  41.829  18.480  1.00 45.97           C  
ANISOU 1897  CB  GLU A 265     5741   5834   5890    -17     21    188       C  
ATOM   1898  CG  GLU A 265      18.276  42.625  18.799  1.00 52.27           C  
ANISOU 1898  CG  GLU A 265     6542   6632   6684    -21     28    186       C  
ATOM   1899  CD  GLU A 265      18.078  44.125  18.683  1.00 57.99           C  
ANISOU 1899  CD  GLU A 265     7267   7343   7423    -20     20    184       C  
ATOM   1900  OE1 GLU A 265      17.366  44.696  19.539  1.00 65.42           O  
ANISOU 1900  OE1 GLU A 265     8195   8281   8378    -15     21    174       O  
ATOM   1901  OE2 GLU A 265      18.638  44.736  17.743  1.00 59.34           O  
ANISOU 1901  OE2 GLU A 265     7449   7505   7591    -25     15    192       O  
ATOM   1902  N   ARG A 266      17.537  41.666  14.791  1.00 49.42           N  
ANISOU 1902  N   ARG A 266     6218   6251   6305    -32      1    218       N  
ATOM   1903  CA  ARG A 266      18.369  41.040  13.758  1.00 49.28           C  
ANISOU 1903  CA  ARG A 266     6217   6237   6270    -41      5    226       C  
ATOM   1904  C   ARG A 266      19.684  41.757  13.474  1.00 52.57           C  
ANISOU 1904  C   ARG A 266     6641   6652   6679    -48     12    227       C  
ATOM   1905  O   ARG A 266      20.660  41.536  14.193  1.00 61.47           O  
ANISOU 1905  O   ARG A 266     7763   7788   7803    -48     26    222       O  
ATOM   1906  CB  ARG A 266      17.568  40.796  12.489  1.00 48.29           C  
ANISOU 1906  CB  ARG A 266     6104   6103   6140    -45     -8    235       C  
ATOM   1907  CG  ARG A 266      16.592  39.650  12.641  1.00 47.52           C  
ANISOU 1907  CG  ARG A 266     5999   6010   6044    -40    -11    234       C  
ATOM   1908  CD  ARG A 266      16.131  39.164  11.288  1.00 49.21           C  
ANISOU 1908  CD  ARG A 266     6229   6219   6249    -46    -22    243       C  
ATOM   1909  NE  ARG A 266      14.966  39.892  10.796  1.00 48.60           N  
ANISOU 1909  NE  ARG A 266     6153   6127   6184    -46    -43    250       N  
ATOM   1910  CZ  ARG A 266      13.782  39.336  10.565  1.00 46.87           C  
ANISOU 1910  CZ  ARG A 266     5931   5904   5971    -42    -54    252       C  
ATOM   1911  NH1 ARG A 266      13.603  38.041  10.779  1.00 46.31           N  
ANISOU 1911  NH1 ARG A 266     5856   5844   5894    -39    -47    249       N  
ATOM   1912  NH2 ARG A 266      12.777  40.077  10.113  1.00 48.02           N  
ANISOU 1912  NH2 ARG A 266     6078   6035   6131    -42    -75    259       N  
ATOM   1913  N   ASN A 267      19.722  42.589  12.434  1.00 50.26           N  
ANISOU 1913  N   ASN A 267     6362   6348   6384    -55      2    236       N  
ATOM   1914  CA  ASN A 267      20.908  43.411  12.088  1.00 51.54           C  
ANISOU 1914  CA  ASN A 267     6533   6507   6541    -63      8    239       C  
ATOM   1915  C   ASN A 267      21.849  42.872  11.017  1.00 49.92           C  
ANISOU 1915  C   ASN A 267     6344   6305   6317    -75     17    244       C  
ATOM   1916  O   ASN A 267      22.267  43.626  10.140  1.00 52.21           O  
ANISOU 1916  O   ASN A 267     6648   6587   6601    -84     13    252       O  
ATOM   1917  CB  ASN A 267      21.734  43.823  13.324  1.00 52.08           C  
ANISOU 1917  CB  ASN A 267     6589   6581   6616    -59     20    230       C  
ATOM   1918  CG  ASN A 267      20.985  44.765  14.243  1.00 55.08           C  
ANISOU 1918  CG  ASN A 267     6956   6955   7015    -50     12    224       C  
ATOM   1919  OD1 ASN A 267      20.310  45.698  13.791  1.00 59.92           O  
ANISOU 1919  OD1 ASN A 267     7572   7555   7638    -50     -2    228       O  
ATOM   1920  ND2 ASN A 267      21.101  44.528  15.545  1.00 53.92           N  
ANISOU 1920  ND2 ASN A 267     6795   6817   6873    -44     21    213       N  
ATOM   1921  N   LEU A 268      22.206  41.595  11.087  1.00 49.54           N  
ANISOU 1921  N   LEU A 268     6294   6267   6260    -75     29    240       N  
ATOM   1922  CA  LEU A 268      23.195  41.057  10.142  1.00 51.82           C  
ANISOU 1922  CA  LEU A 268     6595   6559   6533    -86     41    242       C  
ATOM   1923  C   LEU A 268      22.643  40.830   8.731  1.00 53.68           C  
ANISOU 1923  C   LEU A 268     6851   6790   6756    -96     32    250       C  
ATOM   1924  O   LEU A 268      21.927  39.857   8.468  1.00 53.58           O  
ANISOU 1924  O   LEU A 268     6838   6779   6739    -94     28    250       O  
ATOM   1925  CB  LEU A 268      23.890  39.812  10.696  1.00 50.73           C  
ANISOU 1925  CB  LEU A 268     6448   6433   6394    -83     57    234       C  
ATOM   1926  CG  LEU A 268      25.256  40.067  11.336  1.00 49.78           C  
ANISOU 1926  CG  LEU A 268     6320   6315   6277    -84     72    229       C  
ATOM   1927  CD1 LEU A 268      25.176  40.681  12.727  1.00 48.57           C  
ANISOU 1927  CD1 LEU A 268     6152   6165   6138    -75     69    225       C  
ATOM   1928  CD2 LEU A 268      26.002  38.753  11.403  1.00 51.87           C  
ANISOU 1928  CD2 LEU A 268     6580   6589   6539    -86     87    224       C  
ATOM   1929  N   GLU A 269      22.976  41.760   7.840  1.00 55.45           N  
ANISOU 1929  N   GLU A 269     7089   7005   6972   -107     27    258       N  
ATOM   1930  CA  GLU A 269      22.556  41.720   6.442  1.00 56.61           C  
ANISOU 1930  CA  GLU A 269     7258   7147   7104   -120     17    268       C  
ATOM   1931  C   GLU A 269      23.115  40.473   5.761  1.00 58.06           C  
ANISOU 1931  C   GLU A 269     7450   7338   7271   -129     33    263       C  
ATOM   1932  O   GLU A 269      22.381  39.755   5.086  1.00 60.48           O  
ANISOU 1932  O   GLU A 269     7765   7645   7568   -132     26    266       O  
ATOM   1933  CB  GLU A 269      22.972  43.009   5.703  1.00 59.39           C  
ANISOU 1933  CB  GLU A 269     7624   7488   7451   -132     11    277       C  
ATOM   1934  CG  GLU A 269      24.480  43.240   5.484  1.00 61.91           C  
ANISOU 1934  CG  GLU A 269     7948   7811   7761   -142     31    274       C  
ATOM   1935  CD  GLU A 269      25.274  43.697   6.720  1.00 61.41           C  
ANISOU 1935  CD  GLU A 269     7867   7751   7714   -132     41    267       C  
ATOM   1936  OE1 GLU A 269      24.764  43.668   7.858  1.00 61.73           O  
ANISOU 1936  OE1 GLU A 269     7890   7794   7770   -117     37    261       O  
ATOM   1937  OE2 GLU A 269      26.448  44.088   6.554  1.00 63.05           O  
ANISOU 1937  OE2 GLU A 269     8078   7959   7917   -139     54    266       O  
ATOM   1938  N   ILE A 270      24.409  40.217   5.960  1.00 56.89           N  
ANISOU 1938  N   ILE A 270     7298   7196   7119   -132     55    256       N  
ATOM   1939  CA  ILE A 270      25.069  39.013   5.440  1.00 57.03           C  
ANISOU 1939  CA  ILE A 270     7321   7221   7126   -139     73    249       C  
ATOM   1940  C   ILE A 270      25.932  38.360   6.520  1.00 55.40           C  
ANISOU 1940  C   ILE A 270     7093   7022   6931   -129     90    238       C  
ATOM   1941  O   ILE A 270      26.418  39.035   7.438  1.00 54.24           O  
ANISOU 1941  O   ILE A 270     6935   6875   6797   -123     92    237       O  
ATOM   1942  CB  ILE A 270      25.889  39.265   4.138  1.00 58.98           C  
ANISOU 1942  CB  ILE A 270     7589   7466   7354   -158     83    252       C  
ATOM   1943  CG1 ILE A 270      26.957  40.351   4.327  1.00 58.99           C  
ANISOU 1943  CG1 ILE A 270     7589   7463   7359   -163     91    253       C  
ATOM   1944  CG2 ILE A 270      24.970  39.626   2.972  1.00 62.42           C  
ANISOU 1944  CG2 ILE A 270     8047   7894   7774   -170     65    263       C  
ATOM   1945  CD1 ILE A 270      28.319  39.838   4.753  1.00 60.03           C  
ANISOU 1945  CD1 ILE A 270     7710   7601   7496   -162    116    242       C  
ATOM   1946  N   PHE A 271      26.105  37.045   6.407  1.00 53.82           N  
ANISOU 1946  N   PHE A 271     6891   6829   6730   -129    102    231       N  
ATOM   1947  CA  PHE A 271      26.832  36.272   7.411  1.00 53.11           C  
ANISOU 1947  CA  PHE A 271     6781   6745   6653   -121    115    222       C  
ATOM   1948  C   PHE A 271      27.690  35.175   6.774  1.00 51.63           C  
ANISOU 1948  C   PHE A 271     6596   6560   6461   -129    135    214       C  
ATOM   1949  O   PHE A 271      27.297  34.004   6.725  1.00 51.36           O  
ANISOU 1949  O   PHE A 271     6557   6529   6427   -126    137    210       O  
ATOM   1950  CB  PHE A 271      25.862  35.706   8.462  1.00 50.76           C  
ANISOU 1950  CB  PHE A 271     6467   6451   6366   -106    104    222       C  
ATOM   1951  CG  PHE A 271      26.544  35.078   9.643  1.00 49.62           C  
ANISOU 1951  CG  PHE A 271     6302   6313   6236    -98    114    215       C  
ATOM   1952  CD1 PHE A 271      26.355  33.737   9.932  1.00 49.01           C  
ANISOU 1952  CD1 PHE A 271     6216   6242   6164    -93    117    211       C  
ATOM   1953  CD2 PHE A 271      27.384  35.827  10.461  1.00 50.05           C  
ANISOU 1953  CD2 PHE A 271     6348   6368   6300    -96    118    214       C  
ATOM   1954  CE1 PHE A 271      26.980  33.151  11.020  1.00 50.53           C  
ANISOU 1954  CE1 PHE A 271     6390   6439   6370    -87    124    206       C  
ATOM   1955  CE2 PHE A 271      28.016  35.249  11.547  1.00 51.93           C  
ANISOU 1955  CE2 PHE A 271     6567   6610   6550    -90    125    210       C  
ATOM   1956  CZ  PHE A 271      27.815  33.905  11.827  1.00 51.24           C  
ANISOU 1956  CZ  PHE A 271     6471   6528   6467    -86    127    206       C  
ATOM   1957  N   GLU A 272      28.858  35.584   6.282  1.00 51.56           N  
ANISOU 1957  N   GLU A 272     6592   6549   6448   -140    150    212       N  
ATOM   1958  CA  GLU A 272      29.770  34.714   5.541  1.00 53.25           C  
ANISOU 1958  CA  GLU A 272     6810   6763   6657   -150    172    202       C  
ATOM   1959  C   GLU A 272      30.924  34.253   6.432  1.00 48.62           C  
ANISOU 1959  C   GLU A 272     6202   6179   6091   -145    187    194       C  
ATOM   1960  O   GLU A 272      31.219  34.898   7.438  1.00 48.51           O  
ANISOU 1960  O   GLU A 272     6176   6164   6089   -136    182    197       O  
ATOM   1961  CB  GLU A 272      30.304  35.428   4.282  1.00 60.45           C  
ANISOU 1961  CB  GLU A 272     7743   7671   7552   -169    181    204       C  
ATOM   1962  CG  GLU A 272      29.367  35.384   3.069  1.00 70.84           C  
ANISOU 1962  CG  GLU A 272     9083   8985   8845   -180    171    209       C  
ATOM   1963  CD  GLU A 272      30.089  35.436   1.710  1.00 82.85           C  
ANISOU 1963  CD  GLU A 272    10626  10506  10347   -202    188    205       C  
ATOM   1964  OE1 GLU A 272      29.433  35.759   0.685  1.00 78.21           O  
ANISOU 1964  OE1 GLU A 272    10061   9916   9739   -214    178    213       O  
ATOM   1965  OE2 GLU A 272      31.311  35.148   1.649  1.00 89.10           O  
ANISOU 1965  OE2 GLU A 272    11411  11298  11145   -207    212    195       O  
ATOM   1966  N   PRO A 273      31.576  33.131   6.070  1.00 46.85           N  
ANISOU 1966  N   PRO A 273     5974   5956   5872   -149    205    184       N  
ATOM   1967  CA  PRO A 273      32.735  32.589   6.784  1.00 46.34           C  
ANISOU 1967  CA  PRO A 273     5888   5890   5828   -145    219    177       C  
ATOM   1968  C   PRO A 273      33.780  33.614   7.200  1.00 46.94           C  
ANISOU 1968  C   PRO A 273     5959   5963   5913   -147    225    178       C  
ATOM   1969  O   PRO A 273      34.441  33.410   8.207  1.00 47.46           O  
ANISOU 1969  O   PRO A 273     6005   6028   5998   -140    227    177       O  
ATOM   1970  CB  PRO A 273      33.365  31.649   5.760  1.00 44.38           C  
ANISOU 1970  CB  PRO A 273     5644   5639   5577   -157    241    165       C  
ATOM   1971  CG  PRO A 273      32.243  31.219   4.891  1.00 44.88           C  
ANISOU 1971  CG  PRO A 273     5725   5704   5621   -161    233    166       C  
ATOM   1972  CD  PRO A 273      31.103  32.193   5.038  1.00 46.34           C  
ANISOU 1972  CD  PRO A 273     5921   5891   5794   -157    210    179       C  
ATOM   1973  N   SER A 274      33.934  34.689   6.427  1.00 48.53           N  
ANISOU 1973  N   SER A 274     6177   6160   6099   -158    227    183       N  
ATOM   1974  CA  SER A 274      35.005  35.663   6.653  1.00 49.52           C  
ANISOU 1974  CA  SER A 274     6299   6282   6232   -161    234    184       C  
ATOM   1975  C   SER A 274      34.769  36.513   7.899  1.00 50.77           C  
ANISOU 1975  C   SER A 274     6446   6441   6400   -149    217    191       C  
ATOM   1976  O   SER A 274      35.707  37.057   8.474  1.00 53.75           O  
ANISOU 1976  O   SER A 274     6814   6816   6791   -148    222    191       O  
ATOM   1977  CB  SER A 274      35.200  36.565   5.430  1.00 50.76           C  
ANISOU 1977  CB  SER A 274     6479   6436   6370   -178    241    187       C  
ATOM   1978  OG  SER A 274      34.297  37.659   5.439  1.00 51.97           O  
ANISOU 1978  OG  SER A 274     6644   6588   6511   -176    220    199       O  
ATOM   1979  N   ILE A 275      33.513  36.634   8.305  1.00 49.38           N  
ANISOU 1979  N   ILE A 275     6272   6268   6219   -140    197    197       N  
ATOM   1980  CA  ILE A 275      33.175  37.281   9.567  1.00 51.27           C  
ANISOU 1980  CA  ILE A 275     6500   6509   6468   -128    182    202       C  
ATOM   1981  C   ILE A 275      33.707  36.471  10.760  1.00 51.34           C  
ANISOU 1981  C   ILE A 275     6488   6522   6497   -119    185    198       C  
ATOM   1982  O   ILE A 275      34.027  37.030  11.808  1.00 52.90           O  
ANISOU 1982  O   ILE A 275     6674   6720   6705   -114    179    199       O  
ATOM   1983  CB  ILE A 275      31.653  37.479   9.667  1.00 52.11           C  
ANISOU 1983  CB  ILE A 275     6613   6618   6566   -121    162    208       C  
ATOM   1984  CG1 ILE A 275      31.204  38.482   8.604  1.00 52.87           C  
ANISOU 1984  CG1 ILE A 275     6731   6709   6647   -131    156    215       C  
ATOM   1985  CG2 ILE A 275      31.236  37.933  11.060  1.00 51.82           C  
ANISOU 1985  CG2 ILE A 275     6563   6584   6541   -109    149    210       C  
ATOM   1986  CD1 ILE A 275      29.757  38.327   8.209  1.00 55.15           C  
ANISOU 1986  CD1 ILE A 275     7029   6998   6926   -128    139    220       C  
ATOM   1987  N   MET A 276      33.824  35.160  10.563  1.00 52.19           N  
ANISOU 1987  N   MET A 276     6589   6632   6609   -120    194    192       N  
ATOM   1988  CA  MET A 276      34.246  34.203  11.583  1.00 53.62           C  
ANISOU 1988  CA  MET A 276     6749   6814   6808   -113    195    189       C  
ATOM   1989  C   MET A 276      35.753  34.258  11.802  1.00 53.44           C  
ANISOU 1989  C   MET A 276     6715   6787   6803   -117    209    185       C  
ATOM   1990  O   MET A 276      36.289  33.591  12.687  1.00 51.93           O  
ANISOU 1990  O   MET A 276     6505   6595   6629   -112    208    183       O  
ATOM   1991  CB  MET A 276      33.894  32.796  11.100  1.00 58.96           C  
ANISOU 1991  CB  MET A 276     7424   7492   7484   -113    200    184       C  
ATOM   1992  CG  MET A 276      33.194  31.902  12.106  1.00 60.60           C  
ANISOU 1992  CG  MET A 276     7617   7705   7700   -102    188    186       C  
ATOM   1993  SD  MET A 276      31.409  32.017  11.934  1.00 61.06           S  
ANISOU 1993  SD  MET A 276     7689   7770   7741    -97    171    191       S  
ATOM   1994  CE  MET A 276      31.085  33.579  12.754  1.00 59.96           C  
ANISOU 1994  CE  MET A 276     7550   7630   7598    -92    157    198       C  
ATOM   1995  N   GLU A 277      36.419  35.051  10.972  1.00 53.48           N  
ANISOU 1995  N   GLU A 277     6730   6787   6802   -127    220    184       N  
ATOM   1996  CA  GLU A 277      37.878  35.099  10.858  1.00 53.07           C  
ANISOU 1996  CA  GLU A 277     6669   6728   6764   -133    237    178       C  
ATOM   1997  C   GLU A 277      38.695  35.219  12.149  1.00 48.87           C  
ANISOU 1997  C   GLU A 277     6117   6195   6254   -127    232    180       C  
ATOM   1998  O   GLU A 277      39.661  34.488  12.327  1.00 48.64           O  
ANISOU 1998  O   GLU A 277     6073   6161   6246   -129    242    175       O  
ATOM   1999  CB  GLU A 277      38.262  36.227   9.906  1.00 59.24           C  
ANISOU 1999  CB  GLU A 277     7467   7505   7533   -144    245    180       C  
ATOM   2000  CG  GLU A 277      38.556  35.772   8.493  1.00 66.48           C  
ANISOU 2000  CG  GLU A 277     8397   8420   8440   -157    265    172       C  
ATOM   2001  CD  GLU A 277      40.044  35.723   8.227  1.00 73.77           C  
ANISOU 2001  CD  GLU A 277     9311   9336   9380   -166    287    165       C  
ATOM   2002  OE1 GLU A 277      40.686  36.798   8.246  1.00 74.43           O  
ANISOU 2002  OE1 GLU A 277     9397   9416   9464   -170    290    168       O  
ATOM   2003  OE2 GLU A 277      40.570  34.611   8.004  1.00 80.24           O  
ANISOU 2003  OE2 GLU A 277    10120  10153  10212   -168    302    155       O  
ATOM   2004  N   GLY A 278      38.326  36.143  13.034  1.00 46.46           N  
ANISOU 2004  N   GLY A 278     5812   5893   5947   -121    216    187       N  
ATOM   2005  CA  GLY A 278      39.035  36.322  14.305  1.00 43.35           C  
ANISOU 2005  CA  GLY A 278     5402   5498   5571   -117    209    189       C  
ATOM   2006  C   GLY A 278      39.096  35.094  15.202  1.00 43.34           C  
ANISOU 2006  C   GLY A 278     5382   5498   5585   -111    204    189       C  
ATOM   2007  O   GLY A 278      39.912  35.029  16.116  1.00 41.87           O  
ANISOU 2007  O   GLY A 278     5181   5310   5417   -111    201    190       O  
ATOM   2008  N   LEU A 279      38.244  34.111  14.922  1.00 45.16           N  
ANISOU 2008  N   LEU A 279     5614   5733   5809   -108    203    187       N  
ATOM   2009  CA  LEU A 279      38.149  32.878  15.709  1.00 45.91           C  
ANISOU 2009  CA  LEU A 279     5694   5831   5918   -104    196    188       C  
ATOM   2010  C   LEU A 279      39.275  31.837  15.530  1.00 48.10           C  
ANISOU 2010  C   LEU A 279     5954   6100   6219   -107    209    183       C  
ATOM   2011  O   LEU A 279      39.240  30.795  16.177  1.00 52.65           O  
ANISOU 2011  O   LEU A 279     6517   6677   6809   -104    202    184       O  
ATOM   2012  CB  LEU A 279      36.777  32.221  15.488  1.00 45.42           C  
ANISOU 2012  CB  LEU A 279     5640   5776   5842    -99    189    189       C  
ATOM   2013  CG  LEU A 279      35.560  32.569  16.368  1.00 45.22           C  
ANISOU 2013  CG  LEU A 279     5617   5760   5804    -91    171    195       C  
ATOM   2014  CD1 LEU A 279      35.768  33.748  17.313  1.00 43.81           C  
ANISOU 2014  CD1 LEU A 279     5438   5583   5625    -90    162    199       C  
ATOM   2015  CD2 LEU A 279      34.318  32.788  15.517  1.00 43.27           C  
ANISOU 2015  CD2 LEU A 279     5386   5515   5536    -90    169    194       C  
ATOM   2016  N   CYS A 280      40.263  32.096  14.675  1.00 48.15           N  
ANISOU 2016  N   CYS A 280     5963   6099   6233   -115    227    177       N  
ATOM   2017  CA  CYS A 280      41.429  31.205  14.598  1.00 49.67           C  
ANISOU 2017  CA  CYS A 280     6137   6282   6453   -118    239    171       C  
ATOM   2018  C   CYS A 280      42.411  31.536  15.706  1.00 48.48           C  
ANISOU 2018  C   CYS A 280     5969   6125   6323   -118    231    176       C  
ATOM   2019  O   CYS A 280      43.263  30.720  16.072  1.00 48.14           O  
ANISOU 2019  O   CYS A 280     5907   6075   6309   -118    233    174       O  
ATOM   2020  CB  CYS A 280      42.142  31.335  13.261  1.00 53.92           C  
ANISOU 2020  CB  CYS A 280     6682   6812   6991   -128    264    160       C  
ATOM   2021  SG  CYS A 280      41.026  31.774  11.931  1.00 63.74           S  
ANISOU 2021  SG  CYS A 280     7955   8063   8199   -133    270    158       S  
ATOM   2022  N   ASP A 281      42.281  32.753  16.221  1.00 47.03           N  
ANISOU 2022  N   ASP A 281     5794   5946   6129   -117    221    182       N  
ATOM   2023  CA  ASP A 281      43.143  33.269  17.260  1.00 44.59           C  
ANISOU 2023  CA  ASP A 281     5472   5633   5835   -117    212    187       C  
ATOM   2024  C   ASP A 281      42.533  33.079  18.630  1.00 40.83           C  
ANISOU 2024  C   ASP A 281     4990   5165   5357   -111    189    196       C  
ATOM   2025  O   ASP A 281      43.076  33.556  19.614  1.00 40.37           O  
ANISOU 2025  O   ASP A 281     4924   5106   5308   -112    178    201       O  
ATOM   2026  CB  ASP A 281      43.415  34.747  17.012  1.00 49.19           C  
ANISOU 2026  CB  ASP A 281     6067   6215   6408   -120    215    188       C  
ATOM   2027  CG  ASP A 281      44.369  34.977  15.854  1.00 53.39           C  
ANISOU 2027  CG  ASP A 281     6600   6737   6946   -128    238    181       C  
ATOM   2028  OD1 ASP A 281      45.351  34.205  15.742  1.00 54.35           O  
ANISOU 2028  OD1 ASP A 281     6705   6849   7093   -132    249    176       O  
ATOM   2029  OD2 ASP A 281      44.141  35.935  15.070  1.00 52.80           O  
ANISOU 2029  OD2 ASP A 281     6542   6664   6853   -132    245    180       O  
ATOM   2030  N   VAL A 282      41.398  32.389  18.689  1.00 40.57           N  
ANISOU 2030  N   VAL A 282     4961   5140   5311   -106    183    197       N  
ATOM   2031  CA  VAL A 282      40.760  32.043  19.969  1.00 39.65           C  
ANISOU 2031  CA  VAL A 282     4840   5032   5192   -102    163    204       C  
ATOM   2032  C   VAL A 282      40.648  30.520  20.048  1.00 37.81           C  
ANISOU 2032  C   VAL A 282     4594   4797   4973   -101    161    205       C  
ATOM   2033  O   VAL A 282      40.402  29.876  19.027  1.00 37.09           O  
ANISOU 2033  O   VAL A 282     4506   4704   4881   -101    173    199       O  
ATOM   2034  CB  VAL A 282      39.378  32.753  20.183  1.00 39.19           C  
ANISOU 2034  CB  VAL A 282     4797   4985   5106    -98    154    206       C  
ATOM   2035  CG1 VAL A 282      39.221  33.971  19.283  1.00 39.27           C  
ANISOU 2035  CG1 VAL A 282     4824   4994   5101    -99    163    202       C  
ATOM   2036  CG2 VAL A 282      38.207  31.822  19.948  1.00 39.18           C  
ANISOU 2036  CG2 VAL A 282     4800   4990   5094    -93    151    206       C  
ATOM   2037  N   THR A 283      40.846  29.943  21.235  1.00 36.91           N  
ANISOU 2037  N   THR A 283     4466   4684   4872   -101    146    213       N  
ATOM   2038  CA  THR A 283      40.731  28.477  21.373  1.00 36.52           C  
ANISOU 2038  CA  THR A 283     4404   4633   4838   -100    142    215       C  
ATOM   2039  C   THR A 283      39.368  28.079  21.980  1.00 36.21           C  
ANISOU 2039  C   THR A 283     4370   4606   4779    -96    128    220       C  
ATOM   2040  O   THR A 283      39.062  28.402  23.137  1.00 36.05           O  
ANISOU 2040  O   THR A 283     4350   4594   4751    -97    113    227       O  
ATOM   2041  CB  THR A 283      41.967  27.805  22.068  1.00 35.17           C  
ANISOU 2041  CB  THR A 283     4210   4451   4700   -105    135    220       C  
ATOM   2042  OG1 THR A 283      41.642  27.369  23.389  1.00 34.04           O  
ANISOU 2042  OG1 THR A 283     4061   4314   4558   -106    113    231       O  
ATOM   2043  CG2 THR A 283      43.178  28.743  22.123  1.00 34.74           C  
ANISOU 2043  CG2 THR A 283     4152   4388   4658   -109    139    219       C  
ATOM   2044  N   ILE A 284      38.552  27.403  21.170  1.00 35.38           N  
ANISOU 2044  N   ILE A 284     4271   4503   4666    -93    135    215       N  
ATOM   2045  CA  ILE A 284      37.174  27.062  21.533  1.00 35.88           C  
ANISOU 2045  CA  ILE A 284     4342   4578   4712    -88    125    219       C  
ATOM   2046  C   ILE A 284      37.020  25.563  21.759  1.00 36.07           C  
ANISOU 2046  C   ILE A 284     4352   4600   4750    -88    119    222       C  
ATOM   2047  O   ILE A 284      37.404  24.763  20.911  1.00 37.23           O  
ANISOU 2047  O   ILE A 284     4494   4739   4913    -88    130    216       O  
ATOM   2048  CB  ILE A 284      36.186  27.487  20.415  1.00 36.44           C  
ANISOU 2048  CB  ILE A 284     4430   4653   4760    -84    135    212       C  
ATOM   2049  CG1 ILE A 284      36.370  28.960  20.056  1.00 36.73           C  
ANISOU 2049  CG1 ILE A 284     4480   4689   4784    -86    141    209       C  
ATOM   2050  CG2 ILE A 284      34.742  27.242  20.819  1.00 35.48           C  
ANISOU 2050  CG2 ILE A 284     4315   4542   4621    -80    124    215       C  
ATOM   2051  CD1 ILE A 284      36.060  29.270  18.609  1.00 37.34           C  
ANISOU 2051  CD1 ILE A 284     4573   4765   4850    -86    155    201       C  
ATOM   2052  N   ASP A 285      36.451  25.177  22.895  1.00 37.55           N  
ANISOU 2052  N   ASP A 285     4536   4797   4935    -88    102    231       N  
ATOM   2053  CA  ASP A 285      36.090  23.778  23.106  1.00 37.95           C  
ANISOU 2053  CA  ASP A 285     4575   4846   4996    -87     95    236       C  
ATOM   2054  C   ASP A 285      34.752  23.471  22.434  1.00 36.87           C  
ANISOU 2054  C   ASP A 285     4450   4717   4842    -82     99    232       C  
ATOM   2055  O   ASP A 285      34.667  22.554  21.624  1.00 37.29           O  
ANISOU 2055  O   ASP A 285     4499   4764   4903    -80    107    227       O  
ATOM   2056  CB  ASP A 285      36.058  23.408  24.596  1.00 41.29           C  
ANISOU 2056  CB  ASP A 285     4990   5275   5423    -92     75    249       C  
ATOM   2057  CG  ASP A 285      37.383  23.701  25.328  1.00 47.22           C  
ANISOU 2057  CG  ASP A 285     5729   6019   6193    -99     68    255       C  
ATOM   2058  OD1 ASP A 285      37.386  23.613  26.579  1.00 51.84           O  
ANISOU 2058  OD1 ASP A 285     6310   6610   6777   -104     50    266       O  
ATOM   2059  OD2 ASP A 285      38.415  24.022  24.686  1.00 46.69           O  
ANISOU 2059  OD2 ASP A 285     5657   5940   6141    -99     79    249       O  
ATOM   2060  N   GLU A 286      33.716  24.238  22.766  1.00 37.01           N  
ANISOU 2060  N   GLU A 286     4480   4745   4834    -79     95    233       N  
ATOM   2061  CA  GLU A 286      32.378  24.051  22.190  1.00 37.71           C  
ANISOU 2061  CA  GLU A 286     4581   4841   4907    -74     97    229       C  
ATOM   2062  C   GLU A 286      31.887  25.326  21.523  1.00 37.11           C  
ANISOU 2062  C   GLU A 286     4521   4767   4810    -71    104    223       C  
ATOM   2063  O   GLU A 286      32.001  26.426  22.080  1.00 38.60           O  
ANISOU 2063  O   GLU A 286     4715   4960   4991    -72    101    224       O  
ATOM   2064  CB  GLU A 286      31.374  23.601  23.251  1.00 41.48           C  
ANISOU 2064  CB  GLU A 286     5055   5328   5375    -73     83    237       C  
ATOM   2065  CG  GLU A 286      31.789  22.331  23.999  1.00 49.02           C  
ANISOU 2065  CG  GLU A 286     5993   6281   6349    -77     72    246       C  
ATOM   2066  CD  GLU A 286      30.804  21.886  25.079  1.00 54.32           C  
ANISOU 2066  CD  GLU A 286     6663   6964   7010    -79     59    255       C  
ATOM   2067  OE1 GLU A 286      31.238  21.137  25.985  1.00 58.36           O  
ANISOU 2067  OE1 GLU A 286     7162   7475   7535    -85     47    264       O  
ATOM   2068  OE2 GLU A 286      29.607  22.269  25.033  1.00 55.84           O  
ANISOU 2068  OE2 GLU A 286     6865   7165   7184    -75     59    252       O  
ATOM   2069  N   PHE A 287      31.339  25.184  20.328  1.00 34.02           N  
ANISOU 2069  N   PHE A 287     4139   4373   4411    -68    113    217       N  
ATOM   2070  CA  PHE A 287      30.903  26.340  19.578  1.00 33.20           C  
ANISOU 2070  CA  PHE A 287     4052   4270   4291    -67    118    212       C  
ATOM   2071  C   PHE A 287      29.431  26.243  19.188  1.00 32.60           C  
ANISOU 2071  C   PHE A 287     3986   4200   4200    -62    114    212       C  
ATOM   2072  O   PHE A 287      28.982  25.244  18.618  1.00 33.10           O  
ANISOU 2072  O   PHE A 287     4048   4261   4265    -61    115    210       O  
ATOM   2073  CB  PHE A 287      31.792  26.512  18.353  1.00 34.22           C  
ANISOU 2073  CB  PHE A 287     4186   4389   4424    -71    133    205       C  
ATOM   2074  CG  PHE A 287      31.426  27.680  17.494  1.00 36.10           C  
ANISOU 2074  CG  PHE A 287     4442   4628   4646    -71    138    202       C  
ATOM   2075  CD1 PHE A 287      31.630  28.983  17.937  1.00 36.00           C  
ANISOU 2075  CD1 PHE A 287     4434   4616   4626    -72    136    203       C  
ATOM   2076  CD2 PHE A 287      30.891  27.483  16.232  1.00 37.25           C  
ANISOU 2076  CD2 PHE A 287     4600   4770   4781    -72    145    197       C  
ATOM   2077  CE1 PHE A 287      31.303  30.062  17.138  1.00 36.04           C  
ANISOU 2077  CE1 PHE A 287     4455   4620   4618    -72    139    201       C  
ATOM   2078  CE2 PHE A 287      30.566  28.564  15.427  1.00 38.27           C  
ANISOU 2078  CE2 PHE A 287     4746   4898   4894    -74    147    196       C  
ATOM   2079  CZ  PHE A 287      30.770  29.855  15.882  1.00 36.68           C  
ANISOU 2079  CZ  PHE A 287     4548   4698   4689    -74    144    198       C  
ATOM   2080  N   ARG A 288      28.674  27.286  19.501  1.00 31.79           N  
ANISOU 2080  N   ARG A 288     3892   4102   4084    -60    108    212       N  
ATOM   2081  CA  ARG A 288      27.240  27.277  19.240  1.00 30.69           C  
ANISOU 2081  CA  ARG A 288     3760   3967   3933    -55    103    212       C  
ATOM   2082  C   ARG A 288      26.793  28.460  18.413  1.00 30.07           C  
ANISOU 2082  C   ARG A 288     3697   3885   3842    -54    105    210       C  
ATOM   2083  O   ARG A 288      27.074  29.605  18.741  1.00 30.75           O  
ANISOU 2083  O   ARG A 288     3785   3970   3924    -55    104    209       O  
ATOM   2084  CB  ARG A 288      26.453  27.197  20.548  1.00 31.35           C  
ANISOU 2084  CB  ARG A 288     3836   4059   4013    -53     93    217       C  
ATOM   2085  CG  ARG A 288      26.712  25.909  21.310  1.00 31.04           C  
ANISOU 2085  CG  ARG A 288     3783   4024   3985    -55     88    222       C  
ATOM   2086  CD  ARG A 288      25.449  25.367  21.945  1.00 32.88           C  
ANISOU 2086  CD  ARG A 288     4012   4265   4213    -52     80    225       C  
ATOM   2087  NE  ARG A 288      25.467  25.621  23.377  1.00 35.65           N  
ANISOU 2087  NE  ARG A 288     4358   4624   4563    -55     74    229       N  
ATOM   2088  CZ  ARG A 288      24.646  26.438  24.017  1.00 35.18           C  
ANISOU 2088  CZ  ARG A 288     4302   4572   4493    -54     71    227       C  
ATOM   2089  NH1 ARG A 288      23.704  27.081  23.362  1.00 36.28           N  
ANISOU 2089  NH1 ARG A 288     4449   4708   4624    -49     73    222       N  
ATOM   2090  NH2 ARG A 288      24.771  26.602  25.323  1.00 36.94           N  
ANISOU 2090  NH2 ARG A 288     4519   4801   4712    -60     66    229       N  
ATOM   2091  N   LEU A 289      26.111  28.163  17.319  1.00 30.44           N  
ANISOU 2091  N   LEU A 289     3754   3930   3883    -53    105    208       N  
ATOM   2092  CA  LEU A 289      25.530  29.183  16.485  1.00 31.15           C  
ANISOU 2092  CA  LEU A 289     3858   4015   3961    -54    104    207       C  
ATOM   2093  C   LEU A 289      24.034  29.200  16.621  1.00 30.74           C  
ANISOU 2093  C   LEU A 289     3808   3967   3904    -48     93    209       C  
ATOM   2094  O   LEU A 289      23.366  28.177  16.451  1.00 30.80           O  
ANISOU 2094  O   LEU A 289     3813   3975   3912    -46     90    210       O  
ATOM   2095  CB  LEU A 289      25.920  28.978  15.032  1.00 33.64           C  
ANISOU 2095  CB  LEU A 289     4186   4324   4272    -59    112    204       C  
ATOM   2096  CG  LEU A 289      27.125  29.855  14.699  1.00 37.07           C  
ANISOU 2096  CG  LEU A 289     4624   4753   4706    -65    122    202       C  
ATOM   2097  CD1 LEU A 289      27.976  29.244  13.592  1.00 37.15           C  
ANISOU 2097  CD1 LEU A 289     4639   4757   4716    -73    136    197       C  
ATOM   2098  CD2 LEU A 289      26.650  31.264  14.353  1.00 36.54           C  
ANISOU 2098  CD2 LEU A 289     4570   4683   4628    -66    116    204       C  
ATOM   2099  N   THR A 290      23.511  30.377  16.931  1.00 30.40           N  
ANISOU 2099  N   THR A 290     3769   3923   3857    -46     87    209       N  
ATOM   2100  CA  THR A 290      22.077  30.562  17.052  1.00 30.67           C  
ANISOU 2100  CA  THR A 290     3803   3958   3889    -40     77    210       C  
ATOM   2101  C   THR A 290      21.493  31.271  15.825  1.00 31.64           C  
ANISOU 2101  C   THR A 290     3942   4073   4006    -42     72    212       C  
ATOM   2102  O   THR A 290      22.199  31.526  14.845  1.00 31.09           O  
ANISOU 2102  O   THR A 290     3883   3997   3930    -48     77    212       O  
ATOM   2103  CB  THR A 290      21.725  31.320  18.340  1.00 30.32           C  
ANISOU 2103  CB  THR A 290     3751   3918   3848    -37     74    209       C  
ATOM   2104  OG1 THR A 290      22.144  32.690  18.230  1.00 29.82           O  
ANISOU 2104  OG1 THR A 290     3694   3850   3784    -39     74    207       O  
ATOM   2105  CG2 THR A 290      22.387  30.652  19.547  1.00 28.89           C  
ANISOU 2105  CG2 THR A 290     3557   3746   3672    -39     77    209       C  
ATOM   2106  N   TYR A 291      20.197  31.575  15.878  1.00 33.55           N  
ANISOU 2106  N   TYR A 291     4184   4313   4249    -37     62    213       N  
ATOM   2107  CA  TYR A 291      19.521  32.217  14.761  1.00 34.02           C  
ANISOU 2107  CA  TYR A 291     4256   4363   4304    -38     53    216       C  
ATOM   2108  C   TYR A 291      20.370  33.335  14.188  1.00 34.24           C  
ANISOU 2108  C   TYR A 291     4296   4386   4328    -44     56    217       C  
ATOM   2109  O   TYR A 291      20.972  34.120  14.922  1.00 33.65           O  
ANISOU 2109  O   TYR A 291     4216   4312   4257    -44     60    214       O  
ATOM   2110  CB  TYR A 291      18.157  32.770  15.182  1.00 34.43           C  
ANISOU 2110  CB  TYR A 291     4304   4413   4363    -32     42    216       C  
ATOM   2111  CG  TYR A 291      17.489  33.582  14.093  1.00 36.06           C  
ANISOU 2111  CG  TYR A 291     4523   4608   4568    -34     30    221       C  
ATOM   2112  CD1 TYR A 291      16.808  32.955  13.048  1.00 35.23           C  
ANISOU 2112  CD1 TYR A 291     4428   4499   4459    -36     22    225       C  
ATOM   2113  CD2 TYR A 291      17.560  34.981  14.088  1.00 35.75           C  
ANISOU 2113  CD2 TYR A 291     4488   4562   4533    -34     26    221       C  
ATOM   2114  CE1 TYR A 291      16.213  33.692  12.040  1.00 35.44           C  
ANISOU 2114  CE1 TYR A 291     4466   4514   4483    -40      9    231       C  
ATOM   2115  CE2 TYR A 291      16.953  35.724  13.086  1.00 35.75           C  
ANISOU 2115  CE2 TYR A 291     4499   4550   4532    -37     13    227       C  
ATOM   2116  CZ  TYR A 291      16.282  35.077  12.064  1.00 36.22           C  
ANISOU 2116  CZ  TYR A 291     4568   4605   4586    -40      4    232       C  
ATOM   2117  OH  TYR A 291      15.678  35.810  11.059  1.00 36.94           O  
ANISOU 2117  OH  TYR A 291     4672   4685   4677    -45    -10    240       O  
ATOM   2118  N   THR A 292      20.428  33.387  12.868  1.00 36.44           N  
ANISOU 2118  N   THR A 292     4589   4657   4596    -51     55    220       N  
ATOM   2119  CA  THR A 292      21.021  34.522  12.186  1.00 39.76           C  
ANISOU 2119  CA  THR A 292     5023   5071   5012    -58     55    222       C  
ATOM   2120  C   THR A 292      20.067  34.903  11.079  1.00 42.06           C  
ANISOU 2120  C   THR A 292     5328   5353   5297    -61     41    229       C  
ATOM   2121  O   THR A 292      19.323  34.059  10.573  1.00 43.26           O  
ANISOU 2121  O   THR A 292     5484   5506   5447    -61     36    230       O  
ATOM   2122  CB  THR A 292      22.420  34.224  11.614  1.00 40.67           C  
ANISOU 2122  CB  THR A 292     5144   5186   5119    -67     70    220       C  
ATOM   2123  OG1 THR A 292      23.049  33.173  12.360  1.00 42.99           O  
ANISOU 2123  OG1 THR A 292     5425   5489   5420    -64     81    215       O  
ATOM   2124  CG2 THR A 292      23.283  35.456  11.712  1.00 42.26           C  
ANISOU 2124  CG2 THR A 292     5348   5384   5321    -70     74    221       C  
ATOM   2125  N   ASN A 293      20.060  36.184  10.733  1.00 44.21           N  
ANISOU 2125  N   ASN A 293     5608   5617   5570    -65     34    233       N  
ATOM   2126  CA  ASN A 293      19.195  36.690   9.676  1.00 45.66           C  
ANISOU 2126  CA  ASN A 293     5807   5792   5750    -70     18    241       C  
ATOM   2127  C   ASN A 293      19.573  36.034   8.340  1.00 44.72           C  
ANISOU 2127  C   ASN A 293     5706   5672   5613    -82     22    244       C  
ATOM   2128  O   ASN A 293      18.770  35.318   7.748  1.00 46.82           O  
ANISOU 2128  O   ASN A 293     5978   5937   5874    -84     14    246       O  
ATOM   2129  CB  ASN A 293      19.282  38.223   9.648  1.00 48.63           C  
ANISOU 2129  CB  ASN A 293     6186   6158   6131    -71     10    245       C  
ATOM   2130  CG  ASN A 293      18.479  38.849   8.529  1.00 49.23           C  
ANISOU 2130  CG  ASN A 293     6278   6222   6204    -78     -8    256       C  
ATOM   2131  OD1 ASN A 293      18.983  39.730   7.830  1.00 49.91           O  
ANISOU 2131  OD1 ASN A 293     6377   6301   6283    -88    -11    262       O  
ATOM   2132  ND2 ASN A 293      17.230  38.408   8.353  1.00 47.54           N  
ANISOU 2132  ND2 ASN A 293     6062   6004   5995    -74    -22    259       N  
ATOM   2133  N   ASP A 294      20.813  36.247   7.907  1.00 44.87           N  
ANISOU 2133  N   ASP A 294     5733   5692   5622    -91     35    242       N  
ATOM   2134  CA  ASP A 294      21.407  35.538   6.772  1.00 44.21           C  
ANISOU 2134  CA  ASP A 294     5665   5609   5521   -104     46    241       C  
ATOM   2135  C   ASP A 294      22.228  34.376   7.317  1.00 42.37           C  
ANISOU 2135  C   ASP A 294     5420   5386   5292   -101     64    232       C  
ATOM   2136  O   ASP A 294      22.675  34.425   8.466  1.00 44.18           O  
ANISOU 2136  O   ASP A 294     5632   5619   5534    -92     71    227       O  
ATOM   2137  CB  ASP A 294      22.331  36.492   5.994  1.00 47.38           C  
ANISOU 2137  CB  ASP A 294     6082   6007   5912   -117     51    245       C  
ATOM   2138  CG  ASP A 294      22.853  35.892   4.686  1.00 49.29           C  
ANISOU 2138  CG  ASP A 294     6343   6249   6135   -133     62    244       C  
ATOM   2139  OD1 ASP A 294      22.038  35.320   3.922  1.00 50.29           O  
ANISOU 2139  OD1 ASP A 294     6481   6375   6252   -138     52    246       O  
ATOM   2140  OD2 ASP A 294      24.076  36.005   4.420  1.00 47.58           O  
ANISOU 2140  OD2 ASP A 294     6130   6034   5912   -142     80    239       O  
ATOM   2141  N   PHE A 295      22.417  33.333   6.509  1.00 39.34           N  
ANISOU 2141  N   PHE A 295     5044   5004   4898   -108     73    228       N  
ATOM   2142  CA  PHE A 295      23.341  32.241   6.848  1.00 38.03           C  
ANISOU 2142  CA  PHE A 295     4868   4845   4737   -107     92    218       C  
ATOM   2143  C   PHE A 295      23.891  31.549   5.599  1.00 38.84           C  
ANISOU 2143  C   PHE A 295     4984   4946   4824   -121    105    213       C  
ATOM   2144  O   PHE A 295      23.141  31.009   4.791  1.00 40.94           O  
ANISOU 2144  O   PHE A 295     5263   5212   5081   -126     98    214       O  
ATOM   2145  CB  PHE A 295      22.698  31.210   7.797  1.00 36.15           C  
ANISOU 2145  CB  PHE A 295     4611   4612   4511    -94     88    216       C  
ATOM   2146  CG  PHE A 295      23.671  30.200   8.351  1.00 34.46           C  
ANISOU 2146  CG  PHE A 295     4383   4403   4307    -92    104    207       C  
ATOM   2147  CD1 PHE A 295      24.402  30.473   9.501  1.00 35.37           C  
ANISOU 2147  CD1 PHE A 295     4482   4522   4435    -86    110    206       C  
ATOM   2148  CD2 PHE A 295      23.853  28.971   7.728  1.00 34.45           C  
ANISOU 2148  CD2 PHE A 295     4383   4402   4303    -97    113    201       C  
ATOM   2149  CE1 PHE A 295      25.308  29.544  10.012  1.00 35.83           C  
ANISOU 2149  CE1 PHE A 295     4525   4582   4504    -84    122    200       C  
ATOM   2150  CE2 PHE A 295      24.760  28.041   8.222  1.00 34.30           C  
ANISOU 2150  CE2 PHE A 295     4349   4386   4296    -95    127    194       C  
ATOM   2151  CZ  PHE A 295      25.488  28.326   9.366  1.00 34.87           C  
ANISOU 2151  CZ  PHE A 295     4405   4461   4382    -89    131    194       C  
ATOM   2152  N   SER A 296      25.209  31.563   5.460  1.00 40.34           N  
ANISOU 2152  N   SER A 296     5174   5137   5015   -128    124    207       N  
ATOM   2153  CA  SER A 296      25.882  30.877   4.370  1.00 40.13           C  
ANISOU 2153  CA  SER A 296     5159   5110   4977   -141    141    199       C  
ATOM   2154  C   SER A 296      26.091  29.411   4.757  1.00 40.65           C  
ANISOU 2154  C   SER A 296     5209   5179   5055   -135    152    189       C  
ATOM   2155  O   SER A 296      26.579  29.130   5.836  1.00 39.96           O  
ANISOU 2155  O   SER A 296     5101   5094   4986   -125    156    186       O  
ATOM   2156  CB  SER A 296      27.223  31.563   4.093  1.00 38.56           C  
ANISOU 2156  CB  SER A 296     4965   4909   4776   -151    159    195       C  
ATOM   2157  OG  SER A 296      28.087  30.714   3.363  1.00 39.56           O  
ANISOU 2157  OG  SER A 296     5094   5036   4899   -162    181    184       O  
ATOM   2158  N   ASP A 297      25.729  28.476   3.882  1.00 43.17           N  
ANISOU 2158  N   ASP A 297     5538   5498   5365   -142    155    184       N  
ATOM   2159  CA  ASP A 297      25.921  27.054   4.180  1.00 42.79           C  
ANISOU 2159  CA  ASP A 297     5475   5451   5329   -137    164    174       C  
ATOM   2160  C   ASP A 297      27.374  26.718   4.495  1.00 43.20           C  
ANISOU 2160  C   ASP A 297     5513   5503   5396   -139    186    164       C  
ATOM   2161  O   ASP A 297      27.645  25.934   5.402  1.00 42.52           O  
ANISOU 2161  O   ASP A 297     5406   5419   5331   -129    189    161       O  
ATOM   2162  CB  ASP A 297      25.386  26.159   3.055  1.00 43.28           C  
ANISOU 2162  CB  ASP A 297     5552   5513   5378   -147    166    169       C  
ATOM   2163  CG  ASP A 297      23.860  26.016   3.080  1.00 47.09           C  
ANISOU 2163  CG  ASP A 297     6040   5997   5856   -141    142    177       C  
ATOM   2164  OD1 ASP A 297      23.329  25.244   2.260  1.00 46.97           O  
ANISOU 2164  OD1 ASP A 297     6034   5980   5830   -147    140    174       O  
ATOM   2165  OD2 ASP A 297      23.177  26.666   3.910  1.00 51.01           O  
ANISOU 2165  OD2 ASP A 297     6528   6494   6359   -129    125    188       O  
ATOM   2166  N   ASP A 298      28.311  27.337   3.782  1.00 46.51           N  
ANISOU 2166  N   ASP A 298     5944   5920   5807   -151    202    160       N  
ATOM   2167  CA  ASP A 298      29.722  26.976   3.956  1.00 49.51           C  
ANISOU 2167  CA  ASP A 298     6310   6297   6203   -154    225    149       C  
ATOM   2168  C   ASP A 298      30.425  27.563   5.184  1.00 48.16           C  
ANISOU 2168  C   ASP A 298     6121   6127   6052   -144    223    154       C  
ATOM   2169  O   ASP A 298      31.642  27.490   5.290  1.00 48.24           O  
ANISOU 2169  O   ASP A 298     6120   6133   6074   -148    241    147       O  
ATOM   2170  CB  ASP A 298      30.545  27.155   2.665  1.00 53.00           C  
ANISOU 2170  CB  ASP A 298     6769   6736   6630   -173    246    140       C  
ATOM   2171  CG  ASP A 298      30.546  28.580   2.141  1.00 59.73           C  
ANISOU 2171  CG  ASP A 298     7642   7588   7463   -183    242    149       C  
ATOM   2172  OD1 ASP A 298      30.505  29.534   2.942  1.00 63.58           O  
ANISOU 2172  OD1 ASP A 298     8123   8076   7957   -174    230    159       O  
ATOM   2173  OD2 ASP A 298      30.613  28.746   0.902  1.00 64.00           O  
ANISOU 2173  OD2 ASP A 298     8205   8127   7982   -200    251    145       O  
ATOM   2174  N   ILE A 299      29.670  28.110   6.128  1.00 47.94           N  
ANISOU 2174  N   ILE A 299     6086   6102   6026   -133    203    165       N  
ATOM   2175  CA  ILE A 299      30.297  28.540   7.370  1.00 51.07           C  
ANISOU 2175  CA  ILE A 299     6464   6499   6440   -124    201    168       C  
ATOM   2176  C   ILE A 299      30.691  27.358   8.272  1.00 54.50           C  
ANISOU 2176  C   ILE A 299     6875   6934   6898   -115    205    164       C  
ATOM   2177  O   ILE A 299      31.641  27.450   9.052  1.00 57.28           O  
ANISOU 2177  O   ILE A 299     7212   7284   7267   -112    210    163       O  
ATOM   2178  CB  ILE A 299      29.544  29.711   8.095  1.00 51.44           C  
ANISOU 2178  CB  ILE A 299     6513   6548   6482   -116    182    180       C  
ATOM   2179  CG1 ILE A 299      29.704  29.667   9.625  1.00 52.06           C  
ANISOU 2179  CG1 ILE A 299     6570   6630   6579   -104    175    183       C  
ATOM   2180  CG2 ILE A 299      28.082  29.800   7.711  1.00 50.42           C  
ANISOU 2180  CG2 ILE A 299     6396   6420   6338   -114    165    186       C  
ATOM   2181  CD1 ILE A 299      28.865  28.632  10.337  1.00 50.69           C  
ANISOU 2181  CD1 ILE A 299     6384   6461   6413    -94    164    184       C  
ATOM   2182  N   VAL A 300      29.990  26.234   8.133  1.00 56.10           N  
ANISOU 2182  N   VAL A 300     7075   7137   7101   -112    201    161       N  
ATOM   2183  CA  VAL A 300      30.317  25.023   8.896  1.00 53.10           C  
ANISOU 2183  CA  VAL A 300     6674   6758   6745   -106    203    158       C  
ATOM   2184  C   VAL A 300      31.631  24.402   8.427  1.00 52.90           C  
ANISOU 2184  C   VAL A 300     6640   6725   6734   -113    225    146       C  
ATOM   2185  O   VAL A 300      32.270  23.659   9.167  1.00 53.26           O  
ANISOU 2185  O   VAL A 300     6665   6768   6804   -108    227    144       O  
ATOM   2186  CB  VAL A 300      29.188  23.953   8.846  1.00 55.56           C  
ANISOU 2186  CB  VAL A 300     6983   7071   7053   -101    192    158       C  
ATOM   2187  CG1 VAL A 300      27.905  24.495   9.462  1.00 52.91           C  
ANISOU 2187  CG1 VAL A 300     6652   6742   6708    -92    171    170       C  
ATOM   2188  CG2 VAL A 300      28.948  23.428   7.427  1.00 55.08           C  
ANISOU 2188  CG2 VAL A 300     6939   7007   6979   -110    202    149       C  
ATOM   2189  N   LYS A 301      32.024  24.719   7.197  1.00 51.45           N  
ANISOU 2189  N   LYS A 301     6472   6537   6536   -125    240    138       N  
ATOM   2190  CA  LYS A 301      33.214  24.151   6.577  1.00 50.43           C  
ANISOU 2190  CA  LYS A 301     6338   6401   6420   -134    265    124       C  
ATOM   2191  C   LYS A 301      34.455  25.024   6.838  1.00 49.39           C  
ANISOU 2191  C   LYS A 301     6200   6266   6299   -138    275    123       C  
ATOM   2192  O   LYS A 301      35.546  24.741   6.337  1.00 51.12           O  
ANISOU 2192  O   LYS A 301     6414   6478   6530   -146    297    112       O  
ATOM   2193  CB  LYS A 301      32.937  23.914   5.077  1.00 54.66           C  
ANISOU 2193  CB  LYS A 301     6895   6936   6934   -148    277    114       C  
ATOM   2194  CG  LYS A 301      34.043  24.307   4.099  1.00 62.54           C  
ANISOU 2194  CG  LYS A 301     7902   7929   7928   -163    303    103       C  
ATOM   2195  CD  LYS A 301      33.536  24.486   2.666  1.00 66.29           C  
ANISOU 2195  CD  LYS A 301     8407   8406   8372   -179    310     98       C  
ATOM   2196  CE  LYS A 301      34.072  25.758   1.998  1.00 68.21           C  
ANISOU 2196  CE  LYS A 301     8669   8650   8598   -192    319    100       C  
ATOM   2197  NZ  LYS A 301      35.528  26.036   2.197  1.00 64.63           N  
ANISOU 2197  NZ  LYS A 301     8202   8191   8163   -196    340     92       N  
ATOM   2198  N   PHE A 302      34.288  26.060   7.655  1.00 48.47           N  
ANISOU 2198  N   PHE A 302     6084   6154   6179   -132    261    136       N  
ATOM   2199  CA  PHE A 302      35.339  27.042   7.912  1.00 49.98           C  
ANISOU 2199  CA  PHE A 302     6270   6340   6376   -135    268    137       C  
ATOM   2200  C   PHE A 302      36.503  26.426   8.670  1.00 50.49           C  
ANISOU 2200  C   PHE A 302     6310   6400   6474   -132    276    132       C  
ATOM   2201  O   PHE A 302      36.315  25.817   9.724  1.00 54.53           O  
ANISOU 2201  O   PHE A 302     6805   6913   7002   -122    263    138       O  
ATOM   2202  CB  PHE A 302      34.760  28.232   8.683  1.00 54.87           C  
ANISOU 2202  CB  PHE A 302     6895   6966   6986   -128    248    150       C  
ATOM   2203  CG  PHE A 302      35.665  29.435   8.735  1.00 59.80           C  
ANISOU 2203  CG  PHE A 302     7521   7587   7610   -133    255    153       C  
ATOM   2204  CD1 PHE A 302      36.098  30.057   7.560  1.00 59.67           C  
ANISOU 2204  CD1 PHE A 302     7523   7568   7580   -146    270    148       C  
ATOM   2205  CD2 PHE A 302      36.059  29.971   9.963  1.00 59.75           C  
ANISOU 2205  CD2 PHE A 302     7501   7581   7618   -125    245    159       C  
ATOM   2206  CE1 PHE A 302      36.923  31.171   7.611  1.00 60.33           C  
ANISOU 2206  CE1 PHE A 302     7608   7648   7665   -151    275    150       C  
ATOM   2207  CE2 PHE A 302      36.885  31.085  10.017  1.00 61.20           C  
ANISOU 2207  CE2 PHE A 302     7687   7762   7804   -130    250    161       C  
ATOM   2208  CZ  PHE A 302      37.317  31.685   8.842  1.00 62.54           C  
ANISOU 2208  CZ  PHE A 302     7873   7928   7961   -142    265    157       C  
ATOM   2209  N   HIS A 303      37.704  26.596   8.124  1.00 50.79           N  
ANISOU 2209  N   HIS A 303     6346   6430   6522   -141    297    123       N  
ATOM   2210  CA  HIS A 303      38.921  25.928   8.613  1.00 50.68           C  
ANISOU 2210  CA  HIS A 303     6306   6407   6542   -140    308    117       C  
ATOM   2211  C   HIS A 303      39.263  26.206  10.059  1.00 52.72           C  
ANISOU 2211  C   HIS A 303     6546   6665   6819   -130    291    128       C  
ATOM   2212  O   HIS A 303      39.925  25.392  10.707  1.00 54.28           O  
ANISOU 2212  O   HIS A 303     6720   6856   7046   -127    291    126       O  
ATOM   2213  CB  HIS A 303      40.108  26.291   7.728  1.00 47.88           C  
ANISOU 2213  CB  HIS A 303     5954   6045   6193   -153    334    105       C  
ATOM   2214  CG  HIS A 303      40.528  27.741   7.846  1.00 47.80           C  
ANISOU 2214  CG  HIS A 303     5952   6036   6173   -156    333    112       C  
ATOM   2215  ND1 HIS A 303      39.750  28.764   7.417  1.00 47.17           N  
ANISOU 2215  ND1 HIS A 303     5896   5963   6062   -159    325    120       N  
ATOM   2216  CD2 HIS A 303      41.677  28.320   8.382  1.00 45.57           C  
ANISOU 2216  CD2 HIS A 303     5656   5747   5911   -156    338    114       C  
ATOM   2217  CE1 HIS A 303      40.371  29.932   7.661  1.00 45.28           C  
ANISOU 2217  CE1 HIS A 303     5658   5722   5823   -161    325    125       C  
ATOM   2218  NE2 HIS A 303      41.551  29.660   8.250  1.00 44.32           N  
ANISOU 2218  NE2 HIS A 303     5514   5592   5732   -160    333    121       N  
ATOM   2219  N   CYS A 304      38.829  27.349  10.582  1.00 52.44           N  
ANISOU 2219  N   CYS A 304     6520   6637   6768   -127    276    139       N  
ATOM   2220  CA  CYS A 304      39.144  27.701  11.963  1.00 54.84           C  
ANISOU 2220  CA  CYS A 304     6808   6940   7086   -119    261    149       C  
ATOM   2221  C   CYS A 304      38.209  26.996  12.962  1.00 55.20           C  
ANISOU 2221  C   CYS A 304     6846   6993   7133   -110    240    157       C  
ATOM   2222  O   CYS A 304      38.317  27.205  14.170  1.00 60.44           O  
ANISOU 2222  O   CYS A 304     7498   7659   7806   -104    225    166       O  
ATOM   2223  CB  CYS A 304      39.214  29.237  12.155  1.00 59.73           C  
ANISOU 2223  CB  CYS A 304     7440   7564   7691   -121    255    156       C  
ATOM   2224  SG  CYS A 304      40.488  30.004  11.093  1.00 67.65           S  
ANISOU 2224  SG  CYS A 304     8449   8558   8696   -134    280    147       S  
ATOM   2225  N   LEU A 305      37.321  26.136  12.452  1.00 49.14           N  
ANISOU 2225  N   LEU A 305     6084   6228   6357   -108    239    154       N  
ATOM   2226  CA  LEU A 305      36.469  25.283  13.292  1.00 45.15           C  
ANISOU 2226  CA  LEU A 305     5570   5728   5856   -100    222    161       C  
ATOM   2227  C   LEU A 305      36.925  23.825  13.266  1.00 44.70           C  
ANISOU 2227  C   LEU A 305     5494   5664   5824   -100    228    154       C  
ATOM   2228  O   LEU A 305      36.209  22.934  13.734  1.00 43.12           O  
ANISOU 2228  O   LEU A 305     5288   5467   5628    -94    216    159       O  
ATOM   2229  CB  LEU A 305      35.008  25.347  12.844  1.00 44.66           C  
ANISOU 2229  CB  LEU A 305     5525   5674   5767    -97    214    163       C  
ATOM   2230  CG  LEU A 305      34.311  26.697  12.658  1.00 45.46           C  
ANISOU 2230  CG  LEU A 305     5646   5782   5843    -97    207    168       C  
ATOM   2231  CD1 LEU A 305      32.925  26.460  12.084  1.00 44.14           C  
ANISOU 2231  CD1 LEU A 305     5494   5621   5656    -95    199    169       C  
ATOM   2232  CD2 LEU A 305      34.238  27.506  13.951  1.00 44.60           C  
ANISOU 2232  CD2 LEU A 305     5531   5678   5735    -92    192    178       C  
ATOM   2233  N   ALA A 306      38.117  23.589  12.722  1.00 43.33           N  
ANISOU 2233  N   ALA A 306     5312   5479   5670   -106    246    144       N  
ATOM   2234  CA  ALA A 306      38.646  22.244  12.563  1.00 40.53           C  
ANISOU 2234  CA  ALA A 306     4939   5115   5344   -107    255    136       C  
ATOM   2235  C   ALA A 306      38.884  21.546  13.902  1.00 39.52           C  
ANISOU 2235  C   ALA A 306     4788   4984   5242   -101    237    146       C  
ATOM   2236  O   ALA A 306      38.552  20.373  14.063  1.00 37.60           O  
ANISOU 2236  O   ALA A 306     4535   4739   5013    -98    231    146       O  
ATOM   2237  CB  ALA A 306      39.927  22.280  11.748  1.00 39.53           C  
ANISOU 2237  CB  ALA A 306     4807   4976   5234   -115    280    122       C  
ATOM   2238  N   ASN A 307      39.458  22.275  14.854  1.00 39.65           N  
ANISOU 2238  N   ASN A 307     4797   5000   5265   -100    227    155       N  
ATOM   2239  CA  ASN A 307      39.858  21.697  16.133  1.00 38.76           C  
ANISOU 2239  CA  ASN A 307     4662   4884   5178    -97    209    166       C  
ATOM   2240  C   ASN A 307      38.769  21.790  17.194  1.00 35.99           C  
ANISOU 2240  C   ASN A 307     4317   4547   4810    -91    185    180       C  
ATOM   2241  O   ASN A 307      38.959  21.358  18.325  1.00 37.27           O  
ANISOU 2241  O   ASN A 307     4464   4708   4988    -90    169    190       O  
ATOM   2242  CB  ASN A 307      41.192  22.297  16.625  1.00 41.36           C  
ANISOU 2242  CB  ASN A 307     4980   5205   5529   -101    211    168       C  
ATOM   2243  CG  ASN A 307      42.384  21.904  15.736  1.00 46.26           C  
ANISOU 2243  CG  ASN A 307     5589   5810   6177   -106    234    154       C  
ATOM   2244  OD1 ASN A 307      42.200  21.383  14.627  1.00 45.94           O  
ANISOU 2244  OD1 ASN A 307     5553   5766   6133   -108    252    140       O  
ATOM   2245  ND2 ASN A 307      43.615  22.162  16.218  1.00 45.11           N  
ANISOU 2245  ND2 ASN A 307     5426   5654   6059   -109    234    155       N  
ATOM   2246  N   VAL A 308      37.620  22.337  16.826  1.00 32.99           N  
ANISOU 2246  N   VAL A 308     3957   4178   4397    -89    184    180       N  
ATOM   2247  CA  VAL A 308      36.507  22.440  17.770  1.00 31.96           C  
ANISOU 2247  CA  VAL A 308     3832   4060   4251    -84    164    192       C  
ATOM   2248  C   VAL A 308      36.018  21.043  18.171  1.00 30.64           C  
ANISOU 2248  C   VAL A 308     3652   3893   4096    -81    154    196       C  
ATOM   2249  O   VAL A 308      35.897  20.160  17.326  1.00 30.37           O  
ANISOU 2249  O   VAL A 308     3615   3852   4068    -81    164    187       O  
ATOM   2250  CB  VAL A 308      35.367  23.332  17.208  1.00 30.19           C  
ANISOU 2250  CB  VAL A 308     3631   3846   3993    -82    165    190       C  
ATOM   2251  CG1 VAL A 308      34.062  23.105  17.941  1.00 28.70           C  
ANISOU 2251  CG1 VAL A 308     3445   3668   3789    -77    148    199       C  
ATOM   2252  CG2 VAL A 308      35.775  24.788  17.302  1.00 30.02           C  
ANISOU 2252  CG2 VAL A 308     3618   3826   3960    -84    167    191       C  
ATOM   2253  N   SER A 309      35.762  20.840  19.458  1.00 30.20           N  
ANISOU 2253  N   SER A 309     3588   3842   4043    -80    135    208       N  
ATOM   2254  CA  SER A 309      35.357  19.524  19.932  1.00 31.12           C  
ANISOU 2254  CA  SER A 309     3692   3959   4173    -79    124    214       C  
ATOM   2255  C   SER A 309      33.840  19.298  19.907  1.00 30.65           C  
ANISOU 2255  C   SER A 309     3644   3911   4091    -74    117    216       C  
ATOM   2256  O   SER A 309      33.404  18.209  19.587  1.00 32.05           O  
ANISOU 2256  O   SER A 309     3816   4085   4276    -72    116    215       O  
ATOM   2257  CB  SER A 309      35.916  19.244  21.320  1.00 31.84           C  
ANISOU 2257  CB  SER A 309     3767   4048   4282    -82    105    227       C  
ATOM   2258  OG  SER A 309      34.864  19.258  22.259  1.00 35.06           O  
ANISOU 2258  OG  SER A 309     4180   4470   4671    -81     89    238       O  
ATOM   2259  N   ALA A 310      33.042  20.304  20.265  1.00 30.16           N  
ANISOU 2259  N   ALA A 310     3596   3860   4002    -72    111    220       N  
ATOM   2260  CA  ALA A 310      31.580  20.229  20.068  1.00 29.52           C  
ANISOU 2260  CA  ALA A 310     3526   3788   3899    -68    107    220       C  
ATOM   2261  C   ALA A 310      31.073  21.355  19.177  1.00 29.48           C  
ANISOU 2261  C   ALA A 310     3542   3787   3872    -66    117    213       C  
ATOM   2262  O   ALA A 310      31.326  22.528  19.445  1.00 30.40           O  
ANISOU 2262  O   ALA A 310     3665   3906   3979    -67    117    214       O  
ATOM   2263  CB  ALA A 310      30.839  20.222  21.393  1.00 28.39           C  
ANISOU 2263  CB  ALA A 310     3381   3656   3748    -68     90    232       C  
ATOM   2264  N   MET A 311      30.365  20.986  18.116  1.00 29.55           N  
ANISOU 2264  N   MET A 311     3560   3794   3872    -64    123    207       N  
ATOM   2265  CA  MET A 311      29.814  21.940  17.164  1.00 30.94           C  
ANISOU 2265  CA  MET A 311     3756   3973   4027    -64    130    201       C  
ATOM   2266  C   MET A 311      28.291  21.928  17.247  1.00 31.20           C  
ANISOU 2266  C   MET A 311     3797   4013   4043    -59    119    205       C  
ATOM   2267  O   MET A 311      27.668  20.864  17.326  1.00 30.70           O  
ANISOU 2267  O   MET A 311     3728   3952   3985    -56    114    207       O  
ATOM   2268  CB  MET A 311      30.285  21.584  15.749  1.00 33.19           C  
ANISOU 2268  CB  MET A 311     4046   4248   4314    -68    146    190       C  
ATOM   2269  CG  MET A 311      29.687  22.410  14.620  1.00 34.78           C  
ANISOU 2269  CG  MET A 311     4270   4451   4493    -69    152    186       C  
ATOM   2270  SD  MET A 311      30.114  24.166  14.675  1.00 38.74           S  
ANISOU 2270  SD  MET A 311     4782   4954   4981    -72    154    187       S  
ATOM   2271  CE  MET A 311      31.832  24.095  15.176  1.00 36.50           C  
ANISOU 2271  CE  MET A 311     4482   4663   4722    -76    163    186       C  
ATOM   2272  N   SER A 312      27.684  23.109  17.218  1.00 31.57           N  
ANISOU 2272  N   SER A 312     3857   4065   4073    -57    116    206       N  
ATOM   2273  CA  SER A 312      26.240  23.194  17.415  1.00 31.47           C  
ANISOU 2273  CA  SER A 312     3849   4059   4048    -53    106    209       C  
ATOM   2274  C   SER A 312      25.539  24.273  16.578  1.00 30.58           C  
ANISOU 2274  C   SER A 312     3754   3946   3917    -52    107    207       C  
ATOM   2275  O   SER A 312      26.037  25.387  16.436  1.00 30.72           O  
ANISOU 2275  O   SER A 312     3780   3962   3930    -54    111    206       O  
ATOM   2276  CB  SER A 312      25.951  23.390  18.896  1.00 31.56           C  
ANISOU 2276  CB  SER A 312     3851   4078   4059    -51     96    216       C  
ATOM   2277  OG  SER A 312      24.573  23.327  19.144  1.00 33.44           O  
ANISOU 2277  OG  SER A 312     4092   4323   4289    -46     87    219       O  
ATOM   2278  N   LEU A 313      24.381  23.925  16.026  1.00 28.63           N  
ANISOU 2278  N   LEU A 313     3514   3700   3663    -49    101    207       N  
ATOM   2279  CA  LEU A 313      23.575  24.868  15.267  1.00 27.61           C  
ANISOU 2279  CA  LEU A 313     3401   3569   3520    -49     98    206       C  
ATOM   2280  C   LEU A 313      22.114  24.810  15.706  1.00 27.05           C  
ANISOU 2280  C   LEU A 313     3329   3503   3445    -43     86    210       C  
ATOM   2281  O   LEU A 313      21.513  23.745  15.718  1.00 26.93           O  
ANISOU 2281  O   LEU A 313     3308   3489   3434    -40     82    212       O  
ATOM   2282  CB  LEU A 313      23.680  24.589  13.759  1.00 28.22           C  
ANISOU 2282  CB  LEU A 313     3492   3640   3590    -54    105    202       C  
ATOM   2283  CG  LEU A 313      25.038  24.572  13.043  1.00 28.11           C  
ANISOU 2283  CG  LEU A 313     3481   3620   3579    -62    120    195       C  
ATOM   2284  CD1 LEU A 313      24.839  24.030  11.642  1.00 28.38           C  
ANISOU 2284  CD1 LEU A 313     3528   3649   3604    -67    126    190       C  
ATOM   2285  CD2 LEU A 313      25.687  25.950  12.986  1.00 28.14           C  
ANISOU 2285  CD2 LEU A 313     3493   3622   3576    -65    124    196       C  
ATOM   2286  N   ALA A 314      21.546  25.963  16.047  1.00 26.75           N  
ANISOU 2286  N   ALA A 314     3295   3466   3401    -40     80    212       N  
ATOM   2287  CA  ALA A 314      20.164  26.039  16.474  1.00 26.79           C  
ANISOU 2287  CA  ALA A 314     3297   3474   3405    -35     69    214       C  
ATOM   2288  C   ALA A 314      19.465  27.232  15.844  1.00 27.57           C  
ANISOU 2288  C   ALA A 314     3409   3568   3498    -34     64    215       C  
ATOM   2289  O   ALA A 314      19.935  28.364  15.975  1.00 27.52           O  
ANISOU 2289  O   ALA A 314     3407   3560   3490    -35     66    214       O  
ATOM   2290  CB  ALA A 314      20.087  26.129  17.991  1.00 26.92           C  
ANISOU 2290  CB  ALA A 314     3300   3498   3427    -32     68    216       C  
ATOM   2291  N   GLY A 315      18.336  26.967  15.181  1.00 27.67           N  
ANISOU 2291  N   GLY A 315     3427   3577   3508    -32     55    216       N  
ATOM   2292  CA  GLY A 315      17.497  27.989  14.553  1.00 28.00           C  
ANISOU 2292  CA  GLY A 315     3479   3612   3546    -31     46    218       C  
ATOM   2293  C   GLY A 315      18.027  28.497  13.221  1.00 30.05           C  
ANISOU 2293  C   GLY A 315     3756   3863   3795    -38     47    218       C  
ATOM   2294  O   GLY A 315      17.550  29.505  12.697  1.00 31.13           O  
ANISOU 2294  O   GLY A 315     3903   3994   3930    -40     39    221       O  
ATOM   2295  N   VAL A 316      18.987  27.773  12.654  1.00 29.99           N  
ANISOU 2295  N   VAL A 316     3752   3856   3784    -44     58    216       N  
ATOM   2296  CA  VAL A 316      19.826  28.281  11.577  1.00 30.66           C  
ANISOU 2296  CA  VAL A 316     3853   3936   3858    -53     64    215       C  
ATOM   2297  C   VAL A 316      19.284  28.005  10.155  1.00 31.42           C  
ANISOU 2297  C   VAL A 316     3966   4026   3943    -60     59    216       C  
ATOM   2298  O   VAL A 316      18.740  26.927   9.892  1.00 31.72           O  
ANISOU 2298  O   VAL A 316     4003   4066   3982    -59     56    215       O  
ATOM   2299  CB  VAL A 316      21.256  27.724  11.773  1.00 30.76           C  
ANISOU 2299  CB  VAL A 316     3860   3952   3875    -57     81    210       C  
ATOM   2300  CG1 VAL A 316      22.133  27.986  10.560  1.00 29.72           C  
ANISOU 2300  CG1 VAL A 316     3744   3815   3734    -68     91    207       C  
ATOM   2301  CG2 VAL A 316      21.880  28.290  13.050  1.00 28.64           C  
ANISOU 2301  CG2 VAL A 316     3578   3687   3615    -53     84    210       C  
ATOM   2302  N   SER A 317      19.447  28.977   9.248  1.00 32.23           N  
ANISOU 2302  N   SER A 317     4085   4122   4035    -68     57    219       N  
ATOM   2303  CA  SER A 317      18.974  28.874   7.848  1.00 33.12           C  
ANISOU 2303  CA  SER A 317     4218   4230   4135    -77     50    221       C  
ATOM   2304  C   SER A 317      19.710  27.840   7.000  1.00 33.61           C  
ANISOU 2304  C   SER A 317     4288   4293   4188    -86     64    215       C  
ATOM   2305  O   SER A 317      19.463  27.763   5.799  1.00 37.73           O  
ANISOU 2305  O   SER A 317     4828   4811   4695    -97     61    216       O  
ATOM   2306  CB  SER A 317      19.089  30.217   7.091  1.00 34.88           C  
ANISOU 2306  CB  SER A 317     4458   4445   4347    -86     45    227       C  
ATOM   2307  OG  SER A 317      18.635  31.338   7.831  1.00 39.19           O  
ANISOU 2307  OG  SER A 317     4997   4989   4903    -78     34    232       O  
ATOM   2308  N   ILE A 318      20.614  27.067   7.588  1.00 32.55           N  
ANISOU 2308  N   ILE A 318     4140   4163   4062    -84     80    208       N  
ATOM   2309  CA  ILE A 318      21.417  26.099   6.830  1.00 31.86           C  
ANISOU 2309  CA  ILE A 318     4057   4076   3970    -92     95    199       C  
ATOM   2310  C   ILE A 318      20.532  25.150   6.021  1.00 31.15           C  
ANISOU 2310  C   ILE A 318     3976   3985   3874    -95     88    198       C  
ATOM   2311  O   ILE A 318      19.562  24.632   6.548  1.00 31.73           O  
ANISOU 2311  O   ILE A 318     4039   4059   3955    -86     76    201       O  
ATOM   2312  CB  ILE A 318      22.360  25.316   7.768  1.00 31.79           C  
ANISOU 2312  CB  ILE A 318     4028   4071   3979    -87    109    193       C  
ATOM   2313  CG1 ILE A 318      23.272  24.370   6.967  1.00 32.07           C  
ANISOU 2313  CG1 ILE A 318     4067   4105   4014    -96    127    182       C  
ATOM   2314  CG2 ILE A 318      21.564  24.627   8.879  1.00 30.42           C  
ANISOU 2314  CG2 ILE A 318     3836   3902   3819    -74     98    196       C  
ATOM   2315  CD1 ILE A 318      24.462  23.847   7.738  1.00 31.74           C  
ANISOU 2315  CD1 ILE A 318     4005   4063   3990    -93    141    176       C  
ATOM   2316  N   LYS A 319      20.863  24.936   4.745  1.00 31.91           N  
ANISOU 2316  N   LYS A 319     4090   4078   3955   -109     96    193       N  
ATOM   2317  CA  LYS A 319      20.031  24.106   3.843  1.00 32.47           C  
ANISOU 2317  CA  LYS A 319     4172   4146   4016   -115     89    191       C  
ATOM   2318  C   LYS A 319      20.733  22.826   3.414  1.00 31.91           C  
ANISOU 2318  C   LYS A 319     4099   4076   3948   -120    107    178       C  
ATOM   2319  O   LYS A 319      20.082  21.826   3.102  1.00 30.25           O  
ANISOU 2319  O   LYS A 319     3890   3866   3738   -120    102    175       O  
ATOM   2320  CB  LYS A 319      19.628  24.875   2.572  1.00 33.19           C  
ANISOU 2320  CB  LYS A 319     4292   4234   4085   -129     80    196       C  
ATOM   2321  CG  LYS A 319      19.022  26.250   2.773  1.00 33.21           C  
ANISOU 2321  CG  LYS A 319     4299   4233   4086   -126     63    209       C  
ATOM   2322  CD  LYS A 319      17.679  26.174   3.485  1.00 35.44           C  
ANISOU 2322  CD  LYS A 319     4570   4515   4381   -113     42    217       C  
ATOM   2323  CE  LYS A 319      16.836  27.396   3.173  1.00 35.72           C  
ANISOU 2323  CE  LYS A 319     4616   4543   4411   -115     21    229       C  
ATOM   2324  NZ  LYS A 319      17.680  28.618   3.238  1.00 37.06           N  
ANISOU 2324  NZ  LYS A 319     4791   4712   4578   -119     27    231       N  
ATOM   2325  N   TYR A 320      22.061  22.884   3.365  1.00 32.34           N  
ANISOU 2325  N   TYR A 320     4151   4131   4005   -125    128    170       N  
ATOM   2326  CA  TYR A 320      22.884  21.729   3.030  1.00 33.78           C  
ANISOU 2326  CA  TYR A 320     4327   4312   4194   -130    148    156       C  
ATOM   2327  C   TYR A 320      24.099  21.689   3.925  1.00 35.60           C  
ANISOU 2327  C   TYR A 320     4538   4543   4445   -125    163    151       C  
ATOM   2328  O   TYR A 320      24.828  22.673   4.045  1.00 38.09           O  
ANISOU 2328  O   TYR A 320     4855   4858   4758   -127    169    153       O  
ATOM   2329  CB  TYR A 320      23.339  21.760   1.569  1.00 32.48           C  
ANISOU 2329  CB  TYR A 320     4187   4144   4009   -149    162    146       C  
ATOM   2330  CG  TYR A 320      22.222  21.755   0.568  1.00 32.85           C  
ANISOU 2330  CG  TYR A 320     4256   4190   4034   -158    147    151       C  
ATOM   2331  CD1 TYR A 320      21.716  22.946   0.061  1.00 32.86           C  
ANISOU 2331  CD1 TYR A 320     4278   4191   4017   -165    133    162       C  
ATOM   2332  CD2 TYR A 320      21.667  20.559   0.122  1.00 33.70           C  
ANISOU 2332  CD2 TYR A 320     4365   4297   4141   -160    145    144       C  
ATOM   2333  CE1 TYR A 320      20.687  22.955  -0.860  1.00 33.99           C  
ANISOU 2333  CE1 TYR A 320     4441   4331   4140   -174    116    167       C  
ATOM   2334  CE2 TYR A 320      20.634  20.553  -0.802  1.00 34.56           C  
ANISOU 2334  CE2 TYR A 320     4496   4405   4231   -169    130    148       C  
ATOM   2335  CZ  TYR A 320      20.153  21.759  -1.293  1.00 35.40           C  
ANISOU 2335  CZ  TYR A 320     4621   4509   4317   -176    115    160       C  
ATOM   2336  OH  TYR A 320      19.126  21.774  -2.210  1.00 37.19           O  
ANISOU 2336  OH  TYR A 320     4870   4733   4526   -186     97    166       O  
ATOM   2337  N   LEU A 321      24.305  20.544   4.560  1.00 37.63           N  
ANISOU 2337  N   LEU A 321     4774   4800   4722   -117    167    146       N  
ATOM   2338  CA  LEU A 321      25.512  20.290   5.316  1.00 39.26           C  
ANISOU 2338  CA  LEU A 321     4961   5005   4950   -113    181    141       C  
ATOM   2339  C   LEU A 321      26.215  19.154   4.591  1.00 41.91           C  
ANISOU 2339  C   LEU A 321     5293   5335   5294   -121    200    125       C  
ATOM   2340  O   LEU A 321      25.887  17.987   4.791  1.00 41.73           O  
ANISOU 2340  O   LEU A 321     5259   5311   5284   -116    197    121       O  
ATOM   2341  CB  LEU A 321      25.174  19.904   6.762  1.00 37.76           C  
ANISOU 2341  CB  LEU A 321     4748   4818   4780    -98    167    149       C  
ATOM   2342  CG  LEU A 321      26.183  20.232   7.864  1.00 37.40           C  
ANISOU 2342  CG  LEU A 321     4683   4772   4752    -93    172    152       C  
ATOM   2343  CD1 LEU A 321      25.728  19.673   9.196  1.00 37.62           C  
ANISOU 2343  CD1 LEU A 321     4691   4804   4796    -81    158    160       C  
ATOM   2344  CD2 LEU A 321      27.561  19.689   7.551  1.00 38.64           C  
ANISOU 2344  CD2 LEU A 321     4832   4924   4925    -99    193    140       C  
ATOM   2345  N   GLU A 322      27.169  19.501   3.731  1.00 46.25           N  
ANISOU 2345  N   GLU A 322     5854   5882   5837   -134    220    115       N  
ATOM   2346  CA  GLU A 322      27.816  18.503   2.884  1.00 51.33           C  
ANISOU 2346  CA  GLU A 322     6498   6520   6486   -143    241     97       C  
ATOM   2347  C   GLU A 322      29.319  18.718   2.703  1.00 53.38           C  
ANISOU 2347  C   GLU A 322     6751   6774   6757   -151    266     86       C  
ATOM   2348  O   GLU A 322      30.050  17.794   2.316  1.00 56.01           O  
ANISOU 2348  O   GLU A 322     7075   7101   7105   -156    285     70       O  
ATOM   2349  CB  GLU A 322      27.106  18.398   1.516  1.00 53.11           C  
ANISOU 2349  CB  GLU A 322     6750   6745   6683   -157    242     91       C  
ATOM   2350  CG  GLU A 322      27.126  19.668   0.668  1.00 54.07           C  
ANISOU 2350  CG  GLU A 322     6898   6869   6776   -170    243     95       C  
ATOM   2351  CD  GLU A 322      26.134  19.641  -0.490  1.00 56.65           C  
ANISOU 2351  CD  GLU A 322     7252   7197   7074   -182    234     96       C  
ATOM   2352  OE1 GLU A 322      26.295  20.451  -1.427  1.00 59.85           O  
ANISOU 2352  OE1 GLU A 322     7681   7603   7453   -198    240     96       O  
ATOM   2353  OE2 GLU A 322      25.185  18.827  -0.473  1.00 56.25           O  
ANISOU 2353  OE2 GLU A 322     7200   7146   7024   -177    221     97       O  
ATOM   2354  N   ASP A 323      29.785  19.925   2.997  1.00 53.62           N  
ANISOU 2354  N   ASP A 323     6784   6806   6781   -152    266     93       N  
ATOM   2355  CA  ASP A 323      31.167  20.295   2.659  1.00 58.87           C  
ANISOU 2355  CA  ASP A 323     7447   7466   7453   -161    290     83       C  
ATOM   2356  C   ASP A 323      32.257  19.562   3.468  1.00 51.26           C  
ANISOU 2356  C   ASP A 323     6453   6495   6526   -154    301     76       C  
ATOM   2357  O   ASP A 323      33.340  19.326   2.960  1.00 52.13           O  
ANISOU 2357  O   ASP A 323     6559   6599   6648   -163    325     61       O  
ATOM   2358  CB  ASP A 323      31.379  21.812   2.832  1.00 69.92           C  
ANISOU 2358  CB  ASP A 323     8857   8869   8839   -163    285     94       C  
ATOM   2359  CG  ASP A 323      30.203  22.654   2.333  1.00 76.91           C  
ANISOU 2359  CG  ASP A 323     9768   9761   9694   -167    267    106       C  
ATOM   2360  OD1 ASP A 323      29.434  23.163   3.185  1.00 80.06           O  
ANISOU 2360  OD1 ASP A 323    10162  10163  10093   -155    245    121       O  
ATOM   2361  OD2 ASP A 323      30.062  22.823   1.099  1.00 80.37           O  
ANISOU 2361  OD2 ASP A 323    10229  10198  10107   -182    275    101       O  
ATOM   2362  N   VAL A 324      31.932  19.191   4.704  1.00 44.86           N  
ANISOU 2362  N   VAL A 324     5623   5687   5735   -139    283     86       N  
ATOM   2363  CA  VAL A 324      32.892  19.089   5.807  1.00 40.73           C  
ANISOU 2363  CA  VAL A 324     5073   5159   5243   -131    284     89       C  
ATOM   2364  C   VAL A 324      34.184  18.334   5.520  1.00 39.99           C  
ANISOU 2364  C   VAL A 324     4963   5054   5177   -137    308     72       C  
ATOM   2365  O   VAL A 324      34.150  17.155   5.192  1.00 40.73           O  
ANISOU 2365  O   VAL A 324     5048   5142   5284   -138    315     61       O  
ATOM   2366  CB  VAL A 324      32.244  18.504   7.076  1.00 39.54           C  
ANISOU 2366  CB  VAL A 324     4904   5011   5107   -117    261    101       C  
ATOM   2367  CG1 VAL A 324      33.065  18.866   8.294  1.00 37.46           C  
ANISOU 2367  CG1 VAL A 324     4621   4746   4866   -110    256    110       C  
ATOM   2368  CG2 VAL A 324      30.832  19.034   7.249  1.00 39.09           C  
ANISOU 2368  CG2 VAL A 324     4862   4963   5024   -112    240    115       C  
ATOM   2369  N   PRO A 325      35.333  19.021   5.657  1.00 38.37           N  
ANISOU 2369  N   PRO A 325     4751   4844   4982   -141    321     70       N  
ATOM   2370  CA  PRO A 325      36.615  18.364   5.466  1.00 38.06           C  
ANISOU 2370  CA  PRO A 325     4693   4793   4974   -146    343     55       C  
ATOM   2371  C   PRO A 325      36.785  17.200   6.438  1.00 38.30           C  
ANISOU 2371  C   PRO A 325     4693   4816   5040   -135    333     57       C  
ATOM   2372  O   PRO A 325      36.467  17.315   7.617  1.00 40.89           O  
ANISOU 2372  O   PRO A 325     5011   5148   5375   -124    311     73       O  
ATOM   2373  CB  PRO A 325      37.626  19.476   5.765  1.00 36.52           C  
ANISOU 2373  CB  PRO A 325     4495   4596   4784   -148    350     58       C  
ATOM   2374  CG  PRO A 325      36.874  20.735   5.522  1.00 35.43           C  
ANISOU 2374  CG  PRO A 325     4383   4469   4608   -151    340     70       C  
ATOM   2375  CD  PRO A 325      35.500  20.443   6.003  1.00 36.65           C  
ANISOU 2375  CD  PRO A 325     4542   4631   4749   -141    314     82       C  
ATOM   2376  N   LYS A 326      37.295  16.090   5.932  1.00 38.84           N  
ANISOU 2376  N   LYS A 326     4750   4874   5132   -139    350     40       N  
ATOM   2377  CA  LYS A 326      37.383  14.857   6.689  1.00 39.06           C  
ANISOU 2377  CA  LYS A 326     4750   4893   5195   -130    341     40       C  
ATOM   2378  C   LYS A 326      38.441  14.885   7.804  1.00 37.32           C  
ANISOU 2378  C   LYS A 326     4502   4665   5012   -124    335     48       C  
ATOM   2379  O   LYS A 326      38.594  13.915   8.543  1.00 36.90           O  
ANISOU 2379  O   LYS A 326     4425   4603   4990   -118    324     51       O  
ATOM   2380  CB  LYS A 326      37.617  13.692   5.722  1.00 43.33           C  
ANISOU 2380  CB  LYS A 326     5286   5424   5751   -137    362     18       C  
ATOM   2381  CG  LYS A 326      36.631  13.652   4.552  1.00 47.67           C  
ANISOU 2381  CG  LYS A 326     5865   5982   6264   -145    368     10       C  
ATOM   2382  CD  LYS A 326      37.121  12.776   3.402  1.00 51.40           C  
ANISOU 2382  CD  LYS A 326     6337   6445   6748   -156    397    -15       C  
ATOM   2383  CE  LYS A 326      36.903  11.296   3.697  1.00 55.26           C  
ANISOU 2383  CE  LYS A 326     6804   6924   7267   -149    391    -21       C  
ATOM   2384  NZ  LYS A 326      37.603  10.404   2.727  1.00 57.53           N  
ANISOU 2384  NZ  LYS A 326     7084   7199   7575   -159    421    -49       N  
ATOM   2385  N   HIS A 327      39.149  16.003   7.946  1.00 37.26           N  
ANISOU 2385  N   HIS A 327     4498   4657   4999   -128    341     51       N  
ATOM   2386  CA  HIS A 327      40.153  16.148   9.012  1.00 36.84           C  
ANISOU 2386  CA  HIS A 327     4421   4597   4979   -123    333     60       C  
ATOM   2387  C   HIS A 327      39.664  16.900  10.233  1.00 36.10           C  
ANISOU 2387  C   HIS A 327     4328   4513   4872   -115    306     82       C  
ATOM   2388  O   HIS A 327      40.406  17.055  11.205  1.00 34.38           O  
ANISOU 2388  O   HIS A 327     4092   4290   4679   -112    296     91       O  
ATOM   2389  CB  HIS A 327      41.434  16.776   8.476  1.00 36.30           C  
ANISOU 2389  CB  HIS A 327     4349   4520   4922   -132    358     48       C  
ATOM   2390  CG  HIS A 327      41.326  18.263   8.208  1.00 36.85           C  
ANISOU 2390  CG  HIS A 327     4443   4600   4956   -137    360     54       C  
ATOM   2391  ND1 HIS A 327      40.966  18.763   7.003  1.00 36.75           N  
ANISOU 2391  ND1 HIS A 327     4457   4594   4911   -147    377     44       N  
ATOM   2392  CD2 HIS A 327      41.556  19.360   9.039  1.00 36.21           C  
ANISOU 2392  CD2 HIS A 327     4363   4524   4870   -133    347     69       C  
ATOM   2393  CE1 HIS A 327      40.964  20.104   7.063  1.00 36.17           C  
ANISOU 2393  CE1 HIS A 327     4399   4528   4814   -149    373     54       C  
ATOM   2394  NE2 HIS A 327      41.325  20.469   8.311  1.00 36.82           N  
ANISOU 2394  NE2 HIS A 327     4465   4609   4913   -140    355     68       N  
ATOM   2395  N   PHE A 328      38.421  17.378  10.188  1.00 35.76           N  
ANISOU 2395  N   PHE A 328     4308   4485   4794   -112    293     91       N  
ATOM   2396  CA  PHE A 328      37.810  18.062  11.331  1.00 36.43           C  
ANISOU 2396  CA  PHE A 328     4396   4581   4865   -105    267    111       C  
ATOM   2397  C   PHE A 328      37.682  17.121  12.540  1.00 35.19           C  
ANISOU 2397  C   PHE A 328     4216   4421   4733    -97    247    122       C  
ATOM   2398  O   PHE A 328      37.430  15.932  12.396  1.00 34.42           O  
ANISOU 2398  O   PHE A 328     4108   4318   4650    -95    246    118       O  
ATOM   2399  CB  PHE A 328      36.443  18.659  10.950  1.00 37.42           C  
ANISOU 2399  CB  PHE A 328     4548   4720   4950   -103    259    116       C  
ATOM   2400  CG  PHE A 328      36.513  19.990  10.227  1.00 38.12           C  
ANISOU 2400  CG  PHE A 328     4658   4813   5011   -110    269    114       C  
ATOM   2401  CD1 PHE A 328      35.422  20.864  10.260  1.00 37.44           C  
ANISOU 2401  CD1 PHE A 328     4593   4739   4894   -107    256    124       C  
ATOM   2402  CD2 PHE A 328      37.656  20.381   9.511  1.00 38.62           C  
ANISOU 2402  CD2 PHE A 328     4723   4869   5082   -119    292    103       C  
ATOM   2403  CE1 PHE A 328      35.467  22.087   9.593  1.00 37.29           C  
ANISOU 2403  CE1 PHE A 328     4593   4723   4851   -114    263    123       C  
ATOM   2404  CE2 PHE A 328      37.704  21.605   8.843  1.00 36.70           C  
ANISOU 2404  CE2 PHE A 328     4500   4630   4813   -126    300    102       C  
ATOM   2405  CZ  PHE A 328      36.609  22.456   8.884  1.00 36.67           C  
ANISOU 2405  CZ  PHE A 328     4517   4638   4779   -124    285    113       C  
ATOM   2406  N   LYS A 329      37.852  17.678  13.730  1.00 36.08           N  
ANISOU 2406  N   LYS A 329     4322   4538   4849    -93    229    137       N  
ATOM   2407  CA  LYS A 329      37.975  16.892  14.951  1.00 35.32           C  
ANISOU 2407  CA  LYS A 329     4204   4438   4778    -89    209    149       C  
ATOM   2408  C   LYS A 329      36.689  16.782  15.756  1.00 33.19           C  
ANISOU 2408  C   LYS A 329     3940   4182   4488    -83    187    164       C  
ATOM   2409  O   LYS A 329      36.692  16.173  16.822  1.00 33.14           O  
ANISOU 2409  O   LYS A 329     3918   4175   4499    -81    169    175       O  
ATOM   2410  CB  LYS A 329      39.056  17.491  15.853  1.00 36.81           C  
ANISOU 2410  CB  LYS A 329     4379   4621   4984    -91    203    157       C  
ATOM   2411  CG  LYS A 329      40.308  17.932  15.133  1.00 39.31           C  
ANISOU 2411  CG  LYS A 329     4691   4926   5316    -97    225    145       C  
ATOM   2412  CD  LYS A 329      41.415  16.911  15.240  1.00 41.46           C  
ANISOU 2412  CD  LYS A 329     4936   5181   5635    -98    230    139       C  
ATOM   2413  CE  LYS A 329      42.760  17.575  14.983  1.00 42.62           C  
ANISOU 2413  CE  LYS A 329     5074   5316   5800   -104    246    132       C  
ATOM   2414  NZ  LYS A 329      43.841  16.728  15.556  1.00 46.61           N  
ANISOU 2414  NZ  LYS A 329     5549   5804   6355   -105    242    133       N  
ATOM   2415  N   TRP A 330      35.601  17.369  15.258  1.00 32.47           N  
ANISOU 2415  N   TRP A 330     3871   4101   4362    -82    187    163       N  
ATOM   2416  CA  TRP A 330      34.330  17.427  16.000  1.00 30.69           C  
ANISOU 2416  CA  TRP A 330     3653   3889   4117    -76    168    176       C  
ATOM   2417  C   TRP A 330      34.030  16.137  16.682  1.00 29.63           C  
ANISOU 2417  C   TRP A 330     3502   3753   4002    -74    154    183       C  
ATOM   2418  O   TRP A 330      34.101  15.082  16.065  1.00 29.94           O  
ANISOU 2418  O   TRP A 330     3533   3783   4057    -74    161    174       O  
ATOM   2419  CB  TRP A 330      33.164  17.798  15.091  1.00 29.60           C  
ANISOU 2419  CB  TRP A 330     3538   3760   3948    -75    172    171       C  
ATOM   2420  CG  TRP A 330      33.313  19.117  14.374  1.00 29.81           C  
ANISOU 2420  CG  TRP A 330     3584   3789   3952    -79    183    166       C  
ATOM   2421  CD1 TRP A 330      34.291  20.097  14.568  1.00 29.91           C  
ANISOU 2421  CD1 TRP A 330     3596   3799   3968    -82    189    166       C  
ATOM   2422  CD2 TRP A 330      32.418  19.674  13.347  1.00 30.01           C  
ANISOU 2422  CD2 TRP A 330     3633   3820   3949    -80    188    161       C  
ATOM   2423  NE1 TRP A 330      34.082  21.172  13.742  1.00 29.81           N  
ANISOU 2423  NE1 TRP A 330     3604   3790   3932    -85    198    162       N  
ATOM   2424  CE2 TRP A 330      32.980  20.983  12.979  1.00 29.68           C  
ANISOU 2424  CE2 TRP A 330     3602   3778   3895    -85    197    159       C  
ATOM   2425  CE3 TRP A 330      31.255  19.235  12.713  1.00 29.35           C  
ANISOU 2425  CE3 TRP A 330     3560   3740   3849    -79    185    159       C  
ATOM   2426  CZ2 TRP A 330      32.389  21.789  12.023  1.00 28.89           C  
ANISOU 2426  CZ2 TRP A 330     3525   3681   3768    -88    202    156       C  
ATOM   2427  CZ3 TRP A 330      30.678  20.058  11.745  1.00 29.04           C  
ANISOU 2427  CZ3 TRP A 330     3544   3704   3783    -82    189    156       C  
ATOM   2428  CH2 TRP A 330      31.231  21.302  11.409  1.00 28.86           C  
ANISOU 2428  CH2 TRP A 330     3533   3681   3749    -87    197    155       C  
ATOM   2429  N   GLN A 331      33.727  16.217  17.972  1.00 29.44           N  
ANISOU 2429  N   GLN A 331     3472   3736   3977    -72    134    198       N  
ATOM   2430  CA  GLN A 331      33.292  15.057  18.754  1.00 29.32           C  
ANISOU 2430  CA  GLN A 331     3442   3721   3976    -70    118    207       C  
ATOM   2431  C   GLN A 331      31.767  14.960  18.887  1.00 29.05           C  
ANISOU 2431  C   GLN A 331     3421   3700   3917    -66    108    213       C  
ATOM   2432  O   GLN A 331      31.226  13.851  18.940  1.00 29.51           O  
ANISOU 2432  O   GLN A 331     3470   3756   3983    -64    101    215       O  
ATOM   2433  CB  GLN A 331      33.990  15.018  20.113  1.00 29.48           C  
ANISOU 2433  CB  GLN A 331     3447   3739   4013    -74    102    221       C  
ATOM   2434  CG  GLN A 331      35.432  14.543  20.002  1.00 30.72           C  
ANISOU 2434  CG  GLN A 331     3584   3879   4207    -77    107    217       C  
ATOM   2435  CD  GLN A 331      36.234  14.793  21.259  1.00 31.46           C  
ANISOU 2435  CD  GLN A 331     3665   3971   4315    -82     91    231       C  
ATOM   2436  OE1 GLN A 331      36.456  13.890  22.049  1.00 32.56           O  
ANISOU 2436  OE1 GLN A 331     3788   4105   4478    -84     75    242       O  
ATOM   2437  NE2 GLN A 331      36.661  16.028  21.457  1.00 32.50           N  
ANISOU 2437  NE2 GLN A 331     3806   4107   4434    -84     95    231       N  
ATOM   2438  N   SER A 332      31.073  16.099  18.943  1.00 27.93           N  
ANISOU 2438  N   SER A 332     3296   3569   3745    -65    107    214       N  
ATOM   2439  CA  SER A 332      29.628  16.073  18.767  1.00 28.50           C  
ANISOU 2439  CA  SER A 332     3381   3651   3796    -61    102    216       C  
ATOM   2440  C   SER A 332      29.142  17.131  17.783  1.00 28.90           C  
ANISOU 2440  C   SER A 332     3452   3705   3821    -59    113    208       C  
ATOM   2441  O   SER A 332      29.835  18.123  17.526  1.00 29.53           O  
ANISOU 2441  O   SER A 332     3539   3783   3896    -62    121    204       O  
ATOM   2442  CB  SER A 332      28.862  16.112  20.106  1.00 29.34           C  
ANISOU 2442  CB  SER A 332     3485   3769   3894    -60     84    230       C  
ATOM   2443  OG  SER A 332      29.130  17.288  20.840  1.00 31.03           O  
ANISOU 2443  OG  SER A 332     3703   3990   4097    -62     81    234       O  
ATOM   2444  N   LEU A 333      27.970  16.881  17.200  1.00 27.42           N  
ANISOU 2444  N   LEU A 333     3276   3522   3620    -56    111    205       N  
ATOM   2445  CA  LEU A 333      27.351  17.790  16.257  1.00 26.60           C  
ANISOU 2445  CA  LEU A 333     3192   3421   3492    -56    117    200       C  
ATOM   2446  C   LEU A 333      25.841  17.834  16.498  1.00 27.46           C  
ANISOU 2446  C   LEU A 333     3308   3538   3585    -51    105    205       C  
ATOM   2447  O   LEU A 333      25.152  16.801  16.546  1.00 26.81           O  
ANISOU 2447  O   LEU A 333     3220   3457   3508    -49     99    207       O  
ATOM   2448  CB  LEU A 333      27.675  17.403  14.807  1.00 25.60           C  
ANISOU 2448  CB  LEU A 333     3073   3286   3367    -59    132    187       C  
ATOM   2449  CG  LEU A 333      26.971  18.173  13.677  1.00 25.05           C  
ANISOU 2449  CG  LEU A 333     3027   3218   3272    -61    137    181       C  
ATOM   2450  CD1 LEU A 333      27.222  19.676  13.761  1.00 24.83           C  
ANISOU 2450  CD1 LEU A 333     3009   3193   3230    -62    139    184       C  
ATOM   2451  CD2 LEU A 333      27.362  17.626  12.312  1.00 24.29           C  
ANISOU 2451  CD2 LEU A 333     2937   3113   3176    -67    152    168       C  
ATOM   2452  N   SER A 334      25.343  19.056  16.637  1.00 28.39           N  
ANISOU 2452  N   SER A 334     3438   3663   3686    -50    102    208       N  
ATOM   2453  CA  SER A 334      23.972  19.315  17.011  1.00 27.85           C  
ANISOU 2453  CA  SER A 334     3374   3602   3604    -45     91    213       C  
ATOM   2454  C   SER A 334      23.390  20.229  15.951  1.00 27.59           C  
ANISOU 2454  C   SER A 334     3360   3567   3553    -45     94    208       C  
ATOM   2455  O   SER A 334      23.919  21.310  15.710  1.00 27.79           O  
ANISOU 2455  O   SER A 334     3394   3592   3573    -48    100    206       O  
ATOM   2456  CB  SER A 334      23.959  20.019  18.360  1.00 28.18           C  
ANISOU 2456  CB  SER A 334     3411   3652   3644    -45     84    220       C  
ATOM   2457  OG  SER A 334      23.203  19.298  19.306  1.00 29.58           O  
ANISOU 2457  OG  SER A 334     3578   3836   3825    -43     74    227       O  
ATOM   2458  N   ILE A 335      22.327  19.766  15.300  1.00 27.65           N  
ANISOU 2458  N   ILE A 335     3374   3574   3555    -43     89    207       N  
ATOM   2459  CA  ILE A 335      21.561  20.542  14.334  1.00 27.34           C  
ANISOU 2459  CA  ILE A 335     3353   3534   3500    -43     88    205       C  
ATOM   2460  C   ILE A 335      20.159  20.488  14.905  1.00 27.74           C  
ANISOU 2460  C   ILE A 335     3401   3590   3548    -37     74    211       C  
ATOM   2461  O   ILE A 335      19.529  19.425  14.911  1.00 27.21           O  
ANISOU 2461  O   ILE A 335     3328   3523   3486    -35     69    213       O  
ATOM   2462  CB  ILE A 335      21.525  19.879  12.941  1.00 27.91           C  
ANISOU 2462  CB  ILE A 335     3436   3600   3569    -48     93    199       C  
ATOM   2463  CG1 ILE A 335      22.853  19.186  12.574  1.00 28.56           C  
ANISOU 2463  CG1 ILE A 335     3512   3676   3662    -53    108    191       C  
ATOM   2464  CG2 ILE A 335      21.106  20.868  11.876  1.00 27.94           C  
ANISOU 2464  CG2 ILE A 335     3459   3600   3554    -52     92    197       C  
ATOM   2465  CD1 ILE A 335      23.995  20.138  12.329  1.00 29.52           C  
ANISOU 2465  CD1 ILE A 335     3639   3795   3781    -58    119    187       C  
ATOM   2466  N   ILE A 336      19.692  21.625  15.417  1.00 27.68           N  
ANISOU 2466  N   ILE A 336     3396   3585   3534    -35     69    214       N  
ATOM   2467  CA  ILE A 336      18.405  21.720  16.099  1.00 28.16           C  
ANISOU 2467  CA  ILE A 336     3452   3651   3594    -30     59    219       C  
ATOM   2468  C   ILE A 336      17.564  22.817  15.470  1.00 28.43           C  
ANISOU 2468  C   ILE A 336     3500   3682   3620    -28     53    218       C  
ATOM   2469  O   ILE A 336      18.030  23.947  15.315  1.00 28.66           O  
ANISOU 2469  O   ILE A 336     3537   3709   3644    -30     56    217       O  
ATOM   2470  CB  ILE A 336      18.587  22.030  17.604  1.00 28.28           C  
ANISOU 2470  CB  ILE A 336     3455   3674   3614    -28     58    222       C  
ATOM   2471  CG1 ILE A 336      19.192  20.827  18.333  1.00 29.47           C  
ANISOU 2471  CG1 ILE A 336     3592   3829   3776    -30     59    225       C  
ATOM   2472  CG2 ILE A 336      17.268  22.454  18.245  1.00 27.23           C  
ANISOU 2472  CG2 ILE A 336     3320   3546   3480    -24     50    224       C  
ATOM   2473  CD1 ILE A 336      19.680  21.134  19.740  1.00 30.99           C  
ANISOU 2473  CD1 ILE A 336     3774   4028   3970    -32     59    229       C  
ATOM   2474  N   ARG A 337      16.322  22.480  15.134  1.00 28.97           N  
ANISOU 2474  N   ARG A 337     3569   3748   3687    -25     44    220       N  
ATOM   2475  CA  ARG A 337      15.368  23.419  14.512  1.00 30.33           C  
ANISOU 2475  CA  ARG A 337     3752   3915   3854    -24     35    221       C  
ATOM   2476  C   ARG A 337      15.966  24.198  13.327  1.00 29.69           C  
ANISOU 2476  C   ARG A 337     3689   3827   3763    -30     38    220       C  
ATOM   2477  O   ARG A 337      15.831  25.425  13.231  1.00 29.76           O  
ANISOU 2477  O   ARG A 337     3705   3833   3769    -30     34    221       O  
ATOM   2478  CB  ARG A 337      14.768  24.381  15.546  1.00 31.15           C  
ANISOU 2478  CB  ARG A 337     3849   4022   3963    -19     31    222       C  
ATOM   2479  CG  ARG A 337      13.989  23.730  16.688  1.00 33.02           C  
ANISOU 2479  CG  ARG A 337     4071   4267   4208    -14     29    224       C  
ATOM   2480  CD  ARG A 337      13.865  24.681  17.879  1.00 34.04           C  
ANISOU 2480  CD  ARG A 337     4192   4401   4339    -13     31    222       C  
ATOM   2481  NE  ARG A 337      14.028  26.063  17.428  1.00 37.01           N  
ANISOU 2481  NE  ARG A 337     4577   4770   4712    -13     30    220       N  
ATOM   2482  CZ  ARG A 337      14.964  26.909  17.858  1.00 37.84           C  
ANISOU 2482  CZ  ARG A 337     4684   4878   4815    -15     37    217       C  
ATOM   2483  NH1 ARG A 337      15.005  28.128  17.344  1.00 36.88           N  
ANISOU 2483  NH1 ARG A 337     4571   4748   4691    -16     34    216       N  
ATOM   2484  NH2 ARG A 337      15.833  26.557  18.808  1.00 37.34           N  
ANISOU 2484  NH2 ARG A 337     4613   4823   4752    -18     44    217       N  
ATOM   2485  N   CYS A 338      16.632  23.481  12.430  1.00 28.83           N  
ANISOU 2485  N   CYS A 338     3587   3715   3649    -36     44    217       N  
ATOM   2486  CA  CYS A 338      17.219  24.113  11.259  1.00 28.75           C  
ANISOU 2486  CA  CYS A 338     3595   3699   3627    -44     48    215       C  
ATOM   2487  C   CYS A 338      16.400  23.817  10.009  1.00 28.73           C  
ANISOU 2487  C   CYS A 338     3608   3691   3617    -48     39    216       C  
ATOM   2488  O   CYS A 338      15.287  23.292  10.100  1.00 27.26           O  
ANISOU 2488  O   CYS A 338     3417   3505   3435    -43     28    219       O  
ATOM   2489  CB  CYS A 338      18.662  23.677  11.092  1.00 28.72           C  
ANISOU 2489  CB  CYS A 338     3591   3697   3624    -49     64    209       C  
ATOM   2490  SG  CYS A 338      19.688  24.184  12.473  1.00 29.34           S  
ANISOU 2490  SG  CYS A 338     3654   3780   3712    -46     72    209       S  
ATOM   2491  N   GLN A 339      16.954  24.147   8.846  1.00 29.74           N  
ANISOU 2491  N   GLN A 339     3753   3813   3731    -58     44    214       N  
ATOM   2492  CA  GLN A 339      16.169  24.133   7.621  1.00 31.67           C  
ANISOU 2492  CA  GLN A 339     4015   4052   3964    -65     33    216       C  
ATOM   2493  C   GLN A 339      16.720  23.241   6.521  1.00 32.16           C  
ANISOU 2493  C   GLN A 339     4090   4113   4017    -75     43    209       C  
ATOM   2494  O   GLN A 339      16.549  23.544   5.338  1.00 34.29           O  
ANISOU 2494  O   GLN A 339     4379   4377   4270    -86     39    210       O  
ATOM   2495  CB  GLN A 339      16.007  25.560   7.102  1.00 33.06           C  
ANISOU 2495  CB  GLN A 339     4206   4222   4131    -70     25    222       C  
ATOM   2496  CG  GLN A 339      14.867  26.324   7.758  1.00 34.05           C  
ANISOU 2496  CG  GLN A 339     4323   4345   4266    -61      8    229       C  
ATOM   2497  CD  GLN A 339      15.016  27.834   7.625  1.00 34.28           C  
ANISOU 2497  CD  GLN A 339     4361   4369   4293    -64      3    234       C  
ATOM   2498  OE1 GLN A 339      15.079  28.538   8.622  1.00 34.75           O  
ANISOU 2498  OE1 GLN A 339     4409   4431   4363    -56      4    234       O  
ATOM   2499  NE2 GLN A 339      15.068  28.333   6.394  1.00 34.30           N  
ANISOU 2499  NE2 GLN A 339     4385   4365   4281    -75     -2    238       N  
ATOM   2500  N   LEU A 340      17.370  22.148   6.903  1.00 32.15           N  
ANISOU 2500  N   LEU A 340     4076   4115   4024    -73     56    202       N  
ATOM   2501  CA  LEU A 340      17.994  21.239   5.937  1.00 33.34           C  
ANISOU 2501  CA  LEU A 340     4234   4263   4167    -83     68    193       C  
ATOM   2502  C   LEU A 340      17.028  20.747   4.857  1.00 33.32           C  
ANISOU 2502  C   LEU A 340     4248   4257   4154    -89     57    193       C  
ATOM   2503  O   LEU A 340      15.934  20.278   5.156  1.00 34.17           O  
ANISOU 2503  O   LEU A 340     4348   4364   4268    -82     43    198       O  
ATOM   2504  CB  LEU A 340      18.627  20.047   6.670  1.00 32.72           C  
ANISOU 2504  CB  LEU A 340     4136   4188   4107    -77     80    186       C  
ATOM   2505  CG  LEU A 340      20.101  20.031   7.092  1.00 31.26           C  
ANISOU 2505  CG  LEU A 340     3941   4004   3930    -78     98    180       C  
ATOM   2506  CD1 LEU A 340      20.795  21.371   6.965  1.00 30.30           C  
ANISOU 2506  CD1 LEU A 340     3829   3882   3801    -83    104    182       C  
ATOM   2507  CD2 LEU A 340      20.191  19.510   8.516  1.00 31.69           C  
ANISOU 2507  CD2 LEU A 340     3971   4063   4005    -67     96    183       C  
ATOM   2508  N   LYS A 341      17.434  20.871   3.602  1.00 35.16           N  
ANISOU 2508  N   LYS A 341     4502   4487   4369   -103     64    188       N  
ATOM   2509  CA  LYS A 341      16.641  20.366   2.484  1.00 37.36           C  
ANISOU 2509  CA  LYS A 341     4798   4762   4635   -112     55    188       C  
ATOM   2510  C   LYS A 341      16.956  18.902   2.212  1.00 37.23           C  
ANISOU 2510  C   LYS A 341     4776   4745   4623   -114     67    175       C  
ATOM   2511  O   LYS A 341      16.194  18.211   1.546  1.00 38.01           O  
ANISOU 2511  O   LYS A 341     4884   4842   4716   -118     58    174       O  
ATOM   2512  CB  LYS A 341      16.893  21.189   1.220  1.00 40.31           C  
ANISOU 2512  CB  LYS A 341     5200   5132   4984   -129     55    188       C  
ATOM   2513  CG  LYS A 341      16.193  22.540   1.194  1.00 44.76           C  
ANISOU 2513  CG  LYS A 341     5772   5692   5542   -129     36    202       C  
ATOM   2514  CD  LYS A 341      15.924  22.986  -0.244  1.00 51.59           C  
ANISOU 2514  CD  LYS A 341     6667   6553   6382   -148     27    206       C  
ATOM   2515  CE  LYS A 341      14.734  22.243  -0.863  1.00 55.83           C  
ANISOU 2515  CE  LYS A 341     7213   7086   6914   -151      9    208       C  
ATOM   2516  NZ  LYS A 341      14.547  22.538  -2.313  1.00 57.55           N  
ANISOU 2516  NZ  LYS A 341     7462   7299   7105   -172      2    211       N  
ATOM   2517  N   GLN A 342      18.088  18.448   2.741  1.00 37.55           N  
ANISOU 2517  N   GLN A 342     4801   4787   4676   -111     86    167       N  
ATOM   2518  CA  GLN A 342      18.607  17.104   2.516  1.00 38.38           C  
ANISOU 2518  CA  GLN A 342     4898   4891   4790   -114    100    154       C  
ATOM   2519  C   GLN A 342      19.300  16.573   3.751  1.00 37.40           C  
ANISOU 2519  C   GLN A 342     4747   4769   4692   -102    109    152       C  
ATOM   2520  O   GLN A 342      19.792  17.344   4.573  1.00 38.59           O  
ANISOU 2520  O   GLN A 342     4889   4923   4849    -97    111    157       O  
ATOM   2521  CB  GLN A 342      19.638  17.122   1.407  1.00 39.79           C  
ANISOU 2521  CB  GLN A 342     5093   5067   4956   -130    121    140       C  
ATOM   2522  CG  GLN A 342      19.133  16.617   0.075  1.00 44.46           C  
ANISOU 2522  CG  GLN A 342     5707   5656   5528   -144    120    133       C  
ATOM   2523  CD  GLN A 342      20.240  16.552  -0.957  1.00 46.43           C  
ANISOU 2523  CD  GLN A 342     5972   5904   5765   -161    144    118       C  
ATOM   2524  OE1 GLN A 342      21.417  16.809  -0.654  1.00 45.70           O  
ANISOU 2524  OE1 GLN A 342     5870   5811   5681   -162    163    112       O  
ATOM   2525  NE2 GLN A 342      19.873  16.209  -2.188  1.00 47.77           N  
ANISOU 2525  NE2 GLN A 342     6163   6071   5913   -177    145    111       N  
ATOM   2526  N   PHE A 343      19.359  15.255   3.875  1.00 35.61           N  
ANISOU 2526  N   PHE A 343     4508   4542   4481    -99    113    145       N  
ATOM   2527  CA  PHE A 343      20.086  14.662   4.976  1.00 35.13           C  
ANISOU 2527  CA  PHE A 343     4421   4480   4445    -90    120    143       C  
ATOM   2528  C   PHE A 343      21.589  14.884   4.775  1.00 34.14           C  
ANISOU 2528  C   PHE A 343     4294   4353   4324    -97    143    133       C  
ATOM   2529  O   PHE A 343      22.110  14.590   3.698  1.00 35.03           O  
ANISOU 2529  O   PHE A 343     4418   4461   4429   -109    158    120       O  
ATOM   2530  CB  PHE A 343      19.756  13.173   5.130  1.00 34.36           C  
ANISOU 2530  CB  PHE A 343     4309   4380   4364    -86    118    139       C  
ATOM   2531  CG  PHE A 343      20.159  12.610   6.456  1.00 32.80           C  
ANISOU 2531  CG  PHE A 343     4084   4183   4192    -75    117    144       C  
ATOM   2532  CD1 PHE A 343      19.276  12.633   7.523  1.00 32.84           C  
ANISOU 2532  CD1 PHE A 343     4079   4195   4204    -65    100    157       C  
ATOM   2533  CD2 PHE A 343      21.430  12.087   6.645  1.00 31.93           C  
ANISOU 2533  CD2 PHE A 343     3960   4069   4101    -77    134    134       C  
ATOM   2534  CE1 PHE A 343      19.647  12.124   8.759  1.00 32.41           C  
ANISOU 2534  CE1 PHE A 343     4001   4142   4171    -57     98    163       C  
ATOM   2535  CE2 PHE A 343      21.813  11.585   7.871  1.00 32.10           C  
ANISOU 2535  CE2 PHE A 343     3957   4090   4147    -69    130    141       C  
ATOM   2536  CZ  PHE A 343      20.920  11.601   8.933  1.00 32.61           C  
ANISOU 2536  CZ  PHE A 343     4013   4162   4215    -60    112    155       C  
ATOM   2537  N   PRO A 344      22.280  15.408   5.810  1.00 33.04           N  
ANISOU 2537  N   PRO A 344     4139   4215   4197    -91    145    138       N  
ATOM   2538  CA  PRO A 344      23.700  15.733   5.766  1.00 34.18           C  
ANISOU 2538  CA  PRO A 344     4280   4357   4348    -96    164    131       C  
ATOM   2539  C   PRO A 344      24.559  14.588   5.269  1.00 36.15           C  
ANISOU 2539  C   PRO A 344     4521   4599   4614   -102    183    115       C  
ATOM   2540  O   PRO A 344      24.275  13.418   5.554  1.00 37.46           O  
ANISOU 2540  O   PRO A 344     4673   4762   4797    -96    179    113       O  
ATOM   2541  CB  PRO A 344      24.037  16.002   7.228  1.00 32.75           C  
ANISOU 2541  CB  PRO A 344     4078   4179   4185    -85    158    141       C  
ATOM   2542  CG  PRO A 344      22.777  16.528   7.788  1.00 32.03           C  
ANISOU 2542  CG  PRO A 344     3990   4094   4083    -78    137    154       C  
ATOM   2543  CD  PRO A 344      21.700  15.735   7.123  1.00 32.42           C  
ANISOU 2543  CD  PRO A 344     4047   4142   4126    -79    129    153       C  
ATOM   2544  N   THR A 345      25.597  14.918   4.516  1.00 37.43           N  
ANISOU 2544  N   THR A 345     4692   4758   4773   -112    203    103       N  
ATOM   2545  CA  THR A 345      26.578  13.912   4.160  1.00 39.78           C  
ANISOU 2545  CA  THR A 345     4976   5046   5089   -117    224     86       C  
ATOM   2546  C   THR A 345      27.768  14.103   5.106  1.00 40.98           C  
ANISOU 2546  C   THR A 345     5106   5195   5266   -112    231     87       C  
ATOM   2547  O   THR A 345      28.438  15.141   5.082  1.00 43.48           O  
ANISOU 2547  O   THR A 345     5429   5513   5576   -117    239     89       O  
ATOM   2548  CB  THR A 345      26.951  13.943   2.654  1.00 39.51           C  
ANISOU 2548  CB  THR A 345     4964   5010   5038   -134    244     69       C  
ATOM   2549  OG1 THR A 345      28.214  14.582   2.462  1.00 39.39           O  
ANISOU 2549  OG1 THR A 345     4949   4991   5025   -142    265     61       O  
ATOM   2550  CG2 THR A 345      25.890  14.666   1.841  1.00 39.85           C  
ANISOU 2550  CG2 THR A 345     5036   5058   5044   -141    232     75       C  
ATOM   2551  N   LEU A 346      27.997  13.117   5.965  1.00 39.86           N  
ANISOU 2551  N   LEU A 346     4940   5049   5155   -104    227     89       N  
ATOM   2552  CA  LEU A 346      29.011  13.239   7.000  1.00 39.45           C  
ANISOU 2552  CA  LEU A 346     4866   4994   5128    -99    228     93       C  
ATOM   2553  C   LEU A 346      29.940  12.064   6.979  1.00 42.19           C  
ANISOU 2553  C   LEU A 346     5191   5329   5509   -100    242     80       C  
ATOM   2554  O   LEU A 346      29.496  10.911   6.907  1.00 46.09           O  
ANISOU 2554  O   LEU A 346     5676   5819   6015    -97    237     77       O  
ATOM   2555  CB  LEU A 346      28.376  13.300   8.383  1.00 37.51           C  
ANISOU 2555  CB  LEU A 346     4608   4755   4889    -87    204    112       C  
ATOM   2556  CG  LEU A 346      27.492  14.485   8.734  1.00 36.27           C  
ANISOU 2556  CG  LEU A 346     4466   4609   4705    -83    189    126       C  
ATOM   2557  CD1 LEU A 346      26.632  14.109   9.926  1.00 33.33           C  
ANISOU 2557  CD1 LEU A 346     4081   4243   4340    -73    168    141       C  
ATOM   2558  CD2 LEU A 346      28.344  15.714   9.020  1.00 36.13           C  
ANISOU 2558  CD2 LEU A 346     4450   4592   4683    -86    195    129       C  
ATOM   2559  N   ASP A 347      31.231  12.365   7.052  1.00 42.43           N  
ANISOU 2559  N   ASP A 347     5212   5353   5557   -104    257     74       N  
ATOM   2560  CA  ASP A 347      32.273  11.359   7.176  1.00 42.12           C  
ANISOU 2560  CA  ASP A 347     5147   5300   5556   -104    269     63       C  
ATOM   2561  C   ASP A 347      33.395  11.942   8.011  1.00 40.63           C  
ANISOU 2561  C   ASP A 347     4942   5107   5386   -102    271     69       C  
ATOM   2562  O   ASP A 347      34.493  12.233   7.530  1.00 43.13           O  
ANISOU 2562  O   ASP A 347     5256   5416   5713   -110    292     56       O  
ATOM   2563  CB  ASP A 347      32.739  10.844   5.812  1.00 46.94           C  
ANISOU 2563  CB  ASP A 347     5765   5902   6167   -116    296     38       C  
ATOM   2564  CG  ASP A 347      32.566  11.863   4.717  1.00 55.13           C  
ANISOU 2564  CG  ASP A 347     6833   6947   7167   -127    309     32       C  
ATOM   2565  OD1 ASP A 347      31.694  11.637   3.839  1.00 57.13           O  
ANISOU 2565  OD1 ASP A 347     7105   7203   7395   -132    309     27       O  
ATOM   2566  OD2 ASP A 347      33.288  12.894   4.744  1.00 60.24           O  
ANISOU 2566  OD2 ASP A 347     7484   7595   7807   -131    317     34       O  
ATOM   2567  N   LEU A 348      33.060  12.141   9.278  1.00 38.22           N  
ANISOU 2567  N   LEU A 348     4627   4807   5085    -93    248     88       N  
ATOM   2568  CA  LEU A 348      33.950  12.690  10.270  1.00 35.72           C  
ANISOU 2568  CA  LEU A 348     4297   4490   4786    -91    243     98       C  
ATOM   2569  C   LEU A 348      34.400  11.556  11.173  1.00 35.15           C  
ANISOU 2569  C   LEU A 348     4194   4406   4753    -86    233    102       C  
ATOM   2570  O   LEU A 348      33.573  10.808  11.695  1.00 35.84           O  
ANISOU 2570  O   LEU A 348     4276   4497   4843    -81    215    112       O  
ATOM   2571  CB  LEU A 348      33.231  13.772  11.069  1.00 35.53           C  
ANISOU 2571  CB  LEU A 348     4283   4479   4735    -86    224    116       C  
ATOM   2572  CG  LEU A 348      32.909  15.060  10.308  1.00 35.70           C  
ANISOU 2572  CG  LEU A 348     4332   4509   4721    -91    232    114       C  
ATOM   2573  CD1 LEU A 348      32.061  15.989  11.154  1.00 34.44           C  
ANISOU 2573  CD1 LEU A 348     4181   4361   4540    -85    211    131       C  
ATOM   2574  CD2 LEU A 348      34.191  15.761   9.887  1.00 36.64           C  
ANISOU 2574  CD2 LEU A 348     4451   4621   4847    -98    251    105       C  
ATOM   2575  N   PRO A 349      35.718  11.420  11.358  1.00 34.58           N  
ANISOU 2575  N   PRO A 349     4103   4322   4713    -89    243     97       N  
ATOM   2576  CA  PRO A 349      36.236  10.222  12.006  1.00 33.47           C  
ANISOU 2576  CA  PRO A 349     3933   4168   4615    -86    235     99       C  
ATOM   2577  C   PRO A 349      36.112  10.179  13.531  1.00 32.76           C  
ANISOU 2577  C   PRO A 349     3829   4082   4536    -80    206    122       C  
ATOM   2578  O   PRO A 349      36.155   9.097  14.100  1.00 32.36           O  
ANISOU 2578  O   PRO A 349     3757   4022   4513    -78    194    128       O  
ATOM   2579  CB  PRO A 349      37.699  10.190  11.569  1.00 33.73           C  
ANISOU 2579  CB  PRO A 349     3951   4185   4679    -92    257     84       C  
ATOM   2580  CG  PRO A 349      38.048  11.614  11.276  1.00 34.62           C  
ANISOU 2580  CG  PRO A 349     4082   4306   4766    -96    267     83       C  
ATOM   2581  CD  PRO A 349      36.786  12.349  10.936  1.00 34.24           C  
ANISOU 2581  CD  PRO A 349     4063   4275   4670    -95    262     88       C  
ATOM   2582  N   PHE A 350      35.938  11.323  14.188  1.00 32.94           N  
ANISOU 2582  N   PHE A 350     3863   4116   4534    -79    196    135       N  
ATOM   2583  CA  PHE A 350      35.889  11.334  15.660  1.00 32.84           C  
ANISOU 2583  CA  PHE A 350     3838   4108   4530    -76    171    156       C  
ATOM   2584  C   PHE A 350      34.556  11.772  16.258  1.00 31.68           C  
ANISOU 2584  C   PHE A 350     3707   3978   4349    -72    153    171       C  
ATOM   2585  O   PHE A 350      34.417  11.874  17.479  1.00 30.58           O  
ANISOU 2585  O   PHE A 350     3562   3845   4210    -71    133    188       O  
ATOM   2586  CB  PHE A 350      37.057  12.140  16.246  1.00 34.10           C  
ANISOU 2586  CB  PHE A 350     3989   4262   4702    -79    171    161       C  
ATOM   2587  CG  PHE A 350      38.399  11.538  15.960  1.00 34.12           C  
ANISOU 2587  CG  PHE A 350     3970   4246   4749    -83    183    151       C  
ATOM   2588  CD1 PHE A 350      39.184  12.023  14.925  1.00 34.69           C  
ANISOU 2588  CD1 PHE A 350     4046   4311   4823    -87    210    133       C  
ATOM   2589  CD2 PHE A 350      38.866  10.462  16.706  1.00 34.43           C  
ANISOU 2589  CD2 PHE A 350     3982   4272   4827    -82    168    158       C  
ATOM   2590  CE1 PHE A 350      40.423  11.459  14.652  1.00 35.40           C  
ANISOU 2590  CE1 PHE A 350     4114   4381   4955    -91    223    121       C  
ATOM   2591  CE2 PHE A 350      40.101   9.889  16.439  1.00 34.52           C  
ANISOU 2591  CE2 PHE A 350     3970   4262   4882    -85    180    148       C  
ATOM   2592  CZ  PHE A 350      40.882  10.389  15.410  1.00 35.02           C  
ANISOU 2592  CZ  PHE A 350     4037   4319   4949    -89    208    128       C  
ATOM   2593  N   LEU A 351      33.568  12.004  15.398  1.00 31.89           N  
ANISOU 2593  N   LEU A 351     3755   4014   4347    -71    160    164       N  
ATOM   2594  CA  LEU A 351      32.216  12.331  15.864  1.00 31.21           C  
ANISOU 2594  CA  LEU A 351     3682   3943   4230    -67    145    175       C  
ATOM   2595  C   LEU A 351      31.579  11.166  16.644  1.00 30.75           C  
ANISOU 2595  C   LEU A 351     3611   3885   4186    -64    126    186       C  
ATOM   2596  O   LEU A 351      31.264  10.122  16.074  1.00 29.81           O  
ANISOU 2596  O   LEU A 351     3487   3760   4078    -63    129    179       O  
ATOM   2597  CB  LEU A 351      31.341  12.750  14.684  1.00 30.29           C  
ANISOU 2597  CB  LEU A 351     3590   3833   4084    -67    155    165       C  
ATOM   2598  CG  LEU A 351      30.073  13.531  15.008  1.00 29.78           C  
ANISOU 2598  CG  LEU A 351     3542   3783   3987    -63    143    175       C  
ATOM   2599  CD1 LEU A 351      30.421  14.985  15.282  1.00 29.23           C  
ANISOU 2599  CD1 LEU A 351     3484   3720   3902    -65    145    179       C  
ATOM   2600  CD2 LEU A 351      29.084  13.413  13.856  1.00 29.71           C  
ANISOU 2600  CD2 LEU A 351     3552   3777   3957    -63    149    167       C  
ATOM   2601  N   LYS A 352      31.419  11.349  17.952  1.00 31.72           N  
ANISOU 2601  N   LYS A 352     3727   4015   4308    -63    107    204       N  
ATOM   2602  CA  LYS A 352      30.856  10.314  18.813  1.00 32.71           C  
ANISOU 2602  CA  LYS A 352     3840   4142   4445    -62     88    216       C  
ATOM   2603  C   LYS A 352      29.366  10.455  18.867  1.00 33.12           C  
ANISOU 2603  C   LYS A 352     3907   4208   4468    -59     81    221       C  
ATOM   2604  O   LYS A 352      28.649   9.457  18.971  1.00 35.49           O  
ANISOU 2604  O   LYS A 352     4201   4508   4774    -57     72    225       O  
ATOM   2605  CB  LYS A 352      31.352  10.437  20.248  1.00 34.48           C  
ANISOU 2605  CB  LYS A 352     4051   4368   4679    -66     71    233       C  
ATOM   2606  CG  LYS A 352      32.818  10.141  20.487  1.00 36.22           C  
ANISOU 2606  CG  LYS A 352     4253   4574   4935    -70     71    233       C  
ATOM   2607  CD  LYS A 352      33.038  10.041  21.986  1.00 37.08           C  
ANISOU 2607  CD  LYS A 352     4351   4686   5053    -75     48    254       C  
ATOM   2608  CE  LYS A 352      34.478  10.338  22.372  1.00 38.30           C  
ANISOU 2608  CE  LYS A 352     4491   4828   5232    -80     47    256       C  
ATOM   2609  NZ  LYS A 352      34.693  11.804  22.487  1.00 39.44           N  
ANISOU 2609  NZ  LYS A 352     4651   4982   5351    -81     53    254       N  
ATOM   2610  N   SER A 353      28.896  11.697  18.807  1.00 31.37           N  
ANISOU 2610  N   SER A 353     3704   3998   4217    -58     84    221       N  
ATOM   2611  CA  SER A 353      27.495  11.990  19.089  1.00 29.60           C  
ANISOU 2611  CA  SER A 353     3491   3786   3966    -54     75    227       C  
ATOM   2612  C   SER A 353      26.909  12.950  18.062  1.00 27.58           C  
ANISOU 2612  C   SER A 353     3258   3536   3685    -52     87    217       C  
ATOM   2613  O   SER A 353      27.466  14.008  17.823  1.00 27.18           O  
ANISOU 2613  O   SER A 353     3216   3485   3625    -54     95    213       O  
ATOM   2614  CB  SER A 353      27.383  12.553  20.511  1.00 29.70           C  
ANISOU 2614  CB  SER A 353     3502   3810   3971    -57     62    242       C  
ATOM   2615  OG  SER A 353      26.074  12.999  20.792  1.00 30.78           O  
ANISOU 2615  OG  SER A 353     3651   3960   4084    -54     56    246       O  
ATOM   2616  N   LEU A 354      25.795  12.562  17.450  1.00 26.88           N  
ANISOU 2616  N   LEU A 354     3177   3450   3585    -49     85    214       N  
ATOM   2617  CA  LEU A 354      25.129  13.384  16.436  1.00 26.59           C  
ANISOU 2617  CA  LEU A 354     3161   3415   3523    -48     93    206       C  
ATOM   2618  C   LEU A 354      23.648  13.590  16.748  1.00 27.56           C  
ANISOU 2618  C   LEU A 354     3292   3549   3629    -43     81    213       C  
ATOM   2619  O   LEU A 354      22.902  12.636  16.982  1.00 27.63           O  
ANISOU 2619  O   LEU A 354     3294   3559   3644    -41     72    218       O  
ATOM   2620  CB  LEU A 354      25.298  12.794  15.023  1.00 25.84           C  
ANISOU 2620  CB  LEU A 354     3073   3312   3433    -50    106    192       C  
ATOM   2621  CG  LEU A 354      24.418  13.357  13.886  1.00 25.36           C  
ANISOU 2621  CG  LEU A 354     3034   3253   3347    -50    110    186       C  
ATOM   2622  CD1 LEU A 354      24.756  14.799  13.553  1.00 24.82           C  
ANISOU 2622  CD1 LEU A 354     2981   3188   3261    -53    117    184       C  
ATOM   2623  CD2 LEU A 354      24.499  12.505  12.630  1.00 25.51           C  
ANISOU 2623  CD2 LEU A 354     3057   3264   3370    -53    121    173       C  
ATOM   2624  N   THR A 355      23.235  14.852  16.727  1.00 28.96           N  
ANISOU 2624  N   THR A 355     3484   3733   3786    -43     82    214       N  
ATOM   2625  CA  THR A 355      21.848  15.232  16.966  1.00 29.41           C  
ANISOU 2625  CA  THR A 355     3548   3798   3828    -39     72    219       C  
ATOM   2626  C   THR A 355      21.327  16.115  15.829  1.00 29.48           C  
ANISOU 2626  C   THR A 355     3576   3805   3818    -38     76    213       C  
ATOM   2627  O   THR A 355      21.848  17.206  15.565  1.00 28.82           O  
ANISOU 2627  O   THR A 355     3502   3721   3726    -40     83    210       O  
ATOM   2628  CB  THR A 355      21.701  15.962  18.314  1.00 29.86           C  
ANISOU 2628  CB  THR A 355     3600   3864   3880    -38     65    228       C  
ATOM   2629  OG1 THR A 355      22.012  15.046  19.369  1.00 29.69           O  
ANISOU 2629  OG1 THR A 355     3562   3844   3873    -40     58    236       O  
ATOM   2630  CG2 THR A 355      20.287  16.508  18.489  1.00 29.38           C  
ANISOU 2630  CG2 THR A 355     3547   3811   3804    -34     58    231       C  
ATOM   2631  N   LEU A 356      20.307  15.601  15.155  1.00 28.75           N  
ANISOU 2631  N   LEU A 356     3490   3712   3721    -36     72    211       N  
ATOM   2632  CA  LEU A 356      19.562  16.339  14.173  1.00 28.13           C  
ANISOU 2632  CA  LEU A 356     3430   3633   3626    -36     71    208       C  
ATOM   2633  C   LEU A 356      18.117  16.164  14.592  1.00 28.39           C  
ANISOU 2633  C   LEU A 356     3460   3670   3655    -31     58    214       C  
ATOM   2634  O   LEU A 356      17.556  15.066  14.542  1.00 29.18           O  
ANISOU 2634  O   LEU A 356     3554   3769   3763    -29     53    216       O  
ATOM   2635  CB  LEU A 356      19.799  15.746  12.795  1.00 28.35           C  
ANISOU 2635  CB  LEU A 356     3467   3652   3652    -41     79    198       C  
ATOM   2636  CG  LEU A 356      19.782  16.689  11.591  1.00 29.27           C  
ANISOU 2636  CG  LEU A 356     3605   3765   3750    -46     84    193       C  
ATOM   2637  CD1 LEU A 356      20.303  15.933  10.379  1.00 29.75           C  
ANISOU 2637  CD1 LEU A 356     3672   3818   3810    -53     95    182       C  
ATOM   2638  CD2 LEU A 356      18.405  17.268  11.313  1.00 28.52           C  
ANISOU 2638  CD2 LEU A 356     3521   3672   3641    -44     70    198       C  
ATOM   2639  N   THR A 357      17.511  17.233  15.065  1.00 28.24           N  
ANISOU 2639  N   THR A 357     3446   3656   3628    -28     53    218       N  
ATOM   2640  CA  THR A 357      16.154  17.113  15.550  1.00 28.20           C  
ANISOU 2640  CA  THR A 357     3436   3654   3622    -24     42    224       C  
ATOM   2641  C   THR A 357      15.327  18.347  15.191  1.00 28.39           C  
ANISOU 2641  C   THR A 357     3473   3678   3636    -22     37    224       C  
ATOM   2642  O   THR A 357      15.882  19.444  15.013  1.00 27.50           O  
ANISOU 2642  O   THR A 357     3368   3564   3516    -24     41    222       O  
ATOM   2643  CB  THR A 357      16.138  16.804  17.067  1.00 28.39           C  
ANISOU 2643  CB  THR A 357     3443   3686   3654    -22     39    230       C  
ATOM   2644  OG1 THR A 357      14.806  16.450  17.478  1.00 29.46           O  
ANISOU 2644  OG1 THR A 357     3575   3827   3792    -18     30    235       O  
ATOM   2645  CG2 THR A 357      16.647  17.993  17.879  1.00 28.19           C  
ANISOU 2645  CG2 THR A 357     3418   3666   3624    -23     42    231       C  
ATOM   2646  N   MET A 358      14.012  18.148  15.065  1.00 28.47           N  
ANISOU 2646  N   MET A 358     3482   3687   3646    -18     26    227       N  
ATOM   2647  CA  MET A 358      13.045  19.227  14.798  1.00 29.15           C  
ANISOU 2647  CA  MET A 358     3577   3771   3727    -16     19    228       C  
ATOM   2648  C   MET A 358      13.359  19.992  13.507  1.00 29.15           C  
ANISOU 2648  C   MET A 358     3595   3763   3715    -20     19    225       C  
ATOM   2649  O   MET A 358      13.300  21.205  13.464  1.00 29.21           O  
ANISOU 2649  O   MET A 358     3610   3769   3719    -20     18    225       O  
ATOM   2650  CB  MET A 358      12.902  20.193  16.001  1.00 29.40           C  
ANISOU 2650  CB  MET A 358     3600   3808   3759    -13     20    229       C  
ATOM   2651  CG  MET A 358      12.801  19.512  17.367  1.00 31.27           C  
ANISOU 2651  CG  MET A 358     3821   4055   4005    -12     21    232       C  
ATOM   2652  SD  MET A 358      12.655  20.632  18.786  1.00 34.38           S  
ANISOU 2652  SD  MET A 358     4208   4457   4398    -11     24    232       S  
ATOM   2653  CE  MET A 358      10.924  21.070  18.673  1.00 34.54           C  
ANISOU 2653  CE  MET A 358     4227   4474   4423     -5     16    231       C  
ATOM   2654  N   ASN A 359      13.684  19.277  12.449  1.00 30.27           N  
ANISOU 2654  N   ASN A 359     3747   3901   3854    -25     22    221       N  
ATOM   2655  CA  ASN A 359      13.974  19.932  11.185  1.00 33.41           C  
ANISOU 2655  CA  ASN A 359     4163   4291   4238    -31     22    219       C  
ATOM   2656  C   ASN A 359      12.694  20.404  10.485  1.00 35.40           C  
ANISOU 2656  C   ASN A 359     4426   4537   4485    -31      7    223       C  
ATOM   2657  O   ASN A 359      11.639  19.789  10.647  1.00 34.95           O  
ANISOU 2657  O   ASN A 359     4362   4479   4435    -27     -2    226       O  
ATOM   2658  CB  ASN A 359      14.776  18.987  10.278  1.00 32.78           C  
ANISOU 2658  CB  ASN A 359     4090   4209   4155    -38     32    212       C  
ATOM   2659  CG  ASN A 359      15.654  19.727   9.298  1.00 32.82           C  
ANISOU 2659  CG  ASN A 359     4112   4209   4146    -47     40    208       C  
ATOM   2660  OD1 ASN A 359      15.380  19.750   8.098  1.00 33.36           O  
ANISOU 2660  OD1 ASN A 359     4198   4273   4203    -55     37    206       O  
ATOM   2661  ND2 ASN A 359      16.714  20.349   9.804  1.00 32.95           N  
ANISOU 2661  ND2 ASN A 359     4125   4229   4164    -48     51    206       N  
ATOM   2662  N   LYS A 360      12.789  21.502   9.731  1.00 39.78           N  
ANISOU 2662  N   LYS A 360     4997   5087   5030    -36      4    224       N  
ATOM   2663  CA  LYS A 360      11.705  21.933   8.839  1.00 45.27           C  
ANISOU 2663  CA  LYS A 360     5704   5774   5720    -39    -12    229       C  
ATOM   2664  C   LYS A 360      11.485  20.917   7.703  1.00 46.62           C  
ANISOU 2664  C   LYS A 360     5888   5942   5884    -45    -15    227       C  
ATOM   2665  O   LYS A 360      12.436  20.429   7.090  1.00 48.65           O  
ANISOU 2665  O   LYS A 360     6153   6199   6132    -53     -3    221       O  
ATOM   2666  CB  LYS A 360      11.971  23.341   8.280  1.00 49.69           C  
ANISOU 2666  CB  LYS A 360     6279   6328   6270    -44    -15    232       C  
ATOM   2667  CG  LYS A 360      10.857  23.909   7.390  1.00 56.90           C  
ANISOU 2667  CG  LYS A 360     7206   7232   7181    -48    -35    239       C  
ATOM   2668  CD  LYS A 360      11.288  24.119   5.927  1.00 60.95           C  
ANISOU 2668  CD  LYS A 360     7743   7739   7674    -62    -36    239       C  
ATOM   2669  CE  LYS A 360      10.256  23.633   4.899  1.00 62.56           C  
ANISOU 2669  CE  LYS A 360     7960   7936   7873    -68    -54    244       C  
ATOM   2670  NZ  LYS A 360       8.836  24.052   5.119  1.00 60.82           N  
ANISOU 2670  NZ  LYS A 360     7734   7709   7667    -61    -75    252       N  
ATOM   2671  N   GLY A 361      10.224  20.589   7.449  1.00 48.54           N  
ANISOU 2671  N   GLY A 361     6131   6180   6131    -43    -31    232       N  
ATOM   2672  CA  GLY A 361       9.866  19.612   6.422  1.00 50.71           C  
ANISOU 2672  CA  GLY A 361     6415   6450   6399    -49    -37    230       C  
ATOM   2673  C   GLY A 361      10.347  18.188   6.678  1.00 52.07           C  
ANISOU 2673  C   GLY A 361     6578   6628   6578    -48    -25    223       C  
ATOM   2674  O   GLY A 361      10.847  17.854   7.761  1.00 54.36           O  
ANISOU 2674  O   GLY A 361     6850   6924   6878    -41    -15    221       O  
ATOM   2675  N   SER A 362      10.171  17.342   5.668  1.00 48.40           N  
ANISOU 2675  N   SER A 362     6125   6160   6105    -55    -28    219       N  
ATOM   2676  CA  SER A 362      10.674  15.990   5.709  1.00 44.44           C  
ANISOU 2676  CA  SER A 362     5614   5659   5608    -55    -17    211       C  
ATOM   2677  C   SER A 362      12.041  15.983   5.074  1.00 41.40           C  
ANISOU 2677  C   SER A 362     5240   5275   5212    -65      1    201       C  
ATOM   2678  O   SER A 362      12.389  16.875   4.321  1.00 41.47           O  
ANISOU 2678  O   SER A 362     5268   5282   5206    -74      2    201       O  
ATOM   2679  CB  SER A 362       9.756  15.055   4.946  1.00 45.79           C  
ANISOU 2679  CB  SER A 362     5792   5826   5779    -58    -29    211       C  
ATOM   2680  OG  SER A 362       8.444  15.125   5.470  1.00 49.64           O  
ANISOU 2680  OG  SER A 362     6269   6312   6278    -49    -46    220       O  
ATOM   2681  N   ILE A 363      12.828  14.990   5.438  1.00 39.51           N  
ANISOU 2681  N   ILE A 363     4988   5038   4983    -63     15    194       N  
ATOM   2682  CA  ILE A 363      14.058  14.651   4.750  1.00 36.46           C  
ANISOU 2682  CA  ILE A 363     4609   4650   4591    -73     34    182       C  
ATOM   2683  C   ILE A 363      14.120  13.145   4.882  1.00 34.46           C  
ANISOU 2683  C   ILE A 363     4343   4396   4353    -70     38    175       C  
ATOM   2684  O   ILE A 363      13.538  12.574   5.804  1.00 33.02           O  
ANISOU 2684  O   ILE A 363     4142   4216   4186    -60     30    181       O  
ATOM   2685  CB  ILE A 363      15.310  15.295   5.385  1.00 35.85           C  
ANISOU 2685  CB  ILE A 363     4525   4577   4518    -72     49    180       C  
ATOM   2686  CG1 ILE A 363      15.259  15.194   6.909  1.00 35.12           C  
ANISOU 2686  CG1 ILE A 363     4408   4489   4444    -59     46    187       C  
ATOM   2687  CG2 ILE A 363      15.493  16.741   4.917  1.00 34.48           C  
ANISOU 2687  CG2 ILE A 363     4370   4404   4328    -78     49    183       C  
ATOM   2688  CD1 ILE A 363      16.556  15.576   7.583  1.00 36.09           C  
ANISOU 2688  CD1 ILE A 363     4522   4616   4574    -59     61    184       C  
ATOM   2689  N   SER A 364      14.780  12.494   3.942  1.00 33.71           N  
ANISOU 2689  N   SER A 364     4257   4297   4253    -80     51    162       N  
ATOM   2690  CA  SER A 364      14.954  11.063   4.044  1.00 33.35           C  
ANISOU 2690  CA  SER A 364     4198   4249   4224    -78     57    154       C  
ATOM   2691  C   SER A 364      16.386  10.761   4.457  1.00 32.98           C  
ANISOU 2691  C   SER A 364     4137   4202   4191    -78     77    145       C  
ATOM   2692  O   SER A 364      17.295  11.525   4.158  1.00 33.41           O  
ANISOU 2692  O   SER A 364     4200   4257   4237    -85     90    140       O  
ATOM   2693  CB  SER A 364      14.563  10.363   2.744  1.00 32.87           C  
ANISOU 2693  CB  SER A 364     4154   4183   4152    -89     56    144       C  
ATOM   2694  OG  SER A 364      14.973  11.117   1.627  1.00 33.85           O  
ANISOU 2694  OG  SER A 364     4303   4306   4252   -103     64    138       O  
ATOM   2695  N   PHE A 365      16.566   9.665   5.181  1.00 33.32           N  
ANISOU 2695  N   PHE A 365     4157   4243   4257    -71     78    144       N  
ATOM   2696  CA  PHE A 365      17.883   9.240   5.607  1.00 34.36           C  
ANISOU 2696  CA  PHE A 365     4273   4372   4408    -71     95    136       C  
ATOM   2697  C   PHE A 365      18.777   8.918   4.411  1.00 35.93           C  
ANISOU 2697  C   PHE A 365     4483   4564   4602    -84    115    118       C  
ATOM   2698  O   PHE A 365      18.313   8.359   3.420  1.00 37.45           O  
ANISOU 2698  O   PHE A 365     4689   4754   4786    -90    115    109       O  
ATOM   2699  CB  PHE A 365      17.778   8.022   6.529  1.00 33.34           C  
ANISOU 2699  CB  PHE A 365     4119   4241   4306    -63     89    140       C  
ATOM   2700  CG  PHE A 365      19.098   7.574   7.070  1.00 32.41           C  
ANISOU 2700  CG  PHE A 365     3982   4119   4211    -62    103    134       C  
ATOM   2701  CD1 PHE A 365      19.639   8.182   8.197  1.00 31.28           C  
ANISOU 2701  CD1 PHE A 365     3827   3981   4077    -57    102    144       C  
ATOM   2702  CD2 PHE A 365      19.821   6.572   6.430  1.00 31.70           C  
ANISOU 2702  CD2 PHE A 365     3887   4020   4136    -67    117    118       C  
ATOM   2703  CE1 PHE A 365      20.869   7.787   8.683  1.00 30.42           C  
ANISOU 2703  CE1 PHE A 365     3700   3867   3990    -57    113    140       C  
ATOM   2704  CE2 PHE A 365      21.052   6.176   6.916  1.00 31.40           C  
ANISOU 2704  CE2 PHE A 365     3830   3976   4123    -67    129    113       C  
ATOM   2705  CZ  PHE A 365      21.575   6.788   8.039  1.00 30.53           C  
ANISOU 2705  CZ  PHE A 365     3708   3871   4021    -62    126    125       C  
ATOM   2706  N   LYS A 366      20.051   9.300   4.517  1.00 38.31           N  
ANISOU 2706  N   LYS A 366     4780   4864   4909    -87    133    111       N  
ATOM   2707  CA  LYS A 366      21.099   8.950   3.557  1.00 39.20           C  
ANISOU 2707  CA  LYS A 366     4898   4970   5024    -98    156     92       C  
ATOM   2708  C   LYS A 366      22.276   8.352   4.309  1.00 38.48           C  
ANISOU 2708  C   LYS A 366     4781   4873   4964    -94    168     87       C  
ATOM   2709  O   LYS A 366      22.601   8.813   5.402  1.00 38.36           O  
ANISOU 2709  O   LYS A 366     4752   4861   4959    -86    162     98       O  
ATOM   2710  CB  LYS A 366      21.576  10.199   2.811  1.00 42.63           C  
ANISOU 2710  CB  LYS A 366     5355   5407   5433   -109    167     88       C  
ATOM   2711  CG  LYS A 366      20.970  10.407   1.427  1.00 46.49           C  
ANISOU 2711  CG  LYS A 366     5874   5896   5892   -122    167     82       C  
ATOM   2712  CD  LYS A 366      21.433  11.709   0.772  1.00 49.50           C  
ANISOU 2712  CD  LYS A 366     6277   6281   6249   -134    175     82       C  
ATOM   2713  CE  LYS A 366      22.908  11.691   0.370  1.00 55.07           C  
ANISOU 2713  CE  LYS A 366     6981   6982   6961   -143    204     65       C  
ATOM   2714  NZ  LYS A 366      23.855  12.173   1.430  1.00 55.92           N  
ANISOU 2714  NZ  LYS A 366     7067   7089   7087   -135    210     70       N  
ATOM   2715  N   LYS A 367      22.899   7.322   3.727  1.00 40.28           N  
ANISOU 2715  N   LYS A 367     5002   5092   5208    -99    184     69       N  
ATOM   2716  CA  LYS A 367      24.168   6.735   4.219  1.00 39.37           C  
ANISOU 2716  CA  LYS A 367     4863   4969   5127    -98    198     61       C  
ATOM   2717  C   LYS A 367      25.091   7.761   4.910  1.00 37.30           C  
ANISOU 2717  C   LYS A 367     4595   4709   4868    -96    203     68       C  
ATOM   2718  O   LYS A 367      25.370   8.823   4.357  1.00 35.08           O  
ANISOU 2718  O   LYS A 367     4332   4432   4564   -103    212     65       O  
ATOM   2719  CB  LYS A 367      24.937   6.111   3.035  1.00 42.81           C  
ANISOU 2719  CB  LYS A 367     5302   5394   5567   -110    223     35       C  
ATOM   2720  CG  LYS A 367      25.140   4.596   3.044  1.00 45.15           C  
ANISOU 2720  CG  LYS A 367     5579   5680   5897   -107    228     23       C  
ATOM   2721  CD  LYS A 367      23.883   3.812   2.675  1.00 48.53           C  
ANISOU 2721  CD  LYS A 367     6014   6108   6316   -106    213     24       C  
ATOM   2722  CE  LYS A 367      24.193   2.338   2.436  1.00 47.78           C  
ANISOU 2722  CE  LYS A 367     5900   6000   6252   -107    222      8       C  
ATOM   2723  NZ  LYS A 367      22.994   1.471   2.626  1.00 47.86           N  
ANISOU 2723  NZ  LYS A 367     5908   6011   6265   -100    201     16       N  
ATOM   2724  N   VAL A 368      25.538   7.459   6.126  1.00 35.34           N  
ANISOU 2724  N   VAL A 368     4320   4458   4646    -87    196     78       N  
ATOM   2725  CA  VAL A 368      26.660   8.197   6.715  1.00 34.63           C  
ANISOU 2725  CA  VAL A 368     4222   4369   4567    -87    204     80       C  
ATOM   2726  C   VAL A 368      27.796   7.235   7.037  1.00 34.83           C  
ANISOU 2726  C   VAL A 368     4221   4381   4633    -86    214     71       C  
ATOM   2727  O   VAL A 368      27.595   6.023   7.102  1.00 34.87           O  
ANISOU 2727  O   VAL A 368     4211   4378   4659    -83    210     68       O  
ATOM   2728  CB  VAL A 368      26.295   9.065   7.961  1.00 34.24           C  
ANISOU 2728  CB  VAL A 368     4169   4329   4511    -78    185    102       C  
ATOM   2729  CG1 VAL A 368      25.389  10.229   7.584  1.00 33.47           C  
ANISOU 2729  CG1 VAL A 368     4097   4242   4378    -80    178    109       C  
ATOM   2730  CG2 VAL A 368      25.684   8.247   9.086  1.00 34.30           C  
ANISOU 2730  CG2 VAL A 368     4157   4338   4536    -69    164    116       C  
ATOM   2731  N   ALA A 369      29.000   7.770   7.199  1.00 35.05           N  
ANISOU 2731  N   ALA A 369     4241   4404   4672    -89    228     67       N  
ATOM   2732  CA  ALA A 369      30.135   6.950   7.606  1.00 34.47           C  
ANISOU 2732  CA  ALA A 369     4140   4317   4640    -88    236     61       C  
ATOM   2733  C   ALA A 369      30.805   7.613   8.803  1.00 34.28           C  
ANISOU 2733  C   ALA A 369     4101   4294   4628    -83    226     76       C  
ATOM   2734  O   ALA A 369      31.659   8.488   8.641  1.00 32.95           O  
ANISOU 2734  O   ALA A 369     3936   4125   4456    -88    239     72       O  
ATOM   2735  CB  ALA A 369      31.109   6.753   6.452  1.00 33.44           C  
ANISOU 2735  CB  ALA A 369     4011   4175   4518    -99    265     35       C  
ATOM   2736  N   LEU A 370      30.377   7.205  10.003  1.00 33.30           N  
ANISOU 2736  N   LEU A 370     3962   4173   4517    -75    203     94       N  
ATOM   2737  CA  LEU A 370      30.852   7.785  11.257  1.00 31.42           C  
ANISOU 2737  CA  LEU A 370     3712   3937   4287    -72    190    111       C  
ATOM   2738  C   LEU A 370      31.366   6.690  12.184  1.00 31.91           C  
ANISOU 2738  C   LEU A 370     3744   3988   4390    -68    179    118       C  
ATOM   2739  O   LEU A 370      30.666   6.275  13.105  1.00 31.94           O  
ANISOU 2739  O   LEU A 370     3741   3997   4396    -63    157    135       O  
ATOM   2740  CB  LEU A 370      29.732   8.586  11.929  1.00 30.50           C  
ANISOU 2740  CB  LEU A 370     3611   3838   4140    -67    171    129       C  
ATOM   2741  CG  LEU A 370      29.055   9.672  11.070  1.00 30.28           C  
ANISOU 2741  CG  LEU A 370     3611   3820   4072    -70    178    125       C  
ATOM   2742  CD1 LEU A 370      27.760  10.170  11.689  1.00 28.20           C  
ANISOU 2742  CD1 LEU A 370     3359   3571   3785    -64    158    141       C  
ATOM   2743  CD2 LEU A 370      30.017  10.822  10.795  1.00 30.07           C  
ANISOU 2743  CD2 LEU A 370     3592   3793   4038    -75    193    120       C  
ATOM   2744  N   PRO A 371      32.605   6.216  11.944  1.00 32.41           N  
ANISOU 2744  N   PRO A 371     3789   4035   4487    -72    193    106       N  
ATOM   2745  CA  PRO A 371      33.201   5.112  12.719  1.00 31.85           C  
ANISOU 2745  CA  PRO A 371     3687   3950   4461    -70    182    111       C  
ATOM   2746  C   PRO A 371      33.159   5.259  14.257  1.00 31.28           C  
ANISOU 2746  C   PRO A 371     3604   3884   4397    -66    155    137       C  
ATOM   2747  O   PRO A 371      32.960   4.255  14.952  1.00 32.30           O  
ANISOU 2747  O   PRO A 371     3715   4007   4549    -64    138    147       O  
ATOM   2748  CB  PRO A 371      34.650   5.064  12.215  1.00 32.04           C  
ANISOU 2748  CB  PRO A 371     3698   3958   4517    -75    204     94       C  
ATOM   2749  CG  PRO A 371      34.877   6.378  11.527  1.00 32.04           C  
ANISOU 2749  CG  PRO A 371     3721   3967   4485    -79    222     86       C  
ATOM   2750  CD  PRO A 371      33.550   6.744  10.943  1.00 31.95           C  
ANISOU 2750  CD  PRO A 371     3738   3972   4430    -79    220     86       C  
ATOM   2751  N   SER A 372      33.336   6.473  14.779  1.00 29.98           N  
ANISOU 2751  N   SER A 372     3449   3729   4211    -67    152    147       N  
ATOM   2752  CA  SER A 372      33.268   6.717  16.235  1.00 29.90           C  
ANISOU 2752  CA  SER A 372     3431   3726   4202    -65    128    170       C  
ATOM   2753  C   SER A 372      31.854   6.830  16.835  1.00 30.70           C  
ANISOU 2753  C   SER A 372     3545   3844   4273    -62    109    185       C  
ATOM   2754  O   SER A 372      31.726   6.974  18.058  1.00 32.33           O  
ANISOU 2754  O   SER A 372     3746   4057   4478    -62     90    204       O  
ATOM   2755  CB  SER A 372      34.011   7.997  16.606  1.00 28.42           C  
ANISOU 2755  CB  SER A 372     3249   3543   4004    -68    131    174       C  
ATOM   2756  OG  SER A 372      35.382   7.901  16.332  1.00 28.78           O  
ANISOU 2756  OG  SER A 372     3279   3572   4083    -72    144    164       O  
ATOM   2757  N   LEU A 373      30.811   6.781  16.000  1.00 29.48           N  
ANISOU 2757  N   LEU A 373     3408   3697   4094    -60    116    177       N  
ATOM   2758  CA  LEU A 373      29.460   7.151  16.437  1.00 28.93           C  
ANISOU 2758  CA  LEU A 373     3354   3644   3993    -56    102    189       C  
ATOM   2759  C   LEU A 373      28.843   6.210  17.469  1.00 28.40           C  
ANISOU 2759  C   LEU A 373     3273   3579   3938    -55     80    206       C  
ATOM   2760  O   LEU A 373      28.609   5.039  17.191  1.00 28.80           O  
ANISOU 2760  O   LEU A 373     3313   3621   4007    -54     77    203       O  
ATOM   2761  CB  LEU A 373      28.519   7.305  15.234  1.00 28.92           C  
ANISOU 2761  CB  LEU A 373     3373   3647   3965    -55    113    177       C  
ATOM   2762  CG  LEU A 373      27.090   7.826  15.454  1.00 28.55           C  
ANISOU 2762  CG  LEU A 373     3344   3616   3886    -51    101    186       C  
ATOM   2763  CD1 LEU A 373      27.077   9.297  15.840  1.00 28.71           C  
ANISOU 2763  CD1 LEU A 373     3378   3648   3881    -52    101    192       C  
ATOM   2764  CD2 LEU A 373      26.269   7.611  14.198  1.00 28.17           C  
ANISOU 2764  CD2 LEU A 373     3311   3568   3821    -51    110    174       C  
ATOM   2765  N   SER A 374      28.563   6.741  18.649  1.00 27.11           N  
ANISOU 2765  N   SER A 374     3110   3426   3762    -56     64    223       N  
ATOM   2766  CA  SER A 374      27.876   5.977  19.676  1.00 27.51           C  
ANISOU 2766  CA  SER A 374     3151   3482   3818    -56     43    240       C  
ATOM   2767  C   SER A 374      26.445   6.476  19.995  1.00 27.89           C  
ANISOU 2767  C   SER A 374     3216   3548   3833    -53     36    248       C  
ATOM   2768  O   SER A 374      25.613   5.701  20.456  1.00 29.42           O  
ANISOU 2768  O   SER A 374     3405   3745   4028    -53     23    257       O  
ATOM   2769  CB  SER A 374      28.716   5.935  20.952  1.00 27.38           C  
ANISOU 2769  CB  SER A 374     3119   3463   3820    -61     28    256       C  
ATOM   2770  OG  SER A 374      28.652   7.158  21.657  1.00 26.95           O  
ANISOU 2770  OG  SER A 374     3076   3422   3740    -64     25    264       O  
ATOM   2771  N   TYR A 375      26.170   7.755  19.741  1.00 27.12           N  
ANISOU 2771  N   TYR A 375     3137   3460   3706    -52     44    243       N  
ATOM   2772  CA  TYR A 375      24.909   8.389  20.128  1.00 26.55           C  
ANISOU 2772  CA  TYR A 375     3079   3403   3605    -50     38    250       C  
ATOM   2773  C   TYR A 375      24.226   9.057  18.922  1.00 26.34           C  
ANISOU 2773  C   TYR A 375     3072   3380   3555    -46     51    237       C  
ATOM   2774  O   TYR A 375      24.815   9.927  18.259  1.00 26.41           O  
ANISOU 2774  O   TYR A 375     3091   3386   3556    -46     63    227       O  
ATOM   2775  CB  TYR A 375      25.170   9.408  21.244  1.00 26.03           C  
ANISOU 2775  CB  TYR A 375     3015   3347   3526    -54     32    260       C  
ATOM   2776  CG  TYR A 375      23.938  10.110  21.737  1.00 26.35           C  
ANISOU 2776  CG  TYR A 375     3068   3403   3540    -52     27    265       C  
ATOM   2777  CD1 TYR A 375      23.305   9.702  22.909  1.00 26.25           C  
ANISOU 2777  CD1 TYR A 375     3049   3399   3524    -55     13    279       C  
ATOM   2778  CD2 TYR A 375      23.394  11.192  21.027  1.00 27.08           C  
ANISOU 2778  CD2 TYR A 375     3178   3500   3608    -48     37    256       C  
ATOM   2779  CE1 TYR A 375      22.157  10.340  23.360  1.00 26.73           C  
ANISOU 2779  CE1 TYR A 375     3120   3473   3562    -54     10    283       C  
ATOM   2780  CE2 TYR A 375      22.252  11.847  21.473  1.00 27.28           C  
ANISOU 2780  CE2 TYR A 375     3213   3538   3612    -46     32    260       C  
ATOM   2781  CZ  TYR A 375      21.635  11.416  22.639  1.00 27.12           C  
ANISOU 2781  CZ  TYR A 375     3186   3527   3592    -49     20    272       C  
ATOM   2782  OH  TYR A 375      20.502  12.062  23.080  1.00 27.13           O  
ANISOU 2782  OH  TYR A 375     3195   3539   3573    -48     18    275       O  
ATOM   2783  N   LEU A 376      22.991   8.651  18.638  1.00 25.31           N  
ANISOU 2783  N   LEU A 376     2947   3253   3414    -42     46    237       N  
ATOM   2784  CA  LEU A 376      22.287   9.149  17.447  1.00 25.16           C  
ANISOU 2784  CA  LEU A 376     2947   3236   3377    -39     54    226       C  
ATOM   2785  C   LEU A 376      20.829   9.544  17.721  1.00 25.63           C  
ANISOU 2785  C   LEU A 376     3015   3305   3415    -36     45    233       C  
ATOM   2786  O   LEU A 376      19.960   8.685  17.959  1.00 25.52           O  
ANISOU 2786  O   LEU A 376     2996   3294   3406    -34     36    238       O  
ATOM   2787  CB  LEU A 376      22.376   8.137  16.303  1.00 24.27           C  
ANISOU 2787  CB  LEU A 376     2832   3111   3276    -39     62    214       C  
ATOM   2788  CG  LEU A 376      21.957   8.569  14.896  1.00 24.28           C  
ANISOU 2788  CG  LEU A 376     2853   3111   3259    -39     72    201       C  
ATOM   2789  CD1 LEU A 376      22.590   9.896  14.495  1.00 24.30           C  
ANISOU 2789  CD1 LEU A 376     2870   3115   3246    -42     84    195       C  
ATOM   2790  CD2 LEU A 376      22.301   7.491  13.878  1.00 23.95           C  
ANISOU 2790  CD2 LEU A 376     2808   3057   3233    -41     81    188       C  
ATOM   2791  N   ASP A 377      20.583  10.854  17.708  1.00 25.87           N  
ANISOU 2791  N   ASP A 377     3059   3343   3425    -35     49    232       N  
ATOM   2792  CA  ASP A 377      19.241  11.407  17.865  1.00 25.77           C  
ANISOU 2792  CA  ASP A 377     3056   3340   3395    -32     42    236       C  
ATOM   2793  C   ASP A 377      18.811  12.053  16.551  1.00 26.13           C  
ANISOU 2793  C   ASP A 377     3120   3382   3425    -30     48    226       C  
ATOM   2794  O   ASP A 377      19.284  13.131  16.184  1.00 26.33           O  
ANISOU 2794  O   ASP A 377     3156   3407   3439    -32     56    221       O  
ATOM   2795  CB  ASP A 377      19.190  12.416  19.017  1.00 25.80           C  
ANISOU 2795  CB  ASP A 377     3060   3353   3388    -33     39    243       C  
ATOM   2796  CG  ASP A 377      17.765  12.893  19.326  1.00 26.75           C  
ANISOU 2796  CG  ASP A 377     3186   3482   3495    -29     32    247       C  
ATOM   2797  OD1 ASP A 377      17.579  13.707  20.264  1.00 27.03           O  
ANISOU 2797  OD1 ASP A 377     3221   3525   3521    -30     30    251       O  
ATOM   2798  OD2 ASP A 377      16.820  12.462  18.631  1.00 26.77           O  
ANISOU 2798  OD2 ASP A 377     3193   3482   3495    -26     29    245       O  
ATOM   2799  N   LEU A 378      17.928  11.361  15.841  1.00 26.32           N  
ANISOU 2799  N   LEU A 378     3148   3403   3448    -28     44    223       N  
ATOM   2800  CA  LEU A 378      17.313  11.867  14.609  1.00 25.94           C  
ANISOU 2800  CA  LEU A 378     3118   3352   3385    -28     46    216       C  
ATOM   2801  C   LEU A 378      15.790  11.988  14.797  1.00 25.54           C  
ANISOU 2801  C   LEU A 378     3071   3307   3327    -24     34    222       C  
ATOM   2802  O   LEU A 378      15.012  11.743  13.860  1.00 25.88           O  
ANISOU 2802  O   LEU A 378     3123   3345   3364    -23     30    219       O  
ATOM   2803  CB  LEU A 378      17.611  10.902  13.456  1.00 25.73           C  
ANISOU 2803  CB  LEU A 378     3094   3316   3364    -31     52    206       C  
ATOM   2804  CG  LEU A 378      18.867  10.950  12.581  1.00 25.43           C  
ANISOU 2804  CG  LEU A 378     3061   3270   3328    -37     68    194       C  
ATOM   2805  CD1 LEU A 378      19.957  11.860  13.108  1.00 24.95           C  
ANISOU 2805  CD1 LEU A 378     2999   3211   3268    -39     76    195       C  
ATOM   2806  CD2 LEU A 378      19.376   9.535  12.361  1.00 25.24           C  
ANISOU 2806  CD2 LEU A 378     3025   3238   3325    -38     72    188       C  
ATOM   2807  N   SER A 379      15.381  12.358  16.009  1.00 23.92           N  
ANISOU 2807  N   SER A 379     2857   3109   3121    -21     28    231       N  
ATOM   2808  CA  SER A 379      13.988  12.401  16.391  1.00 23.52           C  
ANISOU 2808  CA  SER A 379     2805   3063   3068    -17     18    237       C  
ATOM   2809  C   SER A 379      13.274  13.618  15.814  1.00 23.71           C  
ANISOU 2809  C   SER A 379     2843   3086   3077    -15     17    234       C  
ATOM   2810  O   SER A 379      13.917  14.605  15.462  1.00 23.62           O  
ANISOU 2810  O   SER A 379     2842   3074   3058    -17     23    230       O  
ATOM   2811  CB  SER A 379      13.875  12.412  17.919  1.00 23.88           C  
ANISOU 2811  CB  SER A 379     2836   3118   3117    -17     15    246       C  
ATOM   2812  OG  SER A 379      14.074  13.712  18.466  1.00 23.51           O  
ANISOU 2812  OG  SER A 379     2794   3076   3060    -18     19    246       O  
ATOM   2813  N   ARG A 380      11.944  13.540  15.713  1.00 24.09           N  
ANISOU 2813  N   ARG A 380     2892   3135   3125    -12      7    237       N  
ATOM   2814  CA  ARG A 380      11.101  14.717  15.440  1.00 24.17           C  
ANISOU 2814  CA  ARG A 380     2912   3144   3127    -10      3    237       C  
ATOM   2815  C   ARG A 380      11.428  15.443  14.115  1.00 24.99           C  
ANISOU 2815  C   ARG A 380     3034   3240   3219    -13      4    231       C  
ATOM   2816  O   ARG A 380      11.481  16.669  14.075  1.00 25.81           O  
ANISOU 2816  O   ARG A 380     3146   3344   3316    -13      5    231       O  
ATOM   2817  CB  ARG A 380      11.190  15.692  16.623  1.00 23.35           C  
ANISOU 2817  CB  ARG A 380     2802   3048   3021     -9      6    239       C  
ATOM   2818  CG  ARG A 380      10.264  15.356  17.765  1.00 23.93           C  
ANISOU 2818  CG  ARG A 380     2862   3129   3102     -6      2    245       C  
ATOM   2819  CD  ARG A 380      10.722  15.938  19.088  1.00 24.49           C  
ANISOU 2819  CD  ARG A 380     2925   3208   3170     -8      8    246       C  
ATOM   2820  NE  ARG A 380      11.693  15.019  19.673  1.00 26.67           N  
ANISOU 2820  NE  ARG A 380     3192   3488   3451    -13     11    250       N  
ATOM   2821  CZ  ARG A 380      11.572  14.378  20.833  1.00 26.26           C  
ANISOU 2821  CZ  ARG A 380     3128   3445   3404    -15      9    256       C  
ATOM   2822  NH1 ARG A 380      10.521  14.548  21.625  1.00 24.78           N  
ANISOU 2822  NH1 ARG A 380     2934   3263   3216    -15      7    259       N  
ATOM   2823  NH2 ARG A 380      12.549  13.564  21.197  1.00 27.67           N  
ANISOU 2823  NH2 ARG A 380     3300   3624   3589    -20     10    260       N  
ATOM   2824  N   ASN A 381      11.663  14.694  13.043  1.00 25.54           N  
ANISOU 2824  N   ASN A 381     3113   3304   3288    -16      5    227       N  
ATOM   2825  CA  ASN A 381      12.091  15.290  11.773  1.00 26.84           C  
ANISOU 2825  CA  ASN A 381     3295   3461   3438    -22      8    221       C  
ATOM   2826  C   ASN A 381      11.155  14.973  10.629  1.00 27.08           C  
ANISOU 2826  C   ASN A 381     3338   3485   3464    -24     -1    221       C  
ATOM   2827  O   ASN A 381      11.489  15.254   9.480  1.00 27.69           O  
ANISOU 2827  O   ASN A 381     3433   3558   3530    -31      0    216       O  
ATOM   2828  CB  ASN A 381      13.503  14.803  11.360  1.00 27.23           C  
ANISOU 2828  CB  ASN A 381     3347   3509   3488    -27     22    214       C  
ATOM   2829  CG  ASN A 381      14.605  15.363  12.238  1.00 27.61           C  
ANISOU 2829  CG  ASN A 381     3388   3563   3540    -27     32    214       C  
ATOM   2830  OD1 ASN A 381      14.682  16.570  12.474  1.00 27.88           O  
ANISOU 2830  OD1 ASN A 381     3427   3598   3566    -27     32    216       O  
ATOM   2831  ND2 ASN A 381      15.474  14.482  12.723  1.00 27.45           N  
ANISOU 2831  ND2 ASN A 381     3354   3542   3531    -28     39    212       N  
ATOM   2832  N   ALA A 382       9.998  14.382  10.920  1.00 27.21           N  
ANISOU 2832  N   ALA A 382     3347   3502   3489    -19    -13    226       N  
ATOM   2833  CA  ALA A 382       9.178  13.798   9.866  1.00 28.30           C  
ANISOU 2833  CA  ALA A 382     3494   3633   3624    -21    -23    225       C  
ATOM   2834  C   ALA A 382      10.115  13.043   8.906  1.00 29.95           C  
ANISOU 2834  C   ALA A 382     3712   3838   3827    -29    -14    216       C  
ATOM   2835  O   ALA A 382       9.899  12.998   7.686  1.00 31.39           O  
ANISOU 2835  O   ALA A 382     3912   4015   3999    -36    -18    212       O  
ATOM   2836  CB  ALA A 382       8.370  14.867   9.138  1.00 27.06           C  
ANISOU 2836  CB  ALA A 382     3352   3470   3458    -23    -35    228       C  
ATOM   2837  N   LEU A 383      11.163  12.460   9.495  1.00 30.82           N  
ANISOU 2837  N   LEU A 383     3810   3951   3946    -29     -1    212       N  
ATOM   2838  CA  LEU A 383      12.210  11.733   8.784  1.00 31.08           C  
ANISOU 2838  CA  LEU A 383     3848   3981   3979    -35     11    202       C  
ATOM   2839  C   LEU A 383      11.661  10.444   8.212  1.00 30.88           C  
ANISOU 2839  C   LEU A 383     3822   3951   3960    -36      5    198       C  
ATOM   2840  O   LEU A 383      10.860   9.767   8.834  1.00 31.82           O  
ANISOU 2840  O   LEU A 383     3927   4071   4091    -30     -3    204       O  
ATOM   2841  CB  LEU A 383      13.382  11.447   9.739  1.00 31.32           C  
ANISOU 2841  CB  LEU A 383     3861   4014   4022    -33     23    200       C  
ATOM   2842  CG  LEU A 383      14.757  10.828   9.427  1.00 30.47           C  
ANISOU 2842  CG  LEU A 383     3751   3903   3921    -38     39    190       C  
ATOM   2843  CD1 LEU A 383      14.778   9.330   9.692  1.00 30.60           C  
ANISOU 2843  CD1 LEU A 383     3751   3917   3957    -36     38    188       C  
ATOM   2844  CD2 LEU A 383      15.239  11.155   8.029  1.00 30.62           C  
ANISOU 2844  CD2 LEU A 383     3790   3917   3925    -48     49    179       C  
ATOM   2845  N   SER A 384      12.110  10.132   7.011  1.00 31.14           N  
ANISOU 2845  N   SER A 384     3869   3977   3983    -45     13    187       N  
ATOM   2846  CA  SER A 384      11.723   8.950   6.287  1.00 31.69           C  
ANISOU 2846  CA  SER A 384     3941   4042   4057    -48      9    181       C  
ATOM   2847  C   SER A 384      12.996   8.111   6.063  1.00 33.74           C  
ANISOU 2847  C   SER A 384     4194   4298   4326    -53     28    168       C  
ATOM   2848  O   SER A 384      13.974   8.565   5.470  1.00 33.70           O  
ANISOU 2848  O   SER A 384     4200   4292   4312    -60     42    159       O  
ATOM   2849  CB  SER A 384      11.003   9.375   4.997  1.00 31.42           C  
ANISOU 2849  CB  SER A 384     3931   4003   4002    -56      0    179       C  
ATOM   2850  OG  SER A 384      11.604   8.890   3.816  1.00 31.76           O  
ANISOU 2850  OG  SER A 384     3988   4041   4035    -68     11    166       O  
ATOM   2851  N   PHE A 385      12.984   6.898   6.595  1.00 34.78           N  
ANISOU 2851  N   PHE A 385     4307   4427   4478    -48     27    168       N  
ATOM   2852  CA  PHE A 385      14.146   6.040   6.604  1.00 35.52           C  
ANISOU 2852  CA  PHE A 385     4389   4516   4588    -50     42    157       C  
ATOM   2853  C   PHE A 385      13.692   4.745   5.958  1.00 35.22           C  
ANISOU 2853  C   PHE A 385     4351   4472   4559    -52     39    149       C  
ATOM   2854  O   PHE A 385      12.880   4.021   6.533  1.00 37.17           O  
ANISOU 2854  O   PHE A 385     4584   4719   4819    -46     25    157       O  
ATOM   2855  CB  PHE A 385      14.591   5.812   8.063  1.00 36.57           C  
ANISOU 2855  CB  PHE A 385     4497   4653   4742    -42     41    166       C  
ATOM   2856  CG  PHE A 385      15.962   5.182   8.223  1.00 38.34           C  
ANISOU 2856  CG  PHE A 385     4707   4871   4985    -44     56    157       C  
ATOM   2857  CD1 PHE A 385      16.851   5.675   9.177  1.00 39.89           C  
ANISOU 2857  CD1 PHE A 385     4893   5072   5191    -42     61    163       C  
ATOM   2858  CD2 PHE A 385      16.364   4.090   7.454  1.00 40.27           C  
ANISOU 2858  CD2 PHE A 385     4950   5108   5243    -49     65    143       C  
ATOM   2859  CE1 PHE A 385      18.112   5.099   9.354  1.00 39.92           C  
ANISOU 2859  CE1 PHE A 385     4882   5069   5216    -44     74    156       C  
ATOM   2860  CE2 PHE A 385      17.625   3.513   7.626  1.00 41.60           C  
ANISOU 2860  CE2 PHE A 385     5103   5269   5433    -51     79    134       C  
ATOM   2861  CZ  PHE A 385      18.497   4.013   8.582  1.00 39.65           C  
ANISOU 2861  CZ  PHE A 385     4844   5024   5196    -48     82    141       C  
ATOM   2862  N   SER A 386      14.177   4.454   4.758  1.00 34.65           N  
ANISOU 2862  N   SER A 386     4292   4394   4479    -62     51    133       N  
ATOM   2863  CA  SER A 386      13.847   3.173   4.153  1.00 36.74           C  
ANISOU 2863  CA  SER A 386     4554   4650   4753    -65     49    123       C  
ATOM   2864  C   SER A 386      15.072   2.278   4.163  1.00 37.58           C  
ANISOU 2864  C   SER A 386     4646   4750   4883    -67     67    109       C  
ATOM   2865  O   SER A 386      16.109   2.637   3.618  1.00 39.74           O  
ANISOU 2865  O   SER A 386     4927   5021   5150    -75     86     96       O  
ATOM   2866  CB  SER A 386      13.277   3.332   2.743  1.00 37.73           C  
ANISOU 2866  CB  SER A 386     4707   4773   4853    -76     47    115       C  
ATOM   2867  OG  SER A 386      14.254   3.096   1.755  1.00 37.90           O  
ANISOU 2867  OG  SER A 386     4739   4790   4870    -88     68     95       O  
ATOM   2868  N   GLY A 387      14.943   1.123   4.804  1.00 37.76           N  
ANISOU 2868  N   GLY A 387     4646   4767   4931    -60     61    112       N  
ATOM   2869  CA  GLY A 387      16.047   0.199   4.975  1.00 39.45           C  
ANISOU 2869  CA  GLY A 387     4841   4973   5174    -61     75    100       C  
ATOM   2870  C   GLY A 387      16.704   0.291   6.335  1.00 41.11           C  
ANISOU 2870  C   GLY A 387     5028   5185   5405    -53     73    113       C  
ATOM   2871  O   GLY A 387      17.921   0.367   6.421  1.00 47.13           O  
ANISOU 2871  O   GLY A 387     5783   5944   6180    -56     89    105       O  
ATOM   2872  N   CYS A 388      15.911   0.298   7.400  1.00 41.44           N  
ANISOU 2872  N   CYS A 388     5060   5234   5451    -45     55    132       N  
ATOM   2873  CA  CYS A 388      16.460   0.193   8.746  1.00 42.56           C  
ANISOU 2873  CA  CYS A 388     5179   5378   5614    -39     51    145       C  
ATOM   2874  C   CYS A 388      16.692  -1.266   9.082  1.00 41.84           C  
ANISOU 2874  C   CYS A 388     5065   5277   5556    -37     48    143       C  
ATOM   2875  O   CYS A 388      15.823  -2.100   8.851  1.00 40.68           O  
ANISOU 2875  O   CYS A 388     4916   5126   5414    -36     38    144       O  
ATOM   2876  CB  CYS A 388      15.510   0.772   9.786  1.00 46.46           C  
ANISOU 2876  CB  CYS A 388     5670   5883   6097    -33     34    165       C  
ATOM   2877  SG  CYS A 388      16.232   1.465  11.302  1.00 53.15           S  
ANISOU 2877  SG  CYS A 388     6504   6738   6952    -30     33    180       S  
ATOM   2878  N   CYS A 389      17.878  -1.599   9.577  1.00 43.26           N  
ANISOU 2878  N   CYS A 389     5226   5449   5760    -38     55    141       N  
ATOM   2879  CA  CYS A 389      19.086  -0.770   9.488  1.00 44.14           C  
ANISOU 2879  CA  CYS A 389     5341   5560   5869    -41     71    134       C  
ATOM   2880  C   CYS A 389      20.234  -1.605   9.982  1.00 42.24           C  
ANISOU 2880  C   CYS A 389     5074   5307   5666    -41     76    131       C  
ATOM   2881  O   CYS A 389      20.038  -2.548  10.748  1.00 41.53           O  
ANISOU 2881  O   CYS A 389     4965   5213   5600    -38     62    142       O  
ATOM   2882  CB  CYS A 389      19.005   0.549  10.265  1.00 48.25           C  
ANISOU 2882  CB  CYS A 389     5868   6094   6369    -39     66    149       C  
ATOM   2883  SG  CYS A 389      17.992   0.468  11.745  1.00 57.15           S  
ANISOU 2883  SG  CYS A 389     6984   7231   7498    -32     43    174       S  
ATOM   2884  N   SER A 390      21.428  -1.258   9.519  1.00 39.24           N  
ANISOU 2884  N   SER A 390     4695   4921   5292    -46     95    117       N  
ATOM   2885  CA  SER A 390      22.614  -2.028   9.787  1.00 36.40           C  
ANISOU 2885  CA  SER A 390     4311   4547   4970    -47    102    111       C  
ATOM   2886  C   SER A 390      23.822  -1.111   9.825  1.00 36.97           C  
ANISOU 2886  C   SER A 390     4385   4619   5043    -51    117    106       C  
ATOM   2887  O   SER A 390      23.718   0.104   9.599  1.00 35.39           O  
ANISOU 2887  O   SER A 390     4204   4429   4811    -52    122    107       O  
ATOM   2888  CB  SER A 390      22.797  -3.086   8.701  1.00 35.15           C  
ANISOU 2888  CB  SER A 390     4150   4375   4830    -51    115     88       C  
ATOM   2889  OG  SER A 390      22.947  -2.476   7.436  1.00 34.75           O  
ANISOU 2889  OG  SER A 390     4123   4325   4754    -58    135     68       O  
ATOM   2890  N   TYR A 391      24.973  -1.717  10.114  1.00 36.64           N  
ANISOU 2890  N   TYR A 391     4319   4562   5038    -52    123    100       N  
ATOM   2891  CA  TYR A 391      26.250  -1.034  10.110  1.00 34.27           C  
ANISOU 2891  CA  TYR A 391     4015   4259   4746    -55    139     94       C  
ATOM   2892  C   TYR A 391      26.424  -0.148   8.876  1.00 33.93           C  
ANISOU 2892  C   TYR A 391     3998   4220   4673    -62    162     75       C  
ATOM   2893  O   TYR A 391      26.871   0.986   8.999  1.00 34.40           O  
ANISOU 2893  O   TYR A 391     4067   4286   4715    -64    168     78       O  
ATOM   2894  CB  TYR A 391      27.381  -2.062  10.218  1.00 34.40           C  
ANISOU 2894  CB  TYR A 391     4003   4255   4811    -56    145     84       C  
ATOM   2895  CG  TYR A 391      28.702  -1.580   9.687  1.00 33.94           C  
ANISOU 2895  CG  TYR A 391     3943   4188   4764    -62    169     67       C  
ATOM   2896  CD1 TYR A 391      29.557  -0.819  10.484  1.00 33.68           C  
ANISOU 2896  CD1 TYR A 391     3902   4157   4738    -61    167     78       C  
ATOM   2897  CD2 TYR A 391      29.095  -1.872   8.387  1.00 33.93           C  
ANISOU 2897  CD2 TYR A 391     3948   4177   4765    -68    195     39       C  
ATOM   2898  CE1 TYR A 391      30.767  -0.361  10.003  1.00 33.78           C  
ANISOU 2898  CE1 TYR A 391     3912   4161   4762    -67    190     62       C  
ATOM   2899  CE2 TYR A 391      30.306  -1.410   7.893  1.00 35.99           C  
ANISOU 2899  CE2 TYR A 391     4207   4431   5036    -74    219     22       C  
ATOM   2900  CZ  TYR A 391      31.136  -0.655   8.711  1.00 35.14           C  
ANISOU 2900  CZ  TYR A 391     4090   4324   4937    -73    216     34       C  
ATOM   2901  OH  TYR A 391      32.345  -0.201   8.241  1.00 36.99           O  
ANISOU 2901  OH  TYR A 391     4320   4550   5183    -79    240     18       O  
ATOM   2902  N   SER A 392      26.049  -0.647   7.701  1.00 34.09           N  
ANISOU 2902  N   SER A 392     4031   4236   4686    -66    173     56       N  
ATOM   2903  CA  SER A 392      26.313   0.076   6.447  1.00 34.92           C  
ANISOU 2903  CA  SER A 392     4160   4344   4764    -76    196     37       C  
ATOM   2904  C   SER A 392      25.494   1.364   6.265  1.00 34.85           C  
ANISOU 2904  C   SER A 392     4179   4351   4708    -77    190     48       C  
ATOM   2905  O   SER A 392      25.807   2.192   5.409  1.00 34.98           O  
ANISOU 2905  O   SER A 392     4216   4371   4701    -85    207     37       O  
ATOM   2906  CB  SER A 392      26.170  -0.843   5.225  1.00 35.79           C  
ANISOU 2906  CB  SER A 392     4275   4444   4878    -82    211     13       C  
ATOM   2907  OG  SER A 392      24.820  -1.203   5.004  1.00 36.95           O  
ANISOU 2907  OG  SER A 392     4435   4598   5006    -80    195     19       O  
ATOM   2908  N   ASP A 393      24.452   1.536   7.067  1.00 34.29           N  
ANISOU 2908  N   ASP A 393     4110   4291   4626    -69    166     69       N  
ATOM   2909  CA  ASP A 393      23.770   2.814   7.101  1.00 33.63           C  
ANISOU 2909  CA  ASP A 393     4048   4222   4505    -69    159     81       C  
ATOM   2910  C   ASP A 393      24.599   3.889   7.828  1.00 32.36           C  
ANISOU 2910  C   ASP A 393     3885   4066   4344    -68    162     89       C  
ATOM   2911  O   ASP A 393      24.484   5.077   7.519  1.00 32.44           O  
ANISOU 2911  O   ASP A 393     3914   4084   4325    -71    165     91       O  
ATOM   2912  CB  ASP A 393      22.373   2.653   7.707  1.00 35.36           C  
ANISOU 2912  CB  ASP A 393     4269   4450   4714    -61    135     99       C  
ATOM   2913  CG  ASP A 393      21.471   1.738   6.864  1.00 37.69           C  
ANISOU 2913  CG  ASP A 393     4572   4741   5006    -63    132     90       C  
ATOM   2914  OD1 ASP A 393      21.364   1.963   5.640  1.00 38.75           O  
ANISOU 2914  OD1 ASP A 393     4727   4875   5120    -72    143     75       O  
ATOM   2915  OD2 ASP A 393      20.859   0.794   7.415  1.00 38.22           O  
ANISOU 2915  OD2 ASP A 393     4625   4807   5090    -57    117     98       O  
ATOM   2916  N   LEU A 394      25.466   3.466   8.751  1.00 31.30           N  
ANISOU 2916  N   LEU A 394     3725   3925   4242    -64    160     94       N  
ATOM   2917  CA  LEU A 394      26.132   4.389   9.687  1.00 30.43           C  
ANISOU 2917  CA  LEU A 394     3609   3820   4133    -62    157    107       C  
ATOM   2918  C   LEU A 394      27.664   4.374   9.692  1.00 30.90           C  
ANISOU 2918  C   LEU A 394     3653   3868   4220    -66    174     97       C  
ATOM   2919  O   LEU A 394      28.303   5.379  10.041  1.00 30.25           O  
ANISOU 2919  O   LEU A 394     3573   3788   4130    -67    177    101       O  
ATOM   2920  CB  LEU A 394      25.622   4.143  11.106  1.00 29.85           C  
ANISOU 2920  CB  LEU A 394     3520   3752   4069    -55    133    129       C  
ATOM   2921  CG  LEU A 394      24.114   4.287  11.305  1.00 29.01           C  
ANISOU 2921  CG  LEU A 394     3426   3657   3937    -51    116    141       C  
ATOM   2922  CD1 LEU A 394      23.758   4.062  12.763  1.00 28.63           C  
ANISOU 2922  CD1 LEU A 394     3363   3615   3900    -45     96    162       C  
ATOM   2923  CD2 LEU A 394      23.649   5.652  10.827  1.00 28.22           C  
ANISOU 2923  CD2 LEU A 394     3352   3568   3801    -52    120    141       C  
ATOM   2924  N   GLY A 395      28.242   3.233   9.315  1.00 31.12           N  
ANISOU 2924  N   GLY A 395     3664   3880   4278    -68    183     83       N  
ATOM   2925  CA  GLY A 395      29.686   3.049   9.307  1.00 30.25           C  
ANISOU 2925  CA  GLY A 395     3536   3756   4201    -72    199     72       C  
ATOM   2926  C   GLY A 395      30.271   2.879  10.693  1.00 30.74           C  
ANISOU 2926  C   GLY A 395     3572   3814   4292    -67    182     89       C  
ATOM   2927  O   GLY A 395      31.479   3.025  10.881  1.00 31.87           O  
ANISOU 2927  O   GLY A 395     3701   3947   4459    -69    192     85       O  
ATOM   2928  N   THR A 396      29.417   2.550  11.659  1.00 31.06           N  
ANISOU 2928  N   THR A 396     3607   3861   4331    -61    157    110       N  
ATOM   2929  CA  THR A 396      29.813   2.453  13.059  1.00 31.63           C  
ANISOU 2929  CA  THR A 396     3660   3933   4425    -58    138    130       C  
ATOM   2930  C   THR A 396      29.458   1.105  13.648  1.00 32.93           C  
ANISOU 2930  C   THR A 396     3804   4090   4618    -55    120    139       C  
ATOM   2931  O   THR A 396      28.488   0.472  13.238  1.00 34.63           O  
ANISOU 2931  O   THR A 396     4025   4307   4825    -53    117    136       O  
ATOM   2932  CB  THR A 396      29.171   3.548  13.949  1.00 30.82           C  
ANISOU 2932  CB  THR A 396     3570   3848   4289    -56    123    150       C  
ATOM   2933  OG1 THR A 396      29.603   3.373  15.307  1.00 29.53           O  
ANISOU 2933  OG1 THR A 396     3388   3684   4147    -55    104    169       O  
ATOM   2934  CG2 THR A 396      27.635   3.483  13.912  1.00 30.53           C  
ANISOU 2934  CG2 THR A 396     3549   3824   4224    -52    111    157       C  
ATOM   2935  N   ASN A 397      30.248   0.699  14.636  1.00 33.66           N  
ANISOU 2935  N   ASN A 397     3871   4172   4743    -55    108    151       N  
ATOM   2936  CA  ASN A 397      30.037  -0.534  15.378  1.00 32.49           C  
ANISOU 2936  CA  ASN A 397     3702   4016   4626    -53     88    163       C  
ATOM   2937  C   ASN A 397      29.782  -0.297  16.852  1.00 30.77           C  
ANISOU 2937  C   ASN A 397     3478   3807   4403    -54     62    191       C  
ATOM   2938  O   ASN A 397      29.596  -1.249  17.602  1.00 30.53           O  
ANISOU 2938  O   ASN A 397     3431   3772   4395    -54     42    205       O  
ATOM   2939  CB  ASN A 397      31.275  -1.420  15.257  1.00 33.22           C  
ANISOU 2939  CB  ASN A 397     3766   4084   4769    -56     94    153       C  
ATOM   2940  CG  ASN A 397      31.169  -2.408  14.135  1.00 33.67           C  
ANISOU 2940  CG  ASN A 397     3818   4128   4844    -55    109    131       C  
ATOM   2941  OD1 ASN A 397      32.175  -2.767  13.525  1.00 35.25           O  
ANISOU 2941  OD1 ASN A 397     4006   4312   5076    -58    127    112       O  
ATOM   2942  ND2 ASN A 397      29.949  -2.862  13.851  1.00 33.16           N  
ANISOU 2942  ND2 ASN A 397     3766   4072   4761    -52    102    132       N  
ATOM   2943  N   SER A 398      29.814   0.960  17.273  1.00 29.74           N  
ANISOU 2943  N   SER A 398     3363   3691   4244    -55     62    199       N  
ATOM   2944  CA  SER A 398      29.747   1.264  18.692  1.00 30.14           C  
ANISOU 2944  CA  SER A 398     3409   3751   4290    -57     40    223       C  
ATOM   2945  C   SER A 398      28.511   2.034  19.071  1.00 29.99           C  
ANISOU 2945  C   SER A 398     3412   3754   4228    -55     33    233       C  
ATOM   2946  O   SER A 398      28.490   2.666  20.121  1.00 30.41           O  
ANISOU 2946  O   SER A 398     3467   3817   4269    -58     20    249       O  
ATOM   2947  CB  SER A 398      31.007   1.994  19.195  1.00 30.16           C  
ANISOU 2947  CB  SER A 398     3405   3749   4305    -61     41    226       C  
ATOM   2948  OG  SER A 398      31.937   2.266  18.172  1.00 30.48           O  
ANISOU 2948  OG  SER A 398     3444   3778   4357    -61     65    205       O  
ATOM   2949  N   LEU A 399      27.485   1.967  18.225  1.00 29.80           N  
ANISOU 2949  N   LEU A 399     3403   3736   4183    -51     40    224       N  
ATOM   2950  CA  LEU A 399      26.245   2.691  18.459  1.00 29.72           C  
ANISOU 2950  CA  LEU A 399     3413   3745   4135    -49     35    231       C  
ATOM   2951  C   LEU A 399      25.566   2.202  19.734  1.00 29.46           C  
ANISOU 2951  C   LEU A 399     3371   3719   4102    -51     12    253       C  
ATOM   2952  O   LEU A 399      25.270   1.021  19.867  1.00 29.55           O  
ANISOU 2952  O   LEU A 399     3369   3723   4134    -51      2    258       O  
ATOM   2953  CB  LEU A 399      25.300   2.573  17.249  1.00 29.30           C  
ANISOU 2953  CB  LEU A 399     3374   3693   4062    -45     46    217       C  
ATOM   2954  CG  LEU A 399      24.152   3.605  17.246  1.00 29.51           C  
ANISOU 2954  CG  LEU A 399     3424   3737   4049    -43     44    221       C  
ATOM   2955  CD1 LEU A 399      24.667   5.007  16.949  1.00 28.60           C  
ANISOU 2955  CD1 LEU A 399     3324   3628   3914    -44     57    214       C  
ATOM   2956  CD2 LEU A 399      23.011   3.235  16.303  1.00 28.93           C  
ANISOU 2956  CD2 LEU A 399     3363   3665   3962    -40     47    213       C  
ATOM   2957  N   ARG A 400      25.336   3.112  20.672  1.00 29.76           N  
ANISOU 2957  N   ARG A 400     3417   3771   4118    -53      5    266       N  
ATOM   2958  CA  ARG A 400      24.680   2.755  21.930  1.00 31.28           C  
ANISOU 2958  CA  ARG A 400     3603   3972   4307    -57    -15    287       C  
ATOM   2959  C   ARG A 400      23.261   3.280  22.082  1.00 29.79           C  
ANISOU 2959  C   ARG A 400     3431   3801   4085    -55    -16    290       C  
ATOM   2960  O   ARG A 400      22.479   2.737  22.861  1.00 29.48           O  
ANISOU 2960  O   ARG A 400     3387   3768   4043    -57    -30    304       O  
ATOM   2961  CB  ARG A 400      25.524   3.190  23.119  1.00 33.98           C  
ANISOU 2961  CB  ARG A 400     3938   4317   4653    -64    -25    301       C  
ATOM   2962  CG  ARG A 400      26.360   2.051  23.650  1.00 38.88           C  
ANISOU 2962  CG  ARG A 400     4535   4922   5313    -70    -39    311       C  
ATOM   2963  CD  ARG A 400      27.718   2.541  24.087  1.00 43.51           C  
ANISOU 2963  CD  ARG A 400     5114   5502   5914    -75    -41    314       C  
ATOM   2964  NE  ARG A 400      28.769   1.734  23.471  1.00 50.67           N  
ANISOU 2964  NE  ARG A 400     6002   6388   6863    -73    -36    305       N  
ATOM   2965  CZ  ARG A 400      29.236   0.585  23.962  1.00 56.14           C  
ANISOU 2965  CZ  ARG A 400     6672   7065   7591    -77    -52    316       C  
ATOM   2966  NH1 ARG A 400      28.744   0.083  25.099  1.00 56.88           N  
ANISOU 2966  NH1 ARG A 400     6761   7166   7684    -84    -75    338       N  
ATOM   2967  NH2 ARG A 400      30.206  -0.062  23.315  1.00 55.80           N  
ANISOU 2967  NH2 ARG A 400     6611   7001   7587    -76    -46    304       N  
ATOM   2968  N   HIS A 401      22.936   4.316  21.310  1.00 28.34           N  
ANISOU 2968  N   HIS A 401     3266   3623   3876    -50     -2    278       N  
ATOM   2969  CA  HIS A 401      21.691   5.055  21.454  1.00 26.92           C  
ANISOU 2969  CA  HIS A 401     3102   3459   3666    -48     -3    280       C  
ATOM   2970  C   HIS A 401      21.193   5.460  20.094  1.00 26.02           C  
ANISOU 2970  C   HIS A 401     3004   3343   3538    -42     10    264       C  
ATOM   2971  O   HIS A 401      21.874   6.176  19.357  1.00 25.75           O  
ANISOU 2971  O   HIS A 401     2979   3306   3500    -41     23    252       O  
ATOM   2972  CB  HIS A 401      21.957   6.265  22.330  1.00 25.87           C  
ANISOU 2972  CB  HIS A 401     2975   3336   3515    -52     -3    286       C  
ATOM   2973  CG  HIS A 401      20.741   7.101  22.636  1.00 25.81           C  
ANISOU 2973  CG  HIS A 401     2983   3345   3479    -50     -4    288       C  
ATOM   2974  ND1 HIS A 401      20.179   7.132  23.858  1.00 26.26           N  
ANISOU 2974  ND1 HIS A 401     3037   3413   3528    -55    -14    302       N  
ATOM   2975  CD2 HIS A 401      20.027   8.010  21.852  1.00 25.71           C  
ANISOU 2975  CD2 HIS A 401     2986   3336   3445    -44      5    278       C  
ATOM   2976  CE1 HIS A 401      19.141   7.990  23.855  1.00 25.93           C  
ANISOU 2976  CE1 HIS A 401     3007   3381   3462    -52    -10    299       C  
ATOM   2977  NE2 HIS A 401      19.049   8.529  22.626  1.00 25.79           N  
ANISOU 2977  NE2 HIS A 401     3001   3359   3438    -45      0    285       N  
ATOM   2978  N   LEU A 402      20.001   4.988  19.746  1.00 25.12           N  
ANISOU 2978  N   LEU A 402     2894   3232   3418    -38      6    263       N  
ATOM   2979  CA  LEU A 402      19.358   5.353  18.496  1.00 25.08           C  
ANISOU 2979  CA  LEU A 402     2905   3226   3397    -34     15    250       C  
ATOM   2980  C   LEU A 402      17.949   5.885  18.758  1.00 26.26           C  
ANISOU 2980  C   LEU A 402     3064   3387   3524    -31      9    256       C  
ATOM   2981  O   LEU A 402      17.045   5.152  19.197  1.00 26.27           O  
ANISOU 2981  O   LEU A 402     3059   3392   3530    -30     -1    264       O  
ATOM   2982  CB  LEU A 402      19.327   4.173  17.530  1.00 24.76           C  
ANISOU 2982  CB  LEU A 402     2860   3174   3373    -32     17    241       C  
ATOM   2983  CG  LEU A 402      18.824   4.346  16.090  1.00 25.03           C  
ANISOU 2983  CG  LEU A 402     2910   3204   3394    -30     27    226       C  
ATOM   2984  CD1 LEU A 402      19.515   5.476  15.335  1.00 24.93           C  
ANISOU 2984  CD1 LEU A 402     2913   3191   3367    -32     42    215       C  
ATOM   2985  CD2 LEU A 402      18.981   3.045  15.323  1.00 24.74           C  
ANISOU 2985  CD2 LEU A 402     2865   3154   3378    -31     29    217       C  
ATOM   2986  N   ASP A 403      17.774   7.180  18.508  1.00 26.80           N  
ANISOU 2986  N   ASP A 403     3148   3461   3571    -30     15    251       N  
ATOM   2987  CA  ASP A 403      16.458   7.785  18.570  1.00 26.28           C  
ANISOU 2987  CA  ASP A 403     3092   3404   3487    -27     11    254       C  
ATOM   2988  C   ASP A 403      15.928   8.138  17.173  1.00 26.63           C  
ANISOU 2988  C   ASP A 403     3153   3445   3520    -23     16    243       C  
ATOM   2989  O   ASP A 403      16.420   9.073  16.513  1.00 26.41           O  
ANISOU 2989  O   ASP A 403     3137   3414   3480    -24     25    235       O  
ATOM   2990  CB  ASP A 403      16.465   9.008  19.472  1.00 25.93           C  
ANISOU 2990  CB  ASP A 403     3052   3370   3428    -28     11    259       C  
ATOM   2991  CG  ASP A 403      15.075   9.519  19.756  1.00 26.30           C  
ANISOU 2991  CG  ASP A 403     3105   3426   3462    -25      7    262       C  
ATOM   2992  OD1 ASP A 403      14.947  10.499  20.520  1.00 27.69           O  
ANISOU 2992  OD1 ASP A 403     3283   3610   3626    -26      8    265       O  
ATOM   2993  OD2 ASP A 403      14.102   8.943  19.232  1.00 26.00           O  
ANISOU 2993  OD2 ASP A 403     3068   3386   3425    -22      2    262       O  
ATOM   2994  N   LEU A 404      14.916   7.382  16.747  1.00 25.92           N  
ANISOU 2994  N   LEU A 404     3062   3351   3432    -21      9    243       N  
ATOM   2995  CA  LEU A 404      14.205   7.645  15.502  1.00 26.29           C  
ANISOU 2995  CA  LEU A 404     3125   3394   3467    -19     10    235       C  
ATOM   2996  C   LEU A 404      12.723   7.982  15.757  1.00 25.60           C  
ANISOU 2996  C   LEU A 404     3041   3314   3371    -15      0    241       C  
ATOM   2997  O   LEU A 404      11.864   7.771  14.899  1.00 26.50           O  
ANISOU 2997  O   LEU A 404     3163   3423   3481    -14     -3    238       O  
ATOM   2998  CB  LEU A 404      14.332   6.436  14.555  1.00 26.51           C  
ANISOU 2998  CB  LEU A 404     3152   3413   3507    -20     12    227       C  
ATOM   2999  CG  LEU A 404      15.682   6.164  13.890  1.00 26.64           C  
ANISOU 2999  CG  LEU A 404     3168   3420   3532    -24     24    215       C  
ATOM   3000  CD1 LEU A 404      15.792   4.749  13.337  1.00 25.60           C  
ANISOU 3000  CD1 LEU A 404     3028   3279   3419    -25     24    209       C  
ATOM   3001  CD2 LEU A 404      15.905   7.171  12.776  1.00 27.46           C  
ANISOU 3001  CD2 LEU A 404     3293   3523   3617    -27     34    205       C  
ATOM   3002  N   SER A 405      12.420   8.507  16.933  1.00 24.64           N  
ANISOU 3002  N   SER A 405     2914   3201   3247    -15     -2    250       N  
ATOM   3003  CA  SER A 405      11.034   8.790  17.288  1.00 24.32           C  
ANISOU 3003  CA  SER A 405     2873   3166   3201    -11    -10    255       C  
ATOM   3004  C   SER A 405      10.461  10.016  16.561  1.00 24.71           C  
ANISOU 3004  C   SER A 405     2938   3214   3236     -9     -9    250       C  
ATOM   3005  O   SER A 405      11.205  10.833  15.980  1.00 24.73           O  
ANISOU 3005  O   SER A 405     2952   3214   3230    -10     -2    243       O  
ATOM   3006  CB  SER A 405      10.882   8.932  18.813  1.00 24.00           C  
ANISOU 3006  CB  SER A 405     2820   3136   3162    -13    -11    264       C  
ATOM   3007  OG  SER A 405      11.610  10.035  19.317  1.00 22.67           O  
ANISOU 3007  OG  SER A 405     2656   2972   2984    -15     -4    263       O  
ATOM   3008  N   PHE A 406       9.129  10.119  16.584  1.00 24.62           N  
ANISOU 3008  N   PHE A 406     2926   3203   3223     -5    -17    253       N  
ATOM   3009  CA  PHE A 406       8.382  11.250  16.005  1.00 24.10           C  
ANISOU 3009  CA  PHE A 406     2872   3134   3148     -3    -20    250       C  
ATOM   3010  C   PHE A 406       8.746  11.566  14.550  1.00 24.24           C  
ANISOU 3010  C   PHE A 406     2909   3144   3157     -5    -19    242       C  
ATOM   3011  O   PHE A 406       8.879  12.729  14.198  1.00 25.04           O  
ANISOU 3011  O   PHE A 406     3020   3244   3248     -6    -18    240       O  
ATOM   3012  CB  PHE A 406       8.525  12.503  16.878  1.00 22.97           C  
ANISOU 3012  CB  PHE A 406     2729   2998   2999     -3    -15    251       C  
ATOM   3013  CG  PHE A 406       7.975  12.346  18.266  1.00 22.83           C  
ANISOU 3013  CG  PHE A 406     2696   2990   2986     -2    -15    257       C  
ATOM   3014  CD1 PHE A 406       8.802  11.978  19.320  1.00 22.84           C  
ANISOU 3014  CD1 PHE A 406     2688   2999   2990     -7    -10    261       C  
ATOM   3015  CD2 PHE A 406       6.616  12.568  18.529  1.00 22.72           C  
ANISOU 3015  CD2 PHE A 406     2678   2977   2977      0    -21    259       C  
ATOM   3016  CE1 PHE A 406       8.294  11.835  20.609  1.00 22.42           C  
ANISOU 3016  CE1 PHE A 406     2623   2955   2938     -9    -10    267       C  
ATOM   3017  CE2 PHE A 406       6.102  12.424  19.820  1.00 22.19           C  
ANISOU 3017  CE2 PHE A 406     2598   2919   2913      0    -19    263       C  
ATOM   3018  CZ  PHE A 406       6.940  12.057  20.859  1.00 22.04           C  
ANISOU 3018  CZ  PHE A 406     2571   2908   2892     -6    -14    267       C  
ATOM   3019  N   ASN A 407       8.905  10.530  13.726  1.00 24.31           N  
ANISOU 3019  N   ASN A 407     2920   3147   3170     -7    -21    239       N  
ATOM   3020  CA  ASN A 407       9.247  10.663  12.305  1.00 24.58           C  
ANISOU 3020  CA  ASN A 407     2971   3172   3193    -11    -19    231       C  
ATOM   3021  C   ASN A 407       8.184  10.030  11.400  1.00 24.56           C  
ANISOU 3021  C   ASN A 407     2975   3163   3192    -11    -31    231       C  
ATOM   3022  O   ASN A 407       7.123   9.615  11.869  1.00 24.44           O  
ANISOU 3022  O   ASN A 407     2950   3149   3186     -7    -41    237       O  
ATOM   3023  CB  ASN A 407      10.600   9.988  12.017  1.00 24.71           C  
ANISOU 3023  CB  ASN A 407     2987   3187   3214    -16     -7    224       C  
ATOM   3024  CG  ASN A 407      11.768  10.706  12.660  1.00 25.52           C  
ANISOU 3024  CG  ASN A 407     3087   3294   3315    -17      3    223       C  
ATOM   3025  OD1 ASN A 407      12.569  10.102  13.367  1.00 25.31           O  
ANISOU 3025  OD1 ASN A 407     3046   3269   3299    -18      8    224       O  
ATOM   3026  ND2 ASN A 407      11.879  11.999  12.410  1.00 26.10           N  
ANISOU 3026  ND2 ASN A 407     3172   3368   3374    -18      5    222       N  
ATOM   3027  N   GLY A 408       8.501   9.926  10.111  1.00 24.34           N  
ANISOU 3027  N   GLY A 408     2964   3129   3155    -17    -29    223       N  
ATOM   3028  CA  GLY A 408       7.616   9.337   9.124  1.00 25.18           C  
ANISOU 3028  CA  GLY A 408     3078   3228   3259    -19    -40    222       C  
ATOM   3029  C   GLY A 408       7.804   7.851   8.892  1.00 26.28           C  
ANISOU 3029  C   GLY A 408     3211   3364   3409    -20    -39    217       C  
ATOM   3030  O   GLY A 408       7.821   7.066   9.829  1.00 27.52           O  
ANISOU 3030  O   GLY A 408     3349   3524   3582    -16    -38    221       O  
ATOM   3031  N   ALA A 409       7.919   7.455   7.631  1.00 27.62           N  
ANISOU 3031  N   ALA A 409     3396   3526   3570    -28    -38    208       N  
ATOM   3032  CA  ALA A 409       7.984   6.040   7.281  1.00 28.14           C  
ANISOU 3032  CA  ALA A 409     3455   3587   3647    -29    -37    202       C  
ATOM   3033  C   ALA A 409       9.364   5.461   7.578  1.00 29.57           C  
ANISOU 3033  C   ALA A 409     3626   3768   3838    -31    -20    194       C  
ATOM   3034  O   ALA A 409      10.380   5.902   7.015  1.00 30.08           O  
ANISOU 3034  O   ALA A 409     3701   3832   3893    -37     -7    184       O  
ATOM   3035  CB  ALA A 409       7.626   5.839   5.818  1.00 27.52           C  
ANISOU 3035  CB  ALA A 409     3398   3501   3555    -38    -42    193       C  
ATOM   3036  N   ILE A 410       9.393   4.486   8.481  1.00 29.52           N  
ANISOU 3036  N   ILE A 410     3599   3764   3853    -26    -22    198       N  
ATOM   3037  CA  ILE A 410      10.599   3.718   8.753  1.00 28.85           C  
ANISOU 3037  CA  ILE A 410     3502   3676   3783    -27     -9    191       C  
ATOM   3038  C   ILE A 410      10.366   2.267   8.308  1.00 30.13           C  
ANISOU 3038  C   ILE A 410     3657   3831   3960    -28    -12    185       C  
ATOM   3039  O   ILE A 410       9.636   1.496   8.949  1.00 28.66           O  
ANISOU 3039  O   ILE A 410     3456   3645   3788    -23    -24    194       O  
ATOM   3040  CB  ILE A 410      11.036   3.846  10.229  1.00 28.27           C  
ANISOU 3040  CB  ILE A 410     3409   3610   3722    -22     -8    202       C  
ATOM   3041  CG1 ILE A 410      11.303   5.324  10.556  1.00 28.00           C  
ANISOU 3041  CG1 ILE A 410     3383   3582   3671    -22     -4    206       C  
ATOM   3042  CG2 ILE A 410      12.281   3.010  10.508  1.00 27.57           C  
ANISOU 3042  CG2 ILE A 410     3305   3515   3652    -24      1    196       C  
ATOM   3043  CD1 ILE A 410      11.628   5.612  12.004  1.00 27.74           C  
ANISOU 3043  CD1 ILE A 410     3334   3557   3647    -18     -4    216       C  
ATOM   3044  N   ILE A 411      10.983   1.922   7.182  1.00 31.87           N  
ANISOU 3044  N   ILE A 411     3888   4043   4176    -35     -2    169       N  
ATOM   3045  CA  ILE A 411      10.813   0.618   6.555  1.00 33.14           C  
ANISOU 3045  CA  ILE A 411     4045   4195   4349    -38     -3    160       C  
ATOM   3046  C   ILE A 411      11.892  -0.333   7.068  1.00 33.78           C  
ANISOU 3046  C   ILE A 411     4106   4271   4457    -36      6    155       C  
ATOM   3047  O   ILE A 411      13.043  -0.248   6.662  1.00 33.15           O  
ANISOU 3047  O   ILE A 411     4028   4187   4379    -42     23    142       O  
ATOM   3048  CB  ILE A 411      10.835   0.748   5.008  1.00 34.19           C  
ANISOU 3048  CB  ILE A 411     4203   4323   4463    -48      2    144       C  
ATOM   3049  CG1 ILE A 411       9.705   1.672   4.541  1.00 35.05           C  
ANISOU 3049  CG1 ILE A 411     4333   4436   4549    -49    -11    152       C  
ATOM   3050  CG2 ILE A 411      10.700  -0.605   4.320  1.00 33.33           C  
ANISOU 3050  CG2 ILE A 411     4092   4205   4367    -51      3    132       C  
ATOM   3051  CD1 ILE A 411       9.756   2.022   3.065  1.00 36.40           C  
ANISOU 3051  CD1 ILE A 411     4531   4602   4695    -62     -6    140       C  
ATOM   3052  N   MET A 412      11.509  -1.220   7.983  1.00 35.73           N  
ANISOU 3052  N   MET A 412     4331   4517   4726    -30     -3    165       N  
ATOM   3053  CA  MET A 412      12.422  -2.224   8.538  1.00 36.39           C  
ANISOU 3053  CA  MET A 412     4392   4593   4838    -29      1    163       C  
ATOM   3054  C   MET A 412      12.791  -3.232   7.469  1.00 38.12           C  
ANISOU 3054  C   MET A 412     4613   4800   5069    -34     10    144       C  
ATOM   3055  O   MET A 412      11.912  -3.834   6.851  1.00 40.50           O  
ANISOU 3055  O   MET A 412     4921   5098   5368    -35      2    140       O  
ATOM   3056  CB  MET A 412      11.772  -2.955   9.710  1.00 36.87           C  
ANISOU 3056  CB  MET A 412     4432   4656   4918    -23    -14    180       C  
ATOM   3057  CG  MET A 412      11.460  -2.070  10.903  1.00 37.54           C  
ANISOU 3057  CG  MET A 412     4514   4754   4995    -19    -21    198       C  
ATOM   3058  SD  MET A 412      12.886  -1.084  11.408  1.00 38.33           S  
ANISOU 3058  SD  MET A 412     4613   4859   5092    -21     -7    197       S  
ATOM   3059  CE  MET A 412      14.065  -2.380  11.794  1.00 38.54           C  
ANISOU 3059  CE  MET A 412     4615   4873   5154    -22     -3    194       C  
ATOM   3060  N   SER A 413      14.089  -3.423   7.264  1.00 38.76           N  
ANISOU 3060  N   SER A 413     4687   4874   5162    -38     27    131       N  
ATOM   3061  CA  SER A 413      14.592  -4.199   6.137  1.00 38.09           C  
ANISOU 3061  CA  SER A 413     4607   4778   5086    -45     40    108       C  
ATOM   3062  C   SER A 413      15.843  -5.033   6.492  1.00 37.71           C  
ANISOU 3062  C   SER A 413     4536   4719   5074    -45     51    100       C  
ATOM   3063  O   SER A 413      16.233  -5.953   5.758  1.00 37.17           O  
ANISOU 3063  O   SER A 413     4463   4638   5022    -49     61     81       O  
ATOM   3064  CB  SER A 413      14.848  -3.241   4.968  1.00 39.64           C  
ANISOU 3064  CB  SER A 413     4831   4977   5252    -54     55     94       C  
ATOM   3065  OG  SER A 413      16.128  -3.411   4.381  1.00 44.50           O  
ANISOU 3065  OG  SER A 413     5446   5584   5877    -61     77     74       O  
ATOM   3066  N   ALA A 414      16.454  -4.695   7.624  1.00 36.07           N  
ANISOU 3066  N   ALA A 414     4312   4514   4879    -41     49    113       N  
ATOM   3067  CA  ALA A 414      17.665  -5.337   8.113  1.00 34.30           C  
ANISOU 3067  CA  ALA A 414     4064   4279   4689    -40     56    109       C  
ATOM   3068  C   ALA A 414      17.611  -5.300   9.635  1.00 33.45           C  
ANISOU 3068  C   ALA A 414     3938   4177   4594    -34     40    134       C  
ATOM   3069  O   ALA A 414      17.342  -4.258  10.216  1.00 34.53           O  
ANISOU 3069  O   ALA A 414     4083   4327   4709    -32     35    147       O  
ATOM   3070  CB  ALA A 414      18.891  -4.596   7.600  1.00 32.24           C  
ANISOU 3070  CB  ALA A 414     3809   4015   4423    -46     79     94       C  
ATOM   3071  N   ASN A 415      17.869  -6.427  10.283  1.00 33.35           N  
ANISOU 3071  N   ASN A 415     3899   4154   4616    -32     31    140       N  
ATOM   3072  CA  ASN A 415      17.755  -6.502  11.743  1.00 33.67           C  
ANISOU 3072  CA  ASN A 415     3923   4200   4668    -28     13    165       C  
ATOM   3073  C   ASN A 415      18.986  -6.128  12.571  1.00 33.60           C  
ANISOU 3073  C   ASN A 415     3900   4189   4674    -30     16    171       C  
ATOM   3074  O   ASN A 415      19.390  -6.867  13.460  1.00 32.54           O  
ANISOU 3074  O   ASN A 415     3744   4049   4570    -30      5    183       O  
ATOM   3075  CB  ASN A 415      17.213  -7.863  12.188  1.00 34.38           C  
ANISOU 3075  CB  ASN A 415     3994   4282   4785    -26     -3    173       C  
ATOM   3076  CG  ASN A 415      17.859  -9.028  11.476  1.00 34.51           C  
ANISOU 3076  CG  ASN A 415     3997   4280   4836    -28      4    155       C  
ATOM   3077  OD1 ASN A 415      17.325 -10.135  11.498  1.00 35.14           O  
ANISOU 3077  OD1 ASN A 415     4065   4351   4935    -26     -6    157       O  
ATOM   3078  ND2 ASN A 415      19.008  -8.799  10.855  1.00 34.93           N  
ANISOU 3078  ND2 ASN A 415     4050   4324   4896    -31     24    136       N  
ATOM   3079  N   PHE A 416      19.557  -4.965  12.273  1.00 34.46           N  
ANISOU 3079  N   PHE A 416     4024   4305   4764    -32     30    164       N  
ATOM   3080  CA  PHE A 416      20.630  -4.354  13.067  1.00 34.94           C  
ANISOU 3080  CA  PHE A 416     4076   4367   4833    -33     32    172       C  
ATOM   3081  C   PHE A 416      21.941  -5.122  13.066  1.00 36.13           C  
ANISOU 3081  C   PHE A 416     4204   4499   5023    -36     39    163       C  
ATOM   3082  O   PHE A 416      22.716  -5.036  14.028  1.00 37.10           O  
ANISOU 3082  O   PHE A 416     4311   4619   5164    -36     33    175       O  
ATOM   3083  CB  PHE A 416      20.175  -4.062  14.507  1.00 34.18           C  
ANISOU 3083  CB  PHE A 416     3973   4282   4730    -32     13    198       C  
ATOM   3084  CG  PHE A 416      19.042  -3.090  14.593  1.00 34.75           C  
ANISOU 3084  CG  PHE A 416     4067   4372   4764    -30      9    206       C  
ATOM   3085  CD1 PHE A 416      17.722  -3.541  14.604  1.00 34.82           C  
ANISOU 3085  CD1 PHE A 416     4079   4386   4765    -27     -2    212       C  
ATOM   3086  CD2 PHE A 416      19.286  -1.721  14.637  1.00 34.19           C  
ANISOU 3086  CD2 PHE A 416     4011   4311   4668    -30     17    205       C  
ATOM   3087  CE1 PHE A 416      16.666  -2.644  14.670  1.00 35.08           C  
ANISOU 3087  CE1 PHE A 416     4129   4433   4766    -25     -6    219       C  
ATOM   3088  CE2 PHE A 416      18.234  -0.816  14.711  1.00 34.72           C  
ANISOU 3088  CE2 PHE A 416     4095   4392   4703    -28     13    212       C  
ATOM   3089  CZ  PHE A 416      16.920  -1.277  14.723  1.00 35.13           C  
ANISOU 3089  CZ  PHE A 416     4150   4449   4748    -26      1    218       C  
ATOM   3090  N   MET A 417      22.212  -5.864  11.995  1.00 36.24           N  
ANISOU 3090  N   MET A 417     4216   4499   5053    -37     53    141       N  
ATOM   3091  CA  MET A 417      23.496  -6.539  11.935  1.00 36.69           C  
ANISOU 3091  CA  MET A 417     4250   4537   5151    -39     62    130       C  
ATOM   3092  C   MET A 417      24.608  -5.497  11.774  1.00 36.33           C  
ANISOU 3092  C   MET A 417     4211   4493   5100    -43     79    122       C  
ATOM   3093  O   MET A 417      24.518  -4.587  10.945  1.00 35.76           O  
ANISOU 3093  O   MET A 417     4161   4428   4995    -45     95    109       O  
ATOM   3094  CB  MET A 417      23.533  -7.691  10.921  1.00 38.11           C  
ANISOU 3094  CB  MET A 417     4423   4701   5355    -41     72    108       C  
ATOM   3095  CG  MET A 417      23.252  -7.343   9.477  1.00 42.04           C  
ANISOU 3095  CG  MET A 417     4945   5200   5824    -45     93     83       C  
ATOM   3096  SD  MET A 417      21.498  -7.276   9.042  1.00 44.36           S  
ANISOU 3096  SD  MET A 417     5264   5509   6079    -43     81     89       S  
ATOM   3097  CE  MET A 417      21.711  -6.730   7.346  1.00 44.30           C  
ANISOU 3097  CE  MET A 417     5285   5502   6045    -51    109     59       C  
ATOM   3098  N   GLY A 418      25.619  -5.607  12.632  1.00 35.86           N  
ANISOU 3098  N   GLY A 418     4129   4425   5071    -43     74    131       N  
ATOM   3099  CA  GLY A 418      26.650  -4.576  12.769  1.00 35.00           C  
ANISOU 3099  CA  GLY A 418     4022   4317   4957    -46     86    129       C  
ATOM   3100  C   GLY A 418      26.427  -3.627  13.943  1.00 33.03           C  
ANISOU 3100  C   GLY A 418     3779   4084   4686    -45     70    153       C  
ATOM   3101  O   GLY A 418      27.336  -2.911  14.346  1.00 32.41           O  
ANISOU 3101  O   GLY A 418     3697   4005   4611    -47     74    156       O  
ATOM   3102  N   LEU A 419      25.216  -3.599  14.483  1.00 32.58           N  
ANISOU 3102  N   LEU A 419     3731   4041   4607    -42     52    170       N  
ATOM   3103  CA  LEU A 419      24.902  -2.656  15.559  1.00 33.80           C  
ANISOU 3103  CA  LEU A 419     3893   4212   4737    -42     39    191       C  
ATOM   3104  C   LEU A 419      24.581  -3.362  16.881  1.00 35.00           C  
ANISOU 3104  C   LEU A 419     4027   4365   4906    -42     14    216       C  
ATOM   3105  O   LEU A 419      23.750  -2.898  17.662  1.00 34.90           O  
ANISOU 3105  O   LEU A 419     4022   4367   4868    -42      1    233       O  
ATOM   3106  CB  LEU A 419      23.770  -1.699  15.144  1.00 32.25           C  
ANISOU 3106  CB  LEU A 419     3724   4033   4495    -40     43    191       C  
ATOM   3107  CG  LEU A 419      23.955  -0.868  13.864  1.00 32.25           C  
ANISOU 3107  CG  LEU A 419     3745   4035   4473    -41     65    170       C  
ATOM   3108  CD1 LEU A 419      22.686  -0.095  13.539  1.00 32.78           C  
ANISOU 3108  CD1 LEU A 419     3836   4117   4499    -39     63    173       C  
ATOM   3109  CD2 LEU A 419      25.155   0.074  13.922  1.00 31.25           C  
ANISOU 3109  CD2 LEU A 419     3619   3907   4346    -44     78    165       C  
ATOM   3110  N   GLU A 420      25.282  -4.468  17.132  1.00 36.02           N  
ANISOU 3110  N   GLU A 420     4131   4477   5078    -44      7    217       N  
ATOM   3111  CA  GLU A 420      24.989  -5.359  18.258  1.00 36.17           C  
ANISOU 3111  CA  GLU A 420     4132   4493   5116    -46    -17    240       C  
ATOM   3112  C   GLU A 420      25.283  -4.784  19.648  1.00 35.95           C  
ANISOU 3112  C   GLU A 420     4101   4475   5083    -50    -34    263       C  
ATOM   3113  O   GLU A 420      25.070  -5.449  20.647  1.00 38.41           O  
ANISOU 3113  O   GLU A 420     4399   4786   5408    -54    -56    284       O  
ATOM   3114  CB  GLU A 420      25.700  -6.698  18.065  1.00 35.79           C  
ANISOU 3114  CB  GLU A 420     4057   4421   5119    -46    -21    234       C  
ATOM   3115  CG  GLU A 420      26.751  -6.668  16.972  1.00 37.86           C  
ANISOU 3115  CG  GLU A 420     4316   4668   5401    -46      3    207       C  
ATOM   3116  CD  GLU A 420      26.221  -7.081  15.605  1.00 40.36           C  
ANISOU 3116  CD  GLU A 420     4643   4981   5711    -43     20    183       C  
ATOM   3117  OE1 GLU A 420      25.270  -7.885  15.511  1.00 41.67           O  
ANISOU 3117  OE1 GLU A 420     4808   5147   5877    -40     10    186       O  
ATOM   3118  OE2 GLU A 420      26.780  -6.621  14.596  1.00 42.32           O  
ANISOU 3118  OE2 GLU A 420     4899   5224   5954    -43     44    160       O  
ATOM   3119  N   GLU A 421      25.743  -3.541  19.700  1.00 35.23           N  
ANISOU 3119  N   GLU A 421     4022   4393   4970    -51    -24    261       N  
ATOM   3120  CA  GLU A 421      26.064  -2.867  20.947  1.00 34.27           C  
ANISOU 3120  CA  GLU A 421     3899   4280   4839    -57    -37    281       C  
ATOM   3121  C   GLU A 421      24.940  -1.960  21.459  1.00 32.37           C  
ANISOU 3121  C   GLU A 421     3680   4063   4554    -57    -41    291       C  
ATOM   3122  O   GLU A 421      25.012  -1.460  22.580  1.00 32.22           O  
ANISOU 3122  O   GLU A 421     3662   4054   4524    -62    -53    308       O  
ATOM   3123  CB  GLU A 421      27.345  -2.046  20.761  1.00 37.33           C  
ANISOU 3123  CB  GLU A 421     4287   4663   5234    -58    -24    272       C  
ATOM   3124  CG  GLU A 421      28.625  -2.871  20.704  1.00 42.41           C  
ANISOU 3124  CG  GLU A 421     4904   5282   5926    -60    -26    268       C  
ATOM   3125  CD  GLU A 421      28.987  -3.463  22.059  1.00 46.80           C  
ANISOU 3125  CD  GLU A 421     5441   5833   6507    -67    -53    293       C  
ATOM   3126  OE1 GLU A 421      28.945  -2.708  23.059  1.00 49.87           O  
ANISOU 3126  OE1 GLU A 421     5837   6236   6875    -73    -64    310       O  
ATOM   3127  OE2 GLU A 421      29.290  -4.679  22.134  1.00 47.61           O  
ANISOU 3127  OE2 GLU A 421     5521   5918   6650    -69    -64    296       O  
ATOM   3128  N   LEU A 422      23.914  -1.750  20.633  1.00 30.52           N  
ANISOU 3128  N   LEU A 422     3463   3837   4295    -51    -31    280       N  
ATOM   3129  CA  LEU A 422      22.807  -0.829  20.929  1.00 29.97           C  
ANISOU 3129  CA  LEU A 422     3414   3788   4186    -50    -32    286       C  
ATOM   3130  C   LEU A 422      22.092  -1.160  22.233  1.00 29.23           C  
ANISOU 3130  C   LEU A 422     3314   3704   4087    -55    -52    308       C  
ATOM   3131  O   LEU A 422      21.776  -2.318  22.487  1.00 28.78           O  
ANISOU 3131  O   LEU A 422     3244   3641   4050    -56    -65    317       O  
ATOM   3132  CB  LEU A 422      21.778  -0.867  19.787  1.00 29.92           C  
ANISOU 3132  CB  LEU A 422     3421   3783   4162    -44    -21    271       C  
ATOM   3133  CG  LEU A 422      21.357   0.394  19.022  1.00 29.19           C  
ANISOU 3133  CG  LEU A 422     3353   3701   4036    -40     -6    259       C  
ATOM   3134  CD1 LEU A 422      20.030   0.152  18.331  1.00 30.10           C  
ANISOU 3134  CD1 LEU A 422     3479   3820   4135    -36     -6    254       C  
ATOM   3135  CD2 LEU A 422      21.243   1.609  19.913  1.00 29.20           C  
ANISOU 3135  CD2 LEU A 422     3363   3717   4012    -43     -9    270       C  
ATOM   3136  N   GLN A 423      21.833  -0.152  23.061  1.00 30.01           N  
ANISOU 3136  N   GLN A 423     3423   3818   4158    -59    -55    318       N  
ATOM   3137  CA  GLN A 423      21.106  -0.394  24.321  1.00 30.59           C  
ANISOU 3137  CA  GLN A 423     3493   3903   4223    -65    -72    339       C  
ATOM   3138  C   GLN A 423      19.852   0.447  24.545  1.00 30.05           C  
ANISOU 3138  C   GLN A 423     3443   3854   4119    -64    -68    340       C  
ATOM   3139  O   GLN A 423      19.066   0.171  25.461  1.00 30.76           O  
ANISOU 3139  O   GLN A 423     3531   3954   4200    -69    -80    354       O  
ATOM   3140  CB  GLN A 423      22.021  -0.396  25.553  1.00 30.15           C  
ANISOU 3140  CB  GLN A 423     3428   3848   4179    -76    -86    356       C  
ATOM   3141  CG  GLN A 423      23.053   0.696  25.598  1.00 31.81           C  
ANISOU 3141  CG  GLN A 423     3644   4059   4383    -77    -77    350       C  
ATOM   3142  CD  GLN A 423      24.225   0.360  26.504  1.00 33.17           C  
ANISOU 3142  CD  GLN A 423     3800   4223   4580    -86    -92    365       C  
ATOM   3143  OE1 GLN A 423      24.465  -0.804  26.853  1.00 33.23           O  
ANISOU 3143  OE1 GLN A 423     3790   4219   4616    -91   -108    376       O  
ATOM   3144  NE2 GLN A 423      24.970   1.388  26.887  1.00 33.81           N  
ANISOU 3144  NE2 GLN A 423     3887   4308   4651    -90    -89    365       N  
ATOM   3145  N   HIS A 424      19.659   1.445  23.692  1.00 28.53           N  
ANISOU 3145  N   HIS A 424     3267   3665   3907    -57    -52    324       N  
ATOM   3146  CA  HIS A 424      18.498   2.313  23.766  1.00 27.84           C  
ANISOU 3146  CA  HIS A 424     3195   3592   3788    -55    -48    323       C  
ATOM   3147  C   HIS A 424      18.018   2.530  22.353  1.00 27.42           C  
ANISOU 3147  C   HIS A 424     3154   3535   3728    -46    -36    305       C  
ATOM   3148  O   HIS A 424      18.780   2.986  21.501  1.00 26.86           O  
ANISOU 3148  O   HIS A 424     3088   3457   3659    -43    -24    292       O  
ATOM   3149  CB  HIS A 424      18.876   3.625  24.459  1.00 27.42           C  
ANISOU 3149  CB  HIS A 424     3151   3551   3716    -58    -44    325       C  
ATOM   3150  CG  HIS A 424      17.703   4.533  24.751  1.00 28.12           C  
ANISOU 3150  CG  HIS A 424     3253   3654   3775    -57    -40    325       C  
ATOM   3151  ND1 HIS A 424      17.079   5.255  23.789  1.00 27.98           N  
ANISOU 3151  ND1 HIS A 424     3249   3638   3743    -49    -30    311       N  
ATOM   3152  CD2 HIS A 424      17.053   4.836  25.950  1.00 28.72           C  
ANISOU 3152  CD2 HIS A 424     3330   3745   3836    -64    -47    336       C  
ATOM   3153  CE1 HIS A 424      16.077   5.969  24.336  1.00 27.64           C  
ANISOU 3153  CE1 HIS A 424     3214   3608   3679    -50    -29    314       C  
ATOM   3154  NE2 HIS A 424      16.061   5.718  25.658  1.00 28.70           N  
ANISOU 3154  NE2 HIS A 424     3341   3751   3813    -59    -38    328       N  
ATOM   3155  N   LEU A 425      16.761   2.174  22.091  1.00 26.95           N  
ANISOU 3155  N   LEU A 425     3097   3479   3661    -42    -39    306       N  
ATOM   3156  CA  LEU A 425      16.169   2.287  20.760  1.00 27.34           C  
ANISOU 3156  CA  LEU A 425     3159   3525   3704    -35    -30    291       C  
ATOM   3157  C   LEU A 425      14.752   2.882  20.852  1.00 28.72           C  
ANISOU 3157  C   LEU A 425     3344   3711   3857    -32    -32    293       C  
ATOM   3158  O   LEU A 425      13.871   2.302  21.511  1.00 28.39           O  
ANISOU 3158  O   LEU A 425     3295   3674   3817    -33    -41    303       O  
ATOM   3159  CB  LEU A 425      16.176   0.922  20.061  1.00 26.59           C  
ANISOU 3159  CB  LEU A 425     3053   3416   3632    -33    -33    287       C  
ATOM   3160  CG  LEU A 425      15.612   0.719  18.648  1.00 26.66           C  
ANISOU 3160  CG  LEU A 425     3072   3418   3637    -27    -27    271       C  
ATOM   3161  CD1 LEU A 425      16.243   1.640  17.615  1.00 27.18           C  
ANISOU 3161  CD1 LEU A 425     3154   3481   3691    -26    -11    255       C  
ATOM   3162  CD2 LEU A 425      15.765  -0.726  18.216  1.00 26.05           C  
ANISOU 3162  CD2 LEU A 425     2982   3328   3587    -27    -31    268       C  
ATOM   3163  N   ASP A 426      14.546   4.044  20.213  1.00 29.27           N  
ANISOU 3163  N   ASP A 426     3430   3784   3907    -28    -22    283       N  
ATOM   3164  CA  ASP A 426      13.267   4.774  20.309  1.00 29.81           C  
ANISOU 3164  CA  ASP A 426     3507   3861   3956    -25    -23    284       C  
ATOM   3165  C   ASP A 426      12.625   5.015  18.940  1.00 30.15           C  
ANISOU 3165  C   ASP A 426     3564   3898   3992    -20    -20    272       C  
ATOM   3166  O   ASP A 426      13.208   5.681  18.080  1.00 30.28           O  
ANISOU 3166  O   ASP A 426     3593   3911   4001    -19    -11    262       O  
ATOM   3167  CB  ASP A 426      13.422   6.103  21.078  1.00 30.04           C  
ANISOU 3167  CB  ASP A 426     3543   3901   3969    -27    -19    286       C  
ATOM   3168  CG  ASP A 426      12.077   6.663  21.588  1.00 30.88           C  
ANISOU 3168  CG  ASP A 426     3652   4016   4061    -26    -21    290       C  
ATOM   3169  OD1 ASP A 426      11.009   6.259  21.075  1.00 31.42           O  
ANISOU 3169  OD1 ASP A 426     3722   4083   4131    -22    -26    289       O  
ATOM   3170  OD2 ASP A 426      12.083   7.511  22.510  1.00 30.10           O  
ANISOU 3170  OD2 ASP A 426     3555   3928   3952    -29    -19    293       O  
ATOM   3171  N   PHE A 427      11.419   4.474  18.763  1.00 29.64           N  
ANISOU 3171  N   PHE A 427     3499   3834   3929    -17    -27    275       N  
ATOM   3172  CA  PHE A 427      10.682   4.548  17.497  1.00 29.93           C  
ANISOU 3172  CA  PHE A 427     3548   3864   3959    -13    -27    266       C  
ATOM   3173  C   PHE A 427       9.305   5.172  17.697  1.00 30.34           C  
ANISOU 3173  C   PHE A 427     3604   3923   4001     -9    -33    269       C  
ATOM   3174  O   PHE A 427       8.480   5.237  16.768  1.00 30.24           O  
ANISOU 3174  O   PHE A 427     3600   3905   3984     -6    -36    265       O  
ATOM   3175  CB  PHE A 427      10.467   3.148  16.934  1.00 29.70           C  
ANISOU 3175  CB  PHE A 427     3511   3826   3946    -12    -33    264       C  
ATOM   3176  CG  PHE A 427      11.626   2.596  16.164  1.00 29.34           C  
ANISOU 3176  CG  PHE A 427     3466   3770   3911    -14    -26    254       C  
ATOM   3177  CD1 PHE A 427      12.204   1.392  16.543  1.00 29.22           C  
ANISOU 3177  CD1 PHE A 427     3434   3749   3919    -16    -29    258       C  
ATOM   3178  CD2 PHE A 427      12.104   3.241  15.031  1.00 29.30           C  
ANISOU 3178  CD2 PHE A 427     3476   3760   3894    -15    -16    241       C  
ATOM   3179  CE1 PHE A 427      13.244   0.848  15.809  1.00 29.44           C  
ANISOU 3179  CE1 PHE A 427     3459   3766   3959    -18    -21    246       C  
ATOM   3180  CE2 PHE A 427      13.142   2.704  14.293  1.00 28.70           C  
ANISOU 3180  CE2 PHE A 427     3399   3674   3829    -18     -7    230       C  
ATOM   3181  CZ  PHE A 427      13.718   1.512  14.684  1.00 29.05           C  
ANISOU 3181  CZ  PHE A 427     3426   3712   3898    -19     -9    232       C  
ATOM   3182  N   GLN A 428       9.063   5.600  18.932  1.00 30.74           N  
ANISOU 3182  N   GLN A 428     3647   3983   4047    -11    -33    278       N  
ATOM   3183  CA  GLN A 428       7.819   6.223  19.363  1.00 30.15           C  
ANISOU 3183  CA  GLN A 428     3573   3915   3965     -9    -36    281       C  
ATOM   3184  C   GLN A 428       7.201   7.129  18.293  1.00 29.33           C  
ANISOU 3184  C   GLN A 428     3485   3806   3852     -4    -36    273       C  
ATOM   3185  O   GLN A 428       7.881   7.971  17.722  1.00 28.42           O  
ANISOU 3185  O   GLN A 428     3381   3689   3728     -4    -30    266       O  
ATOM   3186  CB  GLN A 428       8.111   7.012  20.646  1.00 30.55           C  
ANISOU 3186  CB  GLN A 428     3620   3977   4008    -13    -31    286       C  
ATOM   3187  CG  GLN A 428       6.964   7.823  21.193  1.00 32.11           C  
ANISOU 3187  CG  GLN A 428     3819   4182   4199    -12    -30    287       C  
ATOM   3188  CD  GLN A 428       7.247   8.419  22.559  1.00 33.17           C  
ANISOU 3188  CD  GLN A 428     3948   4328   4326    -18    -25    291       C  
ATOM   3189  OE1 GLN A 428       6.404   8.330  23.455  1.00 35.88           O  
ANISOU 3189  OE1 GLN A 428     4284   4679   4669    -20    -25    296       O  
ATOM   3190  NE2 GLN A 428       8.412   9.043  22.724  1.00 30.41           N  
ANISOU 3190  NE2 GLN A 428     3603   3980   3970    -20    -19    289       N  
ATOM   3191  N   HIS A 429       5.909   6.938  18.027  1.00 30.06           N  
ANISOU 3191  N   HIS A 429     3577   3897   3948     -1    -44    274       N  
ATOM   3192  CA  HIS A 429       5.127   7.823  17.146  1.00 30.44           C  
ANISOU 3192  CA  HIS A 429     3637   3940   3989      2    -47    269       C  
ATOM   3193  C   HIS A 429       5.594   7.899  15.702  1.00 30.89           C  
ANISOU 3193  C   HIS A 429     3709   3986   4039      2    -48    261       C  
ATOM   3194  O   HIS A 429       5.256   8.843  15.007  1.00 33.03           O  
ANISOU 3194  O   HIS A 429     3994   4254   4302      3    -50    257       O  
ATOM   3195  CB  HIS A 429       5.045   9.239  17.728  1.00 29.49           C  
ANISOU 3195  CB  HIS A 429     3519   3824   3859      3    -41    268       C  
ATOM   3196  CG  HIS A 429       4.010   9.405  18.810  1.00 29.99           C  
ANISOU 3196  CG  HIS A 429     3571   3895   3927      3    -42    273       C  
ATOM   3197  ND1 HIS A 429       2.698   9.556  18.540  1.00 31.06           N  
ANISOU 3197  ND1 HIS A 429     3704   4026   4068      7    -49    273       N  
ATOM   3198  CD2 HIS A 429       4.135   9.476  20.191  1.00 30.15           C  
ANISOU 3198  CD2 HIS A 429     3581   3927   3948      0    -36    277       C  
ATOM   3199  CE1 HIS A 429       2.016   9.702  19.691  1.00 30.79           C  
ANISOU 3199  CE1 HIS A 429     3658   4000   4038      6    -46    276       C  
ATOM   3200  NE2 HIS A 429       2.893   9.652  20.702  1.00 30.64           N  
ANISOU 3200  NE2 HIS A 429     3635   3991   4014      1    -38    279       N  
ATOM   3201  N   SER A 430       6.379   6.938  15.236  1.00 30.56           N  
ANISOU 3201  N   SER A 430     3668   3941   4003      0    -46    258       N  
ATOM   3202  CA  SER A 430       6.778   6.907  13.836  1.00 31.49           C  
ANISOU 3202  CA  SER A 430     3800   4049   4113     -2    -44    249       C  
ATOM   3203  C   SER A 430       6.009   5.809  13.128  1.00 32.91           C  
ANISOU 3203  C   SER A 430     3980   4222   4302     -1    -54    248       C  
ATOM   3204  O   SER A 430       5.515   4.869  13.762  1.00 33.26           O  
ANISOU 3204  O   SER A 430     4009   4267   4359      0    -60    254       O  
ATOM   3205  CB  SER A 430       8.270   6.613  13.693  1.00 31.28           C  
ANISOU 3205  CB  SER A 430     3774   4021   4088     -6    -33    243       C  
ATOM   3206  OG  SER A 430       9.038   7.414  14.560  1.00 33.17           O  
ANISOU 3206  OG  SER A 430     4010   4267   4323     -7    -25    245       O  
ATOM   3207  N   THR A 431       5.933   5.906  11.809  1.00 32.91           N  
ANISOU 3207  N   THR A 431     3996   4214   4293     -4    -57    240       N  
ATOM   3208  CA  THR A 431       5.303   4.857  11.025  1.00 34.20           C  
ANISOU 3208  CA  THR A 431     4161   4370   4463     -5    -65    238       C  
ATOM   3209  C   THR A 431       6.302   3.733  10.744  1.00 34.21           C  
ANISOU 3209  C   THR A 431     4158   4367   4473     -8    -58    230       C  
ATOM   3210  O   THR A 431       6.938   3.694   9.686  1.00 32.95           O  
ANISOU 3210  O   THR A 431     4012   4201   4305    -14    -51    219       O  
ATOM   3211  CB  THR A 431       4.713   5.412   9.717  1.00 35.33           C  
ANISOU 3211  CB  THR A 431     4326   4506   4592     -8    -73    233       C  
ATOM   3212  OG1 THR A 431       4.002   6.625  10.001  1.00 35.19           O  
ANISOU 3212  OG1 THR A 431     4311   4490   4568     -5    -79    240       O  
ATOM   3213  CG2 THR A 431       3.783   4.390   9.061  1.00 35.24           C  
ANISOU 3213  CG2 THR A 431     4314   4487   4588     -8    -86    233       C  
ATOM   3214  N   LEU A 432       6.449   2.844  11.725  1.00 35.30           N  
ANISOU 3214  N   LEU A 432     4276   4508   4628     -6    -58    236       N  
ATOM   3215  CA  LEU A 432       7.213   1.611  11.562  1.00 36.10           C  
ANISOU 3215  CA  LEU A 432     4369   4603   4744     -8    -53    231       C  
ATOM   3216  C   LEU A 432       6.533   0.701  10.551  1.00 37.47           C  
ANISOU 3216  C   LEU A 432     4547   4767   4921     -9    -61    225       C  
ATOM   3217  O   LEU A 432       5.308   0.560  10.552  1.00 40.67           O  
ANISOU 3217  O   LEU A 432     4952   5173   5328     -6    -74    231       O  
ATOM   3218  CB  LEU A 432       7.317   0.868  12.889  1.00 34.87           C  
ANISOU 3218  CB  LEU A 432     4190   4451   4606     -6    -56    242       C  
ATOM   3219  CG  LEU A 432       8.548   0.966  13.772  1.00 34.42           C  
ANISOU 3219  CG  LEU A 432     4123   4398   4555     -8    -47    245       C  
ATOM   3220  CD1 LEU A 432       8.330   0.022  14.935  1.00 34.12           C  
ANISOU 3220  CD1 LEU A 432     4064   4363   4535     -7    -55    257       C  
ATOM   3221  CD2 LEU A 432       9.811   0.593  13.016  1.00 34.72           C  
ANISOU 3221  CD2 LEU A 432     4163   4427   4599    -11    -36    232       C  
ATOM   3222  N   LYS A 433       7.332   0.066   9.709  1.00 37.85           N  
ANISOU 3222  N   LYS A 433     4600   4808   4973    -14    -53    212       N  
ATOM   3223  CA  LYS A 433       6.802  -0.731   8.623  1.00 37.88           C  
ANISOU 3223  CA  LYS A 433     4612   4802   4977    -17    -59    204       C  
ATOM   3224  C   LYS A 433       7.560  -2.033   8.574  1.00 37.86           C  
ANISOU 3224  C   LYS A 433     4595   4792   4995    -18    -53    196       C  
ATOM   3225  O   LYS A 433       8.773  -2.067   8.785  1.00 39.26           O  
ANISOU 3225  O   LYS A 433     4768   4969   5181    -20    -40    190       O  
ATOM   3226  CB  LYS A 433       7.000   0.001   7.296  1.00 39.97           C  
ANISOU 3226  CB  LYS A 433     4902   5064   5219    -24    -54    192       C  
ATOM   3227  CG  LYS A 433       5.738   0.265   6.506  1.00 42.18           C  
ANISOU 3227  CG  LYS A 433     5197   5341   5487    -25    -68    194       C  
ATOM   3228  CD  LYS A 433       5.233   1.680   6.733  1.00 44.35           C  
ANISOU 3228  CD  LYS A 433     5481   5623   5746    -23    -74    203       C  
ATOM   3229  CE  LYS A 433       3.940   1.932   5.967  1.00 48.46           C  
ANISOU 3229  CE  LYS A 433     6015   6138   6257    -25    -91    207       C  
ATOM   3230  NZ  LYS A 433       3.720   3.391   5.725  1.00 50.32           N  
ANISOU 3230  NZ  LYS A 433     6266   6376   6475    -26    -94    211       N  
ATOM   3231  N   ARG A 434       6.832  -3.103   8.290  1.00 38.15           N  
ANISOU 3231  N   ARG A 434     4627   4822   5044    -17    -63    195       N  
ATOM   3232  CA  ARG A 434       7.400  -4.426   8.033  1.00 38.64           C  
ANISOU 3232  CA  ARG A 434     4678   4875   5128    -19    -59    186       C  
ATOM   3233  C   ARG A 434       8.149  -5.017   9.223  1.00 38.69           C  
ANISOU 3233  C   ARG A 434     4660   4881   5159    -16    -57    194       C  
ATOM   3234  O   ARG A 434       8.764  -6.065   9.105  1.00 40.50           O  
ANISOU 3234  O   ARG A 434     4876   5101   5409    -17    -53    186       O  
ATOM   3235  CB  ARG A 434       8.251  -4.429   6.754  1.00 38.20           C  
ANISOU 3235  CB  ARG A 434     4638   4812   5064    -27    -44    164       C  
ATOM   3236  CG  ARG A 434       7.541  -3.781   5.565  1.00 41.36           C  
ANISOU 3236  CG  ARG A 434     5065   5211   5436    -33    -48    158       C  
ATOM   3237  CD  ARG A 434       7.962  -4.364   4.226  1.00 44.59           C  
ANISOU 3237  CD  ARG A 434     5487   5611   5841    -42    -38    137       C  
ATOM   3238  NE  ARG A 434       9.415  -4.487   4.143  1.00 48.48           N  
ANISOU 3238  NE  ARG A 434     5976   6101   6343    -46    -17    123       N  
ATOM   3239  CZ  ARG A 434      10.176  -3.912   3.219  1.00 48.46           C  
ANISOU 3239  CZ  ARG A 434     5992   6097   6322    -55     -1    108       C  
ATOM   3240  NH1 ARG A 434       9.618  -3.173   2.260  1.00 48.91           N  
ANISOU 3240  NH1 ARG A 434     6076   6157   6350    -63     -5    105       N  
ATOM   3241  NH2 ARG A 434      11.496  -4.088   3.256  1.00 45.15           N  
ANISOU 3241  NH2 ARG A 434     5564   5674   5915    -58     17     96       N  
ATOM   3242  N   VAL A 435       8.056  -4.360  10.376  1.00 38.34           N  
ANISOU 3242  N   VAL A 435     4607   4847   5111    -12    -60    209       N  
ATOM   3243  CA  VAL A 435       8.671  -4.845  11.614  1.00 39.02           C  
ANISOU 3243  CA  VAL A 435     4672   4935   5218    -11    -61    220       C  
ATOM   3244  C   VAL A 435       8.074  -6.194  12.058  1.00 39.74           C  
ANISOU 3244  C   VAL A 435     4745   5021   5334     -9    -74    228       C  
ATOM   3245  O   VAL A 435       8.621  -6.888  12.911  1.00 39.63           O  
ANISOU 3245  O   VAL A 435     4711   5004   5340     -9    -77    236       O  
ATOM   3246  CB  VAL A 435       8.589  -3.766  12.735  1.00 37.79           C  
ANISOU 3246  CB  VAL A 435     4515   4793   5051     -9    -62    234       C  
ATOM   3247  CG1 VAL A 435       7.242  -3.783  13.438  1.00 36.38           C  
ANISOU 3247  CG1 VAL A 435     4331   4622   4869     -6    -76    249       C  
ATOM   3248  CG2 VAL A 435       9.725  -3.916  13.740  1.00 36.68           C  
ANISOU 3248  CG2 VAL A 435     4359   4654   4924    -11    -58    241       C  
ATOM   3249  N   THR A 436       6.954  -6.567  11.458  1.00 43.65           N  
ANISOU 3249  N   THR A 436     5245   5513   5825     -8    -83    227       N  
ATOM   3250  CA  THR A 436       6.270  -7.792  11.835  1.00 47.02           C  
ANISOU 3250  CA  THR A 436     5656   5935   6273     -6    -97    235       C  
ATOM   3251  C   THR A 436       6.606  -8.948  10.887  1.00 48.25           C  
ANISOU 3251  C   THR A 436     5808   6075   6446     -8    -95    220       C  
ATOM   3252  O   THR A 436       6.449 -10.113  11.240  1.00 50.38           O  
ANISOU 3252  O   THR A 436     6062   6339   6741     -7   -104    225       O  
ATOM   3253  CB  THR A 436       4.750  -7.568  11.934  1.00 48.70           C  
ANISOU 3253  CB  THR A 436     5873   6153   6476     -3   -110    245       C  
ATOM   3254  OG1 THR A 436       4.146  -8.712  12.539  1.00 52.53           O  
ANISOU 3254  OG1 THR A 436     6340   6636   6983     -2   -122    256       O  
ATOM   3255  CG2 THR A 436       4.123  -7.316  10.555  1.00 48.84           C  
ANISOU 3255  CG2 THR A 436     5911   6166   6478     -4   -111    232       C  
ATOM   3256  N   GLU A 437       7.097  -8.608   9.699  1.00 48.65           N  
ANISOU 3256  N   GLU A 437     5877   6121   6485    -11    -83    201       N  
ATOM   3257  CA  GLU A 437       7.441  -9.580   8.662  1.00 48.93           C  
ANISOU 3257  CA  GLU A 437     5914   6144   6534    -15    -78    182       C  
ATOM   3258  C   GLU A 437       8.678 -10.440   8.965  1.00 49.53           C  
ANISOU 3258  C   GLU A 437     5970   6209   6639    -16    -70    176       C  
ATOM   3259  O   GLU A 437       8.885 -11.447   8.295  1.00 53.37           O  
ANISOU 3259  O   GLU A 437     6452   6683   7144    -18    -68    162       O  
ATOM   3260  CB  GLU A 437       7.634  -8.873   7.313  1.00 49.70           C  
ANISOU 3260  CB  GLU A 437     6038   6240   6606    -21    -67    164       C  
ATOM   3261  CG  GLU A 437       6.412  -8.118   6.809  1.00 51.85           C  
ANISOU 3261  CG  GLU A 437     6329   6518   6850    -21    -77    168       C  
ATOM   3262  CD  GLU A 437       6.597  -7.531   5.415  1.00 55.36           C  
ANISOU 3262  CD  GLU A 437     6801   6960   7270    -29    -67    150       C  
ATOM   3263  OE1 GLU A 437       5.729  -6.732   5.000  1.00 55.68           O  
ANISOU 3263  OE1 GLU A 437     6860   7006   7287    -30    -76    155       O  
ATOM   3264  OE2 GLU A 437       7.597  -7.861   4.728  1.00 56.38           O  
ANISOU 3264  OE2 GLU A 437     6934   7082   7402    -35    -51    132       O  
ATOM   3265  N   PHE A 438       9.506 -10.037   9.936  1.00 47.45           N  
ANISOU 3265  N   PHE A 438     5695   5950   6382    -15    -66    186       N  
ATOM   3266  CA  PHE A 438      10.685 -10.832  10.367  1.00 44.48           C  
ANISOU 3266  CA  PHE A 438     5297   5563   6038    -16    -61    183       C  
ATOM   3267  C   PHE A 438      11.115 -10.526  11.806  1.00 41.75           C  
ANISOU 3267  C   PHE A 438     4936   5225   5700    -15    -67    204       C  
ATOM   3268  O   PHE A 438      10.470  -9.733  12.478  1.00 43.04           O  
ANISOU 3268  O   PHE A 438     5106   5403   5844    -13    -74    219       O  
ATOM   3269  CB  PHE A 438      11.868 -10.708   9.383  1.00 43.25           C  
ANISOU 3269  CB  PHE A 438     5148   5398   5884    -21    -40    159       C  
ATOM   3270  CG  PHE A 438      12.488  -9.335   9.312  1.00 42.94           C  
ANISOU 3270  CG  PHE A 438     5125   5369   5820    -23    -27    156       C  
ATOM   3271  CD1 PHE A 438      13.790  -9.127   9.757  1.00 42.62           C  
ANISOU 3271  CD1 PHE A 438     5073   5326   5794    -24    -16    154       C  
ATOM   3272  CD2 PHE A 438      11.789  -8.253   8.773  1.00 43.00           C  
ANISOU 3272  CD2 PHE A 438     5157   5387   5791    -24    -26    155       C  
ATOM   3273  CE1 PHE A 438      14.383  -7.870   9.677  1.00 41.88           C  
ANISOU 3273  CE1 PHE A 438     4993   5240   5678    -26     -4    151       C  
ATOM   3274  CE2 PHE A 438      12.374  -6.993   8.694  1.00 42.72           C  
ANISOU 3274  CE2 PHE A 438     5135   5359   5734    -26    -14    153       C  
ATOM   3275  CZ  PHE A 438      13.676  -6.802   9.144  1.00 42.24           C  
ANISOU 3275  CZ  PHE A 438     5063   5296   5687    -27     -3    151       C  
ATOM   3276  N   SER A 439      12.177 -11.172  12.287  1.00 39.89           N  
ANISOU 3276  N   SER A 439     4681   4980   5495    -16    -66    204       N  
ATOM   3277  CA  SER A 439      12.729 -10.831  13.601  1.00 39.64           C  
ANISOU 3277  CA  SER A 439     4636   4954   5469    -17    -71    223       C  
ATOM   3278  C   SER A 439      13.655  -9.618  13.473  1.00 38.58           C  
ANISOU 3278  C   SER A 439     4513   4826   5317    -19    -55    216       C  
ATOM   3279  O   SER A 439      14.862  -9.748  13.308  1.00 38.43           O  
ANISOU 3279  O   SER A 439     4486   4797   5316    -21    -45    206       O  
ATOM   3280  CB  SER A 439      13.433 -12.031  14.246  1.00 38.71           C  
ANISOU 3280  CB  SER A 439     4491   4823   5393    -18    -80    230       C  
ATOM   3281  OG  SER A 439      12.490 -12.963  14.748  1.00 37.48           O  
ANISOU 3281  OG  SER A 439     4324   4666   5250    -18    -98    245       O  
ATOM   3282  N   ALA A 440      13.066  -8.432  13.534  1.00 39.51           N  
ANISOU 3282  N   ALA A 440     4650   4959   5401    -18    -54    220       N  
ATOM   3283  CA  ALA A 440      13.780  -7.206  13.170  1.00 39.04           C  
ANISOU 3283  CA  ALA A 440     4606   4905   5322    -19    -38    211       C  
ATOM   3284  C   ALA A 440      14.771  -6.735  14.226  1.00 37.35           C  
ANISOU 3284  C   ALA A 440     4381   4694   5114    -21    -37    222       C  
ATOM   3285  O   ALA A 440      15.650  -5.936  13.920  1.00 37.66           O  
ANISOU 3285  O   ALA A 440     4428   4734   5145    -23    -23    212       O  
ATOM   3286  CB  ALA A 440      12.803  -6.089  12.816  1.00 39.42           C  
ANISOU 3286  CB  ALA A 440     4677   4966   5333    -18    -38    212       C  
ATOM   3287  N   PHE A 441      14.632  -7.211  15.458  1.00 34.91           N  
ANISOU 3287  N   PHE A 441     4055   4388   4819    -21    -53    242       N  
ATOM   3288  CA  PHE A 441      15.573  -6.823  16.502  1.00 34.29           C  
ANISOU 3288  CA  PHE A 441     3967   4313   4748    -25    -54    253       C  
ATOM   3289  C   PHE A 441      16.488  -7.969  16.919  1.00 34.62           C  
ANISOU 3289  C   PHE A 441     3984   4339   4830    -27    -61    257       C  
ATOM   3290  O   PHE A 441      17.005  -7.970  18.035  1.00 35.06           O  
ANISOU 3290  O   PHE A 441     4027   4396   4897    -31    -71    274       O  
ATOM   3291  CB  PHE A 441      14.838  -6.258  17.716  1.00 32.97           C  
ANISOU 3291  CB  PHE A 441     3802   4162   4563    -26    -66    275       C  
ATOM   3292  CG  PHE A 441      13.776  -5.265  17.371  1.00 32.70           C  
ANISOU 3292  CG  PHE A 441     3788   4141   4494    -23    -62    272       C  
ATOM   3293  CD1 PHE A 441      14.106  -3.970  17.019  1.00 32.35           C  
ANISOU 3293  CD1 PHE A 441     3760   4103   4426    -22    -49    264       C  
ATOM   3294  CD2 PHE A 441      12.436  -5.625  17.403  1.00 32.81           C  
ANISOU 3294  CD2 PHE A 441     3804   4159   4501    -21    -71    279       C  
ATOM   3295  CE1 PHE A 441      13.118  -3.056  16.699  1.00 31.91           C  
ANISOU 3295  CE1 PHE A 441     3723   4058   4343    -20    -47    262       C  
ATOM   3296  CE2 PHE A 441      11.443  -4.713  17.088  1.00 31.26           C  
ANISOU 3296  CE2 PHE A 441     3624   3973   4277    -18    -69    277       C  
ATOM   3297  CZ  PHE A 441      11.788  -3.428  16.736  1.00 31.16           C  
ANISOU 3297  CZ  PHE A 441     3628   3966   4242    -17    -57    269       C  
ATOM   3298  N   LEU A 442      16.699  -8.923  16.012  1.00 35.17           N  
ANISOU 3298  N   LEU A 442     4046   4392   4923    -26    -56    242       N  
ATOM   3299  CA  LEU A 442      17.395 -10.172  16.331  1.00 35.85           C  
ANISOU 3299  CA  LEU A 442     4106   4461   5051    -28    -65    245       C  
ATOM   3300  C   LEU A 442      18.816  -9.974  16.842  1.00 36.81           C  
ANISOU 3300  C   LEU A 442     4215   4575   5194    -31    -62    247       C  
ATOM   3301  O   LEU A 442      19.216 -10.650  17.785  1.00 39.87           O  
ANISOU 3301  O   LEU A 442     4581   4955   5609    -35    -78    263       O  
ATOM   3302  CB  LEU A 442      17.391 -11.134  15.137  1.00 36.44           C  
ANISOU 3302  CB  LEU A 442     4177   4519   5146    -26    -57    223       C  
ATOM   3303  CG  LEU A 442      17.942 -12.545  15.386  1.00 37.48           C  
ANISOU 3303  CG  LEU A 442     4282   4631   5327    -27    -67    225       C  
ATOM   3304  CD1 LEU A 442      17.100 -13.335  16.382  1.00 36.62           C  
ANISOU 3304  CD1 LEU A 442     4160   4525   5228    -28    -91    250       C  
ATOM   3305  CD2 LEU A 442      18.071 -13.300  14.072  1.00 38.30           C  
ANISOU 3305  CD2 LEU A 442     4384   4718   5447    -25    -53    198       C  
ATOM   3306  N   SER A 443      19.560  -9.044  16.237  1.00 35.64           N  
ANISOU 3306  N   SER A 443     4079   4428   5034    -31    -43    231       N  
ATOM   3307  CA  SER A 443      20.945  -8.766  16.623  1.00 34.79           C  
ANISOU 3307  CA  SER A 443     3959   4313   4945    -34    -38    231       C  
ATOM   3308  C   SER A 443      21.095  -8.104  17.979  1.00 34.45           C  
ANISOU 3308  C   SER A 443     3914   4282   4892    -38    -52    255       C  
ATOM   3309  O   SER A 443      22.188  -8.099  18.538  1.00 35.42           O  
ANISOU 3309  O   SER A 443     4022   4396   5036    -42    -55    260       O  
ATOM   3310  CB  SER A 443      21.609  -7.852  15.597  1.00 36.68           C  
ANISOU 3310  CB  SER A 443     4214   4552   5169    -34    -13    208       C  
ATOM   3311  OG  SER A 443      21.711  -8.475  14.330  1.00 40.38           O  
ANISOU 3311  OG  SER A 443     4684   5008   5650    -33      1    183       O  
ATOM   3312  N   LEU A 444      20.016  -7.534  18.506  1.00 33.09           N  
ANISOU 3312  N   LEU A 444     3756   4129   4687    -38    -60    268       N  
ATOM   3313  CA  LEU A 444      20.128  -6.640  19.654  1.00 33.00           C  
ANISOU 3313  CA  LEU A 444     3749   4131   4656    -42    -67    287       C  
ATOM   3314  C   LEU A 444      20.150  -7.329  21.020  1.00 33.56           C  
ANISOU 3314  C   LEU A 444     3802   4203   4746    -48    -90    312       C  
ATOM   3315  O   LEU A 444      19.306  -7.066  21.869  1.00 32.71           O  
ANISOU 3315  O   LEU A 444     3701   4111   4617    -51   -101    329       O  
ATOM   3316  CB  LEU A 444      19.068  -5.531  19.580  1.00 31.64           C  
ANISOU 3316  CB  LEU A 444     3601   3979   4441    -39    -62    287       C  
ATOM   3317  CG  LEU A 444      19.189  -4.650  18.329  1.00 32.27           C  
ANISOU 3317  CG  LEU A 444     3699   4060   4500    -35    -40    264       C  
ATOM   3318  CD1 LEU A 444      18.131  -3.552  18.284  1.00 32.29           C  
ANISOU 3318  CD1 LEU A 444     3724   4081   4463    -33    -38    266       C  
ATOM   3319  CD2 LEU A 444      20.587  -4.056  18.188  1.00 31.32           C  
ANISOU 3319  CD2 LEU A 444     3578   3934   4388    -37    -28    256       C  
ATOM   3320  N   GLU A 445      21.146  -8.193  21.227  1.00 35.82           N  
ANISOU 3320  N   GLU A 445     4065   4470   5072    -51    -98    315       N  
ATOM   3321  CA  GLU A 445      21.259  -8.988  22.461  1.00 36.62           C  
ANISOU 3321  CA  GLU A 445     4149   4568   5195    -59   -123    340       C  
ATOM   3322  C   GLU A 445      21.643  -8.166  23.692  1.00 35.10           C  
ANISOU 3322  C   GLU A 445     3959   4388   4987    -67   -132    360       C  
ATOM   3323  O   GLU A 445      21.546  -8.645  24.811  1.00 34.31           O  
ANISOU 3323  O   GLU A 445     3849   4290   4894    -76   -153    383       O  
ATOM   3324  CB  GLU A 445      22.214 -10.179  22.275  1.00 40.10           C  
ANISOU 3324  CB  GLU A 445     4563   4983   5688    -60   -129    338       C  
ATOM   3325  CG  GLU A 445      21.668 -11.297  21.379  1.00 45.19           C  
ANISOU 3325  CG  GLU A 445     5200   5615   6353    -54   -127    325       C  
ATOM   3326  CD  GLU A 445      22.519 -12.570  21.385  1.00 47.16           C  
ANISOU 3326  CD  GLU A 445     5421   5838   6657    -56   -138    325       C  
ATOM   3327  OE1 GLU A 445      23.670 -12.551  20.894  1.00 47.77           O  
ANISOU 3327  OE1 GLU A 445     5489   5901   6761    -55   -126    310       O  
ATOM   3328  OE2 GLU A 445      22.024 -13.610  21.867  1.00 48.55           O  
ANISOU 3328  OE2 GLU A 445     5583   6008   6852    -59   -157    340       O  
ATOM   3329  N   LYS A 446      22.037  -6.915  23.482  1.00 34.84           N  
ANISOU 3329  N   LYS A 446     3942   4364   4930    -66   -117    350       N  
ATOM   3330  CA  LYS A 446      22.401  -6.023  24.583  1.00 34.92           C  
ANISOU 3330  CA  LYS A 446     3958   4387   4923    -74   -124    365       C  
ATOM   3331  C   LYS A 446      21.408  -4.881  24.846  1.00 34.27           C  
ANISOU 3331  C   LYS A 446     3898   4328   4792    -73   -117    367       C  
ATOM   3332  O   LYS A 446      21.621  -4.069  25.759  1.00 33.56           O  
ANISOU 3332  O   LYS A 446     3815   4250   4685    -80   -121    378       O  
ATOM   3333  CB  LYS A 446      23.801  -5.446  24.355  1.00 35.42           C  
ANISOU 3333  CB  LYS A 446     4017   4440   5000    -74   -115    356       C  
ATOM   3334  CG  LYS A 446      24.920  -6.454  24.535  1.00 37.39           C  
ANISOU 3334  CG  LYS A 446     4240   4667   5299    -77   -127    361       C  
ATOM   3335  CD  LYS A 446      26.234  -5.858  24.077  1.00 39.13           C  
ANISOU 3335  CD  LYS A 446     4456   4876   5533    -76   -113    347       C  
ATOM   3336  CE  LYS A 446      27.417  -6.556  24.715  1.00 40.79           C  
ANISOU 3336  CE  LYS A 446     4641   5067   5789    -83   -130    359       C  
ATOM   3337  NZ  LYS A 446      28.533  -5.580  24.866  1.00 41.95           N  
ANISOU 3337  NZ  LYS A 446     4789   5212   5935    -85   -123    356       N  
ATOM   3338  N   LEU A 447      20.334  -4.808  24.058  1.00 33.07           N  
ANISOU 3338  N   LEU A 447     3758   4182   4622    -66   -107    355       N  
ATOM   3339  CA  LEU A 447      19.368  -3.718  24.207  1.00 31.68           C  
ANISOU 3339  CA  LEU A 447     3603   4026   4406    -64   -100    354       C  
ATOM   3340  C   LEU A 447      18.682  -3.703  25.579  1.00 31.67           C  
ANISOU 3340  C   LEU A 447     3602   4041   4390    -73   -115    377       C  
ATOM   3341  O   LEU A 447      18.171  -4.730  26.039  1.00 30.91           O  
ANISOU 3341  O   LEU A 447     3494   3942   4305    -77   -129    390       O  
ATOM   3342  CB  LEU A 447      18.321  -3.764  23.099  1.00 31.26           C  
ANISOU 3342  CB  LEU A 447     3561   3974   4340    -55    -89    339       C  
ATOM   3343  CG  LEU A 447      17.594  -2.438  22.870  1.00 30.76           C  
ANISOU 3343  CG  LEU A 447     3519   3926   4239    -51    -77    332       C  
ATOM   3344  CD1 LEU A 447      18.462  -1.524  22.016  1.00 30.67           C  
ANISOU 3344  CD1 LEU A 447     3518   3911   4222    -47    -60    315       C  
ATOM   3345  CD2 LEU A 447      16.250  -2.683  22.196  1.00 31.07           C  
ANISOU 3345  CD2 LEU A 447     3567   3970   4267    -45    -75    326       C  
ATOM   3346  N   LEU A 448      18.678  -2.538  26.225  1.00 30.57           N  
ANISOU 3346  N   LEU A 448     3475   3916   4223    -77   -111    380       N  
ATOM   3347  CA  LEU A 448      18.017  -2.389  27.526  1.00 30.31           C  
ANISOU 3347  CA  LEU A 448     3444   3899   4171    -88   -122    399       C  
ATOM   3348  C   LEU A 448      16.641  -1.720  27.449  1.00 31.07           C  
ANISOU 3348  C   LEU A 448     3557   4012   4237    -84   -113    394       C  
ATOM   3349  O   LEU A 448      15.784  -1.989  28.301  1.00 32.35           O  
ANISOU 3349  O   LEU A 448     3718   4184   4388    -91   -121    407       O  
ATOM   3350  CB  LEU A 448      18.905  -1.625  28.511  1.00 28.88           C  
ANISOU 3350  CB  LEU A 448     3266   3725   3982    -98   -126    408       C  
ATOM   3351  CG  LEU A 448      20.313  -2.173  28.773  1.00 28.38           C  
ANISOU 3351  CG  LEU A 448     3187   3646   3950   -103   -138    416       C  
ATOM   3352  CD1 LEU A 448      21.141  -1.193  29.594  1.00 26.97           C  
ANISOU 3352  CD1 LEU A 448     3013   3474   3758   -112   -139    422       C  
ATOM   3353  CD2 LEU A 448      20.237  -3.533  29.452  1.00 28.60           C  
ANISOU 3353  CD2 LEU A 448     3197   3666   4001   -112   -159    436       C  
ATOM   3354  N   TYR A 449      16.446  -0.871  26.431  1.00 29.74           N  
ANISOU 3354  N   TYR A 449     3401   3843   4054    -73    -96    375       N  
ATOM   3355  CA  TYR A 449      15.290   0.021  26.297  1.00 28.62           C  
ANISOU 3355  CA  TYR A 449     3275   3715   3884    -69    -86    368       C  
ATOM   3356  C   TYR A 449      14.744   0.062  24.852  1.00 28.74           C  
ANISOU 3356  C   TYR A 449     3297   3723   3899    -57    -76    351       C  
ATOM   3357  O   TYR A 449      15.471   0.395  23.904  1.00 27.88           O  
ANISOU 3357  O   TYR A 449     3193   3605   3794    -51    -66    337       O  
ATOM   3358  CB  TYR A 449      15.685   1.434  26.750  1.00 28.63           C  
ANISOU 3358  CB  TYR A 449     3288   3727   3863    -72    -78    365       C  
ATOM   3359  CG  TYR A 449      14.567   2.465  26.774  1.00 29.49           C  
ANISOU 3359  CG  TYR A 449     3410   3848   3944    -69    -69    359       C  
ATOM   3360  CD1 TYR A 449      14.145   3.113  25.603  1.00 29.99           C  
ANISOU 3360  CD1 TYR A 449     3485   3910   4000    -58    -57    342       C  
ATOM   3361  CD2 TYR A 449      13.952   2.818  27.975  1.00 30.23           C  
ANISOU 3361  CD2 TYR A 449     3506   3958   4022    -77    -71    369       C  
ATOM   3362  CE1 TYR A 449      13.132   4.069  25.633  1.00 30.58           C  
ANISOU 3362  CE1 TYR A 449     3570   3994   4052    -55    -50    337       C  
ATOM   3363  CE2 TYR A 449      12.941   3.770  28.020  1.00 30.60           C  
ANISOU 3363  CE2 TYR A 449     3563   4015   4047    -75    -62    362       C  
ATOM   3364  CZ  TYR A 449      12.532   4.394  26.849  1.00 31.12           C  
ANISOU 3364  CZ  TYR A 449     3639   4077   4108    -63    -52    346       C  
ATOM   3365  OH  TYR A 449      11.528   5.335  26.902  1.00 30.63           O  
ANISOU 3365  OH  TYR A 449     3585   4023   4028    -60    -44    340       O  
ATOM   3366  N   LEU A 450      13.460  -0.262  24.700  1.00 28.08           N  
ANISOU 3366  N   LEU A 450     3216   3644   3810    -54    -78    351       N  
ATOM   3367  CA  LEU A 450      12.809  -0.243  23.405  1.00 28.50           C  
ANISOU 3367  CA  LEU A 450     3277   3691   3861    -44    -71    337       C  
ATOM   3368  C   LEU A 450      11.429   0.394  23.479  1.00 29.53           C  
ANISOU 3368  C   LEU A 450     3417   3833   3971    -41    -69    336       C  
ATOM   3369  O   LEU A 450      10.540  -0.122  24.169  1.00 29.91           O  
ANISOU 3369  O   LEU A 450     3458   3886   4018    -44    -76    347       O  
ATOM   3370  CB  LEU A 450      12.692  -1.659  22.832  1.00 28.35           C  
ANISOU 3370  CB  LEU A 450     3246   3659   3866    -42    -79    337       C  
ATOM   3371  CG  LEU A 450      12.013  -1.781  21.459  1.00 28.03           C  
ANISOU 3371  CG  LEU A 450     3214   3611   3823    -33    -73    322       C  
ATOM   3372  CD1 LEU A 450      12.702  -0.883  20.440  1.00 27.59           C  
ANISOU 3372  CD1 LEU A 450     3172   3551   3758    -29    -59    305       C  
ATOM   3373  CD2 LEU A 450      11.975  -3.221  20.961  1.00 27.24           C  
ANISOU 3373  CD2 LEU A 450     3101   3497   3749    -31    -81    321       C  
ATOM   3374  N   ASP A 451      11.254   1.506  22.763  1.00 29.14           N  
ANISOU 3374  N   ASP A 451     3381   3784   3904    -35    -58    323       N  
ATOM   3375  CA  ASP A 451       9.950   2.146  22.647  1.00 29.04           C  
ANISOU 3375  CA  ASP A 451     3377   3779   3876    -31    -56    321       C  
ATOM   3376  C   ASP A 451       9.406   2.006  21.222  1.00 29.58           C  
ANISOU 3376  C   ASP A 451     3454   3838   3946    -23    -54    309       C  
ATOM   3377  O   ASP A 451       9.984   2.568  20.283  1.00 30.69           O  
ANISOU 3377  O   ASP A 451     3605   3973   4082    -20    -47    297       O  
ATOM   3378  CB  ASP A 451      10.027   3.624  23.050  1.00 29.32           C  
ANISOU 3378  CB  ASP A 451     3423   3823   3891    -32    -47    317       C  
ATOM   3379  CG  ASP A 451       8.647   4.233  23.340  1.00 30.34           C  
ANISOU 3379  CG  ASP A 451     3556   3961   4008    -30    -46    317       C  
ATOM   3380  OD1 ASP A 451       7.621   3.625  22.932  1.00 29.66           O  
ANISOU 3380  OD1 ASP A 451     3467   3872   3929    -26    -51    318       O  
ATOM   3381  OD2 ASP A 451       8.591   5.315  23.985  1.00 29.15           O  
ANISOU 3381  OD2 ASP A 451     3411   3820   3844    -32    -40    316       O  
ATOM   3382  N   ILE A 452       8.311   1.250  21.075  1.00 28.13           N  
ANISOU 3382  N   ILE A 452     3265   3652   3769    -21    -62    312       N  
ATOM   3383  CA  ILE A 452       7.571   1.133  19.804  1.00 27.62           C  
ANISOU 3383  CA  ILE A 452     3209   3580   3705    -14    -63    302       C  
ATOM   3384  C   ILE A 452       6.110   1.593  19.955  1.00 27.06           C  
ANISOU 3384  C   ILE A 452     3140   3514   3625    -11    -66    305       C  
ATOM   3385  O   ILE A 452       5.241   1.207  19.180  1.00 26.79           O  
ANISOU 3385  O   ILE A 452     3109   3474   3595     -7    -72    302       O  
ATOM   3386  CB  ILE A 452       7.606  -0.305  19.211  1.00 27.56           C  
ANISOU 3386  CB  ILE A 452     3193   3560   3716    -13    -70    302       C  
ATOM   3387  CG1 ILE A 452       7.181  -1.335  20.255  1.00 27.20           C  
ANISOU 3387  CG1 ILE A 452     3131   3519   3685    -18    -80    317       C  
ATOM   3388  CG2 ILE A 452       8.980  -0.640  18.625  1.00 27.28           C  
ANISOU 3388  CG2 ILE A 452     3158   3516   3691    -15    -64    294       C  
ATOM   3389  CD1 ILE A 452       6.863  -2.696  19.674  1.00 27.77           C  
ANISOU 3389  CD1 ILE A 452     3194   3579   3776    -16    -89    317       C  
ATOM   3390  N   SER A 453       5.852   2.414  20.967  1.00 27.19           N  
ANISOU 3390  N   SER A 453     3156   3542   3631    -14    -62    310       N  
ATOM   3391  CA  SER A 453       4.531   2.958  21.228  1.00 27.47           C  
ANISOU 3391  CA  SER A 453     3193   3583   3661    -12    -63    311       C  
ATOM   3392  C   SER A 453       4.007   3.829  20.081  1.00 28.54           C  
ANISOU 3392  C   SER A 453     3342   3712   3789     -5    -62    300       C  
ATOM   3393  O   SER A 453       4.759   4.592  19.479  1.00 28.86           O  
ANISOU 3393  O   SER A 453     3393   3750   3820     -4    -56    292       O  
ATOM   3394  CB  SER A 453       4.561   3.792  22.499  1.00 28.00           C  
ANISOU 3394  CB  SER A 453     3257   3663   3717    -17    -56    315       C  
ATOM   3395  OG  SER A 453       5.089   3.067  23.591  1.00 29.01           O  
ANISOU 3395  OG  SER A 453     3375   3798   3850    -26    -58    326       O  
ATOM   3396  N   TYR A 454       2.709   3.704  19.797  1.00 29.29           N  
ANISOU 3396  N   TYR A 454     3435   3804   3888     -1    -68    301       N  
ATOM   3397  CA  TYR A 454       2.005   4.513  18.791  1.00 29.75           C  
ANISOU 3397  CA  TYR A 454     3505   3856   3942      3    -71    293       C  
ATOM   3398  C   TYR A 454       2.686   4.469  17.436  1.00 30.78           C  
ANISOU 3398  C   TYR A 454     3648   3976   4068      5    -72    285       C  
ATOM   3399  O   TYR A 454       2.663   5.446  16.695  1.00 33.44           O  
ANISOU 3399  O   TYR A 454     3999   4309   4395      7    -71    278       O  
ATOM   3400  CB  TYR A 454       1.809   5.970  19.251  1.00 29.93           C  
ANISOU 3400  CB  TYR A 454     3531   3884   3953      4    -63    290       C  
ATOM   3401  CG  TYR A 454       1.453   6.086  20.711  1.00 31.13           C  
ANISOU 3401  CG  TYR A 454     3672   4049   4107      0    -58    296       C  
ATOM   3402  CD1 TYR A 454       2.437   6.401  21.651  1.00 31.35           C  
ANISOU 3402  CD1 TYR A 454     3698   4086   4127     -5    -49    298       C  
ATOM   3403  CD2 TYR A 454       0.142   5.848  21.163  1.00 30.87           C  
ANISOU 3403  CD2 TYR A 454     3628   4017   4082      1    -61    300       C  
ATOM   3404  CE1 TYR A 454       2.139   6.488  22.996  1.00 32.20           C  
ANISOU 3404  CE1 TYR A 454     3796   4205   4232    -11    -44    303       C  
ATOM   3405  CE2 TYR A 454      -0.170   5.927  22.511  1.00 31.64           C  
ANISOU 3405  CE2 TYR A 454     3715   4126   4178     -4    -54    305       C  
ATOM   3406  CZ  TYR A 454       0.835   6.246  23.426  1.00 33.48           C  
ANISOU 3406  CZ  TYR A 454     3949   4369   4401    -11    -45    306       C  
ATOM   3407  OH  TYR A 454       0.567   6.349  24.779  1.00 34.24           O  
ANISOU 3407  OH  TYR A 454     4037   4479   4494    -19    -38    311       O  
ATOM   3408  N   THR A 455       3.292   3.337  17.112  1.00 30.81           N  
ANISOU 3408  N   THR A 455     3649   3975   4080      3    -74    285       N  
ATOM   3409  CA  THR A 455       3.941   3.189  15.834  1.00 31.30           C  
ANISOU 3409  CA  THR A 455     3724   4028   4139      3    -73    275       C  
ATOM   3410  C   THR A 455       2.996   2.475  14.905  1.00 32.41           C  
ANISOU 3410  C   THR A 455     3868   4160   4287      5    -84    273       C  
ATOM   3411  O   THR A 455       3.313   2.214  13.741  1.00 32.81           O  
ANISOU 3411  O   THR A 455     3930   4202   4334      4    -85    265       O  
ATOM   3412  CB  THR A 455       5.253   2.407  15.948  1.00 30.92           C  
ANISOU 3412  CB  THR A 455     3670   3978   4098      0    -67    273       C  
ATOM   3413  OG1 THR A 455       4.979   1.065  16.380  1.00 28.98           O  
ANISOU 3413  OG1 THR A 455     3409   3731   3869      0    -74    280       O  
ATOM   3414  CG2 THR A 455       6.181   3.116  16.915  1.00 30.35           C  
ANISOU 3414  CG2 THR A 455     3596   3915   4021     -2    -58    276       C  
ATOM   3415  N   ASN A 456       1.830   2.143  15.439  1.00 35.00           N  
ANISOU 3415  N   ASN A 456     4185   4490   4623      7    -92    281       N  
ATOM   3416  CA  ASN A 456       0.752   1.602  14.629  1.00 36.62           C  
ANISOU 3416  CA  ASN A 456     4392   4686   4834      9   -104    280       C  
ATOM   3417  C   ASN A 456       1.026   0.188  14.144  1.00 35.45           C  
ANISOU 3417  C   ASN A 456     4240   4531   4698      8   -109    279       C  
ATOM   3418  O   ASN A 456       0.845  -0.117  12.960  1.00 36.96           O  
ANISOU 3418  O   ASN A 456     4442   4712   4887      7   -114    271       O  
ATOM   3419  CB  ASN A 456       0.499   2.511  13.425  1.00 38.31           C  
ANISOU 3419  CB  ASN A 456     4625   4893   5036     10   -108    273       C  
ATOM   3420  CG  ASN A 456      -0.807   2.205  12.758  1.00 42.78           C  
ANISOU 3420  CG  ASN A 456     5193   5451   5609     12   -122    275       C  
ATOM   3421  OD1 ASN A 456      -0.914   2.144  11.519  1.00 42.36           O  
ANISOU 3421  OD1 ASN A 456     5155   5389   5550     10   -129    268       O  
ATOM   3422  ND2 ASN A 456      -1.831   1.982  13.585  1.00 46.60           N  
ANISOU 3422  ND2 ASN A 456     5662   5938   6105     15   -127    283       N  
ATOM   3423  N   THR A 457       1.468  -0.672  15.054  1.00 33.47           N  
ANISOU 3423  N   THR A 457     3973   4284   4459      6   -106    285       N  
ATOM   3424  CA  THR A 457       1.872  -2.011  14.675  1.00 33.43           C  
ANISOU 3424  CA  THR A 457     3961   4270   4467      5   -110    283       C  
ATOM   3425  C   THR A 457       0.789  -3.016  15.032  1.00 34.26           C  
ANISOU 3425  C   THR A 457     4053   4373   4588      6   -121    292       C  
ATOM   3426  O   THR A 457       0.378  -3.140  16.186  1.00 33.79           O  
ANISOU 3426  O   THR A 457     3981   4323   4535      5   -123    303       O  
ATOM   3427  CB  THR A 457       3.237  -2.394  15.296  1.00 33.22           C  
ANISOU 3427  CB  THR A 457     3927   4246   4447      1   -101    284       C  
ATOM   3428  OG1 THR A 457       4.221  -1.423  14.916  1.00 31.86           O  
ANISOU 3428  OG1 THR A 457     3767   4075   4261      0    -90    275       O  
ATOM   3429  CG2 THR A 457       3.681  -3.783  14.838  1.00 31.80           C  
ANISOU 3429  CG2 THR A 457     3740   4056   4286      0   -105    280       C  
ATOM   3430  N   LYS A 458       0.307  -3.707  14.014  1.00 36.09           N  
ANISOU 3430  N   LYS A 458     4290   4596   4827      7   -130    286       N  
ATOM   3431  CA  LYS A 458      -0.537  -4.854  14.224  1.00 39.01           C  
ANISOU 3431  CA  LYS A 458     4645   4961   5214      8   -141    293       C  
ATOM   3432  C   LYS A 458       0.415  -6.057  14.353  1.00 40.11           C  
ANISOU 3432  C   LYS A 458     4774   5095   5369      5   -140    292       C  
ATOM   3433  O   LYS A 458       1.022  -6.496  13.360  1.00 40.01           O  
ANISOU 3433  O   LYS A 458     4769   5073   5358      4   -138    280       O  
ATOM   3434  CB  LYS A 458      -1.562  -4.985  13.082  1.00 39.96           C  
ANISOU 3434  CB  LYS A 458     4776   5072   5334     10   -152    288       C  
ATOM   3435  CG  LYS A 458      -2.058  -6.396  12.812  1.00 43.65           C  
ANISOU 3435  CG  LYS A 458     5233   5530   5820     10   -163    289       C  
ATOM   3436  CD  LYS A 458      -3.161  -6.835  13.760  1.00 43.69           C  
ANISOU 3436  CD  LYS A 458     5221   5539   5839     12   -171    304       C  
ATOM   3437  CE  LYS A 458      -4.470  -6.942  13.000  1.00 46.16           C  
ANISOU 3437  CE  LYS A 458     5538   5844   6155     14   -185    303       C  
ATOM   3438  NZ  LYS A 458      -4.347  -7.850  11.819  1.00 47.55           N  
ANISOU 3438  NZ  LYS A 458     5721   6007   6336     13   -192    293       N  
ATOM   3439  N   ILE A 459       0.568  -6.538  15.594  1.00 39.17           N  
ANISOU 3439  N   ILE A 459     4638   4983   5261      3   -140    305       N  
ATOM   3440  CA  ILE A 459       1.463  -7.649  15.937  1.00 39.11           C  
ANISOU 3440  CA  ILE A 459     4617   4970   5272      0   -141    308       C  
ATOM   3441  C   ILE A 459       0.864  -8.986  15.528  1.00 39.29           C  
ANISOU 3441  C   ILE A 459     4630   4982   5314      1   -153    309       C  
ATOM   3442  O   ILE A 459      -0.038  -9.495  16.192  1.00 39.82           O  
ANISOU 3442  O   ILE A 459     4686   5052   5391      1   -162    321       O  
ATOM   3443  CB  ILE A 459       1.720  -7.719  17.460  1.00 39.08           C  
ANISOU 3443  CB  ILE A 459     4598   4976   5273     -3   -141    324       C  
ATOM   3444  CG1 ILE A 459       2.249  -6.385  18.003  1.00 39.14           C  
ANISOU 3444  CG1 ILE A 459     4614   4995   5260     -5   -130    324       C  
ATOM   3445  CG2 ILE A 459       2.627  -8.901  17.807  1.00 38.25           C  
ANISOU 3445  CG2 ILE A 459     4478   4864   5190     -7   -145    329       C  
ATOM   3446  CD1 ILE A 459       3.751  -6.288  18.104  1.00 39.97           C  
ANISOU 3446  CD1 ILE A 459     4719   5099   5367     -8   -122    320       C  
ATOM   3447  N   ASP A 460       1.365  -9.554  14.440  1.00 40.27           N  
ANISOU 3447  N   ASP A 460     4760   5094   5446      1   -152    295       N  
ATOM   3448  CA  ASP A 460       0.917 -10.874  14.004  1.00 41.94           C  
ANISOU 3448  CA  ASP A 460     4963   5294   5678      2   -162    294       C  
ATOM   3449  C   ASP A 460       2.089 -11.837  13.793  1.00 42.16           C  
ANISOU 3449  C   ASP A 460     4981   5311   5726      0   -159    286       C  
ATOM   3450  O   ASP A 460       2.056 -12.705  12.922  1.00 44.32           O  
ANISOU 3450  O   ASP A 460     5254   5572   6012      0   -163    275       O  
ATOM   3451  CB  ASP A 460      -0.030 -10.805  12.785  1.00 45.57           C  
ANISOU 3451  CB  ASP A 460     5437   5747   6129      4   -168    283       C  
ATOM   3452  CG  ASP A 460       0.511  -9.946  11.622  1.00 49.12           C  
ANISOU 3452  CG  ASP A 460     5909   6195   6559      3   -158    266       C  
ATOM   3453  OD1 ASP A 460      -0.008 -10.098  10.486  1.00 50.44           O  
ANISOU 3453  OD1 ASP A 460     6089   6354   6721      3   -164    255       O  
ATOM   3454  OD2 ASP A 460       1.425  -9.118  11.826  1.00 50.81           O  
ANISOU 3454  OD2 ASP A 460     6129   6414   6760      2   -146    263       O  
ATOM   3455  N   PHE A 461       3.119 -11.679  14.619  1.00 41.01           N  
ANISOU 3455  N   PHE A 461     4827   5169   5584     -2   -153    292       N  
ATOM   3456  CA  PHE A 461       4.269 -12.562  14.598  1.00 40.46           C  
ANISOU 3456  CA  PHE A 461     4745   5088   5538     -4   -151    287       C  
ATOM   3457  C   PHE A 461       4.832 -12.749  16.012  1.00 40.24           C  
ANISOU 3457  C   PHE A 461     4700   5066   5522     -8   -155    305       C  
ATOM   3458  O   PHE A 461       5.402 -11.827  16.592  1.00 41.44           O  
ANISOU 3458  O   PHE A 461     4856   5228   5660    -10   -147    309       O  
ATOM   3459  CB  PHE A 461       5.313 -12.017  13.620  1.00 40.60           C  
ANISOU 3459  CB  PHE A 461     4776   5101   5547     -5   -135    266       C  
ATOM   3460  CG  PHE A 461       6.600 -12.790  13.602  1.00 41.87           C  
ANISOU 3460  CG  PHE A 461     4924   5250   5734     -7   -130    259       C  
ATOM   3461  CD1 PHE A 461       7.828 -12.114  13.612  1.00 41.99           C  
ANISOU 3461  CD1 PHE A 461     4943   5267   5745     -9   -117    252       C  
ATOM   3462  CD2 PHE A 461       6.598 -14.184  13.570  1.00 41.64           C  
ANISOU 3462  CD2 PHE A 461     4877   5207   5735     -7   -139    260       C  
ATOM   3463  CE1 PHE A 461       9.025 -12.815  13.599  1.00 42.66           C  
ANISOU 3463  CE1 PHE A 461     5014   5339   5857    -11   -112    245       C  
ATOM   3464  CE2 PHE A 461       7.794 -14.888  13.562  1.00 43.57           C  
ANISOU 3464  CE2 PHE A 461     5107   5439   6007     -9   -135    253       C  
ATOM   3465  CZ  PHE A 461       9.008 -14.205  13.573  1.00 43.12           C  
ANISOU 3465  CZ  PHE A 461     5053   5382   5946    -11   -121    245       C  
ATOM   3466  N   ASP A 462       4.654 -13.950  16.558  1.00 40.57           N  
ANISOU 3466  N   ASP A 462     4722   5101   5589    -10   -167    317       N  
ATOM   3467  CA  ASP A 462       5.096 -14.285  17.918  1.00 41.64           C  
ANISOU 3467  CA  ASP A 462     4840   5240   5737    -16   -175    337       C  
ATOM   3468  C   ASP A 462       6.579 -14.018  18.164  1.00 40.94           C  
ANISOU 3468  C   ASP A 462     4749   5149   5656    -19   -167    334       C  
ATOM   3469  O   ASP A 462       6.980 -13.724  19.290  1.00 41.13           O  
ANISOU 3469  O   ASP A 462     4767   5182   5678    -24   -170    350       O  
ATOM   3470  CB  ASP A 462       4.794 -15.754  18.239  1.00 42.84           C  
ANISOU 3470  CB  ASP A 462     4973   5382   5921    -18   -190    348       C  
ATOM   3471  CG  ASP A 462       3.340 -15.998  18.645  1.00 44.71           C  
ANISOU 3471  CG  ASP A 462     5208   5627   6153    -18   -201    361       C  
ATOM   3472  OD1 ASP A 462       2.517 -15.046  18.655  1.00 43.42           O  
ANISOU 3472  OD1 ASP A 462     5058   5476   5963    -16   -196    361       O  
ATOM   3473  OD2 ASP A 462       3.023 -17.169  18.966  1.00 46.94           O  
ANISOU 3473  OD2 ASP A 462     5475   5901   6459    -21   -214    372       O  
ATOM   3474  N   GLY A 463       7.388 -14.117  17.111  1.00 39.61           N  
ANISOU 3474  N   GLY A 463     4584   4968   5495    -16   -157    313       N  
ATOM   3475  CA  GLY A 463       8.829 -13.933  17.233  1.00 38.63           C  
ANISOU 3475  CA  GLY A 463     4455   4839   5382    -18   -149    308       C  
ATOM   3476  C   GLY A 463       9.331 -12.525  16.961  1.00 38.72           C  
ANISOU 3476  C   GLY A 463     4485   4860   5366    -17   -133    298       C  
ATOM   3477  O   GLY A 463      10.491 -12.343  16.580  1.00 39.10           O  
ANISOU 3477  O   GLY A 463     4532   4900   5421    -18   -123    286       O  
ATOM   3478  N   ILE A 464       8.465 -11.529  17.154  1.00 36.91           N  
ANISOU 3478  N   ILE A 464     4271   4647   5106    -16   -132    303       N  
ATOM   3479  CA  ILE A 464       8.833 -10.132  16.918  1.00 35.50           C  
ANISOU 3479  CA  ILE A 464     4110   4477   4900    -15   -118    295       C  
ATOM   3480  C   ILE A 464       9.942  -9.636  17.857  1.00 35.12           C  
ANISOU 3480  C   ILE A 464     4055   4433   4853    -20   -115    304       C  
ATOM   3481  O   ILE A 464      10.728  -8.781  17.479  1.00 34.88           O  
ANISOU 3481  O   ILE A 464     4034   4404   4811    -19   -102    293       O  
ATOM   3482  CB  ILE A 464       7.609  -9.178  16.942  1.00 34.85           C  
ANISOU 3482  CB  ILE A 464     4043   4409   4788    -13   -118    299       C  
ATOM   3483  CG1 ILE A 464       8.012  -7.793  16.401  1.00 34.49           C  
ANISOU 3483  CG1 ILE A 464     4017   4369   4717    -11   -104    287       C  
ATOM   3484  CG2 ILE A 464       6.992  -9.103  18.337  1.00 34.25           C  
ANISOU 3484  CG2 ILE A 464     3958   4346   4709    -16   -128    321       C  
ATOM   3485  CD1 ILE A 464       6.909  -6.760  16.354  1.00 33.37           C  
ANISOU 3485  CD1 ILE A 464     3889   4239   4548     -9   -104    289       C  
ATOM   3486  N   PHE A 465      10.016 -10.178  19.067  1.00 35.61           N  
ANISOU 3486  N   PHE A 465     4102   4499   4930    -25   -128    323       N  
ATOM   3487  CA  PHE A 465      11.016  -9.716  20.035  1.00 34.75           C  
ANISOU 3487  CA  PHE A 465     3987   4394   4821    -30   -127    334       C  
ATOM   3488  C   PHE A 465      12.133 -10.736  20.267  1.00 35.40           C  
ANISOU 3488  C   PHE A 465     4049   4460   4939    -34   -134    337       C  
ATOM   3489  O   PHE A 465      12.898 -10.623  21.223  1.00 35.47           O  
ANISOU 3489  O   PHE A 465     4049   4471   4955    -40   -140    350       O  
ATOM   3490  CB  PHE A 465      10.360  -9.301  21.358  1.00 32.66           C  
ANISOU 3490  CB  PHE A 465     3722   4146   4540    -36   -136    354       C  
ATOM   3491  CG  PHE A 465       9.345  -8.198  21.221  1.00 32.26           C  
ANISOU 3491  CG  PHE A 465     3689   4110   4457    -33   -128    351       C  
ATOM   3492  CD1 PHE A 465       8.069  -8.331  21.778  1.00 32.34           C  
ANISOU 3492  CD1 PHE A 465     3699   4130   4459    -34   -135    362       C  
ATOM   3493  CD2 PHE A 465       9.651  -7.026  20.538  1.00 31.78           C  
ANISOU 3493  CD2 PHE A 465     3644   4052   4376    -29   -113    336       C  
ATOM   3494  CE1 PHE A 465       7.124  -7.317  21.659  1.00 31.43           C  
ANISOU 3494  CE1 PHE A 465     3597   4026   4318    -31   -128    358       C  
ATOM   3495  CE2 PHE A 465       8.706  -6.010  20.409  1.00 31.22           C  
ANISOU 3495  CE2 PHE A 465     3589   3993   4279    -25   -108    333       C  
ATOM   3496  CZ  PHE A 465       7.444  -6.156  20.970  1.00 31.43           C  
ANISOU 3496  CZ  PHE A 465     3613   4028   4299    -26   -115    344       C  
ATOM   3497  N   LEU A 466      12.228 -11.723  19.382  1.00 36.12           N  
ANISOU 3497  N   LEU A 466     4133   4536   5055    -31   -134    325       N  
ATOM   3498  CA  LEU A 466      13.290 -12.714  19.441  1.00 36.97           C  
ANISOU 3498  CA  LEU A 466     4220   4625   5201    -33   -140    324       C  
ATOM   3499  C   LEU A 466      14.627 -11.972  19.376  1.00 38.00           C  
ANISOU 3499  C   LEU A 466     4352   4752   5332    -34   -128    316       C  
ATOM   3500  O   LEU A 466      14.810 -11.095  18.536  1.00 40.99           O  
ANISOU 3500  O   LEU A 466     4747   5135   5691    -31   -110    298       O  
ATOM   3501  CB  LEU A 466      13.138 -13.696  18.271  1.00 38.48           C  
ANISOU 3501  CB  LEU A 466     4406   4799   5413    -28   -137    306       C  
ATOM   3502  CG  LEU A 466      13.450 -15.209  18.328  1.00 39.71           C  
ANISOU 3502  CG  LEU A 466     4537   4935   5613    -30   -149    309       C  
ATOM   3503  CD1 LEU A 466      13.647 -15.792  19.730  1.00 40.43           C  
ANISOU 3503  CD1 LEU A 466     4609   5026   5724    -37   -170    337       C  
ATOM   3504  CD2 LEU A 466      12.357 -15.977  17.590  1.00 37.71           C  
ANISOU 3504  CD2 LEU A 466     4286   4677   5362    -26   -153    302       C  
ATOM   3505  N   GLY A 467      15.545 -12.284  20.286  1.00 36.81           N  
ANISOU 3505  N   GLY A 467     4184   4596   5204    -40   -138    330       N  
ATOM   3506  CA  GLY A 467      16.839 -11.606  20.323  1.00 34.68           C  
ANISOU 3506  CA  GLY A 467     3914   4323   4938    -42   -128    323       C  
ATOM   3507  C   GLY A 467      17.009 -10.642  21.487  1.00 34.70           C  
ANISOU 3507  C   GLY A 467     3922   4341   4918    -48   -133    341       C  
ATOM   3508  O   GLY A 467      18.143 -10.312  21.866  1.00 35.72           O  
ANISOU 3508  O   GLY A 467     4046   4467   5059    -52   -133    343       O  
ATOM   3509  N   LEU A 468      15.895 -10.203  22.071  1.00 33.15           N  
ANISOU 3509  N   LEU A 468     3737   4163   4692    -50   -138    354       N  
ATOM   3510  CA  LEU A 468      15.921  -9.113  23.047  1.00 32.53           C  
ANISOU 3510  CA  LEU A 468     3670   4103   4587    -55   -139    366       C  
ATOM   3511  C   LEU A 468      16.101  -9.606  24.481  1.00 32.64           C  
ANISOU 3511  C   LEU A 468     3669   4120   4612    -67   -160    393       C  
ATOM   3512  O   LEU A 468      15.354  -9.240  25.400  1.00 32.26           O  
ANISOU 3512  O   LEU A 468     3628   4089   4541    -73   -166    408       O  
ATOM   3513  CB  LEU A 468      14.689  -8.203  22.889  1.00 32.54           C  
ANISOU 3513  CB  LEU A 468     3691   4122   4550    -51   -131    363       C  
ATOM   3514  CG  LEU A 468      14.584  -7.417  21.564  1.00 32.83           C  
ANISOU 3514  CG  LEU A 468     3745   4158   4569    -42   -111    339       C  
ATOM   3515  CD1 LEU A 468      13.236  -6.712  21.428  1.00 32.24           C  
ANISOU 3515  CD1 LEU A 468     3687   4099   4463    -39   -107    338       C  
ATOM   3516  CD2 LEU A 468      15.732  -6.429  21.379  1.00 31.54           C  
ANISOU 3516  CD2 LEU A 468     3589   3995   4400    -43    -98    329       C  
ATOM   3517  N   THR A 469      17.139 -10.411  24.670  1.00 32.59           N  
ANISOU 3517  N   THR A 469     3644   4096   4642    -70   -170    398       N  
ATOM   3518  CA  THR A 469      17.327 -11.130  25.915  1.00 32.61           C  
ANISOU 3518  CA  THR A 469     3631   4097   4661    -82   -193    425       C  
ATOM   3519  C   THR A 469      17.809 -10.273  27.090  1.00 33.05           C  
ANISOU 3519  C   THR A 469     3693   4166   4698    -93   -199    441       C  
ATOM   3520  O   THR A 469      17.717 -10.690  28.252  1.00 34.05           O  
ANISOU 3520  O   THR A 469     3812   4297   4827   -106   -218    465       O  
ATOM   3521  CB  THR A 469      18.223 -12.367  25.717  1.00 33.36           C  
ANISOU 3521  CB  THR A 469     3702   4167   4806    -83   -205    426       C  
ATOM   3522  OG1 THR A 469      19.447 -11.973  25.106  1.00 34.47           O  
ANISOU 3522  OG1 THR A 469     3838   4295   4961    -79   -192    409       O  
ATOM   3523  CG2 THR A 469      17.536 -13.401  24.811  1.00 33.42           C  
ANISOU 3523  CG2 THR A 469     3702   4162   4831    -75   -204    415       C  
ATOM   3524  N   SER A 470      18.277  -9.060  26.812  1.00 32.20           N  
ANISOU 3524  N   SER A 470     3598   4065   4569    -89   -183    428       N  
ATOM   3525  CA  SER A 470      18.674  -8.155  27.896  1.00 32.22           C  
ANISOU 3525  CA  SER A 470     3609   4082   4551   -100   -187    441       C  
ATOM   3526  C   SER A 470      17.655  -7.056  28.191  1.00 31.65           C  
ANISOU 3526  C   SER A 470     3557   4033   4433   -100   -176    439       C  
ATOM   3527  O   SER A 470      17.807  -6.314  29.162  1.00 32.72           O  
ANISOU 3527  O   SER A 470     3700   4182   4548   -109   -179    450       O  
ATOM   3528  CB  SER A 470      20.052  -7.541  27.619  1.00 32.70           C  
ANISOU 3528  CB  SER A 470     3668   4133   4623    -98   -179    431       C  
ATOM   3529  OG  SER A 470      21.008  -8.557  27.407  1.00 33.49           O  
ANISOU 3529  OG  SER A 470     3745   4209   4767    -98   -189    432       O  
ATOM   3530  N   LEU A 471      16.614  -6.960  27.370  1.00 31.16           N  
ANISOU 3530  N   LEU A 471     3505   3976   4358    -90   -164    426       N  
ATOM   3531  CA  LEU A 471      15.631  -5.873  27.488  1.00 30.94           C  
ANISOU 3531  CA  LEU A 471     3496   3967   4291    -88   -152    421       C  
ATOM   3532  C   LEU A 471      15.054  -5.715  28.894  1.00 30.43           C  
ANISOU 3532  C   LEU A 471     3434   3920   4207   -102   -162    442       C  
ATOM   3533  O   LEU A 471      14.677  -6.702  29.512  1.00 30.76           O  
ANISOU 3533  O   LEU A 471     3465   3960   4261   -110   -178    459       O  
ATOM   3534  CB  LEU A 471      14.507  -6.059  26.456  1.00 29.67           C  
ANISOU 3534  CB  LEU A 471     3341   3805   4124    -77   -143    408       C  
ATOM   3535  CG  LEU A 471      13.634  -4.843  26.128  1.00 29.02           C  
ANISOU 3535  CG  LEU A 471     3278   3738   4008    -71   -128    396       C  
ATOM   3536  CD1 LEU A 471      14.438  -3.722  25.478  1.00 28.11           C  
ANISOU 3536  CD1 LEU A 471     3175   3622   3884    -66   -113    380       C  
ATOM   3537  CD2 LEU A 471      12.466  -5.265  25.247  1.00 28.48           C  
ANISOU 3537  CD2 LEU A 471     3213   3667   3940    -62   -125    387       C  
ATOM   3538  N   ASN A 472      15.022  -4.480  29.391  1.00 30.80           N  
ANISOU 3538  N   ASN A 472     3495   3982   4224   -105   -154    440       N  
ATOM   3539  CA  ASN A 472      14.327  -4.149  30.642  1.00 32.41           C  
ANISOU 3539  CA  ASN A 472     3705   4204   4404   -118   -158    455       C  
ATOM   3540  C   ASN A 472      13.014  -3.434  30.390  1.00 32.96           C  
ANISOU 3540  C   ASN A 472     3787   4287   4447   -112   -143    444       C  
ATOM   3541  O   ASN A 472      11.990  -3.760  30.986  1.00 33.67           O  
ANISOU 3541  O   ASN A 472     3877   4387   4528   -118   -147    454       O  
ATOM   3542  CB  ASN A 472      15.152  -3.204  31.514  1.00 32.95           C  
ANISOU 3542  CB  ASN A 472     3780   4282   4456   -128   -158    460       C  
ATOM   3543  CG  ASN A 472      16.448  -3.807  31.981  1.00 34.40           C  
ANISOU 3543  CG  ASN A 472     3951   4454   4665   -137   -175    473       C  
ATOM   3544  OD1 ASN A 472      16.592  -5.029  32.080  1.00 35.80           O  
ANISOU 3544  OD1 ASN A 472     4113   4619   4868   -141   -191    486       O  
ATOM   3545  ND2 ASN A 472      17.409  -2.943  32.284  1.00 35.17           N  
ANISOU 3545  ND2 ASN A 472     4054   4552   4755   -141   -172    472       N  
ATOM   3546  N   THR A 473      13.072  -2.422  29.531  1.00 32.45           N  
ANISOU 3546  N   THR A 473     3734   4222   4371   -100   -127    425       N  
ATOM   3547  CA  THR A 473      11.967  -1.515  29.351  1.00 32.26           C  
ANISOU 3547  CA  THR A 473     3723   4210   4322    -95   -114    415       C  
ATOM   3548  C   THR A 473      11.404  -1.652  27.952  1.00 32.51           C  
ANISOU 3548  C   THR A 473     3758   4233   4362    -80   -107    399       C  
ATOM   3549  O   THR A 473      12.071  -1.367  26.955  1.00 33.00           O  
ANISOU 3549  O   THR A 473     3823   4284   4429    -71   -100    385       O  
ATOM   3550  CB  THR A 473      12.384  -0.064  29.637  1.00 31.91           C  
ANISOU 3550  CB  THR A 473     3692   4176   4256    -96   -102    407       C  
ATOM   3551  OG1 THR A 473      12.953   0.005  30.942  1.00 31.73           O  
ANISOU 3551  OG1 THR A 473     3667   4161   4226   -112   -111    422       O  
ATOM   3552  CG2 THR A 473      11.183   0.860  29.599  1.00 32.60           C  
ANISOU 3552  CG2 THR A 473     3789   4275   4320    -92    -90    397       C  
ATOM   3553  N   LEU A 474      10.161  -2.103  27.897  1.00 31.75           N  
ANISOU 3553  N   LEU A 474     3659   4139   4263    -78   -108    401       N  
ATOM   3554  CA  LEU A 474       9.452  -2.191  26.651  1.00 31.40           C  
ANISOU 3554  CA  LEU A 474     3618   4087   4223    -65   -103    387       C  
ATOM   3555  C   LEU A 474       8.168  -1.381  26.746  1.00 30.93           C  
ANISOU 3555  C   LEU A 474     3568   4039   4143    -63    -95    382       C  
ATOM   3556  O   LEU A 474       7.236  -1.749  27.464  1.00 31.62           O  
ANISOU 3556  O   LEU A 474     3650   4134   4227    -68    -99    392       O  
ATOM   3557  CB  LEU A 474       9.191  -3.651  26.299  1.00 31.54           C  
ANISOU 3557  CB  LEU A 474     3624   4094   4265    -64   -114    393       C  
ATOM   3558  CG  LEU A 474       8.414  -4.010  25.035  1.00 32.32           C  
ANISOU 3558  CG  LEU A 474     3724   4183   4370    -52   -112    381       C  
ATOM   3559  CD1 LEU A 474       8.878  -3.226  23.814  1.00 32.24           C  
ANISOU 3559  CD1 LEU A 474     3727   4167   4355    -43   -101    361       C  
ATOM   3560  CD2 LEU A 474       8.555  -5.505  24.809  1.00 33.18           C  
ANISOU 3560  CD2 LEU A 474     3819   4279   4507    -53   -125    387       C  
ATOM   3561  N   LYS A 475       8.155  -0.254  26.042  1.00 30.63           N  
ANISOU 3561  N   LYS A 475     3543   4002   4093    -55    -83    368       N  
ATOM   3562  CA  LYS A 475       6.953   0.554  25.847  1.00 29.48           C  
ANISOU 3562  CA  LYS A 475     3405   3862   3932    -50    -76    360       C  
ATOM   3563  C   LYS A 475       6.385   0.255  24.457  1.00 29.15           C  
ANISOU 3563  C   LYS A 475     3366   3808   3898    -38    -77    350       C  
ATOM   3564  O   LYS A 475       7.063   0.461  23.443  1.00 27.94           O  
ANISOU 3564  O   LYS A 475     3220   3646   3747    -32    -74    339       O  
ATOM   3565  CB  LYS A 475       7.291   2.036  25.966  1.00 28.72           C  
ANISOU 3565  CB  LYS A 475     3321   3773   3818    -49    -65    351       C  
ATOM   3566  CG  LYS A 475       7.911   2.415  27.287  1.00 28.57           C  
ANISOU 3566  CG  LYS A 475     3301   3766   3789    -61    -63    360       C  
ATOM   3567  CD  LYS A 475       8.316   3.874  27.313  1.00 28.85           C  
ANISOU 3567  CD  LYS A 475     3348   3806   3807    -59    -52    350       C  
ATOM   3568  CE  LYS A 475       9.116   4.138  28.580  1.00 30.13           C  
ANISOU 3568  CE  LYS A 475     3508   3978   3960    -72    -53    359       C  
ATOM   3569  NZ  LYS A 475       9.289   5.579  28.910  1.00 30.07           N  
ANISOU 3569  NZ  LYS A 475     3511   3978   3934    -73    -42    351       N  
ATOM   3570  N   MET A 476       5.159  -0.264  24.423  1.00 29.40           N  
ANISOU 3570  N   MET A 476     3393   3840   3935    -37    -81    353       N  
ATOM   3571  CA  MET A 476       4.471  -0.564  23.161  1.00 30.29           C  
ANISOU 3571  CA  MET A 476     3510   3943   4055    -27    -84    344       C  
ATOM   3572  C   MET A 476       2.976  -0.216  23.249  1.00 30.65           C  
ANISOU 3572  C   MET A 476     3556   3993   4096    -24    -84    344       C  
ATOM   3573  O   MET A 476       2.105  -0.918  22.710  1.00 30.71           O  
ANISOU 3573  O   MET A 476     3559   3993   4114    -20    -91    344       O  
ATOM   3574  CB  MET A 476       4.693  -2.019  22.742  1.00 30.82           C  
ANISOU 3574  CB  MET A 476     3567   3999   4143    -27    -94    348       C  
ATOM   3575  CG  MET A 476       4.244  -3.045  23.768  1.00 32.55           C  
ANISOU 3575  CG  MET A 476     3771   4223   4373    -34   -103    364       C  
ATOM   3576  SD  MET A 476       4.664  -4.740  23.320  1.00 34.99           S  
ANISOU 3576  SD  MET A 476     4067   4517   4710    -34   -116    369       S  
ATOM   3577  CE  MET A 476       3.668  -4.942  21.841  1.00 36.88           C  
ANISOU 3577  CE  MET A 476     4313   4745   4953    -23   -118    356       C  
ATOM   3578  N   ALA A 477       2.693   0.886  23.931  1.00 30.07           N  
ANISOU 3578  N   ALA A 477     3486   3930   4008    -27    -75    342       N  
ATOM   3579  CA  ALA A 477       1.339   1.390  24.035  1.00 30.57           C  
ANISOU 3579  CA  ALA A 477     3549   3996   4069    -24    -73    340       C  
ATOM   3580  C   ALA A 477       0.789   1.811  22.661  1.00 30.80           C  
ANISOU 3580  C   ALA A 477     3587   4014   4100    -13    -75    329       C  
ATOM   3581  O   ALA A 477       1.545   2.214  21.775  1.00 30.26           O  
ANISOU 3581  O   ALA A 477     3530   3940   4027     -9    -74    321       O  
ATOM   3582  CB  ALA A 477       1.291   2.546  25.019  1.00 29.37           C  
ANISOU 3582  CB  ALA A 477     3399   3857   3901    -29    -62    339       C  
ATOM   3583  N   GLY A 478      -0.525   1.685  22.484  1.00 30.15           N  
ANISOU 3583  N   GLY A 478     3500   3929   4024    -10    -79    329       N  
ATOM   3584  CA  GLY A 478      -1.190   2.247  21.317  1.00 30.31           C  
ANISOU 3584  CA  GLY A 478     3530   3940   4046     -1    -83    320       C  
ATOM   3585  C   GLY A 478      -0.937   1.543  19.995  1.00 31.09           C  
ANISOU 3585  C   GLY A 478     3635   4026   4151      2    -92    316       C  
ATOM   3586  O   GLY A 478      -0.869   2.187  18.939  1.00 32.70           O  
ANISOU 3586  O   GLY A 478     3852   4222   4349      6    -94    308       O  
ATOM   3587  N   ASN A 479      -0.804   0.224  20.056  1.00 29.73           N  
ANISOU 3587  N   ASN A 479     3454   3850   3990      0    -99    323       N  
ATOM   3588  CA  ASN A 479      -0.687  -0.608  18.875  1.00 29.48           C  
ANISOU 3588  CA  ASN A 479     3427   3807   3967      3   -107    318       C  
ATOM   3589  C   ASN A 479      -1.867  -1.591  18.888  1.00 29.86           C  
ANISOU 3589  C   ASN A 479     3463   3850   4030      4   -118    325       C  
ATOM   3590  O   ASN A 479      -2.981  -1.209  19.259  1.00 30.78           O  
ANISOU 3590  O   ASN A 479     3575   3970   4149      5   -119    328       O  
ATOM   3591  CB  ASN A 479       0.680  -1.327  18.842  1.00 29.48           C  
ANISOU 3591  CB  ASN A 479     3425   3804   3970      0   -106    318       C  
ATOM   3592  CG  ASN A 479       1.859  -0.365  18.694  1.00 29.77           C  
ANISOU 3592  CG  ASN A 479     3473   3844   3993      0    -95    311       C  
ATOM   3593  OD1 ASN A 479       2.011   0.294  17.667  1.00 31.33           O  
ANISOU 3593  OD1 ASN A 479     3685   4036   4182      2    -93    300       O  
ATOM   3594  ND2 ASN A 479       2.704  -0.294  19.714  1.00 28.86           N  
ANISOU 3594  ND2 ASN A 479     3352   3737   3876     -6    -90    317       N  
ATOM   3595  N   SER A 480      -1.633  -2.842  18.501  1.00 30.60           N  
ANISOU 3595  N   SER A 480     3552   3937   4137      3   -126    326       N  
ATOM   3596  CA  SER A 480      -2.686  -3.870  18.464  1.00 31.31           C  
ANISOU 3596  CA  SER A 480     3631   4022   4243      4   -137    333       C  
ATOM   3597  C   SER A 480      -2.125  -5.259  18.133  1.00 30.85           C  
ANISOU 3597  C   SER A 480     3566   3955   4198      3   -143    334       C  
ATOM   3598  O   SER A 480      -0.953  -5.400  17.791  1.00 30.21           O  
ANISOU 3598  O   SER A 480     3490   3871   4117      2   -139    328       O  
ATOM   3599  CB  SER A 480      -3.792  -3.488  17.464  1.00 31.48           C  
ANISOU 3599  CB  SER A 480     3660   4035   4264     10   -144    327       C  
ATOM   3600  OG  SER A 480      -3.248  -3.211  16.179  1.00 31.66           O  
ANISOU 3600  OG  SER A 480     3700   4049   4279     12   -145    315       O  
ATOM   3601  N   PHE A 481      -2.976  -6.274  18.238  1.00 31.71           N  
ANISOU 3601  N   PHE A 481     3663   4060   4323      3   -153    341       N  
ATOM   3602  CA  PHE A 481      -2.588  -7.668  18.044  1.00 32.83           C  
ANISOU 3602  CA  PHE A 481     3797   4194   4483      1   -161    344       C  
ATOM   3603  C   PHE A 481      -3.598  -8.370  17.169  1.00 33.70           C  
ANISOU 3603  C   PHE A 481     3906   4293   4605      5   -173    341       C  
ATOM   3604  O   PHE A 481      -4.787  -8.066  17.225  1.00 35.38           O  
ANISOU 3604  O   PHE A 481     4118   4507   4817      7   -177    344       O  
ATOM   3605  CB  PHE A 481      -2.525  -8.392  19.398  1.00 33.65           C  
ANISOU 3605  CB  PHE A 481     3883   4305   4597     -5   -163    360       C  
ATOM   3606  CG  PHE A 481      -1.299  -8.067  20.208  1.00 33.60           C  
ANISOU 3606  CG  PHE A 481     3875   4306   4583    -10   -155    364       C  
ATOM   3607  CD1 PHE A 481      -1.215  -6.877  20.926  1.00 32.79           C  
ANISOU 3607  CD1 PHE A 481     3778   4216   4463    -13   -145    365       C  
ATOM   3608  CD2 PHE A 481      -0.226  -8.953  20.251  1.00 32.89           C  
ANISOU 3608  CD2 PHE A 481     3779   4210   4507    -13   -158    366       C  
ATOM   3609  CE1 PHE A 481      -0.080  -6.574  21.669  1.00 33.07           C  
ANISOU 3609  CE1 PHE A 481     3814   4259   4492    -18   -139    369       C  
ATOM   3610  CE2 PHE A 481       0.906  -8.653  20.991  1.00 33.23           C  
ANISOU 3610  CE2 PHE A 481     3820   4259   4545    -19   -153    370       C  
ATOM   3611  CZ  PHE A 481       0.980  -7.463  21.700  1.00 33.01           C  
ANISOU 3611  CZ  PHE A 481     3799   4244   4497    -22   -143    372       C  
ATOM   3612  N   LYS A 482      -3.133  -9.318  16.367  1.00 35.60           N  
ANISOU 3612  N   LYS A 482     4147   4522   4856      6   -179    335       N  
ATOM   3613  CA  LYS A 482      -4.030 -10.204  15.624  1.00 37.70           C  
ANISOU 3613  CA  LYS A 482     4410   4776   5135      8   -191    333       C  
ATOM   3614  C   LYS A 482      -5.131 -10.756  16.545  1.00 38.68           C  
ANISOU 3614  C   LYS A 482     4518   4905   5274      7   -199    348       C  
ATOM   3615  O   LYS A 482      -4.849 -11.256  17.650  1.00 38.62           O  
ANISOU 3615  O   LYS A 482     4496   4903   5274      2   -198    361       O  
ATOM   3616  CB  LYS A 482      -3.216 -11.338  15.010  1.00 39.00           C  
ANISOU 3616  CB  LYS A 482     4573   4930   5315      7   -194    326       C  
ATOM   3617  CG  LYS A 482      -4.019 -12.400  14.290  1.00 42.74           C  
ANISOU 3617  CG  LYS A 482     5042   5390   5804      8   -208    324       C  
ATOM   3618  CD  LYS A 482      -3.113 -13.550  13.885  1.00 46.52           C  
ANISOU 3618  CD  LYS A 482     5515   5858   6301      7   -209    317       C  
ATOM   3619  CE  LYS A 482      -3.868 -14.872  13.858  1.00 51.10           C  
ANISOU 3619  CE  LYS A 482     6081   6429   6905      7   -223    323       C  
ATOM   3620  NZ  LYS A 482      -2.956 -16.010  14.185  1.00 53.27           N  
ANISOU 3620  NZ  LYS A 482     6340   6696   7202      4   -224    324       N  
ATOM   3621  N   ASP A 483      -6.381 -10.635  16.099  1.00 39.07           N  
ANISOU 3621  N   ASP A 483     4569   4950   5325     10   -207    348       N  
ATOM   3622  CA  ASP A 483      -7.562 -11.081  16.868  1.00 37.77           C  
ANISOU 3622  CA  ASP A 483     4389   4788   5173      9   -213    361       C  
ATOM   3623  C   ASP A 483      -7.613 -10.519  18.285  1.00 35.97           C  
ANISOU 3623  C   ASP A 483     4152   4576   4939      5   -203    373       C  
ATOM   3624  O   ASP A 483      -8.222 -11.107  19.174  1.00 35.94           O  
ANISOU 3624  O   ASP A 483     4132   4575   4945      0   -206    385       O  
ATOM   3625  CB  ASP A 483      -7.673 -12.613  16.890  1.00 39.53           C  
ANISOU 3625  CB  ASP A 483     4598   5002   5418      7   -225    368       C  
ATOM   3626  CG  ASP A 483      -7.775 -13.218  15.491  1.00 44.72           C  
ANISOU 3626  CG  ASP A 483     5263   5644   6083     11   -235    356       C  
ATOM   3627  OD1 ASP A 483      -8.380 -12.583  14.595  1.00 47.31           O  
ANISOU 3627  OD1 ASP A 483     5604   5967   6402     15   -239    347       O  
ATOM   3628  OD2 ASP A 483      -7.245 -14.334  15.282  1.00 46.63           O  
ANISOU 3628  OD2 ASP A 483     5499   5878   6340     10   -240    355       O  
ATOM   3629  N   ASN A 484      -6.975  -9.374  18.487  1.00 35.20           N  
ANISOU 3629  N   ASN A 484     4064   4486   4822      4   -191    367       N  
ATOM   3630  CA  ASN A 484      -6.949  -8.694  19.790  1.00 36.15           C  
ANISOU 3630  CA  ASN A 484     4179   4622   4933      0   -180    375       C  
ATOM   3631  C   ASN A 484      -6.636  -9.592  20.983  1.00 36.33           C  
ANISOU 3631  C   ASN A 484     4187   4652   4964     -9   -180    390       C  
ATOM   3632  O   ASN A 484      -7.053  -9.316  22.117  1.00 35.99           O  
ANISOU 3632  O   ASN A 484     4136   4620   4916    -15   -174    399       O  
ATOM   3633  CB  ASN A 484      -8.242  -7.904  20.055  1.00 35.75           C  
ANISOU 3633  CB  ASN A 484     4126   4575   4881      1   -177    376       C  
ATOM   3634  CG  ASN A 484      -8.593  -6.937  18.937  1.00 35.21           C  
ANISOU 3634  CG  ASN A 484     4072   4499   4806      9   -179    363       C  
ATOM   3635  OD1 ASN A 484      -9.739  -6.880  18.530  1.00 36.29           O  
ANISOU 3635  OD1 ASN A 484     4207   4629   4952     12   -186    363       O  
ATOM   3636  ND2 ASN A 484      -7.617  -6.180  18.439  1.00 34.33           N  
ANISOU 3636  ND2 ASN A 484     3976   4388   4679     10   -173    354       N  
ATOM   3637  N   THR A 485      -5.911 -10.673  20.714  1.00 36.18           N  
ANISOU 3637  N   THR A 485     4164   4625   4958    -10   -188    392       N  
ATOM   3638  CA  THR A 485      -5.365 -11.510  21.771  1.00 36.13           C  
ANISOU 3638  CA  THR A 485     4144   4623   4959    -19   -191    407       C  
ATOM   3639  C   THR A 485      -3.847 -11.273  21.958  1.00 36.28           C  
ANISOU 3639  C   THR A 485     4168   4644   4971    -22   -185    405       C  
ATOM   3640  O   THR A 485      -3.079 -11.284  20.996  1.00 37.59           O  
ANISOU 3640  O   THR A 485     4342   4801   5139    -17   -185    393       O  
ATOM   3641  CB  THR A 485      -5.743 -13.019  21.616  1.00 35.98           C  
ANISOU 3641  CB  THR A 485     4111   4592   4964    -20   -205    415       C  
ATOM   3642  OG1 THR A 485      -4.626 -13.842  21.980  1.00 36.34           O  
ANISOU 3642  OG1 THR A 485     4150   4636   5022    -26   -210    422       O  
ATOM   3643  CG2 THR A 485      -6.179 -13.378  20.203  1.00 33.76           C  
ANISOU 3643  CG2 THR A 485     3836   4297   4693    -11   -213    402       C  
ATOM   3644  N   LEU A 486      -3.447 -11.012  23.202  1.00 35.95           N  
ANISOU 3644  N   LEU A 486     4122   4615   4921    -31   -180    416       N  
ATOM   3645  CA  LEU A 486      -2.047 -10.857  23.588  1.00 34.72           C  
ANISOU 3645  CA  LEU A 486     3969   4462   4761    -36   -177    418       C  
ATOM   3646  C   LEU A 486      -1.318 -12.183  23.492  1.00 35.29           C  
ANISOU 3646  C   LEU A 486     4029   4522   4855    -39   -189    424       C  
ATOM   3647  O   LEU A 486      -1.427 -13.017  24.390  1.00 35.99           O  
ANISOU 3647  O   LEU A 486     4105   4613   4955    -48   -197    441       O  
ATOM   3648  CB  LEU A 486      -1.962 -10.326  25.016  1.00 34.46           C  
ANISOU 3648  CB  LEU A 486     3933   4445   4713    -48   -170    430       C  
ATOM   3649  CG  LEU A 486      -0.585 -10.042  25.619  1.00 36.10           C  
ANISOU 3649  CG  LEU A 486     4143   4658   4914    -54   -168    434       C  
ATOM   3650  CD1 LEU A 486       0.180  -8.995  24.820  1.00 36.50           C  
ANISOU 3650  CD1 LEU A 486     4209   4707   4953    -46   -158    417       C  
ATOM   3651  CD2 LEU A 486      -0.747  -9.594  27.063  1.00 35.92           C  
ANISOU 3651  CD2 LEU A 486     4119   4653   4875    -68   -163    447       C  
ATOM   3652  N   SER A 487      -0.572 -12.369  22.405  1.00 35.34           N  
ANISOU 3652  N   SER A 487     4041   4515   4870    -32   -189    410       N  
ATOM   3653  CA  SER A 487       0.087 -13.642  22.117  1.00 36.11           C  
ANISOU 3653  CA  SER A 487     4126   4598   4993    -32   -200    412       C  
ATOM   3654  C   SER A 487       1.442 -13.828  22.823  1.00 36.82           C  
ANISOU 3654  C   SER A 487     4210   4688   5091    -40   -201    420       C  
ATOM   3655  O   SER A 487       1.974 -12.891  23.408  1.00 36.32           O  
ANISOU 3655  O   SER A 487     4153   4635   5009    -43   -193    422       O  
ATOM   3656  CB  SER A 487       0.231 -13.820  20.607  1.00 37.17           C  
ANISOU 3656  CB  SER A 487     4269   4718   5135    -23   -198    392       C  
ATOM   3657  OG  SER A 487       0.873 -12.707  20.019  1.00 39.36           O  
ANISOU 3657  OG  SER A 487     4562   4998   5394    -19   -186    377       O  
ATOM   3658  N   ASN A 488       1.985 -15.047  22.764  1.00 39.07           N  
ANISOU 3658  N   ASN A 488     4481   4960   5403    -42   -212    425       N  
ATOM   3659  CA  ASN A 488       3.237 -15.415  23.454  1.00 40.79           C  
ANISOU 3659  CA  ASN A 488     4688   5173   5634    -49   -218    435       C  
ATOM   3660  C   ASN A 488       4.483 -14.810  22.767  1.00 39.90           C  
ANISOU 3660  C   ASN A 488     4583   5054   5520    -44   -207    418       C  
ATOM   3661  O   ASN A 488       5.244 -15.509  22.093  1.00 40.97           O  
ANISOU 3661  O   ASN A 488     4712   5174   5680    -41   -209    409       O  
ATOM   3662  CB  ASN A 488       3.319 -16.956  23.638  1.00 40.79           C  
ANISOU 3662  CB  ASN A 488     4668   5160   5669    -53   -235    447       C  
ATOM   3663  CG  ASN A 488       4.692 -17.443  24.124  1.00 43.26           C  
ANISOU 3663  CG  ASN A 488     4968   5463   6002    -60   -243    455       C  
ATOM   3664  OD1 ASN A 488       5.251 -16.935  25.104  1.00 43.75           O  
ANISOU 3664  OD1 ASN A 488     5032   5536   6055    -69   -243    467       O  
ATOM   3665  ND2 ASN A 488       5.235 -18.450  23.436  1.00 41.94           N  
ANISOU 3665  ND2 ASN A 488     4790   5276   5868    -56   -249    447       N  
ATOM   3666  N   VAL A 489       4.667 -13.501  22.934  1.00 38.55           N  
ANISOU 3666  N   VAL A 489     4427   4897   5322    -44   -194    413       N  
ATOM   3667  CA  VAL A 489       5.773 -12.781  22.300  1.00 38.35           C  
ANISOU 3667  CA  VAL A 489     4411   4867   5291    -40   -183    397       C  
ATOM   3668  C   VAL A 489       6.903 -12.478  23.264  1.00 39.03           C  
ANISOU 3668  C   VAL A 489     4493   4958   5378    -48   -183    407       C  
ATOM   3669  O   VAL A 489       7.947 -11.993  22.834  1.00 40.89           O  
ANISOU 3669  O   VAL A 489     4733   5189   5614    -46   -175    396       O  
ATOM   3670  CB  VAL A 489       5.333 -11.455  21.607  1.00 39.39           C  
ANISOU 3670  CB  VAL A 489     4563   5008   5394    -33   -168    381       C  
ATOM   3671  CG1 VAL A 489       4.359 -11.729  20.462  1.00 38.82           C  
ANISOU 3671  CG1 VAL A 489     4497   4929   5322    -25   -168    369       C  
ATOM   3672  CG2 VAL A 489       4.759 -10.450  22.604  1.00 37.03           C  
ANISOU 3672  CG2 VAL A 489     4270   4727   5069    -38   -164    391       C  
ATOM   3673  N   PHE A 490       6.691 -12.763  24.552  1.00 40.25           N  
ANISOU 3673  N   PHE A 490     4638   5121   5532    -59   -194    429       N  
ATOM   3674  CA  PHE A 490       7.643 -12.405  25.610  1.00 39.87           C  
ANISOU 3674  CA  PHE A 490     4588   5080   5481    -69   -197    442       C  
ATOM   3675  C   PHE A 490       8.375 -13.586  26.233  1.00 41.12           C  
ANISOU 3675  C   PHE A 490     4727   5227   5670    -78   -215    459       C  
ATOM   3676  O   PHE A 490       8.941 -13.450  27.323  1.00 41.73           O  
ANISOU 3676  O   PHE A 490     4800   5310   5744    -89   -223    476       O  
ATOM   3677  CB  PHE A 490       6.965 -11.643  26.752  1.00 38.53           C  
ANISOU 3677  CB  PHE A 490     4424   4930   5282    -78   -195    455       C  
ATOM   3678  CG  PHE A 490       6.081 -10.520  26.312  1.00 38.17           C  
ANISOU 3678  CG  PHE A 490     4396   4896   5209    -71   -180    442       C  
ATOM   3679  CD1 PHE A 490       6.620  -9.355  25.784  1.00 36.77           C  
ANISOU 3679  CD1 PHE A 490     4232   4722   5016    -64   -165    426       C  
ATOM   3680  CD2 PHE A 490       4.698 -10.617  26.464  1.00 36.83           C  
ANISOU 3680  CD2 PHE A 490     4227   4734   5031    -71   -180    446       C  
ATOM   3681  CE1 PHE A 490       5.790  -8.319  25.393  1.00 36.25           C  
ANISOU 3681  CE1 PHE A 490     4180   4664   4926    -58   -153    414       C  
ATOM   3682  CE2 PHE A 490       3.871  -9.583  26.080  1.00 36.10           C  
ANISOU 3682  CE2 PHE A 490     4147   4650   4917    -64   -167    434       C  
ATOM   3683  CZ  PHE A 490       4.417  -8.433  25.543  1.00 35.67           C  
ANISOU 3683  CZ  PHE A 490     4107   4598   4848    -58   -154    418       C  
ATOM   3684  N   ALA A 491       8.377 -14.730  25.555  1.00 42.29           N  
ANISOU 3684  N   ALA A 491     4862   5356   5847    -73   -223    455       N  
ATOM   3685  CA  ALA A 491       9.022 -15.939  26.088  1.00 45.52           C  
ANISOU 3685  CA  ALA A 491     5250   5752   6291    -81   -242    471       C  
ATOM   3686  C   ALA A 491      10.522 -15.755  26.395  1.00 48.29           C  
ANISOU 3686  C   ALA A 491     5596   6095   6656    -85   -244    473       C  
ATOM   3687  O   ALA A 491      11.013 -16.238  27.416  1.00 50.63           O  
ANISOU 3687  O   ALA A 491     5880   6390   6966    -97   -261    495       O  
ATOM   3688  CB  ALA A 491       8.803 -17.117  25.144  1.00 43.66           C  
ANISOU 3688  CB  ALA A 491     5003   5497   6087    -73   -247    462       C  
ATOM   3689  N   ASN A 492      11.234 -15.053  25.514  1.00 50.71           N  
ANISOU 3689  N   ASN A 492     5911   6397   6959    -76   -228    451       N  
ATOM   3690  CA  ASN A 492      12.674 -14.823  25.666  1.00 53.45           C  
ANISOU 3690  CA  ASN A 492     6252   6736   7321    -79   -228    450       C  
ATOM   3691  C   ASN A 492      13.080 -13.471  26.277  1.00 50.43           C  
ANISOU 3691  C   ASN A 492     5883   6369   6906    -83   -219    452       C  
ATOM   3692  O   ASN A 492      14.261 -13.263  26.557  1.00 53.11           O  
ANISOU 3692  O   ASN A 492     6217   6702   7257    -87   -221    454       O  
ATOM   3693  CB  ASN A 492      13.396 -15.014  24.316  1.00 59.91           C  
ANISOU 3693  CB  ASN A 492     7067   7535   8160    -68   -215    424       C  
ATOM   3694  CG  ASN A 492      13.761 -16.466  24.034  1.00 65.21           C  
ANISOU 3694  CG  ASN A 492     7715   8182   8877    -67   -228    425       C  
ATOM   3695  OD1 ASN A 492      13.012 -17.391  24.366  1.00 67.95           O  
ANISOU 3695  OD1 ASN A 492     8053   8527   9236    -70   -243    438       O  
ATOM   3696  ND2 ASN A 492      14.916 -16.671  23.402  1.00 66.71           N  
ANISOU 3696  ND2 ASN A 492     7896   8355   9095    -63   -222    409       N  
ATOM   3697  N   THR A 493      12.132 -12.551  26.470  1.00 46.53           N  
ANISOU 3697  N   THR A 493     5408   5896   6376    -83   -210    451       N  
ATOM   3698  CA  THR A 493      12.474 -11.237  27.042  1.00 44.77           C  
ANISOU 3698  CA  THR A 493     5198   5688   6123    -87   -201    452       C  
ATOM   3699  C   THR A 493      12.418 -11.316  28.553  1.00 42.20           C  
ANISOU 3699  C   THR A 493     4869   5374   5789   -103   -216    478       C  
ATOM   3700  O   THR A 493      11.531 -10.756  29.190  1.00 45.73           O  
ANISOU 3700  O   THR A 493     5326   5839   6207   -109   -212    485       O  
ATOM   3701  CB  THR A 493      11.586 -10.059  26.539  1.00 43.47           C  
ANISOU 3701  CB  THR A 493     5054   5538   5923    -79   -182    437       C  
ATOM   3702  OG1 THR A 493      10.235 -10.233  26.986  1.00 44.80           O  
ANISOU 3702  OG1 THR A 493     5225   5718   6077    -82   -186    446       O  
ATOM   3703  CG2 THR A 493      11.626  -9.930  25.032  1.00 40.96           C  
ANISOU 3703  CG2 THR A 493     4743   5210   5610    -65   -168    412       C  
ATOM   3704  N   THR A 494      13.406 -11.981  29.118  1.00 40.91           N  
ANISOU 3704  N   THR A 494     4691   5200   5652   -112   -232    493       N  
ATOM   3705  CA  THR A 494      13.360 -12.447  30.500  1.00 40.71           C  
ANISOU 3705  CA  THR A 494     4659   5181   5627   -130   -252    521       C  
ATOM   3706  C   THR A 494      13.725 -11.404  31.558  1.00 39.56           C  
ANISOU 3706  C   THR A 494     4525   5053   5452   -142   -251    531       C  
ATOM   3707  O   THR A 494      13.336 -11.522  32.711  1.00 40.62           O  
ANISOU 3707  O   THR A 494     4660   5200   5573   -158   -262    552       O  
ATOM   3708  CB  THR A 494      14.217 -13.730  30.608  1.00 41.40           C  
ANISOU 3708  CB  THR A 494     4724   5247   5759   -135   -273    533       C  
ATOM   3709  OG1 THR A 494      13.362 -14.863  30.420  1.00 40.18           O  
ANISOU 3709  OG1 THR A 494     4559   5086   5622   -133   -282    539       O  
ATOM   3710  CG2 THR A 494      14.968 -13.849  31.943  1.00 42.35           C  
ANISOU 3710  CG2 THR A 494     4837   5368   5883   -154   -294    560       C  
ATOM   3711  N   ASN A 495      14.442 -10.368  31.146  1.00 39.15           N  
ANISOU 3711  N   ASN A 495     4483   5002   5390   -136   -237    515       N  
ATOM   3712  CA  ASN A 495      14.957  -9.357  32.060  1.00 39.57           C  
ANISOU 3712  CA  ASN A 495     4546   5069   5419   -147   -236    522       C  
ATOM   3713  C   ASN A 495      14.082  -8.115  32.168  1.00 38.57           C  
ANISOU 3713  C   ASN A 495     4439   4963   5250   -145   -217    512       C  
ATOM   3714  O   ASN A 495      14.529  -7.063  32.637  1.00 40.13           O  
ANISOU 3714  O   ASN A 495     4648   5171   5427   -149   -210    510       O  
ATOM   3715  CB  ASN A 495      16.372  -8.959  31.626  1.00 41.59           C  
ANISOU 3715  CB  ASN A 495     4799   5312   5692   -142   -233    512       C  
ATOM   3716  CG  ASN A 495      17.371 -10.074  31.839  1.00 41.62           C  
ANISOU 3716  CG  ASN A 495     4781   5295   5738   -148   -254    526       C  
ATOM   3717  OD1 ASN A 495      17.743 -10.376  32.973  1.00 42.76           O  
ANISOU 3717  OD1 ASN A 495     4920   5441   5886   -164   -274    550       O  
ATOM   3718  ND2 ASN A 495      17.802 -10.699  30.750  1.00 40.98           N  
ANISOU 3718  ND2 ASN A 495     4687   5192   5688   -135   -250    511       N  
ATOM   3719  N   LEU A 496      12.833  -8.252  31.740  1.00 36.60           N  
ANISOU 3719  N   LEU A 496     4193   4719   4991   -138   -208    505       N  
ATOM   3720  CA  LEU A 496      11.903  -7.145  31.638  1.00 35.41           C  
ANISOU 3720  CA  LEU A 496     4059   4585   4807   -133   -190    493       C  
ATOM   3721  C   LEU A 496      11.484  -6.642  33.017  1.00 35.80           C  
ANISOU 3721  C   LEU A 496     4116   4655   4828   -150   -192    507       C  
ATOM   3722  O   LEU A 496      11.093  -7.419  33.876  1.00 36.47           O  
ANISOU 3722  O   LEU A 496     4196   4745   4916   -164   -205    527       O  
ATOM   3723  CB  LEU A 496      10.682  -7.617  30.849  1.00 35.40           C  
ANISOU 3723  CB  LEU A 496     4057   4582   4809   -122   -185    484       C  
ATOM   3724  CG  LEU A 496      10.150  -6.867  29.626  1.00 35.51           C  
ANISOU 3724  CG  LEU A 496     4082   4595   4813   -105   -166    460       C  
ATOM   3725  CD1 LEU A 496      11.259  -6.359  28.710  1.00 33.68           C  
ANISOU 3725  CD1 LEU A 496     3854   4352   4589    -95   -158    444       C  
ATOM   3726  CD2 LEU A 496       9.204  -7.795  28.872  1.00 35.55           C  
ANISOU 3726  CD2 LEU A 496     4081   4592   4833    -97   -169    457       C  
ATOM   3727  N   THR A 497      11.576  -5.338  33.231  1.00 36.63           N  
ANISOU 3727  N   THR A 497     4236   4772   4907   -150   -178    497       N  
ATOM   3728  CA  THR A 497      11.149  -4.744  34.496  1.00 36.58           C  
ANISOU 3728  CA  THR A 497     4239   4786   4872   -167   -176    507       C  
ATOM   3729  C   THR A 497       9.965  -3.776  34.322  1.00 37.50           C  
ANISOU 3729  C   THR A 497     4368   4917   4963   -160   -155    492       C  
ATOM   3730  O   THR A 497       9.247  -3.498  35.284  1.00 39.99           O  
ANISOU 3730  O   THR A 497     4688   5249   5257   -173   -151    498       O  
ATOM   3731  CB  THR A 497      12.317  -4.034  35.212  1.00 36.29           C  
ANISOU 3731  CB  THR A 497     4208   4754   4826   -177   -179    512       C  
ATOM   3732  OG1 THR A 497      12.902  -3.072  34.330  1.00 36.72           O  
ANISOU 3732  OG1 THR A 497     4269   4803   4878   -163   -165    492       O  
ATOM   3733  CG2 THR A 497      13.388  -5.035  35.629  1.00 35.61           C  
ANISOU 3733  CG2 THR A 497     4109   4655   4766   -188   -202    532       C  
ATOM   3734  N   PHE A 498       9.761  -3.281  33.097  1.00 36.22           N  
ANISOU 3734  N   PHE A 498     4210   4748   4804   -141   -142    472       N  
ATOM   3735  CA  PHE A 498       8.689  -2.320  32.789  1.00 34.85           C  
ANISOU 3735  CA  PHE A 498     4046   4583   4610   -133   -125    456       C  
ATOM   3736  C   PHE A 498       8.047  -2.720  31.474  1.00 33.64           C  
ANISOU 3736  C   PHE A 498     3890   4419   4473   -116   -122    444       C  
ATOM   3737  O   PHE A 498       8.736  -2.813  30.465  1.00 34.39           O  
ANISOU 3737  O   PHE A 498     3984   4500   4582   -105   -122    435       O  
ATOM   3738  CB  PHE A 498       9.281  -0.914  32.675  1.00 35.60           C  
ANISOU 3738  CB  PHE A 498     4154   4683   4689   -129   -112    442       C  
ATOM   3739  CG  PHE A 498       8.277   0.171  32.377  1.00 36.03           C  
ANISOU 3739  CG  PHE A 498     4218   4746   4725   -122    -94    426       C  
ATOM   3740  CD1 PHE A 498       7.923   1.091  33.361  1.00 36.16           C  
ANISOU 3740  CD1 PHE A 498     4243   4779   4718   -132    -85    425       C  
ATOM   3741  CD2 PHE A 498       7.721   0.308  31.103  1.00 35.77           C  
ANISOU 3741  CD2 PHE A 498     4187   4703   4699   -104    -88    411       C  
ATOM   3742  CE1 PHE A 498       7.016   2.105  33.097  1.00 35.04           C  
ANISOU 3742  CE1 PHE A 498     4108   4642   4562   -124    -69    410       C  
ATOM   3743  CE2 PHE A 498       6.814   1.317  30.835  1.00 35.02           C  
ANISOU 3743  CE2 PHE A 498     4099   4613   4590    -98    -74    398       C  
ATOM   3744  CZ  PHE A 498       6.463   2.219  31.835  1.00 35.13           C  
ANISOU 3744  CZ  PHE A 498     4119   4642   4583   -107    -64    397       C  
ATOM   3745  N   LEU A 499       6.739  -2.963  31.480  1.00 32.35           N  
ANISOU 3745  N   LEU A 499     3725   4260   4306   -115   -119    444       N  
ATOM   3746  CA  LEU A 499       6.038  -3.375  30.258  1.00 32.52           C  
ANISOU 3746  CA  LEU A 499     3744   4270   4341   -100   -117    434       C  
ATOM   3747  C   LEU A 499       4.731  -2.607  30.036  1.00 32.45           C  
ANISOU 3747  C   LEU A 499     3741   4268   4319    -93   -105    422       C  
ATOM   3748  O   LEU A 499       3.761  -2.783  30.780  1.00 31.02           O  
ANISOU 3748  O   LEU A 499     3557   4097   4131   -101   -104    430       O  
ATOM   3749  CB  LEU A 499       5.793  -4.893  30.253  1.00 32.23           C  
ANISOU 3749  CB  LEU A 499     3692   4224   4327   -102   -133    447       C  
ATOM   3750  CG  LEU A 499       5.016  -5.530  29.098  1.00 31.30           C  
ANISOU 3750  CG  LEU A 499     3571   4095   4226    -89   -134    439       C  
ATOM   3751  CD1 LEU A 499       5.628  -5.161  27.758  1.00 31.56           C  
ANISOU 3751  CD1 LEU A 499     3610   4115   4264    -75   -129    421       C  
ATOM   3752  CD2 LEU A 499       4.982  -7.037  29.266  1.00 31.11           C  
ANISOU 3752  CD2 LEU A 499     3533   4063   4225    -94   -151    453       C  
ATOM   3753  N   ASP A 500       4.721  -1.759  29.006  1.00 33.04           N  
ANISOU 3753  N   ASP A 500     3825   4338   4390    -80    -96    405       N  
ATOM   3754  CA  ASP A 500       3.562  -0.921  28.705  1.00 33.21           C  
ANISOU 3754  CA  ASP A 500     3852   4363   4401    -73    -85    394       C  
ATOM   3755  C   ASP A 500       2.790  -1.428  27.495  1.00 34.39           C  
ANISOU 3755  C   ASP A 500     4000   4500   4565    -61    -89    387       C  
ATOM   3756  O   ASP A 500       3.268  -1.366  26.354  1.00 36.35           O  
ANISOU 3756  O   ASP A 500     4254   4738   4820    -51    -90    377       O  
ATOM   3757  CB  ASP A 500       3.951   0.539  28.502  1.00 33.01           C  
ANISOU 3757  CB  ASP A 500     3839   4341   4359    -69    -73    380       C  
ATOM   3758  CG  ASP A 500       2.751   1.475  28.557  1.00 34.61           C  
ANISOU 3758  CG  ASP A 500     4046   4550   4552    -65    -62    371       C  
ATOM   3759  OD1 ASP A 500       1.589   1.007  28.518  1.00 34.63           O  
ANISOU 3759  OD1 ASP A 500     4042   4552   4561    -64    -63    373       O  
ATOM   3760  OD2 ASP A 500       2.966   2.695  28.652  1.00 36.99           O  
ANISOU 3760  OD2 ASP A 500     4356   4856   4840    -64    -52    362       O  
ATOM   3761  N   LEU A 501       1.579  -1.904  27.771  1.00 32.79           N  
ANISOU 3761  N   LEU A 501     3790   4300   4366    -62    -91    392       N  
ATOM   3762  CA  LEU A 501       0.701  -2.466  26.776  1.00 31.36           C  
ANISOU 3762  CA  LEU A 501     3605   4108   4199    -52    -96    388       C  
ATOM   3763  C   LEU A 501      -0.661  -1.775  26.811  1.00 30.96           C  
ANISOU 3763  C   LEU A 501     3555   4062   4143    -49    -89    381       C  
ATOM   3764  O   LEU A 501      -1.670  -2.355  26.413  1.00 30.66           O  
ANISOU 3764  O   LEU A 501     3512   4019   4117    -45    -94    382       O  
ATOM   3765  CB  LEU A 501       0.537  -3.957  27.040  1.00 30.96           C  
ANISOU 3765  CB  LEU A 501     3542   4054   4166    -58   -109    402       C  
ATOM   3766  CG  LEU A 501       1.588  -4.892  26.470  1.00 31.57           C  
ANISOU 3766  CG  LEU A 501     3616   4119   4259    -56   -120    404       C  
ATOM   3767  CD1 LEU A 501       1.576  -6.198  27.257  1.00 32.38           C  
ANISOU 3767  CD1 LEU A 501     3704   4221   4375    -66   -132    422       C  
ATOM   3768  CD2 LEU A 501       1.324  -5.142  24.992  1.00 31.58           C  
ANISOU 3768  CD2 LEU A 501     3621   4105   4271    -43   -122    391       C  
ATOM   3769  N   SER A 502      -0.686  -0.536  27.294  1.00 30.64           N  
ANISOU 3769  N   SER A 502     3522   4031   4087    -51    -77    375       N  
ATOM   3770  CA  SER A 502      -1.919   0.248  27.340  1.00 30.75           C  
ANISOU 3770  CA  SER A 502     3536   4048   4098    -48    -68    367       C  
ATOM   3771  C   SER A 502      -2.359   0.692  25.943  1.00 31.30           C  
ANISOU 3771  C   SER A 502     3612   4104   4174    -33    -71    355       C  
ATOM   3772  O   SER A 502      -1.525   0.901  25.057  1.00 30.91           O  
ANISOU 3772  O   SER A 502     3573   4048   4124    -27    -74    349       O  
ATOM   3773  CB  SER A 502      -1.746   1.459  28.242  1.00 30.15           C  
ANISOU 3773  CB  SER A 502     3465   3985   4004    -54    -54    362       C  
ATOM   3774  OG  SER A 502      -0.773   2.336  27.710  1.00 30.23           O  
ANISOU 3774  OG  SER A 502     3487   3992   4007    -49    -51    353       O  
ATOM   3775  N   LYS A 503      -3.672   0.836  25.766  1.00 30.80           N  
ANISOU 3775  N   LYS A 503     3544   4038   4119    -29    -71    352       N  
ATOM   3776  CA  LYS A 503      -4.266   1.277  24.505  1.00 31.17           C  
ANISOU 3776  CA  LYS A 503     3596   4072   4172    -17    -76    342       C  
ATOM   3777  C   LYS A 503      -3.979   0.361  23.316  1.00 31.49           C  
ANISOU 3777  C   LYS A 503     3640   4100   4223    -11    -89    343       C  
ATOM   3778  O   LYS A 503      -3.799   0.839  22.190  1.00 31.51           O  
ANISOU 3778  O   LYS A 503     3654   4093   4224     -3    -93    334       O  
ATOM   3779  CB  LYS A 503      -3.857   2.713  24.192  1.00 31.68           C  
ANISOU 3779  CB  LYS A 503     3673   4136   4225    -13    -68    331       C  
ATOM   3780  CG  LYS A 503      -4.679   3.726  24.958  1.00 34.45           C  
ANISOU 3780  CG  LYS A 503     4020   4495   4574    -15    -56    325       C  
ATOM   3781  CD  LYS A 503      -4.057   5.109  24.968  1.00 34.59           C  
ANISOU 3781  CD  LYS A 503     4047   4514   4578    -13    -47    316       C  
ATOM   3782  CE  LYS A 503      -4.815   5.987  25.941  1.00 35.99           C  
ANISOU 3782  CE  LYS A 503     4219   4701   4755    -17    -33    310       C  
ATOM   3783  NZ  LYS A 503      -3.980   7.124  26.411  1.00 40.44           N  
ANISOU 3783  NZ  LYS A 503     4791   5272   5303    -20    -22    303       N  
ATOM   3784  N   CYS A 504      -3.962  -0.948  23.560  1.00 31.45           N  
ANISOU 3784  N   CYS A 504     3626   4094   4229    -15    -97    353       N  
ATOM   3785  CA  CYS A 504      -3.643  -1.918  22.513  1.00 31.95           C  
ANISOU 3785  CA  CYS A 504     3690   4144   4302    -10   -109    353       C  
ATOM   3786  C   CYS A 504      -4.824  -2.712  22.001  1.00 32.65           C  
ANISOU 3786  C   CYS A 504     3773   4225   4407     -6   -120    355       C  
ATOM   3787  O   CYS A 504      -4.622  -3.784  21.411  1.00 33.21           O  
ANISOU 3787  O   CYS A 504     3841   4287   4489     -5   -130    357       O  
ATOM   3788  CB  CYS A 504      -2.557  -2.886  22.992  1.00 32.67           C  
ANISOU 3788  CB  CYS A 504     3778   4239   4397    -17   -112    361       C  
ATOM   3789  SG  CYS A 504      -0.926  -2.138  22.985  1.00 32.80           S  
ANISOU 3789  SG  CYS A 504     3804   4257   4398    -19   -104    356       S  
ATOM   3790  N   GLN A 505      -6.043  -2.202  22.230  1.00 33.62           N  
ANISOU 3790  N   GLN A 505     3890   4349   4533     -5   -117    354       N  
ATOM   3791  CA  GLN A 505      -7.295  -2.848  21.795  1.00 33.24           C  
ANISOU 3791  CA  GLN A 505     3834   4293   4502     -1   -127    357       C  
ATOM   3792  C   GLN A 505      -7.397  -4.329  22.191  1.00 35.61           C  
ANISOU 3792  C   GLN A 505     4122   4592   4815     -6   -135    368       C  
ATOM   3793  O   GLN A 505      -8.093  -5.113  21.521  1.00 36.92           O  
ANISOU 3793  O   GLN A 505     4283   4747   4996     -2   -147    370       O  
ATOM   3794  CB  GLN A 505      -7.463  -2.750  20.276  1.00 31.04           C  
ANISOU 3794  CB  GLN A 505     3567   3999   4227      7   -138    348       C  
ATOM   3795  CG  GLN A 505      -7.407  -1.352  19.702  1.00 31.26           C  
ANISOU 3795  CG  GLN A 505     3608   4024   4244     12   -134    337       C  
ATOM   3796  CD  GLN A 505      -7.453  -1.362  18.183  1.00 31.15           C  
ANISOU 3796  CD  GLN A 505     3607   3996   4231     18   -147    330       C  
ATOM   3797  OE1 GLN A 505      -8.233  -2.099  17.573  1.00 30.44           O  
ANISOU 3797  OE1 GLN A 505     3514   3896   4154     20   -159    332       O  
ATOM   3798  NE2 GLN A 505      -6.609  -0.548  17.565  1.00 30.64           N  
ANISOU 3798  NE2 GLN A 505     3559   3930   4152     19   -143    322       N  
ATOM   3799  N   LEU A 506      -6.702  -4.717  23.260  1.00 36.26           N  
ANISOU 3799  N   LEU A 506     4198   4685   4892    -15   -130    377       N  
ATOM   3800  CA  LEU A 506      -6.646  -6.123  23.670  1.00 37.05           C  
ANISOU 3800  CA  LEU A 506     4287   4784   5005    -21   -139    390       C  
ATOM   3801  C   LEU A 506      -7.962  -6.611  24.262  1.00 38.86           C  
ANISOU 3801  C   LEU A 506     4502   5016   5246    -25   -140    398       C  
ATOM   3802  O   LEU A 506      -8.548  -5.943  25.116  1.00 39.61           O  
ANISOU 3802  O   LEU A 506     4593   5121   5334    -30   -129    399       O  
ATOM   3803  CB  LEU A 506      -5.529  -6.333  24.687  1.00 35.62           C  
ANISOU 3803  CB  LEU A 506     4103   4613   4815    -32   -135    399       C  
ATOM   3804  CG  LEU A 506      -4.096  -6.276  24.186  1.00 33.79           C  
ANISOU 3804  CG  LEU A 506     3881   4378   4579    -29   -136    394       C  
ATOM   3805  CD1 LEU A 506      -3.173  -6.335  25.390  1.00 35.17           C  
ANISOU 3805  CD1 LEU A 506     4052   4563   4745    -41   -132    405       C  
ATOM   3806  CD2 LEU A 506      -3.817  -7.426  23.238  1.00 33.65           C  
ANISOU 3806  CD2 LEU A 506     3861   4345   4579    -25   -149    394       C  
ATOM   3807  N   GLU A 507      -8.415  -7.777  23.812  1.00 41.39           N  
ANISOU 3807  N   GLU A 507     4814   5327   5584    -23   -153    404       N  
ATOM   3808  CA  GLU A 507      -9.620  -8.404  24.362  1.00 45.99           C  
ANISOU 3808  CA  GLU A 507     5382   5911   6180    -27   -156    413       C  
ATOM   3809  C   GLU A 507      -9.334  -9.675  25.167  1.00 50.74           C  
ANISOU 3809  C   GLU A 507     5972   6515   6789    -38   -162    430       C  
ATOM   3810  O   GLU A 507     -10.036  -9.963  26.140  1.00 52.25           O  
ANISOU 3810  O   GLU A 507     6152   6715   6983    -47   -158    440       O  
ATOM   3811  CB  GLU A 507     -10.598  -8.737  23.250  1.00 46.41           C  
ANISOU 3811  CB  GLU A 507     5434   5949   6250    -17   -167    408       C  
ATOM   3812  CG  GLU A 507     -11.359  -7.540  22.721  1.00 49.07           C  
ANISOU 3812  CG  GLU A 507     5776   6282   6583     -9   -163    396       C  
ATOM   3813  CD  GLU A 507     -12.019  -7.830  21.392  1.00 52.04           C  
ANISOU 3813  CD  GLU A 507     6156   6642   6973      0   -178    390       C  
ATOM   3814  OE1 GLU A 507     -12.602  -8.927  21.231  1.00 52.68           O  
ANISOU 3814  OE1 GLU A 507     6227   6716   7071      0   -189    397       O  
ATOM   3815  OE2 GLU A 507     -11.946  -6.958  20.503  1.00 56.23           O  
ANISOU 3815  OE2 GLU A 507     6700   7167   7497      6   -179    379       O  
ATOM   3816  N   GLN A 508      -8.309 -10.423  24.753  1.00 51.57           N  
ANISOU 3816  N   GLN A 508     6079   6614   6900    -37   -172    432       N  
ATOM   3817  CA  GLN A 508      -7.972 -11.716  25.352  1.00 51.93           C  
ANISOU 3817  CA  GLN A 508     6112   6658   6957    -46   -182    448       C  
ATOM   3818  C   GLN A 508      -6.475 -11.864  25.610  1.00 48.66           C  
ANISOU 3818  C   GLN A 508     5703   6246   6539    -50   -183    451       C  
ATOM   3819  O   GLN A 508      -5.656 -11.385  24.836  1.00 47.39           O  
ANISOU 3819  O   GLN A 508     5553   6080   6373    -43   -181    439       O  
ATOM   3820  CB  GLN A 508      -8.406 -12.858  24.431  1.00 56.15           C  
ANISOU 3820  CB  GLN A 508     6640   7177   7515    -39   -197    448       C  
ATOM   3821  CG  GLN A 508      -9.903 -13.000  24.227  1.00 60.29           C  
ANISOU 3821  CG  GLN A 508     7158   7698   8050    -36   -200    448       C  
ATOM   3822  CD  GLN A 508     -10.278 -14.311  23.552  1.00 66.32           C  
ANISOU 3822  CD  GLN A 508     7913   8447   8837    -32   -217    452       C  
ATOM   3823  OE1 GLN A 508      -9.421 -15.157  23.258  1.00 64.95           O  
ANISOU 3823  OE1 GLN A 508     7738   8266   8674    -32   -226    454       O  
ATOM   3824  NE2 GLN A 508     -11.573 -14.489  23.306  1.00 70.52           N  
ANISOU 3824  NE2 GLN A 508     8438   8974   9380    -29   -221    452       N  
ATOM   3825  N   ILE A 509      -6.129 -12.569  26.682  1.00 45.68           N  
ANISOU 3825  N   ILE A 509     5315   5875   6164    -64   -187    468       N  
ATOM   3826  CA  ILE A 509      -4.738 -12.836  27.019  1.00 43.53           C  
ANISOU 3826  CA  ILE A 509     5044   5602   5891    -69   -191    474       C  
ATOM   3827  C   ILE A 509      -4.426 -14.329  26.925  1.00 42.51           C  
ANISOU 3827  C   ILE A 509     4902   5461   5787    -72   -209    485       C  
ATOM   3828  O   ILE A 509      -5.027 -15.126  27.636  1.00 44.36           O  
ANISOU 3828  O   ILE A 509     5125   5698   6030    -81   -216    501       O  
ATOM   3829  CB  ILE A 509      -4.420 -12.312  28.434  1.00 41.91           C  
ANISOU 3829  CB  ILE A 509     4841   5416   5667    -85   -183    485       C  
ATOM   3830  CG1 ILE A 509      -4.656 -10.802  28.484  1.00 39.01           C  
ANISOU 3830  CG1 ILE A 509     4486   5059   5277    -81   -166    472       C  
ATOM   3831  CG2 ILE A 509      -2.995 -12.680  28.838  1.00 42.50           C  
ANISOU 3831  CG2 ILE A 509     4914   5488   5744    -92   -191    494       C  
ATOM   3832  CD1 ILE A 509      -4.450 -10.175  29.839  1.00 40.13           C  
ANISOU 3832  CD1 ILE A 509     4630   5219   5398    -96   -156    480       C  
ATOM   3833  N   SER A 510      -3.486 -14.705  26.060  1.00 41.99           N  
ANISOU 3833  N   SER A 510     4837   5381   5733    -65   -215    477       N  
ATOM   3834  CA  SER A 510      -3.096 -16.120  25.919  1.00 43.12           C  
ANISOU 3834  CA  SER A 510     4967   5510   5904    -67   -231    486       C  
ATOM   3835  C   SER A 510      -2.438 -16.710  27.170  1.00 45.52           C  
ANISOU 3835  C   SER A 510     5261   5820   6213    -82   -240    508       C  
ATOM   3836  O   SER A 510      -1.984 -15.977  28.052  1.00 47.19           O  
ANISOU 3836  O   SER A 510     5479   6045   6406    -91   -233    514       O  
ATOM   3837  CB  SER A 510      -2.235 -16.346  24.685  1.00 41.68           C  
ANISOU 3837  CB  SER A 510     4789   5312   5735    -56   -233    470       C  
ATOM   3838  OG  SER A 510      -3.072 -16.622  23.580  1.00 41.39           O  
ANISOU 3838  OG  SER A 510     4754   5265   5706    -45   -235    457       O  
ATOM   3839  N   TRP A 511      -2.378 -18.035  27.230  1.00 48.68           N  
ANISOU 3839  N   TRP A 511     5646   6208   6639    -86   -256    520       N  
ATOM   3840  CA  TRP A 511      -2.286 -18.712  28.514  1.00 52.86           C  
ANISOU 3840  CA  TRP A 511     6165   6744   7174   -103   -267    545       C  
ATOM   3841  C   TRP A 511      -1.014 -18.578  29.306  1.00 53.08           C  
ANISOU 3841  C   TRP A 511     6193   6775   7198   -114   -271    556       C  
ATOM   3842  O   TRP A 511      -1.071 -18.256  30.504  1.00 54.19           O  
ANISOU 3842  O   TRP A 511     6336   6931   7322   -129   -270    571       O  
ATOM   3843  CB  TRP A 511      -2.728 -20.175  28.432  1.00 57.08           C  
ANISOU 3843  CB  TRP A 511     6683   7265   7738   -105   -285    557       C  
ATOM   3844  CG  TRP A 511      -3.077 -20.696  29.806  1.00 62.67           C  
ANISOU 3844  CG  TRP A 511     7382   7983   8445   -124   -294    584       C  
ATOM   3845  CD1 TRP A 511      -4.136 -20.289  30.630  1.00 63.42           C  
ANISOU 3845  CD1 TRP A 511     7480   8096   8519   -134   -285    593       C  
ATOM   3846  CD2 TRP A 511      -2.347 -21.697  30.590  1.00 65.45           C  
ANISOU 3846  CD2 TRP A 511     7722   8330   8816   -138   -313    607       C  
ATOM   3847  NE1 TRP A 511      -4.116 -20.963  31.825  1.00 68.16           N  
ANISOU 3847  NE1 TRP A 511     8072   8703   9121   -154   -296    619       N  
ATOM   3848  CE2 TRP A 511      -3.070 -21.828  31.868  1.00 70.23           C  
ANISOU 3848  CE2 TRP A 511     8325   8952   9407   -157   -315    629       C  
ATOM   3849  CE3 TRP A 511      -1.218 -22.476  30.370  1.00 71.79           C  
ANISOU 3849  CE3 TRP A 511     8514   9115   9645   -138   -328    611       C  
ATOM   3850  CZ2 TRP A 511      -2.658 -22.713  32.863  1.00 73.64           C  
ANISOU 3850  CZ2 TRP A 511     8745   9382   9850   -176   -333    656       C  
ATOM   3851  CZ3 TRP A 511      -0.810 -23.366  31.383  1.00 80.88           C  
ANISOU 3851  CZ3 TRP A 511     9653  10264  10811   -155   -347    638       C  
ATOM   3852  CH2 TRP A 511      -1.515 -23.480  32.598  1.00 77.04           C  
ANISOU 3852  CH2 TRP A 511     9166   9793  10309   -174   -351    661       C  
ATOM   3853  N   GLY A 512       0.135 -18.819  28.682  1.00 48.17           N  
ANISOU 3853  N   GLY A 512     5569   6139   6594   -107   -276    548       N  
ATOM   3854  CA  GLY A 512       1.393 -18.763  29.432  1.00 47.34           C  
ANISOU 3854  CA  GLY A 512     5461   6034   6490   -118   -282    559       C  
ATOM   3855  C   GLY A 512       2.190 -17.505  29.181  1.00 46.18           C  
ANISOU 3855  C   GLY A 512     5329   5894   6323   -113   -267    543       C  
ATOM   3856  O   GLY A 512       3.399 -17.475  29.398  1.00 48.59           O  
ANISOU 3856  O   GLY A 512     5632   6193   6635   -116   -272    546       O  
ATOM   3857  N   VAL A 513       1.492 -16.457  28.756  1.00 44.23           N  
ANISOU 3857  N   VAL A 513     5095   5656   6051   -104   -250    527       N  
ATOM   3858  CA  VAL A 513       2.098 -15.268  28.167  1.00 41.23           C  
ANISOU 3858  CA  VAL A 513     4731   5279   5655    -95   -234    508       C  
ATOM   3859  C   VAL A 513       3.086 -14.489  29.063  1.00 40.59           C  
ANISOU 3859  C   VAL A 513     4655   5208   5557   -105   -231    515       C  
ATOM   3860  O   VAL A 513       4.029 -13.893  28.546  1.00 39.29           O  
ANISOU 3860  O   VAL A 513     4498   5040   5391    -99   -224    502       O  
ATOM   3861  CB  VAL A 513       1.004 -14.359  27.560  1.00 40.41           C  
ANISOU 3861  CB  VAL A 513     4639   5183   5531    -85   -219    492       C  
ATOM   3862  CG1 VAL A 513       0.456 -13.389  28.588  1.00 39.70           C  
ANISOU 3862  CG1 VAL A 513     4557   5114   5412    -94   -209    498       C  
ATOM   3863  CG2 VAL A 513       1.538 -13.612  26.354  1.00 40.62           C  
ANISOU 3863  CG2 VAL A 513     4678   5203   5553    -71   -208    469       C  
ATOM   3864  N   PHE A 514       2.883 -14.502  30.384  1.00 41.18           N  
ANISOU 3864  N   PHE A 514     4728   5297   5620   -122   -236    535       N  
ATOM   3865  CA  PHE A 514       3.764 -13.782  31.327  1.00 40.02           C  
ANISOU 3865  CA  PHE A 514     4588   5161   5455   -134   -234    543       C  
ATOM   3866  C   PHE A 514       4.660 -14.666  32.210  1.00 40.47           C  
ANISOU 3866  C   PHE A 514     4634   5213   5530   -150   -254    566       C  
ATOM   3867  O   PHE A 514       5.461 -14.143  32.992  1.00 39.56           O  
ANISOU 3867  O   PHE A 514     4523   5105   5402   -161   -256    574       O  
ATOM   3868  CB  PHE A 514       2.960 -12.863  32.252  1.00 39.06           C  
ANISOU 3868  CB  PHE A 514     4477   5062   5300   -144   -222    546       C  
ATOM   3869  CG  PHE A 514       2.142 -11.829  31.542  1.00 41.60           C  
ANISOU 3869  CG  PHE A 514     4810   5390   5605   -131   -202    525       C  
ATOM   3870  CD1 PHE A 514       0.758 -11.782  31.718  1.00 41.17           C  
ANISOU 3870  CD1 PHE A 514     4756   5344   5542   -132   -195    525       C  
ATOM   3871  CD2 PHE A 514       2.743 -10.876  30.710  1.00 41.82           C  
ANISOU 3871  CD2 PHE A 514     4848   5414   5626   -118   -191    505       C  
ATOM   3872  CE1 PHE A 514      -0.012 -10.818  31.067  1.00 39.87           C  
ANISOU 3872  CE1 PHE A 514     4600   5183   5365   -119   -179    506       C  
ATOM   3873  CE2 PHE A 514       1.975  -9.913  30.060  1.00 39.52           C  
ANISOU 3873  CE2 PHE A 514     4567   5127   5320   -106   -175    487       C  
ATOM   3874  CZ  PHE A 514       0.598  -9.885  30.245  1.00 39.43           C  
ANISOU 3874  CZ  PHE A 514     4555   5123   5302   -107   -170    487       C  
ATOM   3875  N   ASP A 515       4.539 -15.986  32.087  1.00 41.46           N  
ANISOU 3875  N   ASP A 515     4743   5325   5684   -151   -271    577       N  
ATOM   3876  CA  ASP A 515       5.137 -16.913  33.067  1.00 44.81           C  
ANISOU 3876  CA  ASP A 515     5155   5745   6125   -168   -294    604       C  
ATOM   3877  C   ASP A 515       6.653 -16.812  33.231  1.00 45.24           C  
ANISOU 3877  C   ASP A 515     5207   5790   6192   -172   -302    607       C  
ATOM   3878  O   ASP A 515       7.200 -17.169  34.276  1.00 49.43           O  
ANISOU 3878  O   ASP A 515     5732   6323   6726   -190   -319    630       O  
ATOM   3879  CB  ASP A 515       4.737 -18.353  32.752  1.00 46.67           C  
ANISOU 3879  CB  ASP A 515     5373   5963   6393   -167   -310    613       C  
ATOM   3880  CG  ASP A 515       3.261 -18.614  33.012  1.00 49.68           C  
ANISOU 3880  CG  ASP A 515     5755   6356   6764   -171   -307    619       C  
ATOM   3881  OD1 ASP A 515       2.584 -17.739  33.615  1.00 48.84           O  
ANISOU 3881  OD1 ASP A 515     5661   6270   6624   -177   -293    619       O  
ATOM   3882  OD2 ASP A 515       2.776 -19.696  32.613  1.00 51.96           O  
ANISOU 3882  OD2 ASP A 515     6031   6632   7078   -167   -318    623       O  
ATOM   3883  N   THR A 516       7.303 -16.291  32.198  1.00 42.06           N  
ANISOU 3883  N   THR A 516     4808   5378   5795   -156   -291    584       N  
ATOM   3884  CA  THR A 516       8.747 -16.194  32.093  1.00 38.69           C  
ANISOU 3884  CA  THR A 516     4377   4939   5385   -155   -296    582       C  
ATOM   3885  C   THR A 516       9.305 -14.876  32.675  1.00 38.95           C  
ANISOU 3885  C   THR A 516     4424   4987   5386   -161   -285    580       C  
ATOM   3886  O   THR A 516      10.509 -14.731  32.859  1.00 38.92           O  
ANISOU 3886  O   THR A 516     4417   4976   5393   -165   -292    583       O  
ATOM   3887  CB  THR A 516       9.111 -16.352  30.603  1.00 38.58           C  
ANISOU 3887  CB  THR A 516     4358   4905   5392   -135   -287    556       C  
ATOM   3888  OG1 THR A 516       9.389 -17.726  30.320  1.00 36.66           O  
ANISOU 3888  OG1 THR A 516     4095   4641   5190   -134   -304    563       O  
ATOM   3889  CG2 THR A 516      10.283 -15.504  30.197  1.00 39.00           C  
ANISOU 3889  CG2 THR A 516     4417   4955   5444   -129   -277    541       C  
ATOM   3890  N   LEU A 517       8.425 -13.933  32.991  1.00 38.59           N  
ANISOU 3890  N   LEU A 517     4394   4962   5305   -163   -270    575       N  
ATOM   3891  CA  LEU A 517       8.844 -12.577  33.328  1.00 38.92           C  
ANISOU 3891  CA  LEU A 517     4452   5018   5317   -165   -256    567       C  
ATOM   3892  C   LEU A 517       9.040 -12.378  34.819  1.00 40.81           C  
ANISOU 3892  C   LEU A 517     4696   5273   5538   -188   -266    590       C  
ATOM   3893  O   LEU A 517       8.324 -11.593  35.459  1.00 40.16           O  
ANISOU 3893  O   LEU A 517     4625   5210   5422   -196   -254    590       O  
ATOM   3894  CB  LEU A 517       7.833 -11.553  32.780  1.00 38.81           C  
ANISOU 3894  CB  LEU A 517     4452   5016   5275   -154   -233    547       C  
ATOM   3895  CG  LEU A 517       7.437 -11.596  31.297  1.00 36.72           C  
ANISOU 3895  CG  LEU A 517     4188   4740   5023   -132   -222    524       C  
ATOM   3896  CD1 LEU A 517       6.419 -10.517  30.978  1.00 35.72           C  
ANISOU 3896  CD1 LEU A 517     4076   4627   4868   -125   -203    508       C  
ATOM   3897  CD2 LEU A 517       8.649 -11.477  30.387  1.00 36.29           C  
ANISOU 3897  CD2 LEU A 517     4132   4669   4985   -122   -220    510       C  
ATOM   3898  N   HIS A 518      10.040 -13.065  35.363  1.00 43.94           N  
ANISOU 3898  N   HIS A 518     5081   5659   5955   -200   -287    608       N  
ATOM   3899  CA  HIS A 518      10.240 -13.099  36.813  1.00 46.15           C  
ANISOU 3899  CA  HIS A 518     5363   5951   6219   -225   -301    634       C  
ATOM   3900  C   HIS A 518      10.701 -11.815  37.459  1.00 44.94           C  
ANISOU 3900  C   HIS A 518     5226   5813   6033   -233   -291    631       C  
ATOM   3901  O   HIS A 518      10.456 -11.607  38.644  1.00 43.68           O  
ANISOU 3901  O   HIS A 518     5074   5670   5849   -254   -295    647       O  
ATOM   3902  CB  HIS A 518      11.115 -14.287  37.218  1.00 50.85           C  
ANISOU 3902  CB  HIS A 518     5941   6529   6850   -236   -330    657       C  
ATOM   3903  CG  HIS A 518      10.508 -15.647  36.884  1.00 58.51           C  
ANISOU 3903  CG  HIS A 518     6895   7486   7849   -233   -343    666       C  
ATOM   3904  ND1 HIS A 518      11.244 -16.780  36.826  1.00 61.77           N  
ANISOU 3904  ND1 HIS A 518     7289   7876   8303   -235   -367    680       N  
ATOM   3905  CD2 HIS A 518       9.193 -16.021  36.575  1.00 58.30           C  
ANISOU 3905  CD2 HIS A 518     6868   7464   7817   -227   -335    662       C  
ATOM   3906  CE1 HIS A 518      10.446 -17.823  36.509  1.00 59.75           C  
ANISOU 3906  CE1 HIS A 518     7022   7613   8067   -232   -374    684       C  
ATOM   3907  NE2 HIS A 518       9.194 -17.356  36.352  1.00 60.67           N  
ANISOU 3907  NE2 HIS A 518     7150   7746   8154   -227   -354    673       N  
ATOM   3908  N   ARG A 519      11.333 -10.919  36.698  1.00 45.19           N  
ANISOU 3908  N   ARG A 519     5264   5841   6064   -218   -277    609       N  
ATOM   3909  CA  ARG A 519      11.800  -9.637  37.266  1.00 44.98           C  
ANISOU 3909  CA  ARG A 519     5252   5828   6006   -225   -266    604       C  
ATOM   3910  C   ARG A 519      10.823  -8.460  37.049  1.00 43.45           C  
ANISOU 3910  C   ARG A 519     5075   5653   5779   -217   -240    584       C  
ATOM   3911  O   ARG A 519      11.092  -7.333  37.475  1.00 42.08           O  
ANISOU 3911  O   ARG A 519     4915   5491   5580   -221   -229    578       O  
ATOM   3912  CB  ARG A 519      13.216  -9.267  36.770  1.00 45.51           C  
ANISOU 3912  CB  ARG A 519     5317   5881   6091   -217   -269    596       C  
ATOM   3913  CG  ARG A 519      14.135 -10.439  36.426  1.00 46.48           C  
ANISOU 3913  CG  ARG A 519     5420   5980   6259   -215   -290    606       C  
ATOM   3914  CD  ARG A 519      15.574 -10.280  36.927  1.00 48.64           C  
ANISOU 3914  CD  ARG A 519     5689   6245   6545   -224   -304    616       C  
ATOM   3915  NE  ARG A 519      16.011  -8.887  37.073  1.00 50.57           N  
ANISOU 3915  NE  ARG A 519     5950   6502   6761   -224   -289    604       N  
ATOM   3916  CZ  ARG A 519      16.624  -8.170  36.127  1.00 50.10           C  
ANISOU 3916  CZ  ARG A 519     5893   6435   6707   -207   -274    582       C  
ATOM   3917  NH1 ARG A 519      16.887  -8.704  34.936  1.00 47.44           N  
ANISOU 3917  NH1 ARG A 519     5544   6078   6401   -189   -270    568       N  
ATOM   3918  NH2 ARG A 519      16.970  -6.908  36.374  1.00 47.31           N  
ANISOU 3918  NH2 ARG A 519     5554   6093   6327   -208   -261    573       N  
ATOM   3919  N   LEU A 520       9.685  -8.736  36.411  1.00 43.63           N  
ANISOU 3919  N   LEU A 520     5097   5676   5804   -205   -230    575       N  
ATOM   3920  CA  LEU A 520       8.748  -7.691  35.978  1.00 43.49           C  
ANISOU 3920  CA  LEU A 520     5091   5669   5762   -194   -206    554       C  
ATOM   3921  C   LEU A 520       8.148  -6.902  37.135  1.00 44.68           C  
ANISOU 3921  C   LEU A 520     5254   5844   5878   -211   -196    558       C  
ATOM   3922  O   LEU A 520       7.534  -7.478  38.025  1.00 45.85           O  
ANISOU 3922  O   LEU A 520     5399   6000   6018   -228   -203    575       O  
ATOM   3923  CB  LEU A 520       7.637  -8.292  35.107  1.00 42.96           C  
ANISOU 3923  CB  LEU A 520     5018   5596   5708   -181   -201    546       C  
ATOM   3924  CG  LEU A 520       6.638  -7.319  34.467  1.00 43.32           C  
ANISOU 3924  CG  LEU A 520     5073   5649   5735   -167   -179    524       C  
ATOM   3925  CD1 LEU A 520       7.301  -6.426  33.427  1.00 43.32           C  
ANISOU 3925  CD1 LEU A 520     5080   5641   5735   -150   -168    502       C  
ATOM   3926  CD2 LEU A 520       5.471  -8.073  33.853  1.00 42.36           C  
ANISOU 3926  CD2 LEU A 520     4944   5522   5626   -158   -179    521       C  
ATOM   3927  N   GLN A 521       8.326  -5.583  37.111  1.00 44.94           N  
ANISOU 3927  N   GLN A 521     5300   5885   5889   -207   -179    542       N  
ATOM   3928  CA  GLN A 521       7.886  -4.730  38.213  1.00 44.51           C  
ANISOU 3928  CA  GLN A 521     5257   5852   5801   -223   -168    543       C  
ATOM   3929  C   GLN A 521       6.618  -3.950  37.908  1.00 45.33           C  
ANISOU 3929  C   GLN A 521     5368   5966   5889   -214   -146    525       C  
ATOM   3930  O   GLN A 521       5.839  -3.654  38.815  1.00 46.54           O  
ANISOU 3930  O   GLN A 521     5527   6136   6020   -229   -137    527       O  
ATOM   3931  CB  GLN A 521       8.988  -3.756  38.604  1.00 44.43           C  
ANISOU 3931  CB  GLN A 521     5257   5846   5777   -229   -167    540       C  
ATOM   3932  CG  GLN A 521      10.070  -4.361  39.480  1.00 47.60           C  
ANISOU 3932  CG  GLN A 521     5655   6245   6184   -248   -190    563       C  
ATOM   3933  CD  GLN A 521      11.264  -3.431  39.684  1.00 49.74           C  
ANISOU 3933  CD  GLN A 521     5935   6516   6447   -250   -189    559       C  
ATOM   3934  OE1 GLN A 521      12.406  -3.888  39.752  1.00 52.14           O  
ANISOU 3934  OE1 GLN A 521     6232   6808   6769   -254   -208    571       O  
ATOM   3935  NE2 GLN A 521      11.010  -2.128  39.773  1.00 46.95           N  
ANISOU 3935  NE2 GLN A 521     5595   6176   6068   -248   -169    542       N  
ATOM   3936  N   LEU A 522       6.418  -3.621  36.633  1.00 44.52           N  
ANISOU 3936  N   LEU A 522     5264   5852   5797   -191   -136    506       N  
ATOM   3937  CA  LEU A 522       5.365  -2.704  36.211  1.00 41.16           C  
ANISOU 3937  CA  LEU A 522     4845   5432   5359   -180   -116    486       C  
ATOM   3938  C   LEU A 522       4.726  -3.206  34.915  1.00 40.49           C  
ANISOU 3938  C   LEU A 522     4753   5333   5295   -161   -116    477       C  
ATOM   3939  O   LEU A 522       5.381  -3.272  33.871  1.00 39.57           O  
ANISOU 3939  O   LEU A 522     4636   5202   5194   -146   -120    469       O  
ATOM   3940  CB  LEU A 522       5.966  -1.302  36.020  1.00 41.87           C  
ANISOU 3940  CB  LEU A 522     4948   5526   5434   -174   -103    470       C  
ATOM   3941  CG  LEU A 522       5.228   0.022  35.719  1.00 43.41           C  
ANISOU 3941  CG  LEU A 522     5152   5728   5614   -165    -82    449       C  
ATOM   3942  CD1 LEU A 522       4.065  -0.102  34.732  1.00 43.01           C  
ANISOU 3942  CD1 LEU A 522     5096   5669   5574   -148    -75    437       C  
ATOM   3943  CD2 LEU A 522       4.774   0.700  37.000  1.00 44.87           C  
ANISOU 3943  CD2 LEU A 522     5343   5931   5772   -183    -70    449       C  
ATOM   3944  N   LEU A 523       3.448  -3.570  34.999  1.00 39.57           N  
ANISOU 3944  N   LEU A 523     4633   5222   5180   -161   -112    478       N  
ATOM   3945  CA  LEU A 523       2.657  -3.920  33.827  1.00 38.73           C  
ANISOU 3945  CA  LEU A 523     4521   5103   5091   -143   -111    468       C  
ATOM   3946  C   LEU A 523       1.439  -2.968  33.700  1.00 40.77           C  
ANISOU 3946  C   LEU A 523     4783   5368   5336   -137    -93    452       C  
ATOM   3947  O   LEU A 523       0.540  -2.984  34.540  1.00 40.64           O  
ANISOU 3947  O   LEU A 523     4765   5364   5311   -149    -86    457       O  
ATOM   3948  CB  LEU A 523       2.265  -5.399  33.893  1.00 36.95           C  
ANISOU 3948  CB  LEU A 523     4282   4871   4885   -148   -126    484       C  
ATOM   3949  CG  LEU A 523       1.385  -6.127  32.871  1.00 36.86           C  
ANISOU 3949  CG  LEU A 523     4262   4847   4893   -134   -130    479       C  
ATOM   3950  CD1 LEU A 523       1.955  -6.081  31.467  1.00 36.31           C  
ANISOU 3950  CD1 LEU A 523     4195   4761   4839   -115   -132    465       C  
ATOM   3951  CD2 LEU A 523       1.189  -7.573  33.304  1.00 36.88           C  
ANISOU 3951  CD2 LEU A 523     4253   4847   4913   -144   -146    499       C  
ATOM   3952  N   ASN A 524       1.468  -2.108  32.673  1.00 41.62           N  
ANISOU 3952  N   ASN A 524     4898   5469   5445   -121    -85    434       N  
ATOM   3953  CA  ASN A 524       0.400  -1.149  32.333  1.00 42.09           C  
ANISOU 3953  CA  ASN A 524     4961   5531   5498   -112    -70    418       C  
ATOM   3954  C   ASN A 524      -0.413  -1.831  31.223  1.00 41.59           C  
ANISOU 3954  C   ASN A 524     4891   5454   5455    -98    -76    415       C  
ATOM   3955  O   ASN A 524       0.084  -2.038  30.117  1.00 41.73           O  
ANISOU 3955  O   ASN A 524     4911   5458   5484    -86    -83    410       O  
ATOM   3956  CB  ASN A 524       1.037   0.199  31.865  1.00 42.82           C  
ANISOU 3956  CB  ASN A 524     5066   5623   5580   -103    -60    403       C  
ATOM   3957  CG  ASN A 524       0.082   1.415  31.904  1.00 45.01           C  
ANISOU 3957  CG  ASN A 524     5347   5905   5847    -99    -44    387       C  
ATOM   3958  OD1 ASN A 524      -1.076   1.334  31.574  1.00 46.17           O  
ANISOU 3958  OD1 ASN A 524     5489   6049   6003    -93    -41    383       O  
ATOM   3959  ND2 ASN A 524       0.570   2.531  32.274  1.00 47.69           N  
ANISOU 3959  ND2 ASN A 524     5695   6252   6172   -102    -34    379       N  
ATOM   3960  N   MET A 525      -1.634  -2.250  31.541  1.00 40.22           N  
ANISOU 3960  N   MET A 525     4710   5284   5286   -101    -75    419       N  
ATOM   3961  CA  MET A 525      -2.548  -2.809  30.538  1.00 39.20           C  
ANISOU 3961  CA  MET A 525     4574   5142   5175    -89    -81    415       C  
ATOM   3962  C   MET A 525      -3.870  -2.066  30.556  1.00 38.29           C  
ANISOU 3962  C   MET A 525     4458   5031   5059    -85    -68    405       C  
ATOM   3963  O   MET A 525      -4.896  -2.598  30.132  1.00 38.66           O  
ANISOU 3963  O   MET A 525     4496   5071   5120    -80    -72    405       O  
ATOM   3964  CB  MET A 525      -2.814  -4.291  30.776  1.00 39.21           C  
ANISOU 3964  CB  MET A 525     4564   5141   5192    -95    -94    432       C  
ATOM   3965  CG  MET A 525      -1.625  -5.178  30.506  1.00 40.94           C  
ANISOU 3965  CG  MET A 525     4781   5351   5422    -96   -109    441       C  
ATOM   3966  SD  MET A 525      -2.128  -6.837  30.056  1.00 44.19           S  
ANISOU 3966  SD  MET A 525     5179   5751   5860    -94   -126    452       S  
ATOM   3967  CE  MET A 525      -2.879  -7.354  31.604  1.00 44.32           C  
ANISOU 3967  CE  MET A 525     5187   5783   5870   -114   -125    471       C  
ATOM   3968  N   SER A 526      -3.832  -0.835  31.057  1.00 36.58           N  
ANISOU 3968  N   SER A 526     4247   4823   4826    -88    -53    395       N  
ATOM   3969  CA  SER A 526      -4.995   0.028  31.101  1.00 35.56           C  
ANISOU 3969  CA  SER A 526     4117   4697   4697    -84    -40    383       C  
ATOM   3970  C   SER A 526      -5.456   0.371  29.685  1.00 36.29           C  
ANISOU 3970  C   SER A 526     4212   4773   4804    -66    -45    372       C  
ATOM   3971  O   SER A 526      -4.672   0.275  28.729  1.00 36.08           O  
ANISOU 3971  O   SER A 526     4191   4736   4779    -57    -55    370       O  
ATOM   3972  CB  SER A 526      -4.649   1.305  31.851  1.00 33.69           C  
ANISOU 3972  CB  SER A 526     3887   4471   4441    -91    -24    374       C  
ATOM   3973  OG  SER A 526      -3.788   2.111  31.072  1.00 33.97           O  
ANISOU 3973  OG  SER A 526     3934   4500   4473    -80    -25    364       O  
ATOM   3974  N   HIS A 527      -6.723   0.773  29.562  1.00 35.51           N  
ANISOU 3974  N   HIS A 527     4105   4671   4714    -61    -39    364       N  
ATOM   3975  CA  HIS A 527      -7.283   1.277  28.304  1.00 34.18           C  
ANISOU 3975  CA  HIS A 527     3940   4488   4558    -45    -44    353       C  
ATOM   3976  C   HIS A 527      -7.330   0.267  27.195  1.00 34.58           C  
ANISOU 3976  C   HIS A 527     3989   4524   4623    -37    -62    358       C  
ATOM   3977  O   HIS A 527      -7.118   0.604  26.029  1.00 35.48           O  
ANISOU 3977  O   HIS A 527     4113   4627   4741    -25    -69    351       O  
ATOM   3978  CB  HIS A 527      -6.546   2.527  27.841  1.00 34.06           C  
ANISOU 3978  CB  HIS A 527     3938   4470   4532    -39    -39    341       C  
ATOM   3979  CG  HIS A 527      -6.872   3.760  28.641  1.00 34.15           C  
ANISOU 3979  CG  HIS A 527     3949   4491   4535    -43    -22    331       C  
ATOM   3980  ND1 HIS A 527      -6.049   4.246  29.594  1.00 34.45           N  
ANISOU 3980  ND1 HIS A 527     3992   4541   4554    -53    -11    331       N  
ATOM   3981  CD2 HIS A 527      -7.969   4.620  28.588  1.00 33.92           C  
ANISOU 3981  CD2 HIS A 527     3914   4458   4516    -38    -13    320       C  
ATOM   3982  CE1 HIS A 527      -6.592   5.355  30.131  1.00 34.76           C  
ANISOU 3982  CE1 HIS A 527     4030   4586   4591    -55      4    319       C  
ATOM   3983  NE2 HIS A 527      -7.773   5.579  29.516  1.00 34.97           N  
ANISOU 3983  NE2 HIS A 527     4049   4602   4636    -46      2    312       N  
ATOM   3984  N   ASN A 528      -7.607  -0.983  27.547  1.00 35.58           N  
ANISOU 3984  N   ASN A 528     4106   4652   4758    -43    -69    371       N  
ATOM   3985  CA  ASN A 528      -7.879  -2.030  26.568  1.00 36.20           C  
ANISOU 3985  CA  ASN A 528     4182   4717   4854    -35    -85    375       C  
ATOM   3986  C   ASN A 528      -9.358  -2.402  26.652  1.00 37.05           C  
ANISOU 3986  C   ASN A 528     4276   4822   4978    -34    -86    377       C  
ATOM   3987  O   ASN A 528     -10.136  -1.657  27.245  1.00 38.01           O  
ANISOU 3987  O   ASN A 528     4393   4949   5099    -37    -73    372       O  
ATOM   3988  CB  ASN A 528      -6.961  -3.241  26.804  1.00 35.87           C  
ANISOU 3988  CB  ASN A 528     4138   4677   4813    -42    -95    388       C  
ATOM   3989  CG  ASN A 528      -5.568  -3.037  26.228  1.00 35.49           C  
ANISOU 3989  CG  ASN A 528     4102   4625   4757    -38    -98    384       C  
ATOM   3990  OD1 ASN A 528      -5.377  -3.036  25.009  1.00 34.59           O  
ANISOU 3990  OD1 ASN A 528     3994   4498   4648    -28   -105    376       O  
ATOM   3991  ND2 ASN A 528      -4.588  -2.870  27.102  1.00 35.21           N  
ANISOU 3991  ND2 ASN A 528     4069   4600   4708    -48    -92    389       N  
ATOM   3992  N   ASN A 529      -9.748  -3.530  26.065  1.00 39.21           N  
ANISOU 3992  N   ASN A 529     4543   5085   5267    -31   -100    384       N  
ATOM   3993  CA  ASN A 529     -11.145  -3.988  26.106  1.00 42.59           C  
ANISOU 3993  CA  ASN A 529     4958   5509   5713    -30   -103    387       C  
ATOM   3994  C   ASN A 529     -11.302  -5.366  26.765  1.00 44.31           C  
ANISOU 3994  C   ASN A 529     5164   5730   5939    -40   -109    402       C  
ATOM   3995  O   ASN A 529     -11.966  -6.256  26.219  1.00 43.37           O  
ANISOU 3995  O   ASN A 529     5037   5601   5838    -36   -121    407       O  
ATOM   3996  CB  ASN A 529     -11.763  -3.998  24.699  1.00 44.56           C  
ANISOU 3996  CB  ASN A 529     5210   5740   5978    -17   -117    380       C  
ATOM   3997  CG  ASN A 529     -11.589  -2.674  23.972  1.00 47.04           C  
ANISOU 3997  CG  ASN A 529     5536   6049   6285     -8   -114    366       C  
ATOM   3998  OD1 ASN A 529     -12.031  -1.626  24.451  1.00 48.57           O  
ANISOU 3998  OD1 ASN A 529     5729   6248   6476     -8   -101    359       O  
ATOM   3999  ND2 ASN A 529     -10.939  -2.717  22.805  1.00 44.72           N  
ANISOU 3999  ND2 ASN A 529     5256   5746   5989     -1   -125    362       N  
ATOM   4000  N   LEU A 530     -10.686  -5.534  27.936  1.00 44.44           N  
ANISOU 4000  N   LEU A 530     5180   5762   5943    -54   -101    411       N  
ATOM   4001  CA  LEU A 530     -10.717  -6.812  28.648  1.00 43.76           C  
ANISOU 4001  CA  LEU A 530     5084   5681   5862    -65   -107    428       C  
ATOM   4002  C   LEU A 530     -12.028  -6.991  29.404  1.00 45.70           C  
ANISOU 4002  C   LEU A 530     5316   5932   6116    -73    -99    432       C  
ATOM   4003  O   LEU A 530     -12.394  -6.146  30.230  1.00 46.82           O  
ANISOU 4003  O   LEU A 530     5456   6085   6246    -80    -81    426       O  
ATOM   4004  CB  LEU A 530      -9.519  -6.940  29.602  1.00 40.90           C  
ANISOU 4004  CB  LEU A 530     4726   5331   5483    -78   -105    437       C  
ATOM   4005  CG  LEU A 530      -8.136  -7.025  28.946  1.00 39.15           C  
ANISOU 4005  CG  LEU A 530     4514   5102   5257    -73   -114    436       C  
ATOM   4006  CD1 LEU A 530      -7.026  -6.868  29.968  1.00 38.37           C  
ANISOU 4006  CD1 LEU A 530     4420   5016   5140    -86   -110    444       C  
ATOM   4007  CD2 LEU A 530      -7.954  -8.310  28.153  1.00 39.01           C  
ANISOU 4007  CD2 LEU A 530     4491   5070   5259    -67   -133    442       C  
ATOM   4008  N   LEU A 531     -12.725  -8.091  29.112  1.00 46.90           N  
ANISOU 4008  N   LEU A 531     5456   6075   6286    -71   -111    440       N  
ATOM   4009  CA  LEU A 531     -14.003  -8.419  29.754  1.00 47.91           C  
ANISOU 4009  CA  LEU A 531     5570   6207   6425    -79   -104    445       C  
ATOM   4010  C   LEU A 531     -13.850  -9.040  31.153  1.00 48.77           C  
ANISOU 4010  C   LEU A 531     5674   6332   6524    -99    -98    461       C  
ATOM   4011  O   LEU A 531     -14.752  -8.940  31.993  1.00 49.75           O  
ANISOU 4011  O   LEU A 531     5788   6465   6648   -110    -85    463       O  
ATOM   4012  CB  LEU A 531     -14.857  -9.317  28.841  1.00 48.70           C  
ANISOU 4012  CB  LEU A 531     5660   6291   6551    -69   -120    448       C  
ATOM   4013  CG  LEU A 531     -15.752  -8.644  27.778  1.00 48.49           C  
ANISOU 4013  CG  LEU A 531     5634   6250   6539    -53   -123    434       C  
ATOM   4014  CD1 LEU A 531     -16.373  -9.673  26.848  1.00 47.71           C  
ANISOU 4014  CD1 LEU A 531     5528   6135   6464    -45   -142    438       C  
ATOM   4015  CD2 LEU A 531     -16.841  -7.771  28.388  1.00 47.33           C  
ANISOU 4015  CD2 LEU A 531     5478   6109   6395    -56   -105    426       C  
ATOM   4016  N   PHE A 532     -12.706  -9.678  31.391  1.00 47.84           N  
ANISOU 4016  N   PHE A 532     5560   6217   6398   -106   -108    473       N  
ATOM   4017  CA  PHE A 532     -12.361 -10.220  32.707  1.00 45.81           C  
ANISOU 4017  CA  PHE A 532     5301   5975   6129   -127   -106    490       C  
ATOM   4018  C   PHE A 532     -10.845 -10.343  32.850  1.00 44.75           C  
ANISOU 4018  C   PHE A 532     5177   5843   5983   -132   -114    496       C  
ATOM   4019  O   PHE A 532     -10.120 -10.336  31.865  1.00 46.34           O  
ANISOU 4019  O   PHE A 532     5384   6032   6190   -118   -125    490       O  
ATOM   4020  CB  PHE A 532     -13.029 -11.591  32.929  1.00 43.46           C  
ANISOU 4020  CB  PHE A 532     4989   5673   5849   -135   -117    507       C  
ATOM   4021  CG  PHE A 532     -12.742 -12.594  31.840  1.00 43.67           C  
ANISOU 4021  CG  PHE A 532     5012   5681   5897   -122   -140    511       C  
ATOM   4022  CD1 PHE A 532     -11.542 -13.323  31.829  1.00 42.66           C  
ANISOU 4022  CD1 PHE A 532     4887   5550   5770   -125   -155    522       C  
ATOM   4023  CD2 PHE A 532     -13.665 -12.815  30.818  1.00 42.59           C  
ANISOU 4023  CD2 PHE A 532     4869   5530   5782   -107   -146    503       C  
ATOM   4024  CE1 PHE A 532     -11.267 -14.242  30.820  1.00 41.83           C  
ANISOU 4024  CE1 PHE A 532     4779   5428   5687   -114   -174    523       C  
ATOM   4025  CE2 PHE A 532     -13.397 -13.737  29.806  1.00 43.74           C  
ANISOU 4025  CE2 PHE A 532     5013   5659   5947    -96   -166    505       C  
ATOM   4026  CZ  PHE A 532     -12.196 -14.452  29.807  1.00 43.48           C  
ANISOU 4026  CZ  PHE A 532     4982   5623   5915    -99   -179    514       C  
ATOM   4027  N   LEU A 533     -10.373 -10.455  34.083  1.00 46.29           N  
ANISOU 4027  N   LEU A 533     5374   6053   6161   -152   -110    509       N  
ATOM   4028  CA  LEU A 533      -9.008 -10.896  34.341  1.00 47.47           C  
ANISOU 4028  CA  LEU A 533     5528   6203   6304   -159   -123    521       C  
ATOM   4029  C   LEU A 533      -8.986 -12.370  34.757  1.00 49.87           C  
ANISOU 4029  C   LEU A 533     5822   6505   6622   -170   -141    544       C  
ATOM   4030  O   LEU A 533      -9.998 -12.919  35.196  1.00 51.17           O  
ANISOU 4030  O   LEU A 533     5977   6673   6793   -179   -139    552       O  
ATOM   4031  CB  LEU A 533      -8.355 -10.044  35.431  1.00 45.67           C  
ANISOU 4031  CB  LEU A 533     5311   5993   6048   -174   -110    522       C  
ATOM   4032  CG  LEU A 533      -8.026  -8.587  35.124  1.00 43.76           C  
ANISOU 4032  CG  LEU A 533     5082   5754   5791   -165    -95    501       C  
ATOM   4033  CD1 LEU A 533      -7.391  -7.963  36.353  1.00 43.17           C  
ANISOU 4033  CD1 LEU A 533     5015   5697   5688   -184    -85    505       C  
ATOM   4034  CD2 LEU A 533      -7.121  -8.438  33.905  1.00 42.38           C  
ANISOU 4034  CD2 LEU A 533     4912   5563   5625   -146   -106    493       C  
ATOM   4035  N   ASP A 534      -7.830 -13.006  34.597  1.00 51.96           N  
ANISOU 4035  N   ASP A 534     6087   6760   6892   -171   -158    554       N  
ATOM   4036  CA  ASP A 534      -7.604 -14.348  35.113  1.00 52.40           C  
ANISOU 4036  CA  ASP A 534     6133   6814   6961   -184   -177    578       C  
ATOM   4037  C   ASP A 534      -6.294 -14.369  35.892  1.00 54.05           C  
ANISOU 4037  C   ASP A 534     6349   7030   7158   -199   -184    591       C  
ATOM   4038  O   ASP A 534      -5.201 -14.340  35.310  1.00 53.46           O  
ANISOU 4038  O   ASP A 534     6277   6944   7090   -189   -193    587       O  
ATOM   4039  CB  ASP A 534      -7.593 -15.379  33.982  1.00 54.34           C  
ANISOU 4039  CB  ASP A 534     6369   7038   7237   -169   -195    578       C  
ATOM   4040  CG  ASP A 534      -7.511 -16.820  34.493  1.00 56.11           C  
ANISOU 4040  CG  ASP A 534     6581   7258   7479   -182   -215    602       C  
ATOM   4041  OD1 ASP A 534      -7.785 -17.751  33.701  1.00 52.40           O  
ANISOU 4041  OD1 ASP A 534     6101   6771   7036   -171   -228    603       O  
ATOM   4042  OD2 ASP A 534      -7.182 -17.023  35.684  1.00 58.21           O  
ANISOU 4042  OD2 ASP A 534     6847   7536   7732   -203   -217    621       O  
ATOM   4043  N   SER A 535      -6.429 -14.434  37.214  1.00 55.46           N  
ANISOU 4043  N   SER A 535     6528   7224   7318   -223   -181    606       N  
ATOM   4044  CA  SER A 535      -5.310 -14.330  38.167  1.00 54.20           C  
ANISOU 4044  CA  SER A 535     6377   7074   7142   -241   -187    620       C  
ATOM   4045  C   SER A 535      -4.060 -15.109  37.783  1.00 49.01           C  
ANISOU 4045  C   SER A 535     5714   6400   6504   -238   -211    631       C  
ATOM   4046  O   SER A 535      -2.953 -14.672  38.057  1.00 46.43           O  
ANISOU 4046  O   SER A 535     5396   6077   6168   -242   -215    633       O  
ATOM   4047  CB  SER A 535      -5.756 -14.800  39.554  1.00 57.78           C  
ANISOU 4047  CB  SER A 535     6828   7543   7580   -270   -188    642       C  
ATOM   4048  OG  SER A 535      -7.164 -14.716  39.694  1.00 66.42           O  
ANISOU 4048  OG  SER A 535     7918   8645   8672   -272   -172    636       O  
ATOM   4049  N   SER A 536      -4.252 -16.263  37.157  1.00 48.57           N  
ANISOU 4049  N   SER A 536     5645   6328   6478   -230   -228    638       N  
ATOM   4050  CA  SER A 536      -3.162 -17.190  36.876  1.00 49.56           C  
ANISOU 4050  CA  SER A 536     5763   6438   6628   -228   -252    650       C  
ATOM   4051  C   SER A 536      -2.252 -16.763  35.713  1.00 48.73           C  
ANISOU 4051  C   SER A 536     5662   6318   6535   -206   -251    631       C  
ATOM   4052  O   SER A 536      -1.217 -17.394  35.457  1.00 47.22           O  
ANISOU 4052  O   SER A 536     5464   6112   6364   -205   -268    637       O  
ATOM   4053  CB  SER A 536      -3.712 -18.606  36.678  1.00 51.73           C  
ANISOU 4053  CB  SER A 536     6022   6700   6932   -229   -269    665       C  
ATOM   4054  OG  SER A 536      -4.802 -18.611  35.776  1.00 53.22           O  
ANISOU 4054  OG  SER A 536     6207   6882   7130   -212   -260    649       O  
ATOM   4055  N   HIS A 537      -2.637 -15.690  35.021  1.00 48.54           N  
ANISOU 4055  N   HIS A 537     5646   6297   6497   -191   -232    606       N  
ATOM   4056  CA  HIS A 537      -1.765 -15.045  34.038  1.00 46.55           C  
ANISOU 4056  CA  HIS A 537     5401   6035   6248   -173   -228    587       C  
ATOM   4057  C   HIS A 537      -0.607 -14.386  34.731  1.00 45.76           C  
ANISOU 4057  C   HIS A 537     5310   5943   6132   -184   -227    591       C  
ATOM   4058  O   HIS A 537       0.476 -14.247  34.157  1.00 44.57           O  
ANISOU 4058  O   HIS A 537     5161   5781   5990   -175   -231    584       O  
ATOM   4059  CB  HIS A 537      -2.518 -13.984  33.233  1.00 44.97           C  
ANISOU 4059  CB  HIS A 537     5210   5838   6037   -157   -208    563       C  
ATOM   4060  CG  HIS A 537      -3.636 -14.525  32.368  1.00 44.11           C  
ANISOU 4060  CG  HIS A 537     5094   5719   5945   -144   -209    556       C  
ATOM   4061  ND1 HIS A 537      -3.513 -15.644  31.628  1.00 43.72           N  
ANISOU 4061  ND1 HIS A 537     5034   5652   5924   -136   -225    559       N  
ATOM   4062  CD2 HIS A 537      -4.911 -14.021  32.109  1.00 42.40           C  
ANISOU 4062  CD2 HIS A 537     4879   5507   5722   -138   -196    545       C  
ATOM   4063  CE1 HIS A 537      -4.660 -15.861  30.952  1.00 41.77           C  
ANISOU 4063  CE1 HIS A 537     4783   5399   5687   -126   -223    551       C  
ATOM   4064  NE2 HIS A 537      -5.509 -14.866  31.244  1.00 41.40           N  
ANISOU 4064  NE2 HIS A 537     4743   5366   5619   -127   -206    543       N  
ATOM   4065  N   TYR A 538      -0.837 -14.005  35.986  1.00 47.36           N  
ANISOU 4065  N   TYR A 538     5519   6165   6310   -204   -221    603       N  
ATOM   4066  CA  TYR A 538       0.052 -13.122  36.742  1.00 49.98           C  
ANISOU 4066  CA  TYR A 538     5862   6509   6619   -215   -217    605       C  
ATOM   4067  C   TYR A 538       0.783 -13.815  37.877  1.00 51.36           C  
ANISOU 4067  C   TYR A 538     6034   6687   6793   -239   -235    632       C  
ATOM   4068  O   TYR A 538       1.741 -13.270  38.417  1.00 51.75           O  
ANISOU 4068  O   TYR A 538     6091   6741   6829   -248   -237    635       O  
ATOM   4069  CB  TYR A 538      -0.731 -11.923  37.284  1.00 48.96           C  
ANISOU 4069  CB  TYR A 538     5744   6399   6457   -220   -193    593       C  
ATOM   4070  CG  TYR A 538      -1.677 -11.346  36.274  1.00 48.64           C  
ANISOU 4070  CG  TYR A 538     5705   6354   6419   -200   -177    570       C  
ATOM   4071  CD1 TYR A 538      -2.978 -11.823  36.169  1.00 48.47           C  
ANISOU 4071  CD1 TYR A 538     5675   6333   6405   -198   -173    571       C  
ATOM   4072  CD2 TYR A 538      -1.267 -10.343  35.402  1.00 49.72           C  
ANISOU 4072  CD2 TYR A 538     5850   6486   6552   -182   -166    549       C  
ATOM   4073  CE1 TYR A 538      -3.849 -11.310  35.233  1.00 49.95           C  
ANISOU 4073  CE1 TYR A 538     5864   6516   6598   -180   -161    551       C  
ATOM   4074  CE2 TYR A 538      -2.135  -9.820  34.461  1.00 49.98           C  
ANISOU 4074  CE2 TYR A 538     5885   6515   6588   -164   -154    529       C  
ATOM   4075  CZ  TYR A 538      -3.424 -10.308  34.386  1.00 49.43           C  
ANISOU 4075  CZ  TYR A 538     5807   6445   6527   -163   -152    531       C  
ATOM   4076  OH  TYR A 538      -4.302  -9.804  33.462  1.00 52.93           O  
ANISOU 4076  OH  TYR A 538     6251   6883   6976   -146   -142    513       O  
ATOM   4077  N   ASN A 539       0.323 -15.004  38.255  1.00 56.89           N  
ANISOU 4077  N   ASN A 539     6723   7384   7509   -249   -251    651       N  
ATOM   4078  CA  ASN A 539       1.148 -15.897  39.053  1.00 61.53           C  
ANISOU 4078  CA  ASN A 539     7304   7967   8107   -268   -275    678       C  
ATOM   4079  C   ASN A 539       2.380 -16.200  38.209  1.00 63.73           C  
ANISOU 4079  C   ASN A 539     7575   8224   8413   -254   -289    674       C  
ATOM   4080  O   ASN A 539       2.268 -16.352  36.983  1.00 70.52           O  
ANISOU 4080  O   ASN A 539     8430   9070   9294   -231   -285    656       O  
ATOM   4081  CB  ASN A 539       0.403 -17.185  39.392  1.00 64.48           C  
ANISOU 4081  CB  ASN A 539     7665   8337   8497   -279   -290    699       C  
ATOM   4082  CG  ASN A 539       1.106 -17.998  40.466  1.00 70.19           C  
ANISOU 4082  CG  ASN A 539     8383   9060   9224   -305   -315    731       C  
ATOM   4083  OD1 ASN A 539       0.832 -19.189  40.637  1.00 74.07           O  
ANISOU 4083  OD1 ASN A 539     8861   9542   9736   -312   -333    750       O  
ATOM   4084  ND2 ASN A 539       2.019 -17.360  41.199  1.00 70.39           N  
ANISOU 4084  ND2 ASN A 539     8419   9094   9230   -318   -317    737       N  
ATOM   4085  N   GLN A 540       3.544 -16.266  38.851  1.00 58.40           N  
ANISOU 4085  N   GLN A 540     6902   7548   7740   -267   -304    689       N  
ATOM   4086  CA  GLN A 540       4.835 -16.336  38.151  1.00 56.29           C  
ANISOU 4086  CA  GLN A 540     6628   7261   7496   -255   -314    682       C  
ATOM   4087  C   GLN A 540       5.440 -14.942  37.898  1.00 53.03           C  
ANISOU 4087  C   GLN A 540     6230   6855   7062   -246   -295    662       C  
ATOM   4088  O   GLN A 540       6.562 -14.833  37.401  1.00 51.72           O  
ANISOU 4088  O   GLN A 540     6061   6676   6912   -237   -301    655       O  
ATOM   4089  CB  GLN A 540       4.734 -17.133  36.842  1.00 58.26           C  
ANISOU 4089  CB  GLN A 540     6864   7489   7783   -232   -318    670       C  
ATOM   4090  CG  GLN A 540       4.336 -18.595  37.011  1.00 61.74           C  
ANISOU 4090  CG  GLN A 540     7288   7917   8251   -240   -339    690       C  
ATOM   4091  CD  GLN A 540       5.443 -19.544  36.624  1.00 64.26           C  
ANISOU 4091  CD  GLN A 540     7591   8213   8612   -236   -361    697       C  
ATOM   4092  OE1 GLN A 540       5.389 -20.172  35.569  1.00 65.50           O  
ANISOU 4092  OE1 GLN A 540     7737   8351   8798   -219   -363    685       O  
ATOM   4093  NE2 GLN A 540       6.469 -19.640  37.466  1.00 70.04           N  
ANISOU 4093  NE2 GLN A 540     8320   8942   9346   -252   -378    717       N  
ATOM   4094  N   LEU A 541       4.692 -13.887  38.231  1.00 49.64           N  
ANISOU 4094  N   LEU A 541     5815   6446   6598   -248   -274    651       N  
ATOM   4095  CA  LEU A 541       5.244 -12.530  38.275  1.00 47.81           C  
ANISOU 4095  CA  LEU A 541     5598   6224   6342   -245   -258    635       C  
ATOM   4096  C   LEU A 541       5.703 -12.187  39.695  1.00 50.17           C  
ANISOU 4096  C   LEU A 541     5906   6539   6617   -272   -264    654       C  
ATOM   4097  O   LEU A 541       5.150 -11.295  40.355  1.00 49.59           O  
ANISOU 4097  O   LEU A 541     5846   6485   6510   -282   -247    649       O  
ATOM   4098  CB  LEU A 541       4.245 -11.494  37.763  1.00 44.07           C  
ANISOU 4098  CB  LEU A 541     5134   5760   5848   -232   -231    611       C  
ATOM   4099  CG  LEU A 541       3.765 -11.652  36.318  1.00 42.38           C  
ANISOU 4099  CG  LEU A 541     4915   5532   5654   -206   -224    591       C  
ATOM   4100  CD1 LEU A 541       2.809 -10.522  35.985  1.00 40.67           C  
ANISOU 4100  CD1 LEU A 541     4710   5327   5416   -196   -200    570       C  
ATOM   4101  CD2 LEU A 541       4.912 -11.718  35.319  1.00 39.93           C  
ANISOU 4101  CD2 LEU A 541     4601   5203   5367   -191   -230    581       C  
ATOM   4102  N   TYR A 542       6.745 -12.892  40.135  1.00 50.11           N  
ANISOU 4102  N   TYR A 542     5890   6521   6626   -284   -289    674       N  
ATOM   4103  CA  TYR A 542       7.233 -12.841  41.510  1.00 51.19           C  
ANISOU 4103  CA  TYR A 542     6035   6671   6744   -312   -302    697       C  
ATOM   4104  C   TYR A 542       7.777 -11.488  41.950  1.00 49.14           C  
ANISOU 4104  C   TYR A 542     5791   6424   6453   -318   -288    687       C  
ATOM   4105  O   TYR A 542       8.041 -11.274  43.131  1.00 49.36           O  
ANISOU 4105  O   TYR A 542     5829   6467   6459   -343   -295    703       O  
ATOM   4106  CB  TYR A 542       8.307 -13.911  41.705  1.00 53.52           C  
ANISOU 4106  CB  TYR A 542     6315   6946   7071   -321   -334    721       C  
ATOM   4107  CG  TYR A 542       7.836 -15.306  41.364  1.00 58.49           C  
ANISOU 4107  CG  TYR A 542     6928   7562   7734   -318   -350    733       C  
ATOM   4108  CD1 TYR A 542       8.258 -15.940  40.189  1.00 61.12           C  
ANISOU 4108  CD1 TYR A 542     7245   7870   8107   -296   -356    723       C  
ATOM   4109  CD2 TYR A 542       6.963 -15.996  42.214  1.00 58.90           C  
ANISOU 4109  CD2 TYR A 542     6978   7623   7775   -338   -358    754       C  
ATOM   4110  CE1 TYR A 542       7.828 -17.224  39.875  1.00 61.43           C  
ANISOU 4110  CE1 TYR A 542     7267   7894   8176   -293   -371    733       C  
ATOM   4111  CE2 TYR A 542       6.528 -17.276  41.909  1.00 60.01           C  
ANISOU 4111  CE2 TYR A 542     7103   7751   7947   -336   -373    766       C  
ATOM   4112  CZ  TYR A 542       6.958 -17.885  40.742  1.00 60.88           C  
ANISOU 4112  CZ  TYR A 542     7196   7835   8097   -313   -380    755       C  
ATOM   4113  OH  TYR A 542       6.518 -19.154  40.446  1.00 59.70           O  
ANISOU 4113  OH  TYR A 542     7030   7671   7979   -310   -395    766       O  
ATOM   4114  N   SER A 543       7.932 -10.575  41.001  1.00 47.50           N  
ANISOU 4114  N   SER A 543     5588   6213   6245   -295   -269    660       N  
ATOM   4115  CA  SER A 543       8.580  -9.304  41.267  1.00 45.26           C  
ANISOU 4115  CA  SER A 543     5319   5939   5937   -297   -258    649       C  
ATOM   4116  C   SER A 543       7.702  -8.091  40.936  1.00 44.18           C  
ANISOU 4116  C   SER A 543     5194   5815   5774   -285   -227    623       C  
ATOM   4117  O   SER A 543       8.140  -6.950  41.051  1.00 45.15           O  
ANISOU 4117  O   SER A 543     5329   5946   5878   -284   -215    610       O  
ATOM   4118  CB  SER A 543       9.897  -9.252  40.505  1.00 43.61           C  
ANISOU 4118  CB  SER A 543     5103   5710   5754   -282   -267    643       C  
ATOM   4119  OG  SER A 543      10.697  -8.200  40.984  1.00 46.83           O  
ANISOU 4119  OG  SER A 543     5524   6127   6142   -289   -262    639       O  
ATOM   4120  N   LEU A 544       6.458  -8.359  40.549  1.00 44.44           N  
ANISOU 4120  N   LEU A 544     5224   5851   5809   -277   -216    616       N  
ATOM   4121  CA  LEU A 544       5.497  -7.340  40.142  1.00 43.88           C  
ANISOU 4121  CA  LEU A 544     5161   5790   5720   -265   -189    592       C  
ATOM   4122  C   LEU A 544       5.000  -6.528  41.320  1.00 44.79           C  
ANISOU 4122  C   LEU A 544     5290   5929   5799   -285   -175    592       C  
ATOM   4123  O   LEU A 544       4.519  -7.090  42.293  1.00 48.03           O  
ANISOU 4123  O   LEU A 544     5699   6349   6198   -307   -180    609       O  
ATOM   4124  CB  LEU A 544       4.303  -8.004  39.446  1.00 42.41           C  
ANISOU 4124  CB  LEU A 544     4966   5599   5549   -253   -185    587       C  
ATOM   4125  CG  LEU A 544       3.317  -7.075  38.728  1.00 41.67           C  
ANISOU 4125  CG  LEU A 544     4876   5508   5446   -235   -161    561       C  
ATOM   4126  CD1 LEU A 544       3.906  -6.612  37.403  1.00 42.29           C  
ANISOU 4126  CD1 LEU A 544     4955   5571   5539   -210   -157    542       C  
ATOM   4127  CD2 LEU A 544       1.971  -7.749  38.497  1.00 41.68           C  
ANISOU 4127  CD2 LEU A 544     4869   5508   5456   -232   -157    562       C  
ATOM   4128  N   SER A 545       5.096  -5.207  41.223  1.00 45.71           N  
ANISOU 4128  N   SER A 545     5417   6052   5896   -279   -156    572       N  
ATOM   4129  CA  SER A 545       4.618  -4.330  42.292  1.00 46.40           C  
ANISOU 4129  CA  SER A 545     5517   6161   5949   -297   -139    568       C  
ATOM   4130  C   SER A 545       3.453  -3.439  41.857  1.00 46.06           C  
ANISOU 4130  C   SER A 545     5478   6125   5897   -284   -112    543       C  
ATOM   4131  O   SER A 545       2.702  -2.943  42.689  1.00 45.68           O  
ANISOU 4131  O   SER A 545     5436   6094   5826   -299    -96    539       O  
ATOM   4132  CB  SER A 545       5.760  -3.471  42.836  1.00 45.68           C  
ANISOU 4132  CB  SER A 545     5439   6076   5841   -307   -141    567       C  
ATOM   4133  OG  SER A 545       5.876  -2.278  42.089  1.00 47.83           O  
ANISOU 4133  OG  SER A 545     5717   6346   6110   -287   -123    542       O  
ATOM   4134  N   THR A 546       3.320  -3.228  40.552  1.00 48.48           N  
ANISOU 4134  N   THR A 546     5779   6417   6222   -257   -107    526       N  
ATOM   4135  CA  THR A 546       2.248  -2.395  40.006  1.00 47.05           C  
ANISOU 4135  CA  THR A 546     5600   6239   6038   -242    -85    504       C  
ATOM   4136  C   THR A 546       1.598  -3.055  38.791  1.00 45.40           C  
ANISOU 4136  C   THR A 546     5380   6014   5857   -221    -89    499       C  
ATOM   4137  O   THR A 546       2.275  -3.426  37.826  1.00 44.46           O  
ANISOU 4137  O   THR A 546     5256   5879   5757   -206   -101    498       O  
ATOM   4138  CB  THR A 546       2.746  -0.972  39.667  1.00 47.19           C  
ANISOU 4138  CB  THR A 546     5628   6257   6045   -232    -71    483       C  
ATOM   4139  OG1 THR A 546       3.182  -0.322  40.866  1.00 46.93           O  
ANISOU 4139  OG1 THR A 546     5606   6240   5985   -253    -66    486       O  
ATOM   4140  CG2 THR A 546       1.642  -0.141  39.040  1.00 49.38           C  
ANISOU 4140  CG2 THR A 546     5905   6533   6322   -216    -51    461       C  
ATOM   4141  N   LEU A 547       0.278  -3.210  38.875  1.00 44.96           N  
ANISOU 4141  N   LEU A 547     5318   5963   5801   -222    -78    495       N  
ATOM   4142  CA  LEU A 547      -0.542  -3.729  37.786  1.00 44.04           C  
ANISOU 4142  CA  LEU A 547     5191   5832   5707   -203    -80    489       C  
ATOM   4143  C   LEU A 547      -1.678  -2.737  37.524  1.00 43.31           C  
ANISOU 4143  C   LEU A 547     5101   5744   5610   -193    -59    469       C  
ATOM   4144  O   LEU A 547      -2.513  -2.482  38.398  1.00 42.72           O  
ANISOU 4144  O   LEU A 547     5026   5683   5522   -207    -45    467       O  
ATOM   4145  CB  LEU A 547      -1.105  -5.114  38.138  1.00 44.11           C  
ANISOU 4145  CB  LEU A 547     5189   5840   5729   -213    -93    509       C  
ATOM   4146  CG  LEU A 547      -1.311  -6.153  37.025  1.00 44.55           C  
ANISOU 4146  CG  LEU A 547     5234   5878   5815   -196   -107    512       C  
ATOM   4147  CD1 LEU A 547      -2.030  -7.385  37.557  1.00 45.59           C  
ANISOU 4147  CD1 LEU A 547     5354   6011   5955   -209   -117    530       C  
ATOM   4148  CD2 LEU A 547      -2.079  -5.592  35.845  1.00 43.54           C  
ANISOU 4148  CD2 LEU A 547     5105   5740   5696   -174    -97    491       C  
ATOM   4149  N   ASP A 548      -1.687  -2.170  36.320  1.00 42.69           N  
ANISOU 4149  N   ASP A 548     5024   5653   5543   -171    -56    452       N  
ATOM   4150  CA  ASP A 548      -2.692  -1.193  35.918  1.00 41.35           C  
ANISOU 4150  CA  ASP A 548     4855   5483   5372   -160    -38    433       C  
ATOM   4151  C   ASP A 548      -3.699  -1.806  34.947  1.00 40.36           C  
ANISOU 4151  C   ASP A 548     4719   5345   5269   -145    -43    430       C  
ATOM   4152  O   ASP A 548      -3.384  -2.053  33.783  1.00 40.26           O  
ANISOU 4152  O   ASP A 548     4706   5317   5271   -129    -54    427       O  
ATOM   4153  CB  ASP A 548      -2.016   0.028  35.293  1.00 41.30           C  
ANISOU 4153  CB  ASP A 548     4859   5473   5360   -147    -32    416       C  
ATOM   4154  CG  ASP A 548      -2.903   1.263  35.306  1.00 42.03           C  
ANISOU 4154  CG  ASP A 548     4953   5569   5446   -143    -12    397       C  
ATOM   4155  OD1 ASP A 548      -2.342   2.375  35.233  1.00 42.58           O  
ANISOU 4155  OD1 ASP A 548     5032   5640   5505   -139     -4    385       O  
ATOM   4156  OD2 ASP A 548      -4.145   1.132  35.390  1.00 40.31           O  
ANISOU 4156  OD2 ASP A 548     4726   5351   5235   -142     -5    394       O  
ATOM   4157  N   CYS A 549      -4.906  -2.074  35.434  1.00 40.04           N  
ANISOU 4157  N   CYS A 549     4670   5310   5231   -152    -35    432       N  
ATOM   4158  CA  CYS A 549      -5.943  -2.652  34.590  1.00 39.64           C  
ANISOU 4158  CA  CYS A 549     4609   5247   5203   -139    -40    430       C  
ATOM   4159  C   CYS A 549      -7.170  -1.761  34.497  1.00 38.98           C  
ANISOU 4159  C   CYS A 549     4523   5165   5122   -133    -23    413       C  
ATOM   4160  O   CYS A 549      -8.276  -2.233  34.220  1.00 39.01           O  
ANISOU 4160  O   CYS A 549     4515   5163   5142   -129    -24    413       O  
ATOM   4161  CB  CYS A 549      -6.316  -4.037  35.078  1.00 41.13           C  
ANISOU 4161  CB  CYS A 549     4788   5438   5401   -151    -51    449       C  
ATOM   4162  SG  CYS A 549      -5.067  -5.263  34.668  1.00 46.06           S  
ANISOU 4162  SG  CYS A 549     5411   6051   6036   -150    -76    466       S  
ATOM   4163  N   SER A 550      -6.948  -0.469  34.715  1.00 38.11           N  
ANISOU 4163  N   SER A 550     4421   5061   4999   -133     -8    399       N  
ATOM   4164  CA  SER A 550      -7.986   0.540  34.627  1.00 38.70           C  
ANISOU 4164  CA  SER A 550     4492   5134   5077   -127      7    381       C  
ATOM   4165  C   SER A 550      -8.479   0.770  33.209  1.00 39.50           C  
ANISOU 4165  C   SER A 550     4590   5217   5199   -105      0    371       C  
ATOM   4166  O   SER A 550      -7.837   0.368  32.232  1.00 38.55           O  
ANISOU 4166  O   SER A 550     4474   5085   5086    -93    -16    375       O  
ATOM   4167  CB  SER A 550      -7.488   1.855  35.208  1.00 38.99           C  
ANISOU 4167  CB  SER A 550     4538   5181   5094   -132     24    368       C  
ATOM   4168  OG  SER A 550      -6.295   2.244  34.580  1.00 38.88           O  
ANISOU 4168  OG  SER A 550     4536   5161   5075   -123     14    367       O  
ATOM   4169  N   PHE A 551      -9.639   1.417  33.118  1.00 39.96           N  
ANISOU 4169  N   PHE A 551     4642   5272   5269    -99     11    359       N  
ATOM   4170  CA  PHE A 551     -10.251   1.768  31.844  1.00 40.73           C  
ANISOU 4170  CA  PHE A 551     4736   5351   5386    -80      4    349       C  
ATOM   4171  C   PHE A 551     -10.333   0.590  30.880  1.00 41.89           C  
ANISOU 4171  C   PHE A 551     4880   5485   5549    -71    -16    360       C  
ATOM   4172  O   PHE A 551     -10.160   0.746  29.670  1.00 42.80           O  
ANISOU 4172  O   PHE A 551     5001   5587   5674    -57    -28    356       O  
ATOM   4173  CB  PHE A 551      -9.542   2.961  31.200  1.00 40.26           C  
ANISOU 4173  CB  PHE A 551     4689   5286   5320    -69      5    337       C  
ATOM   4174  CG  PHE A 551      -9.700   4.247  31.960  1.00 41.56           C  
ANISOU 4174  CG  PHE A 551     4854   5459   5475    -75     25    323       C  
ATOM   4175  CD1 PHE A 551      -8.700   4.683  32.833  1.00 41.26           C  
ANISOU 4175  CD1 PHE A 551     4826   5436   5413    -87     35    322       C  
ATOM   4176  CD2 PHE A 551     -10.843   5.034  31.798  1.00 42.68           C  
ANISOU 4176  CD2 PHE A 551     4988   5594   5633    -68     35    309       C  
ATOM   4177  CE1 PHE A 551      -8.837   5.876  33.530  1.00 41.98           C  
ANISOU 4177  CE1 PHE A 551     4919   5534   5495    -92     54    308       C  
ATOM   4178  CE2 PHE A 551     -10.988   6.230  32.494  1.00 43.12           C  
ANISOU 4178  CE2 PHE A 551     5043   5656   5682    -73     55    294       C  
ATOM   4179  CZ  PHE A 551      -9.984   6.650  33.360  1.00 44.31           C  
ANISOU 4179  CZ  PHE A 551     5205   5823   5808    -85     65    293       C  
ATOM   4180  N   ASN A 552     -10.589  -0.595  31.422  1.00 43.62           N  
ANISOU 4180  N   ASN A 552     5091   5709   5772    -81    -20    374       N  
ATOM   4181  CA  ASN A 552     -11.031  -1.705  30.596  1.00 44.80           C  
ANISOU 4181  CA  ASN A 552     5233   5846   5941    -73    -38    382       C  
ATOM   4182  C   ASN A 552     -12.529  -1.872  30.749  1.00 47.94           C  
ANISOU 4182  C   ASN A 552     5616   6241   6357    -73    -32    380       C  
ATOM   4183  O   ASN A 552     -13.244  -0.901  30.996  1.00 50.69           O  
ANISOU 4183  O   ASN A 552     5961   6590   6707    -73    -17    368       O  
ATOM   4184  CB  ASN A 552     -10.296  -2.990  30.958  1.00 43.13           C  
ANISOU 4184  CB  ASN A 552     5021   5639   5726    -83    -50    400       C  
ATOM   4185  CG  ASN A 552      -8.922  -3.060  30.340  1.00 41.73           C  
ANISOU 4185  CG  ASN A 552     4856   5457   5542    -77    -61    402       C  
ATOM   4186  OD1 ASN A 552      -8.741  -3.670  29.291  1.00 40.67           O  
ANISOU 4186  OD1 ASN A 552     4722   5309   5420    -67    -76    403       O  
ATOM   4187  ND2 ASN A 552      -7.948  -2.418  30.977  1.00 40.32           N  
ANISOU 4187  ND2 ASN A 552     4686   5288   5343    -85    -53    401       N  
ATOM   4188  N   ARG A 553     -13.004  -3.100  30.599  1.00 52.94           N  
ANISOU 4188  N   ARG A 553     6240   6869   7004    -75    -44    392       N  
ATOM   4189  CA  ARG A 553     -14.409  -3.402  30.829  1.00 56.96           C  
ANISOU 4189  CA  ARG A 553     6734   7376   7531    -76    -39    393       C  
ATOM   4190  C   ARG A 553     -14.536  -4.658  31.710  1.00 56.55           C  
ANISOU 4190  C   ARG A 553     6673   7333   7479    -92    -41    410       C  
ATOM   4191  O   ARG A 553     -15.438  -5.489  31.534  1.00 55.73           O  
ANISOU 4191  O   ARG A 553     6557   7223   7394    -91    -48    417       O  
ATOM   4192  CB  ARG A 553     -15.143  -3.518  29.485  1.00 62.11           C  
ANISOU 4192  CB  ARG A 553     7382   8008   8208    -59    -54    388       C  
ATOM   4193  CG  ARG A 553     -15.212  -2.194  28.731  1.00 67.25           C  
ANISOU 4193  CG  ARG A 553     8040   8650   8861    -46    -51    371       C  
ATOM   4194  CD  ARG A 553     -16.052  -2.275  27.468  1.00 76.70           C  
ANISOU 4194  CD  ARG A 553     9232   9827  10081    -31    -67    368       C  
ATOM   4195  NE  ARG A 553     -15.243  -2.463  26.264  1.00 84.81           N  
ANISOU 4195  NE  ARG A 553    10274  10844  11105    -21    -86    368       N  
ATOM   4196  CZ  ARG A 553     -15.731  -2.504  25.024  1.00 90.52           C  
ANISOU 4196  CZ  ARG A 553    10998  11549  11843     -9   -102    365       C  
ATOM   4197  NH1 ARG A 553     -17.039  -2.376  24.798  1.00 87.80           N  
ANISOU 4197  NH1 ARG A 553    10642  11195  11522     -4   -104    362       N  
ATOM   4198  NH2 ARG A 553     -14.904  -2.674  24.002  1.00 93.19           N  
ANISOU 4198  NH2 ARG A 553    11351  11879  12175     -2   -116    365       N  
ATOM   4199  N   ILE A 554     -13.607  -4.769  32.661  1.00 54.51           N  
ANISOU 4199  N   ILE A 554     6422   7090   7198   -107    -36    418       N  
ATOM   4200  CA  ILE A 554     -13.500  -5.914  33.567  1.00 53.38           C  
ANISOU 4200  CA  ILE A 554     6273   6956   7050   -125    -40    437       C  
ATOM   4201  C   ILE A 554     -14.752  -6.061  34.432  1.00 51.20           C  
ANISOU 4201  C   ILE A 554     5984   6689   6780   -137    -25    438       C  
ATOM   4202  O   ILE A 554     -15.139  -5.134  35.150  1.00 45.71           O  
ANISOU 4202  O   ILE A 554     5289   6004   6074   -145     -3    427       O  
ATOM   4203  CB  ILE A 554     -12.220  -5.836  34.449  1.00 51.85           C  
ANISOU 4203  CB  ILE A 554     6091   6777   6831   -140    -38    445       C  
ATOM   4204  CG1 ILE A 554     -10.964  -5.846  33.568  1.00 52.09           C  
ANISOU 4204  CG1 ILE A 554     6133   6799   6860   -128    -54    445       C  
ATOM   4205  CG2 ILE A 554     -12.154  -6.997  35.439  1.00 50.60           C  
ANISOU 4205  CG2 ILE A 554     5927   6629   6668   -160    -44    467       C  
ATOM   4206  CD1 ILE A 554      -9.716  -5.319  34.245  1.00 49.87           C  
ANISOU 4206  CD1 ILE A 554     5864   6529   6555   -138    -50    447       C  
ATOM   4207  N   GLU A 555     -15.376  -7.235  34.334  1.00 52.33           N  
ANISOU 4207  N   GLU A 555     6115   6826   6940   -139    -36    451       N  
ATOM   4208  CA  GLU A 555     -16.540  -7.580  35.146  1.00 55.85           C  
ANISOU 4208  CA  GLU A 555     6548   7279   7392   -152    -23    455       C  
ATOM   4209  C   GLU A 555     -16.121  -8.288  36.438  1.00 57.78           C  
ANISOU 4209  C   GLU A 555     6793   7540   7617   -177    -20    473       C  
ATOM   4210  O   GLU A 555     -16.611  -7.931  37.508  1.00 59.41           O  
ANISOU 4210  O   GLU A 555     6999   7763   7812   -195      0    470       O  
ATOM   4211  CB  GLU A 555     -17.548  -8.402  34.339  1.00 55.64           C  
ANISOU 4211  CB  GLU A 555     6507   7236   7396   -141    -36    458       C  
ATOM   4212  CG  GLU A 555     -18.229  -7.594  33.246  1.00 57.21           C  
ANISOU 4212  CG  GLU A 555     6703   7419   7613   -120    -36    440       C  
ATOM   4213  CD  GLU A 555     -19.161  -8.409  32.372  1.00 60.73           C  
ANISOU 4213  CD  GLU A 555     7136   7847   8089   -108    -52    444       C  
ATOM   4214  OE1 GLU A 555     -18.847  -9.569  32.048  1.00 63.59           O  
ANISOU 4214  OE1 GLU A 555     7498   8204   8459   -108    -71    459       O  
ATOM   4215  OE2 GLU A 555     -20.220  -7.878  31.991  1.00 64.70           O  
ANISOU 4215  OE2 GLU A 555     7629   8341   8611   -100    -46    433       O  
ATOM   4216  N   THR A 556     -15.234  -9.285  36.328  1.00 57.57           N  
ANISOU 4216  N   THR A 556     6771   7512   7590   -180    -41    491       N  
ATOM   4217  CA  THR A 556     -14.456  -9.818  37.468  1.00 59.48           C  
ANISOU 4217  CA  THR A 556     7018   7769   7810   -204    -43    509       C  
ATOM   4218  C   THR A 556     -13.127 -10.411  37.047  1.00 57.46           C  
ANISOU 4218  C   THR A 556     6769   7506   7554   -199    -67    521       C  
ATOM   4219  O   THR A 556     -12.741 -10.351  35.885  1.00 56.72           O  
ANISOU 4219  O   THR A 556     6678   7397   7474   -179    -79    513       O  
ATOM   4220  CB  THR A 556     -15.155 -10.958  38.250  1.00 61.90           C  
ANISOU 4220  CB  THR A 556     7313   8081   8122   -222    -46    528       C  
ATOM   4221  OG1 THR A 556     -15.673 -11.937  37.340  1.00 57.89           O  
ANISOU 4221  OG1 THR A 556     6794   7556   7644   -208    -64    534       O  
ATOM   4222  CG2 THR A 556     -16.239 -10.422  39.164  1.00 64.98           C  
ANISOU 4222  CG2 THR A 556     7699   8486   8504   -237    -18    520       C  
ATOM   4223  N   SER A 557     -12.443 -10.992  38.027  1.00 58.96           N  
ANISOU 4223  N   SER A 557     6964   7708   7730   -221    -73    540       N  
ATOM   4224  CA  SER A 557     -11.289 -11.841  37.797  1.00 59.95           C  
ANISOU 4224  CA  SER A 557     7091   7825   7860   -220    -97    556       C  
ATOM   4225  C   SER A 557     -11.642 -13.271  38.189  1.00 60.24           C  
ANISOU 4225  C   SER A 557     7117   7860   7910   -233   -113    579       C  
ATOM   4226  O   SER A 557     -11.981 -13.538  39.343  1.00 62.51           O  
ANISOU 4226  O   SER A 557     7403   8162   8184   -257   -106    592       O  
ATOM   4227  CB  SER A 557     -10.085 -11.352  38.603  1.00 56.59           C  
ANISOU 4227  CB  SER A 557     6680   7413   7409   -235    -96    561       C  
ATOM   4228  OG  SER A 557      -9.112 -12.369  38.699  1.00 55.80           O  
ANISOU 4228  OG  SER A 557     6579   7307   7315   -242   -120    582       O  
ATOM   4229  N   LYS A 558     -11.565 -14.180  37.225  1.00 58.79           N  
ANISOU 4229  N   LYS A 558     6925   7658   7753   -218   -133    584       N  
ATOM   4230  CA  LYS A 558     -11.813 -15.588  37.484  1.00 64.68           C  
ANISOU 4230  CA  LYS A 558     7660   8400   8516   -228   -150    606       C  
ATOM   4231  C   LYS A 558     -10.526 -16.366  37.821  1.00 71.33           C  
ANISOU 4231  C   LYS A 558     8504   9239   9358   -239   -172    626       C  
ATOM   4232  O   LYS A 558      -9.419 -15.930  37.487  1.00 74.00           O  
ANISOU 4232  O   LYS A 558     8851   9574   9692   -231   -177    620       O  
ATOM   4233  CB  LYS A 558     -12.562 -16.225  36.304  1.00 65.57           C  
ANISOU 4233  CB  LYS A 558     7760   8493   8659   -208   -160    600       C  
ATOM   4234  CG  LYS A 558     -11.966 -15.960  34.926  1.00 64.13           C  
ANISOU 4234  CG  LYS A 558     7583   8294   8490   -183   -169    584       C  
ATOM   4235  CD  LYS A 558     -12.539 -16.908  33.874  1.00 63.82           C  
ANISOU 4235  CD  LYS A 558     7531   8234   8480   -168   -185    584       C  
ATOM   4236  CE  LYS A 558     -13.510 -16.234  32.911  1.00 60.93           C  
ANISOU 4236  CE  LYS A 558     7165   7860   8123   -149   -176    563       C  
ATOM   4237  NZ  LYS A 558     -14.706 -15.644  33.568  1.00 60.22           N  
ANISOU 4237  NZ  LYS A 558     7071   7783   8027   -157   -156    559       N  
ATOM   4238  N   GLY A 559     -10.684 -17.489  38.527  1.00 76.48           N  
ANISOU 4238  N   GLY A 559     9147   9892  10017   -257   -185    650       N  
ATOM   4239  CA  GLY A 559      -9.623 -18.493  38.691  1.00 76.15           C  
ANISOU 4239  CA  GLY A 559     9103   9843   9986   -264   -211    671       C  
ATOM   4240  C   GLY A 559      -8.588 -18.346  39.798  1.00 79.34           C  
ANISOU 4240  C   GLY A 559     9516  10259  10368   -287   -216    687       C  
ATOM   4241  O   GLY A 559      -7.396 -18.196  39.511  1.00 85.26           O  
ANISOU 4241  O   GLY A 559    10271  11002  11120   -281   -227    686       O  
ATOM   4242  N   ILE A 560      -9.038 -18.418  41.052  1.00 78.53           N  
ANISOU 4242  N   ILE A 560     9417  10176  10245   -314   -209    702       N  
ATOM   4243  CA  ILE A 560      -8.159 -18.453  42.247  1.00 79.29           C  
ANISOU 4243  CA  ILE A 560     9522  10285  10319   -341   -217    722       C  
ATOM   4244  C   ILE A 560      -7.352 -17.180  42.484  1.00 75.81           C  
ANISOU 4244  C   ILE A 560     9097   9854   9851   -342   -204    708       C  
ATOM   4245  O   ILE A 560      -6.367 -16.898  41.794  1.00 73.16           O  
ANISOU 4245  O   ILE A 560     8765   9507   9524   -326   -212    700       O  
ATOM   4246  CB  ILE A 560      -7.239 -19.708  42.286  1.00 83.23           C  
ANISOU 4246  CB  ILE A 560    10013  10770  10841   -348   -251    748       C  
ATOM   4247  CG1 ILE A 560      -8.061 -20.978  42.553  1.00 84.96           C  
ANISOU 4247  CG1 ILE A 560    10218  10984  11078   -359   -263    769       C  
ATOM   4248  CG2 ILE A 560      -6.130 -19.556  43.328  1.00 82.97           C  
ANISOU 4248  CG2 ILE A 560     9991  10747  10786   -372   -261    766       C  
ATOM   4249  CD1 ILE A 560      -8.503 -21.178  43.989  1.00 84.37           C  
ANISOU 4249  CD1 ILE A 560    10148  10930  10977   -394   -259    791       C  
ATOM   4250  N   LEU A 561      -7.766 -16.444  43.508  1.00 72.50           N  
ANISOU 4250  N   LEU A 561     8689   9457   9400   -362   -183    706       N  
ATOM   4251  CA  LEU A 561      -7.322 -15.079  43.733  1.00 71.51           C  
ANISOU 4251  CA  LEU A 561     8579   9344   9247   -362   -164    688       C  
ATOM   4252  C   LEU A 561      -6.077 -14.956  44.623  1.00 75.00           C  
ANISOU 4252  C   LEU A 561     9032   9793   9668   -383   -177    704       C  
ATOM   4253  O   LEU A 561      -5.563 -13.851  44.830  1.00 75.58           O  
ANISOU 4253  O   LEU A 561     9120   9877   9720   -384   -164    690       O  
ATOM   4254  CB  LEU A 561      -8.487 -14.248  44.293  1.00 70.54           C  
ANISOU 4254  CB  LEU A 561     8459   9238   9101   -371   -132    673       C  
ATOM   4255  CG  LEU A 561      -9.715 -13.867  43.436  1.00 69.35           C  
ANISOU 4255  CG  LEU A 561     8300   9082   8967   -349   -114    649       C  
ATOM   4256  CD1 LEU A 561      -9.357 -12.847  42.365  1.00 70.75           C  
ANISOU 4256  CD1 LEU A 561     8481   9249   9150   -320   -106    623       C  
ATOM   4257  CD2 LEU A 561     -10.444 -15.055  42.813  1.00 68.64           C  
ANISOU 4257  CD2 LEU A 561     8193   8977   8909   -339   -128    659       C  
ATOM   4258  N   GLN A 562      -5.595 -16.086  45.144  1.00 78.83           N  
ANISOU 4258  N   GLN A 562     9513  10275  10161   -401   -203    733       N  
ATOM   4259  CA  GLN A 562      -4.344 -16.118  45.919  1.00 78.43           C  
ANISOU 4259  CA  GLN A 562     9473  10229  10098   -421   -221    752       C  
ATOM   4260  C   GLN A 562      -3.152 -15.957  44.992  1.00 70.12           C  
ANISOU 4260  C   GLN A 562     8418   9158   9065   -398   -235    744       C  
ATOM   4261  O   GLN A 562      -2.115 -15.434  45.387  1.00 67.45           O  
ANISOU 4261  O   GLN A 562     8091   8824   8713   -406   -241    747       O  
ATOM   4262  CB  GLN A 562      -4.200 -17.439  46.679  1.00 84.16           C  
ANISOU 4262  CB  GLN A 562    10192  10953  10831   -446   -248    787       C  
ATOM   4263  CG  GLN A 562      -4.952 -17.520  47.999  1.00 88.11           C  
ANISOU 4263  CG  GLN A 562    10700  11476  11299   -481   -238    802       C  
ATOM   4264  CD  GLN A 562      -4.815 -18.882  48.669  1.00 89.98           C  
ANISOU 4264  CD  GLN A 562    10931  11710  11547   -505   -267    839       C  
ATOM   4265  OE1 GLN A 562      -5.806 -19.477  49.093  1.00 90.46           O  
ANISOU 4265  OE1 GLN A 562    10986  11778  11606   -520   -263    849       O  
ATOM   4266  NE2 GLN A 562      -3.584 -19.384  48.762  1.00 88.33           N  
ANISOU 4266  NE2 GLN A 562    10720  11488  11350   -511   -298    859       N  
ATOM   4267  N   HIS A 563      -3.341 -16.419  43.759  1.00 67.77           N  
ANISOU 4267  N   HIS A 563     8108   8841   8801   -370   -241    734       N  
ATOM   4268  CA  HIS A 563      -2.343 -16.427  42.691  1.00 68.68           C  
ANISOU 4268  CA  HIS A 563     8217   8935   8940   -346   -253    725       C  
ATOM   4269  C   HIS A 563      -1.742 -15.086  42.335  1.00 64.83           C  
ANISOU 4269  C   HIS A 563     7742   8451   8436   -333   -236    701       C  
ATOM   4270  O   HIS A 563      -0.645 -15.035  41.773  1.00 65.27           O  
ANISOU 4270  O   HIS A 563     7798   8494   8506   -321   -248    698       O  
ATOM   4271  CB  HIS A 563      -2.946 -17.083  41.444  1.00 75.56           C  
ANISOU 4271  CB  HIS A 563     9075   9788   9846   -320   -256    714       C  
ATOM   4272  CG  HIS A 563      -2.678 -18.572  41.334  1.00 81.02           C  
ANISOU 4272  CG  HIS A 563     9751  10463  10570   -324   -285    737       C  
ATOM   4273  ND1 HIS A 563      -2.520 -19.194  40.146  1.00 81.18           N  
ANISOU 4273  ND1 HIS A 563     9759  10460  10624   -300   -295    729       N  
ATOM   4274  CD2 HIS A 563      -2.521 -19.554  42.316  1.00 82.35           C  
ANISOU 4274  CD2 HIS A 563     9914  10633  10741   -349   -306    769       C  
ATOM   4275  CE1 HIS A 563      -2.283 -20.503  40.352  1.00 80.84           C  
ANISOU 4275  CE1 HIS A 563     9702  10404  10607   -310   -321    753       C  
ATOM   4276  NE2 HIS A 563      -2.282 -20.723  41.680  1.00 85.90           N  
ANISOU 4276  NE2 HIS A 563    10348  11060  11229   -340   -329    778       N  
ATOM   4277  N   PHE A 564      -2.445 -13.994  42.636  1.00 61.41           N  
ANISOU 4277  N   PHE A 564     7320   8035   7975   -335   -209    684       N  
ATOM   4278  CA  PHE A 564      -1.882 -12.658  42.458  1.00 60.39           C  
ANISOU 4278  CA  PHE A 564     7204   7911   7828   -326   -194    663       C  
ATOM   4279  C   PHE A 564      -0.653 -12.517  43.347  1.00 62.64           C  
ANISOU 4279  C   PHE A 564     7498   8203   8097   -346   -207    679       C  
ATOM   4280  O   PHE A 564      -0.687 -12.913  44.514  1.00 64.54           O  
ANISOU 4280  O   PHE A 564     7743   8456   8322   -375   -214    700       O  
ATOM   4281  CB  PHE A 564      -2.905 -11.559  42.765  1.00 61.99           C  
ANISOU 4281  CB  PHE A 564     7415   8132   8005   -328   -163    643       C  
ATOM   4282  CG  PHE A 564      -3.834 -11.251  41.618  1.00 61.77           C  
ANISOU 4282  CG  PHE A 564     7380   8094   7993   -301   -148    621       C  
ATOM   4283  CD1 PHE A 564      -5.170 -11.645  41.661  1.00 64.47           C  
ANISOU 4283  CD1 PHE A 564     7714   8439   8341   -303   -139    620       C  
ATOM   4284  CD2 PHE A 564      -3.376 -10.572  40.493  1.00 60.54           C  
ANISOU 4284  CD2 PHE A 564     7227   7926   7847   -275   -145    600       C  
ATOM   4285  CE1 PHE A 564      -6.030 -11.369  40.605  1.00 63.27           C  
ANISOU 4285  CE1 PHE A 564     7555   8277   8205   -279   -128    600       C  
ATOM   4286  CE2 PHE A 564      -4.228 -10.296  39.434  1.00 60.67           C  
ANISOU 4286  CE2 PHE A 564     7238   7934   7878   -252   -134    581       C  
ATOM   4287  CZ  PHE A 564      -5.556 -10.695  39.489  1.00 62.61           C  
ANISOU 4287  CZ  PHE A 564     7475   8182   8130   -254   -126    581       C  
ATOM   4288  N   PRO A 565       0.440 -11.958  42.791  1.00 63.65           N  
ANISOU 4288  N   PRO A 565     7630   8322   8231   -332   -211    669       N  
ATOM   4289  CA  PRO A 565       1.753 -11.949  43.436  1.00 61.68           C  
ANISOU 4289  CA  PRO A 565     7386   8072   7975   -348   -228    684       C  
ATOM   4290  C   PRO A 565       1.730 -11.299  44.812  1.00 60.99           C  
ANISOU 4290  C   PRO A 565     7314   8008   7848   -377   -220    692       C  
ATOM   4291  O   PRO A 565       1.009 -10.326  45.025  1.00 60.40           O  
ANISOU 4291  O   PRO A 565     7249   7949   7749   -378   -193    673       O  
ATOM   4292  CB  PRO A 565       2.607 -11.110  42.480  1.00 62.42           C  
ANISOU 4292  CB  PRO A 565     7483   8155   8076   -324   -223    663       C  
ATOM   4293  CG  PRO A 565       1.892 -11.153  41.175  1.00 60.43           C  
ANISOU 4293  CG  PRO A 565     7223   7891   7844   -296   -212    643       C  
ATOM   4294  CD  PRO A 565       0.446 -11.181  41.539  1.00 62.16           C  
ANISOU 4294  CD  PRO A 565     7441   8123   8051   -302   -196    641       C  
ATOM   4295  N   LYS A 566       2.521 -11.845  45.731  1.00 63.37           N  
ANISOU 4295  N   LYS A 566     7618   8312   8145   -402   -242    718       N  
ATOM   4296  CA  LYS A 566       2.613 -11.333  47.101  1.00 65.70           C  
ANISOU 4296  CA  LYS A 566     7929   8629   8402   -433   -238    728       C  
ATOM   4297  C   LYS A 566       3.158  -9.915  47.077  1.00 62.09           C  
ANISOU 4297  C   LYS A 566     7486   8180   7923   -427   -221    707       C  
ATOM   4298  O   LYS A 566       2.816  -9.079  47.917  1.00 60.59           O  
ANISOU 4298  O   LYS A 566     7311   8010   7698   -445   -202    700       O  
ATOM   4299  CB  LYS A 566       3.537 -12.221  47.943  1.00 71.33           C  
ANISOU 4299  CB  LYS A 566     8642   9339   9119   -459   -272    762       C  
ATOM   4300  CG  LYS A 566       3.451 -13.719  47.660  1.00 77.28           C  
ANISOU 4300  CG  LYS A 566     9378  10076   9908   -458   -298    785       C  
ATOM   4301  CD  LYS A 566       2.170 -14.346  48.204  1.00 81.87           C  
ANISOU 4301  CD  LYS A 566     9957  10669  10480   -474   -291    795       C  
ATOM   4302  CE  LYS A 566       1.092 -14.488  47.137  1.00 79.90           C  
ANISOU 4302  CE  LYS A 566     9695  10411  10249   -447   -274    775       C  
ATOM   4303  NZ  LYS A 566      -0.259 -14.655  47.740  1.00 81.71           N  
ANISOU 4303  NZ  LYS A 566     9926  10657  10460   -463   -257    777       N  
ATOM   4304  N   SER A 567       4.001  -9.673  46.079  1.00 60.63           N  
ANISOU 4304  N   SER A 567     7297   7978   7761   -402   -226    695       N  
ATOM   4305  CA  SER A 567       4.694  -8.413  45.877  1.00 59.50           C  
ANISOU 4305  CA  SER A 567     7164   7837   7605   -393   -214    676       C  
ATOM   4306  C   SER A 567       3.771  -7.291  45.401  1.00 58.54           C  
ANISOU 4306  C   SER A 567     7048   7724   7469   -376   -181    645       C  
ATOM   4307  O   SER A 567       4.083  -6.107  45.572  1.00 58.09           O  
ANISOU 4307  O   SER A 567     7004   7676   7391   -376   -166    629       O  
ATOM   4308  CB  SER A 567       5.817  -8.632  44.865  1.00 60.48           C  
ANISOU 4308  CB  SER A 567     7279   7937   7761   -371   -230    673       C  
ATOM   4309  OG  SER A 567       5.404  -9.557  43.870  1.00 61.68           O  
ANISOU 4309  OG  SER A 567     7415   8072   7946   -351   -236    673       O  
ATOM   4310  N   LEU A 568       2.636  -7.669  44.816  1.00 55.81           N  
ANISOU 4310  N   LEU A 568     6693   7375   7135   -363   -170    637       N  
ATOM   4311  CA  LEU A 568       1.700  -6.712  44.234  1.00 53.04           C  
ANISOU 4311  CA  LEU A 568     6345   7028   6778   -346   -142    608       C  
ATOM   4312  C   LEU A 568       1.191  -5.670  45.231  1.00 54.86           C  
ANISOU 4312  C   LEU A 568     6589   7281   6972   -364   -118    598       C  
ATOM   4313  O   LEU A 568       0.298  -5.943  46.037  1.00 54.94           O  
ANISOU 4313  O   LEU A 568     6600   7305   6967   -383   -109    604       O  
ATOM   4314  CB  LEU A 568       0.537  -7.447  43.577  1.00 49.78           C  
ANISOU 4314  CB  LEU A 568     5918   6608   6386   -333   -138    606       C  
ATOM   4315  CG  LEU A 568      -0.538  -6.604  42.904  1.00 47.60           C  
ANISOU 4315  CG  LEU A 568     5643   6334   6110   -314   -112    579       C  
ATOM   4316  CD1 LEU A 568       0.092  -5.570  41.978  1.00 48.51           C  
ANISOU 4316  CD1 LEU A 568     5763   6440   6229   -291   -105    557       C  
ATOM   4317  CD2 LEU A 568      -1.495  -7.522  42.159  1.00 46.24           C  
ANISOU 4317  CD2 LEU A 568     5455   6150   5963   -300   -116    580       C  
ATOM   4318  N   ALA A 569       1.765  -4.470  45.144  1.00 56.55           N  
ANISOU 4318  N   ALA A 569     6813   7498   7173   -357   -106    580       N  
ATOM   4319  CA  ALA A 569       1.446  -3.364  46.053  1.00 55.68           C  
ANISOU 4319  CA  ALA A 569     6718   7409   7029   -374    -83    567       C  
ATOM   4320  C   ALA A 569       0.356  -2.409  45.543  1.00 54.98           C  
ANISOU 4320  C   ALA A 569     6627   7322   6938   -357    -54    538       C  
ATOM   4321  O   ALA A 569      -0.425  -1.888  46.342  1.00 53.11           O  
ANISOU 4321  O   ALA A 569     6396   7102   6680   -373    -32    529       O  
ATOM   4322  CB  ALA A 569       2.709  -2.593  46.407  1.00 52.39           C  
ANISOU 4322  CB  ALA A 569     6312   6994   6596   -380    -89    567       C  
ATOM   4323  N   PHE A 570       0.318  -2.181  44.226  1.00 55.74           N  
ANISOU 4323  N   PHE A 570     6716   7401   7059   -326    -53    524       N  
ATOM   4324  CA  PHE A 570      -0.641  -1.260  43.598  1.00 55.15           C  
ANISOU 4324  CA  PHE A 570     6640   7326   6989   -308    -29    497       C  
ATOM   4325  C   PHE A 570      -1.366  -1.922  42.431  1.00 54.65           C  
ANISOU 4325  C   PHE A 570     6562   7246   6955   -285    -33    494       C  
ATOM   4326  O   PHE A 570      -0.805  -2.068  41.342  1.00 55.28           O  
ANISOU 4326  O   PHE A 570     6638   7309   7054   -264    -45    492       O  
ATOM   4327  CB  PHE A 570       0.057  -0.001  43.082  1.00 59.06           C  
ANISOU 4327  CB  PHE A 570     7143   7817   7479   -293    -21    478       C  
ATOM   4328  CG  PHE A 570       0.701   0.834  44.152  1.00 65.20           C  
ANISOU 4328  CG  PHE A 570     7934   8609   8226   -313    -13    476       C  
ATOM   4329  CD1 PHE A 570       2.008   0.578  44.569  1.00 65.59           C  
ANISOU 4329  CD1 PHE A 570     7990   8659   8269   -325    -33    492       C  
ATOM   4330  CD2 PHE A 570       0.018   1.908  44.717  1.00 68.58           C  
ANISOU 4330  CD2 PHE A 570     8370   9052   8636   -320     12    456       C  
ATOM   4331  CE1 PHE A 570       2.611   1.358  45.547  1.00 68.27           C  
ANISOU 4331  CE1 PHE A 570     8345   9013   8581   -344    -28    491       C  
ATOM   4332  CE2 PHE A 570       0.618   2.693  45.696  1.00 70.02           C  
ANISOU 4332  CE2 PHE A 570     8566   9248   8790   -340     19    453       C  
ATOM   4333  CZ  PHE A 570       1.915   2.417  46.110  1.00 69.51           C  
ANISOU 4333  CZ  PHE A 570     8509   9184   8717   -352     -1    471       C  
ATOM   4334  N   PHE A 571      -2.615  -2.311  42.659  1.00 52.98           N  
ANISOU 4334  N   PHE A 571     6342   7039   6746   -290    -23    494       N  
ATOM   4335  CA  PHE A 571      -3.417  -2.953  41.636  1.00 50.88           C  
ANISOU 4335  CA  PHE A 571     6064   6759   6509   -270    -28    492       C  
ATOM   4336  C   PHE A 571      -4.592  -2.053  41.284  1.00 52.52           C  
ANISOU 4336  C   PHE A 571     6267   6967   6719   -258     -4    468       C  
ATOM   4337  O   PHE A 571      -5.608  -2.075  41.967  1.00 57.58           O  
ANISOU 4337  O   PHE A 571     6905   7619   7354   -271     11    466       O  
ATOM   4338  CB  PHE A 571      -3.927  -4.303  42.148  1.00 48.35           C  
ANISOU 4338  CB  PHE A 571     5733   6440   6194   -285    -39    514       C  
ATOM   4339  CG  PHE A 571      -4.607  -5.150  41.098  1.00 46.41           C  
ANISOU 4339  CG  PHE A 571     5474   6179   5979   -266    -48    515       C  
ATOM   4340  CD1 PHE A 571      -4.754  -4.704  39.783  1.00 45.91           C  
ANISOU 4340  CD1 PHE A 571     5408   6100   5935   -238    -47    498       C  
ATOM   4341  CD2 PHE A 571      -5.122  -6.393  41.437  1.00 44.04           C  
ANISOU 4341  CD2 PHE A 571     5165   5879   5689   -277    -59    535       C  
ATOM   4342  CE1 PHE A 571      -5.384  -5.488  38.833  1.00 44.37           C  
ANISOU 4342  CE1 PHE A 571     5202   5890   5766   -222    -56    499       C  
ATOM   4343  CE2 PHE A 571      -5.755  -7.181  40.490  1.00 44.17           C  
ANISOU 4343  CE2 PHE A 571     5168   5879   5733   -260    -68    536       C  
ATOM   4344  CZ  PHE A 571      -5.886  -6.726  39.188  1.00 44.44           C  
ANISOU 4344  CZ  PHE A 571     5201   5899   5785   -233    -67    517       C  
ATOM   4345  N   ASN A 572      -4.459  -1.272  40.215  1.00 53.40           N  
ANISOU 4345  N   ASN A 572     6380   7066   6842   -234     -1    451       N  
ATOM   4346  CA  ASN A 572      -5.524  -0.357  39.797  1.00 53.40           C  
ANISOU 4346  CA  ASN A 572     6376   7063   6848   -221     18    428       C  
ATOM   4347  C   ASN A 572      -6.614  -1.048  38.985  1.00 52.52           C  
ANISOU 4347  C   ASN A 572     6251   6940   6763   -207     14    428       C  
ATOM   4348  O   ASN A 572      -6.333  -1.701  37.977  1.00 52.06           O  
ANISOU 4348  O   ASN A 572     6189   6866   6723   -192     -3    434       O  
ATOM   4349  CB  ASN A 572      -4.947   0.829  39.016  1.00 55.70           C  
ANISOU 4349  CB  ASN A 572     6675   7347   7140   -203     22    410       C  
ATOM   4350  CG  ASN A 572      -5.971   1.927  38.760  1.00 57.24           C  
ANISOU 4350  CG  ASN A 572     6867   7540   7339   -193     43    387       C  
ATOM   4351  OD1 ASN A 572      -7.162   1.667  38.561  1.00 54.86           O  
ANISOU 4351  OD1 ASN A 572     6554   7234   7053   -189     49    383       O  
ATOM   4352  ND2 ASN A 572      -5.503   3.167  38.751  1.00 56.59           N  
ANISOU 4352  ND2 ASN A 572     6794   7460   7247   -189     53    372       N  
ATOM   4353  N   LEU A 573      -7.858  -0.885  39.426  1.00 51.29           N  
ANISOU 4353  N   LEU A 573     6087   6790   6608   -213     32    420       N  
ATOM   4354  CA  LEU A 573      -9.001  -1.476  38.737  1.00 52.17           C  
ANISOU 4354  CA  LEU A 573     6185   6890   6745   -201     29    420       C  
ATOM   4355  C   LEU A 573     -10.136  -0.482  38.501  1.00 52.81           C  
ANISOU 4355  C   LEU A 573     6259   6968   6836   -192     49    397       C  
ATOM   4356  O   LEU A 573     -11.216  -0.867  38.039  1.00 55.06           O  
ANISOU 4356  O   LEU A 573     6532   7244   7143   -183     49    395       O  
ATOM   4357  CB  LEU A 573      -9.513  -2.713  39.492  1.00 52.61           C  
ANISOU 4357  CB  LEU A 573     6233   6954   6803   -219     25    439       C  
ATOM   4358  CG  LEU A 573      -8.748  -4.026  39.266  1.00 52.90           C  
ANISOU 4358  CG  LEU A 573     6269   6984   6846   -221     -1    462       C  
ATOM   4359  CD1 LEU A 573      -9.211  -5.107  40.228  1.00 52.45           C  
ANISOU 4359  CD1 LEU A 573     6205   6937   6785   -243     -4    482       C  
ATOM   4360  CD2 LEU A 573      -8.867  -4.516  37.830  1.00 50.95           C  
ANISOU 4360  CD2 LEU A 573     6014   6716   6627   -196    -18    461       C  
ATOM   4361  N   THR A 574      -9.880   0.792  38.802  1.00 51.00           N  
ANISOU 4361  N   THR A 574     6038   6745   6593   -192     66    381       N  
ATOM   4362  CA  THR A 574     -10.863   1.866  38.631  1.00 51.11           C  
ANISOU 4362  CA  THR A 574     6046   6755   6618   -184     86    358       C  
ATOM   4363  C   THR A 574     -11.278   2.035  37.170  1.00 50.72           C  
ANISOU 4363  C   THR A 574     5991   6684   6596   -157     74    351       C  
ATOM   4364  O   THR A 574     -10.554   1.621  36.267  1.00 49.82           O  
ANISOU 4364  O   THR A 574     5882   6560   6487   -145     54    359       O  
ATOM   4365  CB  THR A 574     -10.315   3.215  39.125  1.00 53.39           C  
ANISOU 4365  CB  THR A 574     6345   7051   6886   -188    102    342       C  
ATOM   4366  OG1 THR A 574      -9.361   3.718  38.179  1.00 58.88           O  
ANISOU 4366  OG1 THR A 574     7050   7736   7584   -171     89    339       O  
ATOM   4367  CG2 THR A 574      -9.651   3.072  40.491  1.00 53.20           C  
ANISOU 4367  CG2 THR A 574     6331   7048   6831   -215    109    350       C  
ATOM   4368  N   ASN A 575     -12.441   2.652  36.953  1.00 50.97           N  
ANISOU 4368  N   ASN A 575     6011   6708   6645   -149     88    335       N  
ATOM   4369  CA  ASN A 575     -13.013   2.887  35.612  1.00 50.29           C  
ANISOU 4369  CA  ASN A 575     5919   6601   6586   -126     77    327       C  
ATOM   4370  C   ASN A 575     -13.240   1.617  34.783  1.00 48.96           C  
ANISOU 4370  C   ASN A 575     5744   6421   6435   -117     54    343       C  
ATOM   4371  O   ASN A 575     -13.021   1.591  33.569  1.00 49.17           O  
ANISOU 4371  O   ASN A 575     5774   6432   6474   -100     37    343       O  
ATOM   4372  CB  ASN A 575     -12.200   3.935  34.836  1.00 50.47           C  
ANISOU 4372  CB  ASN A 575     5953   6616   6606   -112     72    317       C  
ATOM   4373  CG  ASN A 575     -12.240   5.301  35.494  1.00 51.87           C  
ANISOU 4373  CG  ASN A 575     6133   6801   6773   -117     94    298       C  
ATOM   4374  OD1 ASN A 575     -13.170   6.074  35.273  1.00 56.31           O  
ANISOU 4374  OD1 ASN A 575     6686   7355   7354   -109    105    283       O  
ATOM   4375  ND2 ASN A 575     -11.229   5.608  36.303  1.00 48.67           N  
ANISOU 4375  ND2 ASN A 575     5740   6410   6340   -130    101    300       N  
ATOM   4376  N   ASN A 576     -13.676   0.561  35.454  1.00 48.84           N  
ANISOU 4376  N   ASN A 576     5721   6414   6420   -131     55    356       N  
ATOM   4377  CA  ASN A 576     -14.068  -0.668  34.775  1.00 49.01           C  
ANISOU 4377  CA  ASN A 576     5735   6424   6461   -124     35    370       C  
ATOM   4378  C   ASN A 576     -15.577  -0.785  34.806  1.00 49.27           C  
ANISOU 4378  C   ASN A 576     5750   6452   6517   -123     44    364       C  
ATOM   4379  O   ASN A 576     -16.267   0.212  35.007  1.00 49.80           O  
ANISOU 4379  O   ASN A 576     5812   6519   6590   -121     62    347       O  
ATOM   4380  CB  ASN A 576     -13.393  -1.886  35.413  1.00 48.39           C  
ANISOU 4380  CB  ASN A 576     5659   6356   6369   -139     25    391       C  
ATOM   4381  CG  ASN A 576     -12.016  -2.154  34.833  1.00 47.01           C  
ANISOU 4381  CG  ASN A 576     5496   6177   6186   -133      6    399       C  
ATOM   4382  OD1 ASN A 576     -10.987  -1.846  35.439  1.00 45.97           O  
ANISOU 4382  OD1 ASN A 576     5376   6056   6032   -143      9    402       O  
ATOM   4383  ND2 ASN A 576     -11.994  -2.705  33.643  1.00 45.24           N  
ANISOU 4383  ND2 ASN A 576     5271   5936   5980   -117    -12    402       N  
ATOM   4384  N   SER A 577     -16.091  -1.988  34.594  1.00 49.57           N  
ANISOU 4384  N   SER A 577     5779   6485   6570   -123     32    378       N  
ATOM   4385  CA  SER A 577     -17.524  -2.214  34.657  1.00 48.83           C  
ANISOU 4385  CA  SER A 577     5667   6385   6499   -123     39    374       C  
ATOM   4386  C   SER A 577     -17.829  -3.549  35.356  1.00 47.49           C  
ANISOU 4386  C   SER A 577     5490   6224   6330   -139     36    393       C  
ATOM   4387  O   SER A 577     -18.132  -4.548  34.714  1.00 47.31           O  
ANISOU 4387  O   SER A 577     5460   6190   6324   -132     18    404       O  
ATOM   4388  CB  SER A 577     -18.150  -2.097  33.253  1.00 51.17           C  
ANISOU 4388  CB  SER A 577     5958   6659   6825   -100     23    368       C  
ATOM   4389  OG  SER A 577     -17.586  -3.014  32.328  1.00 51.47           O  
ANISOU 4389  OG  SER A 577     6002   6687   6866    -91     -2    381       O  
ATOM   4390  N   VAL A 578     -17.733  -3.540  36.686  1.00 48.70           N  
ANISOU 4390  N   VAL A 578     5644   6396   6461   -161     55    396       N  
ATOM   4391  CA  VAL A 578     -17.804  -4.750  37.522  1.00 49.82           C  
ANISOU 4391  CA  VAL A 578     5783   6550   6596   -181     52    416       C  
ATOM   4392  C   VAL A 578     -19.234  -5.250  37.724  1.00 52.75           C  
ANISOU 4392  C   VAL A 578     6135   6917   6989   -185     61    416       C  
ATOM   4393  O   VAL A 578     -20.151  -4.453  37.958  1.00 54.03           O  
ANISOU 4393  O   VAL A 578     6288   7080   7160   -185     82    398       O  
ATOM   4394  CB  VAL A 578     -17.171  -4.493  38.910  1.00 50.12           C  
ANISOU 4394  CB  VAL A 578     5831   6611   6600   -206     69    419       C  
ATOM   4395  CG1 VAL A 578     -17.385  -5.676  39.850  1.00 50.85           C  
ANISOU 4395  CG1 VAL A 578     5919   6715   6685   -229     67    439       C  
ATOM   4396  CG2 VAL A 578     -15.689  -4.178  38.781  1.00 49.61           C  
ANISOU 4396  CG2 VAL A 578     5784   6549   6514   -204     57    422       C  
ATOM   4397  N   ALA A 579     -19.410  -6.570  37.652  1.00 54.25           N  
ANISOU 4397  N   ALA A 579     6318   7105   7189   -189     44    435       N  
ATOM   4398  CA  ALA A 579     -20.714  -7.201  37.873  1.00 55.91           C  
ANISOU 4398  CA  ALA A 579     6510   7311   7419   -194     51    439       C  
ATOM   4399  C   ALA A 579     -20.908  -7.669  39.323  1.00 59.47           C  
ANISOU 4399  C   ALA A 579     6960   7784   7851   -224     68    449       C  
ATOM   4400  O   ALA A 579     -20.196  -8.554  39.809  1.00 59.71           O  
ANISOU 4400  O   ALA A 579     6997   7823   7866   -238     55    470       O  
ATOM   4401  CB  ALA A 579     -20.933  -8.348  36.894  1.00 54.58           C  
ANISOU 4401  CB  ALA A 579     6334   7126   7276   -181     23    452       C  
ATOM   4402  N   CYS A 580     -21.882  -7.063  40.000  1.00 63.51           N  
ANISOU 4402  N   CYS A 580     7462   8303   8366   -234     96    435       N  
ATOM   4403  CA  CYS A 580     -22.180  -7.364  41.406  1.00 67.17           C  
ANISOU 4403  CA  CYS A 580     7924   8786   8809   -264    118    441       C  
ATOM   4404  C   CYS A 580     -23.278  -8.436  41.584  1.00 67.66           C  
ANISOU 4404  C   CYS A 580     7969   8846   8892   -272    117    453       C  
ATOM   4405  O   CYS A 580     -24.201  -8.271  42.379  1.00 67.81           O  
ANISOU 4405  O   CYS A 580     7977   8874   8911   -288    144    445       O  
ATOM   4406  CB  CYS A 580     -22.507  -6.062  42.160  1.00 67.69           C  
ANISOU 4406  CB  CYS A 580     7992   8865   8862   -274    152    417       C  
ATOM   4407  SG  CYS A 580     -21.108  -4.908  42.193  1.00 74.14           S  
ANISOU 4407  SG  CYS A 580     8831   9688   9649   -271    153    406       S  
ATOM   4408  N   ILE A 581     -23.147  -9.535  40.839  1.00 68.24           N  
ANISOU 4408  N   ILE A 581     8038   8906   8982   -262     88    471       N  
ATOM   4409  CA  ILE A 581     -24.065 -10.682  40.910  1.00 70.72           C  
ANISOU 4409  CA  ILE A 581     8336   9216   9316   -268     82    486       C  
ATOM   4410  C   ILE A 581     -23.520 -11.803  41.816  1.00 76.75           C  
ANISOU 4410  C   ILE A 581     9106   9994  10059   -293     73    513       C  
ATOM   4411  O   ILE A 581     -22.414 -11.694  42.356  1.00 80.26           O  
ANISOU 4411  O   ILE A 581     9568  10452  10474   -306     69    521       O  
ATOM   4412  CB  ILE A 581     -24.410 -11.252  39.502  1.00 68.39           C  
ANISOU 4412  CB  ILE A 581     8031   8896   9057   -241     55    489       C  
ATOM   4413  CG1 ILE A 581     -23.140 -11.633  38.725  1.00 64.26           C  
ANISOU 4413  CG1 ILE A 581     7522   8365   8528   -228     25    500       C  
ATOM   4414  CG2 ILE A 581     -25.277 -10.278  38.710  1.00 66.08           C  
ANISOU 4414  CG2 ILE A 581     7728   8587   8790   -219     64    465       C  
ATOM   4415  CD1 ILE A 581     -23.388 -12.504  37.511  1.00 61.60           C  
ANISOU 4415  CD1 ILE A 581     7176   8006   8220   -208     -3    507       C  
ATOM   4416  N   CYS A 582     -24.299 -12.875  41.973  1.00 81.67           N  
ANISOU 4416  N   CYS A 582     9716  10615  10699   -302     67    528       N  
ATOM   4417  CA  CYS A 582     -23.933 -13.991  42.854  1.00 84.67           C  
ANISOU 4417  CA  CYS A 582    10099  11007  11062   -327     58    555       C  
ATOM   4418  C   CYS A 582     -22.909 -14.952  42.243  1.00 80.79           C  
ANISOU 4418  C   CYS A 582     9614  10505  10574   -319     21    576       C  
ATOM   4419  O   CYS A 582     -22.325 -15.774  42.951  1.00 79.52           O  
ANISOU 4419  O   CYS A 582     9459  10355  10398   -339     10    600       O  
ATOM   4420  CB  CYS A 582     -25.179 -14.770  43.311  1.00 92.99           C  
ANISOU 4420  CB  CYS A 582    11135  12062  12132   -341     68    563       C  
ATOM   4421  SG  CYS A 582     -26.257 -13.923  44.499  1.00106.98           S  
ANISOU 4421  SG  CYS A 582    12901  13853  13891   -365    115    544       S  
ATOM   4422  N   GLU A 583     -22.687 -14.857  40.937  1.00 79.20           N  
ANISOU 4422  N   GLU A 583     9411  10284  10395   -289      2    568       N  
ATOM   4423  CA  GLU A 583     -21.707 -15.723  40.281  1.00 82.27           C  
ANISOU 4423  CA  GLU A 583     9806  10662  10790   -279    -30    585       C  
ATOM   4424  C   GLU A 583     -20.275 -15.389  40.715  1.00 77.81           C  
ANISOU 4424  C   GLU A 583     9260  10108  10195   -288    -35    590       C  
ATOM   4425  O   GLU A 583     -19.392 -16.251  40.694  1.00 74.69           O  
ANISOU 4425  O   GLU A 583     8869   9710   9799   -292    -59    610       O  
ATOM   4426  CB  GLU A 583     -21.842 -15.645  38.754  1.00 88.49           C  
ANISOU 4426  CB  GLU A 583    10588  11426  11606   -247    -46    573       C  
ATOM   4427  CG  GLU A 583     -21.419 -16.909  38.014  1.00 95.34           C  
ANISOU 4427  CG  GLU A 583    11452  12278  12493   -238    -79    590       C  
ATOM   4428  CD  GLU A 583     -22.286 -18.118  38.354  1.00102.10           C  
ANISOU 4428  CD  GLU A 583    12293  13132  13368   -249    -85    608       C  
ATOM   4429  OE1 GLU A 583     -23.515 -17.953  38.519  1.00104.12           O  
ANISOU 4429  OE1 GLU A 583    12536  13388  13635   -251    -69    601       O  
ATOM   4430  OE2 GLU A 583     -21.740 -19.240  38.455  1.00100.90           O  
ANISOU 4430  OE2 GLU A 583    12140  12977  13220   -257   -107    630       O  
ATOM   4431  N   HIS A 584     -20.064 -14.140  41.129  1.00 72.86           N  
ANISOU 4431  N   HIS A 584     8644   9494   9546   -292    -12    573       N  
ATOM   4432  CA  HIS A 584     -18.729 -13.636  41.434  1.00 71.36           C  
ANISOU 4432  CA  HIS A 584     8471   9312   9329   -297    -16    574       C  
ATOM   4433  C   HIS A 584     -18.531 -13.306  42.892  1.00 71.71           C  
ANISOU 4433  C   HIS A 584     8525   9381   9339   -328      2    579       C  
ATOM   4434  O   HIS A 584     -17.839 -12.336  43.221  1.00 72.30           O  
ANISOU 4434  O   HIS A 584     8614   9465   9389   -332     13    568       O  
ATOM   4435  CB  HIS A 584     -18.423 -12.407  40.576  1.00 68.01           C  
ANISOU 4435  CB  HIS A 584     8054   8880   8906   -273    -10    549       C  
ATOM   4436  CG  HIS A 584     -18.691 -12.600  39.098  1.00 67.99           C  
ANISOU 4436  CG  HIS A 584     8043   8854   8935   -243    -27    541       C  
ATOM   4437  ND1 HIS A 584     -18.199 -13.646  38.396  1.00 68.06           N  
ANISOU 4437  ND1 HIS A 584     8049   8849   8959   -234    -55    556       N  
ATOM   4438  CD2 HIS A 584     -19.407 -11.821  38.190  1.00 65.52           C  
ANISOU 4438  CD2 HIS A 584     7724   8528   8640   -221    -19    520       C  
ATOM   4439  CE1 HIS A 584     -18.596 -13.551  37.111  1.00 64.70           C  
ANISOU 4439  CE1 HIS A 584     7619   8405   8559   -208    -64    544       C  
ATOM   4440  NE2 HIS A 584     -19.333 -12.433  36.985  1.00 66.26           N  
ANISOU 4440  NE2 HIS A 584     7814   8602   8757   -201    -44    523       N  
ATOM   4441  N   GLN A 585     -19.122 -14.113  43.775  1.00 69.09           N  
ANISOU 4441  N   GLN A 585     8187   9059   9003   -352      6    596       N  
ATOM   4442  CA  GLN A 585     -19.030 -13.897  45.222  1.00 68.29           C  
ANISOU 4442  CA  GLN A 585     8096   8982   8867   -387     25    602       C  
ATOM   4443  C   GLN A 585     -17.587 -13.829  45.672  1.00 67.05           C  
ANISOU 4443  C   GLN A 585     7957   8833   8683   -398     11    615       C  
ATOM   4444  O   GLN A 585     -17.223 -12.964  46.471  1.00 66.18           O  
ANISOU 4444  O   GLN A 585     7860   8740   8542   -414     29    606       O  
ATOM   4445  CB  GLN A 585     -19.688 -15.034  45.992  1.00 69.88           C  
ANISOU 4445  CB  GLN A 585     8289   9191   9069   -411     23    625       C  
ATOM   4446  CG  GLN A 585     -21.175 -15.194  45.807  1.00 72.03           C  
ANISOU 4446  CG  GLN A 585     8542   9457   9366   -407     40    615       C  
ATOM   4447  CD  GLN A 585     -21.662 -16.519  46.351  1.00 73.76           C  
ANISOU 4447  CD  GLN A 585     8752   9679   9591   -428     30    642       C  
ATOM   4448  OE1 GLN A 585     -21.987 -17.432  45.591  1.00 77.28           O  
ANISOU 4448  OE1 GLN A 585     9185  10108  10067   -413      9    652       O  
ATOM   4449  NE2 GLN A 585     -21.710 -16.635  47.674  1.00 74.04           N  
ANISOU 4449  NE2 GLN A 585     8796   9737   9597   -463     45    653       N  
ATOM   4450  N   LYS A 586     -16.780 -14.761  45.163  1.00 66.49           N  
ANISOU 4450  N   LYS A 586     7886   8750   8625   -390    -21    635       N  
ATOM   4451  CA  LYS A 586     -15.369 -14.866  45.528  1.00 70.38           C  
ANISOU 4451  CA  LYS A 586     8393   9247   9099   -401    -40    650       C  
ATOM   4452  C   LYS A 586     -14.645 -13.541  45.304  1.00 67.59           C  
ANISOU 4452  C   LYS A 586     8053   8896   8729   -389    -29    628       C  
ATOM   4453  O   LYS A 586     -14.139 -12.941  46.259  1.00 62.92           O  
ANISOU 4453  O   LYS A 586     7476   8323   8106   -410    -17    628       O  
ATOM   4454  CB  LYS A 586     -14.677 -16.021  44.779  1.00 71.06           C  
ANISOU 4454  CB  LYS A 586     8473   9314   9210   -388    -76    669       C  
ATOM   4455  CG  LYS A 586     -14.692 -17.358  45.513  1.00 72.30           C  
ANISOU 4455  CG  LYS A 586     8625   9474   9369   -413    -95    702       C  
ATOM   4456  CD  LYS A 586     -16.058 -18.040  45.457  1.00 75.69           C  
ANISOU 4456  CD  LYS A 586     9038   9900   9818   -414    -88    705       C  
ATOM   4457  CE  LYS A 586     -16.036 -19.415  46.117  1.00 75.50           C  
ANISOU 4457  CE  LYS A 586     9008   9878   9798   -438   -110    738       C  
ATOM   4458  NZ  LYS A 586     -17.320 -20.146  45.910  1.00 73.44           N  
ANISOU 4458  NZ  LYS A 586     8730   9610   9560   -436   -106    741       N  
ATOM   4459  N   PHE A 587     -14.643 -13.080  44.050  1.00 69.94           N  
ANISOU 4459  N   PHE A 587     8346   9178   9049   -357    -31    609       N  
ATOM   4460  CA  PHE A 587     -14.002 -11.820  43.659  1.00 65.85           C  
ANISOU 4460  CA  PHE A 587     7839   8659   8520   -342    -22    588       C  
ATOM   4461  C   PHE A 587     -14.460 -10.631  44.508  1.00 63.72           C  
ANISOU 4461  C   PHE A 587     7577   8408   8225   -356     10    569       C  
ATOM   4462  O   PHE A 587     -13.638  -9.854  44.999  1.00 61.57           O  
ANISOU 4462  O   PHE A 587     7319   8146   7927   -365     16    564       O  
ATOM   4463  CB  PHE A 587     -14.230 -11.533  42.167  1.00 63.84           C  
ANISOU 4463  CB  PHE A 587     7577   8383   8295   -307    -28    570       C  
ATOM   4464  CG  PHE A 587     -13.594 -10.252  41.697  1.00 65.78           C  
ANISOU 4464  CG  PHE A 587     7834   8628   8531   -291    -19    549       C  
ATOM   4465  CD1 PHE A 587     -12.251 -10.219  41.336  1.00 64.65           C  
ANISOU 4465  CD1 PHE A 587     7701   8479   8383   -284    -37    554       C  
ATOM   4466  CD2 PHE A 587     -14.331  -9.071  41.636  1.00 65.45           C  
ANISOU 4466  CD2 PHE A 587     7792   8589   8487   -284      6    524       C  
ATOM   4467  CE1 PHE A 587     -11.659  -9.041  40.917  1.00 63.95           C  
ANISOU 4467  CE1 PHE A 587     7623   8390   8286   -271    -29    535       C  
ATOM   4468  CE2 PHE A 587     -13.740  -7.888  41.221  1.00 65.69           C  
ANISOU 4468  CE2 PHE A 587     7832   8617   8508   -271     13    505       C  
ATOM   4469  CZ  PHE A 587     -12.404  -7.872  40.861  1.00 64.46           C  
ANISOU 4469  CZ  PHE A 587     7687   8457   8346   -264     -4    511       C  
ATOM   4470  N   LEU A 588     -15.773 -10.506  44.679  1.00 63.30           N  
ANISOU 4470  N   LEU A 588     7513   8358   8180   -359     32    558       N  
ATOM   4471  CA  LEU A 588     -16.366  -9.389  45.404  1.00 63.98           C  
ANISOU 4471  CA  LEU A 588     7602   8459   8248   -370     66    537       C  
ATOM   4472  C   LEU A 588     -15.978  -9.356  46.880  1.00 64.02           C  
ANISOU 4472  C   LEU A 588     7621   8487   8214   -407     78    547       C  
ATOM   4473  O   LEU A 588     -15.663  -8.291  47.414  1.00 59.79           O  
ANISOU 4473  O   LEU A 588     7097   7964   7655   -416     97    532       O  
ATOM   4474  CB  LEU A 588     -17.886  -9.401  45.229  1.00 64.35           C  
ANISOU 4474  CB  LEU A 588     7631   8500   8316   -365     85    524       C  
ATOM   4475  CG  LEU A 588     -18.357  -8.964  43.837  1.00 64.27           C  
ANISOU 4475  CG  LEU A 588     7610   8468   8340   -330     82    506       C  
ATOM   4476  CD1 LEU A 588     -19.637  -9.672  43.413  1.00 62.94           C  
ANISOU 4476  CD1 LEU A 588     7422   8289   8204   -322     81    508       C  
ATOM   4477  CD2 LEU A 588     -18.526  -7.451  43.782  1.00 66.08           C  
ANISOU 4477  CD2 LEU A 588     7843   8700   8564   -321    107    476       C  
ATOM   4478  N   GLN A 589     -15.994 -10.521  47.527  1.00 68.12           N  
ANISOU 4478  N   GLN A 589     8139   9014   8729   -430     64    574       N  
ATOM   4479  CA  GLN A 589     -15.571 -10.631  48.919  1.00 72.89           C  
ANISOU 4479  CA  GLN A 589     8758   9641   9296   -468     70    589       C  
ATOM   4480  C   GLN A 589     -14.115 -10.223  49.011  1.00 74.36           C  
ANISOU 4480  C   GLN A 589     8961   9829   9461   -469     54    594       C  
ATOM   4481  O   GLN A 589     -13.740  -9.351  49.791  1.00 82.52           O  
ANISOU 4481  O   GLN A 589    10009  10878  10464   -486     71    584       O  
ATOM   4482  CB  GLN A 589     -15.756 -12.064  49.441  1.00 76.09           C  
ANISOU 4482  CB  GLN A 589     9158  10048   9702   -489     52    621       C  
ATOM   4483  CG  GLN A 589     -15.282 -12.285  50.874  1.00 71.06           C  
ANISOU 4483  CG  GLN A 589     8538   9435   9026   -531     53    640       C  
ATOM   4484  CD  GLN A 589     -15.823 -11.248  51.840  1.00 72.51           C  
ANISOU 4484  CD  GLN A 589     8730   9639   9179   -553     92    619       C  
ATOM   4485  OE1 GLN A 589     -15.107 -10.779  52.720  1.00 75.13           O  
ANISOU 4485  OE1 GLN A 589     9081   9988   9476   -577     97    621       O  
ATOM   4486  NE2 GLN A 589     -17.090 -10.880  51.677  1.00 72.58           N  
ANISOU 4486  NE2 GLN A 589     8725   9647   9202   -546    121    597       N  
ATOM   4487  N   TRP A 590     -13.316 -10.866  48.172  1.00 71.31           N  
ANISOU 4487  N   TRP A 590     8572   9425   9095   -450     22    608       N  
ATOM   4488  CA  TRP A 590     -11.886 -10.644  48.058  1.00 69.46           C  
ANISOU 4488  CA  TRP A 590     8351   9189   8851   -447      2    615       C  
ATOM   4489  C   TRP A 590     -11.478  -9.184  47.977  1.00 67.77           C  
ANISOU 4489  C   TRP A 590     8148   8979   8621   -438     21    589       C  
ATOM   4490  O   TRP A 590     -10.467  -8.791  48.558  1.00 68.21           O  
ANISOU 4490  O   TRP A 590     8219   9045   8652   -452     16    594       O  
ATOM   4491  CB  TRP A 590     -11.418 -11.446  46.855  1.00 69.72           C  
ANISOU 4491  CB  TRP A 590     8373   9197   8917   -420    -27    625       C  
ATOM   4492  CG  TRP A 590     -10.003 -11.243  46.427  1.00 71.75           C  
ANISOU 4492  CG  TRP A 590     8640   9447   9175   -409    -48    628       C  
ATOM   4493  CD1 TRP A 590      -8.875 -11.911  46.884  1.00 72.41           C  
ANISOU 4493  CD1 TRP A 590     8730   9531   9252   -424    -74    653       C  
ATOM   4494  CD2 TRP A 590      -9.514 -10.323  45.396  1.00 71.77           C  
ANISOU 4494  CD2 TRP A 590     8645   9437   9187   -379    -45    606       C  
ATOM   4495  NE1 TRP A 590      -7.751 -11.472  46.233  1.00 71.89           N  
ANISOU 4495  NE1 TRP A 590     8669   9454   9190   -406    -86    647       N  
ATOM   4496  CE2 TRP A 590      -8.062 -10.519  45.330  1.00 71.18           C  
ANISOU 4496  CE2 TRP A 590     8578   9357   9109   -380    -69    619       C  
ATOM   4497  CE3 TRP A 590     -10.109  -9.384  44.557  1.00 69.44           C  
ANISOU 4497  CE3 TRP A 590     8345   9135   8901   -355    -26    578       C  
ATOM   4498  CZ2 TRP A 590      -7.261  -9.794  44.460  1.00 71.69           C  
ANISOU 4498  CZ2 TRP A 590     8646   9410   9179   -356    -72    604       C  
ATOM   4499  CZ3 TRP A 590      -9.292  -8.660  43.683  1.00 68.70           C  
ANISOU 4499  CZ3 TRP A 590     8257   9031   8813   -332    -31    564       C  
ATOM   4500  CH2 TRP A 590      -7.902  -8.861  43.637  1.00 70.96           C  
ANISOU 4500  CH2 TRP A 590     8552   9313   9096   -333    -53    576       C  
ATOM   4501  N   VAL A 591     -12.270  -8.368  47.281  1.00 66.32           N  
ANISOU 4501  N   VAL A 591     7956   8788   8451   -415     42    561       N  
ATOM   4502  CA  VAL A 591     -12.049  -6.918  47.214  1.00 64.59           C  
ANISOU 4502  CA  VAL A 591     7747   8574   8220   -407     63    534       C  
ATOM   4503  C   VAL A 591     -12.034  -6.268  48.611  1.00 69.46           C  
ANISOU 4503  C   VAL A 591     8376   9214   8798   -439     86    529       C  
ATOM   4504  O   VAL A 591     -11.337  -5.271  48.823  1.00 67.57           O  
ANISOU 4504  O   VAL A 591     8150   8981   8540   -440     94    517       O  
ATOM   4505  CB  VAL A 591     -13.074  -6.233  46.268  1.00 61.89           C  
ANISOU 4505  CB  VAL A 591     7391   8219   7904   -379     80    507       C  
ATOM   4506  CG1 VAL A 591     -13.020  -4.715  46.368  1.00 62.99           C  
ANISOU 4506  CG1 VAL A 591     7539   8364   8031   -374    105    479       C  
ATOM   4507  CG2 VAL A 591     -12.837  -6.655  44.827  1.00 56.99           C  
ANISOU 4507  CG2 VAL A 591     6762   7574   7315   -346     56    510       C  
ATOM   4508  N   LYS A 592     -12.773  -6.842  49.564  1.00 79.15           N  
ANISOU 4508  N   LYS A 592     9603  10457  10014   -467     98    539       N  
ATOM   4509  CA  LYS A 592     -12.817  -6.286  50.925  1.00 85.37           C  
ANISOU 4509  CA  LYS A 592    10404  11268  10762   -501    121    535       C  
ATOM   4510  C   LYS A 592     -11.521  -6.496  51.717  1.00 86.81           C  
ANISOU 4510  C   LYS A 592    10607  11463  10914   -526    102    556       C  
ATOM   4511  O   LYS A 592     -11.100  -5.595  52.443  1.00 86.07           O  
ANISOU 4511  O   LYS A 592    10528  11383  10790   -542    117    545       O  
ATOM   4512  CB  LYS A 592     -14.042  -6.762  51.734  1.00 90.59           C  
ANISOU 4512  CB  LYS A 592    11059  11943  11418   -526    143    537       C  
ATOM   4513  CG  LYS A 592     -13.747  -7.804  52.820  1.00 98.34           C  
ANISOU 4513  CG  LYS A 592    12050  12939  12374   -564    129    569       C  
ATOM   4514  CD  LYS A 592     -14.587  -7.628  54.087  1.00100.53           C  
ANISOU 4514  CD  LYS A 592    12333  13240  12623   -600    162    563       C  
ATOM   4515  CE  LYS A 592     -13.881  -6.768  55.134  1.00 97.56           C  
ANISOU 4515  CE  LYS A 592    11979  12884  12202   -628    175    556       C  
ATOM   4516  NZ  LYS A 592     -14.625  -6.709  56.422  1.00 91.80           N  
ANISOU 4516  NZ  LYS A 592    11257  12179  11441   -668    206    552       N  
ATOM   4517  N   GLU A 593     -10.893  -7.668  51.592  1.00 91.20           N  
ANISOU 4517  N   GLU A 593    11160  12010  11478   -529     67    587       N  
ATOM   4518  CA  GLU A 593      -9.669  -7.926  52.360  1.00 98.88           C  
ANISOU 4518  CA  GLU A 593    12150  12993  12425   -553     46    610       C  
ATOM   4519  C   GLU A 593      -8.418  -7.397  51.659  1.00 96.57           C  
ANISOU 4519  C   GLU A 593    11864  12688  12139   -531     28    606       C  
ATOM   4520  O   GLU A 593      -7.447  -7.013  52.316  1.00 96.93           O  
ANISOU 4520  O   GLU A 593    11925  12743  12158   -548     21    613       O  
ATOM   4521  CB  GLU A 593      -9.510  -9.403  52.755  1.00107.07           C  
ANISOU 4521  CB  GLU A 593    13185  14030  13467   -573     17    647       C  
ATOM   4522  CG  GLU A 593      -8.730  -9.572  54.063  1.00114.98           C  
ANISOU 4522  CG  GLU A 593    14207  15050  14430   -613      6    670       C  
ATOM   4523  CD  GLU A 593      -8.353 -11.009  54.397  1.00117.66           C  
ANISOU 4523  CD  GLU A 593    14544  15386  14776   -631    -28    709       C  
ATOM   4524  OE1 GLU A 593      -8.217 -11.319  55.604  1.00117.67           O  
ANISOU 4524  OE1 GLU A 593    14559  15405  14745   -671    -31    729       O  
ATOM   4525  OE2 GLU A 593      -8.178 -11.828  53.468  1.00116.93           O  
ANISOU 4525  OE2 GLU A 593    14436  15271  14719   -607    -52    721       O  
ATOM   4526  N   GLN A 594      -8.458  -7.352  50.329  1.00 92.40           N  
ANISOU 4526  N   GLN A 594    11322  12138  11645   -493     21    595       N  
ATOM   4527  CA  GLN A 594      -7.379  -6.752  49.546  1.00 87.85           C  
ANISOU 4527  CA  GLN A 594    10751  11550  11077   -470      8    587       C  
ATOM   4528  C   GLN A 594      -7.617  -5.255  49.354  1.00 84.31           C  
ANISOU 4528  C   GLN A 594    10307  11105  10620   -457     37    553       C  
ATOM   4529  O   GLN A 594      -7.374  -4.703  48.287  1.00 86.72           O  
ANISOU 4529  O   GLN A 594    10608  11396  10944   -427     36    538       O  
ATOM   4530  CB  GLN A 594      -7.228  -7.473  48.204  1.00 85.22           C  
ANISOU 4530  CB  GLN A 594    10402  11192  10783   -438    -14    592       C  
ATOM   4531  CG  GLN A 594      -7.059  -8.982  48.317  1.00 85.09           C  
ANISOU 4531  CG  GLN A 594    10379  11170  10781   -448    -43    624       C  
ATOM   4532  CD  GLN A 594      -5.781  -9.397  49.026  1.00 87.65           C  
ANISOU 4532  CD  GLN A 594    10714  11497  11089   -470    -68    649       C  
ATOM   4533  OE1 GLN A 594      -4.780  -9.711  48.382  1.00 89.29           O  
ANISOU 4533  OE1 GLN A 594    10920  11690  11316   -455    -92    658       O  
ATOM   4534  NE2 GLN A 594      -5.809  -9.405  50.357  1.00 85.84           N  
ANISOU 4534  NE2 GLN A 594    10497  11290  10828   -506    -62    662       N  
ATOM   4535  N   LYS A 595      -8.076  -4.610  50.421  1.00 86.22           N  
ANISOU 4535  N   LYS A 595    10559  11368  10832   -482     64    543       N  
ATOM   4536  CA  LYS A 595      -8.456  -3.200  50.420  1.00 88.49           C  
ANISOU 4536  CA  LYS A 595    10849  11660  11110   -475     95    510       C  
ATOM   4537  C   LYS A 595      -7.257  -2.286  50.157  1.00 84.81           C  
ANISOU 4537  C   LYS A 595    10396  11191  10636   -464     88    501       C  
ATOM   4538  O   LYS A 595      -7.330  -1.385  49.323  1.00 79.27           O  
ANISOU 4538  O   LYS A 595     9690  10478   9949   -438     98    478       O  
ATOM   4539  CB  LYS A 595      -9.087  -2.854  51.777  1.00 94.34           C  
ANISOU 4539  CB  LYS A 595    11600  12425  11819   -510    123    503       C  
ATOM   4540  CG  LYS A 595     -10.412  -2.103  51.724  1.00 94.22           C  
ANISOU 4540  CG  LYS A 595    11575  12413  11812   -503    160    473       C  
ATOM   4541  CD  LYS A 595     -11.168  -2.286  53.037  1.00 94.95           C  
ANISOU 4541  CD  LYS A 595    11672  12527  11877   -541    184    474       C  
ATOM   4542  CE  LYS A 595     -12.594  -1.750  52.985  1.00 96.72           C  
ANISOU 4542  CE  LYS A 595    11881  12751  12115   -535    220    446       C  
ATOM   4543  NZ  LYS A 595     -12.715  -0.345  53.467  1.00 91.20           N  
ANISOU 4543  NZ  LYS A 595    11190  12062  11398   -542    253    414       N  
ATOM   4544  N   GLN A 596      -6.159  -2.541  50.872  1.00 85.66           N  
ANISOU 4544  N   GLN A 596    10518  11307  10721   -486     70    521       N  
ATOM   4545  CA  GLN A 596      -4.958  -1.696  50.843  1.00 82.55           C  
ANISOU 4545  CA  GLN A 596    10136  10912  10314   -482     63    515       C  
ATOM   4546  C   GLN A 596      -4.251  -1.704  49.494  1.00 78.88           C  
ANISOU 4546  C   GLN A 596     9664  10425   9880   -447     43    514       C  
ATOM   4547  O   GLN A 596      -3.614  -0.719  49.124  1.00 72.42           O  
ANISOU 4547  O   GLN A 596     8852   9602   9059   -433     46    499       O  
ATOM   4548  CB  GLN A 596      -3.955  -2.141  51.914  1.00 83.79           C  
ANISOU 4548  CB  GLN A 596    10309  11082  10443   -514     43    541       C  
ATOM   4549  CG  GLN A 596      -4.521  -2.291  53.317  1.00 85.22           C  
ANISOU 4549  CG  GLN A 596    10501  11286  10590   -554     59    547       C  
ATOM   4550  CD  GLN A 596      -3.602  -3.084  54.229  1.00 86.67           C  
ANISOU 4550  CD  GLN A 596    10697  11478  10753   -586     31    581       C  
ATOM   4551  OE1 GLN A 596      -2.490  -2.649  54.549  1.00 84.72           O  
ANISOU 4551  OE1 GLN A 596    10464  11234  10490   -594     18    585       O  
ATOM   4552  NE2 GLN A 596      -4.065  -4.254  54.659  1.00 83.81           N  
ANISOU 4552  NE2 GLN A 596    10331  11121  10392   -605     20    605       N  
ATOM   4553  N   PHE A 597      -4.361  -2.820  48.776  1.00 79.71           N  
ANISOU 4553  N   PHE A 597     9756  10515  10013   -433     22    531       N  
ATOM   4554  CA  PHE A 597      -3.609  -3.030  47.533  1.00 79.68           C  
ANISOU 4554  CA  PHE A 597     9746  10489  10037   -403      0    533       C  
ATOM   4555  C   PHE A 597      -4.387  -2.635  46.266  1.00 76.07           C  
ANISOU 4555  C   PHE A 597     9277  10018   9608   -370     12    511       C  
ATOM   4556  O   PHE A 597      -3.860  -2.718  45.148  1.00 69.10           O  
ANISOU 4556  O   PHE A 597     8389   9117   8747   -345     -2    509       O  
ATOM   4557  CB  PHE A 597      -3.097  -4.480  47.451  1.00 83.90           C  
ANISOU 4557  CB  PHE A 597    10274  11015  10588   -408    -31    564       C  
ATOM   4558  CG  PHE A 597      -2.419  -4.965  48.714  1.00 89.94           C  
ANISOU 4558  CG  PHE A 597    11050  11794  11328   -443    -45    589       C  
ATOM   4559  CD1 PHE A 597      -1.269  -4.336  49.200  1.00 88.92           C  
ANISOU 4559  CD1 PHE A 597    10935  11670  11178   -454    -52    591       C  
ATOM   4560  CD2 PHE A 597      -2.927  -6.055  49.417  1.00 89.66           C  
ANISOU 4560  CD2 PHE A 597    11011  11766  11289   -466    -54    612       C  
ATOM   4561  CE1 PHE A 597      -0.649  -4.778  50.358  1.00 84.80           C  
ANISOU 4561  CE1 PHE A 597    10425  11161  10634   -487    -67    615       C  
ATOM   4562  CE2 PHE A 597      -2.306  -6.502  50.574  1.00 88.60           C  
ANISOU 4562  CE2 PHE A 597    10888  11643  11131   -500    -69    636       C  
ATOM   4563  CZ  PHE A 597      -1.168  -5.862  51.045  1.00 86.68           C  
ANISOU 4563  CZ  PHE A 597    10660  11406  10868   -511    -77    638       C  
ATOM   4564  N   LEU A 598      -5.634  -2.200  46.447  1.00 71.42           N  
ANISOU 4564  N   LEU A 598     8683   9435   9017   -371     38    494       N  
ATOM   4565  CA  LEU A 598      -6.478  -1.797  45.329  1.00 67.72           C  
ANISOU 4565  CA  LEU A 598     8203   8953   8575   -342     49    473       C  
ATOM   4566  C   LEU A 598      -6.642  -0.288  45.274  1.00 68.01           C  
ANISOU 4566  C   LEU A 598     8245   8993   8603   -334     73    445       C  
ATOM   4567  O   LEU A 598      -7.096   0.337  46.233  1.00 67.53           O  
ANISOU 4567  O   LEU A 598     8189   8948   8521   -353     96    433       O  
ATOM   4568  CB  LEU A 598      -7.846  -2.482  45.389  1.00 66.04           C  
ANISOU 4568  CB  LEU A 598     7975   8739   8374   -345     57    475       C  
ATOM   4569  CG  LEU A 598      -7.955  -3.985  45.110  1.00 66.38           C  
ANISOU 4569  CG  LEU A 598     8008   8774   8436   -345     34    500       C  
ATOM   4570  CD1 LEU A 598      -9.394  -4.454  45.276  1.00 64.98           C  
ANISOU 4570  CD1 LEU A 598     7818   8599   8270   -350     47    498       C  
ATOM   4571  CD2 LEU A 598      -7.441  -4.347  43.724  1.00 65.12           C  
ANISOU 4571  CD2 LEU A 598     7843   8592   8305   -316     11    502       C  
ATOM   4572  N   VAL A 599      -6.265   0.280  44.133  1.00 69.79           N  
ANISOU 4572  N   VAL A 599     8469   9202   8845   -306     67    433       N  
ATOM   4573  CA  VAL A 599      -6.252   1.726  43.925  1.00 71.49           C  
ANISOU 4573  CA  VAL A 599     8689   9417   9055   -296     86    407       C  
ATOM   4574  C   VAL A 599      -7.668   2.290  43.935  1.00 71.30           C  
ANISOU 4574  C   VAL A 599     8655   9393   9041   -292    112    386       C  
ATOM   4575  O   VAL A 599      -8.557   1.770  43.252  1.00 69.24           O  
ANISOU 4575  O   VAL A 599     8381   9122   8805   -278    109    386       O  
ATOM   4576  CB  VAL A 599      -5.531   2.098  42.603  1.00 72.93           C  
ANISOU 4576  CB  VAL A 599     8872   9580   9255   -267     71    401       C  
ATOM   4577  CG1 VAL A 599      -5.561   3.602  42.355  1.00 71.74           C  
ANISOU 4577  CG1 VAL A 599     8726   9428   9101   -256     90    375       C  
ATOM   4578  CG2 VAL A 599      -4.092   1.596  42.622  1.00 72.33           C  
ANISOU 4578  CG2 VAL A 599     8805   9503   9172   -271     48    420       C  
ATOM   4579  N   ASN A 600      -7.853   3.348  44.725  1.00 71.51           N  
ANISOU 4579  N   ASN A 600     8688   9433   9050   -304    136    368       N  
ATOM   4580  CA  ASN A 600      -9.133   4.050  44.870  1.00 73.96           C  
ANISOU 4580  CA  ASN A 600     8988   9743   9368   -303    164    345       C  
ATOM   4581  C   ASN A 600     -10.348   3.138  45.055  1.00 74.82           C  
ANISOU 4581  C   ASN A 600     9083   9854   9490   -309    170    351       C  
ATOM   4582  O   ASN A 600     -11.366   3.304  44.375  1.00 73.66           O  
ANISOU 4582  O   ASN A 600     8922   9694   9371   -292    178    338       O  
ATOM   4583  CB  ASN A 600      -9.362   5.024  43.705  1.00 74.49           C  
ANISOU 4583  CB  ASN A 600     9049   9792   9459   -273    167    324       C  
ATOM   4584  CG  ASN A 600      -8.570   6.308  43.848  1.00 73.12           C  
ANISOU 4584  CG  ASN A 600     8887   9622   9271   -271    175    308       C  
ATOM   4585  OD1 ASN A 600      -7.341   6.304  43.819  1.00 71.87           O  
ANISOU 4585  OD1 ASN A 600     8742   9465   9098   -272    160    319       O  
ATOM   4586  ND2 ASN A 600      -9.278   7.420  43.988  1.00 74.69           N  
ANISOU 4586  ND2 ASN A 600     9082   9821   9475   -268    200    283       N  
ATOM   4587  N   VAL A 601     -10.234   2.181  45.975  1.00 77.39           N  
ANISOU 4587  N   VAL A 601     9412  10193   9798   -335    166    371       N  
ATOM   4588  CA  VAL A 601     -11.360   1.316  46.341  1.00 81.69           C  
ANISOU 4588  CA  VAL A 601     9945  10742  10351   -346    173    378       C  
ATOM   4589  C   VAL A 601     -12.522   2.131  46.886  1.00 84.81           C  
ANISOU 4589  C   VAL A 601    10333  11144  10746   -354    209    352       C  
ATOM   4590  O   VAL A 601     -13.676   1.708  46.821  1.00 83.58           O  
ANISOU 4590  O   VAL A 601    10162  10985  10609   -353    219    350       O  
ATOM   4591  CB  VAL A 601     -10.985   0.251  47.395  1.00 82.97           C  
ANISOU 4591  CB  VAL A 601    10115  10920  10488   -377    164    404       C  
ATOM   4592  CG1 VAL A 601     -10.736  -1.093  46.730  1.00 81.73           C  
ANISOU 4592  CG1 VAL A 601     9951  10751  10350   -368    132    431       C  
ATOM   4593  CG2 VAL A 601      -9.807   0.694  48.258  1.00 81.70           C  
ANISOU 4593  CG2 VAL A 601     9974  10774  10292   -398    162    409       C  
ATOM   4594  N   GLU A 602     -12.197   3.309  47.411  1.00 90.05           N  
ANISOU 4594  N   GLU A 602    11006  11817  11391   -361    228    333       N  
ATOM   4595  CA  GLU A 602     -13.179   4.217  47.990  1.00 92.75           C  
ANISOU 4595  CA  GLU A 602    11342  12164  11733   -370    264    305       C  
ATOM   4596  C   GLU A 602     -14.282   4.638  47.015  1.00 89.73           C  
ANISOU 4596  C   GLU A 602    10938  11762  11390   -342    273    287       C  
ATOM   4597  O   GLU A 602     -15.405   4.899  47.442  1.00 92.25           O  
ANISOU 4597  O   GLU A 602    11246  12084  11719   -350    299    270       O  
ATOM   4598  CB  GLU A 602     -12.478   5.455  48.561  1.00 98.79           C  
ANISOU 4598  CB  GLU A 602    12122  12939  12473   -378    279    287       C  
ATOM   4599  CG  GLU A 602     -11.532   5.168  49.722  1.00105.06           C  
ANISOU 4599  CG  GLU A 602    12937  13756  13226   -410    275    303       C  
ATOM   4600  CD  GLU A 602     -12.252   4.965  51.048  1.00107.26           C  
ANISOU 4600  CD  GLU A 602    13218  14056  13481   -445    302    299       C  
ATOM   4601  OE1 GLU A 602     -12.915   5.912  51.528  1.00108.83           O  
ANISOU 4601  OE1 GLU A 602    13413  14260  13677   -452    335    271       O  
ATOM   4602  OE2 GLU A 602     -12.141   3.859  51.620  1.00104.57           O  
ANISOU 4602  OE2 GLU A 602    12881  13725  13124   -467    290    324       O  
ATOM   4603  N   GLN A 603     -13.970   4.690  45.718  1.00 84.55           N  
ANISOU 4603  N   GLN A 603    10279  11086  10758   -312    250    290       N  
ATOM   4604  CA  GLN A 603     -14.908   5.228  44.723  1.00 80.51           C  
ANISOU 4604  CA  GLN A 603     9750  10554  10284   -286    255    272       C  
ATOM   4605  C   GLN A 603     -15.384   4.235  43.654  1.00 74.65           C  
ANISOU 4605  C   GLN A 603     8996   9795   9572   -266    231    287       C  
ATOM   4606  O   GLN A 603     -16.147   4.612  42.763  1.00 72.23           O  
ANISOU 4606  O   GLN A 603     8676   9470   9298   -245    231    275       O  
ATOM   4607  CB  GLN A 603     -14.337   6.486  44.054  1.00 86.07           C  
ANISOU 4607  CB  GLN A 603    10460  11248  10994   -266    253    255       C  
ATOM   4608  CG  GLN A 603     -14.039   7.643  45.000  1.00 97.98           C  
ANISOU 4608  CG  GLN A 603    11978  12769  12479   -282    279    234       C  
ATOM   4609  CD  GLN A 603     -12.660   7.556  45.644  1.00105.33           C  
ANISOU 4609  CD  GLN A 603    12931  13716  13372   -299    269    248       C  
ATOM   4610  OE1 GLN A 603     -11.817   6.750  45.240  1.00108.72           O  
ANISOU 4610  OE1 GLN A 603    13367  14143  13796   -295    241    271       O  
ATOM   4611  NE2 GLN A 603     -12.424   8.393  46.652  1.00104.89           N  
ANISOU 4611  NE2 GLN A 603    12884  13675  13291   -318    291    232       N  
ATOM   4612  N   MET A 604     -14.949   2.978  43.739  1.00 71.36           N  
ANISOU 4612  N   MET A 604     8583   9383   9146   -275    211    314       N  
ATOM   4613  CA  MET A 604     -15.356   1.956  42.765  1.00 68.28           C  
ANISOU 4613  CA  MET A 604     8182   8977   8783   -258    188    329       C  
ATOM   4614  C   MET A 604     -16.824   1.586  42.929  1.00 71.91           C  
ANISOU 4614  C   MET A 604     8623   9434   9265   -261    203    323       C  
ATOM   4615  O   MET A 604     -17.233   1.134  44.001  1.00 75.01           O  
ANISOU 4615  O   MET A 604     9014   9843   9644   -286    219    328       O  
ATOM   4616  CB  MET A 604     -14.507   0.699  42.904  1.00 64.71           C  
ANISOU 4616  CB  MET A 604     7738   8530   8317   -268    163    358       C  
ATOM   4617  CG  MET A 604     -13.125   0.794  42.289  1.00 66.33           C  
ANISOU 4617  CG  MET A 604     7958   8730   8515   -256    140    366       C  
ATOM   4618  SD  MET A 604     -12.253  -0.785  42.335  1.00 68.64           S  
ANISOU 4618  SD  MET A 604     8255   9025   8800   -265    109    400       S  
ATOM   4619  CE  MET A 604     -13.231  -1.760  41.190  1.00 63.25           C  
ANISOU 4619  CE  MET A 604     7554   8322   8156   -244     93    406       C  
ATOM   4620  N   THR A 605     -17.601   1.771  41.863  1.00 69.52           N  
ANISOU 4620  N   THR A 605     8305   9110   8997   -237    198    314       N  
ATOM   4621  CA  THR A 605     -19.048   1.524  41.875  1.00 71.38           C  
ANISOU 4621  CA  THR A 605     8520   9339   9259   -236    211    307       C  
ATOM   4622  C   THR A 605     -19.403   0.299  41.017  1.00 71.23           C  
ANISOU 4622  C   THR A 605     8492   9306   9263   -224    185    327       C  
ATOM   4623  O   THR A 605     -18.625  -0.079  40.145  1.00 71.10           O  
ANISOU 4623  O   THR A 605     8484   9281   9249   -209    158    339       O  
ATOM   4624  CB  THR A 605     -19.823   2.760  41.364  1.00 73.19           C  
ANISOU 4624  CB  THR A 605     8737   9553   9515   -219    226    280       C  
ATOM   4625  OG1 THR A 605     -19.441   3.042  40.012  1.00 76.57           O  
ANISOU 4625  OG1 THR A 605     9168   9962   9961   -192    201    281       O  
ATOM   4626  CG2 THR A 605     -19.525   3.991  42.224  1.00 70.89           C  
ANISOU 4626  CG2 THR A 605     8454   9275   9204   -232    254    259       C  
ATOM   4627  N   CYS A 606     -20.562  -0.322  41.265  1.00 71.94           N  
ANISOU 4627  N   CYS A 606     8565   9395   9372   -230    194    329       N  
ATOM   4628  CA  CYS A 606     -21.024  -1.459  40.445  1.00 73.31           C  
ANISOU 4628  CA  CYS A 606     8728   9554   9570   -218    170    345       C  
ATOM   4629  C   CYS A 606     -21.483  -0.966  39.074  1.00 72.40           C  
ANISOU 4629  C   CYS A 606     8604   9414   9488   -189    157    334       C  
ATOM   4630  O   CYS A 606     -21.607   0.241  38.852  1.00 74.56           O  
ANISOU 4630  O   CYS A 606     8876   9681   9769   -179    168    314       O  
ATOM   4631  CB  CYS A 606     -22.185  -2.232  41.107  1.00 73.19           C  
ANISOU 4631  CB  CYS A 606     8697   9544   9567   -234    184    350       C  
ATOM   4632  SG  CYS A 606     -21.871  -3.075  42.682  1.00 73.91           S  
ANISOU 4632  SG  CYS A 606     8796   9663   9621   -272    196    368       S  
ATOM   4633  N   ALA A 607     -21.748  -1.902  38.167  1.00 71.01           N  
ANISOU 4633  N   ALA A 607     8422   9224   9334   -176    132    348       N  
ATOM   4634  CA  ALA A 607     -22.258  -1.564  36.843  1.00 70.43           C  
ANISOU 4634  CA  ALA A 607     8340   9126   9292   -150    116    340       C  
ATOM   4635  C   ALA A 607     -23.361  -2.508  36.342  1.00 70.59           C  
ANISOU 4635  C   ALA A 607     8343   9133   9344   -144    105    349       C  
ATOM   4636  O   ALA A 607     -23.793  -2.399  35.200  1.00 70.05           O  
ANISOU 4636  O   ALA A 607     8268   9044   9302   -124     88    346       O  
ATOM   4637  CB  ALA A 607     -21.113  -1.491  35.841  1.00 65.59           C  
ANISOU 4637  CB  ALA A 607     7743   8505   8670   -134     91    346       C  
ATOM   4638  N   THR A 608     -23.819  -3.434  37.179  1.00 76.67           N  
ANISOU 4638  N   THR A 608     9104   9913  10111   -162    113    360       N  
ATOM   4639  CA  THR A 608     -24.886  -4.355  36.755  1.00 82.96           C  
ANISOU 4639  CA  THR A 608     9883  10698  10938   -157    103    369       C  
ATOM   4640  C   THR A 608     -26.180  -4.331  37.623  1.00 92.00           C  
ANISOU 4640  C   THR A 608    11009  11848  12099   -171    131    360       C  
ATOM   4641  O   THR A 608     -26.376  -3.409  38.425  1.00 89.54           O  
ANISOU 4641  O   THR A 608    10695  11546  11779   -181    160    343       O  
ATOM   4642  CB  THR A 608     -24.355  -5.779  36.482  1.00 78.27           C  
ANISOU 4642  CB  THR A 608     9294  10103  10338   -159     76    394       C  
ATOM   4643  OG1 THR A 608     -23.389  -6.127  37.476  1.00 78.41           O  
ANISOU 4643  OG1 THR A 608     9326  10142  10321   -179     82    406       O  
ATOM   4644  CG2 THR A 608     -23.733  -5.859  35.095  1.00 70.61           C  
ANISOU 4644  CG2 THR A 608     8333   9116   9376   -136     46    397       C  
ATOM   4645  N   PRO A 609     -27.027  -5.377  37.506  1.00 97.06           N  
ANISOU 4645  N   PRO A 609    11634  12481  12761   -172    123    372       N  
ATOM   4646  CA  PRO A 609     -28.481  -5.326  37.608  1.00104.80           C  
ANISOU 4646  CA  PRO A 609    12590  13452  13776   -172    138    362       C  
ATOM   4647  C   PRO A 609     -29.164  -3.948  37.427  1.00112.24           C  
ANISOU 4647  C   PRO A 609    13521  14383  14739   -162    157    336       C  
ATOM   4648  O   PRO A 609     -28.569  -3.015  36.869  1.00102.36           O  
ANISOU 4648  O   PRO A 609    12280  13126  13483   -148    151    325       O  
ATOM   4649  CB  PRO A 609     -28.725  -5.920  39.005  1.00105.03           C  
ANISOU 4649  CB  PRO A 609    12615  13503  13786   -202    162    370       C  
ATOM   4650  CG  PRO A 609     -27.557  -6.855  39.222  1.00 96.02           C  
ANISOU 4650  CG  PRO A 609    11493  12375  12613   -212    142    393       C  
ATOM   4651  CD  PRO A 609     -26.573  -6.649  38.094  1.00 94.43           C  
ANISOU 4651  CD  PRO A 609    11306  12161  12408   -190    114    396       C  
ATOM   4652  N   ASN A 613     -25.960   1.023  40.941  1.00 93.56           N  
ANISOU 4652  N   ASN A 613    11216  12089  12241   -210    263    263       N  
ATOM   4653  CA  ASN A 613     -25.249   1.730  39.902  1.00 87.05           C  
ANISOU 4653  CA  ASN A 613    10402  11251  11421   -187    242    260       C  
ATOM   4654  C   ASN A 613     -24.298   2.597  40.737  1.00 88.86           C  
ANISOU 4654  C   ASN A 613    10649  11499  11615   -201    260    249       C  
ATOM   4655  O   ASN A 613     -23.477   3.351  40.213  1.00 90.89           O  
ANISOU 4655  O   ASN A 613    10918  11751  11863   -188    249    244       O  
ATOM   4656  CB  ASN A 613     -26.278   2.569  39.163  1.00 89.12           C  
ANISOU 4656  CB  ASN A 613    10644  11489  11726   -168    245    241       C  
ATOM   4657  CG  ASN A 613     -25.946   2.846  37.700  1.00 86.52           C  
ANISOU 4657  CG  ASN A 613    10319  11138  11414   -140    213    244       C  
ATOM   4658  OD1 ASN A 613     -24.820   2.685  37.197  1.00 87.41           O  
ANISOU 4658  OD1 ASN A 613    10452  11253  11505   -134    191    257       O  
ATOM   4659  ND2 ASN A 613     -27.013   3.273  36.998  1.00 79.78           N  
ANISOU 4659  ND2 ASN A 613     9446  10261  10603   -125    210    233       N  
ATOM   4660  N   THR A 614     -24.467   2.462  42.058  1.00 87.17           N  
ANISOU 4660  N   THR A 614    10435  11306  11378   -228    288    246       N  
ATOM   4661  CA  THR A 614     -23.514   2.842  43.112  1.00 83.96           C  
ANISOU 4661  CA  THR A 614    10048  10923  10928   -250    303    243       C  
ATOM   4662  C   THR A 614     -23.881   1.953  44.316  1.00 83.59           C  
ANISOU 4662  C   THR A 614    10000  10896  10861   -281    321    253       C  
ATOM   4663  O   THR A 614     -25.061   1.644  44.473  1.00 88.39           O  
ANISOU 4663  O   THR A 614    10588  11499  11494   -284    335    248       O  
ATOM   4664  CB  THR A 614     -23.598   4.339  43.461  0.00 20.00           C  
ATOM   4665  OG1 THR A 614     -24.940   4.670  43.837  0.00 20.00           O  
ATOM   4666  CG2 THR A 614     -23.361   5.191  42.222  0.00 20.00           C  
ATOM   4667  N   SER A 615     -22.940   1.494  45.153  1.00 81.78           N  
ANISOU 4667  N   SER A 615     9790  10689  10591   -303    319    269       N  
ATOM   4668  CA  SER A 615     -21.481   1.584  45.005  1.00 77.53           C  
ANISOU 4668  CA  SER A 615     9275  10156  10024   -301    298    281       C  
ATOM   4669  C   SER A 615     -20.949   0.166  44.724  1.00 78.43           C  
ANISOU 4669  C   SER A 615     9396  10272  10132   -303    266    314       C  
ATOM   4670  O   SER A 615     -21.463  -0.487  43.816  1.00 76.74           O  
ANISOU 4670  O   SER A 615     9169  10040   9947   -285    247    322       O  
ATOM   4671  CB  SER A 615     -20.860   2.207  46.266  1.00 75.64           C  
ANISOU 4671  CB  SER A 615     9052   9941   9744   -328    321    272       C  
ATOM   4672  OG  SER A 615     -19.488   1.904  46.417  1.00 66.86           O  
ANISOU 4672  OG  SER A 615     7962   8839   8600   -335    300    291       O  
ATOM   4673  N   LEU A 616     -19.956  -0.324  45.482  1.00 75.29           N  
ANISOU 4673  N   LEU A 616     9016   9892   9697   -324    258    331       N  
ATOM   4674  CA  LEU A 616     -19.323  -1.628  45.165  1.00 75.79           C  
ANISOU 4674  CA  LEU A 616     9085   9954   9757   -324    225    362       C  
ATOM   4675  C   LEU A 616     -18.919  -2.493  46.355  1.00 74.96           C  
ANISOU 4675  C   LEU A 616     8991   9871   9620   -357    225    384       C  
ATOM   4676  O   LEU A 616     -19.317  -3.654  46.441  1.00 74.42           O  
ANISOU 4676  O   LEU A 616     8914   9801   9559   -365    215    404       O  
ATOM   4677  CB  LEU A 616     -18.094  -1.451  44.267  1.00 74.14           C  
ANISOU 4677  CB  LEU A 616     8888   9734   9545   -304    198    369       C  
ATOM   4678  CG  LEU A 616     -17.303  -2.731  43.974  1.00 73.36           C  
ANISOU 4678  CG  LEU A 616     8795   9633   9443   -304    164    399       C  
ATOM   4679  CD1 LEU A 616     -17.463  -3.147  42.523  1.00 70.76           C  
ANISOU 4679  CD1 LEU A 616     8457   9281   9148   -274    140    403       C  
ATOM   4680  CD2 LEU A 616     -15.836  -2.541  44.312  1.00 73.66           C  
ANISOU 4680  CD2 LEU A 616     8854   9682   9452   -312    153    408       C  
ATOM   4681  N   VAL A 617     -18.092  -1.938  47.239  1.00 76.68           N  
ANISOU 4681  N   VAL A 617     9226  10106   9802   -377    235    381       N  
ATOM   4682  CA  VAL A 617     -17.591  -2.666  48.407  1.00 73.44           C  
ANISOU 4682  CA  VAL A 617     8829   9717   9357   -411    233    403       C  
ATOM   4683  C   VAL A 617     -18.731  -2.961  49.394  1.00 78.92           C  
ANISOU 4683  C   VAL A 617     9515  10424  10046   -437    261    399       C  
ATOM   4684  O   VAL A 617     -18.561  -3.733  50.345  1.00 80.20           O  
ANISOU 4684  O   VAL A 617     9686  10603  10183   -467    260    419       O  
ATOM   4685  CB  VAL A 617     -16.454  -1.904  49.129  1.00 69.99           C  
ANISOU 4685  CB  VAL A 617     8413   9294   8882   -427    237    399       C  
ATOM   4686  CG1 VAL A 617     -15.269  -2.829  49.353  1.00 68.56           C  
ANISOU 4686  CG1 VAL A 617     8247   9119   8682   -438    206    431       C  
ATOM   4687  CG2 VAL A 617     -16.010  -0.683  48.337  1.00 67.62           C  
ANISOU 4687  CG2 VAL A 617     8117   8983   8593   -400    239    377       C  
ATOM   4688  N   LEU A 618     -19.893  -2.350  49.144  1.00 80.83           N  
ANISOU 4688  N   LEU A 618     9739  10658  10312   -426    287    374       N  
ATOM   4689  CA  LEU A 618     -21.095  -2.533  49.961  1.00 80.11           C  
ANISOU 4689  CA  LEU A 618     9636  10577  10222   -448    317    366       C  
ATOM   4690  C   LEU A 618     -21.875  -3.818  49.640  1.00 81.53           C  
ANISOU 4690  C   LEU A 618     9800  10748  10427   -446    304    386       C  
ATOM   4691  O   LEU A 618     -22.854  -4.135  50.325  1.00 83.26           O  
ANISOU 4691  O   LEU A 618    10010  10976  10648   -466    327    383       O  
ATOM   4692  CB  LEU A 618     -22.029  -1.311  49.844  1.00 78.03           C  
ANISOU 4692  CB  LEU A 618     9360  10307   9981   -437    351    329       C  
ATOM   4693  CG  LEU A 618     -21.780   0.018  50.585  1.00 76.18           C  
ANISOU 4693  CG  LEU A 618     9135  10085   9722   -450    382    302       C  
ATOM   4694  CD1 LEU A 618     -20.953  -0.152  51.857  1.00 77.01           C  
ANISOU 4694  CD1 LEU A 618     9264  10217   9776   -487    387    313       C  
ATOM   4695  CD2 LEU A 618     -21.145   1.055  49.679  1.00 73.89           C  
ANISOU 4695  CD2 LEU A 618     8849   9780   9444   -420    371    287       C  
ATOM   4696  N   ASP A 619     -21.438  -4.551  48.612  1.00 78.25           N  
ANISOU 4696  N   ASP A 619     9383  10317  10031   -423    267    405       N  
ATOM   4697  CA  ASP A 619     -22.108  -5.780  48.165  1.00 78.21           C  
ANISOU 4697  CA  ASP A 619     9362  10301  10052   -417    250    424       C  
ATOM   4698  C   ASP A 619     -22.094  -6.891  49.223  1.00 82.80           C  
ANISOU 4698  C   ASP A 619     9949  10900  10610   -452    248    450       C  
ATOM   4699  O   ASP A 619     -21.033  -7.243  49.745  1.00 81.00           O  
ANISOU 4699  O   ASP A 619     9739  10684  10352   -468    232    469       O  
ATOM   4700  CB  ASP A 619     -21.477  -6.277  46.865  1.00 73.86           C  
ANISOU 4700  CB  ASP A 619     8810   9729   9522   -387    211    438       C  
ATOM   4701  CG  ASP A 619     -22.016  -7.628  46.428  1.00 72.45           C  
ANISOU 4701  CG  ASP A 619     8618   9540   9369   -383    190    460       C  
ATOM   4702  OD1 ASP A 619     -23.131  -7.690  45.871  1.00 70.20           O  
ANISOU 4702  OD1 ASP A 619     8314   9241   9117   -368    197    450       O  
ATOM   4703  OD2 ASP A 619     -21.307  -8.634  46.625  1.00 71.74           O  
ANISOU 4703  OD2 ASP A 619     8536   9454   9267   -393    166    487       O  
ATOM   4704  N   PHE A 620     -23.276  -7.447  49.506  1.00 90.71           N  
ANISOU 4704  N   PHE A 620    10935  11903  11628   -462    263    451       N  
ATOM   4705  CA  PHE A 620     -23.484  -8.408  50.602  1.00 93.72           C  
ANISOU 4705  CA  PHE A 620    11320  12302  11987   -497    268    472       C  
ATOM   4706  C   PHE A 620     -23.996  -9.764  50.099  1.00 89.02           C  
ANISOU 4706  C   PHE A 620    10709  11694  11419   -491    244    496       C  
ATOM   4707  O   PHE A 620     -24.733  -9.819  49.113  1.00 79.64           O  
ANISOU 4707  O   PHE A 620     9502  10485  10270   -463    239    488       O  
ATOM   4708  CB  PHE A 620     -24.486  -7.822  51.609  1.00 98.16           C  
ANISOU 4708  CB  PHE A 620    11877  12880  12539   -522    313    451       C  
ATOM   4709  CG  PHE A 620     -24.273  -8.279  53.025  1.00104.75           C  
ANISOU 4709  CG  PHE A 620    12726  13741  13330   -567    325    466       C  
ATOM   4710  CD1 PHE A 620     -24.932  -9.403  53.517  1.00107.83           C  
ANISOU 4710  CD1 PHE A 620    13110  14138  13723   -588    325    487       C  
ATOM   4711  CD2 PHE A 620     -23.418  -7.580  53.876  1.00109.56           C  
ANISOU 4711  CD2 PHE A 620    13360  14371  13898   -589    336    461       C  
ATOM   4712  CE1 PHE A 620     -24.735  -9.827  54.826  1.00109.78           C  
ANISOU 4712  CE1 PHE A 620    13372  14410  13929   -632    335    503       C  
ATOM   4713  CE2 PHE A 620     -23.217  -7.997  55.188  1.00109.72           C  
ANISOU 4713  CE2 PHE A 620    13395  14415  13876   -632    345    476       C  
ATOM   4714  CZ  PHE A 620     -23.877  -9.123  55.663  1.00109.99           C  
ANISOU 4714  CZ  PHE A 620    13422  14456  13911   -654    345    498       C  
ATOM   4715  N   ASN A 621     -23.602 -10.852  50.767  1.00 92.03           N  
ANISOU 4715  N   ASN A 621    11099  12087  11781   -516    228    527       N  
ATOM   4716  CA  ASN A 621     -24.211 -12.165  50.509  1.00 95.94           C  
ANISOU 4716  CA  ASN A 621    11579  12573  12301   -516    210    550       C  
ATOM   4717  C   ASN A 621     -25.567 -12.258  51.190  1.00104.14           C  
ANISOU 4717  C   ASN A 621    12603  13620  13344   -536    243    541       C  
ATOM   4718  O   ASN A 621     -25.659 -12.246  52.424  1.00104.35           O  
ANISOU 4718  O   ASN A 621    12639  13669  13337   -572    265    544       O  
ATOM   4719  CB  ASN A 621     -23.371 -13.341  51.021  1.00 90.78           C  
ANISOU 4719  CB  ASN A 621    10937  11927  11626   -538    180    587       C  
ATOM   4720  CG  ASN A 621     -21.911 -13.257  50.642  1.00 83.38           C  
ANISOU 4720  CG  ASN A 621    10016  10985  10677   -527    150    597       C  
ATOM   4721  OD1 ASN A 621     -21.547 -13.034  49.487  1.00 80.78           O  
ANISOU 4721  OD1 ASN A 621     9682  10637  10371   -493    133    589       O  
ATOM   4722  ND2 ASN A 621     -21.065 -13.469  51.638  1.00 79.30           N  
ANISOU 4722  ND2 ASN A 621     9518  10487  10124   -558    144    616       N  
ATOM   4723  N   ASN A 622     -26.617 -12.362  50.384  1.00108.12           N  
ANISOU 4723  N   ASN A 622    13084  14105  13890   -513    247    530       N  
ATOM   4724  CA  ASN A 622     -27.970 -12.487  50.902  1.00106.10           C  
ANISOU 4724  CA  ASN A 622    12811  13854  13647   -528    277    520       C  
ATOM   4725  C   ASN A 622     -28.711 -13.608  50.185  1.00105.19           C  
ANISOU 4725  C   ASN A 622    12675  13720  13570   -514    256    537       C  
ATOM   4726  O   ASN A 622     -28.482 -14.782  50.478  1.00105.45           O  
ANISOU 4726  O   ASN A 622    12711  13757  13597   -529    235    567       O  
ATOM   4727  CB  ASN A 622     -28.714 -11.146  50.810  1.00105.91           C  
ANISOU 4727  CB  ASN A 622    12776  13826  13636   -517    314    481       C  
ATOM   4728  CG  ASN A 622     -28.157 -10.103  51.768  1.00107.35           C  
ANISOU 4728  CG  ASN A 622    12979  14031  13778   -539    342    465       C  
ATOM   4729  OD1 ASN A 622     -27.560  -9.113  51.347  1.00106.39           O  
ANISOU 4729  OD1 ASN A 622    12865  13904  13653   -521    341    447       O  
ATOM   4730  ND2 ASN A 622     -28.340 -10.330  53.066  1.00108.53           N  
ANISOU 4730  ND2 ASN A 622    13136  14204  13894   -579    365    470       N  
ATOM   4731  N   SER A 623     -29.576 -13.246  49.241  1.00102.90           N  
ANISOU 4731  N   SER A 623    12365  13409  13322   -484    261    517       N  
ATOM   4732  CA  SER A 623     -30.335 -14.213  48.451  1.00104.18           C  
ANISOU 4732  CA  SER A 623    12506  13551  13524   -468    241    530       C  
ATOM   4733  C   SER A 623     -29.397 -15.132  47.670  1.00105.59           C  
ANISOU 4733  C   SER A 623    12692  13718  13707   -452    194    556       C  
ATOM   4734  O   SER A 623     -28.340 -14.689  47.224  1.00103.56           O  
ANISOU 4734  O   SER A 623    12450  13458  13438   -438    178    554       O  
ATOM   4735  CB  SER A 623     -31.265 -13.480  47.484  1.00103.25           C  
ANISOU 4735  CB  SER A 623    12369  13412  13450   -437    250    503       C  
ATOM   4736  OG  SER A 623     -31.888 -12.376  48.115  1.00100.14           O  
ANISOU 4736  OG  SER A 623    11970  13027  13051   -447    292    474       O  
ATOM   4737  N   THR A 624     -29.790 -16.402  47.519  1.00110.02           N  
ANISOU 4737  N   THR A 624    13242  14271  14287   -455    174    579       N  
ATOM   4738  CA  THR A 624     -29.007 -17.443  46.810  1.00111.70           C  
ANISOU 4738  CA  THR A 624    13459  14472  14508   -442    131    605       C  
ATOM   4739  C   THR A 624     -27.587 -17.598  47.354  1.00111.81           C  
ANISOU 4739  C   THR A 624    13497  14500  14485   -458    115    623       C  
ATOM   4740  O   THR A 624     -27.163 -18.697  47.720  1.00106.31           O  
ANISOU 4740  O   THR A 624    12804  13807  13781   -475     93    652       O  
ATOM   4741  CB  THR A 624     -28.926 -17.196  45.277  1.00111.21           C  
ANISOU 4741  CB  THR A 624    13390  14383  14480   -401    108    593       C  
ATOM   4742  OG1 THR A 624     -30.240 -17.006  44.740  1.00115.87           O  
ANISOU 4742  OG1 THR A 624    13958  14958  15106   -386    121    577       O  
ATOM   4743  CG2 THR A 624     -28.244 -18.368  44.555  1.00101.78           C  
ANISOU 4743  CG2 THR A 624    12198  13175  13298   -389     66    618       C  
ATOM   4744  N   CYS A 625     -26.874 -16.477  47.402  1.00115.39           N  
ANISOU 4744  N   CYS A 625    13965  14960  14916   -453    125    605       N  
ATOM   4745  CA  CYS A 625     -25.440 -16.449  47.645  1.00120.90           C  
ANISOU 4745  CA  CYS A 625    14685  15666  15584   -460    107    618       C  
ATOM   4746  C   CYS A 625     -25.077 -15.878  49.020  1.00123.79           C  
ANISOU 4746  C   CYS A 625    15069  16060  15906   -495    132    617       C  
ATOM   4747  O   CYS A 625     -24.060 -16.258  49.607  1.00117.86           O  
ANISOU 4747  O   CYS A 625    14334  15320  15126   -514    116    638       O  
ATOM   4748  CB  CYS A 625     -24.745 -15.670  46.517  1.00113.60           C  
ANISOU 4748  CB  CYS A 625    13765  14726  14669   -426     94    601       C  
ATOM   4749  SG  CYS A 625     -25.255 -13.945  46.281  1.00107.17           S  
ANISOU 4749  SG  CYS A 625    12949  13911  13857   -411    129    561       S  
TER    4750      CYS A 625                                                      
ATOM   4751  N   GLN C  21     -13.255  44.473  25.386  1.00 60.08           N  
ANISOU 4751  N   GLN C  21     6912   7457   8456    105    161  -1492       N  
ATOM   4752  CA  GLN C  21     -12.431  44.572  24.142  1.00 61.63           C  
ANISOU 4752  CA  GLN C  21     7148   7618   8648    148    114  -1401       C  
ATOM   4753  C   GLN C  21     -11.190  45.439  24.349  1.00 62.32           C  
ANISOU 4753  C   GLN C  21     7267   7689   8721    137     98  -1348       C  
ATOM   4754  O   GLN C  21     -11.291  46.605  24.734  1.00 62.39           O  
ANISOU 4754  O   GLN C  21     7261   7670   8771    139     83  -1392       O  
ATOM   4755  CB  GLN C  21     -13.258  45.096  22.962  1.00 61.73           C  
ANISOU 4755  CB  GLN C  21     7144   7582   8728    213     64  -1425       C  
ATOM   4756  CG  GLN C  21     -12.509  45.058  21.636  1.00 68.35           C  
ANISOU 4756  CG  GLN C  21     8022   8392   9554    253     19  -1332       C  
ATOM   4757  CD  GLN C  21     -13.297  45.633  20.466  1.00 72.63           C  
ANISOU 4757  CD  GLN C  21     8551   8884  10158    314    -36  -1350       C  
ATOM   4758  OE1 GLN C  21     -13.038  46.756  20.022  1.00 74.66           O  
ANISOU 4758  OE1 GLN C  21     8817   9096  10452    339    -81  -1335       O  
ATOM   4759  NE2 GLN C  21     -14.252  44.860  19.952  1.00 69.92           N  
ANISOU 4759  NE2 GLN C  21     8188   8548   9828    335    -36  -1380       N  
ATOM   4760  N   GLN C  22     -10.025  44.861  24.063  1.00 62.95           N  
ANISOU 4760  N   GLN C  22     7387   7783   8747    127     99  -1255       N  
ATOM   4761  CA  GLN C  22      -8.735  45.500  24.327  1.00 62.42           C  
ANISOU 4761  CA  GLN C  22     7349   7708   8656    108     89  -1197       C  
ATOM   4762  C   GLN C  22      -8.166  46.229  23.120  1.00 62.10           C  
ANISOU 4762  C   GLN C  22     7332   7622   8638    154     36  -1136       C  
ATOM   4763  O   GLN C  22      -7.549  47.285  23.261  1.00 61.91           O  
ANISOU 4763  O   GLN C  22     7319   7572   8631    151     14  -1120       O  
ATOM   4764  CB  GLN C  22      -7.722  44.461  24.796  1.00 63.35           C  
ANISOU 4764  CB  GLN C  22     7496   7871   8702     66    121  -1131       C  
ATOM   4765  CG  GLN C  22      -8.160  43.671  26.012  1.00 64.59           C  
ANISOU 4765  CG  GLN C  22     7637   8077   8828     12    172  -1177       C  
ATOM   4766  CD  GLN C  22      -8.325  44.543  27.234  1.00 67.75           C  
ANISOU 4766  CD  GLN C  22     8018   8485   9237    -26    191  -1242       C  
ATOM   4767  OE1 GLN C  22      -7.474  45.388  27.535  1.00 66.20           O  
ANISOU 4767  OE1 GLN C  22     7838   8274   9038    -37    177  -1218       O  
ATOM   4768  NE2 GLN C  22      -9.425  44.343  27.952  1.00 69.83           N  
ANISOU 4768  NE2 GLN C  22     8247   8773   9511    -48    223  -1327       N  
ATOM   4769  N   TRP C  23      -8.369  45.652  21.940  1.00 60.53           N  
ANISOU 4769  N   TRP C  23     7143   7416   8439    194     16  -1101       N  
ATOM   4770  CA  TRP C  23      -7.805  46.180  20.702  1.00 61.03           C  
ANISOU 4770  CA  TRP C  23     7231   7445   8511    234    -31  -1034       C  
ATOM   4771  C   TRP C  23      -8.562  45.611  19.523  1.00 60.17           C  
ANISOU 4771  C   TRP C  23     7118   7327   8416    279    -53  -1034       C  
ATOM   4772  O   TRP C  23      -9.286  44.625  19.677  1.00 57.55           O  
ANISOU 4772  O   TRP C  23     6768   7021   8074    276    -26  -1070       O  
ATOM   4773  CB  TRP C  23      -6.302  45.861  20.645  1.00 59.55           C  
ANISOU 4773  CB  TRP C  23     7080   7280   8266    212    -22   -942       C  
ATOM   4774  CG  TRP C  23      -5.627  46.253  19.357  1.00 58.15           C  
ANISOU 4774  CG  TRP C  23     6928   7078   8085    246    -63   -866       C  
ATOM   4775  CD1 TRP C  23      -5.219  47.525  18.961  1.00 59.05           C  
ANISOU 4775  CD1 TRP C  23     7053   7151   8229    258   -106   -840       C  
ATOM   4776  CD2 TRP C  23      -5.273  45.371  18.240  1.00 58.45           C  
ANISOU 4776  CD2 TRP C  23     6986   7135   8088    271    -68   -806       C  
ATOM   4777  NE1 TRP C  23      -4.656  47.493  17.710  1.00 58.77           N  
ANISOU 4777  NE1 TRP C  23     7042   7110   8175    284   -134   -766       N  
ATOM   4778  CE2 TRP C  23      -4.657  46.233  17.217  1.00 59.43           C  
ANISOU 4778  CE2 TRP C  23     7132   7230   8218    295   -112   -746       C  
ATOM   4779  CE3 TRP C  23      -5.403  44.008  17.989  1.00 57.11           C  
ANISOU 4779  CE3 TRP C  23     6817   6999   7883    276    -43   -799       C  
ATOM   4780  CZ2 TRP C  23      -4.196  45.726  16.007  1.00 57.64           C  
ANISOU 4780  CZ2 TRP C  23     6926   7016   7958    320   -125   -683       C  
ATOM   4781  CZ3 TRP C  23      -4.937  43.511  16.766  1.00 58.82           C  
ANISOU 4781  CZ3 TRP C  23     7054   7223   8070    306    -58   -739       C  
ATOM   4782  CH2 TRP C  23      -4.342  44.350  15.804  1.00 59.02           C  
ANISOU 4782  CH2 TRP C  23     7099   7227   8097    327    -96   -683       C  
ATOM   4783  N   PHE C  24      -8.439  46.252  18.356  1.00 60.74           N  
ANISOU 4783  N   PHE C  24     7205   7363   8509    319   -103   -995       N  
ATOM   4784  CA  PHE C  24      -9.033  45.751  17.106  1.00 62.60           C  
ANISOU 4784  CA  PHE C  24     7443   7591   8751    363   -130   -984       C  
ATOM   4785  C   PHE C  24      -8.473  46.428  15.850  1.00 62.34           C  
ANISOU 4785  C   PHE C  24     7439   7527   8719    394   -182   -914       C  
ATOM   4786  O   PHE C  24      -8.061  47.587  15.897  1.00 61.62           O  
ANISOU 4786  O   PHE C  24     7356   7403   8653    391   -211   -897       O  
ATOM   4787  CB  PHE C  24     -10.575  45.843  17.136  1.00 68.00           C  
ANISOU 4787  CB  PHE C  24     8088   8254   9493    386   -141  -1075       C  
ATOM   4788  CG  PHE C  24     -11.127  47.207  16.802  1.00 73.81           C  
ANISOU 4788  CG  PHE C  24     8810   8932  10300    415   -195  -1106       C  
ATOM   4789  CD1 PHE C  24     -11.598  47.488  15.516  1.00 75.88           C  
ANISOU 4789  CD1 PHE C  24     9079   9160  10591    462   -251  -1089       C  
ATOM   4790  CD2 PHE C  24     -11.198  48.207  17.772  1.00 77.84           C  
ANISOU 4790  CD2 PHE C  24     9303   9422  10851    396   -194  -1155       C  
ATOM   4791  CE1 PHE C  24     -12.111  48.741  15.201  1.00 78.47           C  
ANISOU 4791  CE1 PHE C  24     9395   9430  10989    489   -308  -1115       C  
ATOM   4792  CE2 PHE C  24     -11.713  49.463  17.462  1.00 81.97           C  
ANISOU 4792  CE2 PHE C  24     9812   9885  11446    425   -249  -1186       C  
ATOM   4793  CZ  PHE C  24     -12.170  49.730  16.176  1.00 81.14           C  
ANISOU 4793  CZ  PHE C  24     9713   9743  11372    471   -307  -1164       C  
ATOM   4794  N   CYS C  25      -8.455  45.694  14.736  1.00 62.31           N  
ANISOU 4794  N   CYS C  25     7451   7537   8686    421   -194   -874       N  
ATOM   4795  CA  CYS C  25      -8.158  46.263  13.415  1.00 63.59           C  
ANISOU 4795  CA  CYS C  25     7639   7675   8848    453   -245   -816       C  
ATOM   4796  C   CYS C  25      -9.025  45.618  12.345  1.00 62.73           C  
ANISOU 4796  C   CYS C  25     7526   7565   8741    492   -268   -828       C  
ATOM   4797  O   CYS C  25      -9.751  44.659  12.617  1.00 61.51           O  
ANISOU 4797  O   CYS C  25     7351   7431   8586    494   -240   -877       O  
ATOM   4798  CB  CYS C  25      -6.666  46.146  13.039  1.00 67.61           C  
ANISOU 4798  CB  CYS C  25     8182   8209   9296    436   -236   -723       C  
ATOM   4799  SG  CYS C  25      -5.981  44.468  12.844  1.00 78.07           S  
ANISOU 4799  SG  CYS C  25     9519   9596  10545    429   -186   -685       S  
ATOM   4800  N   ASN C  26      -8.948  46.160  11.134  1.00 64.23           N  
ANISOU 4800  N   ASN C  26     7737   7732   8933    520   -319   -783       N  
ATOM   4801  CA  ASN C  26      -9.575  45.553   9.966  1.00 70.00           C  
ANISOU 4801  CA  ASN C  26     8473   8467   9655    556   -345   -781       C  
ATOM   4802  C   ASN C  26      -8.650  45.607   8.755  1.00 73.20           C  
ANISOU 4802  C   ASN C  26     8917   8886  10007    565   -368   -692       C  
ATOM   4803  O   ASN C  26      -7.949  46.598   8.544  1.00 75.86           O  
ANISOU 4803  O   ASN C  26     9273   9204  10344    555   -394   -641       O  
ATOM   4804  CB  ASN C  26     -10.939  46.195   9.649  1.00 72.69           C  
ANISOU 4804  CB  ASN C  26     8790   8759  10068    588   -396   -840       C  
ATOM   4805  CG  ASN C  26     -10.876  47.714   9.530  1.00 74.65           C  
ANISOU 4805  CG  ASN C  26     9044   8953  10366    592   -451   -825       C  
ATOM   4806  OD1 ASN C  26      -9.830  48.330   9.731  1.00 76.01           O  
ANISOU 4806  OD1 ASN C  26     9237   9123  10519    569   -449   -772       O  
ATOM   4807  ND2 ASN C  26     -12.012  48.326   9.205  1.00 76.38           N  
ANISOU 4807  ND2 ASN C  26     9242   9124  10652    623   -503   -874       N  
ATOM   4808  N   SER C  27      -8.632  44.528   7.980  1.00 71.15           N  
ANISOU 4808  N   SER C  27     8669   8662   9702    581   -356   -676       N  
ATOM   4809  CA  SER C  27      -7.892  44.490   6.723  1.00 67.90           C  
ANISOU 4809  CA  SER C  27     8291   8271   9237    592   -377   -602       C  
ATOM   4810  C   SER C  27      -8.843  44.062   5.608  1.00 67.14           C  
ANISOU 4810  C   SER C  27     8196   8170   9142    630   -413   -621       C  
ATOM   4811  O   SER C  27     -10.034  43.852   5.858  1.00 67.10           O  
ANISOU 4811  O   SER C  27     8164   8144   9185    646   -423   -690       O  
ATOM   4812  CB  SER C  27      -6.686  43.554   6.828  1.00 64.83           C  
ANISOU 4812  CB  SER C  27     7915   7936   8779    572   -324   -558       C  
ATOM   4813  OG  SER C  27      -7.076  42.273   7.283  1.00 63.12           O  
ANISOU 4813  OG  SER C  27     7681   7745   8554    574   -283   -604       O  
ATOM   4814  N   SER C  28      -8.319  43.919   4.392  1.00 66.16           N  
ANISOU 4814  N   SER C  28     8102   8069   8965    641   -432   -562       N  
ATOM   4815  CA  SER C  28      -9.152  43.685   3.205  1.00 67.99           C  
ANISOU 4815  CA  SER C  28     8342   8296   9195    675   -477   -571       C  
ATOM   4816  C   SER C  28     -10.073  42.459   3.265  1.00 67.92           C  
ANISOU 4816  C   SER C  28     8311   8302   9193    695   -457   -636       C  
ATOM   4817  O   SER C  28     -10.930  42.296   2.395  1.00 68.66           O  
ANISOU 4817  O   SER C  28     8405   8386   9295    724   -497   -655       O  
ATOM   4818  CB  SER C  28      -8.289  43.636   1.942  1.00 68.48           C  
ANISOU 4818  CB  SER C  28     8441   8393   9185    677   -490   -495       C  
ATOM   4819  OG  SER C  28      -7.500  42.462   1.913  1.00 69.28           O  
ANISOU 4819  OG  SER C  28     8547   8551   9225    671   -435   -482       O  
ATOM   4820  N   ASP C  29      -9.900  41.605   4.277  1.00 68.22           N  
ANISOU 4820  N   ASP C  29     8330   8363   9227    678   -399   -668       N  
ATOM   4821  CA  ASP C  29     -10.755  40.421   4.446  1.00 65.79           C  
ANISOU 4821  CA  ASP C  29     7999   8067   8929    691   -378   -729       C  
ATOM   4822  C   ASP C  29     -10.971  39.960   5.894  1.00 63.63           C  
ANISOU 4822  C   ASP C  29     7695   7795   8683    665   -328   -780       C  
ATOM   4823  O   ASP C  29     -11.453  38.851   6.123  1.00 63.35           O  
ANISOU 4823  O   ASP C  29     7645   7777   8647    666   -303   -819       O  
ATOM   4824  CB  ASP C  29     -10.276  39.248   3.562  1.00 69.06           C  
ANISOU 4824  CB  ASP C  29     8433   8527   9279    704   -362   -703       C  
ATOM   4825  CG  ASP C  29      -8.814  38.854   3.812  1.00 75.06           C  
ANISOU 4825  CG  ASP C  29     9210   9327   9982    680   -316   -650       C  
ATOM   4826  OD1 ASP C  29      -8.326  38.957   4.962  1.00 77.96           O  
ANISOU 4826  OD1 ASP C  29     9566   9694  10360    650   -280   -651       O  
ATOM   4827  OD2 ASP C  29      -8.152  38.416   2.843  1.00 73.49           O  
ANISOU 4827  OD2 ASP C  29     9034   9162   9727    691   -315   -609       O  
ATOM   4828  N   ALA C  30     -10.636  40.803   6.868  1.00 61.41           N  
ANISOU 4828  N   ALA C  30     7406   7497   8427    638   -316   -779       N  
ATOM   4829  CA  ALA C  30     -10.824  40.428   8.274  1.00 62.26           C  
ANISOU 4829  CA  ALA C  30     7487   7612   8556    608   -269   -826       C  
ATOM   4830  C   ALA C  30     -11.049  41.589   9.232  1.00 62.31           C  
ANISOU 4830  C   ALA C  30     7475   7584   8613    590   -274   -855       C  
ATOM   4831  O   ALA C  30     -10.428  42.647   9.102  1.00 60.97           O  
ANISOU 4831  O   ALA C  30     7322   7396   8447    586   -298   -814       O  
ATOM   4832  CB  ALA C  30      -9.650  39.582   8.764  1.00 62.79           C  
ANISOU 4832  CB  ALA C  30     7568   7720   8568    580   -218   -787       C  
ATOM   4833  N   ILE C  31     -11.945  41.380  10.194  1.00 62.78           N  
ANISOU 4833  N   ILE C  31     7499   7638   8713    578   -252   -928       N  
ATOM   4834  CA  ILE C  31     -11.976  42.214  11.392  1.00 65.70           C  
ANISOU 4834  CA  ILE C  31     7849   7992   9119    550   -237   -961       C  
ATOM   4835  C   ILE C  31     -11.466  41.358  12.552  1.00 65.11           C  
ANISOU 4835  C   ILE C  31     7771   7958   9010    507   -174   -966       C  
ATOM   4836  O   ILE C  31     -12.007  40.284  12.846  1.00 63.93           O  
ANISOU 4836  O   ILE C  31     7605   7831   8854    499   -146  -1001       O  
ATOM   4837  CB  ILE C  31     -13.363  42.874  11.687  1.00 68.83           C  
ANISOU 4837  CB  ILE C  31     8206   8351   9592    565   -262  -1044       C  
ATOM   4838  CG1 ILE C  31     -14.073  42.234  12.893  1.00 68.22           C  
ANISOU 4838  CG1 ILE C  31     8092   8296   9532    536   -212  -1118       C  
ATOM   4839  CG2 ILE C  31     -14.250  42.903  10.442  1.00 67.89           C  
ANISOU 4839  CG2 ILE C  31     8086   8208   9501    611   -316  -1055       C  
ATOM   4840  CD1 ILE C  31     -14.951  43.187  13.680  1.00 69.64           C  
ANISOU 4840  CD1 ILE C  31     8232   8446   9781    533   -219  -1196       C  
ATOM   4841  N   ILE C  32     -10.391  41.824  13.175  1.00 64.36           N  
ANISOU 4841  N   ILE C  32     7690   7869   8892    477   -156   -926       N  
ATOM   4842  CA  ILE C  32      -9.758  41.105  14.272  1.00 62.63           C  
ANISOU 4842  CA  ILE C  32     7472   7686   8637    433   -103   -920       C  
ATOM   4843  C   ILE C  32      -9.891  41.946  15.537  1.00 61.70           C  
ANISOU 4843  C   ILE C  32     7335   7558   8550    400    -87   -963       C  
ATOM   4844  O   ILE C  32      -9.768  43.171  15.487  1.00 63.23           O  
ANISOU 4844  O   ILE C  32     7530   7719   8774    407   -116   -961       O  
ATOM   4845  CB  ILE C  32      -8.270  40.806  13.956  1.00 63.80           C  
ANISOU 4845  CB  ILE C  32     7654   7858   8727    424    -92   -835       C  
ATOM   4846  CG1 ILE C  32      -8.148  40.069  12.620  1.00 62.96           C  
ANISOU 4846  CG1 ILE C  32     7565   7763   8591    460   -110   -799       C  
ATOM   4847  CG2 ILE C  32      -7.609  39.989  15.063  1.00 63.24           C  
ANISOU 4847  CG2 ILE C  32     7584   7822   8621    380    -43   -826       C  
ATOM   4848  CD1 ILE C  32      -6.736  39.975  12.095  1.00 64.43           C  
ANISOU 4848  CD1 ILE C  32     7782   7971   8726    458   -106   -718       C  
ATOM   4849  N   SER C  33     -10.168  41.279  16.656  1.00 58.60           N  
ANISOU 4849  N   SER C  33     6923   7192   8149    363    -42  -1004       N  
ATOM   4850  CA  SER C  33     -10.214  41.910  17.973  1.00 55.94           C  
ANISOU 4850  CA  SER C  33     6568   6857   7827    324    -18  -1046       C  
ATOM   4851  C   SER C  33      -9.895  40.896  19.071  1.00 54.38           C  
ANISOU 4851  C   SER C  33     6370   6704   7587    274     34  -1047       C  
ATOM   4852  O   SER C  33      -9.997  39.687  18.856  1.00 56.99           O  
ANISOU 4852  O   SER C  33     6704   7057   7891    272     49  -1034       O  
ATOM   4853  CB  SER C  33     -11.598  42.496  18.221  1.00 54.74           C  
ANISOU 4853  CB  SER C  33     6376   6682   7739    337    -28  -1137       C  
ATOM   4854  OG  SER C  33     -12.550  41.460  18.304  1.00 55.09           O  
ANISOU 4854  OG  SER C  33     6397   6747   7786    335     -7  -1182       O  
ATOM   4855  N   TYR C  34      -9.516  41.386  20.249  1.00 53.57           N  
ANISOU 4855  N   TYR C  34     6263   6611   7477    231     58  -1061       N  
ATOM   4856  CA  TYR C  34      -9.386  40.514  21.418  1.00 53.85           C  
ANISOU 4856  CA  TYR C  34     6295   6689   7476    176    106  -1071       C  
ATOM   4857  C   TYR C  34      -9.778  41.181  22.724  1.00 54.43           C  
ANISOU 4857  C   TYR C  34     6344   6771   7564    135    131  -1136       C  
ATOM   4858  O   TYR C  34      -9.790  42.410  22.841  1.00 53.55           O  
ANISOU 4858  O   TYR C  34     6226   6632   7486    144    112  -1161       O  
ATOM   4859  CB  TYR C  34      -7.967  39.927  21.540  1.00 54.49           C  
ANISOU 4859  CB  TYR C  34     6410   6792   7501    154    117   -987       C  
ATOM   4860  CG  TYR C  34      -6.902  40.895  22.031  1.00 54.24           C  
ANISOU 4860  CG  TYR C  34     6395   6753   7458    133    112   -953       C  
ATOM   4861  CD1 TYR C  34      -6.286  41.789  21.148  1.00 53.62           C  
ANISOU 4861  CD1 TYR C  34     6334   6645   7393    167     75   -910       C  
ATOM   4862  CD2 TYR C  34      -6.499  40.905  23.372  1.00 52.82           C  
ANISOU 4862  CD2 TYR C  34     6215   6599   7253     77    143   -962       C  
ATOM   4863  CE1 TYR C  34      -5.313  42.673  21.586  1.00 53.63           C  
ANISOU 4863  CE1 TYR C  34     6349   6639   7388    147     70   -877       C  
ATOM   4864  CE2 TYR C  34      -5.525  41.786  23.819  1.00 54.60           C  
ANISOU 4864  CE2 TYR C  34     6456   6818   7470     57    137   -932       C  
ATOM   4865  CZ  TYR C  34      -4.938  42.674  22.922  1.00 56.19           C  
ANISOU 4865  CZ  TYR C  34     6671   6986   7689     93    100   -890       C  
ATOM   4866  OH  TYR C  34      -3.964  43.559  23.348  1.00 57.10           O  
ANISOU 4866  OH  TYR C  34     6802   7094   7800     72     92   -859       O  
ATOM   4867  N   SER C  35     -10.095  40.340  23.700  1.00 53.15           N  
ANISOU 4867  N   SER C  35     6170   6647   7374     87    173  -1163       N  
ATOM   4868  CA  SER C  35     -10.261  40.753  25.073  1.00 52.58           C  
ANISOU 4868  CA  SER C  35     6082   6599   7297     35    206  -1215       C  
ATOM   4869  C   SER C  35      -9.524  39.718  25.913  1.00 53.05           C  
ANISOU 4869  C   SER C  35     6162   6701   7292    -21    239  -1169       C  
ATOM   4870  O   SER C  35      -8.905  38.810  25.367  1.00 55.52           O  
ANISOU 4870  O   SER C  35     6498   7018   7576    -12    232  -1103       O  
ATOM   4871  CB  SER C  35     -11.745  40.792  25.423  1.00 51.38           C  
ANISOU 4871  CB  SER C  35     5884   6454   7184     32    223  -1313       C  
ATOM   4872  OG  SER C  35     -12.270  39.488  25.494  1.00 49.78           O  
ANISOU 4872  OG  SER C  35     5674   6281   6958     13    248  -1316       O  
ATOM   4873  N   TYR C  36      -9.568  39.851  27.230  1.00 53.96           N  
ANISOU 4873  N   TYR C  36     6267   6848   7385    -79    273  -1205       N  
ATOM   4874  CA  TYR C  36      -8.952  38.850  28.082  1.00 57.27           C  
ANISOU 4874  CA  TYR C  36     6706   7308   7745   -138    301  -1163       C  
ATOM   4875  C   TYR C  36      -9.920  37.701  28.330  1.00 60.31           C  
ANISOU 4875  C   TYR C  36     7073   7722   8120   -163    328  -1195       C  
ATOM   4876  O   TYR C  36     -11.126  37.848  28.145  1.00 64.29           O  
ANISOU 4876  O   TYR C  36     7542   8222   8662   -146    334  -1266       O  
ATOM   4877  CB  TYR C  36      -8.491  39.465  29.404  1.00 59.60           C  
ANISOU 4877  CB  TYR C  36     7005   7628   8012   -196    324  -1180       C  
ATOM   4878  CG  TYR C  36      -7.469  40.577  29.265  1.00 59.18           C  
ANISOU 4878  CG  TYR C  36     6970   7547   7966   -179    297  -1146       C  
ATOM   4879  CD1 TYR C  36      -7.691  41.827  29.843  1.00 60.00           C  
ANISOU 4879  CD1 TYR C  36     7058   7642   8095   -187    299  -1206       C  
ATOM   4880  CD2 TYR C  36      -6.278  40.380  28.566  1.00 57.76           C  
ANISOU 4880  CD2 TYR C  36     6824   7351   7770   -156    271  -1055       C  
ATOM   4881  CE1 TYR C  36      -6.759  42.847  29.731  1.00 58.43           C  
ANISOU 4881  CE1 TYR C  36     6877   7416   7906   -175    272  -1174       C  
ATOM   4882  CE2 TYR C  36      -5.345  41.397  28.439  1.00 58.10           C  
ANISOU 4882  CE2 TYR C  36     6884   7370   7821   -145    247  -1022       C  
ATOM   4883  CZ  TYR C  36      -5.589  42.626  29.027  1.00 59.07           C  
ANISOU 4883  CZ  TYR C  36     6991   7481   7969   -155    247  -1080       C  
ATOM   4884  OH  TYR C  36      -4.665  43.636  28.911  1.00 59.04           O  
ANISOU 4884  OH  TYR C  36     7004   7451   7975   -146    221  -1046       O  
ATOM   4885  N   CYS C  37      -9.382  36.552  28.724  1.00 64.62           N  
ANISOU 4885  N   CYS C  37     7640   8293   8618   -202    340  -1140       N  
ATOM   4886  CA  CYS C  37     -10.203  35.405  29.097  1.00 70.49           C  
ANISOU 4886  CA  CYS C  37     8368   9066   9347   -238    365  -1162       C  
ATOM   4887  C   CYS C  37     -11.010  35.739  30.353  1.00 72.54           C  
ANISOU 4887  C   CYS C  37     8599   9364   9596   -297    406  -1239       C  
ATOM   4888  O   CYS C  37     -10.560  36.512  31.195  1.00 77.50           O  
ANISOU 4888  O   CYS C  37     9232  10007  10206   -330    418  -1251       O  
ATOM   4889  CB  CYS C  37      -9.327  34.161  29.308  1.00 71.42           C  
ANISOU 4889  CB  CYS C  37     8519   9199   9418   -270    364  -1081       C  
ATOM   4890  SG  CYS C  37      -8.590  33.503  27.782  1.00 76.45           S  
ANISOU 4890  SG  CYS C  37     9182   9797  10068   -200    322  -1004       S  
ATOM   4891  N   ASP C  38     -12.205  35.168  30.465  1.00 75.47           N  
ANISOU 4891  N   ASP C  38     8940   9755   9981   -312    428  -1294       N  
ATOM   4892  CA  ASP C  38     -13.102  35.435  31.595  1.00 79.06           C  
ANISOU 4892  CA  ASP C  38     9359  10252  10426   -369    471  -1376       C  
ATOM   4893  C   ASP C  38     -12.474  35.137  32.959  1.00 78.77           C  
ANISOU 4893  C   ASP C  38     9343  10263  10322   -454    501  -1350       C  
ATOM   4894  O   ASP C  38     -12.794  35.793  33.949  1.00 80.83           O  
ANISOU 4894  O   ASP C  38     9584  10556  10568   -498    532  -1412       O  
ATOM   4895  CB  ASP C  38     -14.401  34.623  31.457  1.00 81.85           C  
ANISOU 4895  CB  ASP C  38     9678  10622  10798   -377    490  -1424       C  
ATOM   4896  CG  ASP C  38     -15.231  35.022  30.244  1.00 82.64           C  
ANISOU 4896  CG  ASP C  38     9750  10680  10969   -299    463  -1467       C  
ATOM   4897  OD1 ASP C  38     -15.045  36.141  29.719  1.00 84.52           O  
ANISOU 4897  OD1 ASP C  38     9985  10882  11244   -247    438  -1483       O  
ATOM   4898  OD2 ASP C  38     -16.084  34.211  29.819  1.00 82.78           O  
ANISOU 4898  OD2 ASP C  38     9748  10700  11005   -292    465  -1485       O  
ATOM   4899  N   HIS C  39     -11.579  34.152  32.993  1.00 78.99           N  
ANISOU 4899  N   HIS C  39     9409  10293  10308   -477    488  -1262       N  
ATOM   4900  CA  HIS C  39     -11.056  33.581  34.237  1.00 81.90           C  
ANISOU 4900  CA  HIS C  39     9800  10707  10610   -562    510  -1227       C  
ATOM   4901  C   HIS C  39      -9.612  33.924  34.515  1.00 81.57           C  
ANISOU 4901  C   HIS C  39     9798  10657  10538   -570    490  -1158       C  
ATOM   4902  O   HIS C  39      -9.035  33.465  35.506  1.00 82.65           O  
ANISOU 4902  O   HIS C  39     9957  10826  10618   -639    500  -1119       O  
ATOM   4903  CB  HIS C  39     -11.245  32.061  34.217  1.00 84.48           C  
ANISOU 4903  CB  HIS C  39    10137  11045  10915   -593    510  -1181       C  
ATOM   4904  CG  HIS C  39     -10.484  31.358  33.106  1.00 87.86           C  
ANISOU 4904  CG  HIS C  39    10594  11428  11360   -537    467  -1101       C  
ATOM   4905  ND1 HIS C  39     -10.010  30.104  33.233  1.00 89.40           N  
ANISOU 4905  ND1 HIS C  39    10814  11625  11525   -568    455  -1031       N  
ATOM   4906  CD2 HIS C  39     -10.118  31.787  31.827  1.00 87.66           C  
ANISOU 4906  CD2 HIS C  39    10574  11355  11378   -452    433  -1082       C  
ATOM   4907  CE1 HIS C  39      -9.380  29.744  32.097  1.00 88.72           C  
ANISOU 4907  CE1 HIS C  39    10746  11496  11465   -503    417   -977       C  
ATOM   4908  NE2 HIS C  39      -9.444  30.776  31.240  1.00 88.96           N  
ANISOU 4908  NE2 HIS C  39    10765  11499  11536   -434    406  -1008       N  
ATOM   4909  N   LEU C  40      -9.018  34.738  33.645  1.00 78.26           N  
ANISOU 4909  N   LEU C  40     9386  10193  10153   -502    459  -1140       N  
ATOM   4910  CA  LEU C  40      -7.605  35.085  33.738  1.00 75.75           C  
ANISOU 4910  CA  LEU C  40     9104   9863   9814   -501    436  -1071       C  
ATOM   4911  C   LEU C  40      -7.414  36.448  33.082  1.00 76.05           C  
ANISOU 4911  C   LEU C  40     9134   9863   9896   -441    416  -1095       C  
ATOM   4912  O   LEU C  40      -7.707  36.619  31.894  1.00 78.49           O  
ANISOU 4912  O   LEU C  40     9434  10134  10252   -372    393  -1099       O  
ATOM   4913  CB  LEU C  40      -6.758  34.011  33.036  1.00 75.04           C  
ANISOU 4913  CB  LEU C  40     9043   9751   9715   -479    406   -978       C  
ATOM   4914  CG  LEU C  40      -5.375  33.590  33.559  1.00 73.95           C  
ANISOU 4914  CG  LEU C  40     8942   9621   9534   -515    390   -893       C  
ATOM   4915  CD1 LEU C  40      -4.281  34.523  33.059  1.00 71.35           C  
ANISOU 4915  CD1 LEU C  40     8627   9261   9218   -472    364   -857       C  
ATOM   4916  CD2 LEU C  40      -5.338  33.451  35.078  1.00 72.33           C  
ANISOU 4916  CD2 LEU C  40     8744   9463   9273   -606    417   -901       C  
ATOM   4917  N   LYS C  41      -6.934  37.422  33.851  1.00 70.82           N  
ANISOU 4917  N   LYS C  41     8476   9210   9219   -468    422  -1112       N  
ATOM   4918  CA  LYS C  41      -6.932  38.806  33.380  1.00 69.73           C  
ANISOU 4918  CA  LYS C  41     8326   9037   9129   -419    404  -1149       C  
ATOM   4919  C   LYS C  41      -5.586  39.550  33.440  1.00 66.16           C  
ANISOU 4919  C   LYS C  41     7903   8566   8667   -415    379  -1093       C  
ATOM   4920  O   LYS C  41      -5.550  40.784  33.387  1.00 64.44           O  
ANISOU 4920  O   LYS C  41     7676   8326   8481   -394    368  -1129       O  
ATOM   4921  CB  LYS C  41      -8.049  39.604  34.077  1.00 74.64           C  
ANISOU 4921  CB  LYS C  41     8910   9678   9770   -439    434  -1259       C  
ATOM   4922  CG  LYS C  41      -9.444  39.330  33.521  1.00 79.77           C  
ANISOU 4922  CG  LYS C  41     9522  10324  10463   -408    444  -1324       C  
ATOM   4923  CD  LYS C  41     -10.344  40.552  33.636  1.00 83.44           C  
ANISOU 4923  CD  LYS C  41     9947  10777  10979   -387    451  -1426       C  
ATOM   4924  CE  LYS C  41     -11.326  40.654  32.473  1.00 85.30           C  
ANISOU 4924  CE  LYS C  41    10153  10974  11281   -317    431  -1464       C  
ATOM   4925  NZ  LYS C  41     -12.503  39.747  32.595  1.00 85.31           N  
ANISOU 4925  NZ  LYS C  41    10124  11007  11283   -336    462  -1510       N  
ATOM   4926  N   PHE C  42      -4.486  38.807  33.523  1.00 62.94           N  
ANISOU 4926  N   PHE C  42     7528   8166   8220   -435    368  -1006       N  
ATOM   4927  CA  PHE C  42      -3.151  39.411  33.509  1.00 60.80           C  
ANISOU 4927  CA  PHE C  42     7282   7878   7941   -431    342   -947       C  
ATOM   4928  C   PHE C  42      -2.919  40.213  32.220  1.00 58.34           C  
ANISOU 4928  C   PHE C  42     6969   7516   7681   -355    309   -932       C  
ATOM   4929  O   PHE C  42      -3.170  39.709  31.128  1.00 57.13           O  
ANISOU 4929  O   PHE C  42     6813   7343   7551   -306    296   -912       O  
ATOM   4930  CB  PHE C  42      -2.065  38.351  33.703  1.00 60.27           C  
ANISOU 4930  CB  PHE C  42     7244   7824   7829   -459    333   -856       C  
ATOM   4931  CG  PHE C  42      -2.098  37.680  35.051  1.00 63.94           C  
ANISOU 4931  CG  PHE C  42     7717   8337   8239   -541    358   -858       C  
ATOM   4932  CD1 PHE C  42      -2.059  36.291  35.153  1.00 64.40           C  
ANISOU 4932  CD1 PHE C  42     7787   8413   8269   -565    359   -813       C  
ATOM   4933  CD2 PHE C  42      -2.161  38.431  36.223  1.00 65.32           C  
ANISOU 4933  CD2 PHE C  42     7889   8541   8388   -595    377   -904       C  
ATOM   4934  CE1 PHE C  42      -2.082  35.666  36.393  1.00 64.75           C  
ANISOU 4934  CE1 PHE C  42     7842   8500   8260   -646    378   -808       C  
ATOM   4935  CE2 PHE C  42      -2.182  37.813  37.466  1.00 65.69           C  
ANISOU 4935  CE2 PHE C  42     7946   8636   8377   -676    399   -903       C  
ATOM   4936  CZ  PHE C  42      -2.144  36.429  37.550  1.00 66.84           C  
ANISOU 4936  CZ  PHE C  42     8104   8797   8493   -702    399   -852       C  
ATOM   4937  N   PRO C  43      -2.460  41.474  32.351  1.00 56.05           N  
ANISOU 4937  N   PRO C  43     6680   7206   7409   -349    295   -943       N  
ATOM   4938  CA  PRO C  43      -2.412  42.379  31.199  1.00 55.27           C  
ANISOU 4938  CA  PRO C  43     6577   7058   7362   -283    263   -939       C  
ATOM   4939  C   PRO C  43      -1.263  42.153  30.204  1.00 54.32           C  
ANISOU 4939  C   PRO C  43     6481   6917   7239   -248    233   -845       C  
ATOM   4940  O   PRO C  43      -0.138  41.852  30.604  1.00 56.24           O  
ANISOU 4940  O   PRO C  43     6746   7175   7447   -277    230   -783       O  
ATOM   4941  CB  PRO C  43      -2.310  43.765  31.849  1.00 54.19           C  
ANISOU 4941  CB  PRO C  43     6435   6910   7244   -299    258   -984       C  
ATOM   4942  CG  PRO C  43      -1.672  43.517  33.170  1.00 51.88           C  
ANISOU 4942  CG  PRO C  43     6156   6658   6897   -370    278   -972       C  
ATOM   4943  CD  PRO C  43      -2.140  42.166  33.615  1.00 53.03           C  
ANISOU 4943  CD  PRO C  43     6300   6845   7001   -406    308   -972       C  
ATOM   4944  N   ILE C  44      -1.589  42.297  28.915  1.00 53.90           N  
ANISOU 4944  N   ILE C  44     6423   6833   7224   -186    211   -838       N  
ATOM   4945  CA  ILE C  44      -0.644  42.352  27.785  1.00 52.43           C  
ANISOU 4945  CA  ILE C  44     6255   6623   7042   -145    182   -761       C  
ATOM   4946  C   ILE C  44      -1.267  43.284  26.753  1.00 51.92           C  
ANISOU 4946  C   ILE C  44     6178   6517   7029    -90    155   -789       C  
ATOM   4947  O   ILE C  44      -2.465  43.185  26.471  1.00 54.31           O  
ANISOU 4947  O   ILE C  44     6461   6812   7359    -67    158   -847       O  
ATOM   4948  CB  ILE C  44      -0.488  40.989  27.042  1.00 52.18           C  
ANISOU 4948  CB  ILE C  44     6231   6605   6991   -123    184   -713       C  
ATOM   4949  CG1 ILE C  44      -0.874  39.796  27.910  1.00 53.19           C  
ANISOU 4949  CG1 ILE C  44     6355   6767   7085   -166    213   -728       C  
ATOM   4950  CG2 ILE C  44       0.886  40.810  26.405  1.00 48.10           C  
ANISOU 4950  CG2 ILE C  44     5734   6084   6456   -108    166   -626       C  
ATOM   4951  CD1 ILE C  44      -2.341  39.453  27.790  1.00 53.29           C  
ANISOU 4951  CD1 ILE C  44     6345   6782   7119   -155    227   -799       C  
ATOM   4952  N   SER C  45      -0.480  44.187  26.180  1.00 50.15           N  
ANISOU 4952  N   SER C  45     5967   6265   6820    -69    125   -746       N  
ATOM   4953  CA  SER C  45      -0.945  44.895  24.991  1.00 51.55           C  
ANISOU 4953  CA  SER C  45     6139   6402   7042    -15     93   -752       C  
ATOM   4954  C   SER C  45      -0.244  44.321  23.761  1.00 50.80           C  
ANISOU 4954  C   SER C  45     6061   6308   6929     19     78   -674       C  
ATOM   4955  O   SER C  45       0.978  44.359  23.649  1.00 52.54           O  
ANISOU 4955  O   SER C  45     6299   6536   7126      9     72   -607       O  
ATOM   4956  CB  SER C  45      -0.792  46.417  25.116  1.00 52.14           C  
ANISOU 4956  CB  SER C  45     6213   6440   7156    -13     65   -768       C  
ATOM   4957  OG  SER C  45       0.445  46.871  24.611  1.00 55.50           O  
ANISOU 4957  OG  SER C  45     6660   6853   7571    -10     42   -690       O  
ATOM   4958  N   ILE C  46      -1.034  43.759  22.858  1.00 50.82           N  
ANISOU 4958  N   ILE C  46     6057   6306   6943     58     73   -689       N  
ATOM   4959  CA  ILE C  46      -0.499  43.054  21.702  1.00 50.91           C  
ANISOU 4959  CA  ILE C  46     6083   6326   6933     91     64   -626       C  
ATOM   4960  C   ILE C  46      -1.246  43.496  20.441  1.00 50.82           C  
ANISOU 4960  C   ILE C  46     6069   6284   6956    143     32   -639       C  
ATOM   4961  O   ILE C  46      -2.471  43.595  20.443  1.00 53.05           O  
ANISOU 4961  O   ILE C  46     6333   6552   7270    158     29   -704       O  
ATOM   4962  CB  ILE C  46      -0.532  41.514  21.924  1.00 50.64           C  
ANISOU 4962  CB  ILE C  46     6048   6327   6865     80     92   -620       C  
ATOM   4963  CG1 ILE C  46       0.086  40.760  20.739  1.00 54.28           C  
ANISOU 4963  CG1 ILE C  46     6521   6796   7304    115     84   -561       C  
ATOM   4964  CG2 ILE C  46      -1.940  41.022  22.224  1.00 50.79           C  
ANISOU 4964  CG2 ILE C  46     6047   6348   6902     81    107   -694       C  
ATOM   4965  CD1 ILE C  46       0.147  39.250  20.909  1.00 53.82           C  
ANISOU 4965  CD1 ILE C  46     6462   6766   7218    107    106   -552       C  
ATOM   4966  N   SER C  47      -0.500  43.798  19.381  1.00 50.09           N  
ANISOU 4966  N   SER C  47     5992   6183   6854    168      8   -576       N  
ATOM   4967  CA  SER C  47      -1.090  44.222  18.109  1.00 50.49           C  
ANISOU 4967  CA  SER C  47     6045   6208   6930    215    -25   -576       C  
ATOM   4968  C   SER C  47      -0.238  43.765  16.921  1.00 51.70           C  
ANISOU 4968  C   SER C  47     6217   6378   7047    238    -33   -504       C  
ATOM   4969  O   SER C  47       0.813  43.148  17.104  1.00 50.97           O  
ANISOU 4969  O   SER C  47     6132   6316   6917    221    -11   -457       O  
ATOM   4970  CB  SER C  47      -1.266  45.742  18.085  1.00 48.57           C  
ANISOU 4970  CB  SER C  47     5801   5921   6731    218    -61   -588       C  
ATOM   4971  OG  SER C  47      -0.024  46.398  17.929  1.00 47.67           O  
ANISOU 4971  OG  SER C  47     5705   5804   6601    203    -73   -520       O  
ATOM   4972  N   SER C  48      -0.691  44.069  15.708  1.00 53.99           N  
ANISOU 4972  N   SER C  48     6512   6650   7349    277    -65   -496       N  
ATOM   4973  CA  SER C  48       0.073  43.744  14.507  1.00 55.81           C  
ANISOU 4973  CA  SER C  48     6759   6900   7544    299    -73   -431       C  
ATOM   4974  C   SER C  48       0.175  44.934  13.572  1.00 57.63           C  
ANISOU 4974  C   SER C  48     7003   7102   7789    315   -117   -396       C  
ATOM   4975  O   SER C  48      -0.624  45.864  13.658  1.00 61.32           O  
ANISOU 4975  O   SER C  48     7466   7528   8304    322   -147   -432       O  
ATOM   4976  CB  SER C  48      -0.544  42.556  13.771  1.00 57.57           C  
ANISOU 4976  CB  SER C  48     6979   7142   7750    330    -65   -449       C  
ATOM   4977  OG  SER C  48      -1.743  42.930  13.113  1.00 64.77           O  
ANISOU 4977  OG  SER C  48     7887   8026   8696    362    -97   -489       O  
ATOM   4978  N   GLU C  49       1.172  44.889  12.691  1.00 59.84           N  
ANISOU 4978  N   GLU C  49     7300   7404   8031    319   -120   -327       N  
ATOM   4979  CA  GLU C  49       1.370  45.892  11.651  1.00 61.35           C  
ANISOU 4979  CA  GLU C  49     7508   7576   8226    331   -161   -281       C  
ATOM   4980  C   GLU C  49       1.817  45.191  10.366  1.00 63.26           C  
ANISOU 4980  C   GLU C  49     7761   7855   8417    353   -158   -236       C  
ATOM   4981  O   GLU C  49       2.927  44.657  10.306  1.00 64.00           O  
ANISOU 4981  O   GLU C  49     7857   7989   8469    341   -129   -192       O  
ATOM   4982  CB  GLU C  49       2.397  46.932  12.102  1.00 64.18           C  
ANISOU 4982  CB  GLU C  49     7873   7922   8588    296   -169   -235       C  
ATOM   4983  CG  GLU C  49       2.863  47.890  11.016  1.00 66.68           C  
ANISOU 4983  CG  GLU C  49     8209   8226   8899    300   -208   -171       C  
ATOM   4984  CD  GLU C  49       3.791  48.960  11.552  1.00 68.60           C  
ANISOU 4984  CD  GLU C  49     8458   8452   9155    263   -219   -129       C  
ATOM   4985  OE1 GLU C  49       3.325  49.809  12.338  1.00 71.88           O  
ANISOU 4985  OE1 GLU C  49     8867   8822   9620    252   -239   -166       O  
ATOM   4986  OE2 GLU C  49       4.983  48.958  11.184  1.00 71.58           O  
ANISOU 4986  OE2 GLU C  49     8843   8860   9493    245   -207    -62       O  
ATOM   4987  N   PRO C  50       0.944  45.165   9.339  1.00 64.62           N  
ANISOU 4987  N   PRO C  50     7941   8018   8594    387   -187   -249       N  
ATOM   4988  CA  PRO C  50      -0.403  45.732   9.342  1.00 63.37           C  
ANISOU 4988  CA  PRO C  50     7776   7812   8488    406   -224   -304       C  
ATOM   4989  C   PRO C  50      -1.403  44.777   9.987  1.00 61.89           C  
ANISOU 4989  C   PRO C  50     7568   7627   8321    418   -200   -379       C  
ATOM   4990  O   PRO C  50      -1.008  43.826  10.659  1.00 62.67           O  
ANISOU 4990  O   PRO C  50     7657   7756   8396    403   -156   -388       O  
ATOM   4991  CB  PRO C  50      -0.706  45.868   7.853  1.00 63.93           C  
ANISOU 4991  CB  PRO C  50     7864   7883   8541    436   -262   -274       C  
ATOM   4992  CG  PRO C  50      -0.010  44.699   7.246  1.00 63.78           C  
ANISOU 4992  CG  PRO C  50     7851   7922   8460    443   -227   -246       C  
ATOM   4993  CD  PRO C  50       1.239  44.483   8.063  1.00 62.81           C  
ANISOU 4993  CD  PRO C  50     7723   7827   8315    410   -185   -215       C  
ATOM   4994  N   CYS C  51      -2.688  45.031   9.780  1.00 63.43           N  
ANISOU 4994  N   CYS C  51     7753   7789   8558    442   -230   -432       N  
ATOM   4995  CA  CYS C  51      -3.725  44.115  10.223  1.00 64.85           C  
ANISOU 4995  CA  CYS C  51     7911   7972   8755    454   -211   -502       C  
ATOM   4996  C   CYS C  51      -3.592  42.797   9.466  1.00 64.04           C  
ANISOU 4996  C   CYS C  51     7815   7911   8605    474   -191   -490       C  
ATOM   4997  O   CYS C  51      -3.088  42.781   8.337  1.00 66.19           O  
ANISOU 4997  O   CYS C  51     8107   8200   8841    489   -206   -439       O  
ATOM   4998  CB  CYS C  51      -5.100  44.721   9.980  1.00 68.97           C  
ANISOU 4998  CB  CYS C  51     8420   8450   9335    480   -253   -557       C  
ATOM   4999  SG  CYS C  51      -6.397  43.912  10.932  1.00 73.43           S  
ANISOU 4999  SG  CYS C  51     8949   9013   9936    481   -225   -655       S  
ATOM   5000  N   ILE C  52      -4.026  41.698  10.084  1.00 61.97           N  
ANISOU 5000  N   ILE C  52     7536   7666   8343    471   -157   -535       N  
ATOM   5001  CA  ILE C  52      -3.858  40.376   9.473  1.00 62.27           C  
ANISOU 5001  CA  ILE C  52     7579   7741   8340    488   -137   -527       C  
ATOM   5002  C   ILE C  52      -4.855  40.133   8.349  1.00 60.18           C  
ANISOU 5002  C   ILE C  52     7315   7467   8082    527   -170   -551       C  
ATOM   5003  O   ILE C  52      -6.071  40.130   8.566  1.00 60.97           O  
ANISOU 5003  O   ILE C  52     7398   7543   8224    538   -183   -611       O  
ATOM   5004  CB  ILE C  52      -3.880  39.210  10.501  1.00 63.34           C  
ANISOU 5004  CB  ILE C  52     7698   7896   8470    467    -93   -559       C  
ATOM   5005  CG1 ILE C  52      -2.526  39.070  11.200  1.00 62.61           C  
ANISOU 5005  CG1 ILE C  52     7612   7828   8349    435    -62   -512       C  
ATOM   5006  CG2 ILE C  52      -4.200  37.879   9.834  1.00 62.20           C  
ANISOU 5006  CG2 ILE C  52     7553   7774   8304    493    -85   -573       C  
ATOM   5007  CD1 ILE C  52      -2.506  39.653  12.592  1.00 64.69           C  
ANISOU 5007  CD1 ILE C  52     7864   8076   8636    396    -47   -532       C  
ATOM   5008  N   ARG C  53      -4.313  39.954   7.148  1.00 56.76           N  
ANISOU 5008  N   ARG C  53     6902   7056   7606    547   -182   -505       N  
ATOM   5009  CA  ARG C  53      -5.073  39.484   6.010  1.00 57.33           C  
ANISOU 5009  CA  ARG C  53     6980   7132   7670    583   -208   -522       C  
ATOM   5010  C   ARG C  53      -4.885  37.978   5.961  1.00 54.21           C  
ANISOU 5010  C   ARG C  53     6579   6772   7244    590   -173   -536       C  
ATOM   5011  O   ARG C  53      -3.758  37.500   5.836  1.00 55.61           O  
ANISOU 5011  O   ARG C  53     6765   6983   7378    583   -147   -496       O  
ATOM   5012  CB  ARG C  53      -4.556  40.135   4.720  1.00 62.76           C  
ANISOU 5012  CB  ARG C  53     7694   7829   8323    596   -241   -464       C  
ATOM   5013  CG  ARG C  53      -5.470  39.941   3.523  1.00 67.81           C  
ANISOU 5013  CG  ARG C  53     8341   8464   8958    631   -281   -481       C  
ATOM   5014  CD  ARG C  53      -4.954  40.610   2.259  1.00 74.74           C  
ANISOU 5014  CD  ARG C  53     9248   9355   9794    638   -314   -419       C  
ATOM   5015  NE  ARG C  53      -4.026  39.765   1.510  1.00 78.86           N  
ANISOU 5015  NE  ARG C  53     9783   9932  10248    643   -286   -385       N  
ATOM   5016  CZ  ARG C  53      -2.806  40.137   1.133  1.00 84.90           C  
ANISOU 5016  CZ  ARG C  53    10563  10728  10966    625   -274   -321       C  
ATOM   5017  NH1 ARG C  53      -2.354  41.354   1.420  1.00 88.02           N  
ANISOU 5017  NH1 ARG C  53    10966  11102  11375    600   -291   -279       N  
ATOM   5018  NH2 ARG C  53      -2.038  39.290   0.460  1.00 84.91           N  
ANISOU 5018  NH2 ARG C  53    10570  10782  10907    632   -246   -301       N  
ATOM   5019  N   LEU C  54      -5.978  37.226   6.068  1.00 52.23           N  
ANISOU 5019  N   LEU C  54     6313   6512   7018    605   -175   -595       N  
ATOM   5020  CA  LEU C  54      -5.898  35.763   6.030  1.00 49.52           C  
ANISOU 5020  CA  LEU C  54     5964   6196   6653    612   -147   -612       C  
ATOM   5021  C   LEU C  54      -5.388  35.231   4.690  1.00 50.79           C  
ANISOU 5021  C   LEU C  54     6145   6389   6764    640   -155   -583       C  
ATOM   5022  O   LEU C  54      -4.897  34.112   4.619  1.00 53.15           O  
ANISOU 5022  O   LEU C  54     6441   6714   7036    645   -129   -582       O  
ATOM   5023  CB  LEU C  54      -7.236  35.113   6.405  1.00 47.92           C  
ANISOU 5023  CB  LEU C  54     5741   5975   6491    619   -149   -681       C  
ATOM   5024  CG  LEU C  54      -7.778  35.317   7.835  1.00 48.15           C  
ANISOU 5024  CG  LEU C  54     5745   5983   6564    587   -130   -721       C  
ATOM   5025  CD1 LEU C  54      -8.856  34.299   8.173  1.00 45.25           C  
ANISOU 5025  CD1 LEU C  54     5357   5612   6223    589   -121   -782       C  
ATOM   5026  CD2 LEU C  54      -6.684  35.277   8.893  1.00 47.39           C  
ANISOU 5026  CD2 LEU C  54     5651   5902   6451    549    -92   -690       C  
ATOM   5027  N   ARG C  55      -5.491  36.044   3.641  1.00 52.94           N  
ANISOU 5027  N   ARG C  55     6434   6658   7022    658   -192   -558       N  
ATOM   5028  CA  ARG C  55      -4.934  35.715   2.333  1.00 56.15           C  
ANISOU 5028  CA  ARG C  55     6860   7100   7372    679   -199   -525       C  
ATOM   5029  C   ARG C  55      -3.431  35.522   2.439  1.00 55.15           C  
ANISOU 5029  C   ARG C  55     6740   7012   7203    662   -162   -475       C  
ATOM   5030  O   ARG C  55      -2.870  34.670   1.758  1.00 56.67           O  
ANISOU 5030  O   ARG C  55     6936   7242   7352    677   -146   -467       O  
ATOM   5031  CB  ARG C  55      -5.205  36.846   1.333  1.00 63.28           C  
ANISOU 5031  CB  ARG C  55     7783   7992   8267    690   -248   -496       C  
ATOM   5032  CG  ARG C  55      -5.008  36.489  -0.142  1.00 66.27           C  
ANISOU 5032  CG  ARG C  55     8183   8408   8589    714   -264   -476       C  
ATOM   5033  CD  ARG C  55      -6.322  36.574  -0.914  1.00 71.78           C  
ANISOU 5033  CD  ARG C  55     8885   9082   9305    742   -314   -511       C  
ATOM   5034  NE  ARG C  55      -7.474  36.169  -0.100  1.00 74.09           N  
ANISOU 5034  NE  ARG C  55     9152   9338   9660    748   -316   -577       N  
ATOM   5035  CZ  ARG C  55      -8.313  35.178  -0.397  1.00 75.87           C  
ANISOU 5035  CZ  ARG C  55     9367   9564   9894    771   -321   -628       C  
ATOM   5036  NH1 ARG C  55      -8.162  34.474  -1.519  1.00 74.28           N  
ANISOU 5036  NH1 ARG C  55     9181   9397   9643    793   -327   -625       N  
ATOM   5037  NH2 ARG C  55      -9.318  34.904   0.428  1.00 75.25           N  
ANISOU 5037  NH2 ARG C  55     9263   9454   9873    770   -320   -685       N  
ATOM   5038  N   GLY C  56      -2.795  36.328   3.288  1.00 52.94           N  
ANISOU 5038  N   GLY C  56     6457   6720   6935    631   -150   -444       N  
ATOM   5039  CA  GLY C  56      -1.342  36.346   3.451  1.00 50.73           C  
ANISOU 5039  CA  GLY C  56     6181   6473   6620    611   -119   -392       C  
ATOM   5040  C   GLY C  56      -0.895  37.697   3.977  1.00 51.54           C  
ANISOU 5040  C   GLY C  56     6288   6555   6737    582   -128   -353       C  
ATOM   5041  O   GLY C  56      -1.485  38.720   3.644  1.00 52.35           O  
ANISOU 5041  O   GLY C  56     6401   6630   6859    584   -167   -348       O  
ATOM   5042  N   THR C  57       0.144  37.707   4.810  1.00 54.44           N  
ANISOU 5042  N   THR C  57     6649   6935   7100    554    -97   -325       N  
ATOM   5043  CA  THR C  57       0.648  38.942   5.427  1.00 53.23           C  
ANISOU 5043  CA  THR C  57     6498   6761   6963    522   -104   -289       C  
ATOM   5044  C   THR C  57       2.132  38.825   5.770  1.00 52.44           C  
ANISOU 5044  C   THR C  57     6395   6694   6834    498    -70   -241       C  
ATOM   5045  O   THR C  57       2.600  37.746   6.126  1.00 51.03           O  
ANISOU 5045  O   THR C  57     6205   6540   6644    499    -38   -251       O  
ATOM   5046  CB  THR C  57      -0.110  39.267   6.733  1.00 52.63           C  
ANISOU 5046  CB  THR C  57     6409   6644   6943    505   -105   -333       C  
ATOM   5047  OG1 THR C  57      -1.471  38.829   6.631  1.00 53.09           O  
ANISOU 5047  OG1 THR C  57     6460   6682   7030    528   -120   -394       O  
ATOM   5048  CG2 THR C  57      -0.083  40.759   7.020  1.00 52.79           C  
ANISOU 5048  CG2 THR C  57     6435   6630   6990    485   -132   -311       C  
ATOM   5049  N   ASN C  58       2.864  39.932   5.651  1.00 52.07           N  
ANISOU 5049  N   ASN C  58     6358   6647   6778    476    -81   -188       N  
ATOM   5050  CA  ASN C  58       4.209  40.044   6.225  1.00 53.57           C  
ANISOU 5050  CA  ASN C  58     6542   6859   6954    447    -53   -144       C  
ATOM   5051  C   ASN C  58       4.244  41.251   7.141  1.00 51.52           C  
ANISOU 5051  C   ASN C  58     6283   6560   6730    415    -68   -132       C  
ATOM   5052  O   ASN C  58       3.867  42.345   6.725  1.00 52.19           O  
ANISOU 5052  O   ASN C  58     6381   6618   6829    413   -104   -116       O  
ATOM   5053  CB  ASN C  58       5.298  40.214   5.155  1.00 58.47           C  
ANISOU 5053  CB  ASN C  58     7169   7524   7521    446    -46    -84       C  
ATOM   5054  CG  ASN C  58       4.926  39.593   3.818  1.00 65.20           C  
ANISOU 5054  CG  ASN C  58     8030   8405   8336    480    -52    -94       C  
ATOM   5055  OD1 ASN C  58       4.609  38.402   3.725  1.00 67.47           O  
ANISOU 5055  OD1 ASN C  58     8308   8708   8618    505    -36   -135       O  
ATOM   5056  ND2 ASN C  58       4.974  40.406   2.766  1.00 68.07           N  
ANISOU 5056  ND2 ASN C  58     8412   8778   8672    480    -79    -55       N  
ATOM   5057  N   GLY C  59       4.698  41.063   8.378  1.00 49.43           N  
ANISOU 5057  N   GLY C  59     6005   6291   6482    389    -44   -138       N  
ATOM   5058  CA  GLY C  59       4.796  42.173   9.319  1.00 48.44           C  
ANISOU 5058  CA  GLY C  59     5880   6131   6390    357    -56   -131       C  
ATOM   5059  C   GLY C  59       5.339  41.841  10.694  1.00 50.00           C  
ANISOU 5059  C   GLY C  59     6065   6331   6599    326    -27   -139       C  
ATOM   5060  O   GLY C  59       6.191  40.962  10.841  1.00 52.66           O  
ANISOU 5060  O   GLY C  59     6393   6703   6911    321      1   -121       O  
ATOM   5061  N   PHE C  60       4.853  42.565  11.703  1.00 48.67           N  
ANISOU 5061  N   PHE C  60     5895   6127   6469    304    -38   -167       N  
ATOM   5062  CA  PHE C  60       5.344  42.418  13.072  1.00 46.60           C  
ANISOU 5062  CA  PHE C  60     5623   5866   6216    269    -15   -174       C  
ATOM   5063  C   PHE C  60       4.206  42.310  14.077  1.00 45.61           C  
ANISOU 5063  C   PHE C  60     5488   5714   6124    261    -13   -242       C  
ATOM   5064  O   PHE C  60       3.233  43.057  14.005  1.00 45.82           O  
ANISOU 5064  O   PHE C  60     5517   5708   6184    270    -37   -278       O  
ATOM   5065  CB  PHE C  60       6.250  43.593  13.461  1.00 45.49           C  
ANISOU 5065  CB  PHE C  60     5487   5714   6082    236    -26   -130       C  
ATOM   5066  CG  PHE C  60       7.466  43.735  12.597  1.00 46.20           C  
ANISOU 5066  CG  PHE C  60     5581   5833   6137    235    -24    -60       C  
ATOM   5067  CD1 PHE C  60       7.419  44.487  11.418  1.00 46.37           C  
ANISOU 5067  CD1 PHE C  60     5616   5850   6151    249    -51    -27       C  
ATOM   5068  CD2 PHE C  60       8.662  43.124  12.954  1.00 46.08           C  
ANISOU 5068  CD2 PHE C  60     5556   5853   6097    217      3    -26       C  
ATOM   5069  CE1 PHE C  60       8.538  44.617  10.610  1.00 44.81           C  
ANISOU 5069  CE1 PHE C  60     5421   5686   5917    244    -46     36       C  
ATOM   5070  CE2 PHE C  60       9.786  43.248  12.147  1.00 46.28           C  
ANISOU 5070  CE2 PHE C  60     5580   5910   6091    216      9     34       C  
ATOM   5071  CZ  PHE C  60       9.724  43.999  10.976  1.00 45.73           C  
ANISOU 5071  CZ  PHE C  60     5524   5839   6010    227    -13     65       C  
ATOM   5072  N   VAL C  61       4.332  41.361  14.997  1.00 43.59           N  
ANISOU 5072  N   VAL C  61     5223   5475   5861    243     15   -261       N  
ATOM   5073  CA  VAL C  61       3.514  41.350  16.194  1.00 42.96           C  
ANISOU 5073  CA  VAL C  61     5135   5379   5806    220     23   -318       C  
ATOM   5074  C   VAL C  61       4.250  42.194  17.225  1.00 42.19           C  
ANISOU 5074  C   VAL C  61     5039   5275   5715    178     25   -300       C  
ATOM   5075  O   VAL C  61       5.403  41.913  17.556  1.00 39.67           O  
ANISOU 5075  O   VAL C  61     4721   4977   5372    157     38   -255       O  
ATOM   5076  CB  VAL C  61       3.285  39.926  16.741  1.00 43.51           C  
ANISOU 5076  CB  VAL C  61     5196   5471   5863    215     50   -342       C  
ATOM   5077  CG1 VAL C  61       2.680  39.978  18.134  1.00 42.87           C  
ANISOU 5077  CG1 VAL C  61     5107   5381   5798    178     63   -391       C  
ATOM   5078  CG2 VAL C  61       2.380  39.131  15.813  1.00 44.74           C  
ANISOU 5078  CG2 VAL C  61     5350   5628   6019    255     46   -371       C  
ATOM   5079  N   HIS C  62       3.581  43.242  17.699  1.00 42.29           N  
ANISOU 5079  N   HIS C  62     5049   5255   5762    168      8   -338       N  
ATOM   5080  CA  HIS C  62       4.115  44.120  18.731  1.00 40.71           C  
ANISOU 5080  CA  HIS C  62     4850   5044   5573    128      7   -333       C  
ATOM   5081  C   HIS C  62       3.604  43.620  20.040  1.00 39.20           C  
ANISOU 5081  C   HIS C  62     4650   4862   5383     97     32   -386       C  
ATOM   5082  O   HIS C  62       2.403  43.487  20.224  1.00 40.01           O  
ANISOU 5082  O   HIS C  62     4741   4953   5506    106     34   -449       O  
ATOM   5083  CB  HIS C  62       3.669  45.564  18.500  1.00 41.50           C  
ANISOU 5083  CB  HIS C  62     4952   5100   5712    135    -26   -349       C  
ATOM   5084  CG  HIS C  62       4.042  46.114  17.139  1.00 43.55           C  
ANISOU 5084  CG  HIS C  62     5225   5351   5971    162    -56   -295       C  
ATOM   5085  ND1 HIS C  62       5.303  46.482  16.822  1.00 45.04           N  
ANISOU 5085  ND1 HIS C  62     5423   5550   6138    148    -60   -225       N  
ATOM   5086  CD2 HIS C  62       3.267  46.354  16.002  1.00 44.63           C  
ANISOU 5086  CD2 HIS C  62     5365   5468   6122    201    -83   -303       C  
ATOM   5087  CE1 HIS C  62       5.337  46.933  15.551  1.00 45.12           C  
ANISOU 5087  CE1 HIS C  62     5444   5552   6147    174    -87   -189       C  
ATOM   5088  NE2 HIS C  62       4.091  46.852  15.049  1.00 46.72           N  
ANISOU 5088  NE2 HIS C  62     5644   5735   6370    207   -103   -235       N  
ATOM   5089  N   VAL C  63       4.506  43.311  20.958  1.00 38.60           N  
ANISOU 5089  N   VAL C  63     4575   4807   5284     58     49   -361       N  
ATOM   5090  CA  VAL C  63       4.108  42.821  22.268  1.00 39.69           C  
ANISOU 5090  CA  VAL C  63     4706   4958   5415     21     73   -404       C  
ATOM   5091  C   VAL C  63       4.698  43.713  23.339  1.00 40.94           C  
ANISOU 5091  C   VAL C  63     4867   5110   5575    -22     71   -403       C  
ATOM   5092  O   VAL C  63       5.876  44.079  23.275  1.00 41.28           O  
ANISOU 5092  O   VAL C  63     4918   5156   5607    -34     62   -345       O  
ATOM   5093  CB  VAL C  63       4.546  41.359  22.502  1.00 39.65           C  
ANISOU 5093  CB  VAL C  63     4702   4986   5376     11     95   -379       C  
ATOM   5094  CG1 VAL C  63       4.211  40.909  23.919  1.00 39.92           C  
ANISOU 5094  CG1 VAL C  63     4732   5035   5398    -36    116   -416       C  
ATOM   5095  CG2 VAL C  63       3.877  40.435  21.499  1.00 40.03           C  
ANISOU 5095  CG2 VAL C  63     4746   5038   5423     53     97   -390       C  
ATOM   5096  N   GLU C  64       3.867  44.058  24.319  1.00 43.21           N  
ANISOU 5096  N   GLU C  64     5147   5392   5878    -47     80   -468       N  
ATOM   5097  CA  GLU C  64       4.262  44.929  25.416  1.00 44.50           C  
ANISOU 5097  CA  GLU C  64     5311   5550   6043    -91     78   -481       C  
ATOM   5098  C   GLU C  64       3.551  44.485  26.685  1.00 42.74           C  
ANISOU 5098  C   GLU C  64     5080   5349   5808   -130    106   -543       C  
ATOM   5099  O   GLU C  64       2.346  44.686  26.815  1.00 40.12           O  
ANISOU 5099  O   GLU C  64     4735   5008   5500   -122    112   -614       O  
ATOM   5100  CB  GLU C  64       3.925  46.386  25.082  1.00 49.07           C  
ANISOU 5100  CB  GLU C  64     5888   6087   6668    -73     49   -506       C  
ATOM   5101  CG  GLU C  64       4.560  47.422  26.004  1.00 55.99           C  
ANISOU 5101  CG  GLU C  64     6768   6952   7551   -113     40   -508       C  
ATOM   5102  CD  GLU C  64       4.715  48.798  25.359  1.00 61.64           C  
ANISOU 5102  CD  GLU C  64     7488   7622   8309    -92      2   -496       C  
ATOM   5103  OE1 GLU C  64       4.157  49.037  24.260  1.00 61.63           O  
ANISOU 5103  OE1 GLU C  64     7484   7595   8334    -48    -18   -496       O  
ATOM   5104  OE2 GLU C  64       5.411  49.649  25.957  1.00 65.69           O  
ANISOU 5104  OE2 GLU C  64     8006   8123   8829   -122    -10   -485       O  
ATOM   5105  N   PHE C  65       4.299  43.866  27.600  1.00 41.98           N  
ANISOU 5105  N   PHE C  65     4992   5283   5673   -175    122   -515       N  
ATOM   5106  CA  PHE C  65       3.769  43.449  28.898  1.00 43.13           C  
ANISOU 5106  CA  PHE C  65     5134   5456   5797   -224    147   -564       C  
ATOM   5107  C   PHE C  65       4.856  43.112  29.907  1.00 43.63           C  
ANISOU 5107  C   PHE C  65     5211   5546   5821   -277    153   -521       C  
ATOM   5108  O   PHE C  65       6.039  43.246  29.619  1.00 43.99           O  
ANISOU 5108  O   PHE C  65     5266   5588   5860   -275    136   -455       O  
ATOM   5109  CB  PHE C  65       2.793  42.266  28.746  1.00 45.60           C  
ANISOU 5109  CB  PHE C  65     5438   5786   6102   -214    168   -593       C  
ATOM   5110  CG  PHE C  65       3.459  40.917  28.604  1.00 44.53           C  
ANISOU 5110  CG  PHE C  65     5312   5672   5932   -219    173   -532       C  
ATOM   5111  CD1 PHE C  65       3.145  39.891  29.482  1.00 43.10           C  
ANISOU 5111  CD1 PHE C  65     5131   5521   5721   -260    194   -545       C  
ATOM   5112  CD2 PHE C  65       4.385  40.670  27.586  1.00 44.38           C  
ANISOU 5112  CD2 PHE C  65     5301   5646   5915   -183    156   -464       C  
ATOM   5113  CE1 PHE C  65       3.743  38.648  29.359  1.00 44.06           C  
ANISOU 5113  CE1 PHE C  65     5262   5657   5820   -264    193   -490       C  
ATOM   5114  CE2 PHE C  65       4.993  39.434  27.463  1.00 44.05           C  
ANISOU 5114  CE2 PHE C  65     5264   5622   5849   -184    159   -415       C  
ATOM   5115  CZ  PHE C  65       4.669  38.420  28.353  1.00 45.69           C  
ANISOU 5115  CZ  PHE C  65     5473   5852   6032   -224    175   -428       C  
ATOM   5116  N   ILE C  66       4.426  42.659  31.084  1.00 45.85           N  
ANISOU 5116  N   ILE C  66     5491   5856   6074   -327    175   -558       N  
ATOM   5117  CA  ILE C  66       5.305  42.302  32.196  1.00 46.45           C  
ANISOU 5117  CA  ILE C  66     5581   5960   6108   -386    179   -524       C  
ATOM   5118  C   ILE C  66       4.916  40.890  32.650  1.00 47.08           C  
ANISOU 5118  C   ILE C  66     5662   6071   6154   -412    199   -522       C  
ATOM   5119  O   ILE C  66       3.916  40.709  33.340  1.00 49.05           O  
ANISOU 5119  O   ILE C  66     5903   6339   6391   -441    222   -583       O  
ATOM   5120  CB  ILE C  66       5.173  43.315  33.366  1.00 45.85           C  
ANISOU 5120  CB  ILE C  66     5504   5890   6026   -433    185   -577       C  
ATOM   5121  CG1 ILE C  66       5.603  44.715  32.922  1.00 45.76           C  
ANISOU 5121  CG1 ILE C  66     5491   5842   6052   -408    160   -576       C  
ATOM   5122  CG2 ILE C  66       5.969  42.869  34.585  1.00 45.14           C  
ANISOU 5122  CG2 ILE C  66     5429   5834   5886   -499    189   -545       C  
ATOM   5123  CD1 ILE C  66       4.855  45.837  33.610  1.00 46.48           C  
ANISOU 5123  CD1 ILE C  66     5572   5924   6164   -426    165   -660       C  
ATOM   5124  N   PRO C  67       5.697  39.879  32.242  1.00 48.32           N  
ANISOU 5124  N   PRO C  67     5828   6232   6298   -402    189   -453       N  
ATOM   5125  CA  PRO C  67       5.361  38.483  32.502  1.00 47.85           C  
ANISOU 5125  CA  PRO C  67     5771   6194   6215   -420    200   -443       C  
ATOM   5126  C   PRO C  67       5.195  38.121  33.972  1.00 47.78           C  
ANISOU 5126  C   PRO C  67     5771   6219   6164   -495    214   -460       C  
ATOM   5127  O   PRO C  67       5.978  38.555  34.816  1.00 46.30           O  
ANISOU 5127  O   PRO C  67     5594   6043   5954   -538    207   -440       O  
ATOM   5128  CB  PRO C  67       6.541  37.714  31.892  1.00 47.54           C  
ANISOU 5128  CB  PRO C  67     5739   6150   6174   -398    179   -361       C  
ATOM   5129  CG  PRO C  67       7.614  38.728  31.665  1.00 48.07           C  
ANISOU 5129  CG  PRO C  67     5809   6203   6252   -387    161   -326       C  
ATOM   5130  CD  PRO C  67       6.872  39.990  31.363  1.00 49.15           C  
ANISOU 5130  CD  PRO C  67     5937   6320   6415   -366    165   -383       C  
ATOM   5131  N   ARG C  68       4.171  37.312  34.240  1.00 48.46           N  
ANISOU 5131  N   ARG C  68     5851   6322   6237   -513    234   -496       N  
ATOM   5132  CA  ARG C  68       3.875  36.791  35.570  1.00 48.65           C  
ANISOU 5132  CA  ARG C  68     5883   6383   6216   -588    250   -510       C  
ATOM   5133  C   ARG C  68       4.771  35.604  35.940  1.00 46.96           C  
ANISOU 5133  C   ARG C  68     5689   6180   5974   -619    232   -434       C  
ATOM   5134  O   ARG C  68       4.649  35.042  37.032  1.00 48.35           O  
ANISOU 5134  O   ARG C  68     5875   6385   6108   -685    239   -431       O  
ATOM   5135  CB  ARG C  68       2.390  36.400  35.678  1.00 52.04           C  
ANISOU 5135  CB  ARG C  68     6297   6828   6647   -596    280   -579       C  
ATOM   5136  CG  ARG C  68       1.399  37.547  35.489  1.00 54.43           C  
ANISOU 5136  CG  ARG C  68     6578   7123   6980   -573    298   -664       C  
ATOM   5137  CD  ARG C  68       1.517  38.587  36.590  1.00 59.28           C  
ANISOU 5137  CD  ARG C  68     7193   7757   7573   -622    309   -705       C  
ATOM   5138  NE  ARG C  68       1.236  39.933  36.090  1.00 66.87           N  
ANISOU 5138  NE  ARG C  68     8139   8689   8579   -578    305   -755       N  
ATOM   5139  CZ  ARG C  68       0.419  40.816  36.670  1.00 69.58           C  
ANISOU 5139  CZ  ARG C  68     8464   9042   8930   -595    326   -841       C  
ATOM   5140  NH1 ARG C  68      -0.214  40.523  37.805  1.00 69.23           N  
ANISOU 5140  NH1 ARG C  68     8415   9043   8846   -659    357   -889       N  
ATOM   5141  NH2 ARG C  68       0.249  42.011  36.115  1.00 67.90           N  
ANISOU 5141  NH2 ARG C  68     8237   8793   8765   -550    313   -879       N  
ATOM   5142  N   GLY C  69       5.665  35.234  35.024  1.00 43.62           N  
ANISOU 5142  N   GLY C  69     5267   5731   5573   -571    207   -372       N  
ATOM   5143  CA  GLY C  69       6.671  34.197  35.265  1.00 41.80           C  
ANISOU 5143  CA  GLY C  69     5051   5503   5327   -590    182   -297       C  
ATOM   5144  C   GLY C  69       7.791  34.278  34.244  1.00 40.98           C  
ANISOU 5144  C   GLY C  69     4943   5373   5253   -533    158   -242       C  
ATOM   5145  O   GLY C  69       7.692  35.025  33.270  1.00 40.91           O  
ANISOU 5145  O   GLY C  69     4923   5346   5274   -479    161   -260       O  
ATOM   5146  N   ASN C  70       8.860  33.516  34.459  1.00 40.51           N  
ANISOU 5146  N   ASN C  70     4892   5313   5186   -546    132   -176       N  
ATOM   5147  CA  ASN C  70       9.952  33.440  33.487  1.00 39.39           C  
ANISOU 5147  CA  ASN C  70     4741   5151   5072   -493    112   -124       C  
ATOM   5148  C   ASN C  70       9.490  32.940  32.137  1.00 39.26           C  
ANISOU 5148  C   ASN C  70     4711   5117   5086   -425    117   -135       C  
ATOM   5149  O   ASN C  70       8.653  32.042  32.056  1.00 40.59           O  
ANISOU 5149  O   ASN C  70     4881   5285   5256   -423    123   -155       O  
ATOM   5150  CB  ASN C  70      11.041  32.522  33.995  1.00 39.38           C  
ANISOU 5150  CB  ASN C  70     4748   5152   5062   -520     82    -57       C  
ATOM   5151  CG  ASN C  70      11.625  33.000  35.289  1.00 40.33           C  
ANISOU 5151  CG  ASN C  70     4883   5291   5150   -588     72    -39       C  
ATOM   5152  OD1 ASN C  70      11.741  34.206  35.529  1.00 40.36           O  
ANISOU 5152  OD1 ASN C  70     4887   5300   5148   -598     80    -61       O  
ATOM   5153  ND2 ASN C  70      11.996  32.060  36.142  1.00 42.35           N  
ANISOU 5153  ND2 ASN C  70     5151   5555   5384   -636     50      0       N  
ATOM   5154  N   LEU C  71      10.046  33.515  31.078  1.00 37.19           N  
ANISOU 5154  N   LEU C  71     4438   4841   4849   -370    113   -120       N  
ATOM   5155  CA  LEU C  71       9.618  33.180  29.732  1.00 35.74           C  
ANISOU 5155  CA  LEU C  71     4243   4644   4691   -304    118   -133       C  
ATOM   5156  C   LEU C  71      10.481  32.113  29.059  1.00 36.15           C  
ANISOU 5156  C   LEU C  71     4288   4690   4758   -270    100    -84       C  
ATOM   5157  O   LEU C  71      10.418  31.937  27.838  1.00 36.83           O  
ANISOU 5157  O   LEU C  71     4362   4766   4862   -212    103    -88       O  
ATOM   5158  CB  LEU C  71       9.552  34.442  28.882  1.00 35.45           C  
ANISOU 5158  CB  LEU C  71     4199   4598   4671   -265    125   -152       C  
ATOM   5159  CG  LEU C  71       8.164  35.044  28.632  1.00 35.90           C  
ANISOU 5159  CG  LEU C  71     4254   4649   4737   -252    143   -219       C  
ATOM   5160  CD1 LEU C  71       7.170  34.764  29.753  1.00 35.73           C  
ANISOU 5160  CD1 LEU C  71     4237   4639   4697   -304    158   -264       C  
ATOM   5161  CD2 LEU C  71       8.279  36.536  28.353  1.00 36.02           C  
ANISOU 5161  CD2 LEU C  71     4267   4653   4764   -240    142   -232       C  
ATOM   5162  N   LYS C  72      11.261  31.391  29.861  1.00 34.84           N  
ANISOU 5162  N   LYS C  72     4126   4528   4582   -307     81    -41       N  
ATOM   5163  CA  LYS C  72      12.261  30.465  29.349  1.00 35.23           C  
ANISOU 5163  CA  LYS C  72     4165   4570   4650   -277     60      6       C  
ATOM   5164  C   LYS C  72      11.652  29.299  28.558  1.00 36.23           C  
ANISOU 5164  C   LYS C  72     4286   4684   4795   -236     60     -9       C  
ATOM   5165  O   LYS C  72      12.248  28.813  27.607  1.00 38.20           O  
ANISOU 5165  O   LYS C  72     4521   4927   5066   -186     52      8       O  
ATOM   5166  CB  LYS C  72      13.109  29.952  30.508  1.00 35.04           C  
ANISOU 5166  CB  LYS C  72     4149   4549   4613   -331     34     52       C  
ATOM   5167  CG  LYS C  72      14.452  29.346  30.138  1.00 34.37           C  
ANISOU 5167  CG  LYS C  72     4048   4457   4552   -305      9    106       C  
ATOM   5168  CD  LYS C  72      15.255  29.093  31.407  1.00 34.97           C  
ANISOU 5168  CD  LYS C  72     4135   4537   4615   -365    -19    151       C  
ATOM   5169  CE  LYS C  72      16.698  28.677  31.138  1.00 35.16           C  
ANISOU 5169  CE  LYS C  72     4138   4554   4665   -343    -47    204       C  
ATOM   5170  NZ  LYS C  72      16.924  27.213  31.248  1.00 34.70           N  
ANISOU 5170  NZ  LYS C  72     4076   4478   4628   -339    -78    229       N  
ATOM   5171  N   TYR C  73      10.460  28.873  28.951  1.00 36.95           N  
ANISOU 5171  N   TYR C  73     4387   4774   4877   -259     69    -46       N  
ATOM   5172  CA  TYR C  73       9.788  27.724  28.356  1.00 35.91           C  
ANISOU 5172  CA  TYR C  73     4251   4629   4762   -229     66    -63       C  
ATOM   5173  C   TYR C  73       8.376  28.128  27.912  1.00 36.03           C  
ANISOU 5173  C   TYR C  73     4266   4645   4776   -214     92   -125       C  
ATOM   5174  O   TYR C  73       7.415  27.358  28.031  1.00 37.25           O  
ANISOU 5174  O   TYR C  73     4424   4796   4934   -223     94   -151       O  
ATOM   5175  CB  TYR C  73       9.714  26.575  29.376  1.00 36.77           C  
ANISOU 5175  CB  TYR C  73     4372   4734   4864   -281     46    -41       C  
ATOM   5176  CG  TYR C  73      11.051  26.048  29.837  1.00 37.51           C  
ANISOU 5176  CG  TYR C  73     4465   4821   4964   -297     13     19       C  
ATOM   5177  CD1 TYR C  73      11.728  26.640  30.906  1.00 37.20           C  
ANISOU 5177  CD1 TYR C  73     4436   4795   4901   -351      5     49       C  
ATOM   5178  CD2 TYR C  73      11.645  24.950  29.203  1.00 38.23           C  
ANISOU 5178  CD2 TYR C  73     4544   4892   5088   -256    -10     45       C  
ATOM   5179  CE1 TYR C  73      12.959  26.160  31.321  1.00 37.70           C  
ANISOU 5179  CE1 TYR C  73     4497   4852   4974   -364    -28    106       C  
ATOM   5180  CE2 TYR C  73      12.874  24.461  29.616  1.00 37.35           C  
ANISOU 5180  CE2 TYR C  73     4427   4772   4988   -268    -43     99       C  
ATOM   5181  CZ  TYR C  73      13.523  25.071  30.670  1.00 38.30           C  
ANISOU 5181  CZ  TYR C  73     4559   4907   5087   -322    -53    130       C  
ATOM   5182  OH  TYR C  73      14.744  24.591  31.073  1.00 40.83           O  
ANISOU 5182  OH  TYR C  73     4872   5217   5422   -332    -89    184       O  
ATOM   5183  N   LEU C  74       8.244  29.347  27.411  1.00 35.66           N  
ANISOU 5183  N   LEU C  74     4214   4603   4729   -190    108   -147       N  
ATOM   5184  CA  LEU C  74       6.958  29.818  26.928  1.00 37.10           C  
ANISOU 5184  CA  LEU C  74     4394   4783   4917   -170    127   -206       C  
ATOM   5185  C   LEU C  74       6.386  28.935  25.804  1.00 38.68           C  
ANISOU 5185  C   LEU C  74     4587   4972   5138   -117    125   -224       C  
ATOM   5186  O   LEU C  74       7.104  28.561  24.865  1.00 37.92           O  
ANISOU 5186  O   LEU C  74     4483   4869   5054    -70    114   -199       O  
ATOM   5187  CB  LEU C  74       7.054  31.276  26.465  1.00 36.60           C  
ANISOU 5187  CB  LEU C  74     4328   4722   4857   -149    136   -219       C  
ATOM   5188  CG  LEU C  74       5.771  31.860  25.858  1.00 36.35           C  
ANISOU 5188  CG  LEU C  74     4291   4682   4837   -122    150   -278       C  
ATOM   5189  CD1 LEU C  74       4.629  31.847  26.860  1.00 35.61           C  
ANISOU 5189  CD1 LEU C  74     4199   4596   4734   -169    165   -327       C  
ATOM   5190  CD2 LEU C  74       6.004  33.263  25.329  1.00 37.40           C  
ANISOU 5190  CD2 LEU C  74     4421   4810   4976    -99    151   -281       C  
ATOM   5191  N   TYR C  75       5.101  28.591  25.940  1.00 38.95           N  
ANISOU 5191  N   TYR C  75     4621   5003   5175   -127    135   -270       N  
ATOM   5192  CA  TYR C  75       4.302  28.029  24.852  1.00 38.78           C  
ANISOU 5192  CA  TYR C  75     4591   4970   5173    -77    135   -302       C  
ATOM   5193  C   TYR C  75       2.827  28.449  24.927  1.00 39.52           C  
ANISOU 5193  C   TYR C  75     4680   5065   5270    -84    153   -365       C  
ATOM   5194  O   TYR C  75       2.356  28.926  25.958  1.00 39.72           O  
ANISOU 5194  O   TYR C  75     4708   5101   5282   -135    167   -386       O  
ATOM   5195  CB  TYR C  75       4.453  26.505  24.767  1.00 41.01           C  
ANISOU 5195  CB  TYR C  75     4874   5241   5466    -73    118   -282       C  
ATOM   5196  CG  TYR C  75       3.776  25.670  25.848  1.00 42.48           C  
ANISOU 5196  CG  TYR C  75     5066   5427   5645   -131    117   -289       C  
ATOM   5197  CD1 TYR C  75       4.515  25.144  26.907  1.00 42.82           C  
ANISOU 5197  CD1 TYR C  75     5120   5472   5674   -183    102   -244       C  
ATOM   5198  CD2 TYR C  75       2.406  25.351  25.774  1.00 43.05           C  
ANISOU 5198  CD2 TYR C  75     5135   5498   5725   -136    128   -339       C  
ATOM   5199  CE1 TYR C  75       3.916  24.359  27.877  1.00 44.09           C  
ANISOU 5199  CE1 TYR C  75     5289   5635   5825   -241     99   -245       C  
ATOM   5200  CE2 TYR C  75       1.794  24.562  26.739  1.00 42.63           C  
ANISOU 5200  CE2 TYR C  75     5087   5447   5663   -193    128   -343       C  
ATOM   5201  CZ  TYR C  75       2.555  24.067  27.785  1.00 45.26           C  
ANISOU 5201  CZ  TYR C  75     5433   5784   5978   -247    114   -295       C  
ATOM   5202  OH  TYR C  75       1.974  23.284  28.757  1.00 48.08           O  
ANISOU 5202  OH  TYR C  75     5798   6146   6324   -310    112   -293       O  
ATOM   5203  N   PHE C  76       2.113  28.269  23.820  1.00 40.12           N  
ANISOU 5203  N   PHE C  76     4748   5130   5365    -33    152   -396       N  
ATOM   5204  CA  PHE C  76       0.693  28.575  23.747  1.00 39.34           C  
ANISOU 5204  CA  PHE C  76     4640   5029   5277    -33    165   -457       C  
ATOM   5205  C   PHE C  76      -0.179  27.345  23.565  1.00 41.16           C  
ANISOU 5205  C   PHE C  76     4866   5252   5520    -30    161   -480       C  
ATOM   5206  O   PHE C  76       0.175  26.411  22.837  1.00 42.92           O  
ANISOU 5206  O   PHE C  76     5090   5464   5752      3    146   -460       O  
ATOM   5207  CB  PHE C  76       0.422  29.520  22.591  1.00 38.80           C  
ANISOU 5207  CB  PHE C  76     4566   4953   5223     22    162   -479       C  
ATOM   5208  CG  PHE C  76       0.762  30.938  22.886  1.00 39.76           C  
ANISOU 5208  CG  PHE C  76     4690   5078   5340     12    167   -478       C  
ATOM   5209  CD1 PHE C  76       1.972  31.474  22.465  1.00 38.92           C  
ANISOU 5209  CD1 PHE C  76     4589   4972   5225     30    158   -430       C  
ATOM   5210  CD2 PHE C  76      -0.130  31.746  23.585  1.00 39.82           C  
ANISOU 5210  CD2 PHE C  76     4690   5087   5352    -16    181   -526       C  
ATOM   5211  CE1 PHE C  76       2.284  32.789  22.740  1.00 39.08           C  
ANISOU 5211  CE1 PHE C  76     4611   4991   5243     19    159   -428       C  
ATOM   5212  CE2 PHE C  76       0.182  33.064  23.863  1.00 39.20           C  
ANISOU 5212  CE2 PHE C  76     4612   5007   5273    -25    182   -528       C  
ATOM   5213  CZ  PHE C  76       1.391  33.583  23.441  1.00 39.52           C  
ANISOU 5213  CZ  PHE C  76     4662   5046   5307     -7    170   -477       C  
ATOM   5214  N   ASN C  77      -1.322  27.354  24.239  1.00 41.11           N  
ANISOU 5214  N   ASN C  77     4852   5252   5514    -67    177   -525       N  
ATOM   5215  CA  ASN C  77      -2.405  26.454  23.912  1.00 41.44           C  
ANISOU 5215  CA  ASN C  77     4884   5286   5573    -59    176   -560       C  
ATOM   5216  C   ASN C  77      -3.452  27.288  23.193  1.00 43.25           C  
ANISOU 5216  C   ASN C  77     5098   5511   5822    -22    183   -618       C  
ATOM   5217  O   ASN C  77      -4.105  28.130  23.806  1.00 45.84           O  
ANISOU 5217  O   ASN C  77     5416   5850   6150    -49    200   -657       O  
ATOM   5218  CB  ASN C  77      -3.008  25.824  25.171  1.00 40.93           C  
ANISOU 5218  CB  ASN C  77     4819   5236   5496   -131    189   -571       C  
ATOM   5219  CG  ASN C  77      -2.083  24.817  25.839  1.00 41.38           C  
ANISOU 5219  CG  ASN C  77     4892   5291   5537   -168    173   -512       C  
ATOM   5220  OD1 ASN C  77      -1.355  24.072  25.178  1.00 40.66           O  
ANISOU 5220  OD1 ASN C  77     4807   5182   5457   -133    150   -476       O  
ATOM   5221  ND2 ASN C  77      -2.121  24.783  27.171  1.00 41.31           N  
ANISOU 5221  ND2 ASN C  77     4890   5303   5503   -242    185   -504       N  
ATOM   5222  N   LEU C  78      -3.577  27.087  21.887  1.00 43.53           N  
ANISOU 5222  N   LEU C  78     5131   5532   5876     39    167   -624       N  
ATOM   5223  CA  LEU C  78      -4.650  27.700  21.124  1.00 45.05           C  
ANISOU 5223  CA  LEU C  78     5309   5716   6090     76    166   -677       C  
ATOM   5224  C   LEU C  78      -5.857  26.766  21.093  1.00 46.06           C  
ANISOU 5224  C   LEU C  78     5423   5840   6236     69    167   -719       C  
ATOM   5225  O   LEU C  78      -5.722  25.573  20.789  1.00 48.58           O  
ANISOU 5225  O   LEU C  78     5748   6151   6558     77    155   -701       O  
ATOM   5226  CB  LEU C  78      -4.205  28.013  19.694  1.00 43.98           C  
ANISOU 5226  CB  LEU C  78     5179   5569   5960    144    146   -661       C  
ATOM   5227  CG  LEU C  78      -2.876  28.720  19.433  1.00 43.13           C  
ANISOU 5227  CG  LEU C  78     5086   5466   5836    159    141   -611       C  
ATOM   5228  CD1 LEU C  78      -2.728  28.949  17.939  1.00 42.60           C  
ANISOU 5228  CD1 LEU C  78     5021   5391   5772    223    124   -606       C  
ATOM   5229  CD2 LEU C  78      -2.756  30.039  20.178  1.00 42.85           C  
ANISOU 5229  CD2 LEU C  78     5049   5435   5796    130    152   -615       C  
ATOM   5230  N   PHE C  79      -7.025  27.310  21.430  1.00 45.49           N  
ANISOU 5230  N   PHE C  79     5332   5772   6180     53    181   -776       N  
ATOM   5231  CA  PHE C  79      -8.293  26.595  21.309  1.00 45.54           C  
ANISOU 5231  CA  PHE C  79     5320   5775   6208     50    183   -823       C  
ATOM   5232  C   PHE C  79      -9.105  27.330  20.265  1.00 45.18           C  
ANISOU 5232  C   PHE C  79     5259   5715   6190    105    170   -868       C  
ATOM   5233  O   PHE C  79      -9.637  28.407  20.527  1.00 45.27           O  
ANISOU 5233  O   PHE C  79     5255   5729   6214    101    180   -907       O  
ATOM   5234  CB  PHE C  79      -9.046  26.543  22.638  1.00 44.53           C  
ANISOU 5234  CB  PHE C  79     5177   5668   6074    -19    211   -856       C  
ATOM   5235  CG  PHE C  79      -8.260  25.929  23.760  1.00 45.86           C  
ANISOU 5235  CG  PHE C  79     5362   5851   6210    -81    221   -809       C  
ATOM   5236  CD1 PHE C  79      -7.396  26.706  24.534  1.00 45.56           C  
ANISOU 5236  CD1 PHE C  79     5336   5828   6146   -110    231   -782       C  
ATOM   5237  CD2 PHE C  79      -8.382  24.576  24.050  1.00 46.75           C  
ANISOU 5237  CD2 PHE C  79     5479   5963   6319   -111    215   -790       C  
ATOM   5238  CE1 PHE C  79      -6.668  26.147  25.572  1.00 44.68           C  
ANISOU 5238  CE1 PHE C  79     5241   5730   6004   -168    236   -737       C  
ATOM   5239  CE2 PHE C  79      -7.659  24.010  25.090  1.00 48.41           C  
ANISOU 5239  CE2 PHE C  79     5707   6185   6501   -170    218   -742       C  
ATOM   5240  CZ  PHE C  79      -6.802  24.799  25.853  1.00 47.60           C  
ANISOU 5240  CZ  PHE C  79     5617   6099   6371   -198    228   -716       C  
ATOM   5241  N   ILE C  80      -9.171  26.744  19.074  1.00 45.39           N  
ANISOU 5241  N   ILE C  80     5291   5727   6229    156    147   -863       N  
ATOM   5242  CA  ILE C  80      -9.735  27.410  17.914  1.00 45.50           C  
ANISOU 5242  CA  ILE C  80     5296   5725   6264    214    127   -893       C  
ATOM   5243  C   ILE C  80     -11.116  26.854  17.585  1.00 48.58           C  
ANISOU 5243  C   ILE C  80     5663   6107   6684    222    121   -949       C  
ATOM   5244  O   ILE C  80     -11.394  25.663  17.754  1.00 48.15           O  
ANISOU 5244  O   ILE C  80     5608   6054   6632    204    122   -950       O  
ATOM   5245  CB  ILE C  80      -8.787  27.341  16.694  1.00 44.93           C  
ANISOU 5245  CB  ILE C  80     5246   5646   6178    268    103   -850       C  
ATOM   5246  CG1 ILE C  80      -7.373  27.785  17.103  1.00 44.49           C  
ANISOU 5246  CG1 ILE C  80     5210   5601   6094    254    111   -792       C  
ATOM   5247  CG2 ILE C  80      -9.325  28.187  15.545  1.00 44.45           C  
ANISOU 5247  CG2 ILE C  80     5180   5572   6134    321     81   -874       C  
ATOM   5248  CD1 ILE C  80      -6.329  27.713  16.012  1.00 42.75           C  
ANISOU 5248  CD1 ILE C  80     5007   5379   5855    300     94   -748       C  
ATOM   5249  N   SER C  81     -11.977  27.752  17.126  1.00 51.92           N  
ANISOU 5249  N   SER C  81     6069   6522   7135    250    111   -994       N  
ATOM   5250  CA  SER C  81     -13.359  27.459  16.811  1.00 51.11           C  
ANISOU 5250  CA  SER C  81     5940   6411   7067    260    104  -1054       C  
ATOM   5251  C   SER C  81     -13.684  28.146  15.490  1.00 50.08           C  
ANISOU 5251  C   SER C  81     5810   6262   6957    325     70  -1068       C  
ATOM   5252  O   SER C  81     -13.320  29.302  15.272  1.00 48.01           O  
ANISOU 5252  O   SER C  81     5553   5993   6693    344     61  -1058       O  
ATOM   5253  CB  SER C  81     -14.250  27.972  17.939  1.00 51.44           C  
ANISOU 5253  CB  SER C  81     5950   6465   7127    213    132  -1106       C  
ATOM   5254  OG  SER C  81     -15.578  28.182  17.510  1.00 57.20           O  
ANISOU 5254  OG  SER C  81     6649   7186   7899    235    121  -1170       O  
ATOM   5255  N   VAL C  82     -14.321  27.407  14.591  1.00 52.13           N  
ANISOU 5255  N   VAL C  82     6064   6511   7231    357     48  -1087       N  
ATOM   5256  CA  VAL C  82     -14.752  27.953  13.307  1.00 56.09           C  
ANISOU 5256  CA  VAL C  82     6566   6995   7750    415     11  -1103       C  
ATOM   5257  C   VAL C  82     -16.254  27.706  13.224  1.00 59.33           C  
ANISOU 5257  C   VAL C  82     6942   7397   8204    418      3  -1170       C  
ATOM   5258  O   VAL C  82     -16.703  26.560  13.127  1.00 62.69           O  
ANISOU 5258  O   VAL C  82     7360   7822   8634    411      2  -1183       O  
ATOM   5259  CB  VAL C  82     -14.011  27.322  12.095  1.00 54.73           C  
ANISOU 5259  CB  VAL C  82     6422   6820   7550    459    -12  -1062       C  
ATOM   5260  CG1 VAL C  82     -14.443  27.980  10.798  1.00 55.69           C  
ANISOU 5260  CG1 VAL C  82     6547   6928   7683    514    -51  -1075       C  
ATOM   5261  CG2 VAL C  82     -12.503  27.447  12.234  1.00 52.77           C  
ANISOU 5261  CG2 VAL C  82     6203   6585   7261    453      0   -998       C  
ATOM   5262  N   ASN C  83     -17.022  28.792  13.295  1.00 60.56           N  
ANISOU 5262  N   ASN C  83     7073   7542   8393    426     -4  -1213       N  
ATOM   5263  CA  ASN C  83     -18.483  28.731  13.320  1.00 60.83           C  
ANISOU 5263  CA  ASN C  83     7067   7569   8475    427    -10  -1283       C  
ATOM   5264  C   ASN C  83     -18.973  27.701  14.344  1.00 62.53           C  
ANISOU 5264  C   ASN C  83     7261   7802   8692    371     24  -1306       C  
ATOM   5265  O   ASN C  83     -19.780  26.818  14.041  1.00 63.38           O  
ANISOU 5265  O   ASN C  83     7353   7907   8819    373     16  -1335       O  
ATOM   5266  CB  ASN C  83     -19.034  28.501  11.908  1.00 60.12           C  
ANISOU 5266  CB  ASN C  83     6980   7460   8402    483    -56  -1294       C  
ATOM   5267  CG  ASN C  83     -18.452  29.480  10.895  1.00 62.76           C  
ANISOU 5267  CG  ASN C  83     7340   7778   8725    531    -92  -1261       C  
ATOM   5268  OD1 ASN C  83     -18.438  30.690  11.121  1.00 64.22           O  
ANISOU 5268  OD1 ASN C  83     7518   7954   8926    535    -97  -1267       O  
ATOM   5269  ND2 ASN C  83     -17.957  28.959   9.783  1.00 62.48           N  
ANISOU 5269  ND2 ASN C  83     7334   7742   8661    567   -118  -1225       N  
ATOM   5270  N   SER C  84     -18.445  27.847  15.561  1.00 62.85           N  
ANISOU 5270  N   SER C  84     7304   7864   8712    319     63  -1292       N  
ATOM   5271  CA  SER C  84     -18.679  26.954  16.704  1.00 64.50           C  
ANISOU 5271  CA  SER C  84     7499   8095   8910    254    100  -1301       C  
ATOM   5272  C   SER C  84     -18.097  25.538  16.583  1.00 63.49           C  
ANISOU 5272  C   SER C  84     7398   7970   8755    241     98  -1253       C  
ATOM   5273  O   SER C  84     -18.107  24.786  17.562  1.00 67.34           O  
ANISOU 5273  O   SER C  84     7882   8474   9229    183    125  -1247       O  
ATOM   5274  CB  SER C  84     -20.156  26.915  17.117  1.00 66.45           C  
ANISOU 5274  CB  SER C  84     7697   8349   9200    232    113  -1377       C  
ATOM   5275  OG  SER C  84     -20.315  26.165  18.316  1.00 69.24           O  
ANISOU 5275  OG  SER C  84     8040   8731   9537    160    153  -1380       O  
ATOM   5276  N   ILE C  85     -17.583  25.173  15.411  1.00 60.97           N  
ANISOU 5276  N   ILE C  85     7104   7632   8426    293     65  -1221       N  
ATOM   5277  CA  ILE C  85     -16.904  23.880  15.255  1.00 61.31           C  
ANISOU 5277  CA  ILE C  85     7174   7674   8447    286     60  -1177       C  
ATOM   5278  C   ILE C  85     -15.474  24.017  15.777  1.00 58.19           C  
ANISOU 5278  C   ILE C  85     6809   7289   8011    268     75  -1115       C  
ATOM   5279  O   ILE C  85     -14.666  24.723  15.181  1.00 61.16           O  
ANISOU 5279  O   ILE C  85     7205   7662   8371    305     63  -1085       O  
ATOM   5280  CB  ILE C  85     -16.878  23.390  13.780  1.00 61.39           C  
ANISOU 5280  CB  ILE C  85     7197   7664   8461    349     20  -1172       C  
ATOM   5281  CG1 ILE C  85     -18.239  23.575  13.080  1.00 62.66           C  
ANISOU 5281  CG1 ILE C  85     7330   7813   8663    379     -2  -1233       C  
ATOM   5282  CG2 ILE C  85     -16.400  21.948  13.701  1.00 58.73           C  
ANISOU 5282  CG2 ILE C  85     6878   7323   8111    340     15  -1142       C  
ATOM   5283  CD1 ILE C  85     -19.405  22.810  13.691  1.00 64.13           C  
ANISOU 5283  CD1 ILE C  85     7483   8003   8881    338     10  -1279       C  
ATOM   5284  N   GLU C  86     -15.157  23.362  16.890  1.00 56.75           N  
ANISOU 5284  N   GLU C  86     6629   7119   7812    209     99  -1093       N  
ATOM   5285  CA  GLU C  86     -13.826  23.536  17.472  1.00 58.53           C  
ANISOU 5285  CA  GLU C  86     6882   7355   8001    188    111  -1035       C  
ATOM   5286  C   GLU C  86     -12.769  22.536  16.998  1.00 57.64           C  
ANISOU 5286  C   GLU C  86     6797   7232   7871    206     94   -981       C  
ATOM   5287  O   GLU C  86     -13.007  21.328  16.932  1.00 59.77           O  
ANISOU 5287  O   GLU C  86     7066   7491   8149    197     83   -980       O  
ATOM   5288  CB  GLU C  86     -13.848  23.691  19.008  1.00 64.74           C  
ANISOU 5288  CB  GLU C  86     7659   8164   8772    113    147  -1035       C  
ATOM   5289  CG  GLU C  86     -14.575  22.625  19.823  1.00 70.42           C  
ANISOU 5289  CG  GLU C  86     8364   8892   9497     54    161  -1050       C  
ATOM   5290  CD  GLU C  86     -14.936  23.113  21.232  1.00 73.01           C  
ANISOU 5290  CD  GLU C  86     8676   9251   9812    -16    199  -1071       C  
ATOM   5291  OE1 GLU C  86     -14.809  22.336  22.209  1.00 70.88           O  
ANISOU 5291  OE1 GLU C  86     8411   8995   9522    -80    214  -1047       O  
ATOM   5292  OE2 GLU C  86     -15.351  24.284  21.369  1.00 72.85           O  
ANISOU 5292  OE2 GLU C  86     8637   9240   9802     -8    213  -1112       O  
ATOM   5293  N   LEU C  87     -11.605  23.075  16.644  1.00 52.86           N  
ANISOU 5293  N   LEU C  87     6213   6627   7241    234     89   -939       N  
ATOM   5294  CA  LEU C  87     -10.455  22.285  16.233  1.00 49.53           C  
ANISOU 5294  CA  LEU C  87     5815   6200   6803    253     75   -889       C  
ATOM   5295  C   LEU C  87      -9.835  21.667  17.482  1.00 49.20           C  
ANISOU 5295  C   LEU C  87     5782   6165   6746    192     89   -851       C  
ATOM   5296  O   LEU C  87     -10.130  22.109  18.589  1.00 51.28           O  
ANISOU 5296  O   LEU C  87     6036   6442   7003    139    113   -859       O  
ATOM   5297  CB  LEU C  87      -9.438  23.176  15.509  1.00 47.54           C  
ANISOU 5297  CB  LEU C  87     5579   5952   6529    297     68   -858       C  
ATOM   5298  CG  LEU C  87      -9.723  23.652  14.077  1.00 48.99           C  
ANISOU 5298  CG  LEU C  87     5763   6129   6718    361     46   -877       C  
ATOM   5299  CD1 LEU C  87     -10.952  24.547  13.995  1.00 52.04           C  
ANISOU 5299  CD1 LEU C  87     6130   6513   7129    366     44   -929       C  
ATOM   5300  CD2 LEU C  87      -8.528  24.394  13.504  1.00 49.10           C  
ANISOU 5300  CD2 LEU C  87     5797   6153   6706    392     43   -834       C  
ATOM   5301  N   PRO C  88      -8.982  20.635  17.323  1.00 49.63           N  
ANISOU 5301  N   PRO C  88     5852   6208   6796    199     74   -812       N  
ATOM   5302  CA  PRO C  88      -8.272  20.126  18.501  1.00 48.43           C  
ANISOU 5302  CA  PRO C  88     5711   6061   6630    141     82   -768       C  
ATOM   5303  C   PRO C  88      -7.333  21.169  19.111  1.00 47.07           C  
ANISOU 5303  C   PRO C  88     5548   5907   6430    124     99   -735       C  
ATOM   5304  O   PRO C  88      -6.894  22.093  18.417  1.00 45.75           O  
ANISOU 5304  O   PRO C  88     5383   5743   6254    167     99   -732       O  
ATOM   5305  CB  PRO C  88      -7.452  18.957  17.942  1.00 48.93           C  
ANISOU 5305  CB  PRO C  88     5786   6103   6699    170     56   -736       C  
ATOM   5306  CG  PRO C  88      -8.134  18.570  16.674  1.00 48.78           C  
ANISOU 5306  CG  PRO C  88     5760   6071   6703    226     37   -775       C  
ATOM   5307  CD  PRO C  88      -8.681  19.843  16.114  1.00 49.03           C  
ANISOU 5307  CD  PRO C  88     5783   6116   6730    255     47   -809       C  
ATOM   5308  N   LYS C  89      -7.046  21.015  20.403  1.00 47.69           N  
ANISOU 5308  N   LYS C  89     5631   5995   6493     59    112   -709       N  
ATOM   5309  CA  LYS C  89      -6.060  21.844  21.106  1.00 47.60           C  
ANISOU 5309  CA  LYS C  89     5630   6000   6454     35    125   -672       C  
ATOM   5310  C   LYS C  89      -4.765  21.915  20.305  1.00 44.96           C  
ANISOU 5310  C   LYS C  89     5309   5658   6114     86    109   -631       C  
ATOM   5311  O   LYS C  89      -4.224  20.894  19.888  1.00 42.49           O  
ANISOU 5311  O   LYS C  89     5003   5331   5811    106     88   -607       O  
ATOM   5312  CB  LYS C  89      -5.805  21.283  22.512  1.00 50.91           C  
ANISOU 5312  CB  LYS C  89     6057   6428   6857    -40    131   -641       C  
ATOM   5313  CG  LYS C  89      -4.636  21.886  23.285  1.00 50.58           C  
ANISOU 5313  CG  LYS C  89     6030   6400   6787    -68    137   -594       C  
ATOM   5314  CD  LYS C  89      -4.238  20.943  24.412  1.00 51.05           C  
ANISOU 5314  CD  LYS C  89     6102   6460   6834   -134    129   -552       C  
ATOM   5315  CE  LYS C  89      -2.804  21.152  24.868  1.00 56.04           C  
ANISOU 5315  CE  LYS C  89     6749   7094   7446   -145    120   -493       C  
ATOM   5316  NZ  LYS C  89      -1.801  20.900  23.791  1.00 56.55           N  
ANISOU 5316  NZ  LYS C  89     6818   7141   7527    -78     98   -466       N  
ATOM   5317  N   ARG C  90      -4.288  23.132  20.093  1.00 44.17           N  
ANISOU 5317  N   ARG C  90     5210   5570   6000    105    118   -625       N  
ATOM   5318  CA  ARG C  90      -3.124  23.377  19.263  1.00 44.67           C  
ANISOU 5318  CA  ARG C  90     5283   5633   6056    152    107   -590       C  
ATOM   5319  C   ARG C  90      -1.987  23.947  20.124  1.00 45.93           C  
ANISOU 5319  C   ARG C  90     5452   5805   6194    118    115   -543       C  
ATOM   5320  O   ARG C  90      -2.173  24.934  20.839  1.00 49.17           O  
ANISOU 5320  O   ARG C  90     5861   6227   6593     86    132   -552       O  
ATOM   5321  CB  ARG C  90      -3.510  24.353  18.161  1.00 44.46           C  
ANISOU 5321  CB  ARG C  90     5252   5608   6033    204    107   -618       C  
ATOM   5322  CG  ARG C  90      -2.708  24.209  16.894  1.00 45.28           C  
ANISOU 5322  CG  ARG C  90     5361   5711   6131    264     92   -597       C  
ATOM   5323  CD  ARG C  90      -3.300  25.054  15.774  1.00 46.04           C  
ANISOU 5323  CD  ARG C  90     5454   5808   6230    310     87   -627       C  
ATOM   5324  NE  ARG C  90      -3.056  24.435  14.472  1.00 48.53           N  
ANISOU 5324  NE  ARG C  90     5771   6121   6543    365     71   -628       N  
ATOM   5325  CZ  ARG C  90      -1.850  24.248  13.937  1.00 49.40           C  
ANISOU 5325  CZ  ARG C  90     5888   6242   6638    390     68   -591       C  
ATOM   5326  NH1 ARG C  90      -0.748  24.632  14.574  1.00 48.24           N  
ANISOU 5326  NH1 ARG C  90     5745   6106   6478    367     78   -546       N  
ATOM   5327  NH2 ARG C  90      -1.746  23.666  12.753  1.00 51.65           N  
ANISOU 5327  NH2 ARG C  90     6174   6530   6921    439     55   -600       N  
ATOM   5328  N   LYS C  91      -0.819  23.313  20.071  1.00 44.09           N  
ANISOU 5328  N   LYS C  91     5225   5568   5957    126    102   -497       N  
ATOM   5329  CA  LYS C  91       0.317  23.721  20.903  1.00 42.55           C  
ANISOU 5329  CA  LYS C  91     5039   5384   5744     93    105   -449       C  
ATOM   5330  C   LYS C  91       1.462  24.345  20.090  1.00 42.21           C  
ANISOU 5330  C   LYS C  91     4996   5348   5693    137    102   -420       C  
ATOM   5331  O   LYS C  91       2.031  23.696  19.206  1.00 44.42           O  
ANISOU 5331  O   LYS C  91     5273   5623   5982    181     90   -408       O  
ATOM   5332  CB  LYS C  91       0.816  22.537  21.727  1.00 41.18           C  
ANISOU 5332  CB  LYS C  91     4871   5200   5574     54     90   -414       C  
ATOM   5333  CG  LYS C  91       1.904  22.890  22.721  1.00 40.82           C  
ANISOU 5333  CG  LYS C  91     4833   5164   5509     12     90   -365       C  
ATOM   5334  CD  LYS C  91       2.322  21.678  23.527  1.00 39.48           C  
ANISOU 5334  CD  LYS C  91     4672   4983   5346    -26     68   -329       C  
ATOM   5335  CE  LYS C  91       3.422  22.057  24.498  1.00 40.63           C  
ANISOU 5335  CE  LYS C  91     4824   5138   5472    -68     64   -280       C  
ATOM   5336  NZ  LYS C  91       3.491  21.116  25.653  1.00 45.19           N  
ANISOU 5336  NZ  LYS C  91     5414   5708   6047   -130     46   -249       N  
ATOM   5337  N   GLU C  92       1.779  25.605  20.386  1.00 40.05           N  
ANISOU 5337  N   GLU C  92     4724   5087   5404    123    115   -411       N  
ATOM   5338  CA  GLU C  92       2.847  26.320  19.691  1.00 39.32           C  
ANISOU 5338  CA  GLU C  92     4632   5004   5302    157    114   -380       C  
ATOM   5339  C   GLU C  92       3.937  26.734  20.676  1.00 38.13           C  
ANISOU 5339  C   GLU C  92     4487   4863   5138    115    116   -334       C  
ATOM   5340  O   GLU C  92       3.771  27.698  21.430  1.00 37.42           O  
ANISOU 5340  O   GLU C  92     4400   4778   5037     79    126   -339       O  
ATOM   5341  CB  GLU C  92       2.318  27.550  18.941  1.00 40.11           C  
ANISOU 5341  CB  GLU C  92     4732   5108   5400    185    121   -405       C  
ATOM   5342  CG  GLU C  92       1.127  27.303  18.023  1.00 43.15           C  
ANISOU 5342  CG  GLU C  92     5111   5483   5798    222    116   -453       C  
ATOM   5343  CD  GLU C  92       1.355  26.191  17.008  1.00 46.42           C  
ANISOU 5343  CD  GLU C  92     5523   5895   6218    268    104   -452       C  
ATOM   5344  OE1 GLU C  92       2.331  26.275  16.227  1.00 48.84           O  
ANISOU 5344  OE1 GLU C  92     5830   6213   6514    301    101   -423       O  
ATOM   5345  OE2 GLU C  92       0.545  25.234  16.979  1.00 47.74           O  
ANISOU 5345  OE2 GLU C  92     5687   6050   6400    269     98   -481       O  
ATOM   5346  N   VAL C  93       5.043  25.990  20.663  1.00 36.33           N  
ANISOU 5346  N   VAL C  93     4256   4634   4912    122    104   -294       N  
ATOM   5347  CA  VAL C  93       6.191  26.253  21.525  1.00 36.26           C  
ANISOU 5347  CA  VAL C  93     4250   4633   4893     86    100   -246       C  
ATOM   5348  C   VAL C  93       6.992  27.416  20.952  1.00 36.71           C  
ANISOU 5348  C   VAL C  93     4303   4704   4940    108    107   -226       C  
ATOM   5349  O   VAL C  93       7.415  27.362  19.800  1.00 38.76           O  
ANISOU 5349  O   VAL C  93     4554   4969   5202    158    107   -221       O  
ATOM   5350  CB  VAL C  93       7.096  25.009  21.640  1.00 36.12           C  
ANISOU 5350  CB  VAL C  93     4227   4607   4889     90     80   -211       C  
ATOM   5351  CG1 VAL C  93       8.250  25.259  22.600  1.00 36.24           C  
ANISOU 5351  CG1 VAL C  93     4244   4629   4896     50     72   -162       C  
ATOM   5352  CG2 VAL C  93       6.291  23.802  22.088  1.00 36.00           C  
ANISOU 5352  CG2 VAL C  93     4216   4573   4887     70     68   -229       C  
ATOM   5353  N   LEU C  94       7.178  28.471  21.739  1.00 36.34           N  
ANISOU 5353  N   LEU C  94     4262   4664   4880     70    114   -215       N  
ATOM   5354  CA  LEU C  94       7.985  29.612  21.309  1.00 37.40           C  
ANISOU 5354  CA  LEU C  94     4394   4809   5007     83    118   -191       C  
ATOM   5355  C   LEU C  94       9.416  29.572  21.870  1.00 39.49           C  
ANISOU 5355  C   LEU C  94     4655   5082   5267     61    110   -137       C  
ATOM   5356  O   LEU C  94      10.366  29.946  21.188  1.00 40.15           O  
ANISOU 5356  O   LEU C  94     4728   5175   5349     87    110   -108       O  
ATOM   5357  CB  LEU C  94       7.309  30.926  21.686  1.00 38.23           C  
ANISOU 5357  CB  LEU C  94     4507   4912   5106     61    127   -216       C  
ATOM   5358  CG  LEU C  94       6.130  31.454  20.856  1.00 38.69           C  
ANISOU 5358  CG  LEU C  94     4565   4962   5172     93    132   -263       C  
ATOM   5359  CD1 LEU C  94       5.564  32.702  21.517  1.00 35.83           C  
ANISOU 5359  CD1 LEU C  94     4208   4595   4811     63    138   -288       C  
ATOM   5360  CD2 LEU C  94       6.534  31.747  19.416  1.00 38.61           C  
ANISOU 5360  CD2 LEU C  94     4551   4957   5161    148    128   -249       C  
ATOM   5361  N   CYS C  95       9.562  29.127  23.118  1.00 40.13           N  
ANISOU 5361  N   CYS C  95     4741   5159   5344     11    102   -123       N  
ATOM   5362  CA  CYS C  95      10.869  29.003  23.752  1.00 37.84           C  
ANISOU 5362  CA  CYS C  95     4448   4875   5053    -13     89    -73       C  
ATOM   5363  C   CYS C  95      11.040  27.598  24.300  1.00 36.86           C  
ANISOU 5363  C   CYS C  95     4324   4740   4940    -29     71    -57       C  
ATOM   5364  O   CYS C  95      10.289  27.176  25.184  1.00 37.05           O  
ANISOU 5364  O   CYS C  95     4361   4758   4958    -70     68    -72       O  
ATOM   5365  CB  CYS C  95      11.029  30.035  24.872  1.00 38.81           C  
ANISOU 5365  CB  CYS C  95     4581   5003   5159    -69     92    -63       C  
ATOM   5366  SG  CYS C  95      10.572  31.722  24.401  1.00 42.19           S  
ANISOU 5366  SG  CYS C  95     5012   5434   5580    -58    109    -89       S  
ATOM   5367  N   HIS C  96      12.023  26.881  23.756  1.00 35.77           N  
ANISOU 5367  N   HIS C  96     4169   4600   4819      3     57    -29       N  
ATOM   5368  CA  HIS C  96      12.314  25.504  24.138  1.00 34.86           C  
ANISOU 5368  CA  HIS C  96     4052   4470   4724     -2     32    -11       C  
ATOM   5369  C   HIS C  96      13.277  25.437  25.279  1.00 35.58           C  
ANISOU 5369  C   HIS C  96     4145   4560   4813    -51     11     35       C  
ATOM   5370  O   HIS C  96      13.513  24.358  25.817  1.00 37.27           O  
ANISOU 5370  O   HIS C  96     4359   4757   5042    -67    -15     55       O  
ATOM   5371  CB  HIS C  96      12.869  24.719  22.954  1.00 34.08           C  
ANISOU 5371  CB  HIS C  96     3931   4367   4650     60     26    -12       C  
ATOM   5372  CG  HIS C  96      11.956  24.704  21.757  1.00 33.89           C  
ANISOU 5372  CG  HIS C  96     3905   4345   4625    109     43    -58       C  
ATOM   5373  ND1 HIS C  96      11.178  23.646  21.449  1.00 33.93           N  
ANISOU 5373  ND1 HIS C  96     3911   4332   4646    128     35    -87       N  
ATOM   5374  CD2 HIS C  96      11.704  25.677  20.785  1.00 33.17           C  
ANISOU 5374  CD2 HIS C  96     3812   4271   4519    142     66    -78       C  
ATOM   5375  CE1 HIS C  96      10.462  23.928  20.339  1.00 33.29           C  
ANISOU 5375  CE1 HIS C  96     3829   4258   4560    171     52   -126       C  
ATOM   5376  NE2 HIS C  96      10.782  25.173  19.939  1.00 33.17           N  
ANISOU 5376  NE2 HIS C  96     3813   4265   4525    179     70   -119       N  
ATOM   5377  N   GLY C  97      13.854  26.578  25.654  1.00 35.19           N  
ANISOU 5377  N   GLY C  97     4097   4526   4747    -74     19     55       N  
ATOM   5378  CA  GLY C  97      14.779  26.652  26.798  1.00 35.93           C  
ANISOU 5378  CA  GLY C  97     4193   4621   4835   -124     -2    100       C  
ATOM   5379  C   GLY C  97      16.259  26.647  26.436  1.00 36.57           C  
ANISOU 5379  C   GLY C  97     4250   4707   4935   -100    -15    141       C  
ATOM   5380  O   GLY C  97      17.122  26.854  27.289  1.00 35.56           O  
ANISOU 5380  O   GLY C  97     4123   4583   4806   -138    -34    180       O  
ATOM   5381  N   HIS C  98      16.545  26.422  25.160  1.00 37.19           N  
ANISOU 5381  N   HIS C  98     4307   4791   5033    -37     -5    131       N  
ATOM   5382  CA  HIS C  98      17.902  26.256  24.685  1.00 37.73           C  
ANISOU 5382  CA  HIS C  98     4345   4866   5122     -8    -15    162       C  
ATOM   5383  C   HIS C  98      18.032  26.960  23.369  1.00 37.08           C  
ANISOU 5383  C   HIS C  98     4247   4805   5034     41     13    146       C  
ATOM   5384  O   HIS C  98      17.333  26.633  22.408  1.00 37.27           O  
ANISOU 5384  O   HIS C  98     4270   4829   5059     83     28    111       O  
ATOM   5385  CB  HIS C  98      18.228  24.763  24.551  1.00 39.20           C  
ANISOU 5385  CB  HIS C  98     4516   5033   5345     17    -42    167       C  
ATOM   5386  CG  HIS C  98      19.539  24.472  23.857  1.00 41.07           C  
ANISOU 5386  CG  HIS C  98     4715   5279   5611     59    -48    187       C  
ATOM   5387  ND1 HIS C  98      20.731  24.606  24.472  1.00 45.09           N  
ANISOU 5387  ND1 HIS C  98     5208   5791   6133     37    -69    230       N  
ATOM   5388  CD2 HIS C  98      19.813  24.027  22.565  1.00 42.99           C  
ANISOU 5388  CD2 HIS C  98     4931   5531   5872    124    -35    164       C  
ATOM   5389  CE1 HIS C  98      21.722  24.266  23.617  1.00 45.68           C  
ANISOU 5389  CE1 HIS C  98     5243   5875   6235     86    -68    234       C  
ATOM   5390  NE2 HIS C  98      21.159  23.914  22.451  1.00 45.82           N  
ANISOU 5390  NE2 HIS C  98     5254   5899   6254    138    -46    193       N  
ATOM   5391  N   ASP C  99      18.923  27.950  23.330  1.00 36.39           N  
ANISOU 5391  N   ASP C  99     4149   4737   4940     32     21    174       N  
ATOM   5392  CA  ASP C  99      19.246  28.693  22.115  1.00 34.51           C  
ANISOU 5392  CA  ASP C  99     3893   4523   4693     71     47    170       C  
ATOM   5393  C   ASP C  99      18.012  29.104  21.307  1.00 35.48           C  
ANISOU 5393  C   ASP C  99     4034   4647   4797     95     69    128       C  
ATOM   5394  O   ASP C  99      17.906  28.822  20.110  1.00 35.84           O  
ANISOU 5394  O   ASP C  99     4068   4705   4844    144     83    109       O  
ATOM   5395  CB  ASP C  99      20.229  27.892  21.269  1.00 33.90           C  
ANISOU 5395  CB  ASP C  99     3780   4458   4640    118     45    179       C  
ATOM   5396  CG  ASP C  99      21.652  28.013  21.759  1.00 33.73           C  
ANISOU 5396  CG  ASP C  99     3733   4446   4635    100     31    224       C  
ATOM   5397  OD1 ASP C  99      22.513  27.268  21.253  1.00 34.48           O  
ANISOU 5397  OD1 ASP C  99     3793   4549   4756    134     26    230       O  
ATOM   5398  OD2 ASP C  99      21.934  28.855  22.637  1.00 33.72           O  
ANISOU 5398  OD2 ASP C  99     3743   4444   4622     52     24    252       O  
ATOM   5399  N   ASP C 100      17.073  29.764  21.979  1.00 36.34           N  
ANISOU 5399  N   ASP C 100     4170   4745   4890     59     71    112       N  
ATOM   5400  CA  ASP C 100      15.828  30.161  21.349  1.00 35.91           C  
ANISOU 5400  CA  ASP C 100     4132   4687   4823     78     87     70       C  
ATOM   5401  C   ASP C 100      15.985  31.381  20.439  1.00 35.78           C  
ANISOU 5401  C   ASP C 100     4113   4687   4792     96    104     75       C  
ATOM   5402  O   ASP C 100      16.977  32.112  20.524  1.00 35.16           O  
ANISOU 5402  O   ASP C 100     4025   4622   4711     82    104    111       O  
ATOM   5403  CB  ASP C 100      14.758  30.377  22.406  1.00 37.51           C  
ANISOU 5403  CB  ASP C 100     4360   4872   5017     34     84     46       C  
ATOM   5404  CG  ASP C 100      14.297  29.079  23.030  1.00 39.59           C  
ANISOU 5404  CG  ASP C 100     4630   5120   5291     22     70     34       C  
ATOM   5405  OD1 ASP C 100      13.981  28.138  22.273  1.00 41.07           O  
ANISOU 5405  OD1 ASP C 100     4809   5302   5491     62     70     15       O  
ATOM   5406  OD2 ASP C 100      14.236  28.990  24.279  1.00 42.19           O  
ANISOU 5406  OD2 ASP C 100     4971   5442   5614    -30     59     45       O  
ATOM   5407  N   ASP C 101      14.995  31.577  19.571  1.00 34.77           N  
ANISOU 5407  N   ASP C 101     3995   4558   4657    127    115     40       N  
ATOM   5408  CA  ASP C 101      15.036  32.563  18.493  1.00 33.99           C  
ANISOU 5408  CA  ASP C 101     3894   4473   4544    150    126     44       C  
ATOM   5409  C   ASP C 101      14.687  33.974  18.904  1.00 33.53           C  
ANISOU 5409  C   ASP C 101     3854   4406   4480    119    125     46       C  
ATOM   5410  O   ASP C 101      15.042  34.926  18.232  1.00 33.23           O  
ANISOU 5410  O   ASP C 101     3813   4378   4433    126    128     66       O  
ATOM   5411  CB  ASP C 101      14.066  32.140  17.393  1.00 34.24           C  
ANISOU 5411  CB  ASP C 101     3931   4506   4571    196    133      5       C  
ATOM   5412  CG  ASP C 101      14.587  30.983  16.595  1.00 35.85           C  
ANISOU 5412  CG  ASP C 101     4114   4726   4779    237    137      3       C  
ATOM   5413  OD1 ASP C 101      15.680  30.474  16.924  1.00 35.80           O  
ANISOU 5413  OD1 ASP C 101     4088   4728   4783    232    134     31       O  
ATOM   5414  OD2 ASP C 101      13.914  30.578  15.634  1.00 37.72           O  
ANISOU 5414  OD2 ASP C 101     4353   4966   5010    276    141    -27       O  
ATOM   5415  N   TYR C 102      13.972  34.108  20.003  1.00 34.99           N  
ANISOU 5415  N   TYR C 102     4054   4571   4669     83    119     25       N  
ATOM   5416  CA  TYR C 102      13.376  35.385  20.330  1.00 36.37           C  
ANISOU 5416  CA  TYR C 102     4244   4731   4842     60    117     11       C  
ATOM   5417  C   TYR C 102      14.013  35.922  21.586  1.00 36.11           C  
ANISOU 5417  C   TYR C 102     4215   4695   4810      8    109     33       C  
ATOM   5418  O   TYR C 102      14.242  35.173  22.539  1.00 36.16           O  
ANISOU 5418  O   TYR C 102     4220   4701   4816    -19    105     39       O  
ATOM   5419  CB  TYR C 102      11.859  35.238  20.516  1.00 36.27           C  
ANISOU 5419  CB  TYR C 102     4245   4701   4834     63    119    -44       C  
ATOM   5420  CG  TYR C 102      11.181  34.424  19.441  1.00 35.49           C  
ANISOU 5420  CG  TYR C 102     4143   4603   4736    111    123    -71       C  
ATOM   5421  CD1 TYR C 102      10.928  33.064  19.638  1.00 36.37           C  
ANISOU 5421  CD1 TYR C 102     4250   4714   4852    118    123    -86       C  
ATOM   5422  CD2 TYR C 102      10.814  34.998  18.227  1.00 34.73           C  
ANISOU 5422  CD2 TYR C 102     4049   4509   4636    148    123    -78       C  
ATOM   5423  CE1 TYR C 102      10.315  32.299  18.660  1.00 36.63           C  
ANISOU 5423  CE1 TYR C 102     4280   4748   4887    162    125   -112       C  
ATOM   5424  CE2 TYR C 102      10.201  34.243  17.239  1.00 36.62           C  
ANISOU 5424  CE2 TYR C 102     4286   4752   4874    191    125   -104       C  
ATOM   5425  CZ  TYR C 102       9.949  32.891  17.462  1.00 37.69           C  
ANISOU 5425  CZ  TYR C 102     4416   4886   5015    199    127   -122       C  
ATOM   5426  OH  TYR C 102       9.342  32.114  16.488  1.00 37.95           O  
ANISOU 5426  OH  TYR C 102     4448   4922   5049    241    128   -150       O  
ATOM   5427  N   SER C 103      14.282  37.224  21.585  1.00 35.80           N  
ANISOU 5427  N   SER C 103     4179   4651   4770     -7    105     48       N  
ATOM   5428  CA  SER C 103      14.958  37.863  22.707  1.00 36.64           C  
ANISOU 5428  CA  SER C 103     4289   4755   4877    -56     97     70       C  
ATOM   5429  C   SER C 103      14.090  37.881  23.966  1.00 37.01           C  
ANISOU 5429  C   SER C 103     4350   4788   4922    -96     95     30       C  
ATOM   5430  O   SER C 103      14.606  38.041  25.066  1.00 37.89           O  
ANISOU 5430  O   SER C 103     4466   4902   5029   -140     88     44       O  
ATOM   5431  CB  SER C 103      15.395  39.271  22.339  1.00 34.73           C  
ANISOU 5431  CB  SER C 103     4047   4507   4639    -62     90     92       C  
ATOM   5432  OG  SER C 103      14.276  40.128  22.288  1.00 34.73           O  
ANISOU 5432  OG  SER C 103     4063   4485   4647    -61     87     51       O  
ATOM   5433  N   PHE C 104      12.783  37.698  23.810  1.00 36.90           N  
ANISOU 5433  N   PHE C 104     4345   4764   4911    -81    103    -20       N  
ATOM   5434  CA  PHE C 104      11.915  37.688  24.977  1.00 38.55           C  
ANISOU 5434  CA  PHE C 104     4564   4965   5115   -120    106    -62       C  
ATOM   5435  C   PHE C 104      11.995  36.414  25.807  1.00 40.97           C  
ANISOU 5435  C   PHE C 104     4872   5282   5411   -145    106    -57       C  
ATOM   5436  O   PHE C 104      11.548  36.402  26.954  1.00 43.03           O  
ANISOU 5436  O   PHE C 104     5143   5545   5661   -190    109    -81       O  
ATOM   5437  CB  PHE C 104      10.458  38.065  24.646  1.00 37.33           C  
ANISOU 5437  CB  PHE C 104     4415   4796   4972   -101    113   -123       C  
ATOM   5438  CG  PHE C 104       9.801  37.188  23.628  1.00 35.85           C  
ANISOU 5438  CG  PHE C 104     4223   4609   4789    -54    118   -139       C  
ATOM   5439  CD1 PHE C 104       9.653  37.627  22.317  1.00 36.10           C  
ANISOU 5439  CD1 PHE C 104     4252   4635   4830     -7    115   -137       C  
ATOM   5440  CD2 PHE C 104       9.289  35.942  23.981  1.00 36.48           C  
ANISOU 5440  CD2 PHE C 104     4302   4694   4863    -59    125   -158       C  
ATOM   5441  CE1 PHE C 104       9.025  36.835  21.364  1.00 35.77           C  
ANISOU 5441  CE1 PHE C 104     4207   4594   4790     35    118   -155       C  
ATOM   5442  CE2 PHE C 104       8.663  35.139  23.036  1.00 36.19           C  
ANISOU 5442  CE2 PHE C 104     4261   4656   4833    -15    128   -176       C  
ATOM   5443  CZ  PHE C 104       8.529  35.588  21.724  1.00 36.01           C  
ANISOU 5443  CZ  PHE C 104     4235   4629   4818     32    125   -177       C  
ATOM   5444  N   CYS C 105      12.569  35.351  25.243  1.00 42.34           N  
ANISOU 5444  N   CYS C 105     5036   5464   5587   -118    103    -28       N  
ATOM   5445  CA  CYS C 105      12.713  34.081  25.969  1.00 41.77           C  
ANISOU 5445  CA  CYS C 105     4964   5395   5508   -140     97    -17       C  
ATOM   5446  C   CYS C 105      13.535  34.230  27.253  1.00 42.04           C  
ANISOU 5446  C   CYS C 105     5004   5436   5531   -197     84     14       C  
ATOM   5447  O   CYS C 105      13.253  33.565  28.260  1.00 39.99           O  
ANISOU 5447  O   CYS C 105     4755   5179   5260   -238     79      9       O  
ATOM   5448  CB  CYS C 105      13.316  33.000  25.069  1.00 42.03           C  
ANISOU 5448  CB  CYS C 105     4982   5432   5553    -96     92      9       C  
ATOM   5449  SG  CYS C 105      12.295  32.564  23.634  1.00 45.10           S  
ANISOU 5449  SG  CYS C 105     5367   5816   5951    -33    104    -30       S  
ATOM   5450  N   ARG C 106      14.534  35.113  27.220  1.00 42.62           N  
ANISOU 5450  N   ARG C 106     5072   5514   5607   -203     77     47       N  
ATOM   5451  CA  ARG C 106      15.379  35.355  28.395  1.00 45.17           C  
ANISOU 5451  CA  ARG C 106     5400   5843   5919   -257     62     78       C  
ATOM   5452  C   ARG C 106      14.755  36.282  29.455  1.00 45.42           C  
ANISOU 5452  C   ARG C 106     5449   5873   5934   -307     67     44       C  
ATOM   5453  O   ARG C 106      15.331  36.487  30.528  1.00 46.37           O  
ANISOU 5453  O   ARG C 106     5576   6000   6040   -357     54     63       O  
ATOM   5454  CB  ARG C 106      16.814  35.775  28.007  1.00 47.19           C  
ANISOU 5454  CB  ARG C 106     5639   6104   6185   -247     51    131       C  
ATOM   5455  CG  ARG C 106      16.954  36.753  26.849  1.00 51.33           C  
ANISOU 5455  CG  ARG C 106     6154   6627   6720   -209     61    133       C  
ATOM   5456  CD  ARG C 106      17.528  38.106  27.271  1.00 57.63           C  
ANISOU 5456  CD  ARG C 106     6955   7423   7518   -240     54    149       C  
ATOM   5457  NE  ARG C 106      16.855  38.687  28.439  1.00 62.02           N  
ANISOU 5457  NE  ARG C 106     7531   7971   8061   -288     52    114       N  
ATOM   5458  CZ  ARG C 106      17.463  39.006  29.582  1.00 59.62           C  
ANISOU 5458  CZ  ARG C 106     7234   7671   7748   -340     37    131       C  
ATOM   5459  NH1 ARG C 106      18.774  38.822  29.706  1.00 60.10           N  
ANISOU 5459  NH1 ARG C 106     7280   7740   7812   -350     21    185       N  
ATOM   5460  NH2 ARG C 106      16.763  39.517  30.596  1.00 53.15           N  
ANISOU 5460  NH2 ARG C 106     6431   6848   6913   -382     39     91       N  
ATOM   5461  N   ALA C 107      13.568  36.809  29.168  1.00 42.92           N  
ANISOU 5461  N   ALA C 107     5138   5548   5620   -294     83     -9       N  
ATOM   5462  CA  ALA C 107      12.867  37.666  30.110  1.00 42.93           C  
ANISOU 5462  CA  ALA C 107     5151   5549   5609   -336     90    -53       C  
ATOM   5463  C   ALA C 107      12.418  36.901  31.353  1.00 44.22           C  
ANISOU 5463  C   ALA C 107     5327   5728   5747   -389     92    -69       C  
ATOM   5464  O   ALA C 107      11.959  35.757  31.262  1.00 45.27           O  
ANISOU 5464  O   ALA C 107     5460   5863   5876   -382     96    -72       O  
ATOM   5465  CB  ALA C 107      11.676  38.325  29.442  1.00 43.69           C  
ANISOU 5465  CB  ALA C 107     5245   5631   5720   -304    104   -109       C  
ATOM   5466  N   LEU C 108      12.543  37.556  32.508  1.00 43.44           N  
ANISOU 5466  N   LEU C 108     5239   5637   5628   -444     90    -80       N  
ATOM   5467  CA  LEU C 108      12.174  36.979  33.801  1.00 41.77           C  
ANISOU 5467  CA  LEU C 108     5041   5446   5383   -506     92    -93       C  
ATOM   5468  C   LEU C 108      10.828  37.500  34.326  1.00 43.22           C  
ANISOU 5468  C   LEU C 108     5229   5637   5555   -529    117   -170       C  
ATOM   5469  O   LEU C 108      10.269  38.466  33.795  1.00 41.39           O  
ANISOU 5469  O   LEU C 108     4989   5391   5345   -499    128   -212       O  
ATOM   5470  CB  LEU C 108      13.265  37.271  34.836  1.00 38.15           C  
ANISOU 5470  CB  LEU C 108     4592   4998   4904   -559     72    -54       C  
ATOM   5471  CG  LEU C 108      14.691  36.824  34.539  1.00 36.62           C  
ANISOU 5471  CG  LEU C 108     4391   4800   4722   -546     45     20       C  
ATOM   5472  CD1 LEU C 108      15.625  37.368  35.605  1.00 35.12           C  
ANISOU 5472  CD1 LEU C 108     4210   4620   4512   -601     24     47       C  
ATOM   5473  CD2 LEU C 108      14.796  35.308  34.451  1.00 36.01           C  
ANISOU 5473  CD2 LEU C 108     4312   4724   4644   -540     34     52       C  
ATOM   5474  N   LYS C 109      10.324  36.844  35.372  1.00 44.67           N  
ANISOU 5474  N   LYS C 109     5423   5843   5705   -583    125   -186       N  
ATOM   5475  CA  LYS C 109       9.168  37.320  36.122  1.00 46.60           C  
ANISOU 5475  CA  LYS C 109     5670   6104   5931   -620    150   -259       C  
ATOM   5476  C   LYS C 109       9.363  38.785  36.551  1.00 47.25           C  
ANISOU 5476  C   LYS C 109     5753   6185   6016   -636    151   -290       C  
ATOM   5477  O   LYS C 109      10.364  39.132  37.181  1.00 47.30           O  
ANISOU 5477  O   LYS C 109     5768   6196   6005   -669    133   -254       O  
ATOM   5478  CB  LYS C 109       8.925  36.421  37.341  1.00 48.13           C  
ANISOU 5478  CB  LYS C 109     5878   6329   6078   -690    154   -255       C  
ATOM   5479  CG  LYS C 109       7.583  36.659  38.022  1.00 52.18           C  
ANISOU 5479  CG  LYS C 109     6389   6866   6570   -727    187   -335       C  
ATOM   5480  CD  LYS C 109       7.117  35.460  38.837  1.00 53.85           C  
ANISOU 5480  CD  LYS C 109     6610   7106   6741   -783    194   -327       C  
ATOM   5481  CE  LYS C 109       7.647  35.489  40.258  1.00 53.34           C  
ANISOU 5481  CE  LYS C 109     6567   7074   6623   -866    186   -308       C  
ATOM   5482  NZ  LYS C 109       7.210  34.276  40.996  1.00 52.79           N  
ANISOU 5482  NZ  LYS C 109     6511   7032   6515   -924    189   -293       N  
ATOM   5483  N   GLY C 110       8.410  39.636  36.181  1.00 47.88           N  
ANISOU 5483  N   GLY C 110     5820   6252   6119   -609    169   -357       N  
ATOM   5484  CA  GLY C 110       8.460  41.055  36.514  1.00 48.45           C  
ANISOU 5484  CA  GLY C 110     5891   6316   6202   -619    168   -396       C  
ATOM   5485  C   GLY C 110       9.278  41.926  35.573  1.00 50.20           C  
ANISOU 5485  C   GLY C 110     6107   6504   6462   -572    145   -361       C  
ATOM   5486  O   GLY C 110       9.336  43.145  35.746  1.00 53.80           O  
ANISOU 5486  O   GLY C 110     6562   6945   6934   -575    139   -390       O  
ATOM   5487  N   GLU C 111       9.916  41.318  34.579  1.00 48.13           N  
ANISOU 5487  N   GLU C 111     5842   6229   6214   -529    132   -299       N  
ATOM   5488  CA  GLU C 111      10.704  42.080  33.618  1.00 46.59           C  
ANISOU 5488  CA  GLU C 111     5642   6007   6052   -487    113   -261       C  
ATOM   5489  C   GLU C 111       9.797  42.700  32.561  1.00 45.06           C  
ANISOU 5489  C   GLU C 111     5437   5787   5896   -432    118   -303       C  
ATOM   5490  O   GLU C 111       8.886  42.061  32.056  1.00 45.42           O  
ANISOU 5490  O   GLU C 111     5476   5832   5946   -405    132   -330       O  
ATOM   5491  CB  GLU C 111      11.779  41.193  32.972  1.00 47.77           C  
ANISOU 5491  CB  GLU C 111     5789   6159   6200   -465     99   -182       C  
ATOM   5492  CG  GLU C 111      12.738  41.914  32.031  1.00 47.74           C  
ANISOU 5492  CG  GLU C 111     5779   6136   6223   -429     81   -136       C  
ATOM   5493  CD  GLU C 111      13.962  41.086  31.673  1.00 47.47           C  
ANISOU 5493  CD  GLU C 111     5739   6111   6185   -420     68    -61       C  
ATOM   5494  OE1 GLU C 111      14.722  41.510  30.780  1.00 47.90           O  
ANISOU 5494  OE1 GLU C 111     5785   6156   6259   -388     58    -22       O  
ATOM   5495  OE2 GLU C 111      14.174  40.018  32.283  1.00 48.36           O  
ANISOU 5495  OE2 GLU C 111     5856   6242   6276   -445     67    -42       O  
ATOM   5496  N   THR C 112      10.051  43.962  32.250  1.00 45.44           N  
ANISOU 5496  N   THR C 112     5483   5809   5971   -419    103   -308       N  
ATOM   5497  CA  THR C 112       9.346  44.670  31.196  1.00 44.69           C  
ANISOU 5497  CA  THR C 112     5380   5684   5916   -368     99   -337       C  
ATOM   5498  C   THR C 112       9.781  44.101  29.846  1.00 44.07           C  
ANISOU 5498  C   THR C 112     5298   5600   5846   -317     92   -280       C  
ATOM   5499  O   THR C 112      10.977  43.965  29.591  1.00 46.38           O  
ANISOU 5499  O   THR C 112     5591   5897   6131   -318     80   -213       O  
ATOM   5500  CB  THR C 112       9.668  46.176  31.278  1.00 45.02           C  
ANISOU 5500  CB  THR C 112     5422   5697   5986   -374     78   -346       C  
ATOM   5501  OG1 THR C 112       9.312  46.656  32.581  1.00 46.26           O  
ANISOU 5501  OG1 THR C 112     5581   5862   6131   -422     86   -404       O  
ATOM   5502  CG2 THR C 112       8.916  46.976  30.223  1.00 45.02           C  
ANISOU 5502  CG2 THR C 112     5415   5660   6030   -323     66   -375       C  
ATOM   5503  N   VAL C 113       8.813  43.740  29.002  1.00 42.24           N  
ANISOU 5503  N   VAL C 113     5059   5360   5629   -274    100   -308       N  
ATOM   5504  CA  VAL C 113       9.096  43.296  27.630  1.00 40.29           C  
ANISOU 5504  CA  VAL C 113     4809   5108   5391   -223     93   -264       C  
ATOM   5505  C   VAL C 113       8.467  44.260  26.626  1.00 40.02           C  
ANISOU 5505  C   VAL C 113     4771   5042   5391   -181     79   -286       C  
ATOM   5506  O   VAL C 113       7.258  44.484  26.644  1.00 39.69           O  
ANISOU 5506  O   VAL C 113     4724   4987   5368   -169     83   -349       O  
ATOM   5507  CB  VAL C 113       8.578  41.863  27.354  1.00 39.13           C  
ANISOU 5507  CB  VAL C 113     4658   4979   5228   -205    110   -269       C  
ATOM   5508  CG1 VAL C 113       8.824  41.462  25.907  1.00 38.56           C  
ANISOU 5508  CG1 VAL C 113     4583   4904   5164   -151    104   -232       C  
ATOM   5509  CG2 VAL C 113       9.225  40.855  28.287  1.00 38.46           C  
ANISOU 5509  CG2 VAL C 113     4579   4922   5112   -246    117   -240       C  
ATOM   5510  N   ASN C 114       9.298  44.846  25.774  1.00 39.91           N  
ANISOU 5510  N   ASN C 114     4760   5017   5388   -161     61   -233       N  
ATOM   5511  CA  ASN C 114       8.816  45.613  24.637  1.00 41.69           C  
ANISOU 5511  CA  ASN C 114     4984   5212   5641   -119     43   -238       C  
ATOM   5512  C   ASN C 114       9.517  45.109  23.373  1.00 43.04           C  
ANISOU 5512  C   ASN C 114     5155   5397   5800    -85     40   -175       C  
ATOM   5513  O   ASN C 114      10.699  45.409  23.145  1.00 44.33           O  
ANISOU 5513  O   ASN C 114     5319   5567   5955    -94     32   -115       O  
ATOM   5514  CB  ASN C 114       9.032  47.124  24.834  1.00 41.40           C  
ANISOU 5514  CB  ASN C 114     4951   5143   5634   -134     17   -241       C  
ATOM   5515  CG  ASN C 114       8.320  47.959  23.772  1.00 43.62           C  
ANISOU 5515  CG  ASN C 114     5233   5388   5950    -94     -6   -255       C  
ATOM   5516  OD1 ASN C 114       7.354  47.498  23.160  1.00 45.81           O  
ANISOU 5516  OD1 ASN C 114     5507   5663   6235    -60     -2   -286       O  
ATOM   5517  ND2 ASN C 114       8.786  49.190  23.552  1.00 42.24           N  
ANISOU 5517  ND2 ASN C 114     5063   5183   5801   -100    -35   -231       N  
ATOM   5518  N   THR C 115       8.809  44.316  22.570  1.00 41.04           N  
ANISOU 5518  N   THR C 115     4899   5149   5542    -47     48   -190       N  
ATOM   5519  CA  THR C 115       9.428  43.726  21.385  1.00 41.13           C  
ANISOU 5519  CA  THR C 115     4909   5180   5538    -14     49   -139       C  
ATOM   5520  C   THR C 115       8.452  43.564  20.244  1.00 41.64           C  
ANISOU 5520  C   THR C 115     4974   5234   5611     32     43   -162       C  
ATOM   5521  O   THR C 115       7.251  43.387  20.457  1.00 41.78           O  
ANISOU 5521  O   THR C 115     4989   5239   5643     41     46   -221       O  
ATOM   5522  CB  THR C 115      10.096  42.363  21.685  1.00 42.04           C  
ANISOU 5522  CB  THR C 115     5018   5328   5625    -21     70   -114       C  
ATOM   5523  OG1 THR C 115      11.059  42.071  20.668  1.00 40.95           O  
ANISOU 5523  OG1 THR C 115     4875   5210   5473      1     70    -57       O  
ATOM   5524  CG2 THR C 115       9.064  41.234  21.745  1.00 42.13           C  
ANISOU 5524  CG2 THR C 115     5027   5346   5632     -5     84   -160       C  
ATOM   5525  N   SER C 116       8.975  43.632  19.025  1.00 42.28           N  
ANISOU 5525  N   SER C 116     5057   5323   5682     60     35   -116       N  
ATOM   5526  CA  SER C 116       8.162  43.335  17.858  1.00 41.35           C  
ANISOU 5526  CA  SER C 116     4942   5204   5565    105     29   -132       C  
ATOM   5527  C   SER C 116       8.738  42.148  17.083  1.00 41.41           C  
ANISOU 5527  C   SER C 116     4944   5247   5541    129     46   -101       C  
ATOM   5528  O   SER C 116       9.929  42.098  16.779  1.00 41.34           O  
ANISOU 5528  O   SER C 116     4932   5261   5513    123     52    -47       O  
ATOM   5529  CB  SER C 116       7.908  44.578  16.990  1.00 39.78           C  
ANISOU 5529  CB  SER C 116     4751   4976   5384    120     -1   -120       C  
ATOM   5530  OG  SER C 116       9.085  45.098  16.429  1.00 39.13           O  
ANISOU 5530  OG  SER C 116     4674   4907   5288    111     -8    -52       O  
ATOM   5531  N   ILE C 117       7.868  41.187  16.795  1.00 41.55           N  
ANISOU 5531  N   ILE C 117     4959   5269   5557    155     55   -140       N  
ATOM   5532  CA  ILE C 117       8.269  39.909  16.242  1.00 41.02           C  
ANISOU 5532  CA  ILE C 117     4886   5234   5466    178     71   -125       C  
ATOM   5533  C   ILE C 117       7.847  39.793  14.789  1.00 39.74           C  
ANISOU 5533  C   ILE C 117     4727   5077   5294    222     63   -125       C  
ATOM   5534  O   ILE C 117       6.653  39.755  14.500  1.00 40.10           O  
ANISOU 5534  O   ILE C 117     4776   5105   5353    243     53   -170       O  
ATOM   5535  CB  ILE C 117       7.639  38.758  17.036  1.00 41.06           C  
ANISOU 5535  CB  ILE C 117     4884   5239   5474    172     86   -168       C  
ATOM   5536  CG1 ILE C 117       7.908  38.950  18.529  1.00 42.59           C  
ANISOU 5536  CG1 ILE C 117     5078   5428   5675    123     92   -172       C  
ATOM   5537  CG2 ILE C 117       8.166  37.417  16.540  1.00 41.03           C  
ANISOU 5537  CG2 ILE C 117     4873   5263   5452    194     99   -152       C  
ATOM   5538  CD1 ILE C 117       6.732  38.585  19.408  1.00 44.38           C  
ANISOU 5538  CD1 ILE C 117     5304   5643   5915    107     99   -232       C  
ATOM   5539  N   PRO C 118       8.827  39.724  13.870  1.00 40.25           N  
ANISOU 5539  N   PRO C 118     4789   5169   5332    236     66    -77       N  
ATOM   5540  CA  PRO C 118       8.520  39.586  12.450  1.00 41.13           C  
ANISOU 5540  CA  PRO C 118     4906   5294   5426    275     59    -74       C  
ATOM   5541  C   PRO C 118       7.879  38.247  12.150  1.00 41.43           C  
ANISOU 5541  C   PRO C 118     4939   5343   5459    306     70   -114       C  
ATOM   5542  O   PRO C 118       8.112  37.274  12.872  1.00 42.07           O  
ANISOU 5542  O   PRO C 118     5010   5431   5542    297     87   -126       O  
ATOM   5543  CB  PRO C 118       9.895  39.672  11.781  1.00 40.77           C  
ANISOU 5543  CB  PRO C 118     4854   5284   5350    273     70    -14       C  
ATOM   5544  CG  PRO C 118      10.856  39.267  12.840  1.00 40.62           C  
ANISOU 5544  CG  PRO C 118     4821   5276   5335    244     87      2       C  
ATOM   5545  CD  PRO C 118      10.279  39.803  14.110  1.00 39.56           C  
ANISOU 5545  CD  PRO C 118     4694   5106   5231    213     78    -24       C  
ATOM   5546  N   PHE C 119       7.081  38.209  11.089  1.00 43.63           N  
ANISOU 5546  N   PHE C 119     5225   5619   5731    339     57   -133       N  
ATOM   5547  CA  PHE C 119       6.433  36.983  10.618  1.00 46.03           C  
ANISOU 5547  CA  PHE C 119     5525   5933   6029    372     63   -172       C  
ATOM   5548  C   PHE C 119       5.953  37.138   9.183  1.00 47.64           C  
ANISOU 5548  C   PHE C 119     5740   6146   6214    407     47   -174       C  
ATOM   5549  O   PHE C 119       5.769  38.260   8.705  1.00 49.64           O  
ANISOU 5549  O   PHE C 119     6005   6387   6467    405     25   -155       O  
ATOM   5550  CB  PHE C 119       5.238  36.619  11.508  1.00 43.00           C  
ANISOU 5550  CB  PHE C 119     5139   5519   5678    366     60   -229       C  
ATOM   5551  CG  PHE C 119       4.114  37.608  11.451  1.00 42.71           C  
ANISOU 5551  CG  PHE C 119     5111   5449   5666    368     36   -257       C  
ATOM   5552  CD1 PHE C 119       3.045  37.413  10.586  1.00 43.80           C  
ANISOU 5552  CD1 PHE C 119     5253   5579   5809    402     19   -292       C  
ATOM   5553  CD2 PHE C 119       4.116  38.733  12.268  1.00 41.54           C  
ANISOU 5553  CD2 PHE C 119     4965   5277   5540    337     27   -253       C  
ATOM   5554  CE1 PHE C 119       1.995  38.321  10.537  1.00 44.60           C  
ANISOU 5554  CE1 PHE C 119     5359   5647   5940    406     -7   -320       C  
ATOM   5555  CE2 PHE C 119       3.080  39.645  12.215  1.00 41.95           C  
ANISOU 5555  CE2 PHE C 119     5021   5295   5622    342      2   -284       C  
ATOM   5556  CZ  PHE C 119       2.015  39.439  11.355  1.00 42.70           C  
ANISOU 5556  CZ  PHE C 119     5118   5380   5724    377    -15   -318       C  
ATOM   5557  N   SER C 120       5.739  36.010   8.508  1.00 48.88           N  
ANISOU 5557  N   SER C 120     5892   6322   6355    439     55   -197       N  
ATOM   5558  CA  SER C 120       5.052  36.000   7.215  1.00 50.29           C  
ANISOU 5558  CA  SER C 120     6082   6509   6517    474     37   -211       C  
ATOM   5559  C   SER C 120       4.343  34.674   6.989  1.00 50.15           C  
ANISOU 5559  C   SER C 120     6058   6494   6503    503     42   -261       C  
ATOM   5560  O   SER C 120       4.870  33.624   7.341  1.00 55.77           O  
ANISOU 5560  O   SER C 120     6757   7220   7213    505     63   -267       O  
ATOM   5561  CB  SER C 120       6.021  36.298   6.062  1.00 49.58           C  
ANISOU 5561  CB  SER C 120     5996   6460   6381    482     41   -163       C  
ATOM   5562  OG  SER C 120       6.797  35.163   5.729  1.00 50.34           O  
ANISOU 5562  OG  SER C 120     6078   6594   6453    498     68   -164       O  
ATOM   5563  N   PHE C 121       3.146  34.722   6.418  1.00 48.73           N  
ANISOU 5563  N   PHE C 121     5886   6296   6331    525     19   -297       N  
ATOM   5564  CA  PHE C 121       2.450  33.500   6.024  1.00 48.41           C  
ANISOU 5564  CA  PHE C 121     5841   6259   6293    555     19   -343       C  
ATOM   5565  C   PHE C 121       1.752  33.648   4.668  1.00 49.09           C  
ANISOU 5565  C   PHE C 121     5940   6352   6358    588     -5   -356       C  
ATOM   5566  O   PHE C 121       1.473  34.763   4.228  1.00 45.79           O  
ANISOU 5566  O   PHE C 121     5536   5924   5937    585    -30   -337       O  
ATOM   5567  CB  PHE C 121       1.495  33.009   7.124  1.00 45.95           C  
ANISOU 5567  CB  PHE C 121     5520   5914   6024    543     20   -390       C  
ATOM   5568  CG  PHE C 121       0.258  33.845   7.295  1.00 45.95           C  
ANISOU 5568  CG  PHE C 121     5524   5878   6054    540     -4   -420       C  
ATOM   5569  CD1 PHE C 121      -0.869  33.628   6.497  1.00 46.43           C  
ANISOU 5569  CD1 PHE C 121     5589   5930   6123    570    -28   -459       C  
ATOM   5570  CD2 PHE C 121       0.199  34.828   8.284  1.00 46.54           C  
ANISOU 5570  CD2 PHE C 121     5597   5929   6156    508     -6   -414       C  
ATOM   5571  CE1 PHE C 121      -2.020  34.391   6.663  1.00 46.78           C  
ANISOU 5571  CE1 PHE C 121     5632   5940   6202    570    -53   -489       C  
ATOM   5572  CE2 PHE C 121      -0.952  35.596   8.457  1.00 47.35           C  
ANISOU 5572  CE2 PHE C 121     5699   5998   6292    507    -29   -448       C  
ATOM   5573  CZ  PHE C 121      -2.061  35.378   7.646  1.00 47.29           C  
ANISOU 5573  CZ  PHE C 121     5693   5981   6295    539    -53   -485       C  
ATOM   5574  N   GLU C 122       1.481  32.515   4.024  1.00 52.73           N  
ANISOU 5574  N   GLU C 122     6398   6829   6806    618     -2   -388       N  
ATOM   5575  CA  GLU C 122       0.951  32.487   2.662  1.00 59.04           C  
ANISOU 5575  CA  GLU C 122     7210   7644   7578    650    -25   -400       C  
ATOM   5576  C   GLU C 122      -0.562  32.343   2.551  1.00 59.58           C  
ANISOU 5576  C   GLU C 122     7281   7679   7677    667    -53   -451       C  
ATOM   5577  O   GLU C 122      -1.141  32.783   1.559  1.00 68.22           O  
ANISOU 5577  O   GLU C 122     8389   8774   8755    686    -83   -454       O  
ATOM   5578  CB  GLU C 122       1.639  31.412   1.812  1.00 69.64           C  
ANISOU 5578  CB  GLU C 122     8548   9029   8881    676     -6   -405       C  
ATOM   5579  CG  GLU C 122       2.659  31.940   0.809  1.00 76.81           C  
ANISOU 5579  CG  GLU C 122     9464   9984   9733    677      1   -358       C  
ATOM   5580  CD  GLU C 122       2.016  32.570  -0.422  1.00 81.79           C  
ANISOU 5580  CD  GLU C 122    10117  10625  10333    693    -30   -354       C  
ATOM   5581  OE1 GLU C 122       1.400  33.655  -0.298  1.00 83.69           O  
ANISOU 5581  OE1 GLU C 122    10370  10834  10592    679    -60   -339       O  
ATOM   5582  OE2 GLU C 122       2.139  31.984  -1.521  1.00 83.04           O  
ANISOU 5582  OE2 GLU C 122    10280  10822  10449    718    -28   -366       O  
ATOM   5583  N   GLY C 123      -1.204  31.708   3.524  1.00 53.07           N  
ANISOU 5583  N   GLY C 123     6443   6827   6895    660    -47   -492       N  
ATOM   5584  CA  GLY C 123      -2.668  31.663   3.524  1.00 51.75           C  
ANISOU 5584  CA  GLY C 123     6273   6627   6762    671    -73   -542       C  
ATOM   5585  C   GLY C 123      -3.309  30.462   2.849  1.00 51.00           C  
ANISOU 5585  C   GLY C 123     6175   6538   6664    702    -80   -586       C  
ATOM   5586  O   GLY C 123      -3.075  30.173   1.678  1.00 51.89           O  
ANISOU 5586  O   GLY C 123     6298   6679   6738    729    -88   -582       O  
ATOM   5587  N   ILE C 124      -4.143  29.777   3.615  1.00 52.20           N  
ANISOU 5587  N   ILE C 124     6312   6664   6856    696    -78   -630       N  
ATOM   5588  CA  ILE C 124      -4.816  28.555   3.203  1.00 50.34           C  
ANISOU 5588  CA  ILE C 124     6071   6426   6628    719    -85   -676       C  
ATOM   5589  C   ILE C 124      -6.256  28.968   2.884  1.00 47.96           C  
ANISOU 5589  C   ILE C 124     5768   6099   6355    732   -119   -716       C  
ATOM   5590  O   ILE C 124      -6.578  30.146   3.019  1.00 46.32           O  
ANISOU 5590  O   ILE C 124     5562   5875   6160    722   -134   -705       O  
ATOM   5591  CB  ILE C 124      -4.695  27.521   4.363  1.00 50.16           C  
ANISOU 5591  CB  ILE C 124     6032   6392   6634    697    -60   -692       C  
ATOM   5592  CG1 ILE C 124      -3.844  26.334   3.940  1.00 51.10           C  
ANISOU 5592  CG1 ILE C 124     6151   6534   6730    715    -46   -689       C  
ATOM   5593  CG2 ILE C 124      -6.030  27.166   5.003  1.00 48.91           C  
ANISOU 5593  CG2 ILE C 124     5859   6202   6521    686    -69   -742       C  
ATOM   5594  CD1 ILE C 124      -2.385  26.699   3.789  1.00 53.95           C  
ANISOU 5594  CD1 ILE C 124     6517   6926   7054    712    -26   -637       C  
ATOM   5595  N   LEU C 125      -7.120  28.052   2.447  1.00 46.16           N  
ANISOU 5595  N   LEU C 125     5534   5864   6140    753   -134   -762       N  
ATOM   5596  CA  LEU C 125      -8.536  28.417   2.306  1.00 46.24           C  
ANISOU 5596  CA  LEU C 125     5537   5846   6186    761   -166   -803       C  
ATOM   5597  C   LEU C 125      -9.260  28.422   3.654  1.00 47.48           C  
ANISOU 5597  C   LEU C 125     5670   5973   6395    730   -153   -833       C  
ATOM   5598  O   LEU C 125      -9.317  27.403   4.337  1.00 48.59           O  
ANISOU 5598  O   LEU C 125     5798   6110   6550    714   -132   -852       O  
ATOM   5599  CB  LEU C 125      -9.284  27.526   1.302  1.00 43.81           C  
ANISOU 5599  CB  LEU C 125     5230   5540   5874    795   -191   -844       C  
ATOM   5600  CG  LEU C 125     -10.726  27.985   0.998  1.00 42.12           C  
ANISOU 5600  CG  LEU C 125     5008   5299   5696    807   -230   -884       C  
ATOM   5601  CD1 LEU C 125     -10.764  29.423   0.491  1.00 40.62           C  
ANISOU 5601  CD1 LEU C 125     4831   5104   5496    813   -258   -854       C  
ATOM   5602  CD2 LEU C 125     -11.448  27.054   0.036  1.00 39.88           C  
ANISOU 5602  CD2 LEU C 125     4725   5017   5408    839   -255   -924       C  
ATOM   5603  N   PHE C 126      -9.808  29.573   4.031  1.00 49.74           N  
ANISOU 5603  N   PHE C 126     5950   6239   6709    718   -165   -837       N  
ATOM   5604  CA  PHE C 126     -10.614  29.678   5.243  1.00 52.75           C  
ANISOU 5604  CA  PHE C 126     6306   6596   7139    689   -153   -873       C  
ATOM   5605  C   PHE C 126     -12.031  30.068   4.883  1.00 55.63           C  
ANISOU 5605  C   PHE C 126     6655   6936   7543    706   -188   -922       C  
ATOM   5606  O   PHE C 126     -12.229  30.858   3.959  1.00 61.70           O  
ANISOU 5606  O   PHE C 126     7436   7698   8306    732   -224   -912       O  
ATOM   5607  CB  PHE C 126     -10.068  30.762   6.172  1.00 53.31           C  
ANISOU 5607  CB  PHE C 126     6376   6662   7216    658   -136   -846       C  
ATOM   5608  CG  PHE C 126      -8.702  30.483   6.709  1.00 53.53           C  
ANISOU 5608  CG  PHE C 126     6414   6711   7211    635   -103   -799       C  
ATOM   5609  CD1 PHE C 126      -8.530  29.657   7.809  1.00 54.53           C  
ANISOU 5609  CD1 PHE C 126     6531   6842   7347    603    -71   -807       C  
ATOM   5610  CD2 PHE C 126      -7.584  31.073   6.133  1.00 56.13           C  
ANISOU 5610  CD2 PHE C 126     6766   7059   7502    643   -104   -745       C  
ATOM   5611  CE1 PHE C 126      -7.264  29.407   8.318  1.00 57.06           C  
ANISOU 5611  CE1 PHE C 126     6860   7179   7641    582    -45   -763       C  
ATOM   5612  CE2 PHE C 126      -6.311  30.825   6.634  1.00 58.41           C  
ANISOU 5612  CE2 PHE C 126     7059   7367   7764    623    -74   -703       C  
ATOM   5613  CZ  PHE C 126      -6.152  29.991   7.732  1.00 57.21           C  
ANISOU 5613  CZ  PHE C 126     6896   7215   7624    594    -46   -712       C  
ATOM   5614  N   PRO C 127     -13.025  29.522   5.607  1.00 57.67           N  
ANISOU 5614  N   PRO C 127     6888   7181   7844    690   -179   -973       N  
ATOM   5615  CA  PRO C 127     -14.339  30.186   5.688  1.00 60.94           C  
ANISOU 5615  CA  PRO C 127     7276   7567   8308    695   -205  -1022       C  
ATOM   5616  C   PRO C 127     -14.119  31.649   6.133  1.00 66.71           C  
ANISOU 5616  C   PRO C 127     8008   8286   9054    684   -208  -1005       C  
ATOM   5617  O   PRO C 127     -13.165  31.891   6.869  1.00 71.02           O  
ANISOU 5617  O   PRO C 127     8561   8842   9579    657   -178   -971       O  
ATOM   5618  CB  PRO C 127     -15.057  29.381   6.770  1.00 59.12           C  
ANISOU 5618  CB  PRO C 127     7017   7334   8111    663   -176  -1068       C  
ATOM   5619  CG  PRO C 127     -14.459  28.014   6.674  1.00 58.76           C  
ANISOU 5619  CG  PRO C 127     6984   7307   8035    660   -158  -1052       C  
ATOM   5620  CD  PRO C 127     -13.034  28.180   6.218  1.00 55.91           C  
ANISOU 5620  CD  PRO C 127     6655   6965   7623    670   -152   -990       C  
ATOM   5621  N   LYS C 128     -14.959  32.630   5.772  1.00 73.93           N  
ANISOU 5621  N   LYS C 128     8910   9173  10004    703   -246  -1030       N  
ATOM   5622  CA  LYS C 128     -16.355  32.504   5.377  1.00 72.03           C  
ANISOU 5622  CA  LYS C 128     8645   8913   9809    724   -278  -1087       C  
ATOM   5623  C   LYS C 128     -17.129  32.252   6.684  1.00 70.14           C  
ANISOU 5623  C   LYS C 128     8366   8668   9615    690   -245  -1143       C  
ATOM   5624  O   LYS C 128     -17.862  31.272   6.813  1.00 71.01           O  
ANISOU 5624  O   LYS C 128     8456   8782   9740    685   -237  -1183       O  
ATOM   5625  CB  LYS C 128     -16.541  31.409   4.317  1.00 79.28           C  
ANISOU 5625  CB  LYS C 128     9576   9844  10701    752   -296  -1091       C  
ATOM   5626  CG  LYS C 128     -17.551  31.720   3.223  1.00 87.19           C  
ANISOU 5626  CG  LYS C 128    10574  10826  11727    790   -353  -1117       C  
ATOM   5627  CD  LYS C 128     -18.887  31.046   3.495  1.00 89.31           C  
ANISOU 5627  CD  LYS C 128    10804  11081  12046    790   -358  -1187       C  
ATOM   5628  CE  LYS C 128     -19.852  31.229   2.337  1.00 85.95           C  
ANISOU 5628  CE  LYS C 128    10376  10637  11641    830   -418  -1211       C  
ATOM   5629  NZ  LYS C 128     -21.099  30.457   2.577  1.00 87.16           N  
ANISOU 5629  NZ  LYS C 128    10492  10781  11843    828   -420  -1278       N  
ATOM   5630  N   GLY C 129     -16.918  33.131   7.671  1.00 68.06           N  
ANISOU 5630  N   GLY C 129     8092   8398   9368    663   -225  -1145       N  
ATOM   5631  CA  GLY C 129     -17.586  33.013   8.979  1.00 67.22           C  
ANISOU 5631  CA  GLY C 129     7947   8293   9298    625   -189  -1198       C  
ATOM   5632  C   GLY C 129     -16.944  33.631  10.222  1.00 65.49           C  
ANISOU 5632  C   GLY C 129     7726   8082   9075    584   -151  -1187       C  
ATOM   5633  O   GLY C 129     -16.248  34.646  10.143  1.00 63.54           O  
ANISOU 5633  O   GLY C 129     7497   7825   8820    590   -163  -1152       O  
ATOM   5634  N   HIS C 130     -17.184  32.988  11.369  1.00 66.04           N  
ANISOU 5634  N   HIS C 130     7773   8169   9148    541   -107  -1217       N  
ATOM   5635  CA  HIS C 130     -16.845  33.496  12.711  1.00 68.12           C  
ANISOU 5635  CA  HIS C 130     8026   8442   9412    495    -69  -1224       C  
ATOM   5636  C   HIS C 130     -15.837  32.617  13.422  1.00 65.83           C  
ANISOU 5636  C   HIS C 130     7757   8181   9072    455    -28  -1179       C  
ATOM   5637  O   HIS C 130     -16.064  31.419  13.607  1.00 64.07           O  
ANISOU 5637  O   HIS C 130     7530   7973   8838    437    -11  -1186       O  
ATOM   5638  CB  HIS C 130     -18.136  33.635  13.538  1.00 71.98           C  
ANISOU 5638  CB  HIS C 130     8466   8930   9951    473    -52  -1305       C  
ATOM   5639  CG  HIS C 130     -17.921  33.911  15.018  1.00 75.16           C  
ANISOU 5639  CG  HIS C 130     8854   9352  10348    418     -5  -1322       C  
ATOM   5640  ND1 HIS C 130     -18.289  35.069  15.600  1.00 80.16           N  
ANISOU 5640  ND1 HIS C 130     9464   9975  11018    412     -3  -1365       N  
ATOM   5641  CD2 HIS C 130     -17.388  33.115  16.035  1.00 74.54           C  
ANISOU 5641  CD2 HIS C 130     8784   9306  10231    364     40  -1303       C  
ATOM   5642  CE1 HIS C 130     -17.995  35.027  16.915  1.00 77.48           C  
ANISOU 5642  CE1 HIS C 130     9116   9661  10658    357     43  -1375       C  
ATOM   5643  NE2 HIS C 130     -17.441  33.832  17.179  1.00 76.73           N  
ANISOU 5643  NE2 HIS C 130     9042   9593  10516    326     69  -1334       N  
ATOM   5644  N   TYR C 131     -14.733  33.224  13.858  1.00 63.39           N  
ANISOU 5644  N   TYR C 131     7470   7878   8736    438    -16  -1134       N  
ATOM   5645  CA  TYR C 131     -13.620  32.510  14.484  1.00 61.13           C  
ANISOU 5645  CA  TYR C 131     7206   7616   8402    403     15  -1085       C  
ATOM   5646  C   TYR C 131     -13.364  32.901  15.935  1.00 60.70           C  
ANISOU 5646  C   TYR C 131     7142   7576   8343    348     52  -1094       C  
ATOM   5647  O   TYR C 131     -13.286  34.082  16.265  1.00 63.04           O  
ANISOU 5647  O   TYR C 131     7434   7863   8656    346     49  -1104       O  
ATOM   5648  CB  TYR C 131     -12.347  32.765  13.696  1.00 60.53           C  
ANISOU 5648  CB  TYR C 131     7167   7540   8290    429     -1  -1014       C  
ATOM   5649  CG  TYR C 131     -12.311  32.100  12.356  1.00 61.25           C  
ANISOU 5649  CG  TYR C 131     7273   7629   8368    473    -28   -995       C  
ATOM   5650  CD1 TYR C 131     -12.989  32.641  11.268  1.00 61.18           C  
ANISOU 5650  CD1 TYR C 131     7263   7601   8382    518    -68  -1014       C  
ATOM   5651  CD2 TYR C 131     -11.580  30.932  12.166  1.00 61.89           C  
ANISOU 5651  CD2 TYR C 131     7372   7727   8414    471    -16   -959       C  
ATOM   5652  CE1 TYR C 131     -12.946  32.027  10.029  1.00 62.68           C  
ANISOU 5652  CE1 TYR C 131     7469   7793   8554    556    -93   -997       C  
ATOM   5653  CE2 TYR C 131     -11.528  30.314  10.932  1.00 59.66           C  
ANISOU 5653  CE2 TYR C 131     7103   7445   8117    512    -40   -947       C  
ATOM   5654  CZ  TYR C 131     -12.213  30.864   9.872  1.00 60.42           C  
ANISOU 5654  CZ  TYR C 131     7198   7526   8230    554    -77   -966       C  
ATOM   5655  OH  TYR C 131     -12.166  30.244   8.655  1.00 62.56           O  
ANISOU 5655  OH  TYR C 131     7484   7801   8482    592   -101   -956       O  
ATOM   5656  N   ARG C 132     -13.210  31.897  16.788  1.00 62.00           N  
ANISOU 5656  N   ARG C 132     7306   7764   8485    304     84  -1088       N  
ATOM   5657  CA  ARG C 132     -12.849  32.098  18.186  1.00 66.28           C  
ANISOU 5657  CA  ARG C 132     7844   8326   9011    246    120  -1089       C  
ATOM   5658  C   ARG C 132     -11.505  31.412  18.423  1.00 67.60           C  
ANISOU 5658  C   ARG C 132     8044   8508   9132    225    130  -1017       C  
ATOM   5659  O   ARG C 132     -11.245  30.341  17.873  1.00 68.16           O  
ANISOU 5659  O   ARG C 132     8128   8580   9189    239    122   -989       O  
ATOM   5660  CB  ARG C 132     -13.918  31.495  19.104  1.00 70.33           C  
ANISOU 5660  CB  ARG C 132     8326   8857   9538    201    149  -1146       C  
ATOM   5661  CG  ARG C 132     -13.915  31.988  20.547  1.00 78.04           C  
ANISOU 5661  CG  ARG C 132     9289   9856  10506    142    186  -1170       C  
ATOM   5662  CD  ARG C 132     -14.817  33.205  20.754  1.00 85.82           C  
ANISOU 5662  CD  ARG C 132    10241  10832  11535    151    186  -1241       C  
ATOM   5663  NE  ARG C 132     -16.199  32.968  20.323  1.00 90.22           N  
ANISOU 5663  NE  ARG C 132    10762  11381  12135    171    178  -1305       N  
ATOM   5664  CZ  ARG C 132     -17.203  32.609  21.123  1.00 91.10           C  
ANISOU 5664  CZ  ARG C 132    10836  11515  12260    130    208  -1365       C  
ATOM   5665  NH1 ARG C 132     -17.010  32.443  22.425  1.00 95.29           N  
ANISOU 5665  NH1 ARG C 132    11364  12080  12760     64    250  -1371       N  
ATOM   5666  NH2 ARG C 132     -18.413  32.419  20.617  1.00 92.09           N  
ANISOU 5666  NH2 ARG C 132    10929  11631  12429    154    197  -1421       N  
ATOM   5667  N   CYS C 133     -10.647  32.038  19.225  1.00 67.01           N  
ANISOU 5667  N   CYS C 133     7980   8442   9035    194    146   -990       N  
ATOM   5668  CA  CYS C 133      -9.357  31.458  19.578  1.00 61.37           C  
ANISOU 5668  CA  CYS C 133     7293   7742   8281    171    155   -924       C  
ATOM   5669  C   CYS C 133      -8.934  31.897  20.968  1.00 56.61           C  
ANISOU 5669  C   CYS C 133     6690   7158   7659    112    182   -922       C  
ATOM   5670  O   CYS C 133      -8.592  33.060  21.166  1.00 58.38           O  
ANISOU 5670  O   CYS C 133     6916   7376   7887    113    180   -922       O  
ATOM   5671  CB  CYS C 133      -8.282  31.863  18.558  1.00 66.48           C  
ANISOU 5671  CB  CYS C 133     7966   8379   8915    216    130   -869       C  
ATOM   5672  SG  CYS C 133      -6.584  31.439  19.045  1.00 73.77           S  
ANISOU 5672  SG  CYS C 133     8915   9318   9794    189    140   -790       S  
ATOM   5673  N   VAL C 134      -8.959  30.982  21.931  1.00 51.06           N  
ANISOU 5673  N   VAL C 134     5987   6476   6936     59    205   -918       N  
ATOM   5674  CA  VAL C 134      -8.358  31.283  23.235  1.00 51.55           C  
ANISOU 5674  CA  VAL C 134     6056   6559   6970      0    228   -903       C  
ATOM   5675  C   VAL C 134      -6.889  30.883  23.270  1.00 48.71           C  
ANISOU 5675  C   VAL C 134     5726   6203   6579     -5    219   -825       C  
ATOM   5676  O   VAL C 134      -6.556  29.698  23.270  1.00 45.01           O  
ANISOU 5676  O   VAL C 134     5268   5738   6096    -15    216   -791       O  
ATOM   5677  CB  VAL C 134      -9.124  30.710  24.459  1.00 52.39           C  
ANISOU 5677  CB  VAL C 134     6145   6692   7065    -65    259   -940       C  
ATOM   5678  CG1 VAL C 134     -10.260  31.630  24.859  1.00 54.87           C  
ANISOU 5678  CG1 VAL C 134     6427   7013   7406    -74    276  -1020       C  
ATOM   5679  CG2 VAL C 134      -9.664  29.323  24.188  1.00 56.55           C  
ANISOU 5679  CG2 VAL C 134     6669   7220   7596    -69    256   -939       C  
ATOM   5680  N   ALA C 135      -6.025  31.900  23.283  1.00 49.08           N  
ANISOU 5680  N   ALA C 135     5784   6245   6618      2    213   -799       N  
ATOM   5681  CA  ALA C 135      -4.579  31.728  23.404  1.00 45.15           C  
ANISOU 5681  CA  ALA C 135     5310   5751   6092     -5    207   -729       C  
ATOM   5682  C   ALA C 135      -4.155  31.781  24.871  1.00 44.30           C  
ANISOU 5682  C   ALA C 135     5209   5667   5956    -74    227   -718       C  
ATOM   5683  O   ALA C 135      -4.120  32.841  25.485  1.00 45.25           O  
ANISOU 5683  O   ALA C 135     5325   5792   6075    -96    236   -738       O  
ATOM   5684  CB  ALA C 135      -3.850  32.786  22.591  1.00 42.77           C  
ANISOU 5684  CB  ALA C 135     5017   5434   5796     37    188   -703       C  
ATOM   5685  N   GLU C 136      -3.843  30.619  25.425  1.00 43.54           N  
ANISOU 5685  N   GLU C 136     5121   5582   5838   -111    230   -687       N  
ATOM   5686  CA  GLU C 136      -3.404  30.517  26.799  1.00 43.77           C  
ANISOU 5686  CA  GLU C 136     5159   5634   5835   -180    245   -669       C  
ATOM   5687  C   GLU C 136      -1.868  30.401  26.824  1.00 42.07           C  
ANISOU 5687  C   GLU C 136     4965   5417   5601   -180    228   -595       C  
ATOM   5688  O   GLU C 136      -1.304  29.445  26.295  1.00 39.51           O  
ANISOU 5688  O   GLU C 136     4651   5084   5278   -159    211   -552       O  
ATOM   5689  CB  GLU C 136      -4.074  29.301  27.433  1.00 45.91           C  
ANISOU 5689  CB  GLU C 136     5427   5920   6095   -226    256   -679       C  
ATOM   5690  CG  GLU C 136      -4.191  29.351  28.943  1.00 49.97           C  
ANISOU 5690  CG  GLU C 136     5943   6465   6576   -308    278   -688       C  
ATOM   5691  CD  GLU C 136      -5.150  28.303  29.497  1.00 53.21           C  
ANISOU 5691  CD  GLU C 136     6345   6892   6979   -354    292   -710       C  
ATOM   5692  OE1 GLU C 136      -5.013  27.108  29.143  1.00 51.48           O  
ANISOU 5692  OE1 GLU C 136     6135   6660   6764   -348    275   -675       O  
ATOM   5693  OE2 GLU C 136      -6.040  28.681  30.300  1.00 57.60           O  
ANISOU 5693  OE2 GLU C 136     6884   7474   7525   -399    321   -765       O  
ATOM   5694  N   ALA C 137      -1.201  31.393  27.410  1.00 41.54           N  
ANISOU 5694  N   ALA C 137     4905   5358   5520   -202    231   -584       N  
ATOM   5695  CA  ALA C 137       0.258  31.419  27.476  1.00 39.67           C  
ANISOU 5695  CA  ALA C 137     4685   5120   5268   -204    216   -516       C  
ATOM   5696  C   ALA C 137       0.730  30.686  28.714  1.00 40.10           C  
ANISOU 5696  C   ALA C 137     4752   5192   5290   -271    218   -484       C  
ATOM   5697  O   ALA C 137       0.430  31.093  29.829  1.00 41.23           O  
ANISOU 5697  O   ALA C 137     4896   5356   5412   -327    234   -508       O  
ATOM   5698  CB  ALA C 137       0.756  32.846  27.495  1.00 39.16           C  
ANISOU 5698  CB  ALA C 137     4621   5051   5205   -196    215   -518       C  
ATOM   5699  N   ILE C 138       1.464  29.596  28.515  1.00 40.77           N  
ANISOU 5699  N   ILE C 138     4846   5270   5372   -265    199   -430       N  
ATOM   5700  CA  ILE C 138       1.892  28.754  29.625  1.00 41.58           C  
ANISOU 5700  CA  ILE C 138     4962   5386   5449   -328    193   -393       C  
ATOM   5701  C   ILE C 138       3.400  28.783  29.766  1.00 43.45           C  
ANISOU 5701  C   ILE C 138     5211   5619   5677   -329    171   -327       C  
ATOM   5702  O   ILE C 138       4.116  28.644  28.771  1.00 45.74           O  
ANISOU 5702  O   ILE C 138     5497   5893   5987   -274    155   -298       O  
ATOM   5703  CB  ILE C 138       1.413  27.291  29.465  1.00 41.20           C  
ANISOU 5703  CB  ILE C 138     4915   5329   5410   -330    183   -386       C  
ATOM   5704  CG1 ILE C 138      -0.057  27.149  29.888  1.00 41.10           C  
ANISOU 5704  CG1 ILE C 138     4892   5330   5393   -363    207   -446       C  
ATOM   5705  CG2 ILE C 138       2.242  26.354  30.330  1.00 41.94           C  
ANISOU 5705  CG2 ILE C 138     5024   5425   5484   -380    162   -326       C  
ATOM   5706  CD1 ILE C 138      -1.071  27.406  28.798  1.00 39.23           C  
ANISOU 5706  CD1 ILE C 138     4636   5081   5188   -305    216   -500       C  
ATOM   5707  N   ALA C 139       3.862  28.986  31.000  1.00 43.07           N  
ANISOU 5707  N   ALA C 139     5174   5589   5598   -393    171   -307       N  
ATOM   5708  CA  ALA C 139       5.268  28.834  31.360  1.00 43.83           C  
ANISOU 5708  CA  ALA C 139     5282   5685   5686   -407    147   -241       C  
ATOM   5709  C   ALA C 139       5.583  27.351  31.531  1.00 47.25           C  
ANISOU 5709  C   ALA C 139     5723   6108   6122   -422    122   -197       C  
ATOM   5710  O   ALA C 139       5.271  26.755  32.573  1.00 50.28           O  
ANISOU 5710  O   ALA C 139     6118   6504   6481   -486    119   -189       O  
ATOM   5711  CB  ALA C 139       5.572  29.590  32.643  1.00 41.95           C  
ANISOU 5711  CB  ALA C 139     5055   5470   5413   -474    153   -238       C  
ATOM   5712  N   GLY C 140       6.208  26.765  30.510  1.00 46.43           N  
ANISOU 5712  N   GLY C 140     5611   5981   6048   -363    102   -168       N  
ATOM   5713  CA  GLY C 140       6.476  25.326  30.457  1.00 47.28           C  
ANISOU 5713  CA  GLY C 140     5722   6071   6170   -363     74   -133       C  
ATOM   5714  C   GLY C 140       7.051  24.657  31.695  1.00 48.98           C  
ANISOU 5714  C   GLY C 140     5954   6290   6366   -431     49    -83       C  
ATOM   5715  O   GLY C 140       6.692  23.522  32.001  1.00 52.70           O  
ANISOU 5715  O   GLY C 140     6431   6750   6840   -456     32    -70       O  
ATOM   5716  N   ASP C 141       7.935  25.347  32.410  1.00 51.51           N  
ANISOU 5716  N   ASP C 141     6282   6624   6665   -463     43    -53       N  
ATOM   5717  CA  ASP C 141       8.630  24.756  33.570  1.00 57.00           C  
ANISOU 5717  CA  ASP C 141     6993   7322   7340   -527     13      0       C  
ATOM   5718  C   ASP C 141       7.724  24.501  34.778  1.00 60.05           C  
ANISOU 5718  C   ASP C 141     7398   7731   7687   -610     22    -12       C  
ATOM   5719  O   ASP C 141       7.747  23.414  35.359  1.00 60.69           O  
ANISOU 5719  O   ASP C 141     7491   7803   7763   -651     -4     22       O  
ATOM   5720  CB  ASP C 141       9.860  25.592  33.985  1.00 56.90           C  
ANISOU 5720  CB  ASP C 141     6983   7319   7317   -539      2     36       C  
ATOM   5721  CG  ASP C 141       9.561  27.086  34.095  1.00 57.85           C  
ANISOU 5721  CG  ASP C 141     7101   7461   7415   -544     36     -5       C  
ATOM   5722  OD1 ASP C 141       8.701  27.598  33.342  1.00 57.11           O  
ANISOU 5722  OD1 ASP C 141     6996   7368   7333   -505     65    -58       O  
ATOM   5723  OD2 ASP C 141      10.204  27.756  34.933  1.00 58.45           O  
ANISOU 5723  OD2 ASP C 141     7187   7554   7467   -586     30     13       O  
ATOM   5724  N   THR C 142       6.926  25.506  35.132  1.00 60.96           N  
ANISOU 5724  N   THR C 142     7513   7874   7775   -634     60    -65       N  
ATOM   5725  CA  THR C 142       6.067  25.465  36.309  1.00 60.04           C  
ANISOU 5725  CA  THR C 142     7410   7789   7614   -715     78    -88       C  
ATOM   5726  C   THR C 142       4.631  25.108  35.938  1.00 62.47           C  
ANISOU 5726  C   THR C 142     7706   8099   7929   -708    106   -143       C  
ATOM   5727  O   THR C 142       3.785  24.898  36.813  1.00 65.81           O  
ANISOU 5727  O   THR C 142     8136   8548   8318   -774    123   -165       O  
ATOM   5728  CB  THR C 142       6.053  26.835  37.011  1.00 58.44           C  
ANISOU 5728  CB  THR C 142     7209   7617   7376   -749    105   -120       C  
ATOM   5729  OG1 THR C 142       5.661  27.841  36.071  1.00 55.60           O  
ANISOU 5729  OG1 THR C 142     6830   7251   7042   -685    132   -174       O  
ATOM   5730  CG2 THR C 142       7.429  27.179  37.571  1.00 56.94           C  
ANISOU 5730  CG2 THR C 142     7031   7429   7172   -770     77    -65       C  
ATOM   5731  N   GLU C 143       4.362  25.067  34.635  1.00 63.87           N  
ANISOU 5731  N   GLU C 143     7866   8251   8149   -629    110   -168       N  
ATOM   5732  CA  GLU C 143       3.012  24.859  34.090  1.00 62.69           C  
ANISOU 5732  CA  GLU C 143     7702   8100   8014   -608    135   -226       C  
ATOM   5733  C   GLU C 143       1.993  25.918  34.531  1.00 58.12           C  
ANISOU 5733  C   GLU C 143     7114   7554   7414   -635    178   -296       C  
ATOM   5734  O   GLU C 143       0.788  25.701  34.428  1.00 55.94           O  
ANISOU 5734  O   GLU C 143     6826   7286   7142   -641    200   -345       O  
ATOM   5735  CB  GLU C 143       2.513  23.437  34.369  1.00 67.18           C  
ANISOU 5735  CB  GLU C 143     8278   8661   8585   -643    118   -206       C  
ATOM   5736  CG  GLU C 143       3.209  22.372  33.529  1.00 75.78           C  
ANISOU 5736  CG  GLU C 143     9368   9709   9715   -592     78   -160       C  
ATOM   5737  CD  GLU C 143       2.626  22.245  32.129  1.00 79.72           C  
ANISOU 5737  CD  GLU C 143     9847  10185  10256   -511     86   -201       C  
ATOM   5738  OE1 GLU C 143       3.351  22.532  31.147  1.00 78.05           O  
ANISOU 5738  OE1 GLU C 143     9627   9957  10071   -442     77   -192       O  
ATOM   5739  OE2 GLU C 143       1.439  21.860  32.012  1.00 81.35           O  
ANISOU 5739  OE2 GLU C 143    10047  10394  10467   -520    102   -241       O  
ATOM   5740  N   GLU C 144       2.493  27.062  35.000  1.00 57.89           N  
ANISOU 5740  N   GLU C 144     7087   7541   7364   -649    188   -302       N  
ATOM   5741  CA  GLU C 144       1.655  28.206  35.368  1.00 59.28           C  
ANISOU 5741  CA  GLU C 144     7253   7745   7527   -666    226   -372       C  
ATOM   5742  C   GLU C 144       1.147  28.926  34.131  1.00 55.95           C  
ANISOU 5742  C   GLU C 144     6809   7301   7147   -586    238   -421       C  
ATOM   5743  O   GLU C 144       1.809  28.952  33.099  1.00 58.16           O  
ANISOU 5743  O   GLU C 144     7087   7553   7457   -522    218   -392       O  
ATOM   5744  CB  GLU C 144       2.424  29.208  36.246  1.00 63.93           C  
ANISOU 5744  CB  GLU C 144     7853   8354   8084   -705    227   -363       C  
ATOM   5745  CG  GLU C 144       2.994  28.658  37.551  1.00 69.38           C  
ANISOU 5745  CG  GLU C 144     8567   9068   8726   -789    213   -314       C  
ATOM   5746  CD  GLU C 144       1.966  28.464  38.653  1.00 72.35           C  
ANISOU 5746  CD  GLU C 144     8944   9486   9058   -869    242   -354       C  
ATOM   5747  OE1 GLU C 144       0.894  27.884  38.389  1.00 73.18           O  
ANISOU 5747  OE1 GLU C 144     9038   9594   9174   -868    259   -388       O  
ATOM   5748  OE2 GLU C 144       2.245  28.875  39.801  1.00 77.09           O  
ANISOU 5748  OE2 GLU C 144     9559  10120   9611   -937    248   -352       O  
ATOM   5749  N   LYS C 145      -0.034  29.515  34.240  1.00 54.61           N  
ANISOU 5749  N   LYS C 145     6621   7147   6978   -593    270   -494       N  
ATOM   5750  CA  LYS C 145      -0.585  30.309  33.159  1.00 55.04           C  
ANISOU 5750  CA  LYS C 145     6656   7182   7074   -523    278   -543       C  
ATOM   5751  C   LYS C 145      -0.110  31.747  33.296  1.00 54.20           C  
ANISOU 5751  C   LYS C 145     6548   7076   6968   -513    282   -559       C  
ATOM   5752  O   LYS C 145      -0.263  32.359  34.357  1.00 55.78           O  
ANISOU 5752  O   LYS C 145     6748   7303   7139   -568    300   -589       O  
ATOM   5753  CB  LYS C 145      -2.114  30.242  33.170  1.00 59.14           C  
ANISOU 5753  CB  LYS C 145     7152   7713   7603   -530    306   -617       C  
ATOM   5754  CG  LYS C 145      -2.657  28.825  33.141  1.00 61.06           C  
ANISOU 5754  CG  LYS C 145     7397   7958   7845   -549    303   -603       C  
ATOM   5755  CD  LYS C 145      -4.172  28.795  33.128  1.00 62.27           C  
ANISOU 5755  CD  LYS C 145     7524   8125   8011   -556    331   -678       C  
ATOM   5756  CE  LYS C 145      -4.660  27.362  32.982  1.00 65.40           C  
ANISOU 5756  CE  LYS C 145     7921   8516   8411   -570    323   -659       C  
ATOM   5757  NZ  LYS C 145      -6.138  27.276  32.801  1.00 70.83           N  
ANISOU 5757  NZ  LYS C 145     8580   9214   9118   -570    348   -731       N  
ATOM   5758  N   LEU C 146       0.475  32.270  32.224  1.00 51.89           N  
ANISOU 5758  N   LEU C 146     6254   6754   6706   -447    264   -540       N  
ATOM   5759  CA  LEU C 146       0.980  33.643  32.189  1.00 52.18           C  
ANISOU 5759  CA  LEU C 146     6290   6784   6750   -432    262   -549       C  
ATOM   5760  C   LEU C 146      -0.118  34.623  31.834  1.00 50.61           C  
ANISOU 5760  C   LEU C 146     6070   6578   6581   -404    278   -626       C  
ATOM   5761  O   LEU C 146      -0.401  35.543  32.586  1.00 54.82           O  
ANISOU 5761  O   LEU C 146     6597   7124   7106   -435    293   -672       O  
ATOM   5762  CB  LEU C 146       2.100  33.772  31.164  1.00 51.63           C  
ANISOU 5762  CB  LEU C 146     6228   6688   6701   -376    235   -491       C  
ATOM   5763  CG  LEU C 146       3.391  33.032  31.475  1.00 51.14           C  
ANISOU 5763  CG  LEU C 146     6182   6629   6617   -396    214   -414       C  
ATOM   5764  CD1 LEU C 146       4.083  32.683  30.170  1.00 50.14           C  
ANISOU 5764  CD1 LEU C 146     6054   6479   6517   -330    193   -370       C  
ATOM   5765  CD2 LEU C 146       4.278  33.878  32.371  1.00 49.98           C  
ANISOU 5765  CD2 LEU C 146     6046   6494   6449   -438    210   -393       C  
ATOM   5766  N   PHE C 147      -0.716  34.432  30.669  1.00 48.82           N  
ANISOU 5766  N   PHE C 147     5830   6328   6388   -344    272   -643       N  
ATOM   5767  CA  PHE C 147      -1.878  35.207  30.268  1.00 49.10           C  
ANISOU 5767  CA  PHE C 147     5844   6355   6457   -315    283   -717       C  
ATOM   5768  C   PHE C 147      -2.837  34.376  29.401  1.00 49.28           C  
ANISOU 5768  C   PHE C 147     5853   6367   6503   -278    283   -739       C  
ATOM   5769  O   PHE C 147      -2.566  33.216  29.094  1.00 49.84           O  
ANISOU 5769  O   PHE C 147     5933   6437   6565   -273    274   -696       O  
ATOM   5770  CB  PHE C 147      -1.456  36.519  29.597  1.00 47.10           C  
ANISOU 5770  CB  PHE C 147     5589   6073   6232   -270    265   -717       C  
ATOM   5771  CG  PHE C 147      -0.659  36.341  28.333  1.00 46.79           C  
ANISOU 5771  CG  PHE C 147     5561   6010   6207   -212    238   -657       C  
ATOM   5772  CD1 PHE C 147       0.727  36.403  28.358  1.00 45.32           C  
ANISOU 5772  CD1 PHE C 147     5393   5823   6003   -217    223   -589       C  
ATOM   5773  CD2 PHE C 147      -1.298  36.134  27.110  1.00 45.54           C  
ANISOU 5773  CD2 PHE C 147     5393   5831   6078   -154    228   -672       C  
ATOM   5774  CE1 PHE C 147       1.460  36.251  27.192  1.00 44.99           C  
ANISOU 5774  CE1 PHE C 147     5358   5764   5972   -166    203   -538       C  
ATOM   5775  CE2 PHE C 147      -0.569  35.985  25.943  1.00 43.51           C  
ANISOU 5775  CE2 PHE C 147     5145   5557   5828   -104    206   -620       C  
ATOM   5776  CZ  PHE C 147       0.810  36.045  25.984  1.00 43.44           C  
ANISOU 5776  CZ  PHE C 147     5152   5551   5800   -110    195   -554       C  
ATOM   5777  N   CYS C 148      -3.967  34.966  29.034  1.00 51.70           N  
ANISOU 5777  N   CYS C 148     6136   6665   6843   -251    290   -807       N  
ATOM   5778  CA  CYS C 148      -4.994  34.264  28.279  1.00 53.00           C  
ANISOU 5778  CA  CYS C 148     6285   6821   7032   -219    290   -837       C  
ATOM   5779  C   CYS C 148      -5.810  35.282  27.514  1.00 51.88           C  
ANISOU 5779  C   CYS C 148     6122   6655   6936   -168    282   -894       C  
ATOM   5780  O   CYS C 148      -6.361  36.207  28.110  1.00 52.03           O  
ANISOU 5780  O   CYS C 148     6122   6678   6967   -185    295   -953       O  
ATOM   5781  CB  CYS C 148      -5.889  33.451  29.215  1.00 57.82           C  
ANISOU 5781  CB  CYS C 148     6882   7463   7624   -277    319   -874       C  
ATOM   5782  SG  CYS C 148      -7.028  32.314  28.393  1.00 63.43           S  
ANISOU 5782  SG  CYS C 148     7575   8165   8359   -248    317   -899       S  
ATOM   5783  N   LEU C 149      -5.879  35.109  26.196  1.00 51.82           N  
ANISOU 5783  N   LEU C 149     6115   6620   6953   -106    258   -877       N  
ATOM   5784  CA  LEU C 149      -6.570  36.058  25.321  1.00 52.81           C  
ANISOU 5784  CA  LEU C 149     6223   6716   7123    -52    240   -919       C  
ATOM   5785  C   LEU C 149      -7.752  35.430  24.602  1.00 55.44           C  
ANISOU 5785  C   LEU C 149     6537   7042   7483    -21    237   -960       C  
ATOM   5786  O   LEU C 149      -7.637  34.343  24.030  1.00 55.85           O  
ANISOU 5786  O   LEU C 149     6599   7095   7525     -6    230   -927       O  
ATOM   5787  CB  LEU C 149      -5.598  36.664  24.306  1.00 49.65           C  
ANISOU 5787  CB  LEU C 149     5843   6290   6729     -5    209   -864       C  
ATOM   5788  CG  LEU C 149      -4.444  37.458  24.918  1.00 48.87           C  
ANISOU 5788  CG  LEU C 149     5761   6194   6611    -31    207   -826       C  
ATOM   5789  CD1 LEU C 149      -3.630  38.161  23.850  1.00 46.48           C  
ANISOU 5789  CD1 LEU C 149     5474   5866   6320     15    177   -777       C  
ATOM   5790  CD2 LEU C 149      -4.991  38.466  25.913  1.00 49.89           C  
ANISOU 5790  CD2 LEU C 149     5873   6326   6754    -63    222   -890       C  
ATOM   5791  N   ASN C 150      -8.890  36.118  24.652  1.00 57.61           N  
ANISOU 5791  N   ASN C 150     6782   7309   7796    -12    240  -1035       N  
ATOM   5792  CA  ASN C 150     -10.085  35.695  23.929  1.00 59.00           C  
ANISOU 5792  CA  ASN C 150     6935   7475   8006     21    233  -1080       C  
ATOM   5793  C   ASN C 150     -10.141  36.440  22.601  1.00 57.37           C  
ANISOU 5793  C   ASN C 150     6731   7230   7835     90    193  -1074       C  
ATOM   5794  O   ASN C 150     -10.605  37.577  22.533  1.00 59.47           O  
ANISOU 5794  O   ASN C 150     6981   7476   8139    108    180  -1117       O  
ATOM   5795  CB  ASN C 150     -11.350  35.936  24.770  1.00 62.15           C  
ANISOU 5795  CB  ASN C 150     7295   7890   8428     -9    260  -1168       C  
ATOM   5796  CG  ASN C 150     -12.516  35.043  24.358  1.00 64.82           C  
ANISOU 5796  CG  ASN C 150     7609   8231   8786      1    264  -1207       C  
ATOM   5797  OD1 ASN C 150     -12.769  34.844  23.169  1.00 68.64           O  
ANISOU 5797  OD1 ASN C 150     8094   8689   9294     55    234  -1197       O  
ATOM   5798  ND2 ASN C 150     -13.240  34.509  25.347  1.00 62.97           N  
ANISOU 5798  ND2 ASN C 150     7352   8031   8541    -53    300  -1252       N  
ATOM   5799  N   PHE C 151      -9.625  35.796  21.557  1.00 55.14           N  
ANISOU 5799  N   PHE C 151     6471   6939   7540    126    171  -1018       N  
ATOM   5800  CA  PHE C 151      -9.575  36.371  20.219  1.00 54.64           C  
ANISOU 5800  CA  PHE C 151     6416   6845   7500    187    132  -1001       C  
ATOM   5801  C   PHE C 151     -10.852  36.091  19.433  1.00 60.31           C  
ANISOU 5801  C   PHE C 151     7110   7548   8254    224    116  -1051       C  
ATOM   5802  O   PHE C 151     -11.547  35.090  19.669  1.00 59.91           O  
ANISOU 5802  O   PHE C 151     7046   7513   8203    208    133  -1079       O  
ATOM   5803  CB  PHE C 151      -8.382  35.818  19.441  1.00 52.67           C  
ANISOU 5803  CB  PHE C 151     6198   6597   7214    207    119   -921       C  
ATOM   5804  CG  PHE C 151      -7.103  36.577  19.651  1.00 51.01           C  
ANISOU 5804  CG  PHE C 151     6009   6386   6983    197    116   -868       C  
ATOM   5805  CD1 PHE C 151      -6.158  36.132  20.570  1.00 49.33           C  
ANISOU 5805  CD1 PHE C 151     5810   6197   6734    152    139   -830       C  
ATOM   5806  CD2 PHE C 151      -6.831  37.728  18.910  1.00 49.61           C  
ANISOU 5806  CD2 PHE C 151     5840   6183   6824    230     86   -851       C  
ATOM   5807  CE1 PHE C 151      -4.972  36.823  20.753  1.00 48.67           C  
ANISOU 5807  CE1 PHE C 151     5744   6112   6633    141    135   -780       C  
ATOM   5808  CE2 PHE C 151      -5.647  38.424  19.092  1.00 47.68           C  
ANISOU 5808  CE2 PHE C 151     5615   5939   6562    218     82   -800       C  
ATOM   5809  CZ  PHE C 151      -4.716  37.970  20.014  1.00 48.63           C  
ANISOU 5809  CZ  PHE C 151     5745   6083   6646    174    107   -766       C  
ATOM   5810  N   THR C 152     -11.145  36.984  18.492  1.00 61.47           N  
ANISOU 5810  N   THR C 152     7255   7664   8434    272     79  -1060       N  
ATOM   5811  CA  THR C 152     -12.307  36.858  17.630  1.00 61.60           C  
ANISOU 5811  CA  THR C 152     7252   7662   8489    312     55  -1103       C  
ATOM   5812  C   THR C 152     -11.967  37.404  16.244  1.00 60.56           C  
ANISOU 5812  C   THR C 152     7142   7503   8363    366      8  -1063       C  
ATOM   5813  O   THR C 152     -11.552  38.555  16.103  1.00 60.29           O  
ANISOU 5813  O   THR C 152     7116   7448   8341    377    -12  -1046       O  
ATOM   5814  CB  THR C 152     -13.536  37.573  18.245  1.00 66.57           C  
ANISOU 5814  CB  THR C 152     7840   8281   9171    305     59  -1190       C  
ATOM   5815  OG1 THR C 152     -13.873  36.954  19.495  1.00 66.54           O  
ANISOU 5815  OG1 THR C 152     7816   8310   9153    250    106  -1227       O  
ATOM   5816  CG2 THR C 152     -14.750  37.501  17.322  1.00 67.28           C  
ANISOU 5816  CG2 THR C 152     7906   8349   9306    349     28  -1235       C  
ATOM   5817  N   ILE C 153     -12.119  36.556  15.230  1.00 60.43           N  
ANISOU 5817  N   ILE C 153     7135   7489   8335    398     -7  -1045       N  
ATOM   5818  CA  ILE C 153     -11.901  36.951  13.839  1.00 58.62           C  
ANISOU 5818  CA  ILE C 153     6926   7240   8105    447    -51  -1009       C  
ATOM   5819  C   ILE C 153     -13.195  36.765  13.056  1.00 57.48           C  
ANISOU 5819  C   ILE C 153     6761   7078   7998    483    -80  -1059       C  
ATOM   5820  O   ILE C 153     -13.873  35.754  13.213  1.00 57.90           O  
ANISOU 5820  O   ILE C 153     6798   7144   8055    476    -64  -1092       O  
ATOM   5821  CB  ILE C 153     -10.790  36.112  13.163  1.00 59.82           C  
ANISOU 5821  CB  ILE C 153     7111   7413   8202    456    -47   -940       C  
ATOM   5822  CG1 ILE C 153      -9.501  36.104  13.995  1.00 63.47           C  
ANISOU 5822  CG1 ILE C 153     7590   7896   8628    418    -17   -891       C  
ATOM   5823  CG2 ILE C 153     -10.493  36.627  11.761  1.00 59.43           C  
ANISOU 5823  CG2 ILE C 153     7084   7351   8145    500    -90   -900       C  
ATOM   5824  CD1 ILE C 153      -9.296  34.855  14.828  1.00 64.32           C  
ANISOU 5824  CD1 ILE C 153     7694   8030   8712    382     20   -891       C  
ATOM   5825  N   ILE C 154     -13.540  37.749  12.232  0.50 56.22           N  
ANISOU 5825  N   ILE C 154     6603   6888   7870    520   -126  -1061       N  
ATOM   5826  CA  ILE C 154     -14.636  37.607  11.283  0.50 57.22           C  
ANISOU 5826  CA  ILE C 154     6716   6996   8028    559   -164  -1096       C  
ATOM   5827  C   ILE C 154     -14.053  37.771   9.883  0.50 57.67           C  
ANISOU 5827  C   ILE C 154     6809   7047   8055    596   -205  -1036       C  
ATOM   5828  O   ILE C 154     -13.457  38.802   9.572  0.50 56.92           O  
ANISOU 5828  O   ILE C 154     6732   6935   7958    603   -229   -996       O  
ATOM   5829  CB  ILE C 154     -15.770  38.625  11.551  0.50 58.77           C  
ANISOU 5829  CB  ILE C 154     6876   7158   8295    570   -189  -1164       C  
ATOM   5830  CG1 ILE C 154     -16.392  38.380  12.934  1.00 62.35           C  
ANISOU 5830  CG1 ILE C 154     7290   7625   8771    530   -142  -1230       C  
ATOM   5831  CG2 ILE C 154     -16.853  38.533  10.484  1.00 54.68           C  
ANISOU 5831  CG2 ILE C 154     6345   6617   7811    614   -236  -1194       C  
ATOM   5832  CD1 ILE C 154     -17.155  39.563  13.499  0.50 60.86           C  
ANISOU 5832  CD1 ILE C 154     7066   7408   8647    531   -155  -1293       C  
ATOM   5833  N   HIS C 155     -14.221  36.742   9.054  1.00 59.90           N  
ANISOU 5833  N   HIS C 155     7101   7345   8314    617   -211  -1029       N  
ATOM   5834  CA  HIS C 155     -13.620  36.694   7.718  1.00 65.18           C  
ANISOU 5834  CA  HIS C 155     7803   8018   8942    648   -243   -973       C  
ATOM   5835  C   HIS C 155     -14.638  36.834   6.624  1.00 66.94           C  
ANISOU 5835  C   HIS C 155     8021   8219   9191    689   -295   -998       C  
ATOM   5836  O   HIS C 155     -15.662  36.147   6.631  1.00 65.38           O  
ANISOU 5836  O   HIS C 155     7799   8019   9021    697   -296  -1052       O  
ATOM   5837  CB  HIS C 155     -12.831  35.392   7.545  1.00 69.37           C  
ANISOU 5837  CB  HIS C 155     8352   8586   9417    642   -211   -941       C  
ATOM   5838  CG  HIS C 155     -12.006  35.325   6.271  1.00 73.38           C  
ANISOU 5838  CG  HIS C 155     8895   9109   9874    668   -232   -882       C  
ATOM   5839  ND1 HIS C 155     -12.196  34.375   5.334  1.00 75.73           N  
ANISOU 5839  ND1 HIS C 155     9202   9423  10148    694   -243   -885       N  
ATOM   5840  CD2 HIS C 155     -10.956  36.124   5.811  1.00 74.99           C  
ANISOU 5840  CD2 HIS C 155     9127   9319  10046    669   -243   -819       C  
ATOM   5841  CE1 HIS C 155     -11.319  34.555   4.324  1.00 77.06           C  
ANISOU 5841  CE1 HIS C 155     9401   9609  10268    710   -258   -830       C  
ATOM   5842  NE2 HIS C 155     -10.563  35.628   4.615  1.00 76.57           N  
ANISOU 5842  NE2 HIS C 155     9350   9541  10200    694   -257   -788       N  
TER    5843      HIS C 155                                                      
ATOM   5844  N   PRO B  27     -18.558 -37.811 -12.203  1.00114.26           N  
ANISOU 5844  N   PRO B  27    14453  14140  14820    114   -175    182       N  
ATOM   5845  CA  PRO B  27     -18.135 -37.559 -13.576  1.00113.21           C  
ANISOU 5845  CA  PRO B  27    14354  13993  14665    122   -188    173       C  
ATOM   5846  C   PRO B  27     -17.070 -36.455 -13.662  1.00110.96           C  
ANISOU 5846  C   PRO B  27    14076  13724  14358    137   -182    183       C  
ATOM   5847  O   PRO B  27     -15.873 -36.754 -13.692  1.00104.52           O  
ANISOU 5847  O   PRO B  27    13276  12908  13528    147   -159    198       O  
ATOM   5848  CB  PRO B  27     -19.438 -37.128 -14.271  1.00111.62           C  
ANISOU 5848  CB  PRO B  27    14151  13786  14471    112   -223    149       C  
ATOM   5849  CG  PRO B  27     -20.554 -37.633 -13.403  1.00110.67           C  
ANISOU 5849  CG  PRO B  27    14001  13668  14380     97   -226    145       C  
ATOM   5850  CD  PRO B  27     -19.977 -38.195 -12.129  1.00113.89           C  
ANISOU 5850  CD  PRO B  27    14390  14085  14797     98   -194    166       C  
ATOM   5851  N   CYS B  28     -17.516 -35.198 -13.691  1.00111.58           N  
ANISOU 5851  N   CYS B  28    14144  13818  14434    138   -202    176       N  
ATOM   5852  CA  CYS B  28     -16.639 -34.032 -13.796  1.00109.27           C  
ANISOU 5852  CA  CYS B  28    13856  13540  14121    151   -198    184       C  
ATOM   5853  C   CYS B  28     -16.811 -33.114 -12.589  1.00109.95           C  
ANISOU 5853  C   CYS B  28    13907  13652  14216    150   -195    191       C  
ATOM   5854  O   CYS B  28     -17.002 -33.580 -11.464  1.00113.74           O  
ANISOU 5854  O   CYS B  28    14362  14141  14712    143   -182    200       O  
ATOM   5855  CB  CYS B  28     -16.969 -33.246 -15.066  1.00111.85           C  
ANISOU 5855  CB  CYS B  28    14205  13859  14433    155   -225    168       C  
ATOM   5856  SG  CYS B  28     -16.487 -34.045 -16.607  1.00122.72           S  
ANISOU 5856  SG  CYS B  28    15627  15206  15791    161   -228    160       S  
ATOM   5857  N   ILE B  29     -16.719 -31.808 -12.836  1.00105.57           N  
ANISOU 5857  N   ILE B  29    13352  13109  13649    156   -207    188       N  
ATOM   5858  CA  ILE B  29     -17.087 -30.786 -11.860  1.00 97.86           C  
ANISOU 5858  CA  ILE B  29    12344  12156  12681    154   -210    191       C  
ATOM   5859  C   ILE B  29     -18.052 -29.809 -12.534  1.00 95.71           C  
ANISOU 5859  C   ILE B  29    12073  11883  12408    153   -241    173       C  
ATOM   5860  O   ILE B  29     -17.891 -29.465 -13.707  1.00 91.02           O  
ANISOU 5860  O   ILE B  29    11505  11278  11798    160   -254    165       O  
ATOM   5861  CB  ILE B  29     -15.864 -30.026 -11.300  1.00 96.63           C  
ANISOU 5861  CB  ILE B  29    12184  12018  12510    165   -190    207       C  
ATOM   5862  CG1 ILE B  29     -14.762 -30.997 -10.852  1.00 96.25           C  
ANISOU 5862  CG1 ILE B  29    12140  11969  12459    169   -161    224       C  
ATOM   5863  CG2 ILE B  29     -16.281 -29.139 -10.133  1.00 98.68           C  
ANISOU 5863  CG2 ILE B  29    12410  12302  12781    161   -191    210       C  
ATOM   5864  CD1 ILE B  29     -13.409 -30.347 -10.628  1.00 94.58           C  
ANISOU 5864  CD1 ILE B  29    11932  11772  12230    181   -142    239       C  
ATOM   5865  N   GLU B  30     -19.056 -29.373 -11.781  1.00 97.03           N  
ANISOU 5865  N   GLU B  30    12210  12061  12592    145   -251    169       N  
ATOM   5866  CA  GLU B  30     -20.108 -28.506 -12.295  1.00 98.16           C  
ANISOU 5866  CA  GLU B  30    12349  12205  12739    143   -280    153       C  
ATOM   5867  C   GLU B  30     -20.041 -27.117 -11.650  1.00103.14           C  
ANISOU 5867  C   GLU B  30    12961  12858  13367    147   -280    157       C  
ATOM   5868  O   GLU B  30     -20.409 -26.952 -10.482  1.00106.61           O  
ANISOU 5868  O   GLU B  30    13371  13313  13822    141   -273    162       O  
ATOM   5869  CB  GLU B  30     -21.465 -29.161 -12.029  1.00 97.90           C  
ANISOU 5869  CB  GLU B  30    12298  12166  12731    128   -294    142       C  
ATOM   5870  CG  GLU B  30     -22.680 -28.393 -12.526  1.00 98.40           C  
ANISOU 5870  CG  GLU B  30    12354  12230  12801    125   -325    126       C  
ATOM   5871  CD  GLU B  30     -23.937 -29.247 -12.542  1.00 97.62           C  
ANISOU 5871  CD  GLU B  30    12244  12121  12726    111   -340    113       C  
ATOM   5872  OE1 GLU B  30     -23.822 -30.489 -12.643  1.00 96.18           O  
ANISOU 5872  OE1 GLU B  30    12071  11924  12549    105   -331    114       O  
ATOM   5873  OE2 GLU B  30     -25.044 -28.676 -12.457  1.00 94.76           O  
ANISOU 5873  OE2 GLU B  30    11862  11764  12376    106   -361    103       O  
ATOM   5874  N   VAL B  31     -19.562 -26.129 -12.406  1.00100.08           N  
ANISOU 5874  N   VAL B  31    12592  12472  12961    158   -287    155       N  
ATOM   5875  CA  VAL B  31     -19.522 -24.741 -11.923  1.00 93.04           C  
ANISOU 5875  CA  VAL B  31    11685  11599  12066    162   -288    157       C  
ATOM   5876  C   VAL B  31     -20.855 -24.035 -12.122  1.00 89.51           C  
ANISOU 5876  C   VAL B  31    11225  11154  11630    158   -315    143       C  
ATOM   5877  O   VAL B  31     -21.415 -23.496 -11.173  1.00 88.55           O  
ANISOU 5877  O   VAL B  31    11075  11047  11522    154   -315    144       O  
ATOM   5878  CB  VAL B  31     -18.392 -23.891 -12.554  1.00 90.93           C  
ANISOU 5878  CB  VAL B  31    11440  11333  11774    176   -281    162       C  
ATOM   5879  CG1 VAL B  31     -17.341 -23.543 -11.510  1.00 90.26           C  
ANISOU 5879  CG1 VAL B  31    11341  11266  11685    179   -255    178       C  
ATOM   5880  CG2 VAL B  31     -17.778 -24.583 -13.763  1.00 91.54           C  
ANISOU 5880  CG2 VAL B  31    11554  11390  11836    182   -281    160       C  
ATOM   5881  N   VAL B  32     -21.349 -24.030 -13.356  1.00 88.01           N  
ANISOU 5881  N   VAL B  32    11057  10949  11434    161   -338    130       N  
ATOM   5882  CA  VAL B  32     -22.651 -23.448 -13.660  1.00 91.18           C  
ANISOU 5882  CA  VAL B  32    11447  11350  11845    158   -366    115       C  
ATOM   5883  C   VAL B  32     -23.520 -24.508 -14.333  1.00 96.34           C  
ANISOU 5883  C   VAL B  32    12108  11986  12508    149   -384    103       C  
ATOM   5884  O   VAL B  32     -23.175 -24.985 -15.416  1.00 98.63           O  
ANISOU 5884  O   VAL B  32    12428  12260  12784    153   -390     98       O  
ATOM   5885  CB  VAL B  32     -22.542 -22.204 -14.570  1.00 89.09           C  
ANISOU 5885  CB  VAL B  32    11200  11086  11562    170   -380    110       C  
ATOM   5886  CG1 VAL B  32     -23.891 -21.500 -14.672  1.00 86.54           C  
ANISOU 5886  CG1 VAL B  32    10861  10767  11251    167   -406     98       C  
ATOM   5887  CG2 VAL B  32     -21.478 -21.243 -14.058  1.00 86.22           C  
ANISOU 5887  CG2 VAL B  32    10835  10737  11186    178   -360    122       C  
ATOM   5888  N   PRO B  33     -24.643 -24.891 -13.687  1.00100.29           N  
ANISOU 5888  N   PRO B  33    12581  12489  13033    137   -392     97       N  
ATOM   5889  CA  PRO B  33     -25.541 -25.924 -14.222  1.00102.25           C  
ANISOU 5889  CA  PRO B  33    12833  12722  13294    127   -409     84       C  
ATOM   5890  C   PRO B  33     -26.023 -25.614 -15.640  1.00101.82           C  
ANISOU 5890  C   PRO B  33    12802  12656  13228    132   -439     69       C  
ATOM   5891  O   PRO B  33     -26.309 -24.455 -15.954  1.00101.81           O  
ANISOU 5891  O   PRO B  33    12800  12662  13220    140   -453     65       O  
ATOM   5892  CB  PRO B  33     -26.718 -25.910 -13.238  1.00102.23           C  
ANISOU 5892  CB  PRO B  33    12793  12729  13320    115   -415     82       C  
ATOM   5893  CG  PRO B  33     -26.126 -25.418 -11.961  1.00100.06           C  
ANISOU 5893  CG  PRO B  33    12497  12473  13048    117   -390     97       C  
ATOM   5894  CD  PRO B  33     -25.102 -24.398 -12.373  1.00100.28           C  
ANISOU 5894  CD  PRO B  33    12544  12506  13050    132   -384    103       C  
ATOM   5895  N   ASN B  34     -26.087 -26.648 -16.480  1.00103.02           N  
ANISOU 5895  N   ASN B  34    12976  12789  13377    128   -446     60       N  
ATOM   5896  CA  ASN B  34     -26.489 -26.531 -17.895  1.00107.45           C  
ANISOU 5896  CA  ASN B  34    13562  13337  13925    132   -474     45       C  
ATOM   5897  C   ASN B  34     -25.622 -25.599 -18.767  1.00104.88           C  
ANISOU 5897  C   ASN B  34    13267  13011  13570    150   -475     48       C  
ATOM   5898  O   ASN B  34     -25.942 -25.377 -19.939  1.00 98.89           O  
ANISOU 5898  O   ASN B  34    12530  12243  12798    155   -498     36       O  
ATOM   5899  CB  ASN B  34     -27.980 -26.148 -18.024  1.00110.74           C  
ANISOU 5899  CB  ASN B  34    13959  13757  14358    126   -505     30       C  
ATOM   5900  CG  ASN B  34     -28.924 -27.251 -17.563  1.00113.72           C  
ANISOU 5900  CG  ASN B  34    14315  14128  14764    108   -510     23       C  
ATOM   5901  OD1 ASN B  34     -28.818 -28.403 -17.988  1.00116.33           O  
ANISOU 5901  OD1 ASN B  34    14661  14442  15094    101   -508     18       O  
ATOM   5902  ND2 ASN B  34     -29.874 -26.890 -16.705  1.00112.50           N  
ANISOU 5902  ND2 ASN B  34    14125  13986  14632    101   -515     22       N  
ATOM   5903  N   ILE B  35     -24.534 -25.067 -18.202  1.00104.76           N  
ANISOU 5903  N   ILE B  35    13251  13006  13544    158   -450     63       N  
ATOM   5904  CA  ILE B  35     -23.723 -24.033 -18.873  1.00102.27           C  
ANISOU 5904  CA  ILE B  35    12959  12693  13204    174   -448     67       C  
ATOM   5905  C   ILE B  35     -22.199 -24.298 -18.887  1.00 98.50           C  
ANISOU 5905  C   ILE B  35    12503  12213  12710    182   -419     81       C  
ATOM   5906  O   ILE B  35     -21.591 -24.302 -19.960  1.00 96.56           O  
ANISOU 5906  O   ILE B  35    12290  11954  12442    192   -421     80       O  
ATOM   5907  CB  ILE B  35     -24.056 -22.606 -18.339  1.00106.82           C  
ANISOU 5907  CB  ILE B  35    13514  13288  13784    179   -453     70       C  
ATOM   5908  CG1 ILE B  35     -25.479 -22.189 -18.751  1.00106.65           C  
ANISOU 5908  CG1 ILE B  35    13481  13267  13772    176   -485     55       C  
ATOM   5909  CG2 ILE B  35     -23.040 -21.573 -18.823  1.00107.16           C  
ANISOU 5909  CG2 ILE B  35    13579  13334  13802    195   -444     77       C  
ATOM   5910  CD1 ILE B  35     -25.930 -20.832 -18.239  1.00102.69           C  
ANISOU 5910  CD1 ILE B  35    12957  12782  13276    181   -491     56       C  
ATOM   5911  N   THR B  36     -21.586 -24.512 -17.719  1.00 95.84           N  
ANISOU 5911  N   THR B  36    12146  11886  12380    178   -393     96       N  
ATOM   5912  CA  THR B  36     -20.116 -24.630 -17.628  1.00 94.38           C  
ANISOU 5912  CA  THR B  36    11978  11701  12180    186   -365    111       C  
ATOM   5913  C   THR B  36     -19.624 -25.797 -16.756  1.00 92.07           C  
ANISOU 5913  C   THR B  36    11675  11409  11899    178   -341    122       C  
ATOM   5914  O   THR B  36     -20.028 -25.931 -15.596  1.00 90.67           O  
ANISOU 5914  O   THR B  36    11467  11244  11740    169   -333    126       O  
ATOM   5915  CB  THR B  36     -19.467 -23.304 -17.159  1.00 95.64           C  
ANISOU 5915  CB  THR B  36    12129  11878  12331    195   -354    120       C  
ATOM   5916  OG1 THR B  36     -19.960 -22.220 -17.956  1.00 93.37           O  
ANISOU 5916  OG1 THR B  36    11851  11591  12034    203   -376    111       O  
ATOM   5917  CG2 THR B  36     -17.943 -23.355 -17.287  1.00 93.76           C  
ANISOU 5917  CG2 THR B  36    11911  11639  12075    205   -328    134       C  
ATOM   5918  N   TYR B  37     -18.740 -26.620 -17.326  1.00 92.82           N  
ANISOU 5918  N   TYR B  37    11796  11489  11980    183   -327    126       N  
ATOM   5919  CA  TYR B  37     -18.231 -27.832 -16.665  1.00 92.16           C  
ANISOU 5919  CA  TYR B  37    11708  11402  11905    177   -304    137       C  
ATOM   5920  C   TYR B  37     -16.707 -27.978 -16.737  1.00 90.73           C  
ANISOU 5920  C   TYR B  37    11546  11220  11707    188   -277    152       C  
ATOM   5921  O   TYR B  37     -16.079 -27.607 -17.734  1.00 86.81           O  
ANISOU 5921  O   TYR B  37    11078  10715  11190    199   -278    151       O  
ATOM   5922  CB  TYR B  37     -18.908 -29.087 -17.238  1.00 92.51           C  
ANISOU 5922  CB  TYR B  37    11764  11426  11958    168   -315    125       C  
ATOM   5923  CG  TYR B  37     -20.388 -29.184 -16.927  1.00 92.54           C  
ANISOU 5923  CG  TYR B  37    11744  11432  11985    155   -337    112       C  
ATOM   5924  CD1 TYR B  37     -21.336 -28.553 -17.736  1.00 93.34           C  
ANISOU 5924  CD1 TYR B  37    11850  11530  12084    155   -368     96       C  
ATOM   5925  CD2 TYR B  37     -20.843 -29.902 -15.823  1.00 93.45           C  
ANISOU 5925  CD2 TYR B  37    11831  11552  12123    143   -327    117       C  
ATOM   5926  CE1 TYR B  37     -22.691 -28.631 -17.450  1.00 94.09           C  
ANISOU 5926  CE1 TYR B  37    11921  11626  12200    143   -388     84       C  
ATOM   5927  CE2 TYR B  37     -22.198 -29.989 -15.535  1.00 95.78           C  
ANISOU 5927  CE2 TYR B  37    12103  11847  12439    131   -346    105       C  
ATOM   5928  CZ  TYR B  37     -23.117 -29.349 -16.350  1.00 94.29           C  
ANISOU 5928  CZ  TYR B  37    11918  11656  12249    131   -377     89       C  
ATOM   5929  OH  TYR B  37     -24.462 -29.425 -16.070  1.00 90.30           O  
ANISOU 5929  OH  TYR B  37    11389  11153  11767    119   -396     77       O  
ATOM   5930  N   GLN B  38     -16.132 -28.530 -15.668  1.00 94.64           N  
ANISOU 5930  N   GLN B  38    12024  11724  12210    185   -252    167       N  
ATOM   5931  CA  GLN B  38     -14.684 -28.738 -15.541  1.00 96.41           C  
ANISOU 5931  CA  GLN B  38    12260  11951  12421    194   -224    184       C  
ATOM   5932  C   GLN B  38     -14.309 -30.222 -15.512  1.00 97.52           C  
ANISOU 5932  C   GLN B  38    12410  12076  12565    191   -207    190       C  
ATOM   5933  O   GLN B  38     -14.629 -30.934 -14.555  1.00 97.23           O  
ANISOU 5933  O   GLN B  38    12352  12045  12546    182   -198    195       O  
ATOM   5934  CB  GLN B  38     -14.150 -28.043 -14.281  1.00 92.79           C  
ANISOU 5934  CB  GLN B  38    11773  11516  11966    195   -207    198       C  
ATOM   5935  CG  GLN B  38     -13.231 -26.862 -14.540  1.00 91.87           C  
ANISOU 5935  CG  GLN B  38    11665  11409  11831    207   -201    204       C  
ATOM   5936  CD  GLN B  38     -11.796 -27.289 -14.778  1.00 94.28           C  
ANISOU 5936  CD  GLN B  38    11989  11710  12120    216   -176    218       C  
ATOM   5937  OE1 GLN B  38     -11.453 -27.799 -15.845  1.00 95.95           O  
ANISOU 5937  OE1 GLN B  38    12232  11903  12321    222   -177    215       O  
ATOM   5938  NE2 GLN B  38     -10.947 -27.079 -13.781  1.00 95.43           N  
ANISOU 5938  NE2 GLN B  38    12116  11873  12266    218   -155    233       N  
ATOM   5939  N   CYS B  39     -13.623 -30.674 -16.560  1.00 97.71           N  
ANISOU 5939  N   CYS B  39    12469  12083  12572    199   -202    190       N  
ATOM   5940  CA  CYS B  39     -13.204 -32.070 -16.674  1.00 99.42           C  
ANISOU 5940  CA  CYS B  39    12700  12283  12791    198   -186    196       C  
ATOM   5941  C   CYS B  39     -11.698 -32.158 -16.910  1.00 94.37           C  
ANISOU 5941  C   CYS B  39    12080  11643  12133    211   -160    212       C  
ATOM   5942  O   CYS B  39     -11.240 -32.560 -17.981  1.00 97.30           O  
ANISOU 5942  O   CYS B  39    12484  11995  12490    218   -159    209       O  
ATOM   5943  CB  CYS B  39     -13.983 -32.778 -17.792  1.00106.98           C  
ANISOU 5943  CB  CYS B  39    13681  13216  13748    193   -206    178       C  
ATOM   5944  SG  CYS B  39     -15.777 -32.516 -17.749  1.00125.04           S  
ANISOU 5944  SG  CYS B  39    15948  15504  16054    178   -240    157       S  
ATOM   5945  N   MET B  40     -10.935 -31.779 -15.891  1.00 87.05           N  
ANISOU 5945  N   MET B  40    11131  10735  11207    215   -140    228       N  
ATOM   5946  CA  MET B  40      -9.484 -31.712 -15.992  1.00 86.78           C  
ANISOU 5946  CA  MET B  40    11111  10704  11157    227   -116    244       C  
ATOM   5947  C   MET B  40      -8.826 -32.836 -15.203  1.00 85.06           C  
ANISOU 5947  C   MET B  40    10884  10487  10946    227    -89    261       C  
ATOM   5948  O   MET B  40      -9.289 -33.187 -14.117  1.00 87.08           O  
ANISOU 5948  O   MET B  40    11112  10753  11218    219    -85    265       O  
ATOM   5949  CB  MET B  40      -8.995 -30.355 -15.481  1.00 89.23           C  
ANISOU 5949  CB  MET B  40    11404  11037  11462    232   -114    251       C  
ATOM   5950  CG  MET B  40      -7.554 -30.022 -15.837  1.00 89.37           C  
ANISOU 5950  CG  MET B  40    11438  11056  11461    246    -94    264       C  
ATOM   5951  SD  MET B  40      -6.974 -28.488 -15.086  1.00 90.40           S  
ANISOU 5951  SD  MET B  40    11545  11214  11586    250    -89    272       S  
ATOM   5952  CE  MET B  40      -8.068 -27.287 -15.848  1.00 85.57           C  
ANISOU 5952  CE  MET B  40    10939  10600  10972    247   -121    251       C  
ATOM   5953  N   ASP B  41      -7.748 -33.391 -15.759  1.00 84.93           N  
ANISOU 5953  N   ASP B  41    10893  10459  10916    237    -70    271       N  
ATOM   5954  CA  ASP B  41      -6.952 -34.439 -15.107  1.00 86.90           C  
ANISOU 5954  CA  ASP B  41    11138  10709  11170    240    -42    289       C  
ATOM   5955  C   ASP B  41      -7.807 -35.648 -14.689  1.00 90.85           C  
ANISOU 5955  C   ASP B  41    11630  11199  11688    229    -42    285       C  
ATOM   5956  O   ASP B  41      -7.584 -36.248 -13.632  1.00 94.40           O  
ANISOU 5956  O   ASP B  41    12059  11659  12150    227    -23    299       O  
ATOM   5957  CB  ASP B  41      -6.174 -33.855 -13.913  1.00 86.92           C  
ANISOU 5957  CB  ASP B  41    11111  10739  11173    244    -24    307       C  
ATOM   5958  CG  ASP B  41      -5.020 -34.740 -13.460  1.00 89.10           C  
ANISOU 5958  CG  ASP B  41    11388  11016  11446    252      6    328       C  
ATOM   5959  OD1 ASP B  41      -4.643 -35.672 -14.203  1.00 91.67           O  
ANISOU 5959  OD1 ASP B  41    11741  11322  11767    257     16    330       O  
ATOM   5960  OD2 ASP B  41      -4.485 -34.500 -12.353  1.00 87.58           O  
ANISOU 5960  OD2 ASP B  41    11170  10848  11258    254     20    342       O  
ATOM   5961  N   GLN B  42      -8.775 -35.999 -15.537  1.00 91.37           N  
ANISOU 5961  N   GLN B  42    11712  11244  11757    222    -63    267       N  
ATOM   5962  CA  GLN B  42      -9.723 -37.087 -15.259  1.00 91.54           C  
ANISOU 5962  CA  GLN B  42    11727  11254  11798    209    -66    260       C  
ATOM   5963  C   GLN B  42      -9.459 -38.363 -16.078  1.00 94.84           C  
ANISOU 5963  C   GLN B  42    12177  11644  12212    211    -56    259       C  
ATOM   5964  O   GLN B  42     -10.247 -39.314 -16.023  1.00 90.86           O  
ANISOU 5964  O   GLN B  42    11672  11126  11723    200    -59    251       O  
ATOM   5965  CB  GLN B  42     -11.165 -36.604 -15.462  1.00 88.87           C  
ANISOU 5965  CB  GLN B  42    11379  10915  11471    197    -98    239       C  
ATOM   5966  CG  GLN B  42     -11.614 -35.507 -14.501  1.00 90.63           C  
ANISOU 5966  CG  GLN B  42    11568  11164  11702    193   -107    240       C  
ATOM   5967  CD  GLN B  42     -12.071 -36.028 -13.145  1.00 93.74           C  
ANISOU 5967  CD  GLN B  42    11928  11569  12117    184    -96    247       C  
ATOM   5968  OE1 GLN B  42     -13.170 -35.708 -12.684  1.00 95.93           O  
ANISOU 5968  OE1 GLN B  42    12183  11854  12410    174   -113    238       O  
ATOM   5969  NE2 GLN B  42     -11.230 -36.829 -12.498  1.00 93.16           N  
ANISOU 5969  NE2 GLN B  42    11851  11498  12045    189    -68    266       N  
ATOM   5970  N   LYS B  43      -8.351 -38.367 -16.827  1.00 99.61           N  
ANISOU 5970  N   LYS B  43    12808  12240  12797    224    -43    266       N  
ATOM   5971  CA  LYS B  43      -7.873 -39.528 -17.611  1.00101.99           C  
ANISOU 5971  CA  LYS B  43    13143  12516  13092    229    -29    268       C  
ATOM   5972  C   LYS B  43      -8.847 -40.024 -18.691  1.00 97.94           C  
ANISOU 5972  C   LYS B  43    12654  11978  12580    220    -51    245       C  
ATOM   5973  O   LYS B  43      -8.808 -41.195 -19.071  1.00100.37           O  
ANISOU 5973  O   LYS B  43    12982  12264  12890    218    -41    244       O  
ATOM   5974  CB  LYS B  43      -7.459 -40.691 -16.691  1.00102.69           C  
ANISOU 5974  CB  LYS B  43    13220  12604  13193    228      0    285       C  
ATOM   5975  CG  LYS B  43      -6.355 -40.357 -15.702  1.00106.64           C  
ANISOU 5975  CG  LYS B  43    13699  13128  13690    238     24    309       C  
ATOM   5976  CD  LYS B  43      -6.399 -41.297 -14.510  1.00107.83           C  
ANISOU 5976  CD  LYS B  43    13826  13284  13858    234     44    323       C  
ATOM   5977  CE  LYS B  43      -5.637 -40.720 -13.329  1.00108.32           C  
ANISOU 5977  CE  LYS B  43    13859  13376  13919    240     60    343       C  
ATOM   5978  NZ  LYS B  43      -5.808 -41.556 -12.109  1.00107.75           N  
ANISOU 5978  NZ  LYS B  43    13762  13312  13865    236     77    356       N  
ATOM   5979  N   LEU B  44      -9.693 -39.129 -19.194  1.00 94.61           N  
ANISOU 5979  N   LEU B  44    12231  11558  12155    215    -81    227       N  
ATOM   5980  CA  LEU B  44     -10.744 -39.489 -20.152  1.00 96.20           C  
ANISOU 5980  CA  LEU B  44    12452  11740  12359    206   -107    204       C  
ATOM   5981  C   LEU B  44     -10.211 -39.801 -21.554  1.00100.04           C  
ANISOU 5981  C   LEU B  44    12983  12202  12824    216   -107    198       C  
ATOM   5982  O   LEU B  44      -9.327 -39.103 -22.066  1.00 98.39           O  
ANISOU 5982  O   LEU B  44    12790  11997  12595    229   -101    204       O  
ATOM   5983  CB  LEU B  44     -11.800 -38.380 -20.238  1.00 92.66           C  
ANISOU 5983  CB  LEU B  44    11987  11303  11913    200   -140    188       C  
ATOM   5984  CG  LEU B  44     -12.409 -37.836 -18.940  1.00 91.01           C  
ANISOU 5984  CG  LEU B  44    11735  11118  11724    191   -143    192       C  
ATOM   5985  CD1 LEU B  44     -13.077 -36.497 -19.204  1.00 90.73           C  
ANISOU 5985  CD1 LEU B  44    11692  11096  11685    191   -172    180       C  
ATOM   5986  CD2 LEU B  44     -13.390 -38.816 -18.310  1.00 91.27           C  
ANISOU 5986  CD2 LEU B  44    11750  11145  11782    176   -145    186       C  
ATOM   5987  N   SER B  45     -10.760 -40.854 -22.162  1.00102.56           N  
ANISOU 5987  N   SER B  45    13322  12497  13147    208   -113    184       N  
ATOM   5988  CA  SER B  45     -10.433 -41.235 -23.540  1.00100.83           C  
ANISOU 5988  CA  SER B  45    13147  12255  12909    214   -116    175       C  
ATOM   5989  C   SER B  45     -11.131 -40.331 -24.546  1.00101.68           C  
ANISOU 5989  C   SER B  45    13268  12360  13004    215   -150    155       C  
ATOM   5990  O   SER B  45     -10.512 -39.843 -25.497  1.00 97.99           O  
ANISOU 5990  O   SER B  45    12829  11886  12513    228   -151    154       O  
ATOM   5991  CB  SER B  45     -10.827 -42.690 -23.810  1.00 96.06           C  
ANISOU 5991  CB  SER B  45    12558  11625  12314    205   -111    167       C  
ATOM   5992  OG  SER B  45      -9.704 -43.545 -23.734  1.00 96.97           O  
ANISOU 5992  OG  SER B  45    12689  11729  12424    214    -77    184       O  
ATOM   5993  N   LYS B  46     -12.429 -40.128 -24.329  1.00102.28           N  
ANISOU 5993  N   LYS B  46    13324  12442  13096    200   -177    139       N  
ATOM   5994  CA  LYS B  46     -13.265 -39.321 -25.209  1.00100.39           C  
ANISOU 5994  CA  LYS B  46    13094  12202  12848    199   -212    118       C  
ATOM   5995  C   LYS B  46     -14.130 -38.351 -24.400  1.00 99.53           C  
ANISOU 5995  C   LYS B  46    12946  12116  12753    192   -231    115       C  
ATOM   5996  O   LYS B  46     -14.011 -38.269 -23.176  1.00 98.63           O  
ANISOU 5996  O   LYS B  46    12800  12020  12656    189   -216    129       O  
ATOM   5997  CB  LYS B  46     -14.130 -40.224 -26.103  1.00 99.69           C  
ANISOU 5997  CB  LYS B  46    13027  12088  12760    189   -232     96       C  
ATOM   5998  CG  LYS B  46     -13.386 -40.852 -27.280  1.00102.40           C  
ANISOU 5998  CG  LYS B  46    13417  12407  13081    198   -222     94       C  
ATOM   5999  CD  LYS B  46     -12.758 -42.207 -26.955  1.00100.17           C  
ANISOU 5999  CD  LYS B  46    13143  12109  12806    196   -191    105       C  
ATOM   6000  CE  LYS B  46     -11.669 -42.575 -27.956  1.00 94.67           C  
ANISOU 6000  CE  LYS B  46    12491  11394  12085    211   -173    110       C  
ATOM   6001  NZ  LYS B  46     -11.017 -43.879 -27.652  1.00 86.45           N  
ANISOU 6001  NZ  LYS B  46    11458  10336  11050    211   -141    122       N  
ATOM   6002  N   VAL B  47     -14.991 -37.617 -25.096  1.00100.13           N  
ANISOU 6002  N   VAL B  47    13026  12193  12824    190   -263     98       N  
ATOM   6003  CA  VAL B  47     -15.855 -36.616 -24.476  1.00104.78           C  
ANISOU 6003  CA  VAL B  47    13581  12804  13426    185   -283     93       C  
ATOM   6004  C   VAL B  47     -16.992 -37.283 -23.690  1.00110.11           C  
ANISOU 6004  C   VAL B  47    14226  13479  14129    166   -292     85       C  
ATOM   6005  O   VAL B  47     -17.681 -38.153 -24.231  1.00112.68           O  
ANISOU 6005  O   VAL B  47    14563  13786  14460    155   -305     69       O  
ATOM   6006  CB  VAL B  47     -16.454 -35.674 -25.544  1.00103.37           C  
ANISOU 6006  CB  VAL B  47    13418  12624  13231    189   -316     76       C  
ATOM   6007  CG1 VAL B  47     -17.081 -34.446 -24.899  1.00104.31           C  
ANISOU 6007  CG1 VAL B  47    13505  12768  13360    188   -332     76       C  
ATOM   6008  CG2 VAL B  47     -15.389 -35.262 -26.552  1.00104.10           C  
ANISOU 6008  CG2 VAL B  47    13548  12709  13294    207   -308     81       C  
ATOM   6009  N   PRO B  48     -17.183 -36.890 -22.408  1.00111.68           N  
ANISOU 6009  N   PRO B  48    14386  13699  14346    161   -284     96       N  
ATOM   6010  CA  PRO B  48     -18.335 -37.372 -21.631  1.00114.85           C  
ANISOU 6010  CA  PRO B  48    14757  14104  14776    144   -293     88       C  
ATOM   6011  C   PRO B  48     -19.641 -36.850 -22.228  1.00121.87           C  
ANISOU 6011  C   PRO B  48    15641  14993  15669    136   -332     66       C  
ATOM   6012  O   PRO B  48     -20.009 -35.695 -21.994  1.00125.28           O  
ANISOU 6012  O   PRO B  48    16055  15443  16102    139   -346     65       O  
ATOM   6013  CB  PRO B  48     -18.105 -36.773 -20.236  1.00108.02           C  
ANISOU 6013  CB  PRO B  48    13855  13264  13923    144   -277    106       C  
ATOM   6014  CG  PRO B  48     -16.658 -36.436 -20.188  1.00104.39           C  
ANISOU 6014  CG  PRO B  48    13408  12809  13443    160   -251    125       C  
ATOM   6015  CD  PRO B  48     -16.286 -36.055 -21.589  1.00106.72           C  
ANISOU 6015  CD  PRO B  48    13741  13092  13713    171   -264    116       C  
ATOM   6016  N   ASP B  49     -20.327 -37.701 -22.991  1.00129.38           N  
ANISOU 6016  N   ASP B  49    16609  15924  16625    126   -348     48       N  
ATOM   6017  CA  ASP B  49     -21.473 -37.272 -23.810  1.00134.30           C  
ANISOU 6017  CA  ASP B  49    17235  16544  17247    121   -386     26       C  
ATOM   6018  C   ASP B  49     -22.852 -37.312 -23.118  1.00136.48           C  
ANISOU 6018  C   ASP B  49    17474  16829  17553    104   -404     16       C  
ATOM   6019  O   ASP B  49     -23.880 -37.517 -23.772  1.00142.29           O  
ANISOU 6019  O   ASP B  49    18213  17556  18294     95   -433     -4       O  
ATOM   6020  CB  ASP B  49     -21.491 -38.002 -25.174  1.00132.32           C  
ANISOU 6020  CB  ASP B  49    17025  16268  16981    121   -398     10       C  
ATOM   6021  CG  ASP B  49     -21.489 -39.526 -25.045  1.00128.61           C  
ANISOU 6021  CG  ASP B  49    16562  15778  16524    109   -383      7       C  
ATOM   6022  OD1 ASP B  49     -20.899 -40.063 -24.081  1.00125.28           O  
ANISOU 6022  OD1 ASP B  49    16127  15359  16114    108   -352     25       O  
ATOM   6023  OD2 ASP B  49     -22.069 -40.191 -25.932  1.00120.86           O  
ANISOU 6023  OD2 ASP B  49    15601  14778  15542    101   -401    -11       O  
ATOM   6024  N   ASP B  50     -22.860 -37.099 -21.801  1.00129.49           N  
ANISOU 6024  N   ASP B  50    16553  15960  16685    101   -388     30       N  
ATOM   6025  CA  ASP B  50     -24.102 -36.953 -21.027  1.00122.83           C  
ANISOU 6025  CA  ASP B  50    15672  15127  15869     87   -403     23       C  
ATOM   6026  C   ASP B  50     -24.202 -35.579 -20.348  1.00117.84           C  
ANISOU 6026  C   ASP B  50    15013  14521  15238     94   -407     31       C  
ATOM   6027  O   ASP B  50     -25.181 -35.280 -19.661  1.00115.09           O  
ANISOU 6027  O   ASP B  50    14632  14184  14911     84   -418     27       O  
ATOM   6028  CB  ASP B  50     -24.268 -38.095 -20.013  1.00124.34           C  
ANISOU 6028  CB  ASP B  50    15842  15314  16086     73   -381     30       C  
ATOM   6029  CG  ASP B  50     -22.946 -38.557 -19.418  1.00125.88           C  
ANISOU 6029  CG  ASP B  50    16045  15509  16274     82   -342     52       C  
ATOM   6030  OD1 ASP B  50     -22.020 -37.730 -19.269  1.00122.87           O  
ANISOU 6030  OD1 ASP B  50    15668  15141  15875     96   -331     66       O  
ATOM   6031  OD2 ASP B  50     -22.838 -39.760 -19.095  1.00126.76           O  
ANISOU 6031  OD2 ASP B  50    16157  15606  16397     74   -324     55       O  
ATOM   6032  N   ILE B  51     -23.173 -34.759 -20.553  1.00114.28           N  
ANISOU 6032  N   ILE B  51    14577  14078  14764    110   -396     43       N  
ATOM   6033  CA  ILE B  51     -23.176 -33.338 -20.200  1.00110.29           C  
ANISOU 6033  CA  ILE B  51    14055  13595  14254    119   -403     49       C  
ATOM   6034  C   ILE B  51     -24.285 -32.627 -20.990  1.00108.42           C  
ANISOU 6034  C   ILE B  51    13819  13359  14016    118   -440     29       C  
ATOM   6035  O   ILE B  51     -24.422 -32.867 -22.193  1.00107.74           O  
ANISOU 6035  O   ILE B  51    13761  13258  13916    120   -458     16       O  
ATOM   6036  CB  ILE B  51     -21.783 -32.723 -20.489  1.00108.17           C  
ANISOU 6036  CB  ILE B  51    13810  13331  13959    136   -384     63       C  
ATOM   6037  CG1 ILE B  51     -20.800 -33.127 -19.385  1.00106.65           C  
ANISOU 6037  CG1 ILE B  51    13605  13145  13770    138   -348     84       C  
ATOM   6038  CG2 ILE B  51     -21.842 -31.206 -20.632  1.00104.97           C  
ANISOU 6038  CG2 ILE B  51    13399  12942  13542    147   -398     63       C  
ATOM   6039  CD1 ILE B  51     -19.355 -33.194 -19.826  1.00105.13           C  
ANISOU 6039  CD1 ILE B  51    13442  12947  13554    152   -326     97       C  
ATOM   6040  N   PRO B  52     -25.089 -31.770 -20.316  1.00105.60           N  
ANISOU 6040  N   PRO B  52    13428  13019  13673    114   -452     29       N  
ATOM   6041  CA  PRO B  52     -26.256 -31.115 -20.924  1.00106.35           C  
ANISOU 6041  CA  PRO B  52    13518  13117  13772    112   -488     11       C  
ATOM   6042  C   PRO B  52     -26.061 -30.667 -22.373  1.00108.41           C  
ANISOU 6042  C   PRO B  52    13815  13369  14005    124   -508      1       C  
ATOM   6043  O   PRO B  52     -25.039 -30.069 -22.713  1.00108.82           O  
ANISOU 6043  O   PRO B  52    13888  13423  14034    139   -496     11       O  
ATOM   6044  CB  PRO B  52     -26.483 -29.910 -20.017  1.00 99.96           C  
ANISOU 6044  CB  PRO B  52    12678  12332  12971    116   -486     20       C  
ATOM   6045  CG  PRO B  52     -26.053 -30.393 -18.678  1.00100.62           C  
ANISOU 6045  CG  PRO B  52    12738  12422  13069    110   -456     36       C  
ATOM   6046  CD  PRO B  52     -24.954 -31.401 -18.893  1.00102.22           C  
ANISOU 6046  CD  PRO B  52    12967  12611  13261    112   -432     44       C  
ATOM   6047  N   SER B  53     -27.057 -30.960 -23.205  1.00112.78           N  
ANISOU 6047  N   SER B  53    14375  13913  14562    118   -538    -18       N  
ATOM   6048  CA  SER B  53     -27.018 -30.664 -24.636  1.00112.42           C  
ANISOU 6048  CA  SER B  53    14364  13857  14491    128   -561    -30       C  
ATOM   6049  C   SER B  53     -27.150 -29.160 -24.917  1.00111.91           C  
ANISOU 6049  C   SER B  53    14298  13808  14414    142   -576    -29       C  
ATOM   6050  O   SER B  53     -27.267 -28.741 -26.072  1.00110.04           O  
ANISOU 6050  O   SER B  53    14087  13565  14157    152   -597    -39       O  
ATOM   6051  CB  SER B  53     -28.126 -31.449 -25.349  1.00116.07           C  
ANISOU 6051  CB  SER B  53    14831  14306  14963    115   -590    -52       C  
ATOM   6052  OG  SER B  53     -27.733 -31.845 -26.651  1.00118.33           O  
ANISOU 6052  OG  SER B  53    15159  14575  15225    122   -599    -61       O  
ATOM   6053  N   SER B  54     -27.116 -28.356 -23.853  1.00111.34           N  
ANISOU 6053  N   SER B  54    14196  13754  14352    144   -563    -16       N  
ATOM   6054  CA  SER B  54     -27.258 -26.902 -23.952  1.00107.90           C  
ANISOU 6054  CA  SER B  54    13754  13333  13907    156   -575    -14       C  
ATOM   6055  C   SER B  54     -26.100 -26.129 -23.299  1.00105.30           C  
ANISOU 6055  C   SER B  54    13424  13016  13569    167   -545      5       C  
ATOM   6056  O   SER B  54     -26.239 -24.942 -22.990  1.00 98.71           O  
ANISOU 6056  O   SER B  54    12575  12196  12733    175   -548     10       O  
ATOM   6057  CB  SER B  54     -28.597 -26.467 -23.345  1.00102.86           C  
ANISOU 6057  CB  SER B  54    13079  12709  13295    147   -595    -21       C  
ATOM   6058  OG  SER B  54     -28.658 -26.795 -21.968  1.00 99.32           O  
ANISOU 6058  OG  SER B  54    12596  12268  12870    136   -574    -11       O  
ATOM   6059  N   THR B  55     -24.958 -26.795 -23.113  1.00108.67           N  
ANISOU 6059  N   THR B  55    13865  13435  13987    169   -517     17       N  
ATOM   6060  CA  THR B  55     -23.810 -26.201 -22.403  1.00109.15           C  
ANISOU 6060  CA  THR B  55    13923  13508  14041    178   -487     36       C  
ATOM   6061  C   THR B  55     -22.985 -25.205 -23.222  1.00107.47           C  
ANISOU 6061  C   THR B  55    13738  13294  13799    196   -486     40       C  
ATOM   6062  O   THR B  55     -22.756 -25.394 -24.420  1.00105.87           O  
ANISOU 6062  O   THR B  55    13569  13077  13577    204   -496     33       O  
ATOM   6063  CB  THR B  55     -22.869 -27.266 -21.796  1.00108.35           C  
ANISOU 6063  CB  THR B  55    13824  13401  13943    173   -456     48       C  
ATOM   6064  OG1 THR B  55     -22.567 -28.267 -22.774  1.00114.87           O  
ANISOU 6064  OG1 THR B  55    14682  14205  14756    173   -457     41       O  
ATOM   6065  CG2 THR B  55     -23.517 -27.918 -20.599  1.00107.16           C  
ANISOU 6065  CG2 THR B  55    13638  13256  13821    157   -449     50       C  
ATOM   6066  N   LYS B  56     -22.540 -24.150 -22.538  1.00105.53           N  
ANISOU 6066  N   LYS B  56    13477  13066  13553    202   -472     52       N  
ATOM   6067  CA  LYS B  56     -21.797 -23.042 -23.139  1.00 99.43           C  
ANISOU 6067  CA  LYS B  56    12725  12295  12756    219   -469     57       C  
ATOM   6068  C   LYS B  56     -20.296 -23.299 -23.183  1.00 93.37           C  
ANISOU 6068  C   LYS B  56    11979  11523  11974    227   -439     71       C  
ATOM   6069  O   LYS B  56     -19.658 -23.147 -24.228  1.00 92.70           O  
ANISOU 6069  O   LYS B  56    11928  11427  11866    239   -438     71       O  
ATOM   6070  CB  LYS B  56     -22.063 -21.738 -22.364  1.00 99.87           C  
ANISOU 6070  CB  LYS B  56    12754  12371  12820    222   -468     62       C  
ATOM   6071  CG  LYS B  56     -22.981 -20.733 -23.048  1.00 99.17           C  
ANISOU 6071  CG  LYS B  56    12667  12284  12727    229   -497     51       C  
ATOM   6072  CD  LYS B  56     -24.455 -21.014 -22.808  1.00100.22           C  
ANISOU 6072  CD  LYS B  56    12774  12420  12882    217   -523     38       C  
ATOM   6073  CE  LYS B  56     -25.321 -20.034 -23.584  1.00100.26           C  
ANISOU 6073  CE  LYS B  56    12783  12427  12880    226   -552     28       C  
ATOM   6074  NZ  LYS B  56     -26.715 -20.531 -23.749  1.00100.22           N  
ANISOU 6074  NZ  LYS B  56    12764  12421  12894    215   -581     13       N  
ATOM   6075  N   ASN B  57     -19.732 -23.670 -22.038  1.00 87.03           N  
ANISOU 6075  N   ASN B  57    11155  10728  11182    220   -413     84       N  
ATOM   6076  CA  ASN B  57     -18.286 -23.763 -21.899  1.00 82.90           C  
ANISOU 6076  CA  ASN B  57    10647  10205  10647    228   -383    100       C  
ATOM   6077  C   ASN B  57     -17.855 -25.089 -21.298  1.00 80.75           C  
ANISOU 6077  C   ASN B  57    10368   9927  10383    219   -363    107       C  
ATOM   6078  O   ASN B  57     -18.492 -25.606 -20.376  1.00 77.69           O  
ANISOU 6078  O   ASN B  57     9953   9547  10018    206   -362    107       O  
ATOM   6079  CB  ASN B  57     -17.750 -22.594 -21.059  1.00 82.63           C  
ANISOU 6079  CB  ASN B  57    10593  10191  10612    233   -368    112       C  
ATOM   6080  CG  ASN B  57     -18.367 -21.256 -21.446  1.00 81.44           C  
ANISOU 6080  CG  ASN B  57    10440  10046  10457    240   -388    104       C  
ATOM   6081  OD1 ASN B  57     -18.951 -20.570 -20.610  1.00 79.10           O  
ANISOU 6081  OD1 ASN B  57    10114   9766  10175    235   -392    104       O  
ATOM   6082  ND2 ASN B  57     -18.251 -20.888 -22.718  1.00 79.49           N  
ANISOU 6082  ND2 ASN B  57    10224   9787  10189    252   -400     98       N  
ATOM   6083  N   ILE B  58     -16.767 -25.636 -21.832  1.00 79.21           N  
ANISOU 6083  N   ILE B  58    10202   9721  10173    227   -345    114       N  
ATOM   6084  CA  ILE B  58     -16.240 -26.913 -21.363  1.00 76.24           C  
ANISOU 6084  CA  ILE B  58     9825   9338   9804    220   -324    123       C  
ATOM   6085  C   ILE B  58     -14.713 -26.964 -21.459  1.00 74.50           C  
ANISOU 6085  C   ILE B  58     9623   9116   9567    232   -295    139       C  
ATOM   6086  O   ILE B  58     -14.125 -26.558 -22.464  1.00 71.86           O  
ANISOU 6086  O   ILE B  58     9319   8772   9212    244   -295    138       O  
ATOM   6087  CB  ILE B  58     -16.916 -28.115 -22.086  1.00 77.66           C  
ANISOU 6087  CB  ILE B  58    10022   9497   9987    213   -338    109       C  
ATOM   6088  CG1 ILE B  58     -16.512 -29.449 -21.450  1.00 78.85           C  
ANISOU 6088  CG1 ILE B  58    10167   9642  10149    205   -316    118       C  
ATOM   6089  CG2 ILE B  58     -16.630 -28.110 -23.582  1.00 77.59           C  
ANISOU 6089  CG2 ILE B  58    10055   9470   9955    224   -349    101       C  
ATOM   6090  CD1 ILE B  58     -17.416 -30.604 -21.823  1.00 82.24           C  
ANISOU 6090  CD1 ILE B  58    10601  10054  10589    193   -330    104       C  
ATOM   6091  N   ASP B  59     -14.088 -27.442 -20.387  1.00 76.57           N  
ANISOU 6091  N   ASP B  59     9866   9387   9839    228   -269    153       N  
ATOM   6092  CA  ASP B  59     -12.651 -27.665 -20.352  1.00 75.60           C  
ANISOU 6092  CA  ASP B  59     9757   9263   9703    237   -241    170       C  
ATOM   6093  C   ASP B  59     -12.365 -29.162 -20.252  1.00 77.52           C  
ANISOU 6093  C   ASP B  59    10008   9493   9952    232   -225    175       C  
ATOM   6094  O   ASP B  59     -12.864 -29.847 -19.354  1.00 77.99           O  
ANISOU 6094  O   ASP B  59    10043   9557  10030    221   -222    176       O  
ATOM   6095  CB  ASP B  59     -12.023 -26.919 -19.173  1.00 75.40           C  
ANISOU 6095  CB  ASP B  59     9703   9261   9682    238   -222    184       C  
ATOM   6096  CG  ASP B  59     -10.502 -26.941 -19.206  1.00 77.31           C  
ANISOU 6096  CG  ASP B  59     9959   9504   9910    249   -194    201       C  
ATOM   6097  OD1 ASP B  59      -9.905 -28.035 -19.322  1.00 75.90           O  
ANISOU 6097  OD1 ASP B  59     9793   9314   9729    250   -178    208       O  
ATOM   6098  OD2 ASP B  59      -9.900 -25.854 -19.103  1.00 79.30           O  
ANISOU 6098  OD2 ASP B  59    10207   9768  10153    256   -188    207       O  
ATOM   6099  N   LEU B  60     -11.559 -29.658 -21.184  1.00 76.91           N  
ANISOU 6099  N   LEU B  60     9964   9398   9857    241   -215    177       N  
ATOM   6100  CA  LEU B  60     -11.196 -31.068 -21.221  1.00 76.22           C  
ANISOU 6100  CA  LEU B  60     9890   9296   9773    239   -199    182       C  
ATOM   6101  C   LEU B  60      -9.693 -31.252 -21.191  1.00 72.70           C  
ANISOU 6101  C   LEU B  60     9457   8851   9315    251   -168    201       C  
ATOM   6102  O   LEU B  60      -9.198 -32.354 -21.418  1.00 73.36           O  
ANISOU 6102  O   LEU B  60     9558   8919   9397    252   -153    206       O  
ATOM   6103  CB  LEU B  60     -11.766 -31.735 -22.474  1.00 80.64           C  
ANISOU 6103  CB  LEU B  60    10482   9832  10326    238   -217    165       C  
ATOM   6104  CG  LEU B  60     -13.203 -32.252 -22.437  1.00 77.99           C  
ANISOU 6104  CG  LEU B  60    10134   9490  10008    223   -242    148       C  
ATOM   6105  CD1 LEU B  60     -13.656 -32.588 -23.847  1.00 77.00           C  
ANISOU 6105  CD1 LEU B  60    10044   9342   9869    225   -263    130       C  
ATOM   6106  CD2 LEU B  60     -13.324 -33.467 -21.529  1.00 78.16           C  
ANISOU 6106  CD2 LEU B  60    10137   9509  10048    212   -226    154       C  
ATOM   6107  N   SER B  61      -8.975 -30.171 -20.906  1.00 72.13           N  
ANISOU 6107  N   SER B  61     9376   8793   9234    259   -159    210       N  
ATOM   6108  CA  SER B  61      -7.515 -30.191 -20.875  1.00 72.49           C  
ANISOU 6108  CA  SER B  61     9432   8841   9268    270   -131    228       C  
ATOM   6109  C   SER B  61      -6.947 -31.241 -19.910  1.00 69.82           C  
ANISOU 6109  C   SER B  61     9078   8508   8941    267   -105    244       C  
ATOM   6110  O   SER B  61      -7.619 -31.669 -18.969  1.00 66.48           O  
ANISOU 6110  O   SER B  61     8629   8094   8537    256   -107    244       O  
ATOM   6111  CB  SER B  61      -6.962 -28.798 -20.546  1.00 74.08           C  
ANISOU 6111  CB  SER B  61     9621   9063   9463    277   -127    235       C  
ATOM   6112  OG  SER B  61      -7.268 -28.419 -19.212  1.00 75.39           O  
ANISOU 6112  OG  SER B  61     9747   9252   9646    268   -125    240       O  
ATOM   6113  N   PHE B  62      -5.709 -31.654 -20.180  1.00 69.09           N  
ANISOU 6113  N   PHE B  62     9004   8409   8837    278    -81    258       N  
ATOM   6114  CA  PHE B  62      -4.969 -32.613 -19.351  1.00 70.17           C  
ANISOU 6114  CA  PHE B  62     9129   8550   8981    278    -53    276       C  
ATOM   6115  C   PHE B  62      -5.601 -34.011 -19.271  1.00 70.80           C  
ANISOU 6115  C   PHE B  62     9212   8614   9073    269    -53    271       C  
ATOM   6116  O   PHE B  62      -5.410 -34.746 -18.298  1.00 68.88           O  
ANISOU 6116  O   PHE B  62     8949   8377   8842    265    -36    283       O  
ATOM   6117  CB  PHE B  62      -4.660 -32.019 -17.967  1.00 69.82           C  
ANISOU 6117  CB  PHE B  62     9046   8534   8947    275    -43    289       C  
ATOM   6118  CG  PHE B  62      -3.702 -30.854 -18.010  1.00 68.25           C  
ANISOU 6118  CG  PHE B  62     8847   8349   8735    285    -34    297       C  
ATOM   6119  CD1 PHE B  62      -4.175 -29.545 -18.100  1.00 66.17           C  
ANISOU 6119  CD1 PHE B  62     8575   8095   8469    283    -53    287       C  
ATOM   6120  CD2 PHE B  62      -2.325 -31.064 -17.976  1.00 64.23           C  
ANISOU 6120  CD2 PHE B  62     8345   7842   8217    296     -7    315       C  
ATOM   6121  CE1 PHE B  62      -3.297 -28.475 -18.148  1.00 64.37           C  
ANISOU 6121  CE1 PHE B  62     8346   7879   8230    292    -44    294       C  
ATOM   6122  CE2 PHE B  62      -1.442 -29.994 -18.023  1.00 65.26           C  
ANISOU 6122  CE2 PHE B  62     8473   7985   8337    304      0    322       C  
ATOM   6123  CZ  PHE B  62      -1.929 -28.699 -18.108  1.00 64.65           C  
ANISOU 6123  CZ  PHE B  62     8389   7917   8258    302    -18    311       C  
ATOM   6124  N   ASN B  63      -6.339 -34.366 -20.321  1.00 74.12           N  
ANISOU 6124  N   ASN B  63     9659   9013   9490    266    -72    254       N  
ATOM   6125  CA  ASN B  63      -6.871 -35.713 -20.506  1.00 79.47           C  
ANISOU 6125  CA  ASN B  63    10346   9670  10176    259    -72    248       C  
ATOM   6126  C   ASN B  63      -6.274 -36.352 -21.757  1.00 85.02           C  
ANISOU 6126  C   ASN B  63    11092  10348  10862    268    -64    246       C  
ATOM   6127  O   ASN B  63      -6.279 -35.725 -22.818  1.00 89.31           O  
ANISOU 6127  O   ASN B  63    11660  10882  11389    275    -78    236       O  
ATOM   6128  CB  ASN B  63      -8.396 -35.676 -20.612  1.00 76.60           C  
ANISOU 6128  CB  ASN B  63     9973   9303   9825    245   -103    227       C  
ATOM   6129  CG  ASN B  63      -9.067 -35.457 -19.270  1.00 79.57           C  
ANISOU 6129  CG  ASN B  63    10308   9700  10223    233   -106    229       C  
ATOM   6130  OD1 ASN B  63      -8.710 -36.090 -18.275  1.00 82.24           O  
ANISOU 6130  OD1 ASN B  63    10627  10046  10572    231    -85    244       O  
ATOM   6131  ND2 ASN B  63     -10.049 -34.561 -19.236  1.00 76.19           N  
ANISOU 6131  ND2 ASN B  63     9864   9282   9800    227   -132    216       N  
ATOM   6132  N   PRO B  64      -5.748 -37.593 -21.642  1.00 88.15           N  
ANISOU 6132  N   PRO B  64    11498  10732  11262    269    -41    256       N  
ATOM   6133  CA  PRO B  64      -5.155 -38.259 -22.812  1.00 88.07           C  
ANISOU 6133  CA  PRO B  64    11530  10696  11235    279    -32    255       C  
ATOM   6134  C   PRO B  64      -6.203 -38.642 -23.868  1.00 87.86           C  
ANISOU 6134  C   PRO B  64    11528  10646  11206    271    -58    231       C  
ATOM   6135  O   PRO B  64      -6.550 -39.817 -24.005  1.00 89.56           O  
ANISOU 6135  O   PRO B  64    11754  10844  11429    264    -54    226       O  
ATOM   6136  CB  PRO B  64      -4.479 -39.502 -22.211  1.00 85.88           C  
ANISOU 6136  CB  PRO B  64    11250  10412  10966    280     -1    272       C  
ATOM   6137  CG  PRO B  64      -5.222 -39.763 -20.945  1.00 88.77           C  
ANISOU 6137  CG  PRO B  64    11578  10793  11355    267     -3    274       C  
ATOM   6138  CD  PRO B  64      -5.624 -38.412 -20.420  1.00 89.57           C  
ANISOU 6138  CD  PRO B  64    11652  10920  11459    264    -21    270       C  
ATOM   6139  N   LEU B  65      -6.690 -37.642 -24.605  1.00 86.31           N  
ANISOU 6139  N   LEU B  65    11342  10452  10999    273    -84    217       N  
ATOM   6140  CA  LEU B  65      -7.700 -37.841 -25.647  1.00 84.82           C  
ANISOU 6140  CA  LEU B  65    11175  10244  10805    267   -112    193       C  
ATOM   6141  C   LEU B  65      -7.134 -38.564 -26.866  1.00 84.39           C  
ANISOU 6141  C   LEU B  65    11167  10163  10733    276   -103    190       C  
ATOM   6142  O   LEU B  65      -7.861 -39.285 -27.548  1.00 86.24           O  
ANISOU 6142  O   LEU B  65    11420  10377  10967    268   -118    173       O  
ATOM   6143  CB  LEU B  65      -8.316 -36.506 -26.083  1.00 84.36           C  
ANISOU 6143  CB  LEU B  65    11115  10197  10740    268   -141    180       C  
ATOM   6144  CG  LEU B  65      -8.997 -35.561 -25.084  1.00 80.24           C  
ANISOU 6144  CG  LEU B  65    10552   9701  10233    260   -155    180       C  
ATOM   6145  CD1 LEU B  65      -9.502 -34.334 -25.826  1.00 80.92           C  
ANISOU 6145  CD1 LEU B  65    10646   9791  10307    265   -182    167       C  
ATOM   6146  CD2 LEU B  65     -10.137 -36.227 -24.329  1.00 79.13           C  
ANISOU 6146  CD2 LEU B  65    10385   9562  10117    242   -166    171       C  
ATOM   6147  N   LYS B  66      -5.843 -38.345 -27.131  1.00 84.30           N  
ANISOU 6147  N   LYS B  66    11171  10151  10705    291    -79    206       N  
ATOM   6148  CA  LYS B  66      -5.076 -39.033 -28.188  1.00 83.90           C  
ANISOU 6148  CA  LYS B  66    11164  10076  10637    303    -64    208       C  
ATOM   6149  C   LYS B  66      -5.516 -38.682 -29.621  1.00 85.07           C  
ANISOU 6149  C   LYS B  66    11348  10207  10765    307    -89    188       C  
ATOM   6150  O   LYS B  66      -4.739 -38.131 -30.405  1.00 83.00           O  
ANISOU 6150  O   LYS B  66    11112   9941  10483    322    -82    193       O  
ATOM   6151  CB  LYS B  66      -5.067 -40.563 -27.974  1.00 81.27           C  
ANISOU 6151  CB  LYS B  66    10838   9726  10315    296    -47    210       C  
ATOM   6152  CG  LYS B  66      -4.488 -41.043 -26.647  1.00 77.16           C  
ANISOU 6152  CG  LYS B  66    10286   9218   9811    294    -19    232       C  
ATOM   6153  CD  LYS B  66      -2.975 -41.204 -26.718  1.00 79.04           C  
ANISOU 6153  CD  LYS B  66    10539   9455  10038    311     14    254       C  
ATOM   6154  CE  LYS B  66      -2.379 -41.681 -25.399  1.00 74.37           C  
ANISOU 6154  CE  LYS B  66     9916   8879   9462    311     42    277       C  
ATOM   6155  NZ  LYS B  66      -2.679 -43.108 -25.110  1.00 72.16           N  
ANISOU 6155  NZ  LYS B  66     9639   8583   9196    303     54    277       N  
ATOM   6156  N   ILE B  67      -6.758 -39.024 -29.952  1.00 87.48           N  
ANISOU 6156  N   ILE B  67    11657  10504  11077    294   -117    167       N  
ATOM   6157  CA  ILE B  67      -7.303 -38.874 -31.300  1.00 88.60           C  
ANISOU 6157  CA  ILE B  67    11833  10629  11200    296   -142    146       C  
ATOM   6158  C   ILE B  67      -8.675 -38.215 -31.176  1.00 87.96           C  
ANISOU 6158  C   ILE B  67    11730  10559  11129    284   -179    128       C  
ATOM   6159  O   ILE B  67      -9.447 -38.535 -30.265  1.00 84.36           O  
ANISOU 6159  O   ILE B  67    11242  10113  10697    269   -186    124       O  
ATOM   6160  CB  ILE B  67      -7.439 -40.252 -32.013  1.00 92.86           C  
ANISOU 6160  CB  ILE B  67    12405  11140  11737    292   -138    135       C  
ATOM   6161  CG1 ILE B  67      -6.134 -41.067 -31.908  1.00 94.72           C  
ANISOU 6161  CG1 ILE B  67    12656  11364  11968    302    -99    156       C  
ATOM   6162  CG2 ILE B  67      -7.849 -40.087 -33.476  1.00 88.31           C  
ANISOU 6162  CG2 ILE B  67    11869  10546  11138    297   -163    115       C  
ATOM   6163  CD1 ILE B  67      -6.326 -42.568 -31.785  1.00 91.46           C  
ANISOU 6163  CD1 ILE B  67    12250  10931  11566    292    -87    152       C  
ATOM   6164  N   LEU B  68      -8.975 -37.291 -32.085  1.00 89.41           N  
ANISOU 6164  N   LEU B  68    11931  10743  11295    292   -202    116       N  
ATOM   6165  CA  LEU B  68     -10.241 -36.571 -32.045  1.00 93.19           C  
ANISOU 6165  CA  LEU B  68    12391  11235  11782    282   -238     99       C  
ATOM   6166  C   LEU B  68     -11.145 -36.958 -33.216  1.00 95.91           C  
ANISOU 6166  C   LEU B  68    12764  11560  12116    278   -267     75       C  
ATOM   6167  O   LEU B  68     -11.066 -36.366 -34.294  1.00 93.03           O  
ANISOU 6167  O   LEU B  68    12429  11188  11728    290   -280     68       O  
ATOM   6168  CB  LEU B  68      -9.984 -35.062 -32.013  1.00 95.33           C  
ANISOU 6168  CB  LEU B  68    12652  11523  12043    294   -243    106       C  
ATOM   6169  CG  LEU B  68     -10.927 -34.182 -31.189  1.00 96.22           C  
ANISOU 6169  CG  LEU B  68    12725  11660  12174    284   -264    102       C  
ATOM   6170  CD1 LEU B  68     -10.982 -34.610 -29.727  1.00 94.62           C  
ANISOU 6170  CD1 LEU B  68    12481  11471  11997    272   -248    113       C  
ATOM   6171  CD2 LEU B  68     -10.483 -32.734 -31.298  1.00 96.35           C  
ANISOU 6171  CD2 LEU B  68    12738  11691  12177    298   -264    110       C  
ATOM   6172  N   LYS B  69     -12.005 -37.951 -32.982  1.00102.71           N  
ANISOU 6172  N   LYS B  69    13617  12412  12994    261   -277     62       N  
ATOM   6173  CA  LYS B  69     -12.860 -38.540 -34.024  1.00108.93           C  
ANISOU 6173  CA  LYS B  69    14431  13181  13774    255   -304     38       C  
ATOM   6174  C   LYS B  69     -13.922 -37.579 -34.555  1.00111.34           C  
ANISOU 6174  C   LYS B  69    14733  13496  14075    254   -344     20       C  
ATOM   6175  O   LYS B  69     -14.206 -36.548 -33.941  1.00115.20           O  
ANISOU 6175  O   LYS B  69    15192  14007  14572    254   -352     25       O  
ATOM   6176  CB  LYS B  69     -13.554 -39.817 -33.523  1.00110.84           C  
ANISOU 6176  CB  LYS B  69    14660  13413  14041    235   -304     29       C  
ATOM   6177  CG  LYS B  69     -12.641 -40.989 -33.177  1.00112.93           C  
ANISOU 6177  CG  LYS B  69    14934  13663  14310    235   -267     43       C  
ATOM   6178  CD  LYS B  69     -12.199 -41.004 -31.714  1.00112.93           C  
ANISOU 6178  CD  LYS B  69    14895  13680  14331    232   -241     65       C  
ATOM   6179  CE  LYS B  69     -13.368 -40.906 -30.740  1.00110.36           C  
ANISOU 6179  CE  LYS B  69    14526  13370  14033    214   -259     58       C  
ATOM   6180  NZ  LYS B  69     -13.663 -39.498 -30.346  1.00105.53           N  
ANISOU 6180  NZ  LYS B  69    13889  12785  13423    218   -275     61       N  
ATOM   6181  N   SER B  70     -14.508 -37.936 -35.696  1.00110.27           N  
ANISOU 6181  N   SER B  70    14628  13344  13926    252   -368      0       N  
ATOM   6182  CA  SER B  70     -15.596 -37.167 -36.292  1.00107.30           C  
ANISOU 6182  CA  SER B  70    14250  12974  13544    251   -408    -19       C  
ATOM   6183  C   SER B  70     -16.888 -37.348 -35.496  1.00104.92           C  
ANISOU 6183  C   SER B  70    13909  12684  13272    230   -429    -30       C  
ATOM   6184  O   SER B  70     -17.087 -38.382 -34.853  1.00101.40           O  
ANISOU 6184  O   SER B  70    13448  12231  12847    215   -418    -31       O  
ATOM   6185  CB  SER B  70     -15.803 -37.585 -37.747  1.00108.18           C  
ANISOU 6185  CB  SER B  70    14407  13063  13630    255   -426    -38       C  
ATOM   6186  OG  SER B  70     -16.624 -36.655 -38.430  1.00116.02           O  
ANISOU 6186  OG  SER B  70    15404  14066  14613    260   -463    -52       O  
ATOM   6187  N   TYR B  71     -17.751 -36.333 -35.540  1.00105.40           N  
ANISOU 6187  N   TYR B  71    13952  12761  13334    230   -459    -39       N  
ATOM   6188  CA  TYR B  71     -19.031 -36.316 -34.810  1.00107.43           C  
ANISOU 6188  CA  TYR B  71    14168  13030  13619    212   -482    -49       C  
ATOM   6189  C   TYR B  71     -18.882 -36.473 -33.286  1.00108.69           C  
ANISOU 6189  C   TYR B  71    14286  13203  13807    203   -458    -33       C  
ATOM   6190  O   TYR B  71     -19.878 -36.666 -32.583  1.00107.27           O  
ANISOU 6190  O   TYR B  71    14073  13032  13652    186   -471    -40       O  
ATOM   6191  CB  TYR B  71     -20.010 -37.373 -35.353  1.00107.74           C  
ANISOU 6191  CB  TYR B  71    14217  13053  13665    196   -505    -73       C  
ATOM   6192  CG  TYR B  71     -20.220 -37.366 -36.856  1.00110.21           C  
ANISOU 6192  CG  TYR B  71    14572  13350  13950    204   -530    -92       C  
ATOM   6193  CD1 TYR B  71     -19.437 -38.168 -37.692  1.00112.27           C  
ANISOU 6193  CD1 TYR B  71    14876  13588  14190    210   -515    -93       C  
ATOM   6194  CD2 TYR B  71     -21.221 -36.586 -37.443  1.00108.87           C  
ANISOU 6194  CD2 TYR B  71    14400  13191  13775    205   -569   -108       C  
ATOM   6195  CE1 TYR B  71     -19.627 -38.177 -39.068  1.00110.48           C  
ANISOU 6195  CE1 TYR B  71    14690  13349  13938    218   -538   -111       C  
ATOM   6196  CE2 TYR B  71     -21.420 -36.593 -38.819  1.00107.53           C  
ANISOU 6196  CE2 TYR B  71    14269  13008  13578    213   -593   -125       C  
ATOM   6197  CZ  TYR B  71     -20.620 -37.389 -39.625  1.00106.78           C  
ANISOU 6197  CZ  TYR B  71    14217  12890  13463    219   -577   -126       C  
ATOM   6198  OH  TYR B  71     -20.804 -37.408 -40.986  1.00101.80           O  
ANISOU 6198  OH  TYR B  71    13626  12246  12804    227   -600   -143       O  
ATOM   6199  N   SER B  72     -17.645 -36.397 -32.788  1.00110.56           N  
ANISOU 6199  N   SER B  72    14524  13443  14039    213   -423    -11       N  
ATOM   6200  CA  SER B  72     -17.355 -36.475 -31.348  1.00106.87           C  
ANISOU 6200  CA  SER B  72    14019  12990  13595    206   -398      6       C  
ATOM   6201  C   SER B  72     -17.936 -35.271 -30.613  1.00106.53           C  
ANISOU 6201  C   SER B  72    13939  12973  13563    205   -412      9       C  
ATOM   6202  O   SER B  72     -18.445 -35.395 -29.497  1.00103.62           O  
ANISOU 6202  O   SER B  72    13532  12616  13220    193   -409     13       O  
ATOM   6203  CB  SER B  72     -15.847 -36.560 -31.096  1.00106.10           C  
ANISOU 6203  CB  SER B  72    13934  12892  13486    220   -359     29       C  
ATOM   6204  OG  SER B  72     -15.297 -37.743 -31.650  1.00104.48           O  
ANISOU 6204  OG  SER B  72    13760  12662  13272    220   -343     28       O  
ATOM   6205  N   PHE B  73     -17.839 -34.107 -31.248  1.00106.19           N  
ANISOU 6205  N   PHE B  73    13908  12937  13501    219   -426      8       N  
ATOM   6206  CA  PHE B  73     -18.527 -32.910 -30.794  1.00106.23           C  
ANISOU 6206  CA  PHE B  73    13883  12963  13514    220   -444      7       C  
ATOM   6207  C   PHE B  73     -19.654 -32.671 -31.790  1.00107.87           C  
ANISOU 6207  C   PHE B  73    14102  13166  13715    218   -484    -14       C  
ATOM   6208  O   PHE B  73     -19.413 -32.261 -32.933  1.00110.12           O  
ANISOU 6208  O   PHE B  73    14422  13444  13975    231   -495    -20       O  
ATOM   6209  CB  PHE B  73     -17.574 -31.710 -30.752  1.00107.67           C  
ANISOU 6209  CB  PHE B  73    14069  13158  13680    237   -429     24       C  
ATOM   6210  CG  PHE B  73     -16.316 -31.946 -29.952  1.00106.40           C  
ANISOU 6210  CG  PHE B  73    13904  13002  13522    241   -390     46       C  
ATOM   6211  CD1 PHE B  73     -16.277 -31.665 -28.590  1.00103.35           C  
ANISOU 6211  CD1 PHE B  73    13477  12634  13157    235   -376     59       C  
ATOM   6212  CD2 PHE B  73     -15.163 -32.433 -30.567  1.00107.04           C  
ANISOU 6212  CD2 PHE B  73    14019  13067  13584    252   -367     54       C  
ATOM   6213  CE1 PHE B  73     -15.118 -31.876 -27.856  1.00106.02           C  
ANISOU 6213  CE1 PHE B  73    13809  12976  13495    239   -341     79       C  
ATOM   6214  CE2 PHE B  73     -14.002 -32.647 -29.837  1.00104.05           C  
ANISOU 6214  CE2 PHE B  73    13634  12693  13208    256   -332     75       C  
ATOM   6215  CZ  PHE B  73     -13.979 -32.368 -28.480  1.00104.82           C  
ANISOU 6215  CZ  PHE B  73    13691  12810  13325    250   -319     87       C  
ATOM   6216  N   SER B  74     -20.881 -32.955 -31.364  1.00103.37           N  
ANISOU 6216  N   SER B  74    13505  12602  13169    201   -505    -27       N  
ATOM   6217  CA  SER B  74     -22.019 -32.941 -32.274  1.00102.79           C  
ANISOU 6217  CA  SER B  74    13441  12523  13091    197   -544    -50       C  
ATOM   6218  C   SER B  74     -23.305 -32.511 -31.573  1.00103.44           C  
ANISOU 6218  C   SER B  74    13481  12621  13198    184   -567    -58       C  
ATOM   6219  O   SER B  74     -24.084 -31.726 -32.119  1.00 99.73           O  
ANISOU 6219  O   SER B  74    13010  12159  12723    189   -597    -69       O  
ATOM   6220  CB  SER B  74     -22.188 -34.323 -32.914  1.00101.39           C  
ANISOU 6220  CB  SER B  74    13288  12322  12913    187   -548    -65       C  
ATOM   6221  OG  SER B  74     -22.921 -34.250 -34.122  1.00102.01           O  
ANISOU 6221  OG  SER B  74    13389  12392  12976    188   -582    -86       O  
ATOM   6222  N   ASN B  75     -23.514 -33.023 -30.364  1.00104.34           N  
ANISOU 6222  N   ASN B  75    13561  12741  13340    170   -552    -51       N  
ATOM   6223  CA  ASN B  75     -24.720 -32.727 -29.595  1.00106.44           C  
ANISOU 6223  CA  ASN B  75    13785  13022  13634    157   -571    -58       C  
ATOM   6224  C   ASN B  75     -24.750 -31.302 -29.042  1.00107.24           C  
ANISOU 6224  C   ASN B  75    13864  13147  13736    167   -572    -47       C  
ATOM   6225  O   ASN B  75     -25.822 -30.718 -28.893  1.00109.06           O  
ANISOU 6225  O   ASN B  75    14070  13389  13979    162   -597    -56       O  
ATOM   6226  CB  ASN B  75     -24.907 -33.751 -28.464  1.00107.76           C  
ANISOU 6226  CB  ASN B  75    13924  13187  13830    139   -552    -53       C  
ATOM   6227  CG  ASN B  75     -25.333 -35.126 -28.970  1.00107.16           C  
ANISOU 6227  CG  ASN B  75    13864  13090  13761    125   -559    -69       C  
ATOM   6228  OD1 ASN B  75     -24.697 -36.137 -28.662  1.00105.46           O  
ANISOU 6228  OD1 ASN B  75    13657  12863  13550    120   -533    -62       O  
ATOM   6229  ND2 ASN B  75     -26.415 -35.170 -29.743  1.00102.67           N  
ANISOU 6229  ND2 ASN B  75    13299  12517  13193    119   -595    -91       N  
ATOM   6230  N   PHE B  76     -23.573 -30.747 -28.757  1.00111.15           N  
ANISOU 6230  N   PHE B  76    14366  13648  14218    180   -545    -28       N  
ATOM   6231  CA  PHE B  76     -23.453 -29.428 -28.123  1.00112.11           C  
ANISOU 6231  CA  PHE B  76    14465  13790  14340    189   -541    -16       C  
ATOM   6232  C   PHE B  76     -23.478 -28.278 -29.134  1.00113.30           C  
ANISOU 6232  C   PHE B  76    14637  13943  14466    206   -560    -21       C  
ATOM   6233  O   PHE B  76     -22.433 -27.705 -29.458  1.00114.34           O  
ANISOU 6233  O   PHE B  76    14790  14075  14577    221   -544    -10       O  
ATOM   6234  CB  PHE B  76     -22.169 -29.348 -27.287  1.00109.11           C  
ANISOU 6234  CB  PHE B  76    14081  13416  13958    195   -502      5       C  
ATOM   6235  CG  PHE B  76     -21.945 -30.529 -26.384  1.00109.00           C  
ANISOU 6235  CG  PHE B  76    14053  13398  13964    181   -479     12       C  
ATOM   6236  CD1 PHE B  76     -22.678 -30.680 -25.210  1.00108.18           C  
ANISOU 6236  CD1 PHE B  76    13908  13306  13888    167   -478     13       C  
ATOM   6237  CD2 PHE B  76     -20.983 -31.484 -26.698  1.00109.89           C  
ANISOU 6237  CD2 PHE B  76    14191  13494  14065    184   -457     18       C  
ATOM   6238  CE1 PHE B  76     -22.463 -31.766 -24.374  1.00107.73           C  
ANISOU 6238  CE1 PHE B  76    13838  13245  13849    156   -456     21       C  
ATOM   6239  CE2 PHE B  76     -20.764 -32.573 -25.865  1.00109.41           C  
ANISOU 6239  CE2 PHE B  76    14118  13430  14023    173   -435     25       C  
ATOM   6240  CZ  PHE B  76     -21.506 -32.713 -24.702  1.00108.29           C  
ANISOU 6240  CZ  PHE B  76    13936  13300  13909    159   -434     27       C  
ATOM   6241  N   SER B  77     -24.675 -27.930 -29.605  1.00113.39           N  
ANISOU 6241  N   SER B  77    14641  13958  14482    203   -595    -37       N  
ATOM   6242  CA  SER B  77     -24.844 -26.903 -30.643  1.00114.09           C  
ANISOU 6242  CA  SER B  77    14751  14048  14548    219   -617    -43       C  
ATOM   6243  C   SER B  77     -24.597 -25.472 -30.155  1.00113.46           C  
ANISOU 6243  C   SER B  77    14655  13987  14465    230   -610    -31       C  
ATOM   6244  O   SER B  77     -24.424 -24.555 -30.967  1.00112.26           O  
ANISOU 6244  O   SER B  77    14525  13836  14292    247   -620    -31       O  
ATOM   6245  CB  SER B  77     -26.235 -27.005 -31.283  1.00112.92           C  
ANISOU 6245  CB  SER B  77    14599  13899  14406    212   -658    -65       C  
ATOM   6246  OG  SER B  77     -27.243 -26.527 -30.408  1.00108.69           O  
ANISOU 6246  OG  SER B  77    14021  13380  13895    203   -670    -66       O  
ATOM   6247  N   GLU B  78     -24.577 -25.284 -28.837  1.00111.44           N  
ANISOU 6247  N   GLU B  78    14363  13745  14231    222   -593    -19       N  
ATOM   6248  CA  GLU B  78     -24.451 -23.946 -28.254  1.00110.88           C  
ANISOU 6248  CA  GLU B  78    14273  13692  14161    231   -586     -8       C  
ATOM   6249  C   GLU B  78     -23.189 -23.754 -27.399  1.00107.07           C  
ANISOU 6249  C   GLU B  78    13786  13216  13678    235   -548     11       C  
ATOM   6250  O   GLU B  78     -23.208 -23.029 -26.399  1.00109.32           O  
ANISOU 6250  O   GLU B  78    14042  13517  13975    233   -538     20       O  
ATOM   6251  CB  GLU B  78     -25.717 -23.589 -27.463  1.00110.08           C  
ANISOU 6251  CB  GLU B  78    14131  13605  14086    220   -604    -14       C  
ATOM   6252  CG  GLU B  78     -26.918 -23.253 -28.336  1.00107.45           C  
ANISOU 6252  CG  GLU B  78    13801  13272  13751    222   -643    -31       C  
ATOM   6253  CD  GLU B  78     -28.242 -23.617 -27.691  1.00106.02           C  
ANISOU 6253  CD  GLU B  78    13584  13099  13601    205   -661    -41       C  
ATOM   6254  OE1 GLU B  78     -28.243 -24.318 -26.656  1.00106.94           O  
ANISOU 6254  OE1 GLU B  78    13676  13217  13739    191   -644    -36       O  
ATOM   6255  OE2 GLU B  78     -29.289 -23.205 -28.229  1.00104.56           O  
ANISOU 6255  OE2 GLU B  78    13393  12916  13417    207   -693    -54       O  
ATOM   6256  N   LEU B  79     -22.096 -24.396 -27.805  1.00 98.09           N  
ANISOU 6256  N   LEU B  79    12677  12065  12525    240   -528     17       N  
ATOM   6257  CA  LEU B  79     -20.812 -24.231 -27.132  1.00 90.34           C  
ANISOU 6257  CA  LEU B  79    11695  11089  11540    245   -493     36       C  
ATOM   6258  C   LEU B  79     -20.121 -22.949 -27.597  1.00 89.03           C  
ANISOU 6258  C   LEU B  79    11545  10928  11352    262   -487     44       C  
ATOM   6259  O   LEU B  79     -20.290 -22.531 -28.742  1.00 92.50           O  
ANISOU 6259  O   LEU B  79    12012  11359  11773    274   -505     35       O  
ATOM   6260  CB  LEU B  79     -19.911 -25.440 -27.385  1.00 84.37           C  
ANISOU 6260  CB  LEU B  79    10962  10316  10776    243   -472     41       C  
ATOM   6261  CG  LEU B  79     -18.873 -25.729 -26.302  1.00 80.93           C  
ANISOU 6261  CG  LEU B  79    10512   9888  10348    241   -436     59       C  
ATOM   6262  CD1 LEU B  79     -19.525 -26.421 -25.114  1.00 80.38           C  
ANISOU 6262  CD1 LEU B  79    10406   9827  10308    223   -433     60       C  
ATOM   6263  CD2 LEU B  79     -17.749 -26.581 -26.860  1.00 80.16           C  
ANISOU 6263  CD2 LEU B  79    10447   9774  10235    247   -415     66       C  
ATOM   6264  N   GLN B  80     -19.349 -22.330 -26.706  1.00 84.03           N  
ANISOU 6264  N   GLN B  80    10896  10308  10723    265   -462     59       N  
ATOM   6265  CA  GLN B  80     -18.627 -21.097 -27.023  1.00 78.21           C  
ANISOU 6265  CA  GLN B  80    10171   9575   9968    281   -453     68       C  
ATOM   6266  C   GLN B  80     -17.139 -21.201 -26.719  1.00 71.63           C  
ANISOU 6266  C   GLN B  80     9347   8741   9126    286   -419     84       C  
ATOM   6267  O   GLN B  80     -16.315 -20.595 -27.406  1.00 69.25           O  
ANISOU 6267  O   GLN B  80     9072   8435   8804    301   -409     90       O  
ATOM   6268  CB  GLN B  80     -19.227 -19.908 -26.268  1.00 81.64           C  
ANISOU 6268  CB  GLN B  80    10574  10029  10415    280   -460     69       C  
ATOM   6269  CG  GLN B  80     -20.468 -19.317 -26.917  1.00 85.25           C  
ANISOU 6269  CG  GLN B  80    11031  10486  10872    283   -494     54       C  
ATOM   6270  CD  GLN B  80     -21.193 -18.338 -26.016  1.00 84.34           C  
ANISOU 6270  CD  GLN B  80    10881  10390  10774    279   -500     55       C  
ATOM   6271  OE1 GLN B  80     -20.633 -17.320 -25.602  1.00 85.02           O  
ANISOU 6271  OE1 GLN B  80    10960  10486  10856    286   -485     65       O  
ATOM   6272  NE2 GLN B  80     -22.451 -18.635 -25.715  1.00 82.10           N  
ANISOU 6272  NE2 GLN B  80    10573  10110  10509    268   -523     45       N  
ATOM   6273  N   TRP B  81     -16.804 -21.979 -25.696  1.00 67.29           N  
ANISOU 6273  N   TRP B  81     8777   8196   8591    275   -399     93       N  
ATOM   6274  CA  TRP B  81     -15.439 -22.060 -25.199  1.00 66.98           C  
ANISOU 6274  CA  TRP B  81     8740   8161   8548    279   -366    110       C  
ATOM   6275  C   TRP B  81     -15.049 -23.495 -24.975  1.00 67.18           C  
ANISOU 6275  C   TRP B  81     8769   8177   8579    271   -351    113       C  
ATOM   6276  O   TRP B  81     -15.560 -24.152 -24.060  1.00 69.02           O  
ANISOU 6276  O   TRP B  81     8975   8415   8832    258   -350    113       O  
ATOM   6277  CB  TRP B  81     -15.322 -21.244 -23.911  1.00 65.57           C  
ANISOU 6277  CB  TRP B  81     8525   8004   8383    275   -353    119       C  
ATOM   6278  CG  TRP B  81     -13.920 -21.052 -23.375  1.00 66.95           C  
ANISOU 6278  CG  TRP B  81     8699   8185   8552    280   -321    137       C  
ATOM   6279  CD1 TRP B  81     -13.005 -20.054 -23.718  1.00 65.77           C  
ANISOU 6279  CD1 TRP B  81     8563   8038   8386    292   -308    145       C  
ATOM   6280  CD2 TRP B  81     -13.238 -21.855 -22.343  1.00 67.30           C  
ANISOU 6280  CD2 TRP B  81     8726   8236   8608    272   -295    149       C  
ATOM   6281  NE1 TRP B  81     -11.839 -20.191 -23.006  1.00 66.19           N  
ANISOU 6281  NE1 TRP B  81     8609   8098   8440    292   -278    160       N  
ATOM   6282  CE2 TRP B  81     -11.910 -21.249 -22.163  1.00 67.80           C  
ANISOU 6282  CE2 TRP B  81     8794   8306   8660    281   -270    164       C  
ATOM   6283  CE3 TRP B  81     -13.581 -22.973 -21.579  1.00 65.05           C  
ANISOU 6283  CE3 TRP B  81     8422   7952   8339    259   -291    150       C  
ATOM   6284  CZ2 TRP B  81     -10.983 -21.761 -21.257  1.00 67.65           C  
ANISOU 6284  CZ2 TRP B  81     8761   8295   8646    278   -243    179       C  
ATOM   6285  CZ3 TRP B  81     -12.637 -23.479 -20.672  1.00 63.12           C  
ANISOU 6285  CZ3 TRP B  81     8165   7715   8100    257   -263    166       C  
ATOM   6286  CH2 TRP B  81     -11.373 -22.886 -20.515  1.00 65.51           C  
ANISOU 6286  CH2 TRP B  81     8473   8026   8392    266   -240    180       C  
ATOM   6287  N   LEU B  82     -14.148 -23.993 -25.824  1.00 66.75           N  
ANISOU 6287  N   LEU B  82     8749   8106   8506    280   -339    117       N  
ATOM   6288  CA  LEU B  82     -13.608 -25.355 -25.705  1.00 65.71           C  
ANISOU 6288  CA  LEU B  82     8625   7963   8377    275   -321    123       C  
ATOM   6289  C   LEU B  82     -12.102 -25.357 -25.434  1.00 64.72           C  
ANISOU 6289  C   LEU B  82     8507   7839   8242    284   -287    141       C  
ATOM   6290  O   LEU B  82     -11.325 -24.732 -26.168  1.00 63.87           O  
ANISOU 6290  O   LEU B  82     8424   7727   8116    298   -280    146       O  
ATOM   6291  CB  LEU B  82     -13.931 -26.188 -26.956  1.00 65.10           C  
ANISOU 6291  CB  LEU B  82     8583   7863   8288    277   -336    109       C  
ATOM   6292  CG  LEU B  82     -13.448 -27.645 -27.031  1.00 64.50           C  
ANISOU 6292  CG  LEU B  82     8522   7771   8213    273   -320    113       C  
ATOM   6293  CD1 LEU B  82     -13.927 -28.473 -25.847  1.00 63.01           C  
ANISOU 6293  CD1 LEU B  82     8300   7590   8050    256   -314    115       C  
ATOM   6294  CD2 LEU B  82     -13.884 -28.297 -28.334  1.00 64.16           C  
ANISOU 6294  CD2 LEU B  82     8514   7706   8157    275   -339     97       C  
ATOM   6295  N   ASP B  83     -11.706 -26.075 -24.384  1.00 63.84           N  
ANISOU 6295  N   ASP B  83     8375   7736   8146    276   -267    152       N  
ATOM   6296  CA  ASP B  83     -10.311 -26.141 -23.954  1.00 63.31           C  
ANISOU 6296  CA  ASP B  83     8308   7673   8073    282   -234    171       C  
ATOM   6297  C   ASP B  83      -9.793 -27.581 -23.998  1.00 62.10           C  
ANISOU 6297  C   ASP B  83     8168   7505   7920    280   -217    177       C  
ATOM   6298  O   ASP B  83     -10.233 -28.446 -23.236  1.00 61.26           O  
ANISOU 6298  O   ASP B  83     8042   7401   7831    269   -215    177       O  
ATOM   6299  CB  ASP B  83     -10.158 -25.540 -22.549  1.00 63.36           C  
ANISOU 6299  CB  ASP B  83     8275   7704   8094    277   -222    182       C  
ATOM   6300  CG  ASP B  83      -8.729 -25.108 -22.236  1.00 64.71           C  
ANISOU 6300  CG  ASP B  83     8447   7883   8256    286   -194    199       C  
ATOM   6301  OD1 ASP B  83      -7.777 -25.872 -22.527  1.00 65.00           O  
ANISOU 6301  OD1 ASP B  83     8502   7909   8284    292   -174    209       O  
ATOM   6302  OD2 ASP B  83      -8.562 -24.001 -21.675  1.00 64.86           O  
ANISOU 6302  OD2 ASP B  83     8447   7920   8277    287   -191    204       O  
ATOM   6303  N   LEU B  84      -8.851 -27.821 -24.902  1.00 62.18           N  
ANISOU 6303  N   LEU B  84     8212   7501   7912    292   -204    182       N  
ATOM   6304  CA  LEU B  84      -8.293 -29.149 -25.111  1.00 63.54           C  
ANISOU 6304  CA  LEU B  84     8402   7656   8082    293   -186    188       C  
ATOM   6305  C   LEU B  84      -6.777 -29.104 -24.973  1.00 65.23           C  
ANISOU 6305  C   LEU B  84     8623   7873   8286    304   -154    207       C  
ATOM   6306  O   LEU B  84      -6.053 -29.762 -25.724  1.00 67.03           O  
ANISOU 6306  O   LEU B  84     8882   8084   8502    312   -140    212       O  
ATOM   6307  CB  LEU B  84      -8.682 -29.669 -26.501  1.00 62.99           C  
ANISOU 6307  CB  LEU B  84     8372   7563   7998    296   -202    173       C  
ATOM   6308  CG  LEU B  84     -10.167 -29.677 -26.875  1.00 62.18           C  
ANISOU 6308  CG  LEU B  84     8266   7455   7902    287   -237    152       C  
ATOM   6309  CD1 LEU B  84     -10.345 -29.838 -28.378  1.00 60.66           C  
ANISOU 6309  CD1 LEU B  84     8116   7241   7689    295   -253    138       C  
ATOM   6310  CD2 LEU B  84     -10.921 -30.754 -26.104  1.00 62.01           C  
ANISOU 6310  CD2 LEU B  84     8223   7434   7904    270   -240    147       C  
ATOM   6311  N   SER B  85      -6.302 -28.323 -24.009  1.00 66.74           N  
ANISOU 6311  N   SER B  85     8787   8086   8484    304   -142    219       N  
ATOM   6312  CA  SER B  85      -4.867 -28.113 -23.831  1.00 68.29           C  
ANISOU 6312  CA  SER B  85     8986   8288   8671    314   -113    238       C  
ATOM   6313  C   SER B  85      -4.179 -29.368 -23.301  1.00 66.19           C  
ANISOU 6313  C   SER B  85     8717   8019   8412    313    -88    251       C  
ATOM   6314  O   SER B  85      -4.731 -30.078 -22.463  1.00 68.14           O  
ANISOU 6314  O   SER B  85     8942   8271   8676    302    -89    251       O  
ATOM   6315  CB  SER B  85      -4.608 -26.920 -22.908  1.00 69.37           C  
ANISOU 6315  CB  SER B  85     9092   8450   8814    313   -108    245       C  
ATOM   6316  OG  SER B  85      -5.324 -25.778 -23.349  1.00 67.36           O  
ANISOU 6316  OG  SER B  85     8839   8198   8555    314   -131    232       O  
ATOM   6317  N   ARG B  86      -2.973 -29.624 -23.799  1.00 66.55           N  
ANISOU 6317  N   ARG B  86     8785   8055   8444    325    -65    264       N  
ATOM   6318  CA  ARG B  86      -2.195 -30.832 -23.474  1.00 71.35           C  
ANISOU 6318  CA  ARG B  86     9396   8658   9056    327    -39    278       C  
ATOM   6319  C   ARG B  86      -3.065 -32.107 -23.374  1.00 75.75           C  
ANISOU 6319  C   ARG B  86     9954   9202   9624    316    -47    270       C  
ATOM   6320  O   ARG B  86      -3.211 -32.720 -22.305  1.00 71.64           O  
ANISOU 6320  O   ARG B  86     9407   8691   9120    308    -38    277       O  
ATOM   6321  CB  ARG B  86      -1.298 -30.607 -22.243  1.00 65.23           C  
ANISOU 6321  CB  ARG B  86     8589   7905   8288    327    -15    297       C  
ATOM   6322  CG  ARG B  86      -0.296 -31.723 -21.998  1.00 65.09           C  
ANISOU 6322  CG  ARG B  86     8577   7883   8271    333     13    315       C  
ATOM   6323  CD  ARG B  86       1.104 -31.207 -21.721  1.00 67.10           C  
ANISOU 6323  CD  ARG B  86     8826   8150   8519    344     38    334       C  
ATOM   6324  NE  ARG B  86       2.004 -31.403 -22.859  1.00 69.09           N  
ANISOU 6324  NE  ARG B  86     9114   8383   8754    358     52    339       N  
ATOM   6325  CZ  ARG B  86       2.663 -30.437 -23.498  1.00 73.41           C  
ANISOU 6325  CZ  ARG B  86     9675   8930   9287    368     56    341       C  
ATOM   6326  NH1 ARG B  86       2.553 -29.169 -23.125  1.00 73.48           N  
ANISOU 6326  NH1 ARG B  86     9665   8957   9298    365     47    338       N  
ATOM   6327  NH2 ARG B  86       3.453 -30.741 -24.518  1.00 80.00           N  
ANISOU 6327  NH2 ARG B  86    10543   9744  10106    380     70    346       N  
ATOM   6328  N   CYS B  87      -3.639 -32.483 -24.515  1.00 75.99           N  
ANISOU 6328  N   CYS B  87    10015   9209   9645    317    -63    254       N  
ATOM   6329  CA  CYS B  87      -4.547 -33.617 -24.595  1.00 75.25           C  
ANISOU 6329  CA  CYS B  87     9926   9101   9562    306    -74    243       C  
ATOM   6330  C   CYS B  87      -4.033 -34.753 -25.466  1.00 77.03           C  
ANISOU 6330  C   CYS B  87    10188   9301   9777    312    -60    244       C  
ATOM   6331  O   CYS B  87      -4.821 -35.542 -25.998  1.00 77.01           O  
ANISOU 6331  O   CYS B  87    10201   9280   9777    305    -74    229       O  
ATOM   6332  CB  CYS B  87      -5.912 -33.155 -25.076  1.00 72.25           C  
ANISOU 6332  CB  CYS B  87     9547   8718   9184    298   -109    220       C  
ATOM   6333  SG  CYS B  87      -6.903 -32.541 -23.712  1.00 73.69           S  
ANISOU 6333  SG  CYS B  87     9680   8927   9390    283   -124    217       S  
ATOM   6334  N   GLU B  88      -2.711 -34.824 -25.611  1.00 78.75           N  
ANISOU 6334  N   GLU B  88    10419   9517   9984    326    -32    261       N  
ATOM   6335  CA  GLU B  88      -2.053 -35.920 -26.322  1.00 82.02           C  
ANISOU 6335  CA  GLU B  88    10866   9907  10388    333    -13    266       C  
ATOM   6336  C   GLU B  88      -2.502 -36.077 -27.786  1.00 78.65           C  
ANISOU 6336  C   GLU B  88    10482   9456   9946    337    -31    248       C  
ATOM   6337  O   GLU B  88      -2.207 -37.094 -28.418  1.00 79.95           O  
ANISOU 6337  O   GLU B  88    10675   9598  10104    340    -20    248       O  
ATOM   6338  CB  GLU B  88      -2.278 -37.231 -25.555  1.00 86.45           C  
ANISOU 6338  CB  GLU B  88    11414  10464  10967    324     -1    271       C  
ATOM   6339  CG  GLU B  88      -1.501 -37.354 -24.254  1.00 88.63           C  
ANISOU 6339  CG  GLU B  88    11658  10762  11256    325     23    293       C  
ATOM   6340  CD  GLU B  88      -0.273 -38.235 -24.396  1.00 93.91           C  
ANISOU 6340  CD  GLU B  88    12344  11419  11918    336     57    311       C  
ATOM   6341  OE1 GLU B  88       0.007 -39.013 -23.457  1.00 98.56           O  
ANISOU 6341  OE1 GLU B  88    12914  12014  12520    334     76    325       O  
ATOM   6342  OE2 GLU B  88       0.404 -38.165 -25.446  1.00 92.83           O  
ANISOU 6342  OE2 GLU B  88    12240  11266  11762    349     64    312       O  
ATOM   6343  N   ILE B  89      -3.197 -35.070 -28.317  1.00 75.40           N  
ANISOU 6343  N   ILE B  89    10073   9047   9526    336    -58    233       N  
ATOM   6344  CA  ILE B  89      -3.825 -35.156 -29.642  1.00 74.74           C  
ANISOU 6344  CA  ILE B  89    10026   8943   9428    338    -81    214       C  
ATOM   6345  C   ILE B  89      -2.818 -35.128 -30.799  1.00 76.42           C  
ANISOU 6345  C   ILE B  89    10281   9138   9616    355    -66    219       C  
ATOM   6346  O   ILE B  89      -2.007 -34.204 -30.908  1.00 71.68           O  
ANISOU 6346  O   ILE B  89     9682   8546   9005    367    -55    230       O  
ATOM   6347  CB  ILE B  89      -4.932 -34.092 -29.841  1.00 72.66           C  
ANISOU 6347  CB  ILE B  89     9753   8689   9164    333   -116    196       C  
ATOM   6348  CG1 ILE B  89      -6.045 -34.278 -28.805  1.00 71.62           C  
ANISOU 6348  CG1 ILE B  89     9582   8571   9057    315   -132    189       C  
ATOM   6349  CG2 ILE B  89      -5.526 -34.189 -31.241  1.00 71.93           C  
ANISOU 6349  CG2 ILE B  89     9699   8576   9054    336   -139    177       C  
ATOM   6350  CD1 ILE B  89      -7.059 -33.153 -28.759  1.00 73.70           C  
ANISOU 6350  CD1 ILE B  89     9829   8848   9324    310   -162    176       C  
ATOM   6351  N   GLU B  90      -2.892 -36.153 -31.653  1.00 80.05           N  
ANISOU 6351  N   GLU B  90    10774   9572  10067    357    -65    211       N  
ATOM   6352  CA  GLU B  90      -2.025 -36.289 -32.826  1.00 79.20           C  
ANISOU 6352  CA  GLU B  90    10710   9444   9936    373    -51    214       C  
ATOM   6353  C   GLU B  90      -2.765 -36.176 -34.155  1.00 78.92           C  
ANISOU 6353  C   GLU B  90    10711   9391   9882    375    -78    192       C  
ATOM   6354  O   GLU B  90      -2.158 -35.841 -35.178  1.00 83.17           O  
ANISOU 6354  O   GLU B  90    11283   9917  10398    390    -73    193       O  
ATOM   6355  CB  GLU B  90      -1.260 -37.609 -32.779  1.00 81.64           C  
ANISOU 6355  CB  GLU B  90    11034   9737  10246    375    -21    225       C  
ATOM   6356  CG  GLU B  90       0.204 -37.454 -32.414  1.00 85.27           C  
ANISOU 6356  CG  GLU B  90    11490  10204  10703    389     14    251       C  
ATOM   6357  CD  GLU B  90       0.734 -38.628 -31.622  1.00 86.90           C  
ANISOU 6357  CD  GLU B  90    11684  10408  10924    386     41    266       C  
ATOM   6358  OE1 GLU B  90      -0.002 -39.138 -30.751  1.00 88.19           O  
ANISOU 6358  OE1 GLU B  90    11820  10579  11107    371     34    262       O  
ATOM   6359  OE2 GLU B  90       1.892 -39.032 -31.859  1.00 90.22           O  
ANISOU 6359  OE2 GLU B  90    12122  10820  11336    399     71    282       O  
ATOM   6360  N   THR B  91      -4.064 -36.471 -34.145  1.00 75.90           N  
ANISOU 6360  N   THR B  91    10321   9007   9509    360   -107    172       N  
ATOM   6361  CA  THR B  91      -4.874 -36.418 -35.362  1.00 74.96           C  
ANISOU 6361  CA  THR B  91    10233   8872   9374    361   -137    150       C  
ATOM   6362  C   THR B  91      -6.249 -35.820 -35.097  1.00 73.76           C  
ANISOU 6362  C   THR B  91    10057   8734   9234    348   -173    132       C  
ATOM   6363  O   THR B  91      -6.965 -36.249 -34.186  1.00 73.77           O  
ANISOU 6363  O   THR B  91    10026   8744   9258    332   -180    129       O  
ATOM   6364  CB  THR B  91      -5.044 -37.813 -36.011  1.00 77.77           C  
ANISOU 6364  CB  THR B  91    10620   9201   9726    357   -134    139       C  
ATOM   6365  OG1 THR B  91      -3.792 -38.515 -36.007  1.00 81.58           O  
ANISOU 6365  OG1 THR B  91    11120   9673  10204    367    -97    157       O  
ATOM   6366  CG2 THR B  91      -5.533 -37.683 -37.450  1.00 78.15           C  
ANISOU 6366  CG2 THR B  91    10709   9231   9750    362   -159    119       C  
ATOM   6367  N   ILE B  92      -6.601 -34.814 -35.893  1.00 74.89           N  
ANISOU 6367  N   ILE B  92    10214   8879   9360    356   -196    123       N  
ATOM   6368  CA  ILE B  92      -7.961 -34.293 -35.924  1.00 77.37           C  
ANISOU 6368  CA  ILE B  92    10513   9202   9681    346   -233    104       C  
ATOM   6369  C   ILE B  92      -8.656 -34.928 -37.119  1.00 80.16           C  
ANISOU 6369  C   ILE B  92    10901   9533  10019    344   -257     82       C  
ATOM   6370  O   ILE B  92      -8.285 -34.683 -38.267  1.00 79.42           O  
ANISOU 6370  O   ILE B  92    10847   9427   9900    359   -259     78       O  
ATOM   6371  CB  ILE B  92      -8.009 -32.755 -36.068  1.00 77.93           C  
ANISOU 6371  CB  ILE B  92    10576   9289   9742    356   -246    105       C  
ATOM   6372  CG1 ILE B  92      -7.073 -32.075 -35.061  1.00 78.36           C  
ANISOU 6372  CG1 ILE B  92    10604   9363   9806    361   -219    128       C  
ATOM   6373  CG2 ILE B  92      -9.442 -32.247 -35.920  1.00 75.49           C  
ANISOU 6373  CG2 ILE B  92    10245   8992   9444    345   -283     88       C  
ATOM   6374  CD1 ILE B  92      -6.681 -30.664 -35.449  1.00 78.17           C  
ANISOU 6374  CD1 ILE B  92    10585   9348   9766    375   -220    133       C  
ATOM   6375  N   GLU B  93      -9.653 -35.759 -36.842  1.00 86.08           N  
ANISOU 6375  N   GLU B  93    11638  10279  10786    327   -274     67       N  
ATOM   6376  CA  GLU B  93     -10.409 -36.416 -37.894  1.00 92.45           C  
ANISOU 6376  CA  GLU B  93    12477  11067  11582    322   -298     44       C  
ATOM   6377  C   GLU B  93     -11.218 -35.365 -38.639  1.00 97.37           C  
ANISOU 6377  C   GLU B  93    13107  11697  12192    328   -333     29       C  
ATOM   6378  O   GLU B  93     -11.648 -34.364 -38.056  1.00100.23           O  
ANISOU 6378  O   GLU B  93    13438  12081  12564    326   -346     32       O  
ATOM   6379  CB  GLU B  93     -11.324 -37.485 -37.297  1.00 97.51           C  
ANISOU 6379  CB  GLU B  93    13097  11704  12248    301   -308     33       C  
ATOM   6380  CG  GLU B  93     -11.529 -38.711 -38.171  1.00101.35           C  
ANISOU 6380  CG  GLU B  93    13618  12164  12725    296   -312     17       C  
ATOM   6381  CD  GLU B  93     -11.617 -39.989 -37.355  1.00102.93           C  
ANISOU 6381  CD  GLU B  93    13802  12356  12949    280   -295     19       C  
ATOM   6382  OE1 GLU B  93     -10.552 -40.508 -36.952  1.00 98.55           O  
ANISOU 6382  OE1 GLU B  93    13251  11796  12396    285   -259     38       O  
ATOM   6383  OE2 GLU B  93     -12.744 -40.479 -37.121  1.00105.01           O  
ANISOU 6383  OE2 GLU B  93    14048  12619  13231    262   -317      2       O  
ATOM   6384  N   ASP B  94     -11.398 -35.585 -39.934  1.00 99.78           N  
ANISOU 6384  N   ASP B  94    13453  11984  12473    334   -349     14       N  
ATOM   6385  CA  ASP B  94     -12.150 -34.665 -40.762  1.00101.48           C  
ANISOU 6385  CA  ASP B  94    13680  12205  12673    341   -383      0       C  
ATOM   6386  C   ASP B  94     -13.559 -34.511 -40.194  1.00103.19           C  
ANISOU 6386  C   ASP B  94    13859  12435  12911    323   -416    -14       C  
ATOM   6387  O   ASP B  94     -14.221 -35.506 -39.888  1.00101.30           O  
ANISOU 6387  O   ASP B  94    13609  12189  12689    306   -424    -26       O  
ATOM   6388  CB  ASP B  94     -12.199 -35.183 -42.196  1.00105.03           C  
ANISOU 6388  CB  ASP B  94    14180  12631  13095    348   -395    -15       C  
ATOM   6389  CG  ASP B  94     -11.987 -34.089 -43.215  1.00107.04           C  
ANISOU 6389  CG  ASP B  94    14462  12886  13320    369   -406    -16       C  
ATOM   6390  OD1 ASP B  94     -11.257 -34.346 -44.195  1.00108.93           O  
ANISOU 6390  OD1 ASP B  94    14746  13107  13535    383   -394    -14       O  
ATOM   6391  OD2 ASP B  94     -12.535 -32.978 -43.036  1.00107.38           O  
ANISOU 6391  OD2 ASP B  94    14485  12948  13367    371   -426    -17       O  
ATOM   6392  N   LYS B  95     -13.995 -33.261 -40.039  1.00104.19           N  
ANISOU 6392  N   LYS B  95    13967  12582  13039    328   -433    -13       N  
ATOM   6393  CA  LYS B  95     -15.289 -32.927 -39.419  1.00102.78           C  
ANISOU 6393  CA  LYS B  95    13749  12420  12882    314   -463    -25       C  
ATOM   6394  C   LYS B  95     -15.407 -33.418 -37.969  1.00 98.38           C  
ANISOU 6394  C   LYS B  95    13148  11873  12357    296   -447    -16       C  
ATOM   6395  O   LYS B  95     -16.462 -33.907 -37.551  1.00 92.64           O  
ANISOU 6395  O   LYS B  95    12397  11149  11651    279   -467    -29       O  
ATOM   6396  CB  LYS B  95     -16.468 -33.436 -40.261  1.00104.24           C  
ANISOU 6396  CB  LYS B  95    13949  12595  13063    305   -500    -51       C  
ATOM   6397  CG  LYS B  95     -16.567 -32.834 -41.654  1.00107.33           C  
ANISOU 6397  CG  LYS B  95    14379  12979  13422    322   -522    -62       C  
ATOM   6398  CD  LYS B  95     -17.269 -33.789 -42.610  1.00108.57           C  
ANISOU 6398  CD  LYS B  95    14564  13118  13569    314   -547    -86       C  
ATOM   6399  CE  LYS B  95     -16.378 -34.968 -42.977  1.00104.98           C  
ANISOU 6399  CE  LYS B  95    14142  12639  13105    314   -520    -83       C  
ATOM   6400  NZ  LYS B  95     -17.121 -36.033 -43.703  1.00106.04           N  
ANISOU 6400  NZ  LYS B  95    14298  12756  13236    302   -542   -108       N  
ATOM   6401  N   ALA B  96     -14.318 -33.286 -37.211  1.00 98.14           N  
ANISOU 6401  N   ALA B  96    13106  11848  12332    302   -412      5       N  
ATOM   6402  CA  ALA B  96     -14.335 -33.550 -35.770  1.00100.33           C  
ANISOU 6402  CA  ALA B  96    13340  12139  12638    289   -396     17       C  
ATOM   6403  C   ALA B  96     -15.279 -32.572 -35.067  1.00 98.78           C  
ANISOU 6403  C   ALA B  96    13105  11966  12458    282   -417     14       C  
ATOM   6404  O   ALA B  96     -15.942 -32.921 -34.089  1.00 97.34           O  
ANISOU 6404  O   ALA B  96    12887  11794  12303    266   -421     12       O  
ATOM   6405  CB  ALA B  96     -12.932 -33.452 -35.190  1.00 98.07           C  
ANISOU 6405  CB  ALA B  96    13053  11857  12351    298   -356     42       C  
ATOM   6406  N   TRP B  97     -15.325 -31.348 -35.586  1.00 98.71           N  
ANISOU 6406  N   TRP B  97    13103  11966  12434    295   -431     13       N  
ATOM   6407  CA  TRP B  97     -16.261 -30.335 -35.137  1.00 99.72           C  
ANISOU 6407  CA  TRP B  97    13200  12114  12574    292   -455      8       C  
ATOM   6408  C   TRP B  97     -17.455 -30.389 -36.047  1.00108.90           C  
ANISOU 6408  C   TRP B  97    14375  13271  13731    288   -494    -14       C  
ATOM   6409  O   TRP B  97     -17.366 -30.000 -37.215  1.00112.71           O  
ANISOU 6409  O   TRP B  97    14892  13745  14187    302   -507    -21       O  
ATOM   6410  CB  TRP B  97     -15.625 -28.949 -35.204  1.00 92.23           C  
ANISOU 6410  CB  TRP B  97    12253  11178  11612    309   -446     21       C  
ATOM   6411  CG  TRP B  97     -14.109 -28.928 -35.216  1.00 89.35           C  
ANISOU 6411  CG  TRP B  97    11906  10807  11233    322   -409     41       C  
ATOM   6412  CD1 TRP B  97     -13.271 -28.699 -36.308  1.00 90.02           C  
ANISOU 6412  CD1 TRP B  97    12033  10878  11289    340   -401     44       C  
ATOM   6413  CD2 TRP B  97     -13.197 -29.131 -34.077  1.00 86.81           C  
ANISOU 6413  CD2 TRP B  97    11563  10495  10927    318   -375     60       C  
ATOM   6414  NE1 TRP B  97     -11.950 -28.744 -35.935  1.00 87.42           N  
ANISOU 6414  NE1 TRP B  97    11707  10549  10957    347   -364     64       N  
ATOM   6415  CE2 TRP B  97     -11.833 -29.001 -34.615  1.00 87.33           C  
ANISOU 6415  CE2 TRP B  97    11658  10550  10970    335   -348     74       C  
ATOM   6416  CE3 TRP B  97     -13.364 -29.401 -32.723  1.00 82.47           C  
ANISOU 6416  CE3 TRP B  97    10972   9958  10403    304   -365     68       C  
ATOM   6417  CZ2 TRP B  97     -10.708 -29.141 -33.812  1.00 86.03           C  
ANISOU 6417  CZ2 TRP B  97    11482  10392  10813    337   -313     95       C  
ATOM   6418  CZ3 TRP B  97     -12.221 -29.542 -31.926  1.00 82.91           C  
ANISOU 6418  CZ3 TRP B  97    11017  10020  10464    307   -329     88       C  
ATOM   6419  CH2 TRP B  97     -10.926 -29.413 -32.459  1.00 82.96           C  
ANISOU 6419  CH2 TRP B  97    11052  10017  10450    322   -305    101       C  
ATOM   6420  N   HIS B  98     -18.583 -30.885 -35.537  1.00117.03           N  
ANISOU 6420  N   HIS B  98    15377  14305  14784    270   -513    -26       N  
ATOM   6421  CA  HIS B  98     -19.789 -31.016 -36.362  1.00122.33           C  
ANISOU 6421  CA  HIS B  98    16057  14971  15451    265   -553    -50       C  
ATOM   6422  C   HIS B  98     -20.883 -30.068 -35.955  1.00120.21           C  
ANISOU 6422  C   HIS B  98    15754  14722  15196    261   -579    -56       C  
ATOM   6423  O   HIS B  98     -21.400 -29.313 -36.784  1.00118.68           O  
ANISOU 6423  O   HIS B  98    15574  14532  14988    271   -606    -65       O  
ATOM   6424  CB  HIS B  98     -20.294 -32.460 -36.383  1.00131.21           C  
ANISOU 6424  CB  HIS B  98    17184  16080  16590    247   -558    -64       C  
ATOM   6425  CG  HIS B  98     -21.128 -32.799 -37.603  1.00135.63           C  
ANISOU 6425  CG  HIS B  98    17770  16628  17135    245   -593    -88       C  
ATOM   6426  ND1 HIS B  98     -20.585 -32.986 -38.822  1.00137.01           N  
ANISOU 6426  ND1 HIS B  98    17991  16785  17279    258   -593    -93       N  
ATOM   6427  CD2 HIS B  98     -22.502 -32.985 -37.754  1.00135.61           C  
ANISOU 6427  CD2 HIS B  98    17751  16627  17145    231   -629   -109       C  
ATOM   6428  CE1 HIS B  98     -21.558 -33.272 -39.708  1.00136.21           C  
ANISOU 6428  CE1 HIS B  98    17904  16677  17172    253   -629   -116       C  
ATOM   6429  NE2 HIS B  98     -22.730 -33.273 -39.053  1.00135.77           N  
ANISOU 6429  NE2 HIS B  98    17809  16633  17142    236   -651   -126       N  
ATOM   6430  N   GLY B  99     -21.248 -30.096 -34.677  1.00115.56           N  
ANISOU 6430  N   GLY B  99    15123  14147  14637    247   -572    -49       N  
ATOM   6431  CA  GLY B  99     -22.297 -29.223 -34.167  1.00112.33           C  
ANISOU 6431  CA  GLY B  99    14678  13757  14244    243   -595    -54       C  
ATOM   6432  C   GLY B  99     -21.730 -28.034 -33.423  1.00110.76           C  
ANISOU 6432  C   GLY B  99    14459  13576  14046    253   -577    -35       C  
ATOM   6433  O   GLY B  99     -22.206 -27.694 -32.343  1.00116.12           O  
ANISOU 6433  O   GLY B  99    15099  14271  14748    244   -576    -31       O  
ATOM   6434  N   LEU B 100     -20.716 -27.398 -34.002  1.00108.44           N  
ANISOU 6434  N   LEU B 100    14195  13280  13728    272   -562    -25       N  
ATOM   6435  CA  LEU B 100     -20.024 -26.299 -33.334  1.00105.09           C  
ANISOU 6435  CA  LEU B 100    13755  12870  13302    281   -542     -7       C  
ATOM   6436  C   LEU B 100     -20.002 -25.011 -34.157  1.00108.91           C  
ANISOU 6436  C   LEU B 100    14257  13359  13765    300   -555     -7       C  
ATOM   6437  O   LEU B 100     -18.991 -24.303 -34.191  1.00115.43           O  
ANISOU 6437  O   LEU B 100    15094  14186  14577    314   -533      6       O  
ATOM   6438  CB  LEU B 100     -18.599 -26.719 -32.950  1.00 98.37           C  
ANISOU 6438  CB  LEU B 100    12914  12014  12447    285   -502     10       C  
ATOM   6439  CG  LEU B 100     -18.385 -27.918 -32.016  1.00 97.37           C  
ANISOU 6439  CG  LEU B 100    12770  11884  12341    269   -482     16       C  
ATOM   6440  CD1 LEU B 100     -16.895 -28.182 -31.857  1.00 95.58           C  
ANISOU 6440  CD1 LEU B 100    12558  11651  12104    278   -444     34       C  
ATOM   6441  CD2 LEU B 100     -19.042 -27.732 -30.652  1.00 92.63           C  
ANISOU 6441  CD2 LEU B 100    12121  11302  11770    256   -482     19       C  
ATOM   6442  N   HIS B 101     -21.122 -24.698 -34.805  1.00111.93           N  
ANISOU 6442  N   HIS B 101    14641  13743  14144    301   -591    -23       N  
ATOM   6443  CA  HIS B 101     -21.227 -23.461 -35.581  1.00114.24           C  
ANISOU 6443  CA  HIS B 101    14949  14039  14417    319   -606    -24       C  
ATOM   6444  C   HIS B 101     -21.472 -22.256 -34.700  1.00113.17           C  
ANISOU 6444  C   HIS B 101    14780  13924  14295    320   -603    -15       C  
ATOM   6445  O   HIS B 101     -21.770 -21.164 -35.192  1.00117.17           O  
ANISOU 6445  O   HIS B 101    15292  14437  14790    334   -618    -16       O  
ATOM   6446  CB  HIS B 101     -22.265 -23.595 -36.707  1.00118.69           C  
ANISOU 6446  CB  HIS B 101    15531  14596  14969    321   -645    -45       C  
ATOM   6447  CG  HIS B 101     -23.707 -23.533 -36.242  1.00123.23           C  
ANISOU 6447  CG  HIS B 101    16069  15183  15566    307   -675    -57       C  
ATOM   6448  ND1 HIS B 101     -24.247 -24.452 -35.418  1.00123.89           N  
ANISOU 6448  ND1 HIS B 101    16125  15268  15677    286   -675    -62       N  
ATOM   6449  CD2 HIS B 101     -24.729 -22.628 -36.544  1.00124.11           C  
ANISOU 6449  CD2 HIS B 101    16170  15306  15678    313   -705    -65       C  
ATOM   6450  CE1 HIS B 101     -25.541 -24.145 -35.190  1.00124.96           C  
ANISOU 6450  CE1 HIS B 101    16232  15415  15830    279   -704    -73       C  
ATOM   6451  NE2 HIS B 101     -25.833 -23.029 -35.880  1.00123.57           N  
ANISOU 6451  NE2 HIS B 101    16066  15246  15637    295   -723    -75       N  
ATOM   6452  N   HIS B 102     -21.325 -22.451 -33.388  1.00106.56           N  
ANISOU 6452  N   HIS B 102    13908  13098  13482    307   -584     -5       N  
ATOM   6453  CA  HIS B 102     -21.462 -21.380 -32.397  1.00 98.14           C  
ANISOU 6453  CA  HIS B 102    12807  12050  12430    308   -577      3       C  
ATOM   6454  C   HIS B 102     -20.212 -21.147 -31.581  1.00 91.74           C  
ANISOU 6454  C   HIS B 102    11989  11245  11621    310   -539     23       C  
ATOM   6455  O   HIS B 102     -20.091 -20.123 -30.907  1.00 89.33           O  
ANISOU 6455  O   HIS B 102    11664  10955  11322    313   -530     32       O  
ATOM   6456  CB  HIS B 102     -22.657 -21.640 -31.481  1.00 97.05           C  
ANISOU 6456  CB  HIS B 102    12628  11924  12322    290   -593     -3       C  
ATOM   6457  CG  HIS B 102     -23.974 -21.179 -32.058  1.00102.79           C  
ANISOU 6457  CG  HIS B 102    13349  12655  13050    291   -631    -19       C  
ATOM   6458  ND1 HIS B 102     -24.329 -19.881 -32.107  1.00103.84           N  
ANISOU 6458  ND1 HIS B 102    13474  12800  13179    302   -641    -17       N  
ATOM   6459  CD2 HIS B 102     -25.028 -21.895 -32.622  1.00106.85           C  
ANISOU 6459  CD2 HIS B 102    13865  13162  13568    283   -662    -37       C  
ATOM   6460  CE1 HIS B 102     -25.545 -19.768 -32.674  1.00101.47           C  
ANISOU 6460  CE1 HIS B 102    13170  12501  12881    302   -677    -32       C  
ATOM   6461  NE2 HIS B 102     -25.973 -21.000 -32.988  1.00108.24           N  
ANISOU 6461  NE2 HIS B 102    14034  13348  13744    289   -690    -45       N  
ATOM   6462  N   LEU B 103     -19.273 -22.091 -31.636  1.00 87.77           N  
ANISOU 6462  N   LEU B 103    11504  10730  11112    308   -516     29       N  
ATOM   6463  CA  LEU B 103     -18.012 -21.994 -30.894  1.00 82.24           C  
ANISOU 6463  CA  LEU B 103    10799  10035  10413    310   -480     47       C  
ATOM   6464  C   LEU B 103     -17.214 -20.761 -31.303  1.00 82.45           C  
ANISOU 6464  C   LEU B 103    10842  10064  10421    328   -468     57       C  
ATOM   6465  O   LEU B 103     -17.114 -20.457 -32.493  1.00 82.28           O  
ANISOU 6465  O   LEU B 103    10854  10031  10376    342   -479     52       O  
ATOM   6466  CB  LEU B 103     -17.165 -23.254 -31.104  1.00 78.12           C  
ANISOU 6466  CB  LEU B 103    10299   9497   9886    308   -460     51       C  
ATOM   6467  CG  LEU B 103     -15.914 -23.418 -30.229  1.00 76.79           C  
ANISOU 6467  CG  LEU B 103    10121   9333   9722    307   -422     71       C  
ATOM   6468  CD1 LEU B 103     -16.275 -23.904 -28.834  1.00 75.60           C  
ANISOU 6468  CD1 LEU B 103     9929   9195   9599    290   -414     74       C  
ATOM   6469  CD2 LEU B 103     -14.905 -24.355 -30.870  1.00 75.85           C  
ANISOU 6469  CD2 LEU B 103    10036   9196   9587    313   -403     75       C  
ATOM   6470  N   SER B 104     -16.648 -20.066 -30.314  1.00 81.33           N  
ANISOU 6470  N   SER B 104    10676   9936  10288    328   -446     71       N  
ATOM   6471  CA  SER B 104     -15.859 -18.848 -30.556  1.00 80.93           C  
ANISOU 6471  CA  SER B 104    10637   9890  10222    343   -433     81       C  
ATOM   6472  C   SER B 104     -14.394 -18.937 -30.094  1.00 80.74           C  
ANISOU 6472  C   SER B 104    10615   9865  10194    346   -395     98       C  
ATOM   6473  O   SER B 104     -13.528 -18.237 -30.633  1.00 78.56           O  
ANISOU 6473  O   SER B 104    10362   9586   9901    360   -382    106       O  
ATOM   6474  CB  SER B 104     -16.541 -17.629 -29.921  1.00 79.19           C  
ANISOU 6474  CB  SER B 104    10387   9687  10014    342   -443     81       C  
ATOM   6475  OG  SER B 104     -16.689 -17.793 -28.521  1.00 77.54           O  
ANISOU 6475  OG  SER B 104    10139   9493   9830    327   -432     86       O  
ATOM   6476  N   ASN B 105     -14.128 -19.780 -29.095  1.00 78.40           N  
ANISOU 6476  N   ASN B 105    10297   9574   9915    333   -379    105       N  
ATOM   6477  CA  ASN B 105     -12.779 -19.947 -28.543  1.00 75.71           C  
ANISOU 6477  CA  ASN B 105     9955   9236   9573    334   -345    122       C  
ATOM   6478  C   ASN B 105     -12.339 -21.408 -28.515  1.00 77.55           C  
ANISOU 6478  C   ASN B 105    10198   9458   9809    328   -332    124       C  
ATOM   6479  O   ASN B 105     -12.969 -22.241 -27.856  1.00 77.33           O  
ANISOU 6479  O   ASN B 105    10149   9434   9799    314   -338    120       O  
ATOM   6480  CB  ASN B 105     -12.694 -19.366 -27.127  1.00 75.83           C  
ANISOU 6480  CB  ASN B 105     9929   9273   9607    326   -332    131       C  
ATOM   6481  CG  ASN B 105     -12.609 -17.851 -27.108  1.00 76.31           C  
ANISOU 6481  CG  ASN B 105     9985   9344   9663    334   -332    133       C  
ATOM   6482  OD1 ASN B 105     -11.640 -17.286 -26.603  1.00 76.50           O  
ANISOU 6482  OD1 ASN B 105    10002   9376   9685    337   -308    146       O  
ATOM   6483  ND2 ASN B 105     -13.628 -17.184 -27.644  1.00 75.78           N  
ANISOU 6483  ND2 ASN B 105     9921   9276   9593    338   -359    121       N  
ATOM   6484  N   LEU B 106     -11.251 -21.709 -29.223  1.00 76.41           N  
ANISOU 6484  N   LEU B 106    10084   9300   9646    339   -314    132       N  
ATOM   6485  CA  LEU B 106     -10.711 -23.069 -29.297  1.00 72.61           C  
ANISOU 6485  CA  LEU B 106     9616   8806   9164    335   -299    136       C  
ATOM   6486  C   LEU B 106      -9.228 -23.096 -28.918  1.00 71.93           C  
ANISOU 6486  C   LEU B 106     9533   8723   9074    341   -263    155       C  
ATOM   6487  O   LEU B 106      -8.403 -22.431 -29.552  1.00 74.92           O  
ANISOU 6487  O   LEU B 106     9933   9096   9435    355   -251    161       O  
ATOM   6488  CB  LEU B 106     -10.930 -23.651 -30.702  1.00 72.37           C  
ANISOU 6488  CB  LEU B 106     9627   8753   9115    342   -313    124       C  
ATOM   6489  CG  LEU B 106     -10.422 -25.058 -31.047  1.00 71.80           C  
ANISOU 6489  CG  LEU B 106     9576   8663   9038    341   -300    125       C  
ATOM   6490  CD1 LEU B 106     -11.185 -26.136 -30.287  1.00 68.41           C  
ANISOU 6490  CD1 LEU B 106     9124   8235   8631    323   -307    119       C  
ATOM   6491  CD2 LEU B 106     -10.508 -25.291 -32.551  1.00 69.96           C  
ANISOU 6491  CD2 LEU B 106     9389   8410   8783    351   -314    114       C  
ATOM   6492  N   ILE B 107      -8.898 -23.865 -27.884  1.00 68.35           N  
ANISOU 6492  N   ILE B 107     9056   8276   8636    331   -245    164       N  
ATOM   6493  CA  ILE B 107      -7.534 -23.902 -27.348  1.00 64.88           C  
ANISOU 6493  CA  ILE B 107     8613   7842   8196    336   -212    183       C  
ATOM   6494  C   ILE B 107      -6.934 -25.304 -27.475  1.00 62.49           C  
ANISOU 6494  C   ILE B 107     8325   7526   7892    335   -194    189       C  
ATOM   6495  O   ILE B 107      -7.488 -26.273 -26.947  1.00 59.53           O  
ANISOU 6495  O   ILE B 107     7935   7149   7531    323   -198    185       O  
ATOM   6496  CB  ILE B 107      -7.488 -23.427 -25.877  1.00 63.84           C  
ANISOU 6496  CB  ILE B 107     8436   7734   8082    326   -202    191       C  
ATOM   6497  CG1 ILE B 107      -8.338 -22.166 -25.697  1.00 64.35           C  
ANISOU 6497  CG1 ILE B 107     8484   7812   8151    325   -223    183       C  
ATOM   6498  CG2 ILE B 107      -6.055 -23.153 -25.444  1.00 60.76           C  
ANISOU 6498  CG2 ILE B 107     8044   7353   7689    333   -170    210       C  
ATOM   6499  CD1 ILE B 107      -9.182 -22.166 -24.442  1.00 69.76           C  
ANISOU 6499  CD1 ILE B 107     9129   8516   8860    310   -231    180       C  
ATOM   6500  N   LEU B 108      -5.801 -25.390 -28.175  1.00 61.37           N  
ANISOU 6500  N   LEU B 108     8212   7372   7732    348   -174    198       N  
ATOM   6501  CA  LEU B 108      -5.171 -26.670 -28.512  1.00 62.81           C  
ANISOU 6501  CA  LEU B 108     8415   7537   7910    350   -157    204       C  
ATOM   6502  C   LEU B 108      -3.712 -26.757 -28.058  1.00 64.43           C  
ANISOU 6502  C   LEU B 108     8617   7748   8113    357   -122    225       C  
ATOM   6503  O   LEU B 108      -2.931 -27.553 -28.593  1.00 64.69           O  
ANISOU 6503  O   LEU B 108     8675   7765   8137    364   -104    232       O  
ATOM   6504  CB  LEU B 108      -5.261 -26.930 -30.026  1.00 62.87           C  
ANISOU 6504  CB  LEU B 108     8469   7521   7896    360   -168    193       C  
ATOM   6505  CG  LEU B 108      -6.619 -26.875 -30.739  1.00 62.61           C  
ANISOU 6505  CG  LEU B 108     8447   7480   7861    356   -204    172       C  
ATOM   6506  CD1 LEU B 108      -6.416 -26.926 -32.248  1.00 62.33           C  
ANISOU 6506  CD1 LEU B 108     8458   7422   7800    370   -209    165       C  
ATOM   6507  CD2 LEU B 108      -7.567 -27.975 -30.270  1.00 59.67           C  
ANISOU 6507  CD2 LEU B 108     8059   7105   7505    340   -216    162       C  
ATOM   6508  N   THR B 109      -3.361 -25.946 -27.061  1.00 63.54           N  
ANISOU 6508  N   THR B 109     8473   7657   8010    355   -112    235       N  
ATOM   6509  CA  THR B 109      -1.990 -25.830 -26.556  1.00 62.43           C  
ANISOU 6509  CA  THR B 109     8324   7525   7868    361    -81    254       C  
ATOM   6510  C   THR B 109      -1.318 -27.181 -26.249  1.00 63.50           C  
ANISOU 6510  C   THR B 109     8463   7655   8009    360    -58    266       C  
ATOM   6511  O   THR B 109      -1.914 -28.042 -25.604  1.00 63.91           O  
ANISOU 6511  O   THR B 109     8498   7709   8075    349    -63    263       O  
ATOM   6512  CB  THR B 109      -1.960 -24.950 -25.290  1.00 59.94           C  
ANISOU 6512  CB  THR B 109     7969   7238   7568    353    -78    260       C  
ATOM   6513  OG1 THR B 109      -2.819 -23.819 -25.474  1.00 63.53           O  
ANISOU 6513  OG1 THR B 109     8418   7698   8022    352   -101    248       O  
ATOM   6514  CG2 THR B 109      -0.547 -24.472 -24.985  1.00 58.06           C  
ANISOU 6514  CG2 THR B 109     7725   7008   7324    362    -49    278       C  
ATOM   6515  N   GLY B 110      -0.082 -27.350 -26.721  1.00 62.03           N  
ANISOU 6515  N   GLY B 110     8297   7459   7810    372    -33    279       N  
ATOM   6516  CA  GLY B 110       0.741 -28.515 -26.386  1.00 62.48           C  
ANISOU 6516  CA  GLY B 110     8355   7512   7871    374     -8    293       C  
ATOM   6517  C   GLY B 110       0.225 -29.861 -26.865  1.00 64.95           C  
ANISOU 6517  C   GLY B 110     8689   7804   8184    371    -13    286       C  
ATOM   6518  O   GLY B 110       0.283 -30.843 -26.127  1.00 67.01           O  
ANISOU 6518  O   GLY B 110     8935   8068   8458    364     -2    293       O  
ATOM   6519  N   ASN B 111      -0.280 -29.900 -28.099  1.00 67.70           N  
ANISOU 6519  N   ASN B 111     9072   8132   8518    375    -30    271       N  
ATOM   6520  CA  ASN B 111      -0.769 -31.130 -28.732  1.00 67.40           C  
ANISOU 6520  CA  ASN B 111     9059   8072   8478    373    -36    262       C  
ATOM   6521  C   ASN B 111       0.059 -31.451 -29.963  1.00 68.56           C  
ANISOU 6521  C   ASN B 111     9250   8196   8604    388    -22    265       C  
ATOM   6522  O   ASN B 111       0.141 -30.629 -30.873  1.00 71.94           O  
ANISOU 6522  O   ASN B 111     9699   8617   9014    397    -30    260       O  
ATOM   6523  CB  ASN B 111      -2.235 -30.982 -29.152  1.00 68.13           C  
ANISOU 6523  CB  ASN B 111     9155   8159   8572    363    -72    239       C  
ATOM   6524  CG  ASN B 111      -3.203 -31.296 -28.032  1.00 66.92           C  
ANISOU 6524  CG  ASN B 111     8963   8019   8441    346    -85    233       C  
ATOM   6525  OD1 ASN B 111      -4.158 -30.557 -27.794  1.00 64.13           O  
ANISOU 6525  OD1 ASN B 111     8592   7677   8094    339   -109    222       O  
ATOM   6526  ND2 ASN B 111      -2.962 -32.395 -27.340  1.00 70.34           N  
ANISOU 6526  ND2 ASN B 111     9385   8452   8887    340    -67    242       N  
ATOM   6527  N   PRO B 112       0.667 -32.650 -30.010  1.00 68.23           N  
ANISOU 6527  N   PRO B 112     9220   8140   8561    390      0    274       N  
ATOM   6528  CA  PRO B 112       1.535 -33.031 -31.134  1.00 68.63           C  
ANISOU 6528  CA  PRO B 112     9313   8168   8592    405     16    279       C  
ATOM   6529  C   PRO B 112       0.778 -33.317 -32.447  1.00 69.45           C  
ANISOU 6529  C   PRO B 112     9457   8248   8681    407     -5    259       C  
ATOM   6530  O   PRO B 112       1.032 -34.335 -33.099  1.00 74.68           O  
ANISOU 6530  O   PRO B 112    10149   8888   9335    412      4    258       O  
ATOM   6531  CB  PRO B 112       2.240 -34.302 -30.622  1.00 66.51           C  
ANISOU 6531  CB  PRO B 112     9042   7894   8332    405     44    294       C  
ATOM   6532  CG  PRO B 112       1.981 -34.345 -29.150  1.00 66.02           C  
ANISOU 6532  CG  PRO B 112     8933   7856   8293    393     46    301       C  
ATOM   6533  CD  PRO B 112       0.651 -33.685 -28.965  1.00 66.42           C  
ANISOU 6533  CD  PRO B 112     8967   7916   8351    381     12    282       C  
ATOM   6534  N   ILE B 113      -0.135 -32.425 -32.828  1.00 66.22           N  
ANISOU 6534  N   ILE B 113     9049   7844   8268    405    -35    243       N  
ATOM   6535  CA  ILE B 113      -0.881 -32.558 -34.083  1.00 66.99           C  
ANISOU 6535  CA  ILE B 113     9183   7921   8349    407    -58    223       C  
ATOM   6536  C   ILE B 113       0.069 -32.452 -35.281  1.00 68.92           C  
ANISOU 6536  C   ILE B 113     9470   8146   8568    426    -42    228       C  
ATOM   6537  O   ILE B 113       0.060 -33.310 -36.165  1.00 71.67           O  
ANISOU 6537  O   ILE B 113     9854   8472   8905    430    -41    221       O  
ATOM   6538  CB  ILE B 113      -2.033 -31.526 -34.187  1.00 66.35           C  
ANISOU 6538  CB  ILE B 113     9089   7851   8268    402    -93    206       C  
ATOM   6539  CG1 ILE B 113      -2.965 -31.651 -32.975  1.00 66.82           C  
ANISOU 6539  CG1 ILE B 113     9105   7928   8353    383   -108    202       C  
ATOM   6540  CG2 ILE B 113      -2.821 -31.715 -35.482  1.00 63.95           C  
ANISOU 6540  CG2 ILE B 113     8823   7527   7947    404   -119    186       C  
ATOM   6541  CD1 ILE B 113      -3.930 -30.497 -32.786  1.00 65.99           C  
ANISOU 6541  CD1 ILE B 113     8980   7839   8252    378   -136    190       C  
ATOM   6542  N   GLN B 114       0.883 -31.396 -35.288  1.00 72.25           N  
ANISOU 6542  N   GLN B 114     9889   8578   8983    437    -29    241       N  
ATOM   6543  CA  GLN B 114       1.961 -31.183 -36.265  1.00 71.63           C  
ANISOU 6543  CA  GLN B 114     9846   8484   8883    456     -8    250       C  
ATOM   6544  C   GLN B 114       1.473 -30.766 -37.646  1.00 74.39           C  
ANISOU 6544  C   GLN B 114    10236   8817   9209    465    -29    235       C  
ATOM   6545  O   GLN B 114       1.750 -29.655 -38.104  1.00 77.45           O  
ANISOU 6545  O   GLN B 114    10632   9208   9586    476    -30    237       O  
ATOM   6546  CB  GLN B 114       2.887 -32.398 -36.351  1.00 69.03           C  
ANISOU 6546  CB  GLN B 114     9534   8139   8552    461     21    263       C  
ATOM   6547  CG  GLN B 114       4.152 -32.138 -37.145  1.00 69.64           C  
ANISOU 6547  CG  GLN B 114     9642   8205   8612    480     48    277       C  
ATOM   6548  CD  GLN B 114       5.315 -33.006 -36.703  1.00 69.81           C  
ANISOU 6548  CD  GLN B 114     9659   8223   8639    485     85    297       C  
ATOM   6549  OE1 GLN B 114       5.130 -34.076 -36.106  1.00 67.21           O  
ANISOU 6549  OE1 GLN B 114     9319   7893   8324    475     90    299       O  
ATOM   6550  NE2 GLN B 114       6.530 -32.548 -36.998  1.00 68.01           N  
ANISOU 6550  NE2 GLN B 114     9442   7993   8402    500    112    314       N  
ATOM   6551  N   SER B 115       0.762 -31.676 -38.302  1.00 77.67           N  
ANISOU 6551  N   SER B 115    10676   9215   9619    461    -45    219       N  
ATOM   6552  CA  SER B 115       0.215 -31.440 -39.629  1.00 77.15           C  
ANISOU 6552  CA  SER B 115    10650   9132   9530    469    -67    202       C  
ATOM   6553  C   SER B 115      -1.291 -31.295 -39.519  1.00 75.53           C  
ANISOU 6553  C   SER B 115    10430   8935   9333    455   -107    181       C  
ATOM   6554  O   SER B 115      -1.963 -32.146 -38.929  1.00 76.23           O  
ANISOU 6554  O   SER B 115    10501   9025   9438    440   -116    173       O  
ATOM   6555  CB  SER B 115       0.571 -32.599 -40.562  1.00 74.74           C  
ANISOU 6555  CB  SER B 115    10388   8800   9210    476    -55    199       C  
ATOM   6556  OG  SER B 115       1.966 -32.834 -40.555  1.00 72.58           O  
ANISOU 6556  OG  SER B 115    10125   8520   8932    488    -17    220       O  
ATOM   6557  N   PHE B 116      -1.815 -30.208 -40.074  1.00 74.84           N  
ANISOU 6557  N   PHE B 116    10349   8852   9233    462   -129    171       N  
ATOM   6558  CA  PHE B 116      -3.251 -29.969 -40.076  1.00 77.07           C  
ANISOU 6558  CA  PHE B 116    10619   9142   9521    450   -168    151       C  
ATOM   6559  C   PHE B 116      -3.785 -30.155 -41.491  1.00 80.76           C  
ANISOU 6559  C   PHE B 116    11131   9589   9964    458   -190    133       C  
ATOM   6560  O   PHE B 116      -3.437 -29.402 -42.409  1.00 80.94           O  
ANISOU 6560  O   PHE B 116    11183   9605   9964    475   -190    134       O  
ATOM   6561  CB  PHE B 116      -3.572 -28.572 -39.541  1.00 76.06           C  
ANISOU 6561  CB  PHE B 116    10461   9036   9400    450   -180    153       C  
ATOM   6562  CG  PHE B 116      -3.253 -28.385 -38.083  1.00 74.32           C  
ANISOU 6562  CG  PHE B 116    10193   8837   9205    440   -163    168       C  
ATOM   6563  CD1 PHE B 116      -1.935 -28.248 -37.651  1.00 74.56           C  
ANISOU 6563  CD1 PHE B 116    10219   8872   9237    447   -128    189       C  
ATOM   6564  CD2 PHE B 116      -4.274 -28.324 -37.141  1.00 75.27           C  
ANISOU 6564  CD2 PHE B 116    10276   8975   9348    423   -184    160       C  
ATOM   6565  CE1 PHE B 116      -1.643 -28.073 -36.308  1.00 76.06           C  
ANISOU 6565  CE1 PHE B 116    10365   9082   9449    438   -114    201       C  
ATOM   6566  CE2 PHE B 116      -3.990 -28.142 -35.796  1.00 75.24           C  
ANISOU 6566  CE2 PHE B 116    10230   8992   9366    414   -169    172       C  
ATOM   6567  CZ  PHE B 116      -2.672 -28.019 -35.379  1.00 77.68           C  
ANISOU 6567  CZ  PHE B 116    10534   9305   9675    421   -135    193       C  
ATOM   6568  N   SER B 117      -4.618 -31.179 -41.652  1.00 84.64           N  
ANISOU 6568  N   SER B 117    11629  10071  10460    446   -209    117       N  
ATOM   6569  CA  SER B 117      -5.147 -31.588 -42.953  1.00 89.26           C  
ANISOU 6569  CA  SER B 117    12256  10635  11022    451   -230     98       C  
ATOM   6570  C   SER B 117      -6.099 -30.545 -43.531  1.00 91.31           C  
ANISOU 6570  C   SER B 117    12519  10903  11270    455   -265     84       C  
ATOM   6571  O   SER B 117      -6.622 -29.711 -42.789  1.00 90.37           O  
ANISOU 6571  O   SER B 117    12363  10804  11166    449   -278     85       O  
ATOM   6572  CB  SER B 117      -5.875 -32.930 -42.816  1.00 88.85           C  
ANISOU 6572  CB  SER B 117    12203  10573  10982    434   -242     83       C  
ATOM   6573  OG  SER B 117      -4.995 -33.951 -42.384  1.00 87.55           O  
ANISOU 6573  OG  SER B 117    12040  10399  10825    432   -208     97       O  
ATOM   6574  N   PRO B 118      -6.324 -30.581 -44.859  1.00 96.12           N  
ANISOU 6574  N   PRO B 118    13171  11495  11852    467   -281     71       N  
ATOM   6575  CA  PRO B 118      -7.347 -29.704 -45.441  1.00 98.52           C  
ANISOU 6575  CA  PRO B 118    13480  11807  12146    470   -318     55       C  
ATOM   6576  C   PRO B 118      -8.707 -29.898 -44.756  1.00 99.06           C  
ANISOU 6576  C   PRO B 118    13511  11888  12237    449   -350     40       C  
ATOM   6577  O   PRO B 118      -9.192 -31.029 -44.650  1.00100.87           O  
ANISOU 6577  O   PRO B 118    13740  12109  12476    435   -358     28       O  
ATOM   6578  CB  PRO B 118      -7.407 -30.159 -46.903  1.00 98.70           C  
ANISOU 6578  CB  PRO B 118    13556  11807  12139    482   -329     42       C  
ATOM   6579  CG  PRO B 118      -6.059 -30.733 -47.176  1.00 97.82           C  
ANISOU 6579  CG  PRO B 118    13472  11677  12016    492   -290     57       C  
ATOM   6580  CD  PRO B 118      -5.602 -31.355 -45.889  1.00 95.13           C  
ANISOU 6580  CD  PRO B 118    13095  11345  11705    478   -264     71       C  
ATOM   6581  N   GLY B 119      -9.293 -28.804 -44.274  1.00 95.27           N  
ANISOU 6581  N   GLY B 119    13001  11429  11766    448   -367     40       N  
ATOM   6582  CA  GLY B 119     -10.592 -28.848 -43.604  1.00 94.73           C  
ANISOU 6582  CA  GLY B 119    12896  11375  11721    430   -397     26       C  
ATOM   6583  C   GLY B 119     -10.554 -29.515 -42.240  1.00 96.65           C  
ANISOU 6583  C   GLY B 119    13098  11627  11995    411   -381     34       C  
ATOM   6584  O   GLY B 119     -11.509 -30.193 -41.846  1.00 96.32           O  
ANISOU 6584  O   GLY B 119    13037  11587  11971    393   -400     20       O  
ATOM   6585  N   SER B 120      -9.443 -29.328 -41.526  1.00 96.36           N  
ANISOU 6585  N   SER B 120    13049  11596  11966    415   -346     55       N  
ATOM   6586  CA  SER B 120      -9.306 -29.788 -40.142  1.00 90.57           C  
ANISOU 6586  CA  SER B 120    12275  10875  11262    400   -329     65       C  
ATOM   6587  C   SER B 120     -10.258 -29.012 -39.244  1.00 88.48           C  
ANISOU 6587  C   SER B 120    11966  10633  11018    389   -349     62       C  
ATOM   6588  O   SER B 120     -10.872 -29.576 -38.339  1.00 90.79           O  
ANISOU 6588  O   SER B 120    12226  10933  11334    371   -355     58       O  
ATOM   6589  CB  SER B 120      -7.873 -29.595 -39.648  1.00 86.60           C  
ANISOU 6589  CB  SER B 120    11769  10374  10759    409   -288     90       C  
ATOM   6590  OG  SER B 120      -6.964 -30.402 -40.371  1.00 86.70           O  
ANISOU 6590  OG  SER B 120    11820  10366  10756    418   -266     95       O  
ATOM   6591  N   PHE B 121     -10.371 -27.715 -39.517  1.00 87.27           N  
ANISOU 6591  N   PHE B 121    11812  10490  10855    400   -360     63       N  
ATOM   6592  CA  PHE B 121     -11.251 -26.826 -38.771  1.00 88.72           C  
ANISOU 6592  CA  PHE B 121    11957  10695  11055    392   -379     60       C  
ATOM   6593  C   PHE B 121     -12.576 -26.590 -39.505  1.00 91.95           C  
ANISOU 6593  C   PHE B 121    12373  11104  11457    391   -421     38       C  
ATOM   6594  O   PHE B 121     -13.233 -25.569 -39.291  1.00 92.00           O  
ANISOU 6594  O   PHE B 121    12359  11125  11469    392   -439     36       O  
ATOM   6595  CB  PHE B 121     -10.553 -25.483 -38.499  1.00 85.04           C  
ANISOU 6595  CB  PHE B 121    11482  10243  10585    405   -363     75       C  
ATOM   6596  CG  PHE B 121      -9.165 -25.613 -37.929  1.00 79.69           C  
ANISOU 6596  CG  PHE B 121    10802   9566   9911    409   -323     97       C  
ATOM   6597  CD1 PHE B 121      -8.971 -26.011 -36.609  1.00 78.26           C  
ANISOU 6597  CD1 PHE B 121    10583   9398   9755    395   -307    106       C  
ATOM   6598  CD2 PHE B 121      -8.052 -25.323 -38.709  1.00 77.29           C  
ANISOU 6598  CD2 PHE B 121    10531   9250   9584    427   -302    107       C  
ATOM   6599  CE1 PHE B 121      -7.693 -26.126 -36.083  1.00 77.39           C  
ANISOU 6599  CE1 PHE B 121    10468   9288   9646    399   -271    126       C  
ATOM   6600  CE2 PHE B 121      -6.772 -25.435 -38.188  1.00 75.36           C  
ANISOU 6600  CE2 PHE B 121    10282   9006   9343    430   -265    127       C  
ATOM   6601  CZ  PHE B 121      -6.593 -25.836 -36.874  1.00 76.80           C  
ANISOU 6601  CZ  PHE B 121    10427   9203   9550    416   -250    136       C  
ATOM   6602  N   SER B 122     -12.969 -27.529 -40.365  1.00 94.55           N  
ANISOU 6602  N   SER B 122    12731  11415  11776    389   -436     23       N  
ATOM   6603  CA  SER B 122     -14.241 -27.417 -41.083  1.00 96.85           C  
ANISOU 6603  CA  SER B 122    13029  11706  12061    386   -477      2       C  
ATOM   6604  C   SER B 122     -15.419 -27.602 -40.120  1.00 93.26           C  
ANISOU 6604  C   SER B 122    12530  11266  11636    366   -498     -7       C  
ATOM   6605  O   SER B 122     -15.582 -28.664 -39.514  1.00 90.39           O  
ANISOU 6605  O   SER B 122    12152  10899  11292    349   -492     -9       O  
ATOM   6606  CB  SER B 122     -14.313 -28.404 -42.257  1.00 98.86           C  
ANISOU 6606  CB  SER B 122    13327  11938  12295    389   -487    -12       C  
ATOM   6607  OG  SER B 122     -14.233 -29.749 -41.816  1.00105.39           O  
ANISOU 6607  OG  SER B 122    14149  12755  13138    373   -475    -14       O  
ATOM   6608  N   GLY B 123     -16.218 -26.549 -39.973  1.00 89.27           N  
ANISOU 6608  N   GLY B 123    12004  10777  11136    368   -521    -11       N  
ATOM   6609  CA  GLY B 123     -17.339 -26.556 -39.040  1.00 87.34           C  
ANISOU 6609  CA  GLY B 123    11715  10548  10919    350   -540    -18       C  
ATOM   6610  C   GLY B 123     -17.412 -25.347 -38.122  1.00 87.83           C  
ANISOU 6610  C   GLY B 123    11742  10632  10995    352   -535     -6       C  
ATOM   6611  O   GLY B 123     -18.493 -25.006 -37.639  1.00 90.99           O  
ANISOU 6611  O   GLY B 123    12111  11046  11413    342   -558    -14       O  
ATOM   6612  N   LEU B 124     -16.271 -24.706 -37.865  1.00 87.02           N  
ANISOU 6612  N   LEU B 124    11643  10533  10886    363   -505     11       N  
ATOM   6613  CA  LEU B 124     -16.246 -23.499 -37.034  1.00 89.08           C  
ANISOU 6613  CA  LEU B 124    11873  10814  11158    366   -499     23       C  
ATOM   6614  C   LEU B 124     -16.455 -22.254 -37.885  1.00 91.46           C  
ANISOU 6614  C   LEU B 124    12192  11119  11440    384   -515     20       C  
ATOM   6615  O   LEU B 124     -15.504 -21.706 -38.436  1.00 90.80           O  
ANISOU 6615  O   LEU B 124    12135  11028  11336    400   -497     30       O  
ATOM   6616  CB  LEU B 124     -14.934 -23.365 -36.249  1.00 88.47           C  
ANISOU 6616  CB  LEU B 124    11787  10741  11085    368   -459     44       C  
ATOM   6617  CG  LEU B 124     -14.422 -24.386 -35.223  1.00 87.37           C  
ANISOU 6617  CG  LEU B 124    11628  10602  10965    354   -434     53       C  
ATOM   6618  CD1 LEU B 124     -15.531 -25.181 -34.537  1.00 81.85           C  
ANISOU 6618  CD1 LEU B 124    10899   9907  10291    334   -451     41       C  
ATOM   6619  CD2 LEU B 124     -13.405 -25.304 -35.883  1.00 87.38           C  
ANISOU 6619  CD2 LEU B 124    11665  10583  10950    360   -412     57       C  
ATOM   6620  N   THR B 125     -17.704 -21.812 -37.986  1.00 96.57           N  
ANISOU 6620  N   THR B 125    12824  11774  12092    381   -548      7       N  
ATOM   6621  CA  THR B 125     -18.041 -20.634 -38.783  1.00 95.67           C  
ANISOU 6621  CA  THR B 125    12725  11663  11960    398   -566      4       C  
ATOM   6622  C   THR B 125     -18.170 -19.389 -37.915  1.00 95.46           C  
ANISOU 6622  C   THR B 125    12665  11656  11947    399   -561     14       C  
ATOM   6623  O   THR B 125     -18.151 -18.270 -38.429  1.00 99.32           O  
ANISOU 6623  O   THR B 125    13166  12148  12422    415   -566     17       O  
ATOM   6624  CB  THR B 125     -19.339 -20.837 -39.589  1.00 97.77           C  
ANISOU 6624  CB  THR B 125    12999  11927  12221    396   -608    -15       C  
ATOM   6625  OG1 THR B 125     -20.338 -21.436 -38.751  1.00 96.71           O  
ANISOU 6625  OG1 THR B 125    12828  11802  12115    375   -624    -25       O  
ATOM   6626  CG2 THR B 125     -19.085 -21.734 -40.795  1.00 99.11           C  
ANISOU 6626  CG2 THR B 125    13213  12076  12366    402   -614    -25       C  
ATOM   6627  N   SER B 126     -18.299 -19.592 -36.603  1.00 89.74           N  
ANISOU 6627  N   SER B 126    11901  10944  11251    383   -550     19       N  
ATOM   6628  CA  SER B 126     -18.423 -18.487 -35.649  1.00 86.91           C  
ANISOU 6628  CA  SER B 126    11508  10604  10908    382   -544     28       C  
ATOM   6629  C   SER B 126     -17.199 -18.344 -34.728  1.00 85.18           C  
ANISOU 6629  C   SER B 126    11277  10391  10696    380   -505     47       C  
ATOM   6630  O   SER B 126     -17.287 -17.721 -33.664  1.00 83.69           O  
ANISOU 6630  O   SER B 126    11054  10218  10525    374   -496     54       O  
ATOM   6631  CB  SER B 126     -19.708 -18.630 -34.819  1.00 85.48           C  
ANISOU 6631  CB  SER B 126    11287  10437  10754    366   -566     19       C  
ATOM   6632  OG  SER B 126     -20.867 -18.368 -35.594  1.00 81.81           O  
ANISOU 6632  OG  SER B 126    10828   9973  10284    370   -602      4       O  
ATOM   6633  N   LEU B 127     -16.065 -18.909 -35.145  1.00 81.80           N  
ANISOU 6633  N   LEU B 127    10877   9949  10253    386   -481     54       N  
ATOM   6634  CA  LEU B 127     -14.841 -18.904 -34.336  1.00 79.06           C  
ANISOU 6634  CA  LEU B 127    10521   9606   9912    385   -445     72       C  
ATOM   6635  C   LEU B 127     -14.139 -17.544 -34.352  1.00 79.13           C  
ANISOU 6635  C   LEU B 127    10532   9621   9911    399   -429     84       C  
ATOM   6636  O   LEU B 127     -13.914 -16.968 -35.420  1.00 80.54           O  
ANISOU 6636  O   LEU B 127    10743   9790  10068    416   -432     83       O  
ATOM   6637  CB  LEU B 127     -13.882 -20.010 -34.801  1.00 78.31           C  
ANISOU 6637  CB  LEU B 127    10455   9494   9806    386   -425     76       C  
ATOM   6638  CG  LEU B 127     -12.791 -20.500 -33.837  1.00 77.72           C  
ANISOU 6638  CG  LEU B 127    10365   9423   9742    380   -390     92       C  
ATOM   6639  CD1 LEU B 127     -13.372 -21.377 -32.735  1.00 77.05           C  
ANISOU 6639  CD1 LEU B 127    10244   9346   9683    360   -392     89       C  
ATOM   6640  CD2 LEU B 127     -11.696 -21.249 -34.582  1.00 76.47           C  
ANISOU 6640  CD2 LEU B 127    10242   9245   9565    388   -369     98       C  
ATOM   6641  N   GLU B 128     -13.795 -17.049 -33.162  1.00 77.01           N  
ANISOU 6641  N   GLU B 128    10231   9368   9660    392   -410     94       N  
ATOM   6642  CA  GLU B 128     -13.163 -15.732 -32.992  1.00 72.73           C  
ANISOU 6642  CA  GLU B 128     9686   8834   9113    402   -394    105       C  
ATOM   6643  C   GLU B 128     -11.688 -15.807 -32.593  1.00 67.69           C  
ANISOU 6643  C   GLU B 128     9051   8194   8473    404   -356    122       C  
ATOM   6644  O   GLU B 128     -10.912 -14.907 -32.906  1.00 65.14           O  
ANISOU 6644  O   GLU B 128     8742   7870   8138    417   -341    131       O  
ATOM   6645  CB  GLU B 128     -13.903 -14.922 -31.930  1.00 74.54           C  
ANISOU 6645  CB  GLU B 128     9875   9083   9364    393   -401    105       C  
ATOM   6646  CG  GLU B 128     -15.387 -14.737 -32.182  1.00 79.68           C  
ANISOU 6646  CG  GLU B 128    10517   9737  10020    391   -437     90       C  
ATOM   6647  CD  GLU B 128     -16.008 -13.730 -31.236  1.00 82.75           C  
ANISOU 6647  CD  GLU B 128    10869  10144  10426    386   -442     91       C  
ATOM   6648  OE1 GLU B 128     -15.300 -12.787 -30.820  1.00 87.18           O  
ANISOU 6648  OE1 GLU B 128    11424  10713  10987    391   -421    101       O  
ATOM   6649  OE2 GLU B 128     -17.207 -13.875 -30.915  1.00 84.59           O  
ANISOU 6649  OE2 GLU B 128    11081  10385  10674    377   -466     80       O  
ATOM   6650  N   ASN B 129     -11.318 -16.868 -31.881  1.00 63.83           N  
ANISOU 6650  N   ASN B 129     8548   7706   7995    392   -343    126       N  
ATOM   6651  CA  ASN B 129      -9.975 -17.011 -31.335  1.00 62.01           C  
ANISOU 6651  CA  ASN B 129     8314   7478   7766    392   -308    142       C  
ATOM   6652  C   ASN B 129      -9.491 -18.461 -31.442  1.00 62.13           C  
ANISOU 6652  C   ASN B 129     8342   7482   7781    387   -297    145       C  
ATOM   6653  O   ASN B 129     -10.119 -19.388 -30.918  1.00 64.90           O  
ANISOU 6653  O   ASN B 129     8675   7834   8146    374   -306    139       O  
ATOM   6654  CB  ASN B 129      -9.951 -16.487 -29.886  1.00 62.69           C  
ANISOU 6654  CB  ASN B 129     8358   7587   7875    380   -297    149       C  
ATOM   6655  CG  ASN B 129      -8.625 -16.724 -29.172  1.00 63.09           C  
ANISOU 6655  CG  ASN B 129     8399   7642   7929    378   -263    166       C  
ATOM   6656  OD1 ASN B 129      -7.545 -16.556 -29.739  1.00 65.34           O  
ANISOU 6656  OD1 ASN B 129     8707   7918   8198    390   -243    175       O  
ATOM   6657  ND2 ASN B 129      -8.710 -17.093 -27.901  1.00 60.98           N  
ANISOU 6657  ND2 ASN B 129     8096   7390   7682    364   -256    170       N  
ATOM   6658  N   LEU B 130      -8.380 -18.649 -32.145  1.00 60.31           N  
ANISOU 6658  N   LEU B 130     8142   7237   7533    399   -276    153       N  
ATOM   6659  CA  LEU B 130      -7.814 -19.974 -32.349  1.00 58.95           C  
ANISOU 6659  CA  LEU B 130     7986   7052   7358    397   -263    157       C  
ATOM   6660  C   LEU B 130      -6.408 -20.042 -31.766  1.00 59.46           C  
ANISOU 6660  C   LEU B 130     8044   7121   7424    399   -227    175       C  
ATOM   6661  O   LEU B 130      -5.505 -19.321 -32.206  1.00 60.93           O  
ANISOU 6661  O   LEU B 130     8247   7304   7597    412   -210    184       O  
ATOM   6662  CB  LEU B 130      -7.820 -20.342 -33.839  1.00 57.46           C  
ANISOU 6662  CB  LEU B 130     7844   6841   7145    410   -272    149       C  
ATOM   6663  CG  LEU B 130      -7.190 -21.667 -34.294  1.00 57.34           C  
ANISOU 6663  CG  LEU B 130     7854   6809   7122    411   -258    151       C  
ATOM   6664  CD1 LEU B 130      -7.763 -22.883 -33.576  1.00 55.36           C  
ANISOU 6664  CD1 LEU B 130     7583   6560   6891    393   -264    146       C  
ATOM   6665  CD2 LEU B 130      -7.342 -21.819 -35.798  1.00 57.76           C  
ANISOU 6665  CD2 LEU B 130     7953   6841   7150    424   -272    142       C  
ATOM   6666  N   VAL B 131      -6.243 -20.915 -30.773  1.00 57.84           N  
ANISOU 6666  N   VAL B 131     7815   6923   7236    386   -215    181       N  
ATOM   6667  CA  VAL B 131      -5.009 -21.010 -30.001  1.00 56.74           C  
ANISOU 6667  CA  VAL B 131     7662   6792   7102    386   -182    199       C  
ATOM   6668  C   VAL B 131      -4.246 -22.304 -30.327  1.00 59.47           C  
ANISOU 6668  C   VAL B 131     8028   7122   7442    389   -164    206       C  
ATOM   6669  O   VAL B 131      -4.599 -23.392 -29.857  1.00 59.49           O  
ANISOU 6669  O   VAL B 131     8020   7124   7457    378   -166    204       O  
ATOM   6670  CB  VAL B 131      -5.282 -20.877 -28.482  1.00 55.49           C  
ANISOU 6670  CB  VAL B 131     7457   6657   6968    371   -180    203       C  
ATOM   6671  CG1 VAL B 131      -3.976 -20.785 -27.702  1.00 55.02           C  
ANISOU 6671  CG1 VAL B 131     7383   6609   6912    372   -147    221       C  
ATOM   6672  CG2 VAL B 131      -6.147 -19.657 -28.192  1.00 52.43           C  
ANISOU 6672  CG2 VAL B 131     7050   6283   6586    369   -199    195       C  
ATOM   6673  N   ALA B 132      -3.192 -22.161 -31.131  1.00 60.55           N  
ANISOU 6673  N   ALA B 132     8196   7248   7562    403   -145    214       N  
ATOM   6674  CA  ALA B 132      -2.433 -23.295 -31.664  1.00 60.77           C  
ANISOU 6674  CA  ALA B 132     8250   7258   7581    408   -127    221       C  
ATOM   6675  C   ALA B 132      -0.972 -23.276 -31.213  1.00 60.61           C  
ANISOU 6675  C   ALA B 132     8223   7242   7560    414    -91    241       C  
ATOM   6676  O   ALA B 132      -0.053 -23.553 -31.998  1.00 59.15           O  
ANISOU 6676  O   ALA B 132     8070   7043   7361    426    -73    248       O  
ATOM   6677  CB  ALA B 132      -2.524 -23.312 -33.184  1.00 61.12           C  
ANISOU 6677  CB  ALA B 132     8340   7279   7601    422   -137    212       C  
ATOM   6678  N   VAL B 133      -0.773 -22.952 -29.940  1.00 59.48           N  
ANISOU 6678  N   VAL B 133     8041   7121   7435    405    -82    249       N  
ATOM   6679  CA  VAL B 133       0.555 -22.896 -29.335  1.00 58.02           C  
ANISOU 6679  CA  VAL B 133     7844   6945   7253    408    -50    268       C  
ATOM   6680  C   VAL B 133       1.088 -24.308 -29.114  1.00 59.10           C  
ANISOU 6680  C   VAL B 133     7985   7075   7395    406    -32    277       C  
ATOM   6681  O   VAL B 133       0.341 -25.202 -28.693  1.00 58.50           O  
ANISOU 6681  O   VAL B 133     7898   6999   7329    396    -43    271       O  
ATOM   6682  CB  VAL B 133       0.523 -22.111 -28.001  1.00 55.05           C  
ANISOU 6682  CB  VAL B 133     7424   6596   6895    398    -48    273       C  
ATOM   6683  CG1 VAL B 133       1.843 -22.206 -27.257  1.00 52.78           C  
ANISOU 6683  CG1 VAL B 133     7120   6321   6613    399    -17    292       C  
ATOM   6684  CG2 VAL B 133       0.174 -20.658 -28.259  1.00 54.54           C  
ANISOU 6684  CG2 VAL B 133     7359   6538   6826    401    -61    266       C  
ATOM   6685  N   GLU B 134       2.375 -24.490 -29.418  1.00 59.89           N  
ANISOU 6685  N   GLU B 134     8099   7168   7485    417     -4    292       N  
ATOM   6686  CA  GLU B 134       3.098 -25.753 -29.209  1.00 61.86           C  
ANISOU 6686  CA  GLU B 134     8353   7411   7738    418     17    304       C  
ATOM   6687  C   GLU B 134       2.405 -26.973 -29.834  1.00 62.19           C  
ANISOU 6687  C   GLU B 134     8418   7432   7776    416      5    293       C  
ATOM   6688  O   GLU B 134       2.217 -28.003 -29.182  1.00 61.93           O  
ANISOU 6688  O   GLU B 134     8372   7401   7755    407      9    296       O  
ATOM   6689  CB  GLU B 134       3.376 -25.973 -27.719  1.00 63.07           C  
ANISOU 6689  CB  GLU B 134     8463   7588   7911    408     29    316       C  
ATOM   6690  CG  GLU B 134       4.734 -26.590 -27.432  1.00 66.23           C  
ANISOU 6690  CG  GLU B 134     8862   7989   8312    414     62    336       C  
ATOM   6691  CD  GLU B 134       4.889 -27.045 -25.992  1.00 70.31           C  
ANISOU 6691  CD  GLU B 134     9339   8527   8846    404     72    346       C  
ATOM   6692  OE1 GLU B 134       5.757 -27.902 -25.734  1.00 73.10           O  
ANISOU 6692  OE1 GLU B 134     9692   8879   9202    408     96    361       O  
ATOM   6693  OE2 GLU B 134       4.146 -26.559 -25.114  1.00 73.83           O  
ANISOU 6693  OE2 GLU B 134     9755   8992   9305    392     57    340       O  
ATOM   6694  N   THR B 135       2.032 -26.844 -31.104  1.00 62.23           N  
ANISOU 6694  N   THR B 135     8461   7418   7764    424     -8    281       N  
ATOM   6695  CA  THR B 135       1.367 -27.924 -31.822  1.00 63.99           C  
ANISOU 6695  CA  THR B 135     8710   7620   7981    423    -21    269       C  
ATOM   6696  C   THR B 135       2.265 -28.556 -32.889  1.00 66.68           C  
ANISOU 6696  C   THR B 135     9093   7938   8304    437     -1    276       C  
ATOM   6697  O   THR B 135       1.768 -29.257 -33.776  1.00 65.09           O  
ANISOU 6697  O   THR B 135     8922   7715   8092    439    -13    264       O  
ATOM   6698  CB  THR B 135       0.063 -27.439 -32.482  1.00 64.67           C  
ANISOU 6698  CB  THR B 135     8808   7702   8062    419    -57    248       C  
ATOM   6699  OG1 THR B 135       0.324 -26.249 -33.236  1.00 66.68           O  
ANISOU 6699  OG1 THR B 135     9080   7955   8300    432    -59    247       O  
ATOM   6700  CG2 THR B 135      -1.004 -27.158 -31.431  1.00 62.58           C  
ANISOU 6700  CG2 THR B 135     8503   7457   7816    403    -78    240       C  
ATOM   6701  N   LYS B 136       3.576 -28.306 -32.790  1.00 67.94           N  
ANISOU 6701  N   LYS B 136     9253   8100   8460    447     28    294       N  
ATOM   6702  CA  LYS B 136       4.575 -28.715 -33.798  1.00 67.59           C  
ANISOU 6702  CA  LYS B 136     9248   8034   8398    463     50    303       C  
ATOM   6703  C   LYS B 136       4.344 -28.113 -35.201  1.00 67.18           C  
ANISOU 6703  C   LYS B 136     9236   7965   8323    475     37    291       C  
ATOM   6704  O   LYS B 136       4.873 -28.614 -36.197  1.00 67.69           O  
ANISOU 6704  O   LYS B 136     9339   8007   8371    488     50    294       O  
ATOM   6705  CB  LYS B 136       4.689 -30.243 -33.884  1.00 68.13           C  
ANISOU 6705  CB  LYS B 136     9330   8086   8467    462     61    305       C  
ATOM   6706  CG  LYS B 136       5.381 -30.906 -32.710  1.00 70.40           C  
ANISOU 6706  CG  LYS B 136     9587   8387   8772    457     86    322       C  
ATOM   6707  CD  LYS B 136       5.881 -32.288 -33.104  1.00 71.09           C  
ANISOU 6707  CD  LYS B 136     9700   8454   8856    462    106    329       C  
ATOM   6708  CE  LYS B 136       6.455 -33.038 -31.913  1.00 71.65           C  
ANISOU 6708  CE  LYS B 136     9740   8538   8945    457    128    346       C  
ATOM   6709  NZ  LYS B 136       5.410 -33.275 -30.880  1.00 68.53           N  
ANISOU 6709  NZ  LYS B 136     9310   8157   8568    439    109    338       N  
ATOM   6710  N   LEU B 137       3.565 -27.034 -35.260  1.00 66.82           N  
ANISOU 6710  N   LEU B 137     9182   7928   8276    473     13    280       N  
ATOM   6711  CA  LEU B 137       3.165 -26.397 -36.513  1.00 66.12           C  
ANISOU 6711  CA  LEU B 137     9128   7825   8167    484     -3    268       C  
ATOM   6712  C   LEU B 137       4.361 -25.757 -37.214  1.00 66.55           C  
ANISOU 6712  C   LEU B 137     9207   7872   8206    501     21    281       C  
ATOM   6713  O   LEU B 137       5.103 -24.982 -36.609  1.00 64.41           O  
ANISOU 6713  O   LEU B 137     8914   7616   7942    503     39    295       O  
ATOM   6714  CB  LEU B 137       2.062 -25.370 -36.231  1.00 68.27           C  
ANISOU 6714  CB  LEU B 137     9380   8113   8445    476    -33    255       C  
ATOM   6715  CG  LEU B 137       1.172 -24.747 -37.315  1.00 69.87           C  
ANISOU 6715  CG  LEU B 137     9610   8306   8631    483    -62    238       C  
ATOM   6716  CD1 LEU B 137       1.595 -23.314 -37.594  1.00 69.99           C  
ANISOU 6716  CD1 LEU B 137     9627   8327   8637    494    -56    243       C  
ATOM   6717  CD2 LEU B 137       1.109 -25.581 -38.595  1.00 71.93           C  
ANISOU 6717  CD2 LEU B 137     9918   8540   8870    492    -66    230       C  
ATOM   6718  N   ALA B 138       4.541 -26.098 -38.490  1.00 67.53           N  
ANISOU 6718  N   ALA B 138     9377   7972   8308    515     23    277       N  
ATOM   6719  CA  ALA B 138       5.754 -25.735 -39.229  1.00 67.81           C  
ANISOU 6719  CA  ALA B 138     9440   7996   8329    533     51    291       C  
ATOM   6720  C   ALA B 138       5.599 -24.457 -40.033  1.00 68.14           C  
ANISOU 6720  C   ALA B 138     9499   8035   8354    544     41    286       C  
ATOM   6721  O   ALA B 138       6.575 -23.735 -40.267  1.00 68.88           O  
ANISOU 6721  O   ALA B 138     9600   8127   8442    556     64    299       O  
ATOM   6722  CB  ALA B 138       6.178 -26.874 -40.145  1.00 67.36           C  
ANISOU 6722  CB  ALA B 138     9424   7913   8257    542     65    292       C  
ATOM   6723  N   SER B 139       4.370 -24.182 -40.451  1.00 67.84           N  
ANISOU 6723  N   SER B 139     9470   7996   8310    541      7    267       N  
ATOM   6724  CA  SER B 139       4.116 -23.103 -41.387  1.00 67.82           C  
ANISOU 6724  CA  SER B 139     9491   7987   8290    554     -4    261       C  
ATOM   6725  C   SER B 139       2.700 -22.547 -41.283  1.00 68.69           C  
ANISOU 6725  C   SER B 139     9588   8108   8403    545    -42    243       C  
ATOM   6726  O   SER B 139       1.750 -23.263 -40.956  1.00 68.01           O  
ANISOU 6726  O   SER B 139     9490   8025   8325    532    -65    230       O  
ATOM   6727  CB  SER B 139       4.374 -23.600 -42.811  1.00 68.48           C  
ANISOU 6727  CB  SER B 139     9628   8043   8346    570      0    258       C  
ATOM   6728  OG  SER B 139       4.114 -22.589 -43.763  1.00 72.24           O  
ANISOU 6728  OG  SER B 139    10131   8513   8804    584    -11    252       O  
ATOM   6729  N   LEU B 140       2.576 -21.255 -41.567  1.00 69.23           N  
ANISOU 6729  N   LEU B 140     9657   8181   8464    553    -49    242       N  
ATOM   6730  CA  LEU B 140       1.278 -20.631 -41.772  1.00 71.75           C  
ANISOU 6730  CA  LEU B 140     9974   8507   8781    550    -85    225       C  
ATOM   6731  C   LEU B 140       0.769 -20.836 -43.210  1.00 75.90           C  
ANISOU 6731  C   LEU B 140    10546   9011   9279    563   -103    212       C  
ATOM   6732  O   LEU B 140      -0.398 -20.568 -43.498  1.00 76.78           O  
ANISOU 6732  O   LEU B 140    10660   9126   9388    561   -136    197       O  
ATOM   6733  CB  LEU B 140       1.347 -19.140 -41.437  1.00 72.79           C  
ANISOU 6733  CB  LEU B 140    10086   8652   8917    553    -83    230       C  
ATOM   6734  CG  LEU B 140       1.382 -18.705 -39.970  1.00 70.73           C  
ANISOU 6734  CG  LEU B 140     9773   8416   8683    538    -77    237       C  
ATOM   6735  CD1 LEU B 140       2.000 -17.323 -39.844  1.00 71.07           C  
ANISOU 6735  CD1 LEU B 140     9808   8467   8726    545    -62    247       C  
ATOM   6736  CD2 LEU B 140      -0.011 -18.725 -39.360  1.00 70.60           C  
ANISOU 6736  CD2 LEU B 140     9729   8414   8680    523   -111    222       C  
ATOM   6737  N   GLU B 141       1.643 -21.313 -44.101  1.00 79.80           N  
ANISOU 6737  N   GLU B 141    11079   9485   9755    577    -82    219       N  
ATOM   6738  CA  GLU B 141       1.263 -21.617 -45.485  1.00 81.70           C  
ANISOU 6738  CA  GLU B 141    11368   9704   9968    590    -97    208       C  
ATOM   6739  C   GLU B 141       0.349 -22.832 -45.554  1.00 79.74           C  
ANISOU 6739  C   GLU B 141    11124   9451   9722    578   -121    191       C  
ATOM   6740  O   GLU B 141      -0.724 -22.776 -46.150  1.00 76.13           O  
ANISOU 6740  O   GLU B 141    10680   8990   9254    578   -154    174       O  
ATOM   6741  CB  GLU B 141       2.495 -21.825 -46.378  1.00 87.83           C  
ANISOU 6741  CB  GLU B 141    12185  10460  10726    609    -65    220       C  
ATOM   6742  CG  GLU B 141       3.335 -20.573 -46.609  1.00 99.91           C  
ANISOU 6742  CG  GLU B 141    13719  11991  12248    624    -43    235       C  
ATOM   6743  CD  GLU B 141       2.568 -19.451 -47.298  1.00109.84           C  
ANISOU 6743  CD  GLU B 141    14992  13250  13492    634    -68    225       C  
ATOM   6744  OE1 GLU B 141       2.412 -18.366 -46.691  1.00111.25           O  
ANISOU 6744  OE1 GLU B 141    15141  13445  13682    631    -70    228       O  
ATOM   6745  OE2 GLU B 141       2.112 -19.650 -48.446  1.00116.62           O  
ANISOU 6745  OE2 GLU B 141    15890  14093  14327    645    -84    214       O  
ATOM   6746  N   SER B 142       0.774 -23.921 -44.923  1.00 83.11           N  
ANISOU 6746  N   SER B 142    11538   9876  10163    568   -105    197       N  
ATOM   6747  CA  SER B 142       0.001 -25.162 -44.911  1.00 85.28           C  
ANISOU 6747  CA  SER B 142    11816  10145  10442    555   -123    182       C  
ATOM   6748  C   SER B 142      -1.169 -25.137 -43.918  1.00 82.55           C  
ANISOU 6748  C   SER B 142    11427   9819  10120    535   -151    171       C  
ATOM   6749  O   SER B 142      -2.044 -26.003 -43.974  1.00 85.88           O  
ANISOU 6749  O   SER B 142    11850  10236  10544    524   -173    156       O  
ATOM   6750  CB  SER B 142       0.916 -26.360 -44.633  1.00 86.66           C  
ANISOU 6750  CB  SER B 142    11994  10308  10622    552    -93    193       C  
ATOM   6751  OG  SER B 142       1.616 -26.194 -43.411  1.00 88.27           O  
ANISOU 6751  OG  SER B 142    12159  10530  10849    545    -70    210       O  
ATOM   6752  N   PHE B 143      -1.181 -24.140 -43.032  1.00 77.50           N  
ANISOU 6752  N   PHE B 143    10750   9200   9495    530   -150    178       N  
ATOM   6753  CA  PHE B 143      -2.194 -24.007 -41.977  1.00 78.20           C  
ANISOU 6753  CA  PHE B 143    10795   9309   9608    512   -172    170       C  
ATOM   6754  C   PHE B 143      -3.593 -23.711 -42.541  1.00 76.71           C  
ANISOU 6754  C   PHE B 143    10613   9121   9412    510   -213    149       C  
ATOM   6755  O   PHE B 143      -3.864 -22.588 -42.976  1.00 76.60           O  
ANISOU 6755  O   PHE B 143    10605   9111   9388    520   -225    147       O  
ATOM   6756  CB  PHE B 143      -1.758 -22.924 -40.975  1.00 82.15           C  
ANISOU 6756  CB  PHE B 143    11257   9830  10123    510   -158    184       C  
ATOM   6757  CG  PHE B 143      -2.370 -23.061 -39.598  1.00 82.87           C  
ANISOU 6757  CG  PHE B 143    11300   9942  10243    489   -167    182       C  
ATOM   6758  CD1 PHE B 143      -2.258 -24.250 -38.873  1.00 81.82           C  
ANISOU 6758  CD1 PHE B 143    11151   9810  10126    476   -157    185       C  
ATOM   6759  CD2 PHE B 143      -3.023 -21.980 -39.005  1.00 80.43           C  
ANISOU 6759  CD2 PHE B 143    10961   9652   9945    484   -183    179       C  
ATOM   6760  CE1 PHE B 143      -2.811 -24.366 -37.603  1.00 81.08           C  
ANISOU 6760  CE1 PHE B 143    11013   9736  10058    459   -164    184       C  
ATOM   6761  CE2 PHE B 143      -3.577 -22.090 -37.737  1.00 79.86           C  
ANISOU 6761  CE2 PHE B 143    10844   9599   9898    467   -190    178       C  
ATOM   6762  CZ  PHE B 143      -3.473 -23.285 -37.036  1.00 81.55           C  
ANISOU 6762  CZ  PHE B 143    11043   9814  10128    454   -181    180       C  
ATOM   6763  N   PRO B 144      -4.490 -24.721 -42.515  1.00 75.89           N  
ANISOU 6763  N   PRO B 144    10507   9013   9314    497   -235    134       N  
ATOM   6764  CA  PRO B 144      -5.789 -24.713 -43.200  1.00 75.09           C  
ANISOU 6764  CA  PRO B 144    10417   8908   9203    495   -275    113       C  
ATOM   6765  C   PRO B 144      -6.851 -23.866 -42.500  1.00 75.90           C  
ANISOU 6765  C   PRO B 144    10482   9033   9323    485   -301    106       C  
ATOM   6766  O   PRO B 144      -7.857 -24.396 -42.016  1.00 75.75           O  
ANISOU 6766  O   PRO B 144    10441   9020   9320    469   -323     93       O  
ATOM   6767  CB  PRO B 144      -6.191 -26.186 -43.167  1.00 75.73           C  
ANISOU 6767  CB  PRO B 144    10503   8979   9292    481   -282    102       C  
ATOM   6768  CG  PRO B 144      -5.609 -26.685 -41.889  1.00 72.73           C  
ANISOU 6768  CG  PRO B 144    10088   8608   8936    469   -256    116       C  
ATOM   6769  CD  PRO B 144      -4.320 -25.936 -41.694  1.00 73.56           C  
ANISOU 6769  CD  PRO B 144    10193   8717   9038    482   -222    137       C  
ATOM   6770  N   ILE B 145      -6.627 -22.558 -42.464  1.00 79.08           N  
ANISOU 6770  N   ILE B 145    10878   9445   9721    496   -297    114       N  
ATOM   6771  CA  ILE B 145      -7.512 -21.643 -41.741  1.00 80.46           C  
ANISOU 6771  CA  ILE B 145    11017   9641   9913    488   -317    110       C  
ATOM   6772  C   ILE B 145      -8.154 -20.572 -42.620  1.00 84.33           C  
ANISOU 6772  C   ILE B 145    11524  10132  10386    502   -341    101       C  
ATOM   6773  O   ILE B 145      -8.965 -19.773 -42.136  1.00 84.01           O  
ANISOU 6773  O   ILE B 145    11455  10106  10356    497   -360     97       O  
ATOM   6774  CB  ILE B 145      -6.792 -20.956 -40.565  1.00 77.65           C  
ANISOU 6774  CB  ILE B 145    10624   9302   9575    484   -291    127       C  
ATOM   6775  CG1 ILE B 145      -5.463 -20.351 -41.030  1.00 76.33           C  
ANISOU 6775  CG1 ILE B 145    10481   9127   9393    501   -259    143       C  
ATOM   6776  CG2 ILE B 145      -6.613 -21.939 -39.420  1.00 75.83           C  
ANISOU 6776  CG2 ILE B 145    10364   9079   9369    466   -277    132       C  
ATOM   6777  CD1 ILE B 145      -5.017 -19.145 -40.233  1.00 76.74           C  
ANISOU 6777  CD1 ILE B 145    10505   9196   9456    502   -244    156       C  
ATOM   6778  N   GLY B 146      -7.797 -20.564 -43.905  1.00 85.41           N  
ANISOU 6778  N   GLY B 146    11706  10250  10493    519   -340     99       N  
ATOM   6779  CA  GLY B 146      -8.357 -19.619 -44.875  1.00 82.26           C  
ANISOU 6779  CA  GLY B 146    11331   9850  10074    535   -363     92       C  
ATOM   6780  C   GLY B 146      -9.862 -19.738 -45.027  1.00 83.92           C  
ANISOU 6780  C   GLY B 146    11530  10065  10287    527   -405     72       C  
ATOM   6781  O   GLY B 146     -10.465 -19.023 -45.822  1.00 85.05           O  
ANISOU 6781  O   GLY B 146    11691  10209  10414    539   -428     64       O  
ATOM   6782  N   GLN B 147     -10.459 -20.642 -44.252  1.00 87.57           N  
ANISOU 6782  N   GLN B 147    11965  10534  10771    506   -416     64       N  
ATOM   6783  CA  GLN B 147     -11.898 -20.894 -44.266  1.00 90.33           C  
ANISOU 6783  CA  GLN B 147    12300  10890  11129    495   -455     45       C  
ATOM   6784  C   GLN B 147     -12.627 -20.008 -43.249  1.00 88.93           C  
ANISOU 6784  C   GLN B 147    12077  10736  10975    486   -467     46       C  
ATOM   6785  O   GLN B 147     -13.734 -19.535 -43.507  1.00 85.99           O  
ANISOU 6785  O   GLN B 147    11698  10371  10602    487   -499     34       O  
ATOM   6786  CB  GLN B 147     -12.192 -22.372 -43.951  1.00 97.41           C  
ANISOU 6786  CB  GLN B 147    13191  11781  12039    477   -459     35       C  
ATOM   6787  CG  GLN B 147     -11.119 -23.378 -44.378  1.00100.36           C  
ANISOU 6787  CG  GLN B 147    13596  12134  12400    480   -432     41       C  
ATOM   6788  CD  GLN B 147     -11.202 -23.794 -45.844  1.00 98.92           C  
ANISOU 6788  CD  GLN B 147    13465  11932  12187    493   -446     29       C  
ATOM   6789  OE1 GLN B 147     -12.167 -23.479 -46.548  1.00 95.99           O  
ANISOU 6789  OE1 GLN B 147    13104  11562  11804    497   -480     14       O  
ATOM   6790  NE2 GLN B 147     -10.181 -24.515 -46.307  1.00 91.35           N  
ANISOU 6790  NE2 GLN B 147    12537  10955  11215    499   -420     36       N  
ATOM   6791  N   LEU B 148     -11.995 -19.784 -42.098  1.00 91.83           N  
ANISOU 6791  N   LEU B 148    12413  11114  11362    479   -440     60       N  
ATOM   6792  CA  LEU B 148     -12.643 -19.117 -40.963  1.00 94.34           C  
ANISOU 6792  CA  LEU B 148    12684  11453  11705    467   -448     62       C  
ATOM   6793  C   LEU B 148     -12.689 -17.598 -41.112  1.00 97.59           C  
ANISOU 6793  C   LEU B 148    13094  11874  12111    481   -450     67       C  
ATOM   6794  O   LEU B 148     -11.708 -16.895 -40.827  1.00 99.43           O  
ANISOU 6794  O   LEU B 148    13326  12110  12343    489   -422     83       O  
ATOM   6795  CB  LEU B 148     -11.977 -19.511 -39.634  1.00 92.37           C  
ANISOU 6795  CB  LEU B 148    12402  11213  11481    453   -420     74       C  
ATOM   6796  CG  LEU B 148     -11.772 -20.982 -39.236  1.00 89.11           C  
ANISOU 6796  CG  LEU B 148    11985  10793  11079    438   -410     73       C  
ATOM   6797  CD1 LEU B 148     -12.898 -21.888 -39.714  1.00 84.75           C  
ANISOU 6797  CD1 LEU B 148    11440  10234  10527    429   -442     53       C  
ATOM   6798  CD2 LEU B 148     -10.430 -21.501 -39.731  1.00 89.78           C  
ANISOU 6798  CD2 LEU B 148    12103  10862  11148    448   -379     84       C  
ATOM   6799  N   ILE B 149     -13.846 -17.107 -41.549  1.00 97.20           N  
ANISOU 6799  N   ILE B 149    13043  11830  12057    485   -484     55       N  
ATOM   6800  CA  ILE B 149     -14.050 -15.690 -41.864  1.00 93.09           C  
ANISOU 6800  CA  ILE B 149    12525  11316  11527    500   -491     58       C  
ATOM   6801  C   ILE B 149     -14.136 -14.832 -40.593  1.00 89.02           C  
ANISOU 6801  C   ILE B 149    11965  10820  11036    491   -481     67       C  
ATOM   6802  O   ILE B 149     -13.636 -13.703 -40.561  1.00 89.73           O  
ANISOU 6802  O   ILE B 149    12057  10914  11122    503   -465     78       O  
ATOM   6803  CB  ILE B 149     -15.302 -15.498 -42.764  1.00 94.00           C  
ANISOU 6803  CB  ILE B 149    12654  11431  11630    507   -531     41       C  
ATOM   6804  CG1 ILE B 149     -15.242 -16.451 -43.969  1.00 93.33           C  
ANISOU 6804  CG1 ILE B 149    12611  11326  11521    513   -542     31       C  
ATOM   6805  CG2 ILE B 149     -15.434 -14.053 -43.239  1.00 93.90           C  
ANISOU 6805  CG2 ILE B 149    12650  11423  11604    526   -536     46       C  
ATOM   6806  CD1 ILE B 149     -16.581 -16.736 -44.622  1.00 94.23           C  
ANISOU 6806  CD1 ILE B 149    12730  11441  11629    512   -585     11       C  
ATOM   6807  N   THR B 150     -14.742 -15.386 -39.546  1.00 86.84           N  
ANISOU 6807  N   THR B 150    11651  10555  10786    471   -488     62       N  
ATOM   6808  CA  THR B 150     -14.999 -14.649 -38.304  1.00 84.07           C  
ANISOU 6808  CA  THR B 150    11257  10223  10459    462   -482     68       C  
ATOM   6809  C   THR B 150     -13.796 -14.568 -37.363  1.00 82.11           C  
ANISOU 6809  C   THR B 150    10994   9981  10223    456   -444     85       C  
ATOM   6810  O   THR B 150     -13.869 -13.920 -36.316  1.00 85.06           O  
ANISOU 6810  O   THR B 150    11333  10370  10615    449   -436     91       O  
ATOM   6811  CB  THR B 150     -16.205 -15.232 -37.528  1.00 84.99           C  
ANISOU 6811  CB  THR B 150    11337  10351  10600    442   -506     56       C  
ATOM   6812  OG1 THR B 150     -16.013 -16.637 -37.316  1.00 82.57           O  
ANISOU 6812  OG1 THR B 150    11032  10038  10302    429   -501     53       O  
ATOM   6813  CG2 THR B 150     -17.522 -14.988 -38.286  1.00 85.63           C  
ANISOU 6813  CG2 THR B 150    11425  10433  10675    447   -546     41       C  
ATOM   6814  N   LEU B 151     -12.697 -15.221 -37.738  1.00 81.33           N  
ANISOU 6814  N   LEU B 151    10921   9869  10112    461   -421     92       N  
ATOM   6815  CA  LEU B 151     -11.493 -15.276 -36.908  1.00 77.97           C  
ANISOU 6815  CA  LEU B 151    10482   9446   9696    456   -385    108       C  
ATOM   6816  C   LEU B 151     -10.903 -13.893 -36.626  1.00 76.71           C  
ANISOU 6816  C   LEU B 151    10315   9295   9535    465   -366    120       C  
ATOM   6817  O   LEU B 151     -10.603 -13.135 -37.549  1.00 76.57           O  
ANISOU 6817  O   LEU B 151    10326   9269   9498    483   -364    122       O  
ATOM   6818  CB  LEU B 151     -10.439 -16.178 -37.556  1.00 78.22           C  
ANISOU 6818  CB  LEU B 151    10547   9461   9712    462   -364    114       C  
ATOM   6819  CG  LEU B 151      -9.353 -16.730 -36.631  1.00 78.53           C  
ANISOU 6819  CG  LEU B 151    10570   9504   9764    453   -331    128       C  
ATOM   6820  CD1 LEU B 151      -9.918 -17.858 -35.782  1.00 79.66           C  
ANISOU 6820  CD1 LEU B 151    10686   9652   9928    433   -339    122       C  
ATOM   6821  CD2 LEU B 151      -8.144 -17.207 -37.420  1.00 76.90           C  
ANISOU 6821  CD2 LEU B 151    10400   9278   9538    465   -307    136       C  
ATOM   6822  N   LYS B 152     -10.750 -13.577 -35.341  1.00 75.92           N  
ANISOU 6822  N   LYS B 152    10176   9211   9457    453   -353    127       N  
ATOM   6823  CA  LYS B 152     -10.194 -12.297 -34.902  1.00 73.45           C  
ANISOU 6823  CA  LYS B 152     9851   8907   9146    458   -335    137       C  
ATOM   6824  C   LYS B 152      -8.744 -12.444 -34.466  1.00 72.06           C  
ANISOU 6824  C   LYS B 152     9675   8731   8972    458   -298    152       C  
ATOM   6825  O   LYS B 152      -7.875 -11.726 -34.957  1.00 71.76           O  
ANISOU 6825  O   LYS B 152     9657   8687   8921    471   -279    161       O  
ATOM   6826  CB  LYS B 152     -11.017 -11.699 -33.754  1.00 74.19           C  
ANISOU 6826  CB  LYS B 152     9902   9021   9263    446   -345    134       C  
ATOM   6827  CG  LYS B 152     -12.393 -11.192 -34.149  1.00 75.50           C  
ANISOU 6827  CG  LYS B 152    10066   9191   9429    449   -379    121       C  
ATOM   6828  CD  LYS B 152     -13.001 -10.356 -33.039  1.00 75.96           C  
ANISOU 6828  CD  LYS B 152    10084   9268   9509    440   -382    121       C  
ATOM   6829  CE  LYS B 152     -14.461 -10.061 -33.327  1.00 80.45           C  
ANISOU 6829  CE  LYS B 152    10646   9841  10080    441   -417    108       C  
ATOM   6830  NZ  LYS B 152     -14.923  -8.862 -32.579  1.00 83.66           N  
ANISOU 6830  NZ  LYS B 152    11023  10261  10499    440   -418    110       N  
ATOM   6831  N   LYS B 153      -8.495 -13.367 -33.536  1.00 71.86           N  
ANISOU 6831  N   LYS B 153     9627   8713   8963    443   -287    156       N  
ATOM   6832  CA  LYS B 153      -7.152 -13.603 -33.006  1.00 70.71           C  
ANISOU 6832  CA  LYS B 153     9476   8568   8820    441   -253    171       C  
ATOM   6833  C   LYS B 153      -6.647 -14.987 -33.371  1.00 68.30           C  
ANISOU 6833  C   LYS B 153     9191   8251   8509    440   -245    173       C  
ATOM   6834  O   LYS B 153      -7.389 -15.965 -33.294  1.00 66.86           O  
ANISOU 6834  O   LYS B 153     9003   8065   8333    430   -262    164       O  
ATOM   6835  CB  LYS B 153      -7.122 -13.481 -31.483  1.00 72.05           C  
ANISOU 6835  CB  LYS B 153     9601   8760   9015    425   -243    176       C  
ATOM   6836  CG  LYS B 153      -7.540 -12.146 -30.904  1.00 74.26           C  
ANISOU 6836  CG  LYS B 153     9857   9054   9303    423   -248    175       C  
ATOM   6837  CD  LYS B 153      -7.618 -12.278 -29.390  1.00 77.73           C  
ANISOU 6837  CD  LYS B 153    10253   9513   9766    406   -241    178       C  
ATOM   6838  CE  LYS B 153      -8.583 -11.277 -28.780  1.00 80.10           C  
ANISOU 6838  CE  LYS B 153    10526   9828  10079    401   -257    172       C  
ATOM   6839  NZ  LYS B 153      -8.935 -11.677 -27.391  1.00 80.78           N  
ANISOU 6839  NZ  LYS B 153    10573   9932  10188    383   -256    172       N  
ATOM   6840  N   LEU B 154      -5.372 -15.056 -33.744  1.00 68.07           N  
ANISOU 6840  N   LEU B 154     9182   8211   8468    449   -217    185       N  
ATOM   6841  CA  LEU B 154      -4.695 -16.320 -34.004  1.00 66.11           C  
ANISOU 6841  CA  LEU B 154     8951   7952   8216    449   -203    190       C  
ATOM   6842  C   LEU B 154      -3.380 -16.364 -33.230  1.00 66.09           C  
ANISOU 6842  C   LEU B 154     8934   7956   8221    446   -168    207       C  
ATOM   6843  O   LEU B 154      -2.583 -15.423 -33.270  1.00 63.44           O  
ANISOU 6843  O   LEU B 154     8600   7623   7880    454   -150    216       O  
ATOM   6844  CB  LEU B 154      -4.475 -16.513 -35.511  1.00 66.35           C  
ANISOU 6844  CB  LEU B 154     9030   7958   8219    466   -205    186       C  
ATOM   6845  CG  LEU B 154      -4.020 -17.847 -36.130  1.00 67.85           C  
ANISOU 6845  CG  LEU B 154     9248   8131   8400    468   -197    187       C  
ATOM   6846  CD1 LEU B 154      -2.540 -17.819 -36.478  1.00 70.35           C  
ANISOU 6846  CD1 LEU B 154     9586   8438   8706    480   -163    203       C  
ATOM   6847  CD2 LEU B 154      -4.351 -19.066 -35.277  1.00 69.09           C  
ANISOU 6847  CD2 LEU B 154     9382   8293   8575    451   -200    185       C  
ATOM   6848  N   ASN B 155      -3.170 -17.462 -32.512  1.00 65.65           N  
ANISOU 6848  N   ASN B 155     8862   7904   8178    435   -159    211       N  
ATOM   6849  CA  ASN B 155      -1.974 -17.634 -31.703  1.00 63.70           C  
ANISOU 6849  CA  ASN B 155     8598   7666   7939    432   -128    227       C  
ATOM   6850  C   ASN B 155      -1.205 -18.888 -32.102  1.00 62.01           C  
ANISOU 6850  C   ASN B 155     8405   7436   7717    436   -111    234       C  
ATOM   6851  O   ASN B 155      -1.681 -20.007 -31.903  1.00 62.75           O  
ANISOU 6851  O   ASN B 155     8495   7527   7817    427   -119    229       O  
ATOM   6852  CB  ASN B 155      -2.356 -17.686 -30.219  1.00 61.96           C  
ANISOU 6852  CB  ASN B 155     8331   7468   7743    415   -130    228       C  
ATOM   6853  CG  ASN B 155      -1.152 -17.617 -29.290  1.00 61.82           C  
ANISOU 6853  CG  ASN B 155     8291   7463   7733    412    -99    245       C  
ATOM   6854  OD1 ASN B 155      -1.313 -17.640 -28.075  1.00 61.35           O  
ANISOU 6854  OD1 ASN B 155     8195   7422   7692    399    -98    247       O  
ATOM   6855  ND2 ASN B 155       0.055 -17.538 -29.849  1.00 61.65           N  
ANISOU 6855  ND2 ASN B 155     8292   7432   7700    423    -75    256       N  
ATOM   6856  N   VAL B 156      -0.016 -18.697 -32.664  1.00 60.70           N  
ANISOU 6856  N   VAL B 156     8261   7261   7539    448    -86    246       N  
ATOM   6857  CA  VAL B 156       0.848 -19.826 -33.037  1.00 62.36           C  
ANISOU 6857  CA  VAL B 156     8493   7458   7743    453    -65    255       C  
ATOM   6858  C   VAL B 156       2.240 -19.750 -32.383  1.00 63.19           C  
ANISOU 6858  C   VAL B 156     8582   7571   7854    455    -31    274       C  
ATOM   6859  O   VAL B 156       3.253 -20.138 -32.980  1.00 64.68           O  
ANISOU 6859  O   VAL B 156     8796   7747   8032    466     -9    284       O  
ATOM   6860  CB  VAL B 156       0.938 -20.037 -34.577  1.00 59.34           C  
ANISOU 6860  CB  VAL B 156     8160   7050   7336    469    -68    250       C  
ATOM   6861  CG1 VAL B 156      -0.341 -20.666 -35.115  1.00 59.00           C  
ANISOU 6861  CG1 VAL B 156     8131   6997   7288    465   -100    232       C  
ATOM   6862  CG2 VAL B 156       1.240 -18.737 -35.305  1.00 59.22           C  
ANISOU 6862  CG2 VAL B 156     8162   7030   7306    483    -65    251       C  
ATOM   6863  N   ALA B 157       2.276 -19.262 -31.146  1.00 62.34           N  
ANISOU 6863  N   ALA B 157     8434   7487   7764    444    -27    278       N  
ATOM   6864  CA  ALA B 157       3.510 -19.218 -30.366  1.00 62.73           C  
ANISOU 6864  CA  ALA B 157     8464   7548   7822    443      2    296       C  
ATOM   6865  C   ALA B 157       4.055 -20.624 -30.110  1.00 60.45           C  
ANISOU 6865  C   ALA B 157     8175   7254   7536    441     17    305       C  
ATOM   6866  O   ALA B 157       3.309 -21.597 -30.191  1.00 62.69           O  
ANISOU 6866  O   ALA B 157     8465   7531   7822    436      3    297       O  
ATOM   6867  CB  ALA B 157       3.274 -18.488 -29.050  1.00 62.11           C  
ANISOU 6867  CB  ALA B 157     8341   7496   7761    430     -1    296       C  
ATOM   6868  N   HIS B 158       5.352 -20.721 -29.820  1.00 58.91           N  
ANISOU 6868  N   HIS B 158     7975   7063   7342    445     47    322       N  
ATOM   6869  CA  HIS B 158       5.991 -21.981 -29.418  1.00 60.78           C  
ANISOU 6869  CA  HIS B 158     8208   7299   7585    444     66    333       C  
ATOM   6870  C   HIS B 158       5.849 -23.081 -30.445  1.00 62.13           C  
ANISOU 6870  C   HIS B 158     8417   7445   7743    452     64    330       C  
ATOM   6871  O   HIS B 158       5.438 -24.195 -30.126  1.00 63.11           O  
ANISOU 6871  O   HIS B 158     8537   7567   7875    445     60    328       O  
ATOM   6872  CB  HIS B 158       5.457 -22.437 -28.056  1.00 60.65           C  
ANISOU 6872  CB  HIS B 158     8151   7303   7588    428     58    333       C  
ATOM   6873  CG  HIS B 158       6.416 -23.302 -27.274  1.00 63.08           C  
ANISOU 6873  CG  HIS B 158     8442   7619   7905    427     84    350       C  
ATOM   6874  ND1 HIS B 158       6.473 -23.278 -25.931  1.00 64.49           N  
ANISOU 6874  ND1 HIS B 158     8580   7822   8100    416     88    356       N  
ATOM   6875  CD2 HIS B 158       7.382 -24.220 -27.693  1.00 62.19           C  
ANISOU 6875  CD2 HIS B 158     8349   7494   7786    436    108    363       C  
ATOM   6876  CE1 HIS B 158       7.417 -24.143 -25.506  1.00 63.86           C  
ANISOU 6876  CE1 HIS B 158     8494   7745   8023    418    112    373       C  
ATOM   6877  NE2 HIS B 158       7.974 -24.715 -26.586  1.00 63.32           N  
ANISOU 6877  NE2 HIS B 158     8463   7654   7942    431    124    377       N  
ATOM   6878  N   ASN B 159       6.189 -22.781 -31.692  1.00 64.49           N  
ANISOU 6878  N   ASN B 159     8754   7725   8024    466     68    329       N  
ATOM   6879  CA  ASN B 159       6.107 -23.771 -32.767  1.00 67.36           C  
ANISOU 6879  CA  ASN B 159     9157   8062   8373    474     68    324       C  
ATOM   6880  C   ASN B 159       7.408 -23.921 -33.579  1.00 70.30           C  
ANISOU 6880  C   ASN B 159     9560   8419   8732    491     97    338       C  
ATOM   6881  O   ASN B 159       8.473 -23.493 -33.126  1.00 71.85           O  
ANISOU 6881  O   ASN B 159     9741   8626   8933    494    122    354       O  
ATOM   6882  CB  ASN B 159       4.894 -23.484 -33.663  1.00 64.52           C  
ANISOU 6882  CB  ASN B 159     8821   7690   8001    475     36    304       C  
ATOM   6883  CG  ASN B 159       3.628 -24.163 -33.167  1.00 63.36           C  
ANISOU 6883  CG  ASN B 159     8658   7548   7866    461     10    290       C  
ATOM   6884  OD1 ASN B 159       3.633 -25.350 -32.838  1.00 65.44           O  
ANISOU 6884  OD1 ASN B 159     8918   7807   8136    455     15    293       O  
ATOM   6885  ND2 ASN B 159       2.533 -23.415 -33.124  1.00 61.13           N  
ANISOU 6885  ND2 ASN B 159     8366   7273   7586    455    -17    276       N  
ATOM   6886  N   PHE B 160       7.320 -24.542 -34.758  1.00 74.59           N  
ANISOU 6886  N   PHE B 160    10145   8936   9257    501     95    333       N  
ATOM   6887  CA  PHE B 160       8.482 -24.726 -35.641  1.00 78.40           C  
ANISOU 6887  CA  PHE B 160    10660   9401   9725    518    123    345       C  
ATOM   6888  C   PHE B 160       8.352 -23.892 -36.925  1.00 78.05           C  
ANISOU 6888  C   PHE B 160    10653   9341   9659    531    115    337       C  
ATOM   6889  O   PHE B 160       8.718 -24.338 -38.022  1.00 80.13           O  
ANISOU 6889  O   PHE B 160    10958   9582   9906    545    125    338       O  
ATOM   6890  CB  PHE B 160       8.706 -26.215 -35.969  1.00 82.26           C  
ANISOU 6890  CB  PHE B 160    11170   9872  10210    520    134    348       C  
ATOM   6891  CG  PHE B 160       8.926 -27.088 -34.759  1.00 86.28           C  
ANISOU 6891  CG  PHE B 160    11646  10396  10739    509    145    358       C  
ATOM   6892  CD1 PHE B 160      10.060 -26.934 -33.961  1.00 88.18           C  
ANISOU 6892  CD1 PHE B 160    11861  10652  10991    511    173    378       C  
ATOM   6893  CD2 PHE B 160       8.007 -28.081 -34.424  1.00 87.48           C  
ANISOU 6893  CD2 PHE B 160    11792  10545  10898    498    128    348       C  
ATOM   6894  CE1 PHE B 160      10.260 -27.742 -32.848  1.00 88.98           C  
ANISOU 6894  CE1 PHE B 160    11931  10766  11108    501    182    387       C  
ATOM   6895  CE2 PHE B 160       8.204 -28.892 -33.313  1.00 87.18           C  
ANISOU 6895  CE2 PHE B 160    11724  10520  10878    488    139    357       C  
ATOM   6896  CZ  PHE B 160       9.330 -28.723 -32.523  1.00 88.45           C  
ANISOU 6896  CZ  PHE B 160    11860  10697  11049    491    166    377       C  
ATOM   6897  N   ILE B 161       7.831 -22.677 -36.767  1.00 75.62           N  
ANISOU 6897  N   ILE B 161    10331   9045   9354    528     99    330       N  
ATOM   6898  CA  ILE B 161       7.626 -21.742 -37.873  1.00 72.87           C  
ANISOU 6898  CA  ILE B 161    10013   8684   8986    541     90    323       C  
ATOM   6899  C   ILE B 161       8.928 -21.017 -38.184  1.00 74.97           C  
ANISOU 6899  C   ILE B 161    10289   8948   9248    554    121    339       C  
ATOM   6900  O   ILE B 161       9.497 -20.343 -37.324  1.00 77.40           O  
ANISOU 6900  O   ILE B 161    10564   9273   9569    549    135    349       O  
ATOM   6901  CB  ILE B 161       6.494 -20.739 -37.559  1.00 68.47           C  
ANISOU 6901  CB  ILE B 161     9438   8142   8435    533     60    309       C  
ATOM   6902  CG1 ILE B 161       5.153 -21.473 -37.505  1.00 66.03           C  
ANISOU 6902  CG1 ILE B 161     9127   7832   8129    522     28    292       C  
ATOM   6903  CG2 ILE B 161       6.450 -19.622 -38.593  1.00 65.73           C  
ANISOU 6903  CG2 ILE B 161     9119   7785   8070    547     55    305       C  
ATOM   6904  CD1 ILE B 161       4.065 -20.715 -36.788  1.00 66.85           C  
ANISOU 6904  CD1 ILE B 161     9199   7954   8245    510      1    280       C  
ATOM   6905  N   HIS B 162       9.395 -21.172 -39.419  1.00 77.80           N  
ANISOU 6905  N   HIS B 162    10691   9283   9586    571    132    342       N  
ATOM   6906  CA  HIS B 162      10.687 -20.626 -39.826  1.00 77.00           C  
ANISOU 6906  CA  HIS B 162    10603   9175   9478    585    164    358       C  
ATOM   6907  C   HIS B 162      10.536 -19.318 -40.549  1.00 73.07           C  
ANISOU 6907  C   HIS B 162    10122   8673   8968    595    159    353       C  
ATOM   6908  O   HIS B 162      11.401 -18.445 -40.445  1.00 66.81           O  
ANISOU 6908  O   HIS B 162     9320   7883   8178    600    180    365       O  
ATOM   6909  CB  HIS B 162      11.472 -21.655 -40.648  1.00 79.91           C  
ANISOU 6909  CB  HIS B 162    11007   9521   9834    598    187    366       C  
ATOM   6910  CG  HIS B 162      11.799 -22.923 -39.880  1.00 84.94           C  
ANISOU 6910  CG  HIS B 162    11625  10162  10483    589    198    374       C  
ATOM   6911  ND1 HIS B 162      12.839 -23.007 -39.023  1.00 86.21           N  
ANISOU 6911  ND1 HIS B 162    11757  10336  10659    586    225    392       N  
ATOM   6912  CD2 HIS B 162      11.167 -24.170 -39.851  1.00 87.89           C  
ANISOU 6912  CD2 HIS B 162    12006  10529  10857    582    186    366       C  
ATOM   6913  CE1 HIS B 162      12.878 -24.243 -38.479  1.00 84.29           C  
ANISOU 6913  CE1 HIS B 162    11505  10095  10427    579    230    395       C  
ATOM   6914  NE2 HIS B 162      11.855 -24.953 -38.985  1.00 86.60           N  
ANISOU 6914  NE2 HIS B 162    11819  10375  10710    577    206    379       N  
ATOM   6915  N   SER B 163       9.417 -19.167 -41.259  1.00 73.09           N  
ANISOU 6915  N   SER B 163    10147   8666   8957    598    129    336       N  
ATOM   6916  CA  SER B 163       9.146 -17.987 -42.083  1.00 72.87           C  
ANISOU 6916  CA  SER B 163    10140   8632   8915    609    121    331       C  
ATOM   6917  C   SER B 163       8.230 -16.987 -41.394  1.00 75.88           C  
ANISOU 6917  C   SER B 163    10490   9032   9307    598     97    321       C  
ATOM   6918  O   SER B 163       7.492 -17.334 -40.474  1.00 77.54           O  
ANISOU 6918  O   SER B 163    10668   9258   9533    582     78    314       O  
ATOM   6919  CB  SER B 163       8.521 -18.402 -43.413  1.00 70.48           C  
ANISOU 6919  CB  SER B 163     9886   8307   8587    622    104    319       C  
ATOM   6920  OG  SER B 163       8.175 -17.267 -44.179  1.00 67.29           O  
ANISOU 6920  OG  SER B 163     9500   7896   8167    634     93    314       O  
ATOM   6921  N   CYS B 164       8.275 -15.744 -41.864  1.00 78.19           N  
ANISOU 6921  N   CYS B 164    10792   9323   9592    608     98    322       N  
ATOM   6922  CA  CYS B 164       7.444 -14.674 -41.327  1.00 77.36           C  
ANISOU 6922  CA  CYS B 164    10662   9235   9496    600     77    313       C  
ATOM   6923  C   CYS B 164       6.366 -14.232 -42.320  1.00 79.51           C  
ANISOU 6923  C   CYS B 164    10963   9496   9750    610     48    298       C  
ATOM   6924  O   CYS B 164       5.638 -13.266 -42.071  1.00 78.96           O  
ANISOU 6924  O   CYS B 164    10879   9438   9685    606     31    291       O  
ATOM   6925  CB  CYS B 164       8.320 -13.484 -40.942  1.00 77.61           C  
ANISOU 6925  CB  CYS B 164    10676   9274   9536    602    102    325       C  
ATOM   6926  SG  CYS B 164       7.426 -12.142 -40.130  1.00 77.41           S  
ANISOU 6926  SG  CYS B 164    10615   9270   9525    591     81    316       S  
ATOM   6927  N   LYS B 165       6.270 -14.945 -43.442  1.00 81.82           N  
ANISOU 6927  N   LYS B 165    11298   9768  10021    622     44    294       N  
ATOM   6928  CA  LYS B 165       5.336 -14.605 -44.518  1.00 80.78           C  
ANISOU 6928  CA  LYS B 165    11199   9625   9868    634     18    281       C  
ATOM   6929  C   LYS B 165       3.904 -14.577 -44.001  1.00 78.76           C  
ANISOU 6929  C   LYS B 165    10919   9384   9621    620    -19    264       C  
ATOM   6930  O   LYS B 165       3.484 -15.466 -43.265  1.00 78.86           O  
ANISOU 6930  O   LYS B 165    10909   9406   9648    604    -30    259       O  
ATOM   6931  CB  LYS B 165       5.484 -15.590 -45.695  1.00 80.90           C  
ANISOU 6931  CB  LYS B 165    11261   9616   9860    647     19    278       C  
ATOM   6932  CG  LYS B 165       4.428 -15.492 -46.794  1.00 77.60           C  
ANISOU 6932  CG  LYS B 165    10878   9187   9419    657    -11    262       C  
ATOM   6933  CD  LYS B 165       4.787 -14.497 -47.887  1.00 76.44           C  
ANISOU 6933  CD  LYS B 165    10766   9026   9249    680     -2    267       C  
ATOM   6934  CE  LYS B 165       3.723 -14.502 -48.979  1.00 77.66           C  
ANISOU 6934  CE  LYS B 165    10956   9170   9379    690    -34    251       C  
ATOM   6935  NZ  LYS B 165       4.000 -13.557 -50.100  1.00 74.93           N  
ANISOU 6935  NZ  LYS B 165    10647   8810   9010    714    -26    256       N  
ATOM   6936  N   LEU B 166       3.180 -13.526 -44.365  1.00 81.02           N  
ANISOU 6936  N   LEU B 166    11210   9672   9900    627    -38    257       N  
ATOM   6937  CA  LEU B 166       1.764 -13.421 -44.065  1.00 82.62           C  
ANISOU 6937  CA  LEU B 166    11395   9886  10108    617    -76    241       C  
ATOM   6938  C   LEU B 166       1.027 -13.994 -45.268  1.00 82.70           C  
ANISOU 6938  C   LEU B 166    11445   9880  10095    627   -100    228       C  
ATOM   6939  O   LEU B 166       0.955 -13.345 -46.314  1.00 83.74           O  
ANISOU 6939  O   LEU B 166    11611  10001  10206    645   -104    226       O  
ATOM   6940  CB  LEU B 166       1.364 -11.961 -43.819  1.00 87.51           C  
ANISOU 6940  CB  LEU B 166    11998  10517  10733    619    -83    240       C  
ATOM   6941  CG  LEU B 166       1.864 -11.216 -42.571  1.00 91.00           C  
ANISOU 6941  CG  LEU B 166    12397  10978  11200    607    -64    250       C  
ATOM   6942  CD1 LEU B 166       3.332 -10.830 -42.677  1.00 90.88           C  
ANISOU 6942  CD1 LEU B 166    12391  10956  11183    615    -25    267       C  
ATOM   6943  CD2 LEU B 166       1.026  -9.970 -42.326  1.00 90.30           C  
ANISOU 6943  CD2 LEU B 166    12291  10900  11115    607    -82    243       C  
ATOM   6944  N   PRO B 167       0.492 -15.221 -45.131  1.00 83.57           N  
ANISOU 6944  N   PRO B 167    11553   9989  10208    616   -117    218       N  
ATOM   6945  CA  PRO B 167      -0.124 -15.976 -46.230  1.00 85.26           C  
ANISOU 6945  CA  PRO B 167    11806  10187  10401    624   -138    205       C  
ATOM   6946  C   PRO B 167      -1.212 -15.212 -46.979  1.00 84.55           C  
ANISOU 6946  C   PRO B 167    11731  10096  10295    634   -171    192       C  
ATOM   6947  O   PRO B 167      -1.923 -14.403 -46.384  1.00 82.26           O  
ANISOU 6947  O   PRO B 167    11412   9823  10018    627   -187    188       O  
ATOM   6948  CB  PRO B 167      -0.732 -17.187 -45.523  1.00 84.07           C  
ANISOU 6948  CB  PRO B 167    11633  10043  10266    604   -154    195       C  
ATOM   6949  CG  PRO B 167       0.125 -17.373 -44.326  1.00 85.82           C  
ANISOU 6949  CG  PRO B 167    11818  10276  10511    592   -126    209       C  
ATOM   6950  CD  PRO B 167       0.459 -15.983 -43.871  1.00 83.09           C  
ANISOU 6950  CD  PRO B 167    11453   9943  10174    595   -114    219       C  
ATOM   6951  N   ALA B 168      -1.331 -15.497 -48.274  1.00 84.21           N  
ANISOU 6951  N   ALA B 168    11735  10036  10225    649   -180    185       N  
ATOM   6952  CA  ALA B 168      -2.256 -14.802 -49.165  1.00 82.75           C  
ANISOU 6952  CA  ALA B 168    11572   9849  10021    662   -209    174       C  
ATOM   6953  C   ALA B 168      -3.720 -14.923 -48.743  1.00 85.81           C  
ANISOU 6953  C   ALA B 168    11933  10250  10418    648   -250    157       C  
ATOM   6954  O   ALA B 168      -4.498 -13.982 -48.931  1.00 86.37           O  
ANISOU 6954  O   ALA B 168    12000  10329  10486    654   -271    151       O  
ATOM   6955  CB  ALA B 168      -2.073 -15.289 -50.595  1.00 80.59           C  
ANISOU 6955  CB  ALA B 168    11353   9552   9715    681   -210    170       C  
ATOM   6956  N   TYR B 169      -4.092 -16.068 -48.167  1.00 85.41           N  
ANISOU 6956  N   TYR B 169    11864  10203  10382    630   -259    149       N  
ATOM   6957  CA  TYR B 169      -5.489 -16.310 -47.787  1.00 86.12           C  
ANISOU 6957  CA  TYR B 169    11930  10306  10484    615   -298    131       C  
ATOM   6958  C   TYR B 169      -6.015 -15.354 -46.707  1.00 86.63           C  
ANISOU 6958  C   TYR B 169    11949  10393  10573    605   -305    133       C  
ATOM   6959  O   TYR B 169      -7.231 -15.238 -46.517  1.00 86.12           O  
ANISOU 6959  O   TYR B 169    11866  10339  10515    598   -338    120       O  
ATOM   6960  CB  TYR B 169      -5.719 -17.775 -47.390  1.00 85.22           C  
ANISOU 6960  CB  TYR B 169    11807  10189  10381    597   -304    123       C  
ATOM   6961  CG  TYR B 169      -4.940 -18.256 -46.182  1.00 83.33           C  
ANISOU 6961  CG  TYR B 169    11535   9958  10168    582   -275    135       C  
ATOM   6962  CD1 TYR B 169      -5.244 -17.800 -44.898  1.00 80.43           C  
ANISOU 6962  CD1 TYR B 169    11119   9612   9828    567   -276    139       C  
ATOM   6963  CD2 TYR B 169      -3.918 -19.196 -46.321  1.00 82.96           C  
ANISOU 6963  CD2 TYR B 169    11506   9896  10116    583   -248    144       C  
ATOM   6964  CE1 TYR B 169      -4.540 -18.246 -43.794  1.00 79.64           C  
ANISOU 6964  CE1 TYR B 169    10989   9519   9749    554   -251    150       C  
ATOM   6965  CE2 TYR B 169      -3.212 -19.652 -45.218  1.00 81.20           C  
ANISOU 6965  CE2 TYR B 169    11253   9681   9916    570   -222    156       C  
ATOM   6966  CZ  TYR B 169      -3.526 -19.170 -43.961  1.00 79.52           C  
ANISOU 6966  CZ  TYR B 169    10992   9490   9729    556   -224    159       C  
ATOM   6967  OH  TYR B 169      -2.832 -19.616 -42.866  1.00 79.57           O  
ANISOU 6967  OH  TYR B 169    10969   9505   9757    544   -200    171       O  
ATOM   6968  N   PHE B 170      -5.094 -14.670 -46.022  1.00 83.22           N  
ANISOU 6968  N   PHE B 170    11498   9968  10153    605   -274    150       N  
ATOM   6969  CA  PHE B 170      -5.418 -13.666 -45.000  1.00 82.03           C  
ANISOU 6969  CA  PHE B 170    11306   9837  10023    597   -276    153       C  
ATOM   6970  C   PHE B 170      -6.421 -12.615 -45.486  1.00 81.63           C  
ANISOU 6970  C   PHE B 170    11259   9791   9963    607   -304    145       C  
ATOM   6971  O   PHE B 170      -7.087 -11.972 -44.675  1.00 81.71           O  
ANISOU 6971  O   PHE B 170    11234   9819   9992    598   -316    142       O  
ATOM   6972  CB  PHE B 170      -4.141 -12.964 -44.516  1.00 84.77           C  
ANISOU 6972  CB  PHE B 170    11644  10186  10378    601   -237    172       C  
ATOM   6973  CG  PHE B 170      -3.422 -13.667 -43.386  1.00 87.67           C  
ANISOU 6973  CG  PHE B 170    11981  10561  10767    584   -214    181       C  
ATOM   6974  CD1 PHE B 170      -3.270 -15.054 -43.370  1.00 91.11           C  
ANISOU 6974  CD1 PHE B 170    12423  10990  11204    576   -212    178       C  
ATOM   6975  CD2 PHE B 170      -2.852 -12.926 -42.350  1.00 87.01           C  
ANISOU 6975  CD2 PHE B 170    11863  10492  10702    577   -193    192       C  
ATOM   6976  CE1 PHE B 170      -2.596 -15.684 -42.329  1.00 88.80           C  
ANISOU 6976  CE1 PHE B 170    12103  10705  10931    561   -190    187       C  
ATOM   6977  CE2 PHE B 170      -2.170 -13.550 -41.313  1.00 84.25           C  
ANISOU 6977  CE2 PHE B 170    11487  10151  10372    562   -172    201       C  
ATOM   6978  CZ  PHE B 170      -2.043 -14.930 -41.302  1.00 87.60           C  
ANISOU 6978  CZ  PHE B 170    11917  10568  10798    555   -170    199       C  
ATOM   6979  N   SER B 171      -6.523 -12.438 -46.805  1.00 80.79           N  
ANISOU 6979  N   SER B 171    11196   9670   9829    627   -313    141       N  
ATOM   6980  CA  SER B 171      -7.508 -11.515 -47.388  1.00 79.12           C  
ANISOU 6980  CA  SER B 171    10992   9462   9606    639   -341    133       C  
ATOM   6981  C   SER B 171      -8.940 -12.065 -47.337  1.00 75.86           C  
ANISOU 6981  C   SER B 171    10566   9058   9199    628   -383    114       C  
ATOM   6982  O   SER B 171      -9.907 -11.317 -47.506  1.00 72.38           O  
ANISOU 6982  O   SER B 171    10119   8626   8756    633   -409    107       O  
ATOM   6983  CB  SER B 171      -7.116 -11.082 -48.811  1.00 77.55           C  
ANISOU 6983  CB  SER B 171    10845   9246   9374    665   -337    136       C  
ATOM   6984  OG  SER B 171      -6.731 -12.185 -49.608  1.00 78.57           O  
ANISOU 6984  OG  SER B 171    11009   9358   9485    669   -334    132       O  
ATOM   6985  N   ASN B 172      -9.072 -13.368 -47.100  1.00 74.93           N  
ANISOU 6985  N   ASN B 172    10443   8938   9088    612   -389    106       N  
ATOM   6986  CA  ASN B 172     -10.369 -13.943 -46.760  1.00 77.61           C  
ANISOU 6986  CA  ASN B 172    10760   9287   9440    597   -425     89       C  
ATOM   6987  C   ASN B 172     -10.631 -13.824 -45.257  1.00 78.80           C  
ANISOU 6987  C   ASN B 172    10857   9458   9625    576   -421     92       C  
ATOM   6988  O   ASN B 172     -11.778 -13.887 -44.815  1.00 76.64           O  
ANISOU 6988  O   ASN B 172    10556   9196   9365    565   -450     81       O  
ATOM   6989  CB  ASN B 172     -10.480 -15.397 -47.238  1.00 80.48           C  
ANISOU 6989  CB  ASN B 172    11144   9638   9796    590   -435     78       C  
ATOM   6990  CG  ASN B 172     -10.825 -15.511 -48.722  1.00 82.25           C  
ANISOU 6990  CG  ASN B 172    11416   9848   9988    608   -456     68       C  
ATOM   6991  OD1 ASN B 172     -10.572 -14.598 -49.513  1.00 79.33           O  
ANISOU 6991  OD1 ASN B 172    11072   9471   9596    629   -452     73       O  
ATOM   6992  ND2 ASN B 172     -11.405 -16.648 -49.106  1.00 81.27           N  
ANISOU 6992  ND2 ASN B 172    11302   9716   9858    599   -478     52       N  
ATOM   6993  N   LEU B 173      -9.556 -13.624 -44.489  1.00 80.64           N  
ANISOU 6993  N   LEU B 173    11075   9693   9870    572   -386    108       N  
ATOM   6994  CA  LEU B 173      -9.618 -13.427 -43.035  1.00 80.33           C  
ANISOU 6994  CA  LEU B 173    10986   9672   9861    554   -378    113       C  
ATOM   6995  C   LEU B 173      -9.874 -11.963 -42.669  1.00 81.14           C  
ANISOU 6995  C   LEU B 173    11070   9788   9971    560   -378    118       C  
ATOM   6996  O   LEU B 173      -9.070 -11.320 -41.984  1.00 77.67           O  
ANISOU 6996  O   LEU B 173    10614   9355   9542    559   -351    131       O  
ATOM   6997  CB  LEU B 173      -8.321 -13.918 -42.387  1.00 80.26           C  
ANISOU 6997  CB  LEU B 173    10971   9662   9862    547   -340    127       C  
ATOM   6998  CG  LEU B 173      -8.188 -15.357 -41.880  1.00 79.54           C  
ANISOU 6998  CG  LEU B 173    10869   9568   9783    531   -335    125       C  
ATOM   6999  CD1 LEU B 173      -8.925 -16.378 -42.735  1.00 77.37           C  
ANISOU 6999  CD1 LEU B 173    10619   9281   9495    531   -362    109       C  
ATOM   7000  CD2 LEU B 173      -6.711 -15.702 -41.776  1.00 80.75           C  
ANISOU 7000  CD2 LEU B 173    11033   9712   9933    534   -296    141       C  
ATOM   7001  N   THR B 174     -11.020 -11.463 -43.122  1.00 84.43           N  
ANISOU 7001  N   THR B 174    11488  10209  10381    566   -410    107       N  
ATOM   7002  CA  THR B 174     -11.415 -10.052 -43.000  1.00 83.15           C  
ANISOU 7002  CA  THR B 174    11314  10057  10222    574   -415    110       C  
ATOM   7003  C   THR B 174     -11.455  -9.483 -41.564  1.00 81.58           C  
ANISOU 7003  C   THR B 174    11068   9877  10052    559   -404    116       C  
ATOM   7004  O   THR B 174     -11.290  -8.274 -41.370  1.00 76.44           O  
ANISOU 7004  O   THR B 174    10409   9231   9402    567   -394    123       O  
ATOM   7005  CB  THR B 174     -12.762  -9.799 -43.732  1.00 83.99           C  
ANISOU 7005  CB  THR B 174    11429  10165  10318    582   -456     96       C  
ATOM   7006  OG1 THR B 174     -13.161  -8.434 -43.573  1.00 90.92           O  
ANISOU 7006  OG1 THR B 174    12294  11052  11198    591   -460     99       O  
ATOM   7007  CG2 THR B 174     -13.871 -10.709 -43.202  1.00 84.33           C  
ANISOU 7007  CG2 THR B 174    11445  10217  10377    563   -485     81       C  
ATOM   7008  N   ASN B 175     -11.666 -10.351 -40.574  1.00 83.62           N  
ANISOU 7008  N   ASN B 175    11294  10144  10332    538   -406    113       N  
ATOM   7009  CA  ASN B 175     -11.793  -9.925 -39.176  1.00 81.70           C  
ANISOU 7009  CA  ASN B 175    11005   9919  10116    523   -397    117       C  
ATOM   7010  C   ASN B 175     -10.525 -10.071 -38.321  1.00 79.85           C  
ANISOU 7010  C   ASN B 175    10758   9688   9894    515   -360    131       C  
ATOM   7011  O   ASN B 175     -10.527  -9.686 -37.152  1.00 82.62           O  
ANISOU 7011  O   ASN B 175    11072  10054  10266    502   -351    135       O  
ATOM   7012  CB  ASN B 175     -12.966 -10.648 -38.494  1.00 82.86           C  
ANISOU 7012  CB  ASN B 175    11121  10078  10283    505   -424    105       C  
ATOM   7013  CG  ASN B 175     -14.306  -9.985 -38.763  1.00 82.52           C  
ANISOU 7013  CG  ASN B 175    11070  10041  10240    509   -458     94       C  
ATOM   7014  OD1 ASN B 175     -14.667  -9.725 -39.910  1.00 83.19           O  
ANISOU 7014  OD1 ASN B 175    11185  10117  10304    525   -475     88       O  
ATOM   7015  ND2 ASN B 175     -15.061  -9.724 -37.698  1.00 80.24           N  
ANISOU 7015  ND2 ASN B 175    10740   9770   9976    495   -467     91       N  
ATOM   7016  N   LEU B 176      -9.452 -10.610 -38.902  1.00 77.78           N  
ANISOU 7016  N   LEU B 176    10524   9411   9616    522   -339    138       N  
ATOM   7017  CA  LEU B 176      -8.214 -10.908 -38.160  1.00 77.05           C  
ANISOU 7017  CA  LEU B 176    10419   9320   9533    514   -304    152       C  
ATOM   7018  C   LEU B 176      -7.407  -9.655 -37.772  1.00 79.92           C  
ANISOU 7018  C   LEU B 176    10775   9689   9900    520   -278    164       C  
ATOM   7019  O   LEU B 176      -7.021  -8.865 -38.639  1.00 83.04           O  
ANISOU 7019  O   LEU B 176    11198  10074  10278    537   -271    168       O  
ATOM   7020  CB  LEU B 176      -7.339 -11.888 -38.957  1.00 75.47           C  
ANISOU 7020  CB  LEU B 176    10255   9102   9317    521   -289    155       C  
ATOM   7021  CG  LEU B 176      -6.177 -12.618 -38.273  1.00 72.93           C  
ANISOU 7021  CG  LEU B 176     9924   8781   9005    512   -258    167       C  
ATOM   7022  CD1 LEU B 176      -6.673 -13.738 -37.372  1.00 71.61           C  
ANISOU 7022  CD1 LEU B 176     9728   8623   8857    493   -267    162       C  
ATOM   7023  CD2 LEU B 176      -5.221 -13.170 -39.320  1.00 72.04           C  
ANISOU 7023  CD2 LEU B 176     9853   8648   8871    526   -240    173       C  
ATOM   7024  N   VAL B 177      -7.149  -9.494 -36.469  1.00 77.22           N  
ANISOU 7024  N   VAL B 177    10394   9364   9581    505   -264    170       N  
ATOM   7025  CA  VAL B 177      -6.434  -8.321 -35.934  1.00 71.30           C  
ANISOU 7025  CA  VAL B 177     9630   8621   8837    507   -240    180       C  
ATOM   7026  C   VAL B 177      -5.174  -8.641 -35.113  1.00 70.74           C  
ANISOU 7026  C   VAL B 177     9543   8556   8777    498   -208    193       C  
ATOM   7027  O   VAL B 177      -4.263  -7.813 -35.020  1.00 70.25           O  
ANISOU 7027  O   VAL B 177     9483   8494   8714    503   -183    203       O  
ATOM   7028  CB  VAL B 177      -7.357  -7.406 -35.091  1.00 68.34           C  
ANISOU 7028  CB  VAL B 177     9222   8265   8480    499   -255    175       C  
ATOM   7029  CG1 VAL B 177      -8.366  -6.695 -35.977  1.00 67.46           C  
ANISOU 7029  CG1 VAL B 177     9127   8147   8355    512   -281    166       C  
ATOM   7030  CG2 VAL B 177      -8.056  -8.188 -33.985  1.00 66.48           C  
ANISOU 7030  CG2 VAL B 177     8949   8043   8265    479   -268    169       C  
ATOM   7031  N   HIS B 178      -5.125  -9.821 -34.501  1.00 67.61           N  
ANISOU 7031  N   HIS B 178     9131   8164   8391    484   -207    193       N  
ATOM   7032  CA  HIS B 178      -3.961 -10.187 -33.701  1.00 69.41           C  
ANISOU 7032  CA  HIS B 178     9343   8398   8629    476   -177    205       C  
ATOM   7033  C   HIS B 178      -3.409 -11.533 -34.061  1.00 65.83           C  
ANISOU 7033  C   HIS B 178     8909   7934   8170    477   -168    209       C  
ATOM   7034  O   HIS B 178      -4.130 -12.527 -34.068  1.00 67.27           O  
ANISOU 7034  O   HIS B 178     9090   8113   8354    470   -187    200       O  
ATOM   7035  CB  HIS B 178      -4.253 -10.101 -32.196  1.00 73.85           C  
ANISOU 7035  CB  HIS B 178     9859   8982   9216    458   -177    205       C  
ATOM   7036  CG  HIS B 178      -3.034 -10.357 -31.325  1.00 79.78           C  
ANISOU 7036  CG  HIS B 178    10591   9742   9977    450   -146    219       C  
ATOM   7037  ND1 HIS B 178      -2.926 -11.434 -30.521  1.00 79.51           N  
ANISOU 7037  ND1 HIS B 178    10538   9717   9956    437   -143    221       N  
ATOM   7038  CD2 HIS B 178      -1.840  -9.639 -31.181  1.00 79.04           C  
ANISOU 7038  CD2 HIS B 178    10497   9650   9882    455   -118    230       C  
ATOM   7039  CE1 HIS B 178      -1.733 -11.405 -29.887  1.00 79.31           C  
ANISOU 7039  CE1 HIS B 178    10499   9698   9936    434   -114    234       C  
ATOM   7040  NE2 HIS B 178      -1.071 -10.307 -30.293  1.00 77.26           N  
ANISOU 7040  NE2 HIS B 178    10251   9435   9668    444    -99    239       N  
ATOM   7041  N   VAL B 179      -2.115 -11.562 -34.374  1.00 63.27           N  
ANISOU 7041  N   VAL B 179     8601   7600   7836    485   -139    221       N  
ATOM   7042  CA  VAL B 179      -1.395 -12.810 -34.634  1.00 62.21           C  
ANISOU 7042  CA  VAL B 179     8483   7456   7698    485   -125    227       C  
ATOM   7043  C   VAL B 179      -0.137 -12.876 -33.759  1.00 62.71           C  
ANISOU 7043  C   VAL B 179     8526   7529   7772    479    -93    242       C  
ATOM   7044  O   VAL B 179       0.726 -11.993 -33.816  1.00 66.40           O  
ANISOU 7044  O   VAL B 179     8995   7996   8237    486    -72    251       O  
ATOM   7045  CB  VAL B 179      -1.024 -12.982 -36.129  1.00 60.56           C  
ANISOU 7045  CB  VAL B 179     8323   7223   7463    504   -122    227       C  
ATOM   7046  CG1 VAL B 179      -0.324 -14.311 -36.357  1.00 58.19           C  
ANISOU 7046  CG1 VAL B 179     8039   6912   7159    504   -107    233       C  
ATOM   7047  CG2 VAL B 179      -2.260 -12.901 -37.013  1.00 60.47           C  
ANISOU 7047  CG2 VAL B 179     8333   7203   7439    510   -156    212       C  
ATOM   7048  N   ASP B 180      -0.048 -13.929 -32.950  1.00 60.53           N  
ANISOU 7048  N   ASP B 180     8229   7261   7509    467    -89    245       N  
ATOM   7049  CA  ASP B 180       1.080 -14.135 -32.048  1.00 57.14           C  
ANISOU 7049  CA  ASP B 180     7777   6842   7091    461    -61    259       C  
ATOM   7050  C   ASP B 180       2.112 -15.089 -32.669  1.00 56.39           C  
ANISOU 7050  C   ASP B 180     7708   6730   6985    469    -39    269       C  
ATOM   7051  O   ASP B 180       1.824 -16.251 -32.968  1.00 52.65           O  
ANISOU 7051  O   ASP B 180     7248   6247   6508    468    -46    266       O  
ATOM   7052  CB  ASP B 180       0.565 -14.666 -30.703  1.00 57.37           C  
ANISOU 7052  CB  ASP B 180     7765   6890   7141    442    -68    257       C  
ATOM   7053  CG  ASP B 180       1.590 -14.558 -29.580  1.00 59.01           C  
ANISOU 7053  CG  ASP B 180     7943   7115   7363    435    -42    271       C  
ATOM   7054  OD1 ASP B 180       2.802 -14.401 -29.855  1.00 56.71           O  
ANISOU 7054  OD1 ASP B 180     7663   6819   7065    443    -16    283       O  
ATOM   7055  OD2 ASP B 180       1.172 -14.641 -28.404  1.00 60.19           O  
ANISOU 7055  OD2 ASP B 180     8056   7283   7529    420    -48    269       O  
ATOM   7056  N   LEU B 181       3.321 -14.584 -32.866  1.00 57.81           N  
ANISOU 7056  N   LEU B 181     7896   6907   7159    478    -11    282       N  
ATOM   7057  CA  LEU B 181       4.390 -15.383 -33.446  1.00 60.37           C  
ANISOU 7057  CA  LEU B 181     8245   7217   7474    487     11    293       C  
ATOM   7058  C   LEU B 181       5.534 -15.606 -32.463  1.00 60.71           C  
ANISOU 7058  C   LEU B 181     8261   7274   7531    481     39    309       C  
ATOM   7059  O   LEU B 181       6.648 -15.957 -32.862  1.00 59.77           O  
ANISOU 7059  O   LEU B 181     8158   7145   7405    490     65    321       O  
ATOM   7060  CB  LEU B 181       4.899 -14.717 -34.729  1.00 64.67           C  
ANISOU 7060  CB  LEU B 181     8829   7742   7998    506     21    296       C  
ATOM   7061  CG  LEU B 181       4.434 -15.202 -36.113  1.00 66.04           C  
ANISOU 7061  CG  LEU B 181     9048   7892   8150    519      7    288       C  
ATOM   7062  CD1 LEU B 181       3.026 -15.775 -36.130  1.00 65.20           C  
ANISOU 7062  CD1 LEU B 181     8940   7787   8045    511    -26    271       C  
ATOM   7063  CD2 LEU B 181       4.562 -14.074 -37.127  1.00 67.62           C  
ANISOU 7063  CD2 LEU B 181     9276   8080   8334    535      9    287       C  
ATOM   7064  N   SER B 182       5.246 -15.408 -31.176  1.00 64.68           N  
ANISOU 7064  N   SER B 182     8722   7799   8052    466     35    308       N  
ATOM   7065  CA  SER B 182       6.241 -15.551 -30.112  1.00 64.45           C  
ANISOU 7065  CA  SER B 182     8663   7787   8037    458     58    322       C  
ATOM   7066  C   SER B 182       6.918 -16.909 -30.115  1.00 65.06           C  
ANISOU 7066  C   SER B 182     8747   7858   8114    460     74    332       C  
ATOM   7067  O   SER B 182       6.329 -17.905 -30.542  1.00 64.19           O  
ANISOU 7067  O   SER B 182     8654   7735   7998    461     62    326       O  
ATOM   7068  CB  SER B 182       5.610 -15.324 -28.740  1.00 65.08           C  
ANISOU 7068  CB  SER B 182     8699   7892   8136    441     46    318       C  
ATOM   7069  OG  SER B 182       5.341 -13.955 -28.530  1.00 70.66           O  
ANISOU 7069  OG  SER B 182     9394   8608   8846    439     40    312       O  
ATOM   7070  N   TYR B 183       8.162 -16.929 -29.640  1.00 64.56           N  
ANISOU 7070  N   TYR B 183     8670   7802   8055    461    102    348       N  
ATOM   7071  CA  TYR B 183       8.882 -18.163 -29.364  1.00 64.63           C  
ANISOU 7071  CA  TYR B 183     8677   7811   8068    462    120    360       C  
ATOM   7072  C   TYR B 183       8.880 -19.082 -30.594  1.00 67.02           C  
ANISOU 7072  C   TYR B 183     9023   8086   8354    474    121    359       C  
ATOM   7073  O   TYR B 183       8.252 -20.147 -30.608  1.00 66.60           O  
ANISOU 7073  O   TYR B 183     8976   8027   8302    470    109    354       O  
ATOM   7074  CB  TYR B 183       8.290 -18.839 -28.116  1.00 61.32           C  
ANISOU 7074  CB  TYR B 183     8222   7409   7664    446    109    358       C  
ATOM   7075  CG  TYR B 183       9.244 -19.749 -27.391  1.00 62.65           C  
ANISOU 7075  CG  TYR B 183     8374   7587   7841    444    132    374       C  
ATOM   7076  CD1 TYR B 183      10.282 -19.234 -26.618  1.00 64.12           C  
ANISOU 7076  CD1 TYR B 183     8534   7792   8036    442    153    387       C  
ATOM   7077  CD2 TYR B 183       9.104 -21.128 -27.468  1.00 65.69           C  
ANISOU 7077  CD2 TYR B 183     8768   7963   8226    445    133    377       C  
ATOM   7078  CE1 TYR B 183      11.157 -20.073 -25.943  1.00 66.04           C  
ANISOU 7078  CE1 TYR B 183     8760   8044   8286    442    174    403       C  
ATOM   7079  CE2 TYR B 183       9.973 -21.977 -26.800  1.00 67.52           C  
ANISOU 7079  CE2 TYR B 183     8985   8203   8466    444    155    392       C  
ATOM   7080  CZ  TYR B 183      10.997 -21.448 -26.042  1.00 66.46           C  
ANISOU 7080  CZ  TYR B 183     8824   8087   8338    443    175    406       C  
ATOM   7081  OH  TYR B 183      11.854 -22.301 -25.386  1.00 66.86           O  
ANISOU 7081  OH  TYR B 183     8859   8146   8396    444    196    422       O  
ATOM   7082  N   ASN B 184       9.567 -18.634 -31.639  1.00 67.00           N  
ANISOU 7082  N   ASN B 184     9051   8067   8337    489    135    364       N  
ATOM   7083  CA  ASN B 184       9.701 -19.406 -32.867  1.00 66.36           C  
ANISOU 7083  CA  ASN B 184     9014   7960   8239    502    140    364       C  
ATOM   7084  C   ASN B 184      11.127 -19.362 -33.406  1.00 66.24           C  
ANISOU 7084  C   ASN B 184     9016   7934   8216    516    173    380       C  
ATOM   7085  O   ASN B 184      12.069 -19.142 -32.640  1.00 64.19           O  
ANISOU 7085  O   ASN B 184     8730   7689   7968    512    194    394       O  
ATOM   7086  CB  ASN B 184       8.674 -18.953 -33.908  1.00 65.81           C  
ANISOU 7086  CB  ASN B 184     8974   7874   8154    508    114    347       C  
ATOM   7087  CG  ASN B 184       7.340 -19.656 -33.746  1.00 67.05           C  
ANISOU 7087  CG  ASN B 184     9128   8032   8315    498     84    332       C  
ATOM   7088  OD1 ASN B 184       7.238 -20.862 -33.946  1.00 65.10           O  
ANISOU 7088  OD1 ASN B 184     8894   7774   8065    498     84    331       O  
ATOM   7089  ND2 ASN B 184       6.308 -18.902 -33.387  1.00 68.73           N  
ANISOU 7089  ND2 ASN B 184     9323   8256   8533    489     59    319       N  
ATOM   7090  N   TYR B 185      11.283 -19.573 -34.712  1.00 68.96           N  
ANISOU 7090  N   TYR B 185     9405   8254   8542    531    177    379       N  
ATOM   7091  CA  TYR B 185      12.608 -19.678 -35.326  1.00 70.02           C  
ANISOU 7091  CA  TYR B 185     9560   8375   8668    545    209    395       C  
ATOM   7092  C   TYR B 185      12.839 -18.677 -36.462  1.00 69.22           C  
ANISOU 7092  C   TYR B 185     9491   8257   8550    560    214    393       C  
ATOM   7093  O   TYR B 185      13.777 -18.826 -37.249  1.00 72.13           O  
ANISOU 7093  O   TYR B 185     9887   8610   8908    574    239    404       O  
ATOM   7094  CB  TYR B 185      12.869 -21.121 -35.783  1.00 73.87           C  
ANISOU 7094  CB  TYR B 185    10072   8846   9149    551    219    400       C  
ATOM   7095  CG  TYR B 185      12.973 -22.098 -34.630  1.00 79.45           C  
ANISOU 7095  CG  TYR B 185    10746   9567   9872    539    224    406       C  
ATOM   7096  CD1 TYR B 185      11.887 -22.905 -34.272  1.00 80.06           C  
ANISOU 7096  CD1 TYR B 185    10816   9646   9954    528    200    394       C  
ATOM   7097  CD2 TYR B 185      14.149 -22.201 -33.877  1.00 80.76           C  
ANISOU 7097  CD2 TYR B 185    10886   9747  10050    539    251    425       C  
ATOM   7098  CE1 TYR B 185      11.971 -23.794 -33.206  1.00 81.35           C  
ANISOU 7098  CE1 TYR B 185    10950   9824  10133    518    205    401       C  
ATOM   7099  CE2 TYR B 185      14.242 -23.086 -32.810  1.00 85.29           C  
ANISOU 7099  CE2 TYR B 185    11431  10336  10639    529    256    432       C  
ATOM   7100  CZ  TYR B 185      13.153 -23.881 -32.478  1.00 84.53           C  
ANISOU 7100  CZ  TYR B 185    11330  10240  10547    519    233    420       C  
ATOM   7101  OH  TYR B 185      13.245 -24.763 -31.422  1.00 79.58           O  
ANISOU 7101  OH  TYR B 185    10673   9627   9934    510    238    428       O  
ATOM   7102  N   ILE B 186      11.991 -17.653 -36.525  1.00 66.73           N  
ANISOU 7102  N   ILE B 186     9172   7947   8233    556    192    381       N  
ATOM   7103  CA  ILE B 186      12.095 -16.609 -37.539  1.00 64.42           C  
ANISOU 7103  CA  ILE B 186     8908   7641   7926    570    195    379       C  
ATOM   7104  C   ILE B 186      13.377 -15.804 -37.354  1.00 67.11           C  
ANISOU 7104  C   ILE B 186     9238   7987   8273    574    226    394       C  
ATOM   7105  O   ILE B 186      13.588 -15.187 -36.302  1.00 66.02           O  
ANISOU 7105  O   ILE B 186     9061   7870   8152    562    230    397       O  
ATOM   7106  CB  ILE B 186      10.878 -15.669 -37.499  1.00 61.89           C  
ANISOU 7106  CB  ILE B 186     8582   7328   7606    565    165    363       C  
ATOM   7107  CG1 ILE B 186       9.585 -16.480 -37.655  1.00 61.03           C  
ANISOU 7107  CG1 ILE B 186     8481   7215   7492    559    133    347       C  
ATOM   7108  CG2 ILE B 186      11.010 -14.590 -38.569  1.00 62.63           C  
ANISOU 7108  CG2 ILE B 186     8706   7406   7683    580    169    362       C  
ATOM   7109  CD1 ILE B 186       8.355 -15.856 -37.027  1.00 59.01           C  
ANISOU 7109  CD1 ILE B 186     8199   6975   7245    547    102    333       C  
ATOM   7110  N   GLN B 187      14.231 -15.829 -38.377  1.00 68.85           N  
ANISOU 7110  N   GLN B 187     9493   8187   8479    591    249    404       N  
ATOM   7111  CA  GLN B 187      15.518 -15.132 -38.324  1.00 73.39           C  
ANISOU 7111  CA  GLN B 187    10061   8763   9060    597    282    419       C  
ATOM   7112  C   GLN B 187      15.536 -13.895 -39.209  1.00 72.59           C  
ANISOU 7112  C   GLN B 187     9984   8650   8947    608    285    416       C  
ATOM   7113  O   GLN B 187      16.278 -12.945 -38.945  1.00 73.11           O  
ANISOU 7113  O   GLN B 187    10034   8722   9021    608    304    424       O  
ATOM   7114  CB  GLN B 187      16.672 -16.069 -38.701  1.00 76.83           C  
ANISOU 7114  CB  GLN B 187    10512   9186   9491    607    312    435       C  
ATOM   7115  CG  GLN B 187      17.060 -17.058 -37.608  1.00 80.74           C  
ANISOU 7115  CG  GLN B 187    10975   9698  10003    595    319    444       C  
ATOM   7116  CD  GLN B 187      18.327 -17.835 -37.921  1.00 81.47           C  
ANISOU 7116  CD  GLN B 187    11080   9780  10094    606    352    462       C  
ATOM   7117  OE1 GLN B 187      19.250 -17.323 -38.558  1.00 83.24           O  
ANISOU 7117  OE1 GLN B 187    11321   9993  10313    619    377    472       O  
ATOM   7118  NE2 GLN B 187      18.381 -19.079 -37.460  1.00 78.70           N  
ANISOU 7118  NE2 GLN B 187    10721   9432   9749    602    354    466       N  
ATOM   7119  N   THR B 188      14.724 -13.915 -40.261  1.00 72.28           N  
ANISOU 7119  N   THR B 188     9982   8592   8887    619    266    405       N  
ATOM   7120  CA  THR B 188      14.654 -12.796 -41.191  1.00 74.15           C  
ANISOU 7120  CA  THR B 188    10246   8816   9111    632    268    403       C  
ATOM   7121  C   THR B 188      13.232 -12.274 -41.347  1.00 73.99           C  
ANISOU 7121  C   THR B 188    10230   8798   9084    629    232    385       C  
ATOM   7122  O   THR B 188      12.270 -13.054 -41.394  1.00 72.50           O  
ANISOU 7122  O   THR B 188    10046   8608   8890    625    205    373       O  
ATOM   7123  CB  THR B 188      15.204 -13.149 -42.601  1.00 76.52           C  
ANISOU 7123  CB  THR B 188    10598   9087   9388    654    285    409       C  
ATOM   7124  OG1 THR B 188      14.260 -13.967 -43.307  1.00 75.04           O  
ANISOU 7124  OG1 THR B 188    10441   8887   9183    659    260    397       O  
ATOM   7125  CG2 THR B 188      16.561 -13.866 -42.524  1.00 76.56           C  
ANISOU 7125  CG2 THR B 188    10602   9087   9398    658    320    427       C  
ATOM   7126  N   ILE B 189      13.114 -10.950 -41.416  1.00 73.36           N  
ANISOU 7126  N   ILE B 189    10146   8721   9005    632    231    383       N  
ATOM   7127  CA  ILE B 189      11.906 -10.305 -41.915  1.00 73.42           C  
ANISOU 7127  CA  ILE B 189    10168   8725   9001    636    202    368       C  
ATOM   7128  C   ILE B 189      12.275  -9.684 -43.257  1.00 75.06           C  
ANISOU 7128  C   ILE B 189    10421   8909   9187    658    215    372       C  
ATOM   7129  O   ILE B 189      13.061  -8.732 -43.318  1.00 72.74           O  
ANISOU 7129  O   ILE B 189    10125   8613   8897    663    240    381       O  
ATOM   7130  CB  ILE B 189      11.362  -9.230 -40.950  1.00 72.41           C  
ANISOU 7130  CB  ILE B 189    10002   8618   8890    622    189    362       C  
ATOM   7131  CG1 ILE B 189      10.994  -9.852 -39.604  1.00 71.36           C  
ANISOU 7131  CG1 ILE B 189     9826   8508   8778    601    177    358       C  
ATOM   7132  CG2 ILE B 189      10.135  -8.551 -41.541  1.00 72.97           C  
ANISOU 7132  CG2 ILE B 189    10091   8685   8949    628    160    347       C  
ATOM   7133  CD1 ILE B 189      10.890  -8.852 -38.475  1.00 70.88           C  
ANISOU 7133  CD1 ILE B 189     9723   8470   8737    586    175    356       C  
ATOM   7134  N   THR B 190      11.723 -10.245 -44.331  1.00 77.88           N  
ANISOU 7134  N   THR B 190    10818   9248   9522    671    201    365       N  
ATOM   7135  CA  THR B 190      12.062  -9.813 -45.690  1.00 79.52           C  
ANISOU 7135  CA  THR B 190    11073   9432   9706    693    213    369       C  
ATOM   7136  C   THR B 190      10.928  -9.027 -46.336  1.00 79.98           C  
ANISOU 7136  C   THR B 190    11151   9486   9750    702    185    356       C  
ATOM   7137  O   THR B 190       9.777  -9.100 -45.891  1.00 78.22           O  
ANISOU 7137  O   THR B 190    10911   9277   9532    691    153    342       O  
ATOM   7138  CB  THR B 190      12.439 -11.005 -46.602  1.00 78.86           C  
ANISOU 7138  CB  THR B 190    11029   9329   9605    706    222    372       C  
ATOM   7139  OG1 THR B 190      11.261 -11.750 -46.945  1.00 79.82           O  
ANISOU 7139  OG1 THR B 190    11165   9447   9714    704    187    356       O  
ATOM   7140  CG2 THR B 190      13.457 -11.921 -45.921  1.00 77.62           C  
ANISOU 7140  CG2 THR B 190    10851   9176   9462    697    246    385       C  
ATOM   7141  N   VAL B 191      11.263  -8.289 -47.395  1.00 81.49           N  
ANISOU 7141  N   VAL B 191    11377   9659   9923    722    199    361       N  
ATOM   7142  CA  VAL B 191      10.280  -7.530 -48.174  1.00 82.95           C  
ANISOU 7142  CA  VAL B 191    11586   9838  10090    734    175    351       C  
ATOM   7143  C   VAL B 191       9.092  -8.391 -48.599  1.00 81.99           C  
ANISOU 7143  C   VAL B 191    11482   9714   9954    734    138    335       C  
ATOM   7144  O   VAL B 191       7.952  -7.921 -48.637  1.00 83.07           O  
ANISOU 7144  O   VAL B 191    11615   9857  10087    733    107    322       O  
ATOM   7145  CB  VAL B 191      10.911  -6.881 -49.432  1.00 85.61           C  
ANISOU 7145  CB  VAL B 191    11969  10152  10406    758    198    360       C  
ATOM   7146  CG1 VAL B 191      11.983  -5.869 -49.044  1.00 84.54           C  
ANISOU 7146  CG1 VAL B 191    11816  10018  10285    758    233    374       C  
ATOM   7147  CG2 VAL B 191      11.475  -7.935 -50.381  1.00 87.74           C  
ANISOU 7147  CG2 VAL B 191    12279  10401  10656    772    211    365       C  
ATOM   7148  N   ASN B 192       9.379  -9.655 -48.899  1.00 84.26           N  
ANISOU 7148  N   ASN B 192    11787   9993  10234    735    141    336       N  
ATOM   7149  CA  ASN B 192       8.403 -10.591 -49.434  1.00 86.31           C  
ANISOU 7149  CA  ASN B 192    12068  10246  10478    736    110    321       C  
ATOM   7150  C   ASN B 192       7.417 -11.096 -48.384  1.00 87.59           C  
ANISOU 7150  C   ASN B 192    12191  10429  10659    714     80    308       C  
ATOM   7151  O   ASN B 192       6.268 -11.411 -48.706  1.00 86.98           O  
ANISOU 7151  O   ASN B 192    12123  10352  10572    713     46    293       O  
ATOM   7152  CB  ASN B 192       9.128 -11.766 -50.088  1.00 87.95           C  
ANISOU 7152  CB  ASN B 192    12307  10435  10672    744    128    327       C  
ATOM   7153  CG  ASN B 192       8.294 -12.446 -51.152  1.00 89.74           C  
ANISOU 7153  CG  ASN B 192    12574  10647  10872    755    101    313       C  
ATOM   7154  OD1 ASN B 192       7.323 -13.142 -50.852  1.00 89.83           O  
ANISOU 7154  OD1 ASN B 192    12575  10667  10888    742     71    299       O  
ATOM   7155  ND2 ASN B 192       8.677 -12.254 -52.407  1.00 90.71           N  
ANISOU 7155  ND2 ASN B 192    12745  10749  10970    777    113    317       N  
ATOM   7156  N   ASP B 193       7.873 -11.173 -47.134  1.00 88.43           N  
ANISOU 7156  N   ASP B 193    12254  10553  10792    696     93    315       N  
ATOM   7157  CA  ASP B 193       7.034 -11.608 -46.017  1.00 85.98           C  
ANISOU 7157  CA  ASP B 193    11903  10264  10502    674     69    305       C  
ATOM   7158  C   ASP B 193       5.823 -10.702 -45.832  1.00 83.80           C  
ANISOU 7158  C   ASP B 193    11612   9999  10227    671     38    293       C  
ATOM   7159  O   ASP B 193       4.693 -11.178 -45.711  1.00 84.34           O  
ANISOU 7159  O   ASP B 193    11674  10073  10296    663      6    278       O  
ATOM   7160  CB  ASP B 193       7.842 -11.645 -44.715  1.00 86.62           C  
ANISOU 7160  CB  ASP B 193    11939  10361  10609    658     92    316       C  
ATOM   7161  CG  ASP B 193       8.921 -12.708 -44.720  1.00 85.64           C  
ANISOU 7161  CG  ASP B 193    11823  10229  10487    659    119    328       C  
ATOM   7162  OD1 ASP B 193       8.689 -13.802 -45.278  1.00 86.18           O  
ANISOU 7162  OD1 ASP B 193    11916  10285  10542    663    110    323       O  
ATOM   7163  OD2 ASP B 193      10.003 -12.451 -44.150  1.00 87.77           O  
ANISOU 7163  OD2 ASP B 193    12073  10505  10770    656    148    342       O  
ATOM   7164  N   LEU B 194       6.072  -9.395 -45.832  1.00 82.67           N  
ANISOU 7164  N   LEU B 194    11464   9858  10086    677     49    298       N  
ATOM   7165  CA  LEU B 194       5.046  -8.398 -45.530  1.00 84.65           C  
ANISOU 7165  CA  LEU B 194    11698  10122  10343    674     25    289       C  
ATOM   7166  C   LEU B 194       4.315  -7.893 -46.779  1.00 85.51           C  
ANISOU 7166  C   LEU B 194    11846  10217  10426    693      6    281       C  
ATOM   7167  O   LEU B 194       3.652  -6.849 -46.745  1.00 84.81           O  
ANISOU 7167  O   LEU B 194    11750  10135  10338    696     -7    276       O  
ATOM   7168  CB  LEU B 194       5.666  -7.225 -44.754  1.00 85.74           C  
ANISOU 7168  CB  LEU B 194    11806  10271  10499    668     47    298       C  
ATOM   7169  CG  LEU B 194       6.622  -7.529 -43.589  1.00 86.19           C  
ANISOU 7169  CG  LEU B 194    11826  10341  10579    652     72    309       C  
ATOM   7170  CD1 LEU B 194       7.228  -6.243 -43.043  1.00 82.54           C  
ANISOU 7170  CD1 LEU B 194    11343   9888  10131    649     94    317       C  
ATOM   7171  CD2 LEU B 194       5.942  -8.318 -42.476  1.00 83.30           C  
ANISOU 7171  CD2 LEU B 194    11423   9994  10232    631     52    300       C  
ATOM   7172  N   GLN B 195       4.431  -8.645 -47.872  1.00 85.62           N  
ANISOU 7172  N   GLN B 195    11902  10212  10417    707      4    280       N  
ATOM   7173  CA  GLN B 195       3.797  -8.288 -49.137  1.00 85.71           C  
ANISOU 7173  CA  GLN B 195    11954  10209  10400    727    -13    273       C  
ATOM   7174  C   GLN B 195       2.279  -8.146 -49.004  1.00 83.82           C  
ANISOU 7174  C   GLN B 195    11703   9982  10162    721    -55    256       C  
ATOM   7175  O   GLN B 195       1.689  -7.238 -49.596  1.00 84.58           O  
ANISOU 7175  O   GLN B 195    11815  10076  10246    734    -69    252       O  
ATOM   7176  CB  GLN B 195       4.152  -9.308 -50.228  1.00 91.00           C  
ANISOU 7176  CB  GLN B 195    12670  10858  11046    740     -8    272       C  
ATOM   7177  CG  GLN B 195       3.935  -8.822 -51.660  1.00 91.90           C  
ANISOU 7177  CG  GLN B 195    12834  10954  11129    765    -14    270       C  
ATOM   7178  CD  GLN B 195       4.843  -7.663 -52.044  1.00 91.68           C  
ANISOU 7178  CD  GLN B 195    12820  10917  11096    781     17    286       C  
ATOM   7179  OE1 GLN B 195       6.063  -7.727 -51.875  1.00 89.15           O  
ANISOU 7179  OE1 GLN B 195    12498  10590  10782    782     53    300       O  
ATOM   7180  NE2 GLN B 195       4.250  -6.597 -52.569  1.00 90.33           N  
ANISOU 7180  NE2 GLN B 195    12662  10745  10914    795      4    283       N  
ATOM   7181  N   PHE B 196       1.661  -9.034 -48.222  1.00 80.30           N  
ANISOU 7181  N   PHE B 196    11229   9549   9731    701    -75    246       N  
ATOM   7182  CA  PHE B 196       0.213  -9.008 -48.013  1.00 77.65           C  
ANISOU 7182  CA  PHE B 196    10878   9226   9399    694   -116    230       C  
ATOM   7183  C   PHE B 196      -0.238  -7.661 -47.474  1.00 77.06           C  
ANISOU 7183  C   PHE B 196    10776   9164   9336    692   -121    230       C  
ATOM   7184  O   PHE B 196      -1.160  -7.050 -48.019  1.00 76.99           O  
ANISOU 7184  O   PHE B 196    10780   9156   9316    702   -146    222       O  
ATOM   7185  CB  PHE B 196      -0.246 -10.124 -47.065  1.00 75.25           C  
ANISOU 7185  CB  PHE B 196    10541   8933   9114    671   -131    222       C  
ATOM   7186  CG  PHE B 196      -1.664  -9.961 -46.584  1.00 73.75           C  
ANISOU 7186  CG  PHE B 196    10325   8760   8935    660   -168    207       C  
ATOM   7187  CD1 PHE B 196      -2.738 -10.289 -47.405  1.00 74.03           C  
ANISOU 7187  CD1 PHE B 196    10383   8790   8953    666   -202    192       C  
ATOM   7188  CD2 PHE B 196      -1.930  -9.466 -45.312  1.00 73.69           C  
ANISOU 7188  CD2 PHE B 196    10271   8773   8954    643   -169    208       C  
ATOM   7189  CE1 PHE B 196      -4.048 -10.131 -46.964  1.00 74.47           C  
ANISOU 7189  CE1 PHE B 196    10414   8861   9020    656   -237    179       C  
ATOM   7190  CE2 PHE B 196      -3.236  -9.308 -44.867  1.00 74.15           C  
ANISOU 7190  CE2 PHE B 196    10304   8845   9022    633   -203    195       C  
ATOM   7191  CZ  PHE B 196      -4.298  -9.639 -45.694  1.00 72.01           C  
ANISOU 7191  CZ  PHE B 196    10055   8569   8736    640   -236    181       C  
ATOM   7192  N   LEU B 197       0.417  -7.216 -46.402  1.00 72.65           N  
ANISOU 7192  N   LEU B 197    10183   8618   8801    680    -98    240       N  
ATOM   7193  CA  LEU B 197       0.117  -5.934 -45.777  1.00 73.02           C  
ANISOU 7193  CA  LEU B 197    10203   8678   8861    677    -99    241       C  
ATOM   7194  C   LEU B 197       0.272  -4.762 -46.738  1.00 76.18           C  
ANISOU 7194  C   LEU B 197    10635   9066   9244    699    -90    247       C  
ATOM   7195  O   LEU B 197      -0.521  -3.825 -46.707  1.00 78.83           O  
ANISOU 7195  O   LEU B 197    10962   9408   9580    703   -107    242       O  
ATOM   7196  CB  LEU B 197       0.994  -5.721 -44.542  1.00 69.95           C  
ANISOU 7196  CB  LEU B 197     9777   8303   8499    661    -71    252       C  
ATOM   7197  CG  LEU B 197       0.357  -5.634 -43.148  1.00 68.13           C  
ANISOU 7197  CG  LEU B 197     9495   8095   8295    639    -84    246       C  
ATOM   7198  CD1 LEU B 197      -0.900  -6.487 -42.979  1.00 65.98           C  
ANISOU 7198  CD1 LEU B 197     9212   7830   8025    629   -121    231       C  
ATOM   7199  CD2 LEU B 197       1.400  -5.986 -42.096  1.00 67.11           C  
ANISOU 7199  CD2 LEU B 197     9336   7975   8186    623    -56    256       C  
ATOM   7200  N   ARG B 198       1.285  -4.830 -47.595  1.00 80.44           N  
ANISOU 7200  N   ARG B 198    11209   9586   9766    715    -64    257       N  
ATOM   7201  CA  ARG B 198       1.595  -3.744 -48.522  1.00 83.32           C  
ANISOU 7201  CA  ARG B 198    11605   9937  10113    737    -50    264       C  
ATOM   7202  C   ARG B 198       0.488  -3.499 -49.548  1.00 86.81           C  
ANISOU 7202  C   ARG B 198    12078  10373  10532    754    -82    254       C  
ATOM   7203  O   ARG B 198       0.235  -2.354 -49.922  1.00 92.32           O  
ANISOU 7203  O   ARG B 198    12785  11069  11223    767    -83    256       O  
ATOM   7204  CB  ARG B 198       2.920  -4.016 -49.226  1.00 83.24           C  
ANISOU 7204  CB  ARG B 198    11628   9908  10090    750    -15    277       C  
ATOM   7205  CG  ARG B 198       3.606  -2.770 -49.749  1.00 81.77           C  
ANISOU 7205  CG  ARG B 198    11460   9710   9896    767     11    289       C  
ATOM   7206  CD  ARG B 198       4.994  -3.101 -50.264  1.00 83.34           C  
ANISOU 7206  CD  ARG B 198    11683   9892  10087    776     48    303       C  
ATOM   7207  NE  ARG B 198       5.976  -3.194 -49.183  1.00 85.66           N  
ANISOU 7207  NE  ARG B 198    11942  10196  10408    759     76    313       N  
ATOM   7208  CZ  ARG B 198       6.413  -4.327 -48.637  1.00 82.88           C  
ANISOU 7208  CZ  ARG B 198    11574   9848  10065    745     82    314       C  
ATOM   7209  NH1 ARG B 198       5.967  -5.508 -49.052  1.00 82.92           N  
ANISOU 7209  NH1 ARG B 198    11598   9849  10059    745     62    306       N  
ATOM   7210  NH2 ARG B 198       7.312  -4.276 -47.668  1.00 82.51           N  
ANISOU 7210  NH2 ARG B 198    11496   9811  10042    731    107    323       N  
ATOM   7211  N   GLU B 199      -0.162  -4.573 -49.998  1.00 88.18           N  
ANISOU 7211  N   GLU B 199    12266  10545  10693    753   -109    242       N  
ATOM   7212  CA  GLU B 199      -1.305  -4.464 -50.910  1.00 87.88           C  
ANISOU 7212  CA  GLU B 199    12253  10503  10633    767   -144    230       C  
ATOM   7213  C   GLU B 199      -2.619  -4.218 -50.170  1.00 88.54           C  
ANISOU 7213  C   GLU B 199    12301  10607  10733    754   -178    218       C  
ATOM   7214  O   GLU B 199      -3.670  -4.079 -50.794  1.00 90.95           O  
ANISOU 7214  O   GLU B 199    12620  10912  11023    763   -210    208       O  
ATOM   7215  CB  GLU B 199      -1.433  -5.715 -51.782  1.00 85.50           C  
ANISOU 7215  CB  GLU B 199    11985  10188  10310    772   -158    223       C  
ATOM   7216  CG  GLU B 199      -0.451  -5.772 -52.938  1.00 89.67           C  
ANISOU 7216  CG  GLU B 199    12563  10694  10813    794   -132    233       C  
ATOM   7217  CD  GLU B 199       0.880  -6.377 -52.540  1.00 91.21           C  
ANISOU 7217  CD  GLU B 199    12753  10882  11018    786    -95    245       C  
ATOM   7218  OE1 GLU B 199       0.981  -7.620 -52.497  1.00 87.83           O  
ANISOU 7218  OE1 GLU B 199    12329  10451  10590    777    -98    240       O  
ATOM   7219  OE2 GLU B 199       1.828  -5.610 -52.278  1.00 94.37           O  
ANISOU 7219  OE2 GLU B 199    13147  11280  11427    789    -61    259       O  
ATOM   7220  N   ASN B 200      -2.558  -4.171 -48.841  1.00 90.30           N  
ANISOU 7220  N   ASN B 200    12478  10847  10986    732   -172    219       N  
ATOM   7221  CA  ASN B 200      -3.751  -4.001 -48.010  1.00 90.69           C  
ANISOU 7221  CA  ASN B 200    12489  10915  11053    717   -202    208       C  
ATOM   7222  C   ASN B 200      -3.541  -3.047 -46.821  1.00 94.35           C  
ANISOU 7222  C   ASN B 200    12911  11394  11543    705   -186    215       C  
ATOM   7223  O   ASN B 200      -3.577  -3.477 -45.663  1.00100.08           O  
ANISOU 7223  O   ASN B 200    13598  12134  12293    683   -185    213       O  
ATOM   7224  CB  ASN B 200      -4.253  -5.366 -47.519  1.00 85.30           C  
ANISOU 7224  CB  ASN B 200    11788  10240  10380    698   -222    197       C  
ATOM   7225  CG  ASN B 200      -4.622  -6.296 -48.655  1.00 82.37           C  
ANISOU 7225  CG  ASN B 200    11457   9855   9984    709   -243    188       C  
ATOM   7226  OD1 ASN B 200      -5.688  -6.172 -49.252  1.00 80.90           O  
ANISOU 7226  OD1 ASN B 200    11282   9670   9785    716   -275    177       O  
ATOM   7227  ND2 ASN B 200      -3.739  -7.238 -48.958  1.00 82.24           N  
ANISOU 7227  ND2 ASN B 200    11460   9826   9960    709   -224    192       N  
ATOM   7228  N   PRO B 201      -3.337  -1.743 -47.099  1.00 93.37           N  
ANISOU 7228  N   PRO B 201    12795  11265  11413    719   -172    222       N  
ATOM   7229  CA  PRO B 201      -3.044  -0.771 -46.038  1.00 93.65           C  
ANISOU 7229  CA  PRO B 201    12795  11314  11473    708   -154    229       C  
ATOM   7230  C   PRO B 201      -4.231  -0.485 -45.117  1.00 90.11           C  
ANISOU 7230  C   PRO B 201    12308  10885  11044    694   -181    218       C  
ATOM   7231  O   PRO B 201      -4.078   0.223 -44.121  1.00 88.90           O  
ANISOU 7231  O   PRO B 201    12121  10743  10911    682   -168    222       O  
ATOM   7232  CB  PRO B 201      -2.672   0.504 -46.816  1.00 94.88           C  
ANISOU 7232  CB  PRO B 201    12977  11456  11614    730   -136    238       C  
ATOM   7233  CG  PRO B 201      -2.424   0.061 -48.220  1.00 94.43           C  
ANISOU 7233  CG  PRO B 201    12971  11379  11527    751   -137    239       C  
ATOM   7234  CD  PRO B 201      -3.345  -1.101 -48.423  1.00 93.91           C  
ANISOU 7234  CD  PRO B 201    12909  11318  11455    746   -172    225       C  
ATOM   7235  N   GLN B 202      -5.395  -1.038 -45.447  1.00 90.03           N  
ANISOU 7235  N   GLN B 202    12301  10879  11027    694   -218    206       N  
ATOM   7236  CA  GLN B 202      -6.618  -0.800 -44.681  1.00 92.83           C  
ANISOU 7236  CA  GLN B 202    12620  11251  11398    683   -246    196       C  
ATOM   7237  C   GLN B 202      -6.776  -1.738 -43.479  1.00 92.48           C  
ANISOU 7237  C   GLN B 202    12537  11223  11379    656   -251    190       C  
ATOM   7238  O   GLN B 202      -7.664  -1.536 -42.645  1.00 92.11           O  
ANISOU 7238  O   GLN B 202    12456  11192  11350    644   -270    183       O  
ATOM   7239  CB  GLN B 202      -7.851  -0.881 -45.599  1.00 92.13           C  
ANISOU 7239  CB  GLN B 202    12553  11161  11292    696   -284    184       C  
ATOM   7240  CG  GLN B 202      -8.361  -2.290 -45.900  1.00 93.15           C  
ANISOU 7240  CG  GLN B 202    12688  11288  11414    689   -310    173       C  
ATOM   7241  CD  GLN B 202      -7.472  -3.077 -46.852  1.00 91.65           C  
ANISOU 7241  CD  GLN B 202    12540  11080  11203    699   -295    177       C  
ATOM   7242  OE1 GLN B 202      -6.548  -2.535 -47.459  1.00 92.44           O  
ANISOU 7242  OE1 GLN B 202    12667  11167  11289    715   -269    188       O  
ATOM   7243  NE2 GLN B 202      -7.758  -4.366 -46.990  1.00 85.61           N  
ANISOU 7243  NE2 GLN B 202    11779  10313  10434    690   -312    167       N  
ATOM   7244  N   VAL B 203      -5.910  -2.749 -43.395  1.00 92.57           N  
ANISOU 7244  N   VAL B 203    12553  11227  11389    649   -235    194       N  
ATOM   7245  CA  VAL B 203      -6.019  -3.813 -42.382  1.00 88.90           C  
ANISOU 7245  CA  VAL B 203    12056  10775  10945    626   -240    190       C  
ATOM   7246  C   VAL B 203      -5.379  -3.448 -41.032  1.00 85.40           C  
ANISOU 7246  C   VAL B 203    11574  10346  10528    609   -215    197       C  
ATOM   7247  O   VAL B 203      -4.166  -3.235 -40.945  1.00 85.64           O  
ANISOU 7247  O   VAL B 203    11609  10370  10558    611   -183    209       O  
ATOM   7248  CB  VAL B 203      -5.440  -5.153 -42.906  1.00 85.65           C  
ANISOU 7248  CB  VAL B 203    11668  10351  10521    626   -234    190       C  
ATOM   7249  CG1 VAL B 203      -5.544  -6.244 -41.848  1.00 84.76           C  
ANISOU 7249  CG1 VAL B 203    11524  10251  10431    603   -238    186       C  
ATOM   7250  CG2 VAL B 203      -6.157  -5.585 -44.178  1.00 81.75           C  
ANISOU 7250  CG2 VAL B 203    11213   9845  10003    641   -262    180       C  
ATOM   7251  N   ASN B 204      -6.209  -3.373 -39.991  1.00 79.60           N  
ANISOU 7251  N   ASN B 204    10799   9629   9813    593   -231    191       N  
ATOM   7252  CA  ASN B 204      -5.740  -3.175 -38.619  1.00 77.81           C  
ANISOU 7252  CA  ASN B 204    10532   9418   9611    575   -213    196       C  
ATOM   7253  C   ASN B 204      -5.194  -4.501 -38.091  1.00 76.01           C  
ANISOU 7253  C   ASN B 204    10295   9193   9392    560   -204    198       C  
ATOM   7254  O   ASN B 204      -5.967  -5.403 -37.762  1.00 77.05           O  
ANISOU 7254  O   ASN B 204    10412   9331   9531    549   -226    189       O  
ATOM   7255  CB  ASN B 204      -6.884  -2.669 -37.720  1.00 76.43           C  
ANISOU 7255  CB  ASN B 204    10322   9261   9456    563   -234    188       C  
ATOM   7256  CG  ASN B 204      -6.404  -2.179 -36.355  1.00 78.97           C  
ANISOU 7256  CG  ASN B 204    10605   9599   9801    547   -213    193       C  
ATOM   7257  OD1 ASN B 204      -5.294  -1.660 -36.220  1.00 80.46           O  
ANISOU 7257  OD1 ASN B 204    10795   9784   9990    549   -183    204       O  
ATOM   7258  ND2 ASN B 204      -7.254  -2.326 -35.337  1.00 74.44           N  
ANISOU 7258  ND2 ASN B 204     9994   9042   9246    531   -230    186       N  
ATOM   7259  N   LEU B 205      -3.869  -4.624 -38.029  1.00 71.65           N  
ANISOU 7259  N   LEU B 205     9748   8635   8838    561   -172    210       N  
ATOM   7260  CA  LEU B 205      -3.248  -5.882 -37.612  1.00 70.96           C  
ANISOU 7260  CA  LEU B 205     9655   8549   8758    550   -161    213       C  
ATOM   7261  C   LEU B 205      -2.119  -5.700 -36.605  1.00 69.31           C  
ANISOU 7261  C   LEU B 205     9420   8349   8565    539   -129    225       C  
ATOM   7262  O   LEU B 205      -1.268  -4.824 -36.765  1.00 67.35           O  
ANISOU 7262  O   LEU B 205     9179   8097   8314    546   -105    234       O  
ATOM   7263  CB  LEU B 205      -2.756  -6.683 -38.827  1.00 71.11           C  
ANISOU 7263  CB  LEU B 205     9717   8547   8754    563   -157    215       C  
ATOM   7264  CG  LEU B 205      -2.376  -8.156 -38.610  1.00 69.92           C  
ANISOU 7264  CG  LEU B 205     9565   8394   8607    554   -152    216       C  
ATOM   7265  CD1 LEU B 205      -3.596  -9.012 -38.306  1.00 70.02           C  
ANISOU 7265  CD1 LEU B 205     9562   8413   8626    542   -184    203       C  
ATOM   7266  CD2 LEU B 205      -1.639  -8.715 -39.816  1.00 71.25           C  
ANISOU 7266  CD2 LEU B 205     9778   8541   8752    570   -140    221       C  
ATOM   7267  N   SER B 206      -2.129  -6.545 -35.574  1.00 67.12           N  
ANISOU 7267  N   SER B 206     9112   8085   8304    521   -130    224       N  
ATOM   7268  CA  SER B 206      -1.086  -6.567 -34.559  1.00 65.21           C  
ANISOU 7268  CA  SER B 206     8844   7855   8078    510   -102    235       C  
ATOM   7269  C   SER B 206      -0.242  -7.833 -34.627  1.00 64.28           C  
ANISOU 7269  C   SER B 206     8735   7730   7957    508    -87    242       C  
ATOM   7270  O   SER B 206      -0.749  -8.927 -34.887  1.00 62.74           O  
ANISOU 7270  O   SER B 206     8549   7530   7758    506   -103    236       O  
ATOM   7271  CB  SER B 206      -1.689  -6.411 -33.171  1.00 67.29           C  
ANISOU 7271  CB  SER B 206     9061   8139   8363    491   -111    230       C  
ATOM   7272  OG  SER B 206      -2.056  -5.064 -32.947  1.00 72.00           O  
ANISOU 7272  OG  SER B 206     9648   8743   8965    493   -114    228       O  
ATOM   7273  N   LEU B 207       1.051  -7.665 -34.383  1.00 62.74           N  
ANISOU 7273  N   LEU B 207     8537   7536   7765    508    -55    255       N  
ATOM   7274  CA  LEU B 207       2.021  -8.738 -34.508  1.00 61.15           C  
ANISOU 7274  CA  LEU B 207     8346   7327   7560    509    -36    264       C  
ATOM   7275  C   LEU B 207       2.887  -8.851 -33.265  1.00 59.73           C  
ANISOU 7275  C   LEU B 207     8131   7164   7399    495    -14    274       C  
ATOM   7276  O   LEU B 207       3.720  -7.978 -32.996  1.00 60.03           O  
ANISOU 7276  O   LEU B 207     8160   7206   7441    496      7    282       O  
ATOM   7277  CB  LEU B 207       2.915  -8.493 -35.730  1.00 62.28           C  
ANISOU 7277  CB  LEU B 207     8529   7448   7683    528    -17    272       C  
ATOM   7278  CG  LEU B 207       2.719  -9.231 -37.061  1.00 63.51           C  
ANISOU 7278  CG  LEU B 207     8730   7583   7817    543    -26    269       C  
ATOM   7279  CD1 LEU B 207       1.264  -9.535 -37.386  1.00 65.98           C  
ANISOU 7279  CD1 LEU B 207     9049   7895   8125    542    -63    253       C  
ATOM   7280  CD2 LEU B 207       3.353  -8.422 -38.184  1.00 62.19           C  
ANISOU 7280  CD2 LEU B 207     8598   7398   7631    562    -10    275       C  
ATOM   7281  N   ASP B 208       2.685  -9.924 -32.506  1.00 57.85           N  
ANISOU 7281  N   ASP B 208     7871   6935   7171    482    -20    273       N  
ATOM   7282  CA  ASP B 208       3.604 -10.267 -31.431  1.00 57.38           C  
ANISOU 7282  CA  ASP B 208     7782   6891   7126    471      1    284       C  
ATOM   7283  C   ASP B 208       4.730 -11.109 -32.020  1.00 58.42           C  
ANISOU 7283  C   ASP B 208     7937   7009   7248    480     24    296       C  
ATOM   7284  O   ASP B 208       4.504 -12.227 -32.488  1.00 57.71           O  
ANISOU 7284  O   ASP B 208     7866   6909   7152    483     17    294       O  
ATOM   7285  CB  ASP B 208       2.889 -11.012 -30.308  1.00 55.49           C  
ANISOU 7285  CB  ASP B 208     7509   6668   6903    455    -13    279       C  
ATOM   7286  CG  ASP B 208       3.773 -11.219 -29.084  1.00 56.84           C  
ANISOU 7286  CG  ASP B 208     7647   6858   7090    443      7    290       C  
ATOM   7287  OD1 ASP B 208       4.879 -10.636 -29.012  1.00 54.06           O  
ANISOU 7287  OD1 ASP B 208     7292   6508   6738    446     32    300       O  
ATOM   7288  OD2 ASP B 208       3.351 -11.971 -28.182  1.00 60.06           O  
ANISOU 7288  OD2 ASP B 208     8029   7279   7510    431      0    288       O  
ATOM   7289  N   MET B 209       5.937 -10.553 -31.998  1.00 58.17           N  
ANISOU 7289  N   MET B 209     7906   6978   7217    485     52    308       N  
ATOM   7290  CA  MET B 209       7.078 -11.139 -32.683  1.00 58.54           C  
ANISOU 7290  CA  MET B 209     7977   7009   7254    496     77    320       C  
ATOM   7291  C   MET B 209       8.182 -11.488 -31.701  1.00 57.76           C  
ANISOU 7291  C   MET B 209     7850   6925   7169    487    102    333       C  
ATOM   7292  O   MET B 209       9.335 -11.672 -32.082  1.00 59.04           O  
ANISOU 7292  O   MET B 209     8025   7080   7327    496    128    346       O  
ATOM   7293  CB  MET B 209       7.613 -10.143 -33.709  1.00 61.66           C  
ANISOU 7293  CB  MET B 209     8402   7389   7635    511     91    324       C  
ATOM   7294  CG  MET B 209       8.142 -10.788 -34.977  1.00 66.29           C  
ANISOU 7294  CG  MET B 209     9032   7951   8203    528    102    329       C  
ATOM   7295  SD  MET B 209       6.790 -11.203 -36.086  1.00 69.18           S  
ANISOU 7295  SD  MET B 209     9433   8300   8550    537     69    313       S  
ATOM   7296  CE  MET B 209       6.373  -9.564 -36.660  1.00 69.11           C  
ANISOU 7296  CE  MET B 209     9436   8287   8533    547     62    308       C  
ATOM   7297  N   SER B 210       7.818 -11.573 -30.428  1.00 59.71           N  
ANISOU 7297  N   SER B 210     8058   7195   7433    471     94    331       N  
ATOM   7298  CA  SER B 210       8.785 -11.725 -29.341  1.00 57.19           C  
ANISOU 7298  CA  SER B 210     7706   6895   7129    462    115    343       C  
ATOM   7299  C   SER B 210       9.393 -13.120 -29.300  1.00 55.67           C  
ANISOU 7299  C   SER B 210     7517   6698   6935    463    127    353       C  
ATOM   7300  O   SER B 210       8.756 -14.090 -29.699  1.00 56.75           O  
ANISOU 7300  O   SER B 210     7671   6824   7066    465    114    348       O  
ATOM   7301  CB  SER B 210       8.110 -11.416 -28.006  1.00 54.95           C  
ANISOU 7301  CB  SER B 210     7381   6635   6862    444    101    336       C  
ATOM   7302  OG  SER B 210       7.308 -10.257 -28.113  1.00 54.14           O  
ANISOU 7302  OG  SER B 210     7277   6533   6758    443     85    325       O  
ATOM   7303  N   LEU B 211      10.625 -13.202 -28.810  1.00 54.40           N  
ANISOU 7303  N   LEU B 211     7341   6546   6781    462    154    367       N  
ATOM   7304  CA  LEU B 211      11.328 -14.476 -28.623  1.00 56.85           C  
ANISOU 7304  CA  LEU B 211     7650   6855   7092    464    169    379       C  
ATOM   7305  C   LEU B 211      11.704 -15.213 -29.914  1.00 57.26           C  
ANISOU 7305  C   LEU B 211     7745   6880   7128    480    179    384       C  
ATOM   7306  O   LEU B 211      11.799 -16.444 -29.933  1.00 56.30           O  
ANISOU 7306  O   LEU B 211     7631   6754   7006    481    182    389       O  
ATOM   7307  CB  LEU B 211      10.561 -15.411 -27.673  1.00 55.62           C  
ANISOU 7307  CB  LEU B 211     7470   6713   6948    451    153    375       C  
ATOM   7308  CG  LEU B 211      10.515 -15.128 -26.171  1.00 53.86           C  
ANISOU 7308  CG  LEU B 211     7201   6520   6743    435    151    376       C  
ATOM   7309  CD1 LEU B 211      11.795 -14.468 -25.673  1.00 51.09           C  
ANISOU 7309  CD1 LEU B 211     6831   6182   6398    434    176    389       C  
ATOM   7310  CD2 LEU B 211       9.295 -14.285 -25.848  1.00 56.86           C  
ANISOU 7310  CD2 LEU B 211     7569   6908   7127    426    125    360       C  
ATOM   7311  N   ASN B 212      11.923 -14.450 -30.981  1.00 59.99           N  
ANISOU 7311  N   ASN B 212     8121   7209   7461    492    184    383       N  
ATOM   7312  CA  ASN B 212      12.498 -14.981 -32.211  1.00 62.40           C  
ANISOU 7312  CA  ASN B 212     8467   7489   7750    509    199    389       C  
ATOM   7313  C   ASN B 212      13.928 -14.478 -32.397  1.00 63.33           C  
ANISOU 7313  C   ASN B 212     8587   7605   7869    517    232    405       C  
ATOM   7314  O   ASN B 212      14.210 -13.316 -32.114  1.00 64.68           O  
ANISOU 7314  O   ASN B 212     8743   7785   8045    514    238    405       O  
ATOM   7315  CB  ASN B 212      11.633 -14.615 -33.415  1.00 62.65           C  
ANISOU 7315  CB  ASN B 212     8537   7501   7764    519    180    377       C  
ATOM   7316  CG  ASN B 212      10.410 -15.502 -33.542  1.00 64.38           C  
ANISOU 7316  CG  ASN B 212     8765   7715   7980    515    152    364       C  
ATOM   7317  OD1 ASN B 212      10.379 -16.404 -34.372  1.00 66.67           O  
ANISOU 7317  OD1 ASN B 212     9086   7986   8257    524    152    363       O  
ATOM   7318  ND2 ASN B 212       9.400 -15.257 -32.712  1.00 64.89           N  
ANISOU 7318  ND2 ASN B 212     8802   7797   8056    501    128    353       N  
ATOM   7319  N   PRO B 213      14.839 -15.348 -32.870  1.00 64.73           N  
ANISOU 7319  N   PRO B 213     8783   7770   8040    527    254    418       N  
ATOM   7320  CA  PRO B 213      16.228 -14.924 -32.984  1.00 65.83           C  
ANISOU 7320  CA  PRO B 213     8920   7908   8181    534    286    433       C  
ATOM   7321  C   PRO B 213      16.451 -14.190 -34.303  1.00 68.15           C  
ANISOU 7321  C   PRO B 213     9253   8179   8459    550    295    432       C  
ATOM   7322  O   PRO B 213      16.861 -14.799 -35.293  1.00 71.93           O  
ANISOU 7322  O   PRO B 213     9768   8636   8924    564    307    438       O  
ATOM   7323  CB  PRO B 213      17.002 -16.247 -32.943  1.00 66.93           C  
ANISOU 7323  CB  PRO B 213     9063   8044   8321    539    305    447       C  
ATOM   7324  CG  PRO B 213      16.012 -17.309 -33.336  1.00 68.93           C  
ANISOU 7324  CG  PRO B 213     9338   8285   8566    540    284    437       C  
ATOM   7325  CD  PRO B 213      14.638 -16.694 -33.433  1.00 65.77           C  
ANISOU 7325  CD  PRO B 213     8940   7886   8162    533    251    418       C  
ATOM   7326  N   ILE B 214      16.166 -12.890 -34.311  1.00 67.46           N  
ANISOU 7326  N   ILE B 214     9161   8096   8373    548    288    425       N  
ATOM   7327  CA  ILE B 214      16.217 -12.101 -35.538  1.00 68.31           C  
ANISOU 7327  CA  ILE B 214     9306   8181   8465    563    293    423       C  
ATOM   7328  C   ILE B 214      17.548 -11.365 -35.666  1.00 70.64           C  
ANISOU 7328  C   ILE B 214     9598   8474   8764    568    327    437       C  
ATOM   7329  O   ILE B 214      17.911 -10.575 -34.793  1.00 72.35           O  
ANISOU 7329  O   ILE B 214     9781   8710   8997    557    333    439       O  
ATOM   7330  CB  ILE B 214      15.017 -11.128 -35.638  1.00 65.92           C  
ANISOU 7330  CB  ILE B 214     9005   7881   8160    559    266    407       C  
ATOM   7331  CG1 ILE B 214      13.705 -11.920 -35.740  1.00 64.24           C  
ANISOU 7331  CG1 ILE B 214     8801   7666   7940    556    234    393       C  
ATOM   7332  CG2 ILE B 214      15.170 -10.195 -36.835  1.00 64.02           C  
ANISOU 7332  CG2 ILE B 214     8800   7619   7903    575    275    407       C  
ATOM   7333  CD1 ILE B 214      12.448 -11.099 -35.539  1.00 62.25           C  
ANISOU 7333  CD1 ILE B 214     8540   7421   7689    549    204    377       C  
ATOM   7334  N   ASP B 215      18.273 -11.637 -36.753  1.00 73.82           N  
ANISOU 7334  N   ASP B 215    10038   8855   9155    586    348    447       N  
ATOM   7335  CA  ASP B 215      19.524 -10.928 -37.047  1.00 74.96           C  
ANISOU 7335  CA  ASP B 215    10184   8993   9301    593    380    460       C  
ATOM   7336  C   ASP B 215      19.507 -10.171 -38.385  1.00 76.53           C  
ANISOU 7336  C   ASP B 215    10426   9167   9483    610    387    458       C  
ATOM   7337  O   ASP B 215      20.376  -9.334 -38.643  1.00 77.86           O  
ANISOU 7337  O   ASP B 215    10597   9331   9654    616    411    467       O  
ATOM   7338  CB  ASP B 215      20.747 -11.861 -36.933  1.00 76.85           C  
ANISOU 7338  CB  ASP B 215    10419   9232   9546    597    408    477       C  
ATOM   7339  CG  ASP B 215      20.752 -12.986 -37.968  1.00 79.24           C  
ANISOU 7339  CG  ASP B 215    10765   9512   9831    613    412    481       C  
ATOM   7340  OD1 ASP B 215      20.091 -12.868 -39.024  1.00 80.57           O  
ANISOU 7340  OD1 ASP B 215    10971   9659   9981    624    400    472       O  
ATOM   7341  OD2 ASP B 215      21.443 -14.000 -37.724  1.00 78.76           O  
ANISOU 7341  OD2 ASP B 215    10697   9452   9775    614    428    493       O  
ATOM   7342  N   PHE B 216      18.513 -10.464 -39.223  1.00 77.26           N  
ANISOU 7342  N   PHE B 216    10552   9244   9556    619    365    447       N  
ATOM   7343  CA  PHE B 216      18.402  -9.832 -40.536  1.00 76.85           C  
ANISOU 7343  CA  PHE B 216    10544   9169   9486    637    368    445       C  
ATOM   7344  C   PHE B 216      16.981  -9.358 -40.832  1.00 73.76           C  
ANISOU 7344  C   PHE B 216    10165   8775   9084    637    334    428       C  
ATOM   7345  O   PHE B 216      16.020 -10.128 -40.748  1.00 68.75           O  
ANISOU 7345  O   PHE B 216     9533   8144   8445    633    307    417       O  
ATOM   7346  CB  PHE B 216      18.909 -10.777 -41.644  1.00 81.01           C  
ANISOU 7346  CB  PHE B 216    11113   9671   9994    655    384    453       C  
ATOM   7347  CG  PHE B 216      18.759 -10.227 -43.046  1.00 84.97           C  
ANISOU 7347  CG  PHE B 216    11664  10147  10474    675    386    451       C  
ATOM   7348  CD1 PHE B 216      19.711  -9.359 -43.577  1.00 86.34           C  
ANISOU 7348  CD1 PHE B 216    11850  10309  10646    687    416    463       C  
ATOM   7349  CD2 PHE B 216      17.669 -10.588 -43.842  1.00 87.09           C  
ANISOU 7349  CD2 PHE B 216    11965  10403  10722    684    359    438       C  
ATOM   7350  CE1 PHE B 216      19.572  -8.856 -44.866  1.00 87.23           C  
ANISOU 7350  CE1 PHE B 216    12008  10398  10737    706    420    461       C  
ATOM   7351  CE2 PHE B 216      17.527 -10.088 -45.130  1.00 86.56           C  
ANISOU 7351  CE2 PHE B 216    11943  10313  10632    703    361    437       C  
ATOM   7352  CZ  PHE B 216      18.481  -9.222 -45.643  1.00 87.69           C  
ANISOU 7352  CZ  PHE B 216    12099  10444  10774    715    392    448       C  
ATOM   7353  N   ILE B 217      16.868  -8.076 -41.163  1.00 71.45           N  
ANISOU 7353  N   ILE B 217     9879   8479   8789    642    336    425       N  
ATOM   7354  CA  ILE B 217      15.651  -7.524 -41.741  1.00 73.86           C  
ANISOU 7354  CA  ILE B 217    10204   8777   9080    648    308    410       C  
ATOM   7355  C   ILE B 217      16.044  -6.892 -43.070  1.00 76.86           C  
ANISOU 7355  C   ILE B 217    10628   9132   9441    669    325    416       C  
ATOM   7356  O   ILE B 217      16.942  -6.049 -43.121  1.00 75.92           O  
ANISOU 7356  O   ILE B 217    10506   9010   9329    673    352    426       O  
ATOM   7357  CB  ILE B 217      14.971  -6.477 -40.832  1.00 72.61           C  
ANISOU 7357  CB  ILE B 217    10012   8639   8938    633    291    401       C  
ATOM   7358  CG1 ILE B 217      14.707  -7.060 -39.435  1.00 74.41           C  
ANISOU 7358  CG1 ILE B 217    10193   8893   9185    611    279    397       C  
ATOM   7359  CG2 ILE B 217      13.673  -5.987 -41.468  1.00 71.35           C  
ANISOU 7359  CG2 ILE B 217     9873   8472   8762    640    262    387       C  
ATOM   7360  CD1 ILE B 217      14.065  -6.100 -38.455  1.00 71.55           C  
ANISOU 7360  CD1 ILE B 217     9795   8551   8838    596    263    388       C  
ATOM   7361  N   GLN B 218      15.376  -7.314 -44.141  1.00 78.56           N  
ANISOU 7361  N   GLN B 218    10885   9330   9634    684    309    409       N  
ATOM   7362  CA  GLN B 218      15.736  -6.883 -45.485  1.00 82.27           C  
ANISOU 7362  CA  GLN B 218    11400   9774  10081    707    324    414       C  
ATOM   7363  C   GLN B 218      15.537  -5.388 -45.691  1.00 85.12           C  
ANISOU 7363  C   GLN B 218    11764  10134  10443    712    326    412       C  
ATOM   7364  O   GLN B 218      14.651  -4.779 -45.088  1.00 86.07           O  
ANISOU 7364  O   GLN B 218    11861  10269  10571    701    303    402       O  
ATOM   7365  CB  GLN B 218      14.953  -7.665 -46.537  1.00 81.35           C  
ANISOU 7365  CB  GLN B 218    11328   9642   9940    720    303    406       C  
ATOM   7366  CG  GLN B 218      15.686  -7.788 -47.861  1.00 76.47           C  
ANISOU 7366  CG  GLN B 218    10758   8996   9300    743    327    415       C  
ATOM   7367  CD  GLN B 218      14.766  -8.146 -49.004  1.00 75.40           C  
ANISOU 7367  CD  GLN B 218    10667   8844   9136    759    302    404       C  
ATOM   7368  OE1 GLN B 218      13.925  -9.034 -48.887  1.00 74.92           O  
ANISOU 7368  OE1 GLN B 218    10606   8787   9071    752    274    393       O  
ATOM   7369  NE2 GLN B 218      14.924  -7.454 -50.123  1.00 78.27           N  
ANISOU 7369  NE2 GLN B 218    11070   9188   9480    779    313    408       N  
ATOM   7370  N   ASP B 219      16.381  -4.812 -46.543  1.00 88.86           N  
ANISOU 7370  N   ASP B 219    12266  10589  10908    728    355    424       N  
ATOM   7371  CA  ASP B 219      16.315  -3.398 -46.881  1.00 90.10           C  
ANISOU 7371  CA  ASP B 219    12430  10740  11063    736    362    424       C  
ATOM   7372  C   ASP B 219      14.954  -3.039 -47.464  1.00 88.20           C  
ANISOU 7372  C   ASP B 219    12211  10495  10804    744    328    410       C  
ATOM   7373  O   ASP B 219      14.467  -3.713 -48.374  1.00 89.03           O  
ANISOU 7373  O   ASP B 219    12353  10587  10887    758    314    405       O  
ATOM   7374  CB  ASP B 219      17.424  -3.037 -47.868  1.00 94.81           C  
ANISOU 7374  CB  ASP B 219    13060  11313  11648    755    399    438       C  
ATOM   7375  CG  ASP B 219      17.641  -1.545 -47.970  1.00102.26           C  
ANISOU 7375  CG  ASP B 219    14003  12253  12598    759    415    442       C  
ATOM   7376  OD1 ASP B 219      17.221  -0.953 -48.987  1.00106.69           O  
ANISOU 7376  OD1 ASP B 219    14601  12797  13139    778    411    440       O  
ATOM   7377  OD2 ASP B 219      18.215  -0.960 -47.024  1.00105.36           O  
ANISOU 7377  OD2 ASP B 219    14357  12660  13014    744    430    446       O  
ATOM   7378  N   GLN B 220      14.343  -1.992 -46.908  1.00 86.80           N  
ANISOU 7378  N   GLN B 220    12011  10330  10638    736    316    402       N  
ATOM   7379  CA  GLN B 220      13.059  -1.456 -47.383  1.00 86.33           C  
ANISOU 7379  CA  GLN B 220    11968  10269  10564    744    285    390       C  
ATOM   7380  C   GLN B 220      11.872  -2.418 -47.155  1.00 88.21           C  
ANISOU 7380  C   GLN B 220    12200  10517  10797    736    245    376       C  
ATOM   7381  O   GLN B 220      10.804  -2.264 -47.758  1.00 85.11           O  
ANISOU 7381  O   GLN B 220    11829  10121  10389    745    218    365       O  
ATOM   7382  CB  GLN B 220      13.180  -1.019 -48.854  1.00 86.62           C  
ANISOU 7382  CB  GLN B 220    12057  10279  10574    771    296    395       C  
ATOM   7383  CG  GLN B 220      12.242   0.101 -49.271  1.00 90.14           C  
ANISOU 7383  CG  GLN B 220    12515  10722  11010    781    278    387       C  
ATOM   7384  CD  GLN B 220      12.946   1.187 -50.059  1.00 88.91           C  
ANISOU 7384  CD  GLN B 220    12385  10547  10846    799    309    399       C  
ATOM   7385  OE1 GLN B 220      13.786   1.911 -49.524  1.00 84.13           O  
ANISOU 7385  OE1 GLN B 220    11759   9946  10260    792    337    407       O  
ATOM   7386  NE2 GLN B 220      12.597   1.314 -51.335  1.00 88.65           N  
ANISOU 7386  NE2 GLN B 220    12400  10495  10786    823    303    399       N  
ATOM   7387  N   ALA B 221      12.066  -3.388 -46.259  1.00 90.35           N  
ANISOU 7387  N   ALA B 221    12441  10802  11083    719    243    375       N  
ATOM   7388  CA  ALA B 221      11.050  -4.404 -45.947  1.00 85.39           C  
ANISOU 7388  CA  ALA B 221    11805  10184  10454    709    209    363       C  
ATOM   7389  C   ALA B 221       9.782  -3.841 -45.310  1.00 82.92           C  
ANISOU 7389  C   ALA B 221    11466   9888  10149    698    176    349       C  
ATOM   7390  O   ALA B 221       8.693  -4.360 -45.538  1.00 84.46           O  
ANISOU 7390  O   ALA B 221    11670  10085  10336    698    144    337       O  
ATOM   7391  CB  ALA B 221      11.640  -5.493 -45.061  1.00 81.98           C  
ANISOU 7391  CB  ALA B 221    11345   9763  10038    693    218    367       C  
ATOM   7392  N   PHE B 222       9.928  -2.787 -44.513  1.00 80.62           N  
ANISOU 7392  N   PHE B 222    11144   9609   9876    688    185    351       N  
ATOM   7393  CA  PHE B 222       8.804  -2.218 -43.772  1.00 79.25           C  
ANISOU 7393  CA  PHE B 222    10941   9453   9713    676    157    338       C  
ATOM   7394  C   PHE B 222       8.183  -1.001 -44.443  1.00 79.30           C  
ANISOU 7394  C   PHE B 222    10968   9452   9709    690    149    335       C  
ATOM   7395  O   PHE B 222       7.331  -0.327 -43.858  1.00 72.41           O  
ANISOU 7395  O   PHE B 222    10072   8592   8846    682    131    326       O  
ATOM   7396  CB  PHE B 222       9.222  -1.898 -42.333  1.00 79.01           C  
ANISOU 7396  CB  PHE B 222    10862   9446   9712    654    168    341       C  
ATOM   7397  CG  PHE B 222       9.183  -3.091 -41.426  1.00 80.38           C  
ANISOU 7397  CG  PHE B 222    11007   9634   9898    637    159    339       C  
ATOM   7398  CD1 PHE B 222      10.283  -3.935 -41.313  1.00 79.71           C  
ANISOU 7398  CD1 PHE B 222    10922   9547   9817    635    183    350       C  
ATOM   7399  CD2 PHE B 222       8.031  -3.391 -40.707  1.00 77.32           C  
ANISOU 7399  CD2 PHE B 222    10594   9263   9519    623    128    326       C  
ATOM   7400  CE1 PHE B 222      10.237  -5.047 -40.488  1.00 79.97           C  
ANISOU 7400  CE1 PHE B 222    10930   9594   9862    620    176    348       C  
ATOM   7401  CE2 PHE B 222       7.978  -4.501 -39.884  1.00 75.17           C  
ANISOU 7401  CE2 PHE B 222    10298   9004   9258    608    120    325       C  
ATOM   7402  CZ  PHE B 222       9.083  -5.330 -39.773  1.00 78.02           C  
ANISOU 7402  CZ  PHE B 222    10658   9362   9622    607    144    336       C  
ATOM   7403  N   GLN B 223       8.597  -0.745 -45.682  1.00 84.02           N  
ANISOU 7403  N   GLN B 223    11609  10027  10285    713    163    341       N  
ATOM   7404  CA  GLN B 223       8.150   0.429 -46.424  1.00 84.96           C  
ANISOU 7404  CA  GLN B 223    11751  10136  10392    729    161    340       C  
ATOM   7405  C   GLN B 223       6.661   0.367 -46.760  1.00 84.61           C  
ANISOU 7405  C   GLN B 223    11716  10095  10335    734    119    326       C  
ATOM   7406  O   GLN B 223       6.173  -0.625 -47.311  1.00 84.47           O  
ANISOU 7406  O   GLN B 223    11719  10073  10302    739     99    320       O  
ATOM   7407  CB  GLN B 223       8.986   0.622 -47.691  1.00 85.98           C  
ANISOU 7407  CB  GLN B 223    11926  10240  10500    753    187    351       C  
ATOM   7408  CG  GLN B 223       9.224   2.081 -48.058  1.00 91.69           C  
ANISOU 7408  CG  GLN B 223    12660  10954  11221    765    206    357       C  
ATOM   7409  CD  GLN B 223       9.950   2.866 -46.967  1.00 92.74           C  
ANISOU 7409  CD  GLN B 223    12754  11099  11383    748    230    363       C  
ATOM   7410  OE1 GLN B 223      10.999   2.449 -46.469  1.00 91.52           O  
ANISOU 7410  OE1 GLN B 223    12583  10948  11242    737    254    371       O  
ATOM   7411  NE2 GLN B 223       9.393   4.015 -46.600  1.00 89.45           N  
ANISOU 7411  NE2 GLN B 223    12322  10689  10975    745    224    358       N  
ATOM   7412  N   GLY B 224       5.953   1.435 -46.399  1.00 84.67           N  
ANISOU 7412  N   GLY B 224    11707  10111  10350    732    108    321       N  
ATOM   7413  CA  GLY B 224       4.527   1.574 -46.678  1.00 82.66           C  
ANISOU 7413  CA  GLY B 224    11458   9861  10085    737     70    308       C  
ATOM   7414  C   GLY B 224       3.644   0.528 -46.025  1.00 80.09           C  
ANISOU 7414  C   GLY B 224    11108   9552   9768    720     38    296       C  
ATOM   7415  O   GLY B 224       2.700   0.043 -46.646  1.00 82.62           O  
ANISOU 7415  O   GLY B 224    11448   9870  10073    728      8    286       O  
ATOM   7416  N   ILE B 225       3.951   0.168 -44.780  1.00 77.64           N  
ANISOU 7416  N   ILE B 225    10758   9259   9483    698     44    296       N  
ATOM   7417  CA  ILE B 225       3.104  -0.767 -44.032  1.00 74.02           C  
ANISOU 7417  CA  ILE B 225    10271   8816   9034    680     15    285       C  
ATOM   7418  C   ILE B 225       2.613  -0.195 -42.693  1.00 70.45           C  
ANISOU 7418  C   ILE B 225     9772   8387   8609    661      7    280       C  
ATOM   7419  O   ILE B 225       3.325   0.559 -42.018  1.00 62.29           O  
ANISOU 7419  O   ILE B 225     8716   7359   7589    653     32    287       O  
ATOM   7420  CB  ILE B 225       3.750  -2.172 -43.838  1.00 74.57           C  
ANISOU 7420  CB  ILE B 225    10340   8886   9107    671     23    288       C  
ATOM   7421  CG1 ILE B 225       4.761  -2.181 -42.693  1.00 71.94           C  
ANISOU 7421  CG1 ILE B 225     9971   8565   8797    654     50    297       C  
ATOM   7422  CG2 ILE B 225       4.386  -2.687 -45.127  1.00 76.29           C  
ANISOU 7422  CG2 ILE B 225    10606   9081   9300    691     36    294       C  
ATOM   7423  CD1 ILE B 225       4.714  -3.456 -41.882  1.00 72.65           C  
ANISOU 7423  CD1 ILE B 225    10036   8667   8899    637     42    294       C  
ATOM   7424  N   LYS B 226       1.385  -0.561 -42.332  1.00 72.50           N  
ANISOU 7424  N   LYS B 226    10015   8658   8871    652    -26    267       N  
ATOM   7425  CA  LYS B 226       0.749  -0.093 -41.108  1.00 72.82           C  
ANISOU 7425  CA  LYS B 226    10012   8720   8935    635    -37    261       C  
ATOM   7426  C   LYS B 226       0.425  -1.259 -40.178  1.00 72.62           C  
ANISOU 7426  C   LYS B 226     9957   8710   8925    615    -52    255       C  
ATOM   7427  O   LYS B 226      -0.080  -2.297 -40.611  1.00 70.77           O  
ANISOU 7427  O   LYS B 226     9736   8472   8681    616    -72    249       O  
ATOM   7428  CB  LYS B 226      -0.521   0.694 -41.435  1.00 78.44           C  
ANISOU 7428  CB  LYS B 226    10728   9434   9642    643    -65    252       C  
ATOM   7429  CG  LYS B 226      -1.025   1.569 -40.299  1.00 83.71           C  
ANISOU 7429  CG  LYS B 226    11355  10119  10331    629    -69    248       C  
ATOM   7430  CD  LYS B 226      -2.015   2.600 -40.809  1.00 86.68           C  
ANISOU 7430  CD  LYS B 226    11742  10493  10699    643    -87    243       C  
ATOM   7431  CE  LYS B 226      -2.429   3.554 -39.702  1.00 89.41           C  
ANISOU 7431  CE  LYS B 226    12050  10855  11067    630    -87    240       C  
ATOM   7432  NZ  LYS B 226      -2.993   4.814 -40.262  1.00 90.03           N  
ANISOU 7432  NZ  LYS B 226    12142  10926  11136    647    -91    240       N  
ATOM   7433  N   LEU B 227       0.739  -1.069 -38.899  1.00 70.56           N  
ANISOU 7433  N   LEU B 227     9655   8465   8686    596    -40    257       N  
ATOM   7434  CA  LEU B 227       0.459  -2.041 -37.849  1.00 66.26           C  
ANISOU 7434  CA  LEU B 227     9077   7937   8158    576    -51    253       C  
ATOM   7435  C   LEU B 227      -0.087  -1.319 -36.626  1.00 65.97           C  
ANISOU 7435  C   LEU B 227     8999   7921   8144    560    -58    248       C  
ATOM   7436  O   LEU B 227       0.266  -0.161 -36.367  1.00 65.07           O  
ANISOU 7436  O   LEU B 227     8876   7809   8035    561    -42    252       O  
ATOM   7437  CB  LEU B 227       1.728  -2.807 -37.461  1.00 63.15           C  
ANISOU 7437  CB  LEU B 227     8677   7544   7771    569    -24    263       C  
ATOM   7438  CG  LEU B 227       2.284  -3.894 -38.386  1.00 62.64           C  
ANISOU 7438  CG  LEU B 227     8647   7463   7689    579    -17    268       C  
ATOM   7439  CD1 LEU B 227       3.662  -4.324 -37.910  1.00 60.12           C  
ANISOU 7439  CD1 LEU B 227     8318   7146   7379    572     14    281       C  
ATOM   7440  CD2 LEU B 227       1.359  -5.099 -38.474  1.00 60.86           C  
ANISOU 7440  CD2 LEU B 227     8423   7239   7461    574    -46    258       C  
ATOM   7441  N   HIS B 228      -0.949  -2.008 -35.882  1.00 63.57           N  
ANISOU 7441  N   HIS B 228     8669   7631   7851    546    -81    240       N  
ATOM   7442  CA  HIS B 228      -1.483  -1.482 -34.634  1.00 62.40           C  
ANISOU 7442  CA  HIS B 228     8480   7504   7725    530    -87    235       C  
ATOM   7443  C   HIS B 228      -0.447  -1.583 -33.541  1.00 63.10           C  
ANISOU 7443  C   HIS B 228     8540   7605   7830    515    -61    243       C  
ATOM   7444  O   HIS B 228       0.136  -0.568 -33.158  1.00 63.73           O  
ANISOU 7444  O   HIS B 228     8609   7688   7916    513    -41    248       O  
ATOM   7445  CB  HIS B 228      -2.776  -2.189 -34.261  1.00 63.26           C  
ANISOU 7445  CB  HIS B 228     8573   7623   7840    521   -120    224       C  
ATOM   7446  CG  HIS B 228      -3.497  -1.560 -33.098  1.00 63.28           C  
ANISOU 7446  CG  HIS B 228     8536   7644   7863    507   -129    218       C  
ATOM   7447  ND1 HIS B 228      -4.252  -0.453 -33.229  1.00 63.81           N  
ANISOU 7447  ND1 HIS B 228     8602   7712   7929    513   -140    213       N  
ATOM   7448  CD2 HIS B 228      -3.560  -1.923 -31.759  1.00 60.97           C  
ANISOU 7448  CD2 HIS B 228     8204   7371   7590    487   -128    217       C  
ATOM   7449  CE1 HIS B 228      -4.771  -0.123 -32.034  1.00 64.03           C  
ANISOU 7449  CE1 HIS B 228     8592   7758   7977    498   -146    209       C  
ATOM   7450  NE2 HIS B 228      -4.346  -1.022 -31.134  1.00 64.94           N  
ANISOU 7450  NE2 HIS B 228     8683   7884   8104    482   -139    211       N  
ATOM   7451  N   GLU B 229      -0.187  -2.791 -33.033  1.00 61.67           N  
ANISOU 7451  N   GLU B 229     8346   7430   7654    504    -61    245       N  
ATOM   7452  CA  GLU B 229       0.941  -2.970 -32.115  1.00 61.07           C  
ANISOU 7452  CA  GLU B 229     8246   7365   7592    492    -34    254       C  
ATOM   7453  C   GLU B 229       1.984  -3.996 -32.562  1.00 59.29           C  
ANISOU 7453  C   GLU B 229     8040   7130   7358    497    -16    264       C  
ATOM   7454  O   GLU B 229       1.649  -5.084 -33.025  1.00 60.71           O  
ANISOU 7454  O   GLU B 229     8234   7301   7529    499    -29    261       O  
ATOM   7455  CB  GLU B 229       0.490  -3.191 -30.665  1.00 66.01           C  
ANISOU 7455  CB  GLU B 229     8828   8014   8238    472    -43    250       C  
ATOM   7456  CG  GLU B 229      -0.067  -4.562 -30.306  1.00 67.68           C  
ANISOU 7456  CG  GLU B 229     9029   8230   8454    463    -60    246       C  
ATOM   7457  CD  GLU B 229      -0.212  -4.753 -28.799  1.00 67.50           C  
ANISOU 7457  CD  GLU B 229     8962   8231   8452    444    -60    245       C  
ATOM   7458  OE1 GLU B 229      -0.165  -3.749 -28.046  1.00 63.96           O  
ANISOU 7458  OE1 GLU B 229     8491   7795   8015    437    -53    245       O  
ATOM   7459  OE2 GLU B 229      -0.372  -5.915 -28.366  1.00 68.62           O  
ANISOU 7459  OE2 GLU B 229     9093   8379   8600    435    -67    245       O  
ATOM   7460  N   LEU B 230       3.251  -3.607 -32.437  1.00 57.47           N  
ANISOU 7460  N   LEU B 230     7808   6898   7130    497     13    275       N  
ATOM   7461  CA  LEU B 230       4.381  -4.456 -32.781  1.00 55.44           C  
ANISOU 7461  CA  LEU B 230     7565   6632   6867    502     35    286       C  
ATOM   7462  C   LEU B 230       5.210  -4.710 -31.544  1.00 56.46           C  
ANISOU 7462  C   LEU B 230     7658   6780   7013    486     53    293       C  
ATOM   7463  O   LEU B 230       5.751  -3.778 -30.939  1.00 57.09           O  
ANISOU 7463  O   LEU B 230     7718   6869   7103    480     69    296       O  
ATOM   7464  CB  LEU B 230       5.256  -3.812 -33.860  1.00 55.94           C  
ANISOU 7464  CB  LEU B 230     7661   6676   6915    519     57    294       C  
ATOM   7465  CG  LEU B 230       6.549  -4.542 -34.274  1.00 57.71           C  
ANISOU 7465  CG  LEU B 230     7902   6890   7134    525     83    307       C  
ATOM   7466  CD1 LEU B 230       6.288  -5.951 -34.793  1.00 54.46           C  
ANISOU 7466  CD1 LEU B 230     7510   6469   6711    529     72    306       C  
ATOM   7467  CD2 LEU B 230       7.318  -3.735 -35.311  1.00 57.71           C  
ANISOU 7467  CD2 LEU B 230     7934   6871   7121    542    105    314       C  
ATOM   7468  N   THR B 231       5.310  -5.982 -31.180  1.00 56.48           N  
ANISOU 7468  N   THR B 231     7653   6787   7020    480     51    296       N  
ATOM   7469  CA  THR B 231       6.040  -6.384 -29.992  1.00 53.72           C  
ANISOU 7469  CA  THR B 231     7269   6456   6686    465     66    303       C  
ATOM   7470  C   THR B 231       7.335  -7.078 -30.382  1.00 50.55           C  
ANISOU 7470  C   THR B 231     6882   6046   6279    472     92    317       C  
ATOM   7471  O   THR B 231       7.312  -8.157 -30.967  1.00 48.95           O  
ANISOU 7471  O   THR B 231     6700   5831   6067    479     89    319       O  
ATOM   7472  CB  THR B 231       5.180  -7.305 -29.111  1.00 52.84           C  
ANISOU 7472  CB  THR B 231     7132   6358   6584    452     45    297       C  
ATOM   7473  OG1 THR B 231       3.837  -6.805 -29.085  1.00 54.27           O  
ANISOU 7473  OG1 THR B 231     7309   6542   6767    450     18    284       O  
ATOM   7474  CG2 THR B 231       5.728  -7.357 -27.697  1.00 50.48           C  
ANISOU 7474  CG2 THR B 231     6791   6083   6303    436     57    303       C  
ATOM   7475  N   LEU B 232       8.454  -6.437 -30.055  1.00 49.63           N  
ANISOU 7475  N   LEU B 232     6753   5934   6168    471    118    326       N  
ATOM   7476  CA  LEU B 232       9.782  -6.984 -30.312  1.00 49.40           C  
ANISOU 7476  CA  LEU B 232     6733   5899   6136    476    146    341       C  
ATOM   7477  C   LEU B 232      10.572  -7.161 -29.021  1.00 48.01           C  
ANISOU 7477  C   LEU B 232     6517   5746   5977    462    161    348       C  
ATOM   7478  O   LEU B 232      11.567  -6.473 -28.779  1.00 48.65           O  
ANISOU 7478  O   LEU B 232     6588   5832   6065    460    184    356       O  
ATOM   7479  CB  LEU B 232      10.563  -6.097 -31.294  1.00 50.55           C  
ANISOU 7479  CB  LEU B 232     6905   6027   6271    490    167    347       C  
ATOM   7480  CG  LEU B 232      10.038  -5.928 -32.722  1.00 51.14           C  
ANISOU 7480  CG  LEU B 232     7025   6077   6327    508    157    342       C  
ATOM   7481  CD1 LEU B 232      10.744  -4.755 -33.393  1.00 50.84           C  
ANISOU 7481  CD1 LEU B 232     7005   6026   6283    519    179    347       C  
ATOM   7482  CD2 LEU B 232      10.173  -7.213 -33.537  1.00 49.64           C  
ANISOU 7482  CD2 LEU B 232     6865   5871   6123    519    157    346       C  
ATOM   7483  N   ARG B 233      10.121  -8.094 -28.194  1.00 49.73           N  
ANISOU 7483  N   ARG B 233     6714   5978   6203    451    148    347       N  
ATOM   7484  CA  ARG B 233      10.775  -8.366 -26.915  1.00 48.99           C  
ANISOU 7484  CA  ARG B 233     6581   5907   6124    438    160    354       C  
ATOM   7485  C   ARG B 233      11.687  -9.577 -26.997  1.00 47.80           C  
ANISOU 7485  C   ARG B 233     6436   5753   5972    442    177    367       C  
ATOM   7486  O   ARG B 233      11.325 -10.588 -27.593  1.00 46.45           O  
ANISOU 7486  O   ARG B 233     6286   5568   5792    449    169    367       O  
ATOM   7487  CB  ARG B 233       9.738  -8.540 -25.803  1.00 47.73           C  
ANISOU 7487  CB  ARG B 233     6390   5766   5976    423    137    344       C  
ATOM   7488  CG  ARG B 233       9.163  -7.224 -25.315  1.00 47.67           C  
ANISOU 7488  CG  ARG B 233     6365   5770   5976    415    128    334       C  
ATOM   7489  CD  ARG B 233       8.393  -7.398 -24.021  1.00 47.61           C  
ANISOU 7489  CD  ARG B 233     6322   5785   5982    399    111    328       C  
ATOM   7490  NE  ARG B 233       9.260  -7.441 -22.844  1.00 45.65           N  
ANISOU 7490  NE  ARG B 233     6038   5558   5745    388    127    336       N  
ATOM   7491  CZ  ARG B 233       8.862  -7.843 -21.639  1.00 46.32           C  
ANISOU 7491  CZ  ARG B 233     6091   5665   5841    375    118    334       C  
ATOM   7492  NH1 ARG B 233       7.613  -8.242 -21.447  1.00 45.83           N  
ANISOU 7492  NH1 ARG B 233     6026   5604   5782    371     94    324       N  
ATOM   7493  NH2 ARG B 233       9.714  -7.857 -20.619  1.00 47.61           N  
ANISOU 7493  NH2 ARG B 233     6225   5849   6014    365    133    341       N  
ATOM   7494  N   GLY B 234      12.875  -9.454 -26.407  1.00 49.89           N  
ANISOU 7494  N   GLY B 234     6679   6030   6245    438    201    379       N  
ATOM   7495  CA  GLY B 234      13.859 -10.542 -26.364  1.00 53.91           C  
ANISOU 7495  CA  GLY B 234     7188   6538   6754    442    220    394       C  
ATOM   7496  C   GLY B 234      14.196 -11.128 -27.726  1.00 57.28           C  
ANISOU 7496  C   GLY B 234     7659   6939   7166    460    229    400       C  
ATOM   7497  O   GLY B 234      14.303 -12.348 -27.874  1.00 58.15           O  
ANISOU 7497  O   GLY B 234     7778   7043   7273    464    231    406       O  
ATOM   7498  N   ASN B 235      14.357 -10.255 -28.719  1.00 58.74           N  
ANISOU 7498  N   ASN B 235     7871   7106   7341    470    236    398       N  
ATOM   7499  CA  ASN B 235      14.606 -10.671 -30.099  1.00 62.08           C  
ANISOU 7499  CA  ASN B 235     8338   7502   7747    488    244    402       C  
ATOM   7500  C   ASN B 235      16.074 -10.706 -30.504  1.00 64.14           C  
ANISOU 7500  C   ASN B 235     8607   7754   8006    497    277    418       C  
ATOM   7501  O   ASN B 235      16.466 -11.503 -31.355  1.00 63.90           O  
ANISOU 7501  O   ASN B 235     8607   7706   7965    510    288    425       O  
ATOM   7502  CB  ASN B 235      13.859  -9.758 -31.077  1.00 62.16           C  
ANISOU 7502  CB  ASN B 235     8376   7494   7744    497    231    391       C  
ATOM   7503  CG  ASN B 235      12.425 -10.186 -31.304  1.00 62.29           C  
ANISOU 7503  CG  ASN B 235     8405   7507   7755    496    199    376       C  
ATOM   7504  OD1 ASN B 235      12.102 -11.372 -31.317  1.00 63.93           O  
ANISOU 7504  OD1 ASN B 235     8618   7712   7960    496    190    376       O  
ATOM   7505  ND2 ASN B 235      11.559  -9.215 -31.503  1.00 61.68           N  
ANISOU 7505  ND2 ASN B 235     8332   7429   7676    496    181    365       N  
ATOM   7506  N   PHE B 236      16.876  -9.837 -29.899  1.00 64.38           N  
ANISOU 7506  N   PHE B 236     8613   7799   8049    491    294    423       N  
ATOM   7507  CA  PHE B 236      18.202  -9.547 -30.419  1.00 66.10           C  
ANISOU 7507  CA  PHE B 236     8840   8007   8265    500    325    437       C  
ATOM   7508  C   PHE B 236      19.308 -10.000 -29.484  1.00 68.68           C  
ANISOU 7508  C   PHE B 236     9134   8353   8605    493    345    451       C  
ATOM   7509  O   PHE B 236      19.212  -9.828 -28.271  1.00 71.32           O  
ANISOU 7509  O   PHE B 236     9430   8713   8954    478    338    448       O  
ATOM   7510  CB  PHE B 236      18.324  -8.056 -30.729  1.00 66.93           C  
ANISOU 7510  CB  PHE B 236     8950   8109   8372    501    332    432       C  
ATOM   7511  CG  PHE B 236      17.230  -7.531 -31.626  1.00 68.37           C  
ANISOU 7511  CG  PHE B 236     9163   8273   8540    509    312    419       C  
ATOM   7512  CD1 PHE B 236      16.205  -6.737 -31.110  1.00 68.71           C  
ANISOU 7512  CD1 PHE B 236     9191   8328   8588    499    289    405       C  
ATOM   7513  CD2 PHE B 236      17.219  -7.831 -32.986  1.00 66.40           C  
ANISOU 7513  CD2 PHE B 236     8959   7996   8272    528    316    422       C  
ATOM   7514  CE1 PHE B 236      15.198  -6.252 -31.933  1.00 67.28           C  
ANISOU 7514  CE1 PHE B 236     9037   8131   8394    507    271    394       C  
ATOM   7515  CE2 PHE B 236      16.213  -7.350 -33.810  1.00 66.79           C  
ANISOU 7515  CE2 PHE B 236     9037   8031   8308    536    297    410       C  
ATOM   7516  CZ  PHE B 236      15.201  -6.560 -33.285  1.00 67.38           C  
ANISOU 7516  CZ  PHE B 236     9094   8117   8388    526    274    396       C  
ATOM   7517  N   ASN B 237      20.362 -10.568 -30.066  1.00 71.89           N  
ANISOU 7517  N   ASN B 237     9557   8748   9008    505    370    465       N  
ATOM   7518  CA  ASN B 237      21.449 -11.171 -29.298  1.00 75.84           C  
ANISOU 7518  CA  ASN B 237    10029   9264   9520    501    390    480       C  
ATOM   7519  C   ASN B 237      22.549 -10.191 -28.884  1.00 75.22           C  
ANISOU 7519  C   ASN B 237     9927   9198   9454    495    412    487       C  
ATOM   7520  O   ASN B 237      23.134 -10.335 -27.805  1.00 71.22           O  
ANISOU 7520  O   ASN B 237     9383   8716   8961    485    419    494       O  
ATOM   7521  CB  ASN B 237      22.047 -12.354 -30.067  1.00 79.69           C  
ANISOU 7521  CB  ASN B 237    10544   9734   9998    516    406    494       C  
ATOM   7522  CG  ASN B 237      22.468 -13.491 -29.153  1.00 83.15           C  
ANISOU 7522  CG  ASN B 237    10956  10190  10445    511    411    504       C  
ATOM   7523  OD1 ASN B 237      21.661 -14.023 -28.387  1.00 84.87           O  
ANISOU 7523  OD1 ASN B 237    11157  10422  10668    501    390    498       O  
ATOM   7524  ND2 ASN B 237      23.734 -13.879 -29.238  1.00 85.08           N  
ANISOU 7524  ND2 ASN B 237    11197  10434  10693    518    439    522       N  
ATOM   7525  N   SER B 238      22.817  -9.207 -29.747  1.00 76.88           N  
ANISOU 7525  N   SER B 238    10159   9391   9659    503    424    486       N  
ATOM   7526  CA  SER B 238      23.846  -8.179 -29.524  1.00 80.61           C  
ANISOU 7526  CA  SER B 238    10614   9870  10142    499    446    492       C  
ATOM   7527  C   SER B 238      23.365  -6.784 -29.947  1.00 85.54           C  
ANISOU 7527  C   SER B 238    11249  10486  10764    498    441    480       C  
ATOM   7528  O   SER B 238      22.405  -6.654 -30.717  1.00 86.94           O  
ANISOU 7528  O   SER B 238    11458  10646  10929    506    425    470       O  
ATOM   7529  CB  SER B 238      25.124  -8.526 -30.293  1.00 78.07           C  
ANISOU 7529  CB  SER B 238    10310   9534   9818    513    478    509       C  
ATOM   7530  OG  SER B 238      24.940  -8.348 -31.689  1.00 72.51           O  
ANISOU 7530  OG  SER B 238     9653   8799   9098    530    483    508       O  
ATOM   7531  N   SER B 239      24.046  -5.750 -29.453  1.00 86.80           N  
ANISOU 7531  N   SER B 239    11385  10656  10937    489    455    480       N  
ATOM   7532  CA  SER B 239      23.683  -4.361 -29.758  1.00 85.98           C  
ANISOU 7532  CA  SER B 239    11289  10545  10833    487    453    470       C  
ATOM   7533  C   SER B 239      23.785  -4.039 -31.251  1.00 86.92           C  
ANISOU 7533  C   SER B 239    11455  10632  10938    506    466    473       C  
ATOM   7534  O   SER B 239      22.930  -3.335 -31.794  1.00 88.54           O  
ANISOU 7534  O   SER B 239    11681  10825  11135    510    453    462       O  
ATOM   7535  CB  SER B 239      24.526  -3.378 -28.936  1.00 83.21           C  
ANISOU 7535  CB  SER B 239    10903  10212  10501    472    469    471       C  
ATOM   7536  OG  SER B 239      25.900  -3.463 -29.274  1.00 78.24           O  
ANISOU 7536  OG  SER B 239    10273   9577   9875    479    501    486       O  
ATOM   7537  N   ASN B 240      24.826  -4.562 -31.901  1.00 90.06           N  
ANISOU 7537  N   ASN B 240    11868  11016  11332    518    492    488       N  
ATOM   7538  CA  ASN B 240      25.047  -4.357 -33.337  1.00 91.01           C  
ANISOU 7538  CA  ASN B 240    12034  11105  11438    538    507    493       C  
ATOM   7539  C   ASN B 240      23.912  -4.887 -34.205  1.00 88.67           C  
ANISOU 7539  C   ASN B 240    11777  10791  11121    551    485    485       C  
ATOM   7540  O   ASN B 240      23.491  -4.223 -35.157  1.00 88.83           O  
ANISOU 7540  O   ASN B 240    11830  10791  11130    562    484    480       O  
ATOM   7541  CB  ASN B 240      26.383  -4.966 -33.786  1.00 93.92           C  
ANISOU 7541  CB  ASN B 240    12411  11465  11808    549    539    512       C  
ATOM   7542  CG  ASN B 240      27.465  -3.920 -34.000  1.00 96.56           C  
ANISOU 7542  CG  ASN B 240    12740  11794  12152    549    569    519       C  
ATOM   7543  OD1 ASN B 240      27.595  -2.969 -33.225  1.00 93.38           O  
ANISOU 7543  OD1 ASN B 240    12306  11407  11764    534    570    513       O  
ATOM   7544  ND2 ASN B 240      28.254  -4.095 -35.057  1.00 95.86           N  
ANISOU 7544  ND2 ASN B 240    12682  11682  12056    567    595    532       N  
ATOM   7545  N   ILE B 241      23.425  -6.080 -33.869  1.00 83.67           N  
ANISOU 7545  N   ILE B 241    11140  10165  10484    549    468    484       N  
ATOM   7546  CA  ILE B 241      22.307  -6.690 -34.583  1.00 81.05           C  
ANISOU 7546  CA  ILE B 241    10841   9818  10135    558    444    476       C  
ATOM   7547  C   ILE B 241      21.014  -5.908 -34.345  1.00 74.75           C  
ANISOU 7547  C   ILE B 241    10038   9026   9335    551    415    458       C  
ATOM   7548  O   ILE B 241      20.224  -5.728 -35.271  1.00 73.43           O  
ANISOU 7548  O   ILE B 241     9905   8840   9152    562    402    450       O  
ATOM   7549  CB  ILE B 241      22.169  -8.201 -34.255  1.00 84.39           C  
ANISOU 7549  CB  ILE B 241    11260  10248  10556    557    435    479       C  
ATOM   7550  CG1 ILE B 241      23.013  -9.027 -35.240  1.00 85.29           C  
ANISOU 7550  CG1 ILE B 241    11406  10340  10659    575    459    494       C  
ATOM   7551  CG2 ILE B 241      20.715  -8.659 -34.301  1.00 83.37           C  
ANISOU 7551  CG2 ILE B 241    11142  10118  10418    555    401    465       C  
ATOM   7552  CD1 ILE B 241      23.392 -10.415 -34.753  1.00 81.52           C  
ANISOU 7552  CD1 ILE B 241    10916   9871  10186    574    463    503       C  
ATOM   7553  N   MET B 242      20.821  -5.425 -33.118  1.00 71.37           N  
ANISOU 7553  N   MET B 242     9569   8623   8924    532    406    452       N  
ATOM   7554  CA  MET B 242      19.629  -4.642 -32.772  1.00 70.93           C  
ANISOU 7554  CA  MET B 242     9505   8575   8869    523    380    435       C  
ATOM   7555  C   MET B 242      19.572  -3.323 -33.533  1.00 68.63           C  
ANISOU 7555  C   MET B 242     9234   8267   8572    531    387    432       C  
ATOM   7556  O   MET B 242      18.548  -3.006 -34.140  1.00 63.37           O  
ANISOU 7556  O   MET B 242     8592   7589   7894    538    368    421       O  
ATOM   7557  CB  MET B 242      19.537  -4.385 -31.260  1.00 73.23           C  
ANISOU 7557  CB  MET B 242     9746   8896   9179    502    371    431       C  
ATOM   7558  CG  MET B 242      18.187  -3.836 -30.807  1.00 72.45           C  
ANISOU 7558  CG  MET B 242     9638   8806   9081    493    341    414       C  
ATOM   7559  SD  MET B 242      18.044  -3.627 -29.021  1.00 77.94           S  
ANISOU 7559  SD  MET B 242    10277   9538   9798    468    331    408       S  
ATOM   7560  CE  MET B 242      16.323  -3.161 -28.829  1.00 71.99           C  
ANISOU 7560  CE  MET B 242     9523   8787   9041    463    296    389       C  
ATOM   7561  N   LYS B 243      20.672  -2.567 -33.496  1.00 69.97           N  
ANISOU 7561  N   LYS B 243     9396   8436   8751    530    415    440       N  
ATOM   7562  CA  LYS B 243      20.766  -1.288 -34.204  1.00 72.26           C  
ANISOU 7562  CA  LYS B 243     9706   8711   9039    538    427    438       C  
ATOM   7563  C   LYS B 243      20.532  -1.470 -35.700  1.00 70.53           C  
ANISOU 7563  C   LYS B 243     9538   8461   8797    561    429    440       C  
ATOM   7564  O   LYS B 243      19.792  -0.699 -36.322  1.00 67.05           O  
ANISOU 7564  O   LYS B 243     9120   8009   8347    568    419    432       O  
ATOM   7565  CB  LYS B 243      22.128  -0.619 -33.975  1.00 73.90           C  
ANISOU 7565  CB  LYS B 243     9896   8921   9260    533    461    448       C  
ATOM   7566  CG  LYS B 243      22.105   0.881 -34.256  1.00 80.88           C  
ANISOU 7566  CG  LYS B 243    10785   9795  10147    534    470    443       C  
ATOM   7567  CD  LYS B 243      23.321   1.366 -35.041  1.00 83.39           C  
ANISOU 7567  CD  LYS B 243    11121  10095  10466    545    506    455       C  
ATOM   7568  CE  LYS B 243      23.118   2.797 -35.532  1.00 79.70           C  
ANISOU 7568  CE  LYS B 243    10668   9613   9998    549    514    450       C  
ATOM   7569  NZ  LYS B 243      24.022   3.171 -36.653  1.00 74.82           N  
ANISOU 7569  NZ  LYS B 243    10083   8971   9375    566    546    462       N  
ATOM   7570  N   THR B 244      21.165  -2.501 -36.259  1.00 71.47           N  
ANISOU 7570  N   THR B 244     9676   8570   8909    572    442    452       N  
ATOM   7571  CA  THR B 244      21.081  -2.790 -37.683  1.00 73.07           C  
ANISOU 7571  CA  THR B 244     9928   8744   9089    594    447    455       C  
ATOM   7572  C   THR B 244      19.641  -3.093 -38.094  1.00 70.80           C  
ANISOU 7572  C   THR B 244     9662   8451   8785    599    412    442       C  
ATOM   7573  O   THR B 244      19.148  -2.557 -39.088  1.00 72.26           O  
ANISOU 7573  O   THR B 244     9882   8617   8955    613    408    438       O  
ATOM   7574  CB  THR B 244      22.078  -3.901 -38.112  1.00 75.50           C  
ANISOU 7574  CB  THR B 244    10250   9043   9393    604    469    470       C  
ATOM   7575  OG1 THR B 244      22.724  -3.515 -39.328  1.00 80.52           O  
ANISOU 7575  OG1 THR B 244    10924   9652  10017    623    494    479       O  
ATOM   7576  CG2 THR B 244      21.400  -5.276 -38.299  1.00 76.75           C  
ANISOU 7576  CG2 THR B 244    10423   9199   9539    608    447    467       C  
ATOM   7577  N   CYS B 245      18.968  -3.924 -37.303  1.00 69.95           N  
ANISOU 7577  N   CYS B 245     9533   8361   8683    587    388    435       N  
ATOM   7578  CA  CYS B 245      17.596  -4.331 -37.590  1.00 75.02           C  
ANISOU 7578  CA  CYS B 245    10191   8999   9312    589    354    422       C  
ATOM   7579  C   CYS B 245      16.591  -3.184 -37.495  1.00 72.19           C  
ANISOU 7579  C   CYS B 245     9829   8645   8954    586    335    409       C  
ATOM   7580  O   CYS B 245      15.741  -3.031 -38.377  1.00 69.18           O  
ANISOU 7580  O   CYS B 245     9480   8249   8556    598    318    401       O  
ATOM   7581  CB  CYS B 245      17.179  -5.477 -36.672  1.00 80.72           C  
ANISOU 7581  CB  CYS B 245    10887   9740  10042    576    336    419       C  
ATOM   7582  SG  CYS B 245      17.955  -7.059 -37.078  1.00 88.12           S  
ANISOU 7582  SG  CYS B 245    11841  10667  10971    585    351    432       S  
ATOM   7583  N   LEU B 246      16.701  -2.384 -36.433  1.00 70.43           N  
ANISOU 7583  N   LEU B 246     9567   8441   8750    570    337    406       N  
ATOM   7584  CA  LEU B 246      15.798  -1.249 -36.210  1.00 72.19           C  
ANISOU 7584  CA  LEU B 246     9782   8668   8975    565    321    394       C  
ATOM   7585  C   LEU B 246      15.866  -0.221 -37.337  1.00 74.10           C  
ANISOU 7585  C   LEU B 246    10060   8888   9205    582    332    395       C  
ATOM   7586  O   LEU B 246      14.862   0.435 -37.635  1.00 72.64           O  
ANISOU 7586  O   LEU B 246     9886   8699   9013    586    313    385       O  
ATOM   7587  CB  LEU B 246      16.054  -0.573 -34.854  1.00 70.13           C  
ANISOU 7587  CB  LEU B 246     9475   8433   8737    544    325    391       C  
ATOM   7588  CG  LEU B 246      15.818  -1.349 -33.547  1.00 69.39           C  
ANISOU 7588  CG  LEU B 246     9341   8365   8657    525    310    388       C  
ATOM   7589  CD1 LEU B 246      16.065  -0.440 -32.354  1.00 69.50           C  
ANISOU 7589  CD1 LEU B 246     9314   8400   8691    507    316    385       C  
ATOM   7590  CD2 LEU B 246      14.434  -1.979 -33.461  1.00 65.87           C  
ANISOU 7590  CD2 LEU B 246     8898   7923   8205    524    275    376       C  
ATOM   7591  N   GLN B 247      17.046  -0.089 -37.950  1.00 72.82           N  
ANISOU 7591  N   GLN B 247     9915   8712   9041    592    364    408       N  
ATOM   7592  CA  GLN B 247      17.227   0.744 -39.138  1.00 72.58           C  
ANISOU 7592  CA  GLN B 247     9923   8657   8997    611    379    412       C  
ATOM   7593  C   GLN B 247      16.305   0.277 -40.255  1.00 73.22           C  
ANISOU 7593  C   GLN B 247    10045   8721   9053    629    358    406       C  
ATOM   7594  O   GLN B 247      15.597   1.081 -40.863  1.00 70.16           O  
ANISOU 7594  O   GLN B 247     9679   8323   8656    639    348    400       O  
ATOM   7595  CB  GLN B 247      18.676   0.698 -39.617  1.00 74.92           C  
ANISOU 7595  CB  GLN B 247    10230   8941   9295    619    417    427       C  
ATOM   7596  CG  GLN B 247      19.600   1.678 -38.916  1.00 78.73           C  
ANISOU 7596  CG  GLN B 247    10682   9432   9798    607    443    432       C  
ATOM   7597  CD  GLN B 247      21.068   1.409 -39.203  1.00 80.33           C  
ANISOU 7597  CD  GLN B 247    10889   9627  10005    612    479    448       C  
ATOM   7598  OE1 GLN B 247      21.870   1.256 -38.282  1.00 83.50           O  
ANISOU 7598  OE1 GLN B 247    11255  10045  10425    597    492    453       O  
ATOM   7599  NE2 GLN B 247      21.426   1.344 -40.482  1.00 79.66           N  
ANISOU 7599  NE2 GLN B 247    10847   9515   9903    633    495    457       N  
ATOM   7600  N   ASN B 248      16.306  -1.034 -40.494  1.00 76.85           N  
ANISOU 7600  N   ASN B 248    10517   9178   9505    632    351    409       N  
ATOM   7601  CA  ASN B 248      15.487  -1.651 -41.536  1.00 74.68           C  
ANISOU 7601  CA  ASN B 248    10281   8886   9205    648    330    403       C  
ATOM   7602  C   ASN B 248      14.019  -1.824 -41.138  1.00 73.97           C  
ANISOU 7602  C   ASN B 248    10180   8808   9114    640    290    387       C  
ATOM   7603  O   ASN B 248      13.290  -2.610 -41.746  1.00 75.25           O  
ANISOU 7603  O   ASN B 248    10367   8963   9260    648    269    382       O  
ATOM   7604  CB  ASN B 248      16.105  -2.978 -41.991  1.00 76.78           C  
ANISOU 7604  CB  ASN B 248    10566   9143   9463    655    341    412       C  
ATOM   7605  CG  ASN B 248      17.317  -2.782 -42.889  1.00 79.97           C  
ANISOU 7605  CG  ASN B 248    10999   9527   9859    672    377    427       C  
ATOM   7606  OD1 ASN B 248      17.361  -3.302 -44.003  1.00 81.43           O  
ANISOU 7606  OD1 ASN B 248    11225   9690  10023    690    380    430       O  
ATOM   7607  ND2 ASN B 248      18.306  -2.026 -42.411  1.00 78.00           N  
ANISOU 7607  ND2 ASN B 248    10727   9282   9627    665    405    436       N  
ATOM   7608  N   LEU B 249      13.600  -1.089 -40.110  1.00 74.14           N  
ANISOU 7608  N   LEU B 249    10165   8850   9153    624    281    381       N  
ATOM   7609  CA  LEU B 249      12.186  -0.899 -39.801  1.00 71.87           C  
ANISOU 7609  CA  LEU B 249     9869   8573   8866    618    245    366       C  
ATOM   7610  C   LEU B 249      11.659   0.372 -40.462  1.00 72.04           C  
ANISOU 7610  C   LEU B 249     9911   8583   8878    631    242    361       C  
ATOM   7611  O   LEU B 249      10.484   0.711 -40.313  1.00 73.49           O  
ANISOU 7611  O   LEU B 249    10088   8772   9059    628    214    350       O  
ATOM   7612  CB  LEU B 249      11.958  -0.841 -38.291  1.00 71.78           C  
ANISOU 7612  CB  LEU B 249     9807   8589   8878    595    236    360       C  
ATOM   7613  CG  LEU B 249      11.176  -1.995 -37.659  1.00 72.73           C  
ANISOU 7613  CG  LEU B 249     9909   8723   9001    583    209    353       C  
ATOM   7614  CD1 LEU B 249      11.901  -3.326 -37.786  1.00 72.54           C  
ANISOU 7614  CD1 LEU B 249     9892   8695   8974    584    220    362       C  
ATOM   7615  CD2 LEU B 249      10.899  -1.681 -36.201  1.00 73.26           C  
ANISOU 7615  CD2 LEU B 249     9927   8815   9090    561    202    347       C  
ATOM   7616  N   ALA B 250      12.537   1.054 -41.201  1.00 71.42           N  
ANISOU 7616  N   ALA B 250     9855   8487   8793    644    271    371       N  
ATOM   7617  CA  ALA B 250      12.217   2.302 -41.899  1.00 70.02           C  
ANISOU 7617  CA  ALA B 250     9700   8297   8607    658    274    370       C  
ATOM   7618  C   ALA B 250      10.895   2.242 -42.656  1.00 67.91           C  
ANISOU 7618  C   ALA B 250     9459   8022   8320    670    241    360       C  
ATOM   7619  O   ALA B 250      10.631   1.284 -43.383  1.00 67.03           O  
ANISOU 7619  O   ALA B 250     9374   7901   8191    681    229    359       O  
ATOM   7620  CB  ALA B 250      13.347   2.683 -42.844  1.00 69.93           C  
ANISOU 7620  CB  ALA B 250     9719   8263   8586    674    309    383       C  
ATOM   7621  N   GLY B 251      10.067   3.263 -42.457  1.00 67.21           N  
ANISOU 7621  N   GLY B 251     9362   7939   8235    669    227    352       N  
ATOM   7622  CA  GLY B 251       8.805   3.402 -43.177  1.00 68.70           C  
ANISOU 7622  CA  GLY B 251     9574   8121   8405    683    197    343       C  
ATOM   7623  C   GLY B 251       7.609   2.706 -42.557  1.00 70.91           C  
ANISOU 7623  C   GLY B 251     9833   8419   8690    670    159    329       C  
ATOM   7624  O   GLY B 251       6.620   2.456 -43.240  1.00 74.17           O  
ANISOU 7624  O   GLY B 251    10268   8825   9086    681    132    322       O  
ATOM   7625  N   LEU B 252       7.689   2.401 -41.264  1.00 72.46           N  
ANISOU 7625  N   LEU B 252     9986   8635   8908    648    157    327       N  
ATOM   7626  CA  LEU B 252       6.602   1.721 -40.556  1.00 73.79           C  
ANISOU 7626  CA  LEU B 252    10131   8822   9084    634    124    315       C  
ATOM   7627  C   LEU B 252       5.777   2.684 -39.710  1.00 75.24           C  
ANISOU 7627  C   LEU B 252    10284   9021   9282    623    110    307       C  
ATOM   7628  O   LEU B 252       6.330   3.448 -38.914  1.00 77.25           O  
ANISOU 7628  O   LEU B 252    10513   9284   9554    612    129    310       O  
ATOM   7629  CB  LEU B 252       7.166   0.605 -39.665  1.00 74.71           C  
ANISOU 7629  CB  LEU B 252    10220   8952   9214    617    129    318       C  
ATOM   7630  CG  LEU B 252       6.317   0.070 -38.501  1.00 74.20           C  
ANISOU 7630  CG  LEU B 252    10117   8909   9165    597    104    308       C  
ATOM   7631  CD1 LEU B 252       5.330  -0.995 -38.962  1.00 72.42           C  
ANISOU 7631  CD1 LEU B 252     9906   8681   8927    600     73    299       C  
ATOM   7632  CD2 LEU B 252       7.213  -0.466 -37.398  1.00 72.97           C  
ANISOU 7632  CD2 LEU B 252     9927   8769   9028    579    122    314       C  
ATOM   7633  N   HIS B 253       4.457   2.643 -39.879  1.00 77.79           N  
ANISOU 7633  N   HIS B 253    10609   9346   9598    626     76    296       N  
ATOM   7634  CA  HIS B 253       3.558   3.326 -38.950  1.00 83.12           C  
ANISOU 7634  CA  HIS B 253    11252  10039  10289    614     60    287       C  
ATOM   7635  C   HIS B 253       2.981   2.347 -37.961  1.00 78.85           C  
ANISOU 7635  C   HIS B 253    10679   9518   9762    595     38    279       C  
ATOM   7636  O   HIS B 253       2.213   1.453 -38.329  1.00 83.44           O  
ANISOU 7636  O   HIS B 253    11271  10098  10334    598     13    273       O  
ATOM   7637  CB  HIS B 253       2.447   4.096 -39.675  1.00 92.69           C  
ANISOU 7637  CB  HIS B 253    12484  11244  11489    629     38    280       C  
ATOM   7638  CG  HIS B 253       1.539   4.887 -38.742  1.00103.20           C  
ANISOU 7638  CG  HIS B 253    13782  12592  12837    618     23    272       C  
ATOM   7639  ND1 HIS B 253       1.674   6.214 -38.549  1.00105.06           N  
ANISOU 7639  ND1 HIS B 253    14011  12826  13079    620     38    274       N  
ATOM   7640  CD2 HIS B 253       0.472   4.481 -37.931  1.00104.41           C  
ANISOU 7640  CD2 HIS B 253    13906  12762  13001    604     -5    261       C  
ATOM   7641  CE1 HIS B 253       0.742   6.639 -37.670  1.00103.78           C  
ANISOU 7641  CE1 HIS B 253    13819  12680  12931    608     20    265       C  
ATOM   7642  NE2 HIS B 253       0.009   5.578 -37.292  1.00104.02           N  
ANISOU 7642  NE2 HIS B 253    13834  12722  12964    599     -5    258       N  
ATOM   7643  N   VAL B 254       3.363   2.503 -36.697  1.00 70.65           N  
ANISOU 7643  N   VAL B 254     9601   8497   8745    576     49    280       N  
ATOM   7644  CA  VAL B 254       2.787   1.713 -35.612  1.00 64.44           C  
ANISOU 7644  CA  VAL B 254     8780   7730   7974    557     30    273       C  
ATOM   7645  C   VAL B 254       2.147   2.593 -34.565  1.00 59.40           C  
ANISOU 7645  C   VAL B 254     8106   7109   7352    544     23    266       C  
ATOM   7646  O   VAL B 254       2.684   3.647 -34.204  1.00 55.93           O  
ANISOU 7646  O   VAL B 254     7656   6670   6921    541     43    269       O  
ATOM   7647  CB  VAL B 254       3.810   0.796 -34.903  1.00 64.02           C  
ANISOU 7647  CB  VAL B 254     8707   7685   7930    543     49    280       C  
ATOM   7648  CG1 VAL B 254       3.826  -0.581 -35.544  1.00 64.68           C  
ANISOU 7648  CG1 VAL B 254     8813   7760   8001    549     40    281       C  
ATOM   7649  CG2 VAL B 254       5.199   1.427 -34.863  1.00 62.97           C  
ANISOU 7649  CG2 VAL B 254     8575   7548   7801    544     85    291       C  
ATOM   7650  N   HIS B 255       0.996   2.143 -34.082  1.00 55.96           N  
ANISOU 7650  N   HIS B 255     7653   6685   6922    536     -6    256       N  
ATOM   7651  CA  HIS B 255       0.331   2.793 -32.973  1.00 56.79           C  
ANISOU 7651  CA  HIS B 255     7723   6808   7046    522    -15    249       C  
ATOM   7652  C   HIS B 255       1.074   2.515 -31.694  1.00 58.56           C  
ANISOU 7652  C   HIS B 255     7910   7049   7287    502      1    253       C  
ATOM   7653  O   HIS B 255       1.303   3.419 -30.889  1.00 59.96           O  
ANISOU 7653  O   HIS B 255     8064   7237   7478    492     13    252       O  
ATOM   7654  CB  HIS B 255      -1.119   2.337 -32.873  1.00 56.15           C  
ANISOU 7654  CB  HIS B 255     7634   6734   6966    519    -50    238       C  
ATOM   7655  CG  HIS B 255      -1.915   3.082 -31.835  1.00 56.58           C  
ANISOU 7655  CG  HIS B 255     7654   6804   7036    507    -60    231       C  
ATOM   7656  ND1 HIS B 255      -2.368   2.496 -30.715  1.00 59.82           N  
ANISOU 7656  ND1 HIS B 255     8030   7234   7463    490    -72    226       N  
ATOM   7657  CD2 HIS B 255      -2.314   4.410 -31.772  1.00 56.86           C  
ANISOU 7657  CD2 HIS B 255     7687   6840   7076    512    -59    229       C  
ATOM   7658  CE1 HIS B 255      -3.033   3.399 -29.975  1.00 59.31           C  
ANISOU 7658  CE1 HIS B 255     7942   7180   7411    483    -78    221       C  
ATOM   7659  NE2 HIS B 255      -2.997   4.571 -30.623  1.00 59.38           N  
ANISOU 7659  NE2 HIS B 255     7969   7177   7412    496    -70    222       N  
ATOM   7660  N   ARG B 256       1.477   1.262 -31.508  1.00 57.41           N  
ANISOU 7660  N   ARG B 256     7761   6907   7143    496      1    256       N  
ATOM   7661  CA  ARG B 256       2.119   0.837 -30.278  1.00 55.17           C  
ANISOU 7661  CA  ARG B 256     7444   6642   6876    477     14    260       C  
ATOM   7662  C   ARG B 256       3.334  -0.036 -30.602  1.00 54.35           C  
ANISOU 7662  C   ARG B 256     7352   6531   6766    480     35    271       C  
ATOM   7663  O   ARG B 256       3.207  -1.072 -31.251  1.00 55.09           O  
ANISOU 7663  O   ARG B 256     7466   6615   6849    487     26    271       O  
ATOM   7664  CB  ARG B 256       1.101   0.090 -29.404  1.00 55.92           C  
ANISOU 7664  CB  ARG B 256     7510   6753   6981    464    -10    251       C  
ATOM   7665  CG  ARG B 256       1.455  -0.004 -27.925  1.00 57.01           C  
ANISOU 7665  CG  ARG B 256     7608   6914   7139    444     -1    253       C  
ATOM   7666  CD  ARG B 256       0.299  -0.543 -27.081  1.00 56.39           C  
ANISOU 7666  CD  ARG B 256     7502   6851   7071    432    -27    244       C  
ATOM   7667  NE  ARG B 256      -0.820   0.397 -27.025  1.00 56.79           N  
ANISOU 7667  NE  ARG B 256     7548   6904   7126    433    -44    234       N  
ATOM   7668  CZ  ARG B 256      -2.038   0.164 -27.507  1.00 57.46           C  
ANISOU 7668  CZ  ARG B 256     7642   6983   7205    439    -72    226       C  
ATOM   7669  NH1 ARG B 256      -2.331  -1.005 -28.070  1.00 57.49           N  
ANISOU 7669  NH1 ARG B 256     7662   6980   7201    443    -86    225       N  
ATOM   7670  NH2 ARG B 256      -2.970   1.105 -27.413  1.00 55.58           N  
ANISOU 7670  NH2 ARG B 256     7398   6748   6971    441    -85    219       N  
ATOM   7671  N   LEU B 257       4.512   0.403 -30.170  1.00 51.75           N  
ANISOU 7671  N   LEU B 257     7011   6206   6445    475     63    279       N  
ATOM   7672  CA  LEU B 257       5.731  -0.387 -30.304  1.00 51.81           C  
ANISOU 7672  CA  LEU B 257     7025   6210   6450    476     85    290       C  
ATOM   7673  C   LEU B 257       6.280  -0.803 -28.927  1.00 53.30           C  
ANISOU 7673  C   LEU B 257     7173   6421   6656    457     94    293       C  
ATOM   7674  O   LEU B 257       6.721   0.039 -28.133  1.00 52.96           O  
ANISOU 7674  O   LEU B 257     7106   6391   6625    447    107    294       O  
ATOM   7675  CB  LEU B 257       6.780   0.378 -31.118  1.00 50.93           C  
ANISOU 7675  CB  LEU B 257     6937   6082   6330    488    112    299       C  
ATOM   7676  CG  LEU B 257       8.217  -0.156 -31.172  1.00 51.53           C  
ANISOU 7676  CG  LEU B 257     7016   6156   6407    488    141    312       C  
ATOM   7677  CD1 LEU B 257       8.283  -1.498 -31.888  1.00 52.95           C  
ANISOU 7677  CD1 LEU B 257     7219   6323   6573    497    136    316       C  
ATOM   7678  CD2 LEU B 257       9.146   0.861 -31.825  1.00 50.57           C  
ANISOU 7678  CD2 LEU B 257     6912   6019   6281    498    168    319       C  
ATOM   7679  N   ILE B 258       6.235  -2.106 -28.657  1.00 52.38           N  
ANISOU 7679  N   ILE B 258     7051   6311   6540    452     87    296       N  
ATOM   7680  CA  ILE B 258       6.738  -2.669 -27.402  1.00 50.76           C  
ANISOU 7680  CA  ILE B 258     6810   6127   6350    436     94    300       C  
ATOM   7681  C   ILE B 258       8.152  -3.230 -27.607  1.00 51.28           C  
ANISOU 7681  C   ILE B 258     6882   6188   6413    440    121    314       C  
ATOM   7682  O   ILE B 258       8.373  -4.098 -28.462  1.00 50.63           O  
ANISOU 7682  O   ILE B 258     6826   6090   6318    451    123    319       O  
ATOM   7683  CB  ILE B 258       5.790  -3.757 -26.840  1.00 49.81           C  
ANISOU 7683  CB  ILE B 258     6674   6016   6233    428     70    294       C  
ATOM   7684  CG1 ILE B 258       4.400  -3.184 -26.552  1.00 49.37           C  
ANISOU 7684  CG1 ILE B 258     6609   5967   6183    423     44    281       C  
ATOM   7685  CG2 ILE B 258       6.355  -4.368 -25.565  1.00 50.11           C  
ANISOU 7685  CG2 ILE B 258     6676   6076   6285    413     80    300       C  
ATOM   7686  CD1 ILE B 258       3.387  -3.394 -27.656  1.00 50.08           C  
ANISOU 7686  CD1 ILE B 258     6729   6038   6258    436     22    273       C  
ATOM   7687  N   LEU B 259       9.100  -2.732 -26.816  1.00 49.39           N  
ANISOU 7687  N   LEU B 259     6617   5962   6185    430    142    319       N  
ATOM   7688  CA  LEU B 259      10.506  -3.064 -26.992  1.00 49.61           C  
ANISOU 7688  CA  LEU B 259     6649   5987   6212    434    170    333       C  
ATOM   7689  C   LEU B 259      11.161  -3.423 -25.674  1.00 50.36           C  
ANISOU 7689  C   LEU B 259     6704   6106   6322    418    179    338       C  
ATOM   7690  O   LEU B 259      10.744  -2.939 -24.626  1.00 50.03           O  
ANISOU 7690  O   LEU B 259     6632   6084   6292    404    171    331       O  
ATOM   7691  CB  LEU B 259      11.228  -1.866 -27.575  1.00 51.39           C  
ANISOU 7691  CB  LEU B 259     6888   6201   6435    441    191    336       C  
ATOM   7692  CG  LEU B 259      12.186  -2.122 -28.722  1.00 55.10           C  
ANISOU 7692  CG  LEU B 259     7391   6649   6893    457    212    347       C  
ATOM   7693  CD1 LEU B 259      11.414  -2.598 -29.948  1.00 56.41           C  
ANISOU 7693  CD1 LEU B 259     7597   6794   7042    473    196    344       C  
ATOM   7694  CD2 LEU B 259      12.927  -0.829 -29.018  1.00 56.61           C  
ANISOU 7694  CD2 LEU B 259     7587   6833   7086    460    235    350       C  
ATOM   7695  N   GLY B 260      12.198  -4.258 -25.736  1.00 51.32           N  
ANISOU 7695  N   GLY B 260     6827   6227   6442    421    197    351       N  
ATOM   7696  CA  GLY B 260      12.943  -4.684 -24.551  1.00 49.90           C  
ANISOU 7696  CA  GLY B 260     6612   6071   6276    408    208    358       C  
ATOM   7697  C   GLY B 260      13.275  -6.168 -24.538  1.00 51.59           C  
ANISOU 7697  C   GLY B 260     6828   6285   6487    412    211    368       C  
ATOM   7698  O   GLY B 260      13.101  -6.865 -25.542  1.00 51.66           O  
ANISOU 7698  O   GLY B 260     6869   6274   6483    424    208    370       O  
ATOM   7699  N   GLU B 261      13.758  -6.650 -23.396  1.00 51.91           N  
ANISOU 7699  N   GLU B 261     6836   6349   6539    400    216    374       N  
ATOM   7700  CA  GLU B 261      14.075  -8.068 -23.229  1.00 54.47           C  
ANISOU 7700  CA  GLU B 261     7157   6675   6862    402    220    384       C  
ATOM   7701  C   GLU B 261      13.631  -8.603 -21.865  1.00 55.33           C  
ANISOU 7701  C   GLU B 261     7230   6809   6982    388    207    382       C  
ATOM   7702  O   GLU B 261      12.989  -7.883 -21.098  1.00 58.84           O  
ANISOU 7702  O   GLU B 261     7653   7269   7434    377    195    372       O  
ATOM   7703  CB  GLU B 261      15.564  -8.327 -23.474  1.00 57.82           C  
ANISOU 7703  CB  GLU B 261     7584   7097   7285    409    249    400       C  
ATOM   7704  CG  GLU B 261      16.522  -7.488 -22.640  1.00 58.53           C  
ANISOU 7704  CG  GLU B 261     7643   7207   7388    399    266    404       C  
ATOM   7705  CD  GLU B 261      17.950  -7.556 -23.156  1.00 61.99           C  
ANISOU 7705  CD  GLU B 261     8089   7637   7824    408    295    419       C  
ATOM   7706  OE1 GLU B 261      18.765  -6.693 -22.754  1.00 65.67           O  
ANISOU 7706  OE1 GLU B 261     8538   8115   8300    401    310    421       O  
ATOM   7707  OE2 GLU B 261      18.264  -8.467 -23.960  1.00 60.04           O  
ANISOU 7707  OE2 GLU B 261     7868   7373   7569    421    303    428       O  
ATOM   7708  N   PHE B 262      13.967  -9.863 -21.579  1.00 52.08           N  
ANISOU 7708  N   PHE B 262     6813   6402   6571    389    212    392       N  
ATOM   7709  CA  PHE B 262      13.550 -10.540 -20.348  1.00 50.04           C  
ANISOU 7709  CA  PHE B 262     6523   6167   6322    378    201    392       C  
ATOM   7710  C   PHE B 262      14.723 -10.868 -19.415  1.00 51.04           C  
ANISOU 7710  C   PHE B 262     6620   6314   6456    373    221    405       C  
ATOM   7711  O   PHE B 262      15.852 -11.053 -19.874  1.00 53.25           O  
ANISOU 7711  O   PHE B 262     6909   6588   6733    381    242    418       O  
ATOM   7712  CB  PHE B 262      12.839 -11.845 -20.688  1.00 48.21           C  
ANISOU 7712  CB  PHE B 262     6307   5923   6084    383    189    392       C  
ATOM   7713  CG  PHE B 262      11.622 -11.686 -21.545  1.00 46.75           C  
ANISOU 7713  CG  PHE B 262     6150   5720   5893    387    167    378       C  
ATOM   7714  CD1 PHE B 262      11.694 -11.882 -22.914  1.00 46.19           C  
ANISOU 7714  CD1 PHE B 262     6118   5621   5808    402    170    379       C  
ATOM   7715  CD2 PHE B 262      10.391 -11.381 -20.978  1.00 47.02           C  
ANISOU 7715  CD2 PHE B 262     6169   5762   5932    377    144    365       C  
ATOM   7716  CE1 PHE B 262      10.563 -11.753 -23.707  1.00 46.98           C  
ANISOU 7716  CE1 PHE B 262     6243   5705   5900    406    149    366       C  
ATOM   7717  CE2 PHE B 262       9.251 -11.263 -21.765  1.00 47.12           C  
ANISOU 7717  CE2 PHE B 262     6206   5758   5938    382    123    353       C  
ATOM   7718  CZ  PHE B 262       9.336 -11.449 -23.134  1.00 46.08           C  
ANISOU 7718  CZ  PHE B 262     6114   5601   5793    396    125    353       C  
ATOM   7719  N   LYS B 263      14.446 -10.972 -18.113  1.00 51.45           N  
ANISOU 7719  N   LYS B 263     6638   6392   6519    360    213    404       N  
ATOM   7720  CA  LYS B 263      15.455 -11.369 -17.113  1.00 53.10           C  
ANISOU 7720  CA  LYS B 263     6816   6624   6734    355    228    416       C  
ATOM   7721  C   LYS B 263      15.972 -12.797 -17.309  1.00 53.47           C  
ANISOU 7721  C   LYS B 263     6871   6666   6778    364    239    431       C  
ATOM   7722  O   LYS B 263      17.183 -13.046 -17.245  1.00 52.06           O  
ANISOU 7722  O   LYS B 263     6686   6493   6600    368    260    445       O  
ATOM   7723  CB  LYS B 263      14.902 -11.241 -15.695  1.00 52.93           C  
ANISOU 7723  CB  LYS B 263     6758   6630   6722    340    215    410       C  
ATOM   7724  CG  LYS B 263      14.866  -9.829 -15.167  1.00 54.89           C  
ANISOU 7724  CG  LYS B 263     6987   6891   6975    329    213    400       C  
ATOM   7725  CD  LYS B 263      14.812  -9.858 -13.655  1.00 55.71           C  
ANISOU 7725  CD  LYS B 263     7051   7026   7088    316    208    399       C  
ATOM   7726  CE  LYS B 263      14.963  -8.465 -13.080  1.00 54.65           C  
ANISOU 7726  CE  LYS B 263     6897   6906   6959    304    209    390       C  
ATOM   7727  NZ  LYS B 263      15.180  -8.542 -11.614  1.00 53.78           N  
ANISOU 7727  NZ  LYS B 263     6748   6827   6856    292    208    392       N  
ATOM   7728  N   ASP B 264      15.041 -13.723 -17.536  1.00 53.57           N  
ANISOU 7728  N   ASP B 264     6897   6667   6787    367    224    428       N  
ATOM   7729  CA  ASP B 264      15.360 -15.128 -17.772  1.00 56.05           C  
ANISOU 7729  CA  ASP B 264     7222   6974   7098    376    233    440       C  
ATOM   7730  C   ASP B 264      15.813 -15.406 -19.220  1.00 61.11           C  
ANISOU 7730  C   ASP B 264     7904   7586   7729    391    245    445       C  
ATOM   7731  O   ASP B 264      15.562 -16.481 -19.768  1.00 61.47           O  
ANISOU 7731  O   ASP B 264     7971   7616   7769    399    244    449       O  
ATOM   7732  CB  ASP B 264      14.168 -16.007 -17.382  1.00 52.72           C  
ANISOU 7732  CB  ASP B 264     6799   6553   6679    371    213    434       C  
ATOM   7733  CG  ASP B 264      12.916 -15.699 -18.187  1.00 53.90           C  
ANISOU 7733  CG  ASP B 264     6973   6682   6823    372    191    418       C  
ATOM   7734  OD1 ASP B 264      12.088 -16.621 -18.360  1.00 53.95           O  
ANISOU 7734  OD1 ASP B 264     6991   6679   6828    373    179    414       O  
ATOM   7735  OD2 ASP B 264      12.748 -14.542 -18.642  1.00 52.95           O  
ANISOU 7735  OD2 ASP B 264     6862   6557   6700    371    187    408       O  
ATOM   7736  N   GLU B 265      16.471 -14.423 -19.830  1.00 65.78           N  
ANISOU 7736  N   GLU B 265     8505   8169   8316    395    257    446       N  
ATOM   7737  CA  GLU B 265      17.100 -14.584 -21.135  1.00 70.17           C  
ANISOU 7737  CA  GLU B 265     9098   8700   8863    410    272    452       C  
ATOM   7738  C   GLU B 265      18.475 -13.934 -21.132  1.00 78.00           C  
ANISOU 7738  C   GLU B 265    10079   9698   9857    413    297    463       C  
ATOM   7739  O   GLU B 265      18.709 -12.980 -20.385  1.00 83.42           O  
ANISOU 7739  O   GLU B 265    10739  10404  10552    402    298    460       O  
ATOM   7740  CB  GLU B 265      16.231 -13.987 -22.240  1.00 67.90           C  
ANISOU 7740  CB  GLU B 265     8843   8389   8564    416    258    438       C  
ATOM   7741  CG  GLU B 265      15.316 -14.996 -22.919  1.00 72.38           C  
ANISOU 7741  CG  GLU B 265     9438   8937   9123    422    243    433       C  
ATOM   7742  CD  GLU B 265      16.056 -16.000 -23.803  1.00 77.71           C  
ANISOU 7742  CD  GLU B 265    10142   9593   9790    437    261    446       C  
ATOM   7743  OE1 GLU B 265      15.513 -17.112 -24.015  1.00 80.42           O  
ANISOU 7743  OE1 GLU B 265    10499   9926  10130    439    253    445       O  
ATOM   7744  OE2 GLU B 265      17.172 -15.691 -24.292  1.00 74.78           O  
ANISOU 7744  OE2 GLU B 265     9780   9215   9416    445    284    457       O  
ATOM   7745  N   ARG B 266      19.387 -14.463 -21.949  1.00 85.77           N  
ANISOU 7745  N   ARG B 266    11085  10666  10835    426    318    476       N  
ATOM   7746  CA  ARG B 266      20.710 -13.853 -22.124  1.00 88.18           C  
ANISOU 7746  CA  ARG B 266    11386  10974  11143    430    343    487       C  
ATOM   7747  C   ARG B 266      20.567 -12.516 -22.858  1.00 84.17           C  
ANISOU 7747  C   ARG B 266    10895  10453  10632    431    342    477       C  
ATOM   7748  O   ARG B 266      19.905 -12.430 -23.899  1.00 80.66           O  
ANISOU 7748  O   ARG B 266    10485   9984  10177    440    334    469       O  
ATOM   7749  CB  ARG B 266      21.703 -14.809 -22.815  1.00 94.20           C  
ANISOU 7749  CB  ARG B 266    12167  11721  11900    445    367    504       C  
ATOM   7750  CG  ARG B 266      21.222 -15.463 -24.106  1.00 99.84           C  
ANISOU 7750  CG  ARG B 266    12928  12405  12601    459    364    502       C  
ATOM   7751  CD  ARG B 266      22.180 -16.569 -24.535  1.00102.96           C  
ANISOU 7751  CD  ARG B 266    13336  12790  12993    472    387    521       C  
ATOM   7752  NE  ARG B 266      22.114 -16.858 -25.971  1.00105.20           N  
ANISOU 7752  NE  ARG B 266    13666  13040  13262    488    393    520       N  
ATOM   7753  CZ  ARG B 266      22.902 -16.306 -26.896  1.00101.26           C  
ANISOU 7753  CZ  ARG B 266    13190  12526  12758    499    412    526       C  
ATOM   7754  NH1 ARG B 266      23.828 -15.414 -26.555  1.00 98.92           N  
ANISOU 7754  NH1 ARG B 266    12871  12242  12470    495    429    532       N  
ATOM   7755  NH2 ARG B 266      22.759 -16.642 -28.171  1.00 94.14           N  
ANISOU 7755  NH2 ARG B 266    12331  11594  11842    513    416    525       N  
ATOM   7756  N   ASN B 267      21.179 -11.479 -22.291  1.00 79.00           N  
ANISOU 7756  N   ASN B 267    10214   9814   9986    422    351    476       N  
ATOM   7757  CA  ASN B 267      20.854 -10.099 -22.648  1.00 78.47           C  
ANISOU 7757  CA  ASN B 267    10154   9740   9918    419    346    464       C  
ATOM   7758  C   ASN B 267      21.965  -9.283 -23.315  1.00 79.26           C  
ANISOU 7758  C   ASN B 267    10265   9831  10019    425    372    471       C  
ATOM   7759  O   ASN B 267      23.147  -9.609 -23.206  1.00 79.32           O  
ANISOU 7759  O   ASN B 267    10262   9843  10031    428    394    485       O  
ATOM   7760  CB  ASN B 267      20.353  -9.352 -21.403  1.00 75.06           C  
ANISOU 7760  CB  ASN B 267     9686   9335   9497    401    331    453       C  
ATOM   7761  CG  ASN B 267      19.089  -9.958 -20.815  1.00 73.66           C  
ANISOU 7761  CG  ASN B 267     9502   9166   9320    394    305    443       C  
ATOM   7762  OD1 ASN B 267      18.883  -9.921 -19.603  1.00 71.01           O  
ANISOU 7762  OD1 ASN B 267     9132   8855   8993    381    296    441       O  
ATOM   7763  ND2 ASN B 267      18.238 -10.523 -21.669  1.00 74.09           N  
ANISOU 7763  ND2 ASN B 267     9588   9199   9364    404    292    439       N  
ATOM   7764  N   LEU B 268      21.555  -8.211 -23.992  1.00 80.51           N  
ANISOU 7764  N   LEU B 268    10442   9973  10173    427    368    460       N  
ATOM   7765  CA  LEU B 268      22.459  -7.228 -24.589  1.00 83.66           C  
ANISOU 7765  CA  LEU B 268    10851  10363  10574    431    390    464       C  
ATOM   7766  C   LEU B 268      23.318  -6.547 -23.524  1.00 80.13           C  
ANISOU 7766  C   LEU B 268    10361   9940  10141    417    402    466       C  
ATOM   7767  O   LEU B 268      22.798  -5.876 -22.628  1.00 79.07           O  
ANISOU 7767  O   LEU B 268    10202   9824  10014    402    388    455       O  
ATOM   7768  CB  LEU B 268      21.655  -6.160 -25.342  1.00 88.55           C  
ANISOU 7768  CB  LEU B 268    11495  10964  11187    434    380    450       C  
ATOM   7769  CG  LEU B 268      20.397  -6.578 -26.110  1.00 92.81           C  
ANISOU 7769  CG  LEU B 268    12066  11484  11711    443    358    441       C  
ATOM   7770  CD1 LEU B 268      19.373  -5.453 -26.113  1.00 92.85           C  
ANISOU 7770  CD1 LEU B 268    12074  11488  11716    438    340    425       C  
ATOM   7771  CD2 LEU B 268      20.728  -7.024 -27.527  1.00 97.30           C  
ANISOU 7771  CD2 LEU B 268    12679  12024  12266    463    371    449       C  
ATOM   7772  N   GLU B 269      24.632  -6.717 -23.641  1.00 81.75           N  
ANISOU 7772  N   GLU B 269    10561  10146  10351    421    428    481       N  
ATOM   7773  CA  GLU B 269      25.582  -6.213 -22.652  1.00 85.35           C  
ANISOU 7773  CA  GLU B 269    10977  10627  10822    408    441    485       C  
ATOM   7774  C   GLU B 269      25.613  -4.687 -22.596  1.00 85.74           C  
ANISOU 7774  C   GLU B 269    11020  10678  10878    399    444    474       C  
ATOM   7775  O   GLU B 269      25.234  -4.101 -21.584  1.00 85.56           O  
ANISOU 7775  O   GLU B 269    10969  10676  10864    383    431    463       O  
ATOM   7776  CB  GLU B 269      26.986  -6.785 -22.902  1.00 88.83           C  
ANISOU 7776  CB  GLU B 269    11415  11067  11266    417    468    504       C  
ATOM   7777  CG  GLU B 269      27.159  -8.252 -22.519  1.00 91.74           C  
ANISOU 7777  CG  GLU B 269    11777  11446  11633    422    467    517       C  
ATOM   7778  CD  GLU B 269      27.478  -8.460 -21.045  1.00 95.18           C  
ANISOU 7778  CD  GLU B 269    12166  11917  12081    408    462    519       C  
ATOM   7779  OE1 GLU B 269      26.583  -8.260 -20.191  1.00 91.68           O  
ANISOU 7779  OE1 GLU B 269    11704  11490  11639    395    440    507       O  
ATOM   7780  OE2 GLU B 269      28.628  -8.843 -20.739  1.00 99.11           O  
ANISOU 7780  OE2 GLU B 269    12644  12427  12585    409    481    534       O  
ATOM   7781  N   ILE B 270      26.053  -4.056 -23.685  1.00 90.49           N  
ANISOU 7781  N   ILE B 270    11649  11254  11476    409    462    476       N  
ATOM   7782  CA  ILE B 270      26.133  -2.592 -23.775  1.00 92.41           C  
ANISOU 7782  CA  ILE B 270    11890  11494  11726    402    468    466       C  
ATOM   7783  C   ILE B 270      24.855  -2.042 -24.414  1.00 94.36           C  
ANISOU 7783  C   ILE B 270    12165  11722  11962    406    450    452       C  
ATOM   7784  O   ILE B 270      24.485  -2.445 -25.523  1.00 92.84           O  
ANISOU 7784  O   ILE B 270    12012  11505  11756    423    449    455       O  
ATOM   7785  CB  ILE B 270      27.372  -2.114 -24.584  1.00 92.28           C  
ANISOU 7785  CB  ILE B 270    11887  11462  11713    410    500    477       C  
ATOM   7786  CG1 ILE B 270      28.583  -3.036 -24.354  1.00 93.64           C  
ANISOU 7786  CG1 ILE B 270    12043  11645  11891    413    519    495       C  
ATOM   7787  CG2 ILE B 270      27.718  -0.670 -24.233  1.00 88.44           C  
ANISOU 7787  CG2 ILE B 270    11382  10982  11239    397    509    469       C  
ATOM   7788  CD1 ILE B 270      29.584  -3.058 -25.496  1.00 92.67           C  
ANISOU 7788  CD1 ILE B 270    11946  11498  11766    429    548    509       C  
ATOM   7789  N   PHE B 271      24.184  -1.130 -23.709  1.00 93.90           N  
ANISOU 7789  N   PHE B 271    12090  11677  11911    392    435    438       N  
ATOM   7790  CA  PHE B 271      22.937  -0.539 -24.200  1.00 94.90           C  
ANISOU 7790  CA  PHE B 271    12239  11788  12028    396    417    424       C  
ATOM   7791  C   PHE B 271      22.972   0.999 -24.241  1.00 95.19           C  
ANISOU 7791  C   PHE B 271    12274  11821  12072    389    424    414       C  
ATOM   7792  O   PHE B 271      22.540   1.676 -23.300  1.00 91.48           O  
ANISOU 7792  O   PHE B 271    11778  11369  11611    373    413    403       O  
ATOM   7793  CB  PHE B 271      21.740  -1.052 -23.390  1.00 92.80           C  
ANISOU 7793  CB  PHE B 271    11959  11539  11761    387    386    414       C  
ATOM   7794  CG  PHE B 271      20.408  -0.769 -24.026  1.00 93.79           C  
ANISOU 7794  CG  PHE B 271    12111  11647  11876    394    366    402       C  
ATOM   7795  CD1 PHE B 271      19.662   0.343 -23.650  1.00 95.04           C  
ANISOU 7795  CD1 PHE B 271    12261  11809  12038    385    354    388       C  
ATOM   7796  CD2 PHE B 271      19.897  -1.616 -25.002  1.00 96.43           C  
ANISOU 7796  CD2 PHE B 271    12481  11962  12196    410    357    406       C  
ATOM   7797  CE1 PHE B 271      18.433   0.604 -24.237  1.00 97.16           C  
ANISOU 7797  CE1 PHE B 271    12554  12063  12297    392    335    378       C  
ATOM   7798  CE2 PHE B 271      18.667  -1.361 -25.592  1.00 97.60           C  
ANISOU 7798  CE2 PHE B 271    12653  12096  12334    417    337    395       C  
ATOM   7799  CZ  PHE B 271      17.935  -0.250 -25.209  1.00 95.76           C  
ANISOU 7799  CZ  PHE B 271    12410  11867  12105    408    326    381       C  
ATOM   7800  N   GLU B 272      23.489   1.532 -25.349  1.00 96.08           N  
ANISOU 7800  N   GLU B 272    12415  11909  12180    401    445    419       N  
ATOM   7801  CA  GLU B 272      23.561   2.979 -25.585  1.00 95.53           C  
ANISOU 7801  CA  GLU B 272    12350  11829  12116    397    456    412       C  
ATOM   7802  C   GLU B 272      22.253   3.483 -26.217  1.00 90.76           C  
ANISOU 7802  C   GLU B 272    11775  11209  11501    405    437    400       C  
ATOM   7803  O   GLU B 272      21.474   2.685 -26.746  1.00 94.05           O  
ANISOU 7803  O   GLU B 272    12214  11616  11904    417    420    400       O  
ATOM   7804  CB  GLU B 272      24.763   3.325 -26.487  1.00 97.54           C  
ANISOU 7804  CB  GLU B 272    12622  12065  12372    408    488    423       C  
ATOM   7805  CG  GLU B 272      26.123   2.803 -26.019  1.00 98.45           C  
ANISOU 7805  CG  GLU B 272    12712  12195  12498    402    509    437       C  
ATOM   7806  CD  GLU B 272      26.806   3.699 -24.991  1.00 98.26           C  
ANISOU 7806  CD  GLU B 272    12648  12192  12493    382    519    431       C  
ATOM   7807  OE1 GLU B 272      26.386   3.710 -23.812  1.00 95.81           O  
ANISOU 7807  OE1 GLU B 272    12306  11907  12189    366    501    422       O  
ATOM   7808  OE2 GLU B 272      27.786   4.380 -25.358  1.00 94.39           O  
ANISOU 7808  OE2 GLU B 272    12159  11693  12011    382    545    437       O  
ATOM   7809  N   PRO B 273      21.995   4.803 -26.151  1.00 86.75           N  
ANISOU 7809  N   PRO B 273    11264  10697  10998    399    439    390       N  
ATOM   7810  CA  PRO B 273      20.817   5.357 -26.823  1.00 85.73           C  
ANISOU 7810  CA  PRO B 273    11164  10550  10859    409    424    380       C  
ATOM   7811  C   PRO B 273      20.894   5.254 -28.341  1.00 84.78           C  
ANISOU 7811  C   PRO B 273    11090  10399  10723    432    434    388       C  
ATOM   7812  O   PRO B 273      19.859   5.187 -28.998  1.00 84.98           O  
ANISOU 7812  O   PRO B 273    11142  10411  10735    443    416    383       O  
ATOM   7813  CB  PRO B 273      20.833   6.830 -26.401  1.00 84.38           C  
ANISOU 7813  CB  PRO B 273    10978  10382  10699    397    432    370       C  
ATOM   7814  CG  PRO B 273      21.556   6.835 -25.099  1.00 85.79           C  
ANISOU 7814  CG  PRO B 273    11112  10588  10894    376    438    369       C  
ATOM   7815  CD  PRO B 273      22.631   5.801 -25.270  1.00 90.65           C  
ANISOU 7815  CD  PRO B 273    11727  11207  11510    381    453    385       C  
ATOM   7816  N   SER B 274      22.112   5.231 -28.882  1.00 85.71           N  
ANISOU 7816  N   SER B 274    11216  10505  10842    438    463    401       N  
ATOM   7817  CA  SER B 274      22.349   5.194 -30.331  1.00 80.42           C  
ANISOU 7817  CA  SER B 274    10590   9805  10158    460    478    410       C  
ATOM   7818  C   SER B 274      21.866   3.906 -31.007  1.00 82.19           C  
ANISOU 7818  C   SER B 274    10841  10020  10365    475    463    415       C  
ATOM   7819  O   SER B 274      21.812   3.825 -32.232  1.00 84.36           O  
ANISOU 7819  O   SER B 274    11156  10270  10626    495    469    420       O  
ATOM   7820  CB  SER B 274      23.832   5.410 -30.625  1.00 76.79           C  
ANISOU 7820  CB  SER B 274    10130   9339   9708    462    513    422       C  
ATOM   7821  OG  SER B 274      24.598   4.341 -30.106  1.00 75.73           O  
ANISOU 7821  OG  SER B 274     9974   9220   9579    457    518    432       O  
ATOM   7822  N   ILE B 275      21.522   2.901 -30.208  1.00 83.86           N  
ANISOU 7822  N   ILE B 275    11030  10251  10578    467    444    413       N  
ATOM   7823  CA  ILE B 275      20.950   1.662 -30.730  1.00 82.50           C  
ANISOU 7823  CA  ILE B 275    10881  10073  10392    479    427    416       C  
ATOM   7824  C   ILE B 275      19.504   1.914 -31.192  1.00 83.47           C  
ANISOU 7824  C   ILE B 275    11026  10185  10502    485    400    404       C  
ATOM   7825  O   ILE B 275      18.943   1.158 -31.990  1.00 87.67           O  
ANISOU 7825  O   ILE B 275    11588  10703  11017    499    387    404       O  
ATOM   7826  CB  ILE B 275      21.088   0.516 -29.695  1.00 83.51           C  
ANISOU 7826  CB  ILE B 275    10977  10224  10526    467    418    419       C  
ATOM   7827  CG1 ILE B 275      22.507  -0.075 -29.735  1.00 86.20           C  
ANISOU 7827  CG1 ILE B 275    11312  10566  10873    470    445    435       C  
ATOM   7828  CG2 ILE B 275      20.095  -0.609 -29.951  1.00 83.21           C  
ANISOU 7828  CG2 ILE B 275    10955  10183  10475    474    392    416       C  
ATOM   7829  CD1 ILE B 275      23.581   0.755 -29.056  1.00 85.89           C  
ANISOU 7829  CD1 ILE B 275    11242  10541  10851    457    468    439       C  
ATOM   7830  N   MET B 276      18.938   3.018 -30.716  1.00 80.59           N  
ANISOU 7830  N   MET B 276    10648   9827  10144    476    392    392       N  
ATOM   7831  CA  MET B 276      17.584   3.436 -31.045  1.00 79.87           C  
ANISOU 7831  CA  MET B 276    10573   9729  10043    481    367    380       C  
ATOM   7832  C   MET B 276      17.517   4.203 -32.371  1.00 79.96           C  
ANISOU 7832  C   MET B 276    10625   9712  10041    500    377    382       C  
ATOM   7833  O   MET B 276      16.425   4.457 -32.884  1.00 75.53           O  
ANISOU 7833  O   MET B 276    10085   9142   9470    509    357    374       O  
ATOM   7834  CB  MET B 276      17.074   4.344 -29.928  1.00 86.17           C  
ANISOU 7834  CB  MET B 276    11337  10547  10856    463    357    368       C  
ATOM   7835  CG  MET B 276      15.690   4.022 -29.391  1.00 94.04           C  
ANISOU 7835  CG  MET B 276    12323  11555  11850    457    323    356       C  
ATOM   7836  SD  MET B 276      15.737   3.018 -27.893  1.00 92.88           S  
ANISOU 7836  SD  MET B 276    12131  11440  11717    437    311    356       S  
ATOM   7837  CE  MET B 276      16.027   1.386 -28.578  1.00 89.46           C  
ANISOU 7837  CE  MET B 276    11720  10998  11271    450    310    367       C  
ATOM   7838  N   GLU B 277      18.685   4.556 -32.916  1.00 82.11           N  
ANISOU 7838  N   GLU B 277    10909   9971  10315    507    409    393       N  
ATOM   7839  CA  GLU B 277      18.819   5.492 -34.051  1.00 79.13           C  
ANISOU 7839  CA  GLU B 277    10567   9568   9929    523    425    395       C  
ATOM   7840  C   GLU B 277      17.891   5.244 -35.234  1.00 76.49           C  
ANISOU 7840  C   GLU B 277    10276   9213   9572    544    408    393       C  
ATOM   7841  O   GLU B 277      17.386   6.190 -35.837  1.00 76.62           O  
ANISOU 7841  O   GLU B 277    10313   9215   9581    553    407    389       O  
ATOM   7842  CB  GLU B 277      20.273   5.566 -34.545  1.00 82.85           C  
ANISOU 7842  CB  GLU B 277    11047  10027  10404    529    462    410       C  
ATOM   7843  CG  GLU B 277      21.161   6.560 -33.797  1.00 85.13           C  
ANISOU 7843  CG  GLU B 277    11305  10326  10714    513    485    410       C  
ATOM   7844  CD  GLU B 277      20.884   8.012 -34.158  1.00 87.91           C  
ANISOU 7844  CD  GLU B 277    11668  10664  11066    516    493    404       C  
ATOM   7845  OE1 GLU B 277      20.760   8.323 -35.364  1.00 88.35           O  
ANISOU 7845  OE1 GLU B 277    11765  10694  11108    536    501    408       O  
ATOM   7846  OE2 GLU B 277      20.801   8.850 -33.233  1.00 85.51           O  
ANISOU 7846  OE2 GLU B 277    11335  10375  10779    499    493    395       O  
ATOM   7847  N   GLY B 278      17.671   3.976 -35.564  1.00 75.28           N  
ANISOU 7847  N   GLY B 278    10137   9059   9408    551    395    396       N  
ATOM   7848  CA  GLY B 278      16.809   3.617 -36.684  1.00 76.27           C  
ANISOU 7848  CA  GLY B 278    10302   9165   9510    570    378    394       C  
ATOM   7849  C   GLY B 278      15.376   4.083 -36.510  1.00 75.58           C  
ANISOU 7849  C   GLY B 278    10213   9083   9419    568    346    379       C  
ATOM   7850  O   GLY B 278      14.691   4.391 -37.485  1.00 76.23           O  
ANISOU 7850  O   GLY B 278    10330   9148   9485    584    336    376       O  
ATOM   7851  N   LEU B 279      14.939   4.157 -35.256  1.00 76.65           N  
ANISOU 7851  N   LEU B 279    10309   9242   9570    548    331    371       N  
ATOM   7852  CA  LEU B 279      13.542   4.419 -34.919  1.00 74.87           C  
ANISOU 7852  CA  LEU B 279    10076   9026   9344    544    300    357       C  
ATOM   7853  C   LEU B 279      12.935   5.708 -35.467  1.00 74.09           C  
ANISOU 7853  C   LEU B 279     9995   8914   9240    553    298    352       C  
ATOM   7854  O   LEU B 279      11.758   5.720 -35.824  1.00 71.66           O  
ANISOU 7854  O   LEU B 279     9701   8603   8921    561    272    343       O  
ATOM   7855  CB  LEU B 279      13.324   4.316 -33.408  1.00 73.11           C  
ANISOU 7855  CB  LEU B 279     9805   8831   9140    520    289    350       C  
ATOM   7856  CG  LEU B 279      12.430   3.167 -32.922  1.00 73.99           C  
ANISOU 7856  CG  LEU B 279     9905   8956   9251    514    259    344       C  
ATOM   7857  CD1 LEU B 279      12.457   1.951 -33.842  1.00 72.93           C  
ANISOU 7857  CD1 LEU B 279     9802   8808   9100    528    254    350       C  
ATOM   7858  CD2 LEU B 279      12.793   2.781 -31.497  1.00 71.32           C  
ANISOU 7858  CD2 LEU B 279     9521   8644   8930    492    260    344       C  
ATOM   7859  N   CYS B 280      13.720   6.781 -35.550  1.00 75.86           N  
ANISOU 7859  N   CYS B 280    10220   9131   9472    554    325    356       N  
ATOM   7860  CA  CYS B 280      13.168   8.057 -36.033  1.00 80.56           C  
ANISOU 7860  CA  CYS B 280    10831   9714  10063    563    326    352       C  
ATOM   7861  C   CYS B 280      13.007   8.135 -37.559  1.00 78.73           C  
ANISOU 7861  C   CYS B 280    10650   9455   9808    589    328    357       C  
ATOM   7862  O   CYS B 280      12.835   9.218 -38.121  1.00 79.41           O  
ANISOU 7862  O   CYS B 280    10754   9527   9889    600    337    357       O  
ATOM   7863  CB  CYS B 280      13.902   9.280 -35.454  1.00 81.89           C  
ANISOU 7863  CB  CYS B 280    10979   9886  10249    552    352    352       C  
ATOM   7864  SG  CYS B 280      15.695   9.152 -35.311  1.00 84.89           S  
ANISOU 7864  SG  CYS B 280    11348  10263  10640    545    391    365       S  
ATOM   7865  N   ASP B 281      13.054   6.975 -38.210  1.00 75.99           N  
ANISOU 7865  N   ASP B 281    10324   9101   9446    600    321    361       N  
ATOM   7866  CA  ASP B 281      12.634   6.836 -39.599  1.00 72.42           C  
ANISOU 7866  CA  ASP B 281     9920   8627   8970    624    315    364       C  
ATOM   7867  C   ASP B 281      11.340   6.013 -39.641  1.00 71.40           C  
ANISOU 7867  C   ASP B 281     9793   8504   8829    625    275    354       C  
ATOM   7868  O   ASP B 281      10.844   5.655 -40.710  1.00 71.49           O  
ANISOU 7868  O   ASP B 281     9841   8500   8819    644    263    353       O  
ATOM   7869  CB  ASP B 281      13.743   6.195 -40.445  1.00 73.65           C  
ANISOU 7869  CB  ASP B 281    10103   8766   9115    637    340    377       C  
ATOM   7870  CG  ASP B 281      14.987   7.080 -40.562  1.00 74.84           C  
ANISOU 7870  CG  ASP B 281    10253   8906   9275    638    379    387       C  
ATOM   7871  OD1 ASP B 281      16.110   6.556 -40.395  1.00 73.96           O  
ANISOU 7871  OD1 ASP B 281    10134   8795   9171    633    402    397       O  
ATOM   7872  OD2 ASP B 281      14.848   8.297 -40.823  1.00 75.13           O  
ANISOU 7872  OD2 ASP B 281    10298   8933   9312    643    388    386       O  
ATOM   7873  N   VAL B 282      10.810   5.706 -38.458  1.00 70.20           N  
ANISOU 7873  N   VAL B 282     9603   8375   8692    606    256    345       N  
ATOM   7874  CA  VAL B 282       9.483   5.101 -38.325  1.00 67.49           C  
ANISOU 7874  CA  VAL B 282     9257   8041   8344    604    219    334       C  
ATOM   7875  C   VAL B 282       8.629   6.042 -37.474  1.00 63.55           C  
ANISOU 7875  C   VAL B 282     8730   7557   7858    592    204    324       C  
ATOM   7876  O   VAL B 282       9.151   6.768 -36.625  1.00 62.80           O  
ANISOU 7876  O   VAL B 282     8607   7472   7781    579    221    325       O  
ATOM   7877  CB  VAL B 282       9.518   3.639 -37.768  1.00 69.22           C  
ANISOU 7877  CB  VAL B 282     9459   8273   8567    592    206    334       C  
ATOM   7878  CG1 VAL B 282      10.906   3.025 -37.889  1.00 70.38           C  
ANISOU 7878  CG1 VAL B 282     9610   8415   8714    593    236    346       C  
ATOM   7879  CG2 VAL B 282       9.058   3.549 -36.323  1.00 69.48           C  
ANISOU 7879  CG2 VAL B 282     9446   8333   8620    569    192    326       C  
ATOM   7880  N   THR B 283       7.325   6.058 -37.726  1.00 61.98           N  
ANISOU 7880  N   THR B 283     8539   7359   7651    598    173    315       N  
ATOM   7881  CA  THR B 283       6.426   6.919 -36.961  1.00 62.23           C  
ANISOU 7881  CA  THR B 283     8545   7403   7694    589    159    305       C  
ATOM   7882  C   THR B 283       5.669   6.112 -35.910  1.00 59.84           C  
ANISOU 7882  C   THR B 283     8208   7123   7403    571    133    296       C  
ATOM   7883  O   THR B 283       5.036   5.101 -36.222  1.00 59.53           O  
ANISOU 7883  O   THR B 283     8179   7084   7354    574    109    292       O  
ATOM   7884  CB  THR B 283       5.459   7.720 -37.862  1.00 62.26           C  
ANISOU 7884  CB  THR B 283     8576   7394   7683    607    144    301       C  
ATOM   7885  OG1 THR B 283       4.878   6.853 -38.841  1.00 65.10           O  
ANISOU 7885  OG1 THR B 283     8966   7743   8022    622    122    299       O  
ATOM   7886  CG2 THR B 283       6.202   8.843 -38.570  1.00 62.57           C  
ANISOU 7886  CG2 THR B 283     8639   7414   7718    621    174    309       C  
ATOM   7887  N   ILE B 284       5.766   6.567 -34.664  1.00 56.23           N  
ANISOU 7887  N   ILE B 284     7713   6684   6967    552    138    293       N  
ATOM   7888  CA  ILE B 284       5.234   5.849 -33.511  1.00 55.28           C  
ANISOU 7888  CA  ILE B 284     7556   6586   6859    533    118    286       C  
ATOM   7889  C   ILE B 284       4.245   6.729 -32.739  1.00 56.30           C  
ANISOU 7889  C   ILE B 284     7661   6728   7001    524    103    276       C  
ATOM   7890  O   ILE B 284       4.556   7.878 -32.407  1.00 59.43           O  
ANISOU 7890  O   ILE B 284     8048   7125   7406    520    120    276       O  
ATOM   7891  CB  ILE B 284       6.379   5.425 -32.563  1.00 53.33           C  
ANISOU 7891  CB  ILE B 284     7282   6353   6628    516    140    292       C  
ATOM   7892  CG1 ILE B 284       7.447   4.615 -33.315  1.00 52.32           C  
ANISOU 7892  CG1 ILE B 284     7177   6212   6489    525    158    303       C  
ATOM   7893  CG2 ILE B 284       5.832   4.631 -31.389  1.00 52.30           C  
ANISOU 7893  CG2 ILE B 284     7115   6245   6509    497    121    285       C  
ATOM   7894  CD1 ILE B 284       8.849   4.726 -32.749  1.00 50.10           C  
ANISOU 7894  CD1 ILE B 284     6878   5937   6221    515    190    312       C  
ATOM   7895  N   ASP B 285       3.057   6.197 -32.458  1.00 54.23           N  
ANISOU 7895  N   ASP B 285     7389   6476   6739    520     72    267       N  
ATOM   7896  CA  ASP B 285       2.110   6.895 -31.590  1.00 53.54           C  
ANISOU 7896  CA  ASP B 285     7274   6402   6664    510     58    257       C  
ATOM   7897  C   ASP B 285       2.478   6.661 -30.123  1.00 53.71           C  
ANISOU 7897  C   ASP B 285     7254   6447   6707    487     64    256       C  
ATOM   7898  O   ASP B 285       2.708   7.612 -29.375  1.00 54.59           O  
ANISOU 7898  O   ASP B 285     7343   6565   6830    477     77    254       O  
ATOM   7899  CB  ASP B 285       0.662   6.464 -31.868  1.00 55.21           C  
ANISOU 7899  CB  ASP B 285     7490   6615   6869    516     22    249       C  
ATOM   7900  CG  ASP B 285       0.244   6.662 -33.331  1.00 55.51           C  
ANISOU 7900  CG  ASP B 285     7571   6632   6886    540     13    250       C  
ATOM   7901  OD1 ASP B 285       1.043   7.175 -34.137  1.00 56.92           O  
ANISOU 7901  OD1 ASP B 285     7776   6794   7055    553     35    258       O  
ATOM   7902  OD2 ASP B 285      -0.896   6.297 -33.680  1.00 55.37           O  
ANISOU 7902  OD2 ASP B 285     7560   6615   6862    546    -15    243       O  
ATOM   7903  N   GLU B 286       2.550   5.389 -29.726  1.00 53.51           N  
ANISOU 7903  N   GLU B 286     7216   6431   6683    478     55    257       N  
ATOM   7904  CA  GLU B 286       2.858   4.999 -28.347  1.00 51.00           C  
ANISOU 7904  CA  GLU B 286     6859   6135   6382    457     59    256       C  
ATOM   7905  C   GLU B 286       4.088   4.085 -28.318  1.00 49.45           C  
ANISOU 7905  C   GLU B 286     6663   5939   6185    454     78    266       C  
ATOM   7906  O   GLU B 286       4.226   3.203 -29.161  1.00 50.04           O  
ANISOU 7906  O   GLU B 286     6762   6002   6247    465     75    270       O  
ATOM   7907  CB  GLU B 286       1.646   4.314 -27.697  1.00 51.08           C  
ANISOU 7907  CB  GLU B 286     6849   6160   6399    448     30    247       C  
ATOM   7908  CG  GLU B 286       0.313   4.982 -28.024  1.00 52.79           C  
ANISOU 7908  CG  GLU B 286     7072   6372   6612    456      7    238       C  
ATOM   7909  CD  GLU B 286      -0.904   4.321 -27.387  1.00 56.90           C  
ANISOU 7909  CD  GLU B 286     7571   6906   7140    447    -21    230       C  
ATOM   7910  OE1 GLU B 286      -1.980   4.961 -27.395  1.00 60.41           O  
ANISOU 7910  OE1 GLU B 286     8013   7351   7586    450    -38    222       O  
ATOM   7911  OE2 GLU B 286      -0.812   3.177 -26.886  1.00 56.91           O  
ANISOU 7911  OE2 GLU B 286     7559   6917   7146    438    -26    231       O  
ATOM   7912  N   PHE B 287       4.975   4.309 -27.351  1.00 47.14           N  
ANISOU 7912  N   PHE B 287     6343   5661   5906    440     98    269       N  
ATOM   7913  CA  PHE B 287       6.231   3.578 -27.241  1.00 45.67           C  
ANISOU 7913  CA  PHE B 287     6154   5477   5720    436    118    279       C  
ATOM   7914  C   PHE B 287       6.386   2.964 -25.855  1.00 46.82           C  
ANISOU 7914  C   PHE B 287     6259   5647   5880    417    116    279       C  
ATOM   7915  O   PHE B 287       6.348   3.673 -24.840  1.00 47.49           O  
ANISOU 7915  O   PHE B 287     6315   5747   5978    403    119    274       O  
ATOM   7916  CB  PHE B 287       7.406   4.521 -27.526  1.00 45.53           C  
ANISOU 7916  CB  PHE B 287     6143   5450   5703    439    149    286       C  
ATOM   7917  CG  PHE B 287       8.756   3.851 -27.507  1.00 44.96           C  
ANISOU 7917  CG  PHE B 287     6070   5379   5633    437    172    298       C  
ATOM   7918  CD1 PHE B 287       9.263   3.243 -28.648  1.00 44.65           C  
ANISOU 7918  CD1 PHE B 287     6064   5321   5580    453    180    306       C  
ATOM   7919  CD2 PHE B 287       9.532   3.845 -26.352  1.00 44.59           C  
ANISOU 7919  CD2 PHE B 287     5987   5352   5600    420    185    300       C  
ATOM   7920  CE1 PHE B 287      10.507   2.630 -28.633  1.00 44.01           C  
ANISOU 7920  CE1 PHE B 287     5981   5241   5500    452    202    318       C  
ATOM   7921  CE2 PHE B 287      10.778   3.236 -26.335  1.00 44.33           C  
ANISOU 7921  CE2 PHE B 287     5953   5321   5569    419    206    311       C  
ATOM   7922  CZ  PHE B 287      11.266   2.630 -27.478  1.00 43.36           C  
ANISOU 7922  CZ  PHE B 287     5863   5179   5433    435    215    320       C  
ATOM   7923  N   ARG B 288       6.582   1.647 -25.820  1.00 47.16           N  
ANISOU 7923  N   ARG B 288     6303   5694   5921    416    112    284       N  
ATOM   7924  CA  ARG B 288       6.729   0.916 -24.557  1.00 45.54           C  
ANISOU 7924  CA  ARG B 288     6062   5511   5728    400    110    285       C  
ATOM   7925  C   ARG B 288       8.055   0.178 -24.452  1.00 45.11           C  
ANISOU 7925  C   ARG B 288     6005   5460   5675    398    132    297       C  
ATOM   7926  O   ARG B 288       8.281  -0.823 -25.135  1.00 45.27           O  
ANISOU 7926  O   ARG B 288     6045   5470   5686    408    132    304       O  
ATOM   7927  CB  ARG B 288       5.567  -0.063 -24.358  1.00 44.85           C  
ANISOU 7927  CB  ARG B 288     5971   5429   5641    398     82    279       C  
ATOM   7928  CG  ARG B 288       4.257   0.623 -24.028  1.00 44.32           C  
ANISOU 7928  CG  ARG B 288     5894   5367   5578    394     60    267       C  
ATOM   7929  CD  ARG B 288       3.503  -0.094 -22.925  1.00 44.44           C  
ANISOU 7929  CD  ARG B 288     5879   5402   5604    380     43    262       C  
ATOM   7930  NE  ARG B 288       2.243  -0.662 -23.393  1.00 46.46           N  
ANISOU 7930  NE  ARG B 288     6146   5650   5854    386     15    255       N  
ATOM   7931  CZ  ARG B 288       1.996  -1.959 -23.536  1.00 47.61           C  
ANISOU 7931  CZ  ARG B 288     6296   5794   5997    386      5    257       C  
ATOM   7932  NH1 ARG B 288       2.922  -2.865 -23.252  1.00 48.08           N  
ANISOU 7932  NH1 ARG B 288     6351   5859   6058    383     19    266       N  
ATOM   7933  NH2 ARG B 288       0.806  -2.352 -23.962  1.00 50.01           N  
ANISOU 7933  NH2 ARG B 288     6610   6091   6298    390    -20    249       N  
ATOM   7934  N   LEU B 289       8.939   0.687 -23.604  1.00 46.22           N  
ANISOU 7934  N   LEU B 289     6120   5616   5827    387    150    300       N  
ATOM   7935  CA  LEU B 289      10.175  -0.018 -23.295  1.00 46.71           C  
ANISOU 7935  CA  LEU B 289     6171   5685   5891    384    170    312       C  
ATOM   7936  C   LEU B 289       9.991  -0.828 -22.022  1.00 46.44           C  
ANISOU 7936  C   LEU B 289     6102   5675   5866    369    160    312       C  
ATOM   7937  O   LEU B 289       9.529  -0.318 -21.002  1.00 47.74           O  
ANISOU 7937  O   LEU B 289     6238   5857   6041    356    152    304       O  
ATOM   7938  CB  LEU B 289      11.362   0.937 -23.153  1.00 47.81           C  
ANISOU 7938  CB  LEU B 289     6302   5826   6036    380    197    317       C  
ATOM   7939  CG  LEU B 289      12.716   0.230 -22.980  1.00 51.37           C  
ANISOU 7939  CG  LEU B 289     6744   6282   6489    379    219    330       C  
ATOM   7940  CD1 LEU B 289      13.231  -0.325 -24.301  1.00 52.12           C  
ANISOU 7940  CD1 LEU B 289     6877   6354   6572    396    230    340       C  
ATOM   7941  CD2 LEU B 289      13.755   1.153 -22.363  1.00 53.18           C  
ANISOU 7941  CD2 LEU B 289     6952   6523   6730    368    241    332       C  
ATOM   7942  N   THR B 290      10.342  -2.101 -22.099  1.00 45.11           N  
ANISOU 7942  N   THR B 290     5936   5506   5694    372    162    321       N  
ATOM   7943  CA  THR B 290      10.279  -2.979 -20.953  1.00 44.92           C  
ANISOU 7943  CA  THR B 290     5882   5504   5679    360    156    323       C  
ATOM   7944  C   THR B 290      11.693  -3.265 -20.443  1.00 45.28           C  
ANISOU 7944  C   THR B 290     5911   5563   5730    356    180    335       C  
ATOM   7945  O   THR B 290      12.634  -2.536 -20.770  1.00 45.11           O  
ANISOU 7945  O   THR B 290     5893   5535   5708    359    200    339       O  
ATOM   7946  CB  THR B 290       9.549  -4.285 -21.295  1.00 46.27           C  
ANISOU 7946  CB  THR B 290     6066   5668   5844    366    139    323       C  
ATOM   7947  OG1 THR B 290      10.455  -5.193 -21.938  1.00 47.89           O  
ANISOU 7947  OG1 THR B 290     6289   5862   6042    376    154    336       O  
ATOM   7948  CG2 THR B 290       8.361  -4.005 -22.208  1.00 45.27           C  
ANISOU 7948  CG2 THR B 290     5966   5523   5709    375    118    313       C  
ATOM   7949  N   TYR B 291      11.831  -4.317 -19.641  1.00 46.80           N  
ANISOU 7949  N   TYR B 291     6082   5771   5927    350    177    341       N  
ATOM   7950  CA  TYR B 291      13.098  -4.640 -18.992  1.00 49.16           C  
ANISOU 7950  CA  TYR B 291     6359   6085   6232    345    198    353       C  
ATOM   7951  C   TYR B 291      14.276  -4.679 -19.958  1.00 50.26           C  
ANISOU 7951  C   TYR B 291     6521   6209   6365    357    221    364       C  
ATOM   7952  O   TYR B 291      14.179  -5.229 -21.054  1.00 47.93           O  
ANISOU 7952  O   TYR B 291     6259   5892   6060    371    221    368       O  
ATOM   7953  CB  TYR B 291      13.004  -5.969 -18.229  1.00 49.03           C  
ANISOU 7953  CB  TYR B 291     6325   6084   6218    341    192    359       C  
ATOM   7954  CG  TYR B 291      14.346  -6.472 -17.760  1.00 48.65           C  
ANISOU 7954  CG  TYR B 291     6261   6049   6174    340    213    373       C  
ATOM   7955  CD1 TYR B 291      14.937  -5.967 -16.603  1.00 49.14           C  
ANISOU 7955  CD1 TYR B 291     6288   6137   6246    327    220    374       C  
ATOM   7956  CD2 TYR B 291      15.042  -7.431 -18.491  1.00 50.28           C  
ANISOU 7956  CD2 TYR B 291     6486   6242   6373    352    226    386       C  
ATOM   7957  CE1 TYR B 291      16.177  -6.414 -16.180  1.00 49.89           C  
ANISOU 7957  CE1 TYR B 291     6366   6245   6345    326    239    387       C  
ATOM   7958  CE2 TYR B 291      16.282  -7.885 -18.078  1.00 50.53           C  
ANISOU 7958  CE2 TYR B 291     6502   6287   6410    352    246    401       C  
ATOM   7959  CZ  TYR B 291      16.847  -7.375 -16.925  1.00 50.29           C  
ANISOU 7959  CZ  TYR B 291     6435   6282   6388    339    252    401       C  
ATOM   7960  OH  TYR B 291      18.081  -7.831 -16.522  1.00 51.11           O  
ANISOU 7960  OH  TYR B 291     6523   6399   6497    339    271    415       O  
ATOM   7961  N   THR B 292      15.380  -4.077 -19.525  1.00 56.47           N  
ANISOU 7961  N   THR B 292     7289   7006   7158    351    241    369       N  
ATOM   7962  CA  THR B 292      16.649  -4.111 -20.243  1.00 62.52           C  
ANISOU 7962  CA  THR B 292     8070   7761   7922    360    266    382       C  
ATOM   7963  C   THR B 292      17.784  -4.317 -19.244  1.00 64.39           C  
ANISOU 7963  C   THR B 292     8273   8022   8169    351    282    391       C  
ATOM   7964  O   THR B 292      17.822  -3.669 -18.193  1.00 65.80           O  
ANISOU 7964  O   THR B 292     8420   8223   8357    336    280    385       O  
ATOM   7965  CB  THR B 292      16.891  -2.810 -21.027  1.00 64.75           C  
ANISOU 7965  CB  THR B 292     8370   8027   8203    364    278    377       C  
ATOM   7966  OG1 THR B 292      15.653  -2.349 -21.573  1.00 75.06           O  
ANISOU 7966  OG1 THR B 292     9696   9318   9501    369    258    365       O  
ATOM   7967  CG2 THR B 292      17.869  -3.044 -22.169  1.00 67.62           C  
ANISOU 7967  CG2 THR B 292     8762   8369   8559    379    300    389       C  
ATOM   7968  N   ASN B 293      18.703  -5.220 -19.581  1.00 66.80           N  
ANISOU 7968  N   ASN B 293     8585   8324   8472    359    298    406       N  
ATOM   7969  CA  ASN B 293      19.815  -5.576 -18.701  1.00 69.42           C  
ANISOU 7969  CA  ASN B 293     8885   8678   8812    353    313    417       C  
ATOM   7970  C   ASN B 293      20.749  -4.404 -18.405  1.00 69.81           C  
ANISOU 7970  C   ASN B 293     8917   8737   8870    344    330    416       C  
ATOM   7971  O   ASN B 293      21.130  -4.180 -17.253  1.00 70.01           O  
ANISOU 7971  O   ASN B 293     8906   8788   8904    331    331    416       O  
ATOM   7972  CB  ASN B 293      20.599  -6.754 -19.272  1.00 71.74           C  
ANISOU 7972  CB  ASN B 293     9194   8963   9101    366    328    434       C  
ATOM   7973  CG  ASN B 293      21.445  -7.448 -18.227  1.00 75.99           C  
ANISOU 7973  CG  ASN B 293     9699   9527   9647    360    337    446       C  
ATOM   7974  OD1 ASN B 293      22.653  -7.236 -18.157  1.00 80.46           O  
ANISOU 7974  OD1 ASN B 293    10253  10099  10218    360    358    456       O  
ATOM   7975  ND2 ASN B 293      20.813  -8.276 -17.399  1.00 74.44           N  
ANISOU 7975  ND2 ASN B 293     9485   9346   9451    355    321    445       N  
ATOM   7976  N   ASP B 294      21.120  -3.663 -19.444  1.00 68.83           N  
ANISOU 7976  N   ASP B 294     8818   8590   8742    352    344    416       N  
ATOM   7977  CA  ASP B 294      21.806  -2.396 -19.247  1.00 67.50           C  
ANISOU 7977  CA  ASP B 294     8636   8427   8583    344    359    412       C  
ATOM   7978  C   ASP B 294      20.874  -1.259 -19.643  1.00 64.93           C  
ANISOU 7978  C   ASP B 294     8326   8088   8255    342    348    397       C  
ATOM   7979  O   ASP B 294      20.026  -1.416 -20.518  1.00 65.46           O  
ANISOU 7979  O   ASP B 294     8424   8134   8312    353    337    393       O  
ATOM   7980  CB  ASP B 294      23.111  -2.336 -20.043  1.00 69.22           C  
ANISOU 7980  CB  ASP B 294     8866   8631   8801    353    387    426       C  
ATOM   7981  CG  ASP B 294      24.087  -1.295 -19.495  1.00 73.07           C  
ANISOU 7981  CG  ASP B 294     9328   9133   9302    341    404    424       C  
ATOM   7982  OD1 ASP B 294      24.227  -1.186 -18.252  1.00 69.88           O  
ANISOU 7982  OD1 ASP B 294     8886   8757   8907    325    398    421       O  
ATOM   7983  OD2 ASP B 294      24.722  -0.591 -20.315  1.00 74.83           O  
ANISOU 7983  OD2 ASP B 294     9567   9337   9525    346    423    427       O  
ATOM   7984  N   PHE B 295      21.022  -0.120 -18.978  1.00 64.74           N  
ANISOU 7984  N   PHE B 295     8280   8076   8241    328    351    388       N  
ATOM   7985  CA  PHE B 295      20.173   1.038 -19.235  1.00 61.49           C  
ANISOU 7985  CA  PHE B 295     7881   7654   7829    326    342    373       C  
ATOM   7986  C   PHE B 295      20.915   2.332 -18.937  1.00 60.25           C  
ANISOU 7986  C   PHE B 295     7708   7502   7682    315    360    368       C  
ATOM   7987  O   PHE B 295      21.684   2.403 -17.982  1.00 61.71           O  
ANISOU 7987  O   PHE B 295     7860   7710   7877    302    367    370       O  
ATOM   7988  CB  PHE B 295      18.895   0.966 -18.397  1.00 58.72           C  
ANISOU 7988  CB  PHE B 295     7514   7317   7478    317    315    361       C  
ATOM   7989  CG  PHE B 295      17.872   1.984 -18.782  1.00 56.85           C  
ANISOU 7989  CG  PHE B 295     7294   7066   7239    317    304    347       C  
ATOM   7990  CD1 PHE B 295      17.012   1.750 -19.854  1.00 54.27           C  
ANISOU 7990  CD1 PHE B 295     7002   6716   6901    332    293    346       C  
ATOM   7991  CD2 PHE B 295      17.777   3.191 -18.089  1.00 56.61           C  
ANISOU 7991  CD2 PHE B 295     7244   7046   7217    304    305    336       C  
ATOM   7992  CE1 PHE B 295      16.070   2.702 -20.222  1.00 55.50           C  
ANISOU 7992  CE1 PHE B 295     7173   6859   7054    334    283    334       C  
ATOM   7993  CE2 PHE B 295      16.840   4.147 -18.457  1.00 55.57           C  
ANISOU 7993  CE2 PHE B 295     7128   6902   7084    305    296    324       C  
ATOM   7994  CZ  PHE B 295      15.982   3.901 -19.521  1.00 55.11           C  
ANISOU 7994  CZ  PHE B 295     7104   6820   7014    321    285    323       C  
ATOM   7995  N   SER B 296      20.688   3.346 -19.762  1.00 59.81           N  
ANISOU 7995  N   SER B 296     7676   7424   7624    320    366    362       N  
ATOM   7996  CA  SER B 296      21.275   4.658 -19.538  1.00 62.67           C  
ANISOU 7996  CA  SER B 296     8026   7788   7997    310    382    356       C  
ATOM   7997  C   SER B 296      20.161   5.667 -19.349  1.00 63.33           C  
ANISOU 7997  C   SER B 296     8112   7868   8081    304    367    340       C  
ATOM   7998  O   SER B 296      19.279   5.785 -20.189  1.00 57.38           O  
ANISOU 7998  O   SER B 296     7388   7094   7317    316    358    337       O  
ATOM   7999  CB  SER B 296      22.162   5.068 -20.714  1.00 62.48           C  
ANISOU 7999  CB  SER B 296     8028   7738   7971    322    408    365       C  
ATOM   8000  OG  SER B 296      23.258   4.185 -20.846  1.00 66.95           O  
ANISOU 8000  OG  SER B 296     8590   8309   8539    327    423    380       O  
ATOM   8001  N   ASP B 297      20.204   6.401 -18.245  1.00 67.45           N  
ANISOU 8001  N   ASP B 297     8602   8410   8613    286    366    330       N  
ATOM   8002  CA  ASP B 297      19.160   7.376 -17.945  1.00 70.74           C  
ANISOU 8002  CA  ASP B 297     9019   8826   9032    279    353    314       C  
ATOM   8003  C   ASP B 297      18.803   8.278 -19.133  1.00 73.48           C  
ANISOU 8003  C   ASP B 297     9400   9142   9374    292    360    311       C  
ATOM   8004  O   ASP B 297      17.639   8.643 -19.310  1.00 73.94           O  
ANISOU 8004  O   ASP B 297     9472   9193   9428    295    344    302       O  
ATOM   8005  CB  ASP B 297      19.528   8.195 -16.706  1.00 68.14           C  
ANISOU 8005  CB  ASP B 297     8653   8520   8716    258    357    304       C  
ATOM   8006  CG  ASP B 297      19.465   7.373 -15.432  1.00 68.13           C  
ANISOU 8006  CG  ASP B 297     8617   8549   8717    246    343    304       C  
ATOM   8007  OD1 ASP B 297      18.894   6.258 -15.457  1.00 64.93           O  
ANISOU 8007  OD1 ASP B 297     8217   8147   8304    254    327    309       O  
ATOM   8008  OD2 ASP B 297      19.988   7.841 -14.403  1.00 71.04           O  
ANISOU 8008  OD2 ASP B 297     8955   8940   9096    229    348    298       O  
ATOM   8009  N   ASP B 298      19.793   8.604 -19.960  1.00 77.45           N  
ANISOU 8009  N   ASP B 298     9920   9629   9878    299    385    319       N  
ATOM   8010  CA  ASP B 298      19.545   9.463 -21.118  1.00 81.49           C  
ANISOU 8010  CA  ASP B 298    10466  10111  10384    312    394    318       C  
ATOM   8011  C   ASP B 298      19.127   8.716 -22.398  1.00 81.09           C  
ANISOU 8011  C   ASP B 298    10455  10037  10318    335    389    327       C  
ATOM   8012  O   ASP B 298      19.206   9.269 -23.497  1.00 83.83           O  
ANISOU 8012  O   ASP B 298    10832  10358  10658    348    401    330       O  
ATOM   8013  CB  ASP B 298      20.708  10.447 -21.361  1.00 83.27           C  
ANISOU 8013  CB  ASP B 298    10690  10328  10620    307    425    320       C  
ATOM   8014  CG  ASP B 298      22.051   9.762 -21.497  1.00 87.00           C  
ANISOU 8014  CG  ASP B 298    11155  10804  11095    309    444    334       C  
ATOM   8015  OD1 ASP B 298      22.197   8.897 -22.385  1.00 91.84           O  
ANISOU 8015  OD1 ASP B 298    11792  11402  11697    326    446    346       O  
ATOM   8016  OD2 ASP B 298      22.971  10.114 -20.728  1.00 89.44           O  
ANISOU 8016  OD2 ASP B 298    11435  11130  11418    293    458    333       O  
ATOM   8017  N   ILE B 299      18.669   7.472 -22.251  1.00 77.01           N  
ANISOU 8017  N   ILE B 299     9937   9529   9794    339    370    331       N  
ATOM   8018  CA  ILE B 299      18.054   6.755 -23.375  1.00 74.35           C  
ANISOU 8018  CA  ILE B 299     9636   9171   9440    359    360    336       C  
ATOM   8019  C   ILE B 299      16.567   7.121 -23.502  1.00 72.02           C  
ANISOU 8019  C   ILE B 299     9353   8870   9139    362    335    324       C  
ATOM   8020  O   ILE B 299      15.961   6.922 -24.555  1.00 70.73           O  
ANISOU 8020  O   ILE B 299     9224   8687   8963    379    327    326       O  
ATOM   8021  CB  ILE B 299      18.379   5.220 -23.392  1.00 75.21           C  
ANISOU 8021  CB  ILE B 299     9745   9287   9544    364    355    348       C  
ATOM   8022  CG1 ILE B 299      17.499   4.433 -24.379  1.00 79.68           C  
ANISOU 8022  CG1 ILE B 299    10346   9835  10094    382    339    350       C  
ATOM   8023  CG2 ILE B 299      18.316   4.600 -22.012  1.00 72.09           C  
ANISOU 8023  CG2 ILE B 299     9311   8922   9158    347    343    345       C  
ATOM   8024  CD1 ILE B 299      16.352   3.659 -23.755  1.00 77.48           C  
ANISOU 8024  CD1 ILE B 299    10054   9569   9812    377    309    343       C  
ATOM   8025  N   VAL B 300      15.993   7.689 -22.442  1.00 73.71           N  
ANISOU 8025  N   VAL B 300     9540   9102   9363    347    323    313       N  
ATOM   8026  CA  VAL B 300      14.605   8.170 -22.510  1.00 74.34           C  
ANISOU 8026  CA  VAL B 300     9629   9178   9439    350    302    301       C  
ATOM   8027  C   VAL B 300      14.497   9.571 -23.093  1.00 72.18           C  
ANISOU 8027  C   VAL B 300     9373   8885   9166    354    314    296       C  
ATOM   8028  O   VAL B 300      13.525   9.873 -23.779  1.00 72.65           O  
ANISOU 8028  O   VAL B 300     9457   8930   9217    366    301    292       O  
ATOM   8029  CB  VAL B 300      13.833   8.087 -21.165  1.00 72.46           C  
ANISOU 8029  CB  VAL B 300     9357   8965   9209    333    281    291       C  
ATOM   8030  CG1 VAL B 300      13.705   6.640 -20.721  1.00 72.07           C  
ANISOU 8030  CG1 VAL B 300     9295   8930   9156    331    267    296       C  
ATOM   8031  CG2 VAL B 300      14.467   8.951 -20.080  1.00 68.70           C  
ANISOU 8031  CG2 VAL B 300     8849   8507   8747    314    295    285       C  
ATOM   8032  N   LYS B 301      15.488  10.419 -22.826  1.00 71.89           N  
ANISOU 8032  N   LYS B 301     9324   8850   9139    345    338    296       N  
ATOM   8033  CA  LYS B 301      15.486  11.776 -23.383  1.00 75.74           C  
ANISOU 8033  CA  LYS B 301     9829   9319   9629    349    353    292       C  
ATOM   8034  C   LYS B 301      16.077  11.827 -24.806  1.00 71.91           C  
ANISOU 8034  C   LYS B 301     9381   8806   9134    369    372    303       C  
ATOM   8035  O   LYS B 301      16.689  12.815 -25.213  1.00 72.41           O  
ANISOU 8035  O   LYS B 301     9454   8855   9202    370    395    304       O  
ATOM   8036  CB  LYS B 301      16.131  12.791 -22.415  1.00 81.63           C  
ANISOU 8036  CB  LYS B 301    10545  10079  10392    329    369    284       C  
ATOM   8037  CG  LYS B 301      17.596  12.571 -22.047  1.00 88.22           C  
ANISOU 8037  CG  LYS B 301    11360  10923  11235    319    392    292       C  
ATOM   8038  CD  LYS B 301      18.032  13.568 -20.973  1.00 93.40           C  
ANISOU 8038  CD  LYS B 301    11984  11595  11908    297    403    281       C  
ATOM   8039  CE  LYS B 301      19.545  13.755 -20.903  1.00 98.38           C  
ANISOU 8039  CE  LYS B 301    12601  12227  12548    289    431    288       C  
ATOM   8040  NZ  LYS B 301      20.129  14.393 -22.120  1.00 97.57           N  
ANISOU 8040  NZ  LYS B 301    12530  12096  12444    303    456    295       N  
ATOM   8041  N   PHE B 302      15.846  10.756 -25.561  1.00 70.50           N  
ANISOU 8041  N   PHE B 302     9225   8619   8942    384    361    311       N  
ATOM   8042  CA  PHE B 302      16.403  10.585 -26.896  1.00 72.28           C  
ANISOU 8042  CA  PHE B 302     9487   8819   9156    404    378    322       C  
ATOM   8043  C   PHE B 302      15.548  11.258 -27.958  1.00 71.26           C  
ANISOU 8043  C   PHE B 302     9394   8666   9014    421    372    319       C  
ATOM   8044  O   PHE B 302      14.322  11.232 -27.879  1.00 73.12           O  
ANISOU 8044  O   PHE B 302     9632   8904   9244    424    347    311       O  
ATOM   8045  CB  PHE B 302      16.553   9.097 -27.207  1.00 74.44           C  
ANISOU 8045  CB  PHE B 302     9768   9094   9419    412    369    332       C  
ATOM   8046  CG  PHE B 302      17.304   8.816 -28.474  1.00 76.41           C  
ANISOU 8046  CG  PHE B 302    10052   9320   9658    430    389    345       C  
ATOM   8047  CD1 PHE B 302      18.574   9.350 -28.680  1.00 78.94           C  
ANISOU 8047  CD1 PHE B 302    10372   9633   9986    429    421    352       C  
ATOM   8048  CD2 PHE B 302      16.748   8.008 -29.457  1.00 77.43           C  
ANISOU 8048  CD2 PHE B 302    10215   9435   9770    449    375    349       C  
ATOM   8049  CE1 PHE B 302      19.272   9.090 -29.847  1.00 79.93           C  
ANISOU 8049  CE1 PHE B 302    10529   9736  10102    446    440    365       C  
ATOM   8050  CE2 PHE B 302      17.443   7.737 -30.622  1.00 77.19           C  
ANISOU 8050  CE2 PHE B 302    10216   9381   9728    466    394    361       C  
ATOM   8051  CZ  PHE B 302      18.704   8.281 -30.820  1.00 81.30           C  
ANISOU 8051  CZ  PHE B 302    10736   9895  10256    465    427    369       C  
ATOM   8052  N   HIS B 303      16.206  11.833 -28.963  1.00 71.23           N  
ANISOU 8052  N   HIS B 303     9417   8639   9006    434    396    327       N  
ATOM   8053  CA  HIS B 303      15.533  12.674 -29.956  1.00 70.58           C  
ANISOU 8053  CA  HIS B 303     9369   8533   8913    452    396    325       C  
ATOM   8054  C   HIS B 303      14.551  11.943 -30.834  1.00 70.58           C  
ANISOU 8054  C   HIS B 303     9399   8522   8893    470    372    326       C  
ATOM   8055  O   HIS B 303      13.610  12.553 -31.336  1.00 72.64           O  
ANISOU 8055  O   HIS B 303     9680   8773   9147    481    360    321       O  
ATOM   8056  CB  HIS B 303      16.545  13.477 -30.788  1.00 72.19           C  
ANISOU 8056  CB  HIS B 303     9594   8715   9118    461    430    333       C  
ATOM   8057  CG  HIS B 303      17.232  12.675 -31.875  1.00 75.36           C  
ANISOU 8057  CG  HIS B 303    10025   9099   9506    478    443    347       C  
ATOM   8058  ND1 HIS B 303      18.332  11.932 -31.646  1.00 74.99           N  
ANISOU 8058  ND1 HIS B 303     9966   9061   9466    472    457    356       N  
ATOM   8059  CD2 HIS B 303      16.936  12.530 -33.232  1.00 74.23           C  
ANISOU 8059  CD2 HIS B 303     9926   8932   9344    503    442    354       C  
ATOM   8060  CE1 HIS B 303      18.717  11.333 -32.790  1.00 72.74           C  
ANISOU 8060  CE1 HIS B 303     9714   8755   9166    492    467    368       C  
ATOM   8061  NE2 HIS B 303      17.862  11.701 -33.760  1.00 74.30           N  
ANISOU 8061  NE2 HIS B 303     9947   8934   9347    510    457    366       N  
ATOM   8062  N   CYS B 304      14.732  10.636 -31.017  1.00 71.96           N  
ANISOU 8062  N   CYS B 304     9579   8701   9061    474    364    333       N  
ATOM   8063  CA  CYS B 304      13.841   9.880 -31.907  1.00 75.68           C  
ANISOU 8063  CA  CYS B 304    10081   9161   9513    492    341    333       C  
ATOM   8064  C   CYS B 304      12.481   9.574 -31.274  1.00 74.18           C  
ANISOU 8064  C   CYS B 304     9874   8986   9322    485    306    322       C  
ATOM   8065  O   CYS B 304      11.560   9.122 -31.957  1.00 77.25           O  
ANISOU 8065  O   CYS B 304    10287   9367   9697    499    285    320       O  
ATOM   8066  CB  CYS B 304      14.513   8.609 -32.455  1.00 79.08           C  
ANISOU 8066  CB  CYS B 304    10525   9586   9933    501    347    344       C  
ATOM   8067  SG  CYS B 304      16.095   8.891 -33.315  1.00 89.64           S  
ANISOU 8067  SG  CYS B 304    11884  10903  11270    511    388    359       S  
ATOM   8068  N   LEU B 305      12.359   9.846 -29.978  1.00 68.31           N  
ANISOU 8068  N   LEU B 305     9092   8265   8595    465    302    314       N  
ATOM   8069  CA  LEU B 305      11.121   9.601 -29.241  1.00 63.15           C  
ANISOU 8069  CA  LEU B 305     8420   7628   7944    457    271    303       C  
ATOM   8070  C   LEU B 305      10.305  10.883 -29.041  1.00 63.53           C  
ANISOU 8070  C   LEU B 305     8465   7675   7998    455    265    293       C  
ATOM   8071  O   LEU B 305       9.254  10.868 -28.389  1.00 61.99           O  
ANISOU 8071  O   LEU B 305     8252   7492   7806    448    242    284       O  
ATOM   8072  CB  LEU B 305      11.438   8.952 -27.888  1.00 58.92           C  
ANISOU 8072  CB  LEU B 305     7843   7120   7423    435    267    301       C  
ATOM   8073  CG  LEU B 305      12.199   7.620 -27.884  1.00 57.32           C  
ANISOU 8073  CG  LEU B 305     7638   6922   7218    435    271    311       C  
ATOM   8074  CD1 LEU B 305      12.688   7.284 -26.485  1.00 55.50           C  
ANISOU 8074  CD1 LEU B 305     7365   6719   7003    413    274    310       C  
ATOM   8075  CD2 LEU B 305      11.361   6.482 -28.454  1.00 56.51           C  
ANISOU 8075  CD2 LEU B 305     7555   6815   7101    446    247    311       C  
ATOM   8076  N   ALA B 306      10.790  11.981 -29.621  1.00 60.80           N  
ANISOU 8076  N   ALA B 306     8137   7312   7652    462    288    296       N  
ATOM   8077  CA  ALA B 306      10.203  13.301 -29.418  1.00 57.96           C  
ANISOU 8077  CA  ALA B 306     7774   6950   7298    461    289    288       C  
ATOM   8078  C   ALA B 306       8.761  13.418 -29.910  1.00 58.79           C  
ANISOU 8078  C   ALA B 306     7896   7048   7392    474    262    282       C  
ATOM   8079  O   ALA B 306       7.928  14.047 -29.249  1.00 55.41           O  
ANISOU 8079  O   ALA B 306     7451   6630   6972    466    249    272       O  
ATOM   8080  CB  ALA B 306      11.078  14.370 -30.048  1.00 55.66           C  
ANISOU 8080  CB  ALA B 306     7500   6639   7008    468    321    293       C  
ATOM   8081  N   ASN B 307       8.467  12.802 -31.054  1.00 62.09           N  
ANISOU 8081  N   ASN B 307     8348   7451   7792    494    252    287       N  
ATOM   8082  CA  ASN B 307       7.138  12.910 -31.674  1.00 66.01           C  
ANISOU 8082  CA  ASN B 307     8864   7940   8275    509    226    282       C  
ATOM   8083  C   ASN B 307       6.166  11.791 -31.280  1.00 61.60           C  
ANISOU 8083  C   ASN B 307     8293   7396   7714    504    192    276       C  
ATOM   8084  O   ASN B 307       5.236  11.476 -32.018  1.00 62.44           O  
ANISOU 8084  O   ASN B 307     8421   7495   7807    519    170    275       O  
ATOM   8085  CB  ASN B 307       7.252  13.030 -33.210  1.00 71.81           C  
ANISOU 8085  CB  ASN B 307     9645   8648   8990    535    233    290       C  
ATOM   8086  CG  ASN B 307       7.666  14.428 -33.672  1.00 74.64           C  
ANISOU 8086  CG  ASN B 307    10019   8989   9349    543    259    293       C  
ATOM   8087  OD1 ASN B 307       7.737  15.371 -32.877  1.00 71.47           O  
ANISOU 8087  OD1 ASN B 307     9595   8595   8964    530    270    288       O  
ATOM   8088  ND2 ASN B 307       7.939  14.564 -34.971  1.00 74.48           N  
ANISOU 8088  ND2 ASN B 307    10039   8946   9313    565    270    302       N  
ATOM   8089  N   VAL B 308       6.387  11.206 -30.107  1.00 60.68           N  
ANISOU 8089  N   VAL B 308     8141   7302   7612    484    189    273       N  
ATOM   8090  CA  VAL B 308       5.541  10.132 -29.575  1.00 56.69           C  
ANISOU 8090  CA  VAL B 308     7619   6811   7106    477    160    268       C  
ATOM   8091  C   VAL B 308       4.486  10.724 -28.632  1.00 54.89           C  
ANISOU 8091  C   VAL B 308     7365   6599   6891    466    143    257       C  
ATOM   8092  O   VAL B 308       4.786  11.639 -27.862  1.00 56.26           O  
ANISOU 8092  O   VAL B 308     7517   6779   7077    454    157    253       O  
ATOM   8093  CB  VAL B 308       6.408   9.074 -28.854  1.00 55.39           C  
ANISOU 8093  CB  VAL B 308     7433   6662   6950    462    167    273       C  
ATOM   8094  CG1 VAL B 308       5.613   8.324 -27.800  1.00 55.50           C  
ANISOU 8094  CG1 VAL B 308     7416   6698   6972    448    143    265       C  
ATOM   8095  CG2 VAL B 308       7.021   8.107 -29.855  1.00 52.55           C  
ANISOU 8095  CG2 VAL B 308     7101   6288   6575    476    173    283       C  
ATOM   8096  N   SER B 309       3.259  10.210 -28.694  1.00 53.17           N  
ANISOU 8096  N   SER B 309     7148   6385   6668    470    112    251       N  
ATOM   8097  CA  SER B 309       2.159  10.741 -27.868  1.00 53.55           C  
ANISOU 8097  CA  SER B 309     7172   6447   6727    461     95    241       C  
ATOM   8098  C   SER B 309       2.025  10.064 -26.493  1.00 51.86           C  
ANISOU 8098  C   SER B 309     6919   6258   6528    439     86    236       C  
ATOM   8099  O   SER B 309       1.537  10.671 -25.539  1.00 50.07           O  
ANISOU 8099  O   SER B 309     6666   6044   6313    428     82    229       O  
ATOM   8100  CB  SER B 309       0.822  10.708 -28.626  1.00 53.54           C  
ANISOU 8100  CB  SER B 309     7190   6437   6715    476     67    236       C  
ATOM   8101  OG  SER B 309       0.156   9.470 -28.451  1.00 54.67           O  
ANISOU 8101  OG  SER B 309     7326   6590   6856    473     42    233       O  
ATOM   8102  N   ALA B 310       2.447   8.805 -26.406  1.00 50.20           N  
ANISOU 8102  N   ALA B 310     6705   6053   6315    435     83    240       N  
ATOM   8103  CA  ALA B 310       2.449   8.071 -25.145  1.00 47.60           C  
ANISOU 8103  CA  ALA B 310     6340   5747   5998    416     76    238       C  
ATOM   8104  C   ALA B 310       3.788   7.375 -24.963  1.00 46.33           C  
ANISOU 8104  C   ALA B 310     6174   5590   5838    410     97    247       C  
ATOM   8105  O   ALA B 310       4.256   6.688 -25.862  1.00 48.34           O  
ANISOU 8105  O   ALA B 310     6453   5832   6081    421    101    254       O  
ATOM   8106  CB  ALA B 310       1.311   7.064 -25.114  1.00 46.07           C  
ANISOU 8106  CB  ALA B 310     6143   5559   5802    417     46    233       C  
ATOM   8107  N   MET B 311       4.401   7.560 -23.803  1.00 44.43           N  
ANISOU 8107  N   MET B 311     5902   5367   5611    393    109    246       N  
ATOM   8108  CA  MET B 311       5.694   6.960 -23.503  1.00 45.59           C  
ANISOU 8108  CA  MET B 311     6040   5521   5761    386    129    255       C  
ATOM   8109  C   MET B 311       5.568   6.063 -22.264  1.00 44.62           C  
ANISOU 8109  C   MET B 311     5882   5422   5647    369    119    253       C  
ATOM   8110  O   MET B 311       4.980   6.467 -21.263  1.00 44.25           O  
ANISOU 8110  O   MET B 311     5810   5391   5612    357    110    245       O  
ATOM   8111  CB  MET B 311       6.734   8.076 -23.313  1.00 45.24           C  
ANISOU 8111  CB  MET B 311     5989   5475   5723    380    157    257       C  
ATOM   8112  CG  MET B 311       8.082   7.669 -22.735  1.00 48.64           C  
ANISOU 8112  CG  MET B 311     6402   5918   6161    369    178    264       C  
ATOM   8113  SD  MET B 311       9.157   6.632 -23.765  1.00 55.22           S  
ANISOU 8113  SD  MET B 311     7262   6737   6983    382    192    279       S  
ATOM   8114  CE  MET B 311       8.978   7.400 -25.373  1.00 52.85           C  
ANISOU 8114  CE  MET B 311     7007   6405   6669    405    198    280       C  
ATOM   8115  N   SER B 312       6.096   4.843 -22.338  1.00 45.22           N  
ANISOU 8115  N   SER B 312     5959   5500   5719    370    120    261       N  
ATOM   8116  CA  SER B 312       6.030   3.915 -21.193  1.00 44.77           C  
ANISOU 8116  CA  SER B 312     5872   5467   5672    356    112    261       C  
ATOM   8117  C   SER B 312       7.341   3.232 -20.855  1.00 43.29           C  
ANISOU 8117  C   SER B 312     5673   5287   5486    351    131    272       C  
ATOM   8118  O   SER B 312       8.044   2.744 -21.735  1.00 43.98           O  
ANISOU 8118  O   SER B 312     5783   5360   5564    361    142    281       O  
ATOM   8119  CB  SER B 312       4.965   2.841 -21.399  1.00 43.89           C  
ANISOU 8119  CB  SER B 312     5767   5353   5555    360     86    259       C  
ATOM   8120  OG  SER B 312       3.670   3.376 -21.232  1.00 45.31           O  
ANISOU 8120  OG  SER B 312     5942   5535   5738    360     66    248       O  
ATOM   8121  N   LEU B 313       7.642   3.203 -19.562  1.00 41.91           N  
ANISOU 8121  N   LEU B 313     5463   5136   5323    334    135    271       N  
ATOM   8122  CA  LEU B 313       8.742   2.425 -19.010  1.00 41.16           C  
ANISOU 8122  CA  LEU B 313     5351   5054   5231    328    149    280       C  
ATOM   8123  C   LEU B 313       8.187   1.446 -17.979  1.00 40.77           C  
ANISOU 8123  C   LEU B 313     5277   5025   5188    318    133    279       C  
ATOM   8124  O   LEU B 313       7.374   1.827 -17.135  1.00 41.67           O  
ANISOU 8124  O   LEU B 313     5370   5152   5309    308    120    270       O  
ATOM   8125  CB  LEU B 313       9.762   3.347 -18.350  1.00 40.45           C  
ANISOU 8125  CB  LEU B 313     5241   4976   5150    316    170    281       C  
ATOM   8126  CG  LEU B 313      10.406   4.426 -19.213  1.00 41.42           C  
ANISOU 8126  CG  LEU B 313     5385   5081   5271    324    190    282       C  
ATOM   8127  CD1 LEU B 313      11.435   5.176 -18.383  1.00 42.86           C  
ANISOU 8127  CD1 LEU B 313     5542   5278   5464    310    210    281       C  
ATOM   8128  CD2 LEU B 313      11.049   3.832 -20.459  1.00 42.54           C  
ANISOU 8128  CD2 LEU B 313     5558   5201   5401    340    200    293       C  
ATOM   8129  N   ALA B 314       8.610   0.186 -18.053  1.00 40.99           N  
ANISOU 8129  N   ALA B 314     5306   5054   5212    321    134    289       N  
ATOM   8130  CA  ALA B 314       8.150  -0.841 -17.105  1.00 39.52           C  
ANISOU 8130  CA  ALA B 314     5097   4887   5031    313    121    290       C  
ATOM   8131  C   ALA B 314       9.253  -1.854 -16.768  1.00 39.43           C  
ANISOU 8131  C   ALA B 314     5076   4885   5020    311    135    303       C  
ATOM   8132  O   ALA B 314       9.705  -2.595 -17.630  1.00 40.05           O  
ANISOU 8132  O   ALA B 314     5176   4949   5091    322    142    312       O  
ATOM   8133  CB  ALA B 314       6.899  -1.540 -17.624  1.00 36.62           C  
ANISOU 8133  CB  ALA B 314     4747   4508   4659    320     98    285       C  
ATOM   8134  N   GLY B 315       9.683  -1.862 -15.508  1.00 38.89           N  
ANISOU 8134  N   GLY B 315     4973   4842   4960    298    141    304       N  
ATOM   8135  CA  GLY B 315      10.716  -2.769 -15.037  1.00 37.86           C  
ANISOU 8135  CA  GLY B 315     4828   4724   4831    296    154    317       C  
ATOM   8136  C   GLY B 315      12.092  -2.332 -15.486  1.00 39.32           C  
ANISOU 8136  C   GLY B 315     5019   4904   5015    299    178    325       C  
ATOM   8137  O   GLY B 315      12.956  -3.173 -15.775  1.00 39.67           O  
ANISOU 8137  O   GLY B 315     5069   4946   5056    306    191    338       O  
ATOM   8138  N   VAL B 316      12.298  -1.016 -15.517  1.00 39.08           N  
ANISOU 8138  N   VAL B 316     4987   4872   4987    295    186    318       N  
ATOM   8139  CA  VAL B 316      13.492  -0.419 -16.116  1.00 39.59           C  
ANISOU 8139  CA  VAL B 316     5062   4928   5052    299    209    324       C  
ATOM   8140  C   VAL B 316      14.449   0.161 -15.065  1.00 40.52           C  
ANISOU 8140  C   VAL B 316     5147   5068   5179    285    224    324       C  
ATOM   8141  O   VAL B 316      14.019   0.766 -14.088  1.00 39.66           O  
ANISOU 8141  O   VAL B 316     5014   4977   5077    272    216    314       O  
ATOM   8142  CB  VAL B 316      13.100   0.624 -17.200  1.00 39.74           C  
ANISOU 8142  CB  VAL B 316     5111   4922   5066    308    210    317       C  
ATOM   8143  CG1 VAL B 316      14.260   1.540 -17.545  1.00 39.55           C  
ANISOU 8143  CG1 VAL B 316     5090   4893   5045    307    235    320       C  
ATOM   8144  CG2 VAL B 316      12.596  -0.073 -18.461  1.00 38.47           C  
ANISOU 8144  CG2 VAL B 316     4986   4737   4893    325    202    320       C  
ATOM   8145  N   SER B 317      15.750  -0.030 -15.283  1.00 42.67           N  
ANISOU 8145  N   SER B 317     5418   5341   5452    287    245    336       N  
ATOM   8146  CA  SER B 317      16.790   0.411 -14.341  1.00 43.52           C  
ANISOU 8146  CA  SER B 317     5494   5472   5569    274    259    337       C  
ATOM   8147  C   SER B 317      17.052   1.924 -14.342  1.00 43.42           C  
ANISOU 8147  C   SER B 317     5478   5456   5562    266    269    327       C  
ATOM   8148  O   SER B 317      18.139   2.353 -13.945  1.00 45.36           O  
ANISOU 8148  O   SER B 317     5706   5713   5815    258    286    330       O  
ATOM   8149  CB  SER B 317      18.122  -0.302 -14.625  1.00 44.44           C  
ANISOU 8149  CB  SER B 317     5610   5588   5684    280    279    354       C  
ATOM   8150  OG  SER B 317      17.934  -1.574 -15.223  1.00 49.37           O  
ANISOU 8150  OG  SER B 317     6253   6202   6301    293    275    364       O  
ATOM   8151  N   ILE B 318      16.086   2.731 -14.778  1.00 41.39           N  
ANISOU 8151  N   ILE B 318     5238   5184   5303    268    260    316       N  
ATOM   8152  CA  ILE B 318      16.253   4.191 -14.750  1.00 42.71           C  
ANISOU 8152  CA  ILE B 318     5404   5348   5477    261    270    306       C  
ATOM   8153  C   ILE B 318      16.419   4.714 -13.316  1.00 43.66           C  
ANISOU 8153  C   ILE B 318     5485   5495   5606    241    268    297       C  
ATOM   8154  O   ILE B 318      15.685   4.316 -12.407  1.00 45.08           O  
ANISOU 8154  O   ILE B 318     5647   5694   5788    234    251    292       O  
ATOM   8155  CB  ILE B 318      15.115   4.933 -15.492  1.00 41.94           C  
ANISOU 8155  CB  ILE B 318     5331   5228   5374    268    259    296       C  
ATOM   8156  CG1 ILE B 318      15.470   6.415 -15.695  1.00 42.68           C  
ANISOU 8156  CG1 ILE B 318     5428   5312   5473    263    274    288       C  
ATOM   8157  CG2 ILE B 318      13.782   4.750 -14.781  1.00 41.25           C  
ANISOU 8157  CG2 ILE B 318     5233   5151   5287    263    234    286       C  
ATOM   8158  CD1 ILE B 318      14.617   7.130 -16.733  1.00 42.96           C  
ANISOU 8158  CD1 ILE B 318     5496   5322   5503    275    270    282       C  
ATOM   8159  N   LYS B 319      17.398   5.588 -13.122  1.00 42.84           N  
ANISOU 8159  N   LYS B 319     5369   5396   5510    232    287    295       N  
ATOM   8160  CA  LYS B 319      17.703   6.102 -11.798  1.00 44.23           C  
ANISOU 8160  CA  LYS B 319     5509   5599   5694    213    288    287       C  
ATOM   8161  C   LYS B 319      17.297   7.567 -11.687  1.00 43.74           C  
ANISOU 8161  C   LYS B 319     5448   5531   5638    204    290    272       C  
ATOM   8162  O   LYS B 319      16.938   8.044 -10.618  1.00 42.64           O  
ANISOU 8162  O   LYS B 319     5285   5410   5504    190    282    261       O  
ATOM   8163  CB  LYS B 319      19.196   5.941 -11.487  1.00 46.16           C  
ANISOU 8163  CB  LYS B 319     5735   5858   5945    207    307    296       C  
ATOM   8164  CG  LYS B 319      19.801   4.584 -11.824  1.00 45.83           C  
ANISOU 8164  CG  LYS B 319     5697   5817   5898    218    311    314       C  
ATOM   8165  CD  LYS B 319      19.514   3.554 -10.750  1.00 50.12           C  
ANISOU 8165  CD  LYS B 319     6216   6387   6440    213    295    317       C  
ATOM   8166  CE  LYS B 319      20.255   2.251 -11.009  1.00 50.99           C  
ANISOU 8166  CE  LYS B 319     6328   6500   6546    224    302    335       C  
ATOM   8167  NZ  LYS B 319      19.531   1.406 -11.997  1.00 52.65           N  
ANISOU 8167  NZ  LYS B 319     6570   6687   6747    241    294    341       N  
ATOM   8168  N   TYR B 320      17.364   8.279 -12.804  1.00 45.25           N  
ANISOU 8168  N   TYR B 320     5668   5696   5828    214    302    271       N  
ATOM   8169  CA  TYR B 320      17.000   9.688 -12.843  1.00 45.78           C  
ANISOU 8169  CA  TYR B 320     5739   5752   5900    207    306    258       C  
ATOM   8170  C   TYR B 320      16.275   9.992 -14.139  1.00 45.22           C  
ANISOU 8170  C   TYR B 320     5707   5651   5822    225    304    258       C  
ATOM   8171  O   TYR B 320      16.686   9.529 -15.203  1.00 46.04           O  
ANISOU 8171  O   TYR B 320     5836   5737   5920    239    313    270       O  
ATOM   8172  CB  TYR B 320      18.241  10.584 -12.726  1.00 46.28           C  
ANISOU 8172  CB  TYR B 320     5792   5818   5973    197    331    256       C  
ATOM   8173  CG  TYR B 320      19.041  10.403 -11.459  1.00 46.18           C  
ANISOU 8173  CG  TYR B 320     5740   5837   5968    179    333    255       C  
ATOM   8174  CD1 TYR B 320      20.154   9.563 -11.432  1.00 48.25           C  
ANISOU 8174  CD1 TYR B 320     5992   6110   6231    180    343    268       C  
ATOM   8175  CD2 TYR B 320      18.697  11.073 -10.293  1.00 47.09           C  
ANISOU 8175  CD2 TYR B 320     5830   5971   6089    162    326    241       C  
ATOM   8176  CE1 TYR B 320      20.900   9.388 -10.274  1.00 49.62           C  
ANISOU 8176  CE1 TYR B 320     6130   6313   6411    165    345    268       C  
ATOM   8177  CE2 TYR B 320      19.434  10.907  -9.126  1.00 50.24           C  
ANISOU 8177  CE2 TYR B 320     6194   6400   6493    146    328    239       C  
ATOM   8178  CZ  TYR B 320      20.538  10.064  -9.121  1.00 50.23           C  
ANISOU 8178  CZ  TYR B 320     6181   6409   6492    148    337    253       C  
ATOM   8179  OH  TYR B 320      21.275   9.886  -7.969  1.00 49.39           O  
ANISOU 8179  OH  TYR B 320     6040   6334   6390    133    337    252       O  
ATOM   8180  N   LEU B 321      15.199  10.767 -14.041  1.00 46.34           N  
ANISOU 8180  N   LEU B 321     5854   5787   5964    223    293    246       N  
ATOM   8181  CA  LEU B 321      14.455  11.236 -15.209  1.00 50.32           C  
ANISOU 8181  CA  LEU B 321     6393   6263   6462    239    291    245       C  
ATOM   8182  C   LEU B 321      14.365  12.749 -15.091  1.00 52.36           C  
ANISOU 8182  C   LEU B 321     6651   6514   6728    232    302    233       C  
ATOM   8183  O   LEU B 321      13.522  13.253 -14.360  1.00 53.24           O  
ANISOU 8183  O   LEU B 321     6750   6634   6843    223    290    222       O  
ATOM   8184  CB  LEU B 321      13.047  10.614 -15.230  1.00 48.60           C  
ANISOU 8184  CB  LEU B 321     6183   6045   6237    247    264    243       C  
ATOM   8185  CG  LEU B 321      12.349  10.258 -16.552  1.00 48.27           C  
ANISOU 8185  CG  LEU B 321     6178   5978   6184    268    255    248       C  
ATOM   8186  CD1 LEU B 321      11.132   9.379 -16.315  1.00 47.29           C  
ANISOU 8186  CD1 LEU B 321     6052   5860   6054    272    228    246       C  
ATOM   8187  CD2 LEU B 321      11.924  11.490 -17.316  1.00 49.09           C  
ANISOU 8187  CD2 LEU B 321     6305   6059   6287    276    261    242       C  
ATOM   8188  N   GLU B 322      15.237  13.482 -15.776  1.00 57.58           N  
ANISOU 8188  N   GLU B 322     7326   7159   7392    234    326    236       N  
ATOM   8189  CA  GLU B 322      15.263  14.933 -15.560  1.00 64.51           C  
ANISOU 8189  CA  GLU B 322     8201   8031   8279    225    339    225       C  
ATOM   8190  C   GLU B 322      15.341  15.866 -16.781  1.00 68.85           C  
ANISOU 8190  C   GLU B 322     8783   8549   8826    238    356    226       C  
ATOM   8191  O   GLU B 322      14.425  16.659 -17.014  1.00 74.29           O  
ANISOU 8191  O   GLU B 322     9485   9225   9514    243    350    218       O  
ATOM   8192  CB  GLU B 322      16.274  15.326 -14.471  1.00 63.32           C  
ANISOU 8192  CB  GLU B 322     8016   7902   8140    203    352    219       C  
ATOM   8193  CG  GLU B 322      17.687  14.802 -14.635  1.00 67.43           C  
ANISOU 8193  CG  GLU B 322     8529   8426   8663    201    370    230       C  
ATOM   8194  CD  GLU B 322      18.576  15.158 -13.452  1.00 69.92           C  
ANISOU 8194  CD  GLU B 322     8808   8767   8990    179    379    224       C  
ATOM   8195  OE1 GLU B 322      19.797  14.884 -13.518  1.00 73.67           O  
ANISOU 8195  OE1 GLU B 322     9273   9246   9469    176    395    232       O  
ATOM   8196  OE2 GLU B 322      18.059  15.711 -12.454  1.00 65.87           O  
ANISOU 8196  OE2 GLU B 322     8274   8268   8482    164    370    210       O  
ATOM   8197  N   ASP B 323      16.411  15.793 -17.556  1.00 69.10           N  
ANISOU 8197  N   ASP B 323     8828   8567   8858    244    377    236       N  
ATOM   8198  CA  ASP B 323      16.585  16.775 -18.619  1.00 71.56           C  
ANISOU 8198  CA  ASP B 323     9169   8851   9170    255    396    238       C  
ATOM   8199  C   ASP B 323      15.790  16.431 -19.882  1.00 70.34           C  
ANISOU 8199  C   ASP B 323     9053   8673   9000    280    386    245       C  
ATOM   8200  O   ASP B 323      16.335  16.439 -20.989  1.00 70.99           O  
ANISOU 8200  O   ASP B 323     9161   8733   9077    294    402    255       O  
ATOM   8201  CB  ASP B 323      18.075  17.005 -18.914  1.00 78.23           C  
ANISOU 8201  CB  ASP B 323    10011   9690  10022    251    425    245       C  
ATOM   8202  CG  ASP B 323      18.788  17.758 -17.787  1.00 85.06           C  
ANISOU 8202  CG  ASP B 323    10842  10574  10903    227    438    234       C  
ATOM   8203  OD1 ASP B 323      18.209  18.724 -17.244  1.00 85.86           O  
ANISOU 8203  OD1 ASP B 323    10936  10677  11010    217    435    221       O  
ATOM   8204  OD2 ASP B 323      19.933  17.389 -17.444  1.00 87.64           O  
ANISOU 8204  OD2 ASP B 323    11149  10913  11236    217    450    240       O  
ATOM   8205  N   VAL B 324      14.502  16.129 -19.706  1.00 66.05           N  
ANISOU 8205  N   VAL B 324     8512   8134   8450    284    360    240       N  
ATOM   8206  CA  VAL B 324      13.610  15.859 -20.837  1.00 63.64           C  
ANISOU 8206  CA  VAL B 324     8241   7808   8131    306    347    244       C  
ATOM   8207  C   VAL B 324      13.322  17.188 -21.520  1.00 64.75           C  
ANISOU 8207  C   VAL B 324     8404   7924   8271    315    360    240       C  
ATOM   8208  O   VAL B 324      12.888  18.134 -20.858  1.00 65.70           O  
ANISOU 8208  O   VAL B 324     8511   8050   8400    304    360    229       O  
ATOM   8209  CB  VAL B 324      12.276  15.210 -20.406  1.00 63.55           C  
ANISOU 8209  CB  VAL B 324     8223   7808   8113    308    315    239       C  
ATOM   8210  CG1 VAL B 324      11.457  14.806 -21.622  1.00 65.12           C  
ANISOU 8210  CG1 VAL B 324     8457   7986   8297    331    301    245       C  
ATOM   8211  CG2 VAL B 324      12.518  13.993 -19.537  1.00 62.25           C  
ANISOU 8211  CG2 VAL B 324     8031   7668   7950    297    303    242       C  
ATOM   8212  N   PRO B 325      13.583  17.272 -22.839  1.00 64.47           N  
ANISOU 8212  N   PRO B 325     8404   7863   8226    334    372    250       N  
ATOM   8213  CA  PRO B 325      13.394  18.508 -23.608  1.00 64.57           C  
ANISOU 8213  CA  PRO B 325     8441   7852   8238    345    387    248       C  
ATOM   8214  C   PRO B 325      11.936  18.966 -23.658  1.00 64.71           C  
ANISOU 8214  C   PRO B 325     8468   7866   8251    352    366    240       C  
ATOM   8215  O   PRO B 325      11.033  18.141 -23.811  1.00 65.79           O  
ANISOU 8215  O   PRO B 325     8610   8006   8377    361    340    241       O  
ATOM   8216  CB  PRO B 325      13.875  18.125 -25.012  1.00 62.52           C  
ANISOU 8216  CB  PRO B 325     8219   7569   7966    366    398    262       C  
ATOM   8217  CG  PRO B 325      14.775  16.959 -24.803  1.00 63.15           C  
ANISOU 8217  CG  PRO B 325     8285   7661   8045    361    401    270       C  
ATOM   8218  CD  PRO B 325      14.151  16.200 -23.673  1.00 64.09           C  
ANISOU 8218  CD  PRO B 325     8374   7808   8168    347    374    263       C  
ATOM   8219  N   LYS B 326      11.725  20.277 -23.540  1.00 66.68           N  
ANISOU 8219  N   LYS B 326     8720   8107   8509    349    378    232       N  
ATOM   8220  CA  LYS B 326      10.383  20.873 -23.504  1.00 67.49           C  
ANISOU 8220  CA  LYS B 326     8828   8205   8608    355    361    224       C  
ATOM   8221  C   LYS B 326       9.571  20.696 -24.790  1.00 63.52           C  
ANISOU 8221  C   LYS B 326     8363   7683   8089    382    348    231       C  
ATOM   8222  O   LYS B 326       8.346  20.798 -24.762  1.00 63.12           O  
ANISOU 8222  O   LYS B 326     8316   7633   8034    389    326    226       O  
ATOM   8223  CB  LYS B 326      10.459  22.364 -23.149  1.00 71.98           C  
ANISOU 8223  CB  LYS B 326     9392   8767   9190    347    380    215       C  
ATOM   8224  CG  LYS B 326      10.400  22.663 -21.658  1.00 75.19           C  
ANISOU 8224  CG  LYS B 326     9760   9198   9611    321    377    202       C  
ATOM   8225  CD  LYS B 326      10.161  24.145 -21.403  1.00 80.10           C  
ANISOU 8225  CD  LYS B 326    10381   9810  10243    316    392    193       C  
ATOM   8226  CE  LYS B 326       9.703  24.400 -19.972  1.00 81.73           C  
ANISOU 8226  CE  LYS B 326    10552  10039  10460    295    382    179       C  
ATOM   8227  NZ  LYS B 326       9.507  25.848 -19.676  1.00 80.96           N  
ANISOU 8227  NZ  LYS B 326    10455   9933  10373    288    398    169       N  
ATOM   8228  N   HIS B 327      10.250  20.431 -25.904  1.00 61.39           N  
ANISOU 8228  N   HIS B 327     8122   7395   7809    397    362    243       N  
ATOM   8229  CA  HIS B 327       9.578  20.290 -27.203  1.00 62.00           C  
ANISOU 8229  CA  HIS B 327     8237   7451   7869    424    352    250       C  
ATOM   8230  C   HIS B 327       9.042  18.903 -27.480  1.00 61.38           C  
ANISOU 8230  C   HIS B 327     8163   7379   7776    432    324    254       C  
ATOM   8231  O   HIS B 327       8.612  18.608 -28.601  1.00 59.13           O  
ANISOU 8231  O   HIS B 327     7911   7079   7476    453    316    260       O  
ATOM   8232  CB  HIS B 327      10.487  20.758 -28.341  1.00 59.81           C  
ANISOU 8232  CB  HIS B 327     7991   7148   7586    438    381    260       C  
ATOM   8233  CG  HIS B 327      11.736  19.924 -28.512  1.00 59.51           C  
ANISOU 8233  CG  HIS B 327     7951   7111   7547    435    396    269       C  
ATOM   8234  ND1 HIS B 327      12.913  20.257 -27.944  1.00 59.16           N  
ANISOU 8234  ND1 HIS B 327     7886   7072   7518    418    421    269       N  
ATOM   8235  CD2 HIS B 327      11.960  18.746 -29.225  1.00 58.04           C  
ANISOU 8235  CD2 HIS B 327     7783   6922   7348    447    388    279       C  
ATOM   8236  CE1 HIS B 327      13.845  19.345 -28.278  1.00 57.55           C  
ANISOU 8236  CE1 HIS B 327     7686   6869   7310    420    430    279       C  
ATOM   8237  NE2 HIS B 327      13.260  18.418 -29.058  1.00 58.83           N  
ANISOU 8237  NE2 HIS B 327     7872   7025   7455    438    410    286       N  
ATOM   8238  N   PHE B 328       9.062  18.043 -26.462  1.00 60.24           N  
ANISOU 8238  N   PHE B 328     7988   7260   7639    415    311    250       N  
ATOM   8239  CA  PHE B 328       8.537  16.681 -26.580  1.00 59.32           C  
ANISOU 8239  CA  PHE B 328     7873   7152   7513    420    284    253       C  
ATOM   8240  C   PHE B 328       7.008  16.675 -26.506  1.00 58.61           C  
ANISOU 8240  C   PHE B 328     7784   7066   7418    426    254    245       C  
ATOM   8241  O   PHE B 328       6.415  17.471 -25.775  1.00 59.22           O  
ANISOU 8241  O   PHE B 328     7844   7151   7505    417    250    236       O  
ATOM   8242  CB  PHE B 328       9.148  15.782 -25.506  1.00 58.03           C  
ANISOU 8242  CB  PHE B 328     7676   7013   7358    400    283    252       C  
ATOM   8243  CG  PHE B 328      10.420  15.098 -25.931  1.00 57.98           C  
ANISOU 8243  CG  PHE B 328     7677   7002   7349    402    301    263       C  
ATOM   8244  CD1 PHE B 328      10.550  13.720 -25.809  1.00 57.25           C  
ANISOU 8244  CD1 PHE B 328     7578   6921   7252    401    288    269       C  
ATOM   8245  CD2 PHE B 328      11.488  15.823 -26.452  1.00 57.88           C  
ANISOU 8245  CD2 PHE B 328     7677   6974   7340    405    332    269       C  
ATOM   8246  CE1 PHE B 328      11.717  13.078 -26.197  1.00 57.19           C  
ANISOU 8246  CE1 PHE B 328     7577   6909   7242    404    306    280       C  
ATOM   8247  CE2 PHE B 328      12.655  15.186 -26.844  1.00 56.42           C  
ANISOU 8247  CE2 PHE B 328     7498   6786   7153    407    349    280       C  
ATOM   8248  CZ  PHE B 328      12.770  13.812 -26.716  1.00 55.94           C  
ANISOU 8248  CZ  PHE B 328     7431   6735   7086    407    336    285       C  
ATOM   8249  N   LYS B 329       6.384  15.776 -27.268  1.00 58.00           N  
ANISOU 8249  N   LYS B 329     7726   6982   7325    441    233    249       N  
ATOM   8250  CA  LYS B 329       4.931  15.803 -27.491  1.00 56.95           C  
ANISOU 8250  CA  LYS B 329     7601   6848   7186    451    205    243       C  
ATOM   8251  C   LYS B 329       4.177  14.826 -26.599  1.00 54.19           C  
ANISOU 8251  C   LYS B 329     7225   6521   6841    439    177    237       C  
ATOM   8252  O   LYS B 329       2.987  14.583 -26.810  1.00 56.95           O  
ANISOU 8252  O   LYS B 329     7580   6871   7185    447    151    233       O  
ATOM   8253  CB  LYS B 329       4.595  15.501 -28.964  1.00 60.54           C  
ANISOU 8253  CB  LYS B 329     8098   7283   7621    476    197    250       C  
ATOM   8254  CG  LYS B 329       5.522  16.134 -29.995  1.00 66.56           C  
ANISOU 8254  CG  LYS B 329     8891   8022   8376    490    225    259       C  
ATOM   8255  CD  LYS B 329       5.136  17.559 -30.364  1.00 66.16           C  
ANISOU 8255  CD  LYS B 329     8854   7957   8326    500    235    257       C  
ATOM   8256  CE  LYS B 329       4.375  17.588 -31.680  1.00 70.81           C  
ANISOU 8256  CE  LYS B 329     9482   8527   8895    527    222    261       C  
ATOM   8257  NZ  LYS B 329       4.404  18.945 -32.294  1.00 73.30           N  
ANISOU 8257  NZ  LYS B 329     9818   8822   9208    540    241    264       N  
ATOM   8258  N   TRP B 330       4.876  14.273 -25.611  1.00 50.39           N  
ANISOU 8258  N   TRP B 330     6716   6059   6371    420    184    237       N  
ATOM   8259  CA  TRP B 330       4.332  13.262 -24.706  1.00 46.93           C  
ANISOU 8259  CA  TRP B 330     6251   5642   5937    408    161    233       C  
ATOM   8260  C   TRP B 330       3.069  13.678 -24.010  1.00 45.95           C  
ANISOU 8260  C   TRP B 330     6108   5528   5820    402    141    222       C  
ATOM   8261  O   TRP B 330       3.060  14.642 -23.238  1.00 46.16           O  
ANISOU 8261  O   TRP B 330     6117   5562   5858    391    151    216       O  
ATOM   8262  CB  TRP B 330       5.379  12.880 -23.668  1.00 46.84           C  
ANISOU 8262  CB  TRP B 330     6210   5649   5937    388    176    234       C  
ATOM   8263  CG  TRP B 330       6.597  12.197 -24.242  1.00 45.43           C  
ANISOU 8263  CG  TRP B 330     6044   5463   5753    392    193    245       C  
ATOM   8264  CD1 TRP B 330       6.794  11.754 -25.551  1.00 45.35           C  
ANISOU 8264  CD1 TRP B 330     6070   5434   5728    412    195    254       C  
ATOM   8265  CD2 TRP B 330       7.810  11.805 -23.521  1.00 44.24           C  
ANISOU 8265  CD2 TRP B 330     5870   5326   5610    378    210    250       C  
ATOM   8266  NE1 TRP B 330       8.018  11.161 -25.689  1.00 46.70           N  
ANISOU 8266  NE1 TRP B 330     6241   5603   5897    410    213    263       N  
ATOM   8267  CE2 TRP B 330       8.680  11.152 -24.507  1.00 45.99           C  
ANISOU 8267  CE2 TRP B 330     6117   5533   5821    390    223    261       C  
ATOM   8268  CE3 TRP B 330       8.251  11.929 -22.210  1.00 45.04           C  
ANISOU 8268  CE3 TRP B 330     5935   5450   5726    357    217    245       C  
ATOM   8269  CZ2 TRP B 330       9.931  10.655 -24.168  1.00 44.51           C  
ANISOU 8269  CZ2 TRP B 330     5916   5354   5639    382    241    269       C  
ATOM   8270  CZ3 TRP B 330       9.517  11.432 -21.880  1.00 44.74           C  
ANISOU 8270  CZ3 TRP B 330     5884   5421   5692    348    234    252       C  
ATOM   8271  CH2 TRP B 330      10.334  10.809 -22.837  1.00 45.59           C  
ANISOU 8271  CH2 TRP B 330     6015   5515   5791    361    246    264       C  
ATOM   8272  N   GLN B 331       1.994  12.946 -24.283  1.00 43.44           N  
ANISOU 8272  N   GLN B 331     5797   5212   5496    410    113    221       N  
ATOM   8273  CA  GLN B 331       0.693  13.219 -23.697  1.00 43.62           C  
ANISOU 8273  CA  GLN B 331     5803   5244   5525    406     92    211       C  
ATOM   8274  C   GLN B 331       0.464  12.389 -22.433  1.00 43.52           C  
ANISOU 8274  C   GLN B 331     5756   5257   5523    388     79    207       C  
ATOM   8275  O   GLN B 331      -0.163  12.856 -21.477  1.00 42.62           O  
ANISOU 8275  O   GLN B 331     5617   5156   5421    377     73    199       O  
ATOM   8276  CB  GLN B 331      -0.406  12.948 -24.716  1.00 45.77           C  
ANISOU 8276  CB  GLN B 331     6100   5504   5784    425     68    211       C  
ATOM   8277  CG  GLN B 331      -0.678  14.083 -25.691  1.00 48.36           C  
ANISOU 8277  CG  GLN B 331     6457   5812   6105    443     74    212       C  
ATOM   8278  CD  GLN B 331      -2.015  13.895 -26.376  1.00 51.94           C  
ANISOU 8278  CD  GLN B 331     6926   6260   6549    459     45    210       C  
ATOM   8279  OE1 GLN B 331      -2.126  13.159 -27.356  1.00 55.79           O  
ANISOU 8279  OE1 GLN B 331     7438   6738   7022    472     34    214       O  
ATOM   8280  NE2 GLN B 331      -3.047  14.534 -25.841  1.00 53.22           N  
ANISOU 8280  NE2 GLN B 331     7072   6428   6719    456     33    202       N  
ATOM   8281  N   SER B 332       0.962  11.153 -22.439  1.00 43.09           N  
ANISOU 8281  N   SER B 332     5699   5207   5465    385     77    213       N  
ATOM   8282  CA  SER B 332       1.030  10.346 -21.221  1.00 41.53           C  
ANISOU 8282  CA  SER B 332     5468   5032   5277    367     71    211       C  
ATOM   8283  C   SER B 332       2.421   9.744 -21.003  1.00 40.11           C  
ANISOU 8283  C   SER B 332     5283   4859   5098    360     90    219       C  
ATOM   8284  O   SER B 332       3.135   9.417 -21.955  1.00 38.07           O  
ANISOU 8284  O   SER B 332     5048   4585   4829    371    101    227       O  
ATOM   8285  CB  SER B 332      -0.029   9.254 -21.209  1.00 40.56           C  
ANISOU 8285  CB  SER B 332     5342   4915   5151    369     42    209       C  
ATOM   8286  OG  SER B 332       0.383   8.191 -22.033  1.00 44.72           O  
ANISOU 8286  OG  SER B 332     5890   5433   5667    378     40    216       O  
ATOM   8287  N   LEU B 333       2.787   9.621 -19.731  1.00 38.49           N  
ANISOU 8287  N   LEU B 333     5044   4675   4904    341     96    216       N  
ATOM   8288  CA  LEU B 333       4.059   9.055 -19.326  1.00 37.58           C  
ANISOU 8288  CA  LEU B 333     4916   4568   4791    332    113    223       C  
ATOM   8289  C   LEU B 333       3.789   8.080 -18.208  1.00 38.33           C  
ANISOU 8289  C   LEU B 333     4982   4687   4893    319    100    222       C  
ATOM   8290  O   LEU B 333       3.176   8.422 -17.180  1.00 38.29           O  
ANISOU 8290  O   LEU B 333     4952   4697   4897    307     92    214       O  
ATOM   8291  CB  LEU B 333       5.030  10.141 -18.849  1.00 37.14           C  
ANISOU 8291  CB  LEU B 333     4850   4517   4744    322    138    222       C  
ATOM   8292  CG  LEU B 333       6.353   9.691 -18.210  1.00 36.37           C  
ANISOU 8292  CG  LEU B 333     4733   4434   4651    310    156    228       C  
ATOM   8293  CD1 LEU B 333       7.153   8.801 -19.147  1.00 35.81           C  
ANISOU 8293  CD1 LEU B 333     4684   4351   4570    322    164    240       C  
ATOM   8294  CD2 LEU B 333       7.192  10.884 -17.773  1.00 36.20           C  
ANISOU 8294  CD2 LEU B 333     4700   4414   4638    300    179    224       C  
ATOM   8295  N   SER B 334       4.263   6.862 -18.418  1.00 37.85           N  
ANISOU 8295  N   SER B 334     4925   4627   4827    322     99    231       N  
ATOM   8296  CA  SER B 334       4.000   5.771 -17.514  1.00 36.53           C  
ANISOU 8296  CA  SER B 334     4734   4479   4665    312     87    231       C  
ATOM   8297  C   SER B 334       5.334   5.205 -17.042  1.00 36.07           C  
ANISOU 8297  C   SER B 334     4662   4432   4608    304    105    240       C  
ATOM   8298  O   SER B 334       6.173   4.798 -17.853  1.00 34.81           O  
ANISOU 8298  O   SER B 334     4522   4260   4441    313    117    249       O  
ATOM   8299  CB  SER B 334       3.181   4.716 -18.241  1.00 37.57           C  
ANISOU 8299  CB  SER B 334     4884   4601   4788    323     66    233       C  
ATOM   8300  OG  SER B 334       2.100   4.278 -17.447  1.00 41.81           O  
ANISOU 8300  OG  SER B 334     5401   5152   5332    315     45    227       O  
ATOM   8301  N   ILE B 335       5.537   5.229 -15.728  1.00 35.41           N  
ANISOU 8301  N   ILE B 335     4545   4372   4535    288    108    237       N  
ATOM   8302  CA  ILE B 335       6.734   4.674 -15.091  1.00 35.58           C  
ANISOU 8302  CA  ILE B 335     4549   4410   4559    279    123    245       C  
ATOM   8303  C   ILE B 335       6.299   3.609 -14.080  1.00 35.32           C  
ANISOU 8303  C   ILE B 335     4492   4397   4531    271    109    246       C  
ATOM   8304  O   ILE B 335       5.839   3.938 -12.986  1.00 35.21           O  
ANISOU 8304  O   ILE B 335     4451   4400   4524    259    103    239       O  
ATOM   8305  CB  ILE B 335       7.537   5.770 -14.358  1.00 35.41           C  
ANISOU 8305  CB  ILE B 335     4507   4399   4546    267    141    241       C  
ATOM   8306  CG1 ILE B 335       7.816   6.958 -15.280  1.00 35.20           C  
ANISOU 8306  CG1 ILE B 335     4504   4351   4516    274    155    239       C  
ATOM   8307  CG2 ILE B 335       8.815   5.209 -13.747  1.00 35.07           C  
ANISOU 8307  CG2 ILE B 335     4445   4373   4505    259    156    250       C  
ATOM   8308  CD1 ILE B 335       8.570   6.600 -16.541  1.00 37.77           C  
ANISOU 8308  CD1 ILE B 335     4860   4658   4834    289    167    250       C  
ATOM   8309  N   ILE B 336       6.432   2.340 -14.454  1.00 34.93           N  
ANISOU 8309  N   ILE B 336     4451   4344   4476    278    105    255       N  
ATOM   8310  CA  ILE B 336       5.979   1.227 -13.608  1.00 35.56           C  
ANISOU 8310  CA  ILE B 336     4510   4441   4559    271     92    257       C  
ATOM   8311  C   ILE B 336       7.155   0.331 -13.215  1.00 35.17           C  
ANISOU 8311  C   ILE B 336     4449   4403   4509    269    106    269       C  
ATOM   8312  O   ILE B 336       7.949  -0.065 -14.070  1.00 34.84           O  
ANISOU 8312  O   ILE B 336     4427   4349   4461    278    118    278       O  
ATOM   8313  CB  ILE B 336       4.869   0.392 -14.303  1.00 35.71           C  
ANISOU 8313  CB  ILE B 336     4549   4446   4574    281     71    256       C  
ATOM   8314  CG1 ILE B 336       3.643   1.265 -14.588  1.00 36.64           C  
ANISOU 8314  CG1 ILE B 336     4675   4555   4692    284     56    244       C  
ATOM   8315  CG2 ILE B 336       4.447  -0.790 -13.443  1.00 34.88           C  
ANISOU 8315  CG2 ILE B 336     4423   4357   4473    275     60    259       C  
ATOM   8316  CD1 ILE B 336       2.852   0.828 -15.799  1.00 37.23           C  
ANISOU 8316  CD1 ILE B 336     4779   4607   4758    298     40    244       C  
ATOM   8317  N   ARG B 337       7.253   0.028 -11.919  1.00 34.75           N  
ANISOU 8317  N   ARG B 337     4363   4374   4462    256    105    270       N  
ATOM   8318  CA  ARG B 337       8.299  -0.854 -11.356  1.00 34.74           C  
ANISOU 8318  CA  ARG B 337     4347   4389   4462    253    117    281       C  
ATOM   8319  C   ARG B 337       9.726  -0.529 -11.819  1.00 34.84           C  
ANISOU 8319  C   ARG B 337     4367   4398   4473    256    140    289       C  
ATOM   8320  O   ARG B 337      10.511  -1.415 -12.134  1.00 36.51           O  
ANISOU 8320  O   ARG B 337     4584   4608   4681    262    150    301       O  
ATOM   8321  CB  ARG B 337       7.974  -2.320 -11.617  1.00 33.90           C  
ANISOU 8321  CB  ARG B 337     4248   4278   4352    260    108    289       C  
ATOM   8322  CG  ARG B 337       7.031  -2.957 -10.620  1.00 35.30           C  
ANISOU 8322  CG  ARG B 337     4405   4471   4535    253     92    286       C  
ATOM   8323  CD  ARG B 337       6.153  -3.976 -11.312  1.00 36.84           C  
ANISOU 8323  CD  ARG B 337     4620   4651   4727    262     77    288       C  
ATOM   8324  NE  ARG B 337       6.791  -4.397 -12.549  1.00 41.98           N  
ANISOU 8324  NE  ARG B 337     5300   5281   5368    274     86    296       N  
ATOM   8325  CZ  ARG B 337       6.153  -4.741 -13.661  1.00 43.31           C  
ANISOU 8325  CZ  ARG B 337     5498   5427   5531    285     75    294       C  
ATOM   8326  NH1 ARG B 337       6.857  -5.092 -14.735  1.00 44.66           N  
ANISOU 8326  NH1 ARG B 337     5695   5580   5693    297     86    301       N  
ATOM   8327  NH2 ARG B 337       4.828  -4.740 -13.702  1.00 44.06           N  
ANISOU 8327  NH2 ARG B 337     5595   5517   5628    285     55    284       N  
ATOM   8328  N   CYS B 338      10.047   0.754 -11.858  1.00 34.96           N  
ANISOU 8328  N   CYS B 338     4380   4410   4490    251    150    282       N  
ATOM   8329  CA  CYS B 338      11.378   1.201 -12.206  1.00 34.96           C  
ANISOU 8329  CA  CYS B 338     4383   4408   4490    252    172    288       C  
ATOM   8330  C   CYS B 338      12.159   1.477 -10.929  1.00 35.32           C  
ANISOU 8330  C   CYS B 338     4394   4482   4544    237    181    288       C  
ATOM   8331  O   CYS B 338      11.764   0.994  -9.864  1.00 34.26           O  
ANISOU 8331  O   CYS B 338     4236   4368   4412    228    171    287       O  
ATOM   8332  CB  CYS B 338      11.295   2.415 -13.131  1.00 35.58           C  
ANISOU 8332  CB  CYS B 338     4485   4466   4568    257    178    282       C  
ATOM   8333  SG  CYS B 338      10.462   1.995 -14.686  1.00 37.04           S  
ANISOU 8333  SG  CYS B 338     4712   4618   4741    277    167    283       S  
ATOM   8334  N   GLN B 339      13.255   2.236 -11.022  1.00 36.31           N  
ANISOU 8334  N   GLN B 339     4515   4607   4671    233    201    289       N  
ATOM   8335  CA  GLN B 339      14.243   2.281  -9.932  1.00 37.08           C  
ANISOU 8335  CA  GLN B 339     4582   4732   4775    220    211    292       C  
ATOM   8336  C   GLN B 339      14.800   3.658  -9.620  1.00 37.53           C  
ANISOU 8336  C   GLN B 339     4627   4794   4839    208    224    283       C  
ATOM   8337  O   GLN B 339      15.931   3.791  -9.127  1.00 37.07           O  
ANISOU 8337  O   GLN B 339     4549   4750   4784    200    238    286       O  
ATOM   8338  CB  GLN B 339      15.381   1.310 -10.226  1.00 38.31           C  
ANISOU 8338  CB  GLN B 339     4737   4889   4927    227    225    308       C  
ATOM   8339  CG  GLN B 339      14.939  -0.145 -10.219  1.00 39.50           C  
ANISOU 8339  CG  GLN B 339     4892   5042   5074    235    213    318       C  
ATOM   8340  CD  GLN B 339      16.015  -1.097 -10.692  1.00 41.41           C  
ANISOU 8340  CD  GLN B 339     5140   5281   5312    244    228    335       C  
ATOM   8341  OE1 GLN B 339      15.711  -2.198 -11.143  1.00 42.53           O  
ANISOU 8341  OE1 GLN B 339     5296   5413   5448    255    222    343       O  
ATOM   8342  NE2 GLN B 339      17.281  -0.685 -10.586  1.00 41.30           N  
ANISOU 8342  NE2 GLN B 339     5115   5275   5302    240    247    340       N  
ATOM   8343  N   LEU B 340      13.986   4.671  -9.909  1.00 38.38           N  
ANISOU 8343  N   LEU B 340     4747   4888   4947    208    218    270       N  
ATOM   8344  CA  LEU B 340      14.269   6.076  -9.597  1.00 39.60           C  
ANISOU 8344  CA  LEU B 340     4892   5044   5108    196    229    259       C  
ATOM   8345  C   LEU B 340      14.763   6.253  -8.172  1.00 40.13           C  
ANISOU 8345  C   LEU B 340     4922   5142   5181    178    231    254       C  
ATOM   8346  O   LEU B 340      14.159   5.735  -7.225  1.00 41.00           O  
ANISOU 8346  O   LEU B 340     5014   5272   5292    173    216    252       O  
ATOM   8347  CB  LEU B 340      12.991   6.916  -9.777  1.00 39.64           C  
ANISOU 8347  CB  LEU B 340     4910   5037   5114    197    217    246       C  
ATOM   8348  CG  LEU B 340      12.580   7.667 -11.048  1.00 37.17           C  
ANISOU 8348  CG  LEU B 340     4630   4693   4797    209    220    243       C  
ATOM   8349  CD1 LEU B 340      13.355   7.256 -12.288  1.00 37.18           C  
ANISOU 8349  CD1 LEU B 340     4658   4675   4794    223    233    255       C  
ATOM   8350  CD2 LEU B 340      11.091   7.467 -11.251  1.00 37.22           C  
ANISOU 8350  CD2 LEU B 340     4650   4692   4801    216    198    237       C  
ATOM   8351  N   LYS B 341      15.860   6.983  -8.025  1.00 41.17           N  
ANISOU 8351  N   LYS B 341     5043   5279   5318    170    249    253       N  
ATOM   8352  CA  LYS B 341      16.399   7.299  -6.710  1.00 42.82           C  
ANISOU 8352  CA  LYS B 341     5218   5518   5533    152    251    247       C  
ATOM   8353  C   LYS B 341      15.868   8.653  -6.248  1.00 42.42           C  
ANISOU 8353  C   LYS B 341     5161   5466   5487    140    250    229       C  
ATOM   8354  O   LYS B 341      16.030   9.027  -5.085  1.00 41.55           O  
ANISOU 8354  O   LYS B 341     5023   5380   5381    124    249    220       O  
ATOM   8355  CB  LYS B 341      17.933   7.309  -6.737  1.00 46.58           C  
ANISOU 8355  CB  LYS B 341     5682   6001   6013    148    271    254       C  
ATOM   8356  CG  LYS B 341      18.573   6.004  -7.193  1.00 50.81           C  
ANISOU 8356  CG  LYS B 341     6223   6537   6544    160    274    273       C  
ATOM   8357  CD  LYS B 341      20.076   6.000  -6.944  1.00 53.79           C  
ANISOU 8357  CD  LYS B 341     6582   6929   6927    154    292    280       C  
ATOM   8358  CE  LYS B 341      20.746   4.762  -7.534  1.00 57.91           C  
ANISOU 8358  CE  LYS B 341     7111   7447   7444    168    299    300       C  
ATOM   8359  NZ  LYS B 341      20.275   3.462  -6.959  1.00 60.62           N  
ANISOU 8359  NZ  LYS B 341     7445   7805   7781    172    283    308       N  
ATOM   8360  N   GLN B 342      15.235   9.372  -7.174  1.00 40.99           N  
ANISOU 8360  N   GLN B 342     5007   5259   5306    148    251    224       N  
ATOM   8361  CA  GLN B 342      14.732  10.718  -6.943  1.00 42.55           C  
ANISOU 8361  CA  GLN B 342     5206   5452   5510    139    253    208       C  
ATOM   8362  C   GLN B 342      13.428  10.900  -7.685  1.00 41.80           C  
ANISOU 8362  C   GLN B 342     5137   5334   5411    151    241    204       C  
ATOM   8363  O   GLN B 342      13.228  10.302  -8.746  1.00 42.67           O  
ANISOU 8363  O   GLN B 342     5272   5426   5515    167    238    214       O  
ATOM   8364  CB  GLN B 342      15.715  11.741  -7.497  1.00 47.24           C  
ANISOU 8364  CB  GLN B 342     5807   6032   6109    135    276    205       C  
ATOM   8365  CG  GLN B 342      16.587  12.454  -6.478  1.00 51.81           C  
ANISOU 8365  CG  GLN B 342     6356   6632   6696    115    287    196       C  
ATOM   8366  CD  GLN B 342      16.966  13.853  -6.943  1.00 54.33           C  
ANISOU 8366  CD  GLN B 342     6685   6933   7022    110    305    187       C  
ATOM   8367  OE1 GLN B 342      17.189  14.085  -8.136  1.00 52.43           O  
ANISOU 8367  OE1 GLN B 342     6471   6666   6781    122    317    193       O  
ATOM   8368  NE2 GLN B 342      17.021  14.800  -6.000  1.00 55.89           N  
ANISOU 8368  NE2 GLN B 342     6863   7144   7227     92    309    172       N  
ATOM   8369  N   PHE B 343      12.539  11.731  -7.154  1.00 40.17           N  
ANISOU 8369  N   PHE B 343     4924   5129   5207    144    234    191       N  
ATOM   8370  CA  PHE B 343      11.350  12.096  -7.921  1.00 39.97           C  
ANISOU 8370  CA  PHE B 343     4925   5082   5180    156    224    187       C  
ATOM   8371  C   PHE B 343      11.797  12.938  -9.123  1.00 40.67           C  
ANISOU 8371  C   PHE B 343     5041   5143   5269    165    241    188       C  
ATOM   8372  O   PHE B 343      12.676  13.799  -8.989  1.00 39.23           O  
ANISOU 8372  O   PHE B 343     4852   4961   5093    155    260    183       O  
ATOM   8373  CB  PHE B 343      10.329  12.841  -7.059  1.00 38.41           C  
ANISOU 8373  CB  PHE B 343     4714   4891   4986    147    214    172       C  
ATOM   8374  CG  PHE B 343       8.951  12.902  -7.657  1.00 37.64           C  
ANISOU 8374  CG  PHE B 343     4637   4777   4885    159    199    170       C  
ATOM   8375  CD1 PHE B 343       8.050  11.852  -7.484  1.00 36.69           C  
ANISOU 8375  CD1 PHE B 343     4515   4663   4762    165    178    174       C  
ATOM   8376  CD2 PHE B 343       8.547  14.013  -8.391  1.00 38.32           C  
ANISOU 8376  CD2 PHE B 343     4744   4840   4973    165    205    164       C  
ATOM   8377  CE1 PHE B 343       6.772  11.906  -8.030  1.00 35.60           C  
ANISOU 8377  CE1 PHE B 343     4394   4509   4621    177    163    172       C  
ATOM   8378  CE2 PHE B 343       7.272  14.071  -8.945  1.00 37.99           C  
ANISOU 8378  CE2 PHE B 343     4721   4784   4929    178    190    162       C  
ATOM   8379  CZ  PHE B 343       6.384  13.018  -8.759  1.00 36.75           C  
ANISOU 8379  CZ  PHE B 343     4560   4634   4768    183    169    166       C  
ATOM   8380  N   PRO B 344      11.218  12.669 -10.306  1.00 42.47           N  
ANISOU 8380  N   PRO B 344     5298   5347   5490    183    235    194       N  
ATOM   8381  CA  PRO B 344      11.633  13.333 -11.545  1.00 44.49           C  
ANISOU 8381  CA  PRO B 344     5583   5575   5744    194    251    197       C  
ATOM   8382  C   PRO B 344      11.348  14.828 -11.595  1.00 46.87           C  
ANISOU 8382  C   PRO B 344     5891   5865   6051    190    261    185       C  
ATOM   8383  O   PRO B 344      10.320  15.294 -11.100  1.00 46.80           O  
ANISOU 8383  O   PRO B 344     5877   5860   6045    186    249    175       O  
ATOM   8384  CB  PRO B 344      10.802  12.625 -12.622  1.00 44.62           C  
ANISOU 8384  CB  PRO B 344     5628   5573   5750    214    237    205       C  
ATOM   8385  CG  PRO B 344      10.395  11.326 -12.014  1.00 44.50           C  
ANISOU 8385  CG  PRO B 344     5598   5577   5732    213    218    209       C  
ATOM   8386  CD  PRO B 344      10.207  11.627 -10.560  1.00 42.59           C  
ANISOU 8386  CD  PRO B 344     5323   5360   5498    194    214    199       C  
ATOM   8387  N   THR B 345      12.282  15.570 -12.174  1.00 51.73           N  
ANISOU 8387  N   THR B 345     6516   6466   6670    190    284    187       N  
ATOM   8388  CA  THR B 345      12.003  16.919 -12.649  1.00 55.41           C  
ANISOU 8388  CA  THR B 345     6999   6912   7140    192    295    179       C  
ATOM   8389  C   THR B 345      11.281  16.798 -13.984  1.00 55.79           C  
ANISOU 8389  C   THR B 345     7084   6934   7179    215    289    186       C  
ATOM   8390  O   THR B 345      11.798  16.195 -14.933  1.00 55.30           O  
ANISOU 8390  O   THR B 345     7041   6860   7110    227    295    198       O  
ATOM   8391  CB  THR B 345      13.292  17.737 -12.840  1.00 55.06           C  
ANISOU 8391  CB  THR B 345     6955   6862   7104    184    324    178       C  
ATOM   8392  OG1 THR B 345      14.422  16.897 -12.576  1.00 56.09           O  
ANISOU 8392  OG1 THR B 345     7069   7007   7234    178    330    187       O  
ATOM   8393  CG2 THR B 345      13.325  18.906 -11.887  1.00 54.13           C  
ANISOU 8393  CG2 THR B 345     6817   6753   6997    165    332    163       C  
ATOM   8394  N   LEU B 346      10.076  17.352 -14.041  1.00 55.45           N  
ANISOU 8394  N   LEU B 346     7049   6883   7134    220    277    178       N  
ATOM   8395  CA  LEU B 346       9.289  17.374 -15.270  1.00 55.94           C  
ANISOU 8395  CA  LEU B 346     7145   6921   7187    241    270    183       C  
ATOM   8396  C   LEU B 346       8.599  18.714 -15.441  1.00 58.70           C  
ANISOU 8396  C   LEU B 346     7505   7256   7541    244    274    174       C  
ATOM   8397  O   LEU B 346       8.016  19.249 -14.489  1.00 58.98           O  
ANISOU 8397  O   LEU B 346     7522   7304   7583    232    269    163       O  
ATOM   8398  CB  LEU B 346       8.238  16.269 -15.252  1.00 55.31           C  
ANISOU 8398  CB  LEU B 346     7066   6849   7101    249    241    186       C  
ATOM   8399  CG  LEU B 346       8.648  14.835 -15.569  1.00 54.19           C  
ANISOU 8399  CG  LEU B 346     6927   6712   6951    255    234    198       C  
ATOM   8400  CD1 LEU B 346       7.566  13.884 -15.080  1.00 51.29           C  
ANISOU 8400  CD1 LEU B 346     6549   6357   6580    256    207    196       C  
ATOM   8401  CD2 LEU B 346       8.880  14.677 -17.065  1.00 54.54           C  
ANISOU 8401  CD2 LEU B 346     7007   6729   6984    276    241    208       C  
ATOM   8402  N   ASP B 347       8.671  19.263 -16.651  1.00 63.59           N  
ANISOU 8402  N   ASP B 347     8156   7849   8155    260    286    179       N  
ATOM   8403  CA  ASP B 347       7.906  20.470 -16.972  1.00 65.45           C  
ANISOU 8403  CA  ASP B 347     8407   8068   8393    267    289    172       C  
ATOM   8404  C   ASP B 347       7.263  20.447 -18.362  1.00 62.49           C  
ANISOU 8404  C   ASP B 347     8068   7668   8005    292    283    180       C  
ATOM   8405  O   ASP B 347       6.808  21.484 -18.848  1.00 69.88           O  
ANISOU 8405  O   ASP B 347     9022   8586   8941    301    290    177       O  
ATOM   8406  CB  ASP B 347       8.743  21.735 -16.757  1.00 69.26           C  
ANISOU 8406  CB  ASP B 347     8885   8544   8886    255    318    166       C  
ATOM   8407  CG  ASP B 347       9.997  21.751 -17.592  1.00 75.48           C  
ANISOU 8407  CG  ASP B 347     9688   9316   9671    260    341    175       C  
ATOM   8408  OD1 ASP B 347      10.817  22.673 -17.396  1.00 80.79           O  
ANISOU 8408  OD1 ASP B 347    10356   9985  10354    249    365    171       O  
ATOM   8409  OD2 ASP B 347      10.165  20.846 -18.440  1.00 77.73           O  
ANISOU 8409  OD2 ASP B 347     9991   9594   9946    275    336    187       O  
ATOM   8410  N   LEU B 348       7.229  19.266 -18.982  1.00 55.22           N  
ANISOU 8410  N   LEU B 348     7159   6746   7073    303    269    190       N  
ATOM   8411  CA  LEU B 348       6.507  19.039 -20.238  1.00 51.60           C  
ANISOU 8411  CA  LEU B 348     6735   6268   6602    327    258    196       C  
ATOM   8412  C   LEU B 348       5.140  19.729 -20.245  1.00 49.93           C  
ANISOU 8412  C   LEU B 348     6528   6051   6390    334    243    189       C  
ATOM   8413  O   LEU B 348       4.265  19.415 -19.437  1.00 48.66           O  
ANISOU 8413  O   LEU B 348     6347   5906   6232    327    222    182       O  
ATOM   8414  CB  LEU B 348       6.330  17.544 -20.511  1.00 50.72           C  
ANISOU 8414  CB  LEU B 348     6626   6163   6480    334    238    204       C  
ATOM   8415  CG  LEU B 348       7.585  16.674 -20.547  1.00 52.83           C  
ANISOU 8415  CG  LEU B 348     6890   6436   6747    329    250    213       C  
ATOM   8416  CD1 LEU B 348       7.210  15.252 -20.925  1.00 51.24           C  
ANISOU 8416  CD1 LEU B 348     6696   6238   6535    338    228    219       C  
ATOM   8417  CD2 LEU B 348       8.623  17.238 -21.511  1.00 53.84           C  
ANISOU 8417  CD2 LEU B 348     7042   6543   6872    338    277    220       C  
ATOM   8418  N   PRO B 349       4.957  20.679 -21.167  1.00 47.92           N  
ANISOU 8418  N   PRO B 349     6301   5773   6131    349    254    191       N  
ATOM   8419  CA  PRO B 349       3.773  21.501 -21.068  1.00 45.94           C  
ANISOU 8419  CA  PRO B 349     6053   5519   5883    355    244    184       C  
ATOM   8420  C   PRO B 349       2.488  20.839 -21.606  1.00 43.69           C  
ANISOU 8420  C   PRO B 349     5780   5232   5587    371    213    186       C  
ATOM   8421  O   PRO B 349       1.388  21.334 -21.330  1.00 43.06           O  
ANISOU 8421  O   PRO B 349     5695   5153   5510    374    200    179       O  
ATOM   8422  CB  PRO B 349       4.165  22.754 -21.863  1.00 46.38           C  
ANISOU 8422  CB  PRO B 349     6134   5550   5939    365    269    186       C  
ATOM   8423  CG  PRO B 349       5.129  22.256 -22.887  1.00 46.36           C  
ANISOU 8423  CG  PRO B 349     6154   5533   5926    376    282    197       C  
ATOM   8424  CD  PRO B 349       5.848  21.098 -22.269  1.00 46.98           C  
ANISOU 8424  CD  PRO B 349     6211   5632   6007    362    277    199       C  
ATOM   8425  N   PHE B 350       2.614  19.729 -22.334  1.00 41.24           N  
ANISOU 8425  N   PHE B 350     5485   4918   5265    382    202    194       N  
ATOM   8426  CA  PHE B 350       1.432  19.092 -22.950  1.00 40.79           C  
ANISOU 8426  CA  PHE B 350     5442   4859   5197    398    173    196       C  
ATOM   8427  C   PHE B 350       1.016  17.725 -22.373  1.00 40.24           C  
ANISOU 8427  C   PHE B 350     5353   4809   5127    390    148    195       C  
ATOM   8428  O   PHE B 350       0.067  17.094 -22.858  1.00 39.50           O  
ANISOU 8428  O   PHE B 350     5269   4713   5025    401    123    196       O  
ATOM   8429  CB  PHE B 350       1.569  19.057 -24.473  1.00 39.81           C  
ANISOU 8429  CB  PHE B 350     5358   4710   5057    421    176    205       C  
ATOM   8430  CG  PHE B 350       1.718  20.417 -25.084  1.00 41.79           C  
ANISOU 8430  CG  PHE B 350     5630   4941   5307    432    197    206       C  
ATOM   8431  CD1 PHE B 350       2.953  20.862 -25.539  1.00 41.98           C  
ANISOU 8431  CD1 PHE B 350     5667   4952   5331    433    227    212       C  
ATOM   8432  CD2 PHE B 350       0.628  21.279 -25.169  1.00 44.16           C  
ANISOU 8432  CD2 PHE B 350     5935   5236   5608    441    188    202       C  
ATOM   8433  CE1 PHE B 350       3.096  22.127 -26.087  1.00 41.95           C  
ANISOU 8433  CE1 PHE B 350     5683   4928   5327    443    248    214       C  
ATOM   8434  CE2 PHE B 350       0.767  22.550 -25.716  1.00 43.97           C  
ANISOU 8434  CE2 PHE B 350     5929   5191   5583    452    209    203       C  
ATOM   8435  CZ  PHE B 350       2.004  22.972 -26.177  1.00 42.47           C  
ANISOU 8435  CZ  PHE B 350     5754   4988   5393    452    239    209       C  
ATOM   8436  N   LEU B 351       1.700  17.310 -21.307  1.00 40.21           N  
ANISOU 8436  N   LEU B 351     5320   4823   5132    369    155    193       N  
ATOM   8437  CA  LEU B 351       1.437  16.047 -20.618  1.00 40.43           C  
ANISOU 8437  CA  LEU B 351     5327   4872   5163    360    136    192       C  
ATOM   8438  C   LEU B 351       0.100  16.039 -19.860  1.00 40.03           C  
ANISOU 8438  C   LEU B 351     5257   4834   5118    355    112    183       C  
ATOM   8439  O   LEU B 351      -0.077  16.784 -18.891  1.00 39.21           O  
ANISOU 8439  O   LEU B 351     5130   4740   5025    342    118    176       O  
ATOM   8440  CB  LEU B 351       2.594  15.746 -19.660  1.00 39.80           C  
ANISOU 8440  CB  LEU B 351     5222   4808   5091    340    152    192       C  
ATOM   8441  CG  LEU B 351       2.713  14.340 -19.072  1.00 40.56           C  
ANISOU 8441  CG  LEU B 351     5299   4923   5187    332    138    195       C  
ATOM   8442  CD1 LEU B 351       3.049  13.300 -20.137  1.00 39.96           C  
ANISOU 8442  CD1 LEU B 351     5247   4835   5098    345    134    206       C  
ATOM   8443  CD2 LEU B 351       3.766  14.346 -17.975  1.00 39.89           C  
ANISOU 8443  CD2 LEU B 351     5186   4856   5113    311    155    194       C  
ATOM   8444  N   LYS B 352      -0.828  15.190 -20.304  1.00 39.61           N  
ANISOU 8444  N   LYS B 352     5211   4779   5057    365     87    185       N  
ATOM   8445  CA  LYS B 352      -2.152  15.071 -19.682  1.00 40.46           C  
ANISOU 8445  CA  LYS B 352     5301   4898   5171    362     63    178       C  
ATOM   8446  C   LYS B 352      -2.186  14.065 -18.534  1.00 38.46           C  
ANISOU 8446  C   LYS B 352     5016   4668   4925    345     53    175       C  
ATOM   8447  O   LYS B 352      -2.993  14.191 -17.605  1.00 37.95           O  
ANISOU 8447  O   LYS B 352     4929   4618   4871    336     42    168       O  
ATOM   8448  CB  LYS B 352      -3.202  14.626 -20.700  1.00 43.02           C  
ANISOU 8448  CB  LYS B 352     5648   5212   5485    380     39    180       C  
ATOM   8449  CG  LYS B 352      -3.384  15.519 -21.907  1.00 47.44           C  
ANISOU 8449  CG  LYS B 352     6240   5748   6035    401     44    182       C  
ATOM   8450  CD  LYS B 352      -4.620  15.083 -22.683  1.00 51.20           C  
ANISOU 8450  CD  LYS B 352     6731   6218   6502    417     15    182       C  
ATOM   8451  CE  LYS B 352      -4.967  16.072 -23.788  1.00 55.99           C  
ANISOU 8451  CE  LYS B 352     7368   6805   7100    437     18    184       C  
ATOM   8452  NZ  LYS B 352      -4.798  17.501 -23.374  1.00 59.22           N  
ANISOU 8452  NZ  LYS B 352     7772   7210   7518    434     39    181       N  
ATOM   8453  N   SER B 353      -1.326  13.058 -18.620  1.00 36.92           N  
ANISOU 8453  N   SER B 353     4822   4477   4726    342     57    182       N  
ATOM   8454  CA  SER B 353      -1.436  11.886 -17.763  1.00 36.56           C  
ANISOU 8454  CA  SER B 353     4753   4451   4686    330     45    182       C  
ATOM   8455  C   SER B 353      -0.091  11.377 -17.271  1.00 35.50           C  
ANISOU 8455  C   SER B 353     4606   4327   4553    318     63    188       C  
ATOM   8456  O   SER B 353       0.835  11.186 -18.054  1.00 35.94           O  
ANISOU 8456  O   SER B 353     4681   4371   4601    325     76    195       O  
ATOM   8457  CB  SER B 353      -2.168  10.775 -18.511  1.00 36.59           C  
ANISOU 8457  CB  SER B 353     4771   4449   4681    341     22    185       C  
ATOM   8458  OG  SER B 353      -2.534   9.749 -17.612  1.00 37.74           O  
ANISOU 8458  OG  SER B 353     4893   4613   4833    330      8    184       O  
ATOM   8459  N   LEU B 354       0.022  11.163 -15.968  1.00 34.69           N  
ANISOU 8459  N   LEU B 354     4473   4247   4461    301     64    184       N  
ATOM   8460  CA  LEU B 354       1.273  10.674 -15.413  1.00 35.19           C  
ANISOU 8460  CA  LEU B 354     4521   4322   4526    289     80    189       C  
ATOM   8461  C   LEU B 354       1.049   9.564 -14.401  1.00 36.47           C  
ANISOU 8461  C   LEU B 354     4657   4506   4693    278     67    190       C  
ATOM   8462  O   LEU B 354       0.337   9.740 -13.401  1.00 35.85           O  
ANISOU 8462  O   LEU B 354     4556   4443   4623    268     59    182       O  
ATOM   8463  CB  LEU B 354       2.100  11.806 -14.798  1.00 34.57           C  
ANISOU 8463  CB  LEU B 354     4429   4249   4454    278    102    185       C  
ATOM   8464  CG  LEU B 354       3.408  11.401 -14.121  1.00 34.06           C  
ANISOU 8464  CG  LEU B 354     4347   4200   4392    265    119    189       C  
ATOM   8465  CD1 LEU B 354       4.426  10.992 -15.167  1.00 34.50           C  
ANISOU 8465  CD1 LEU B 354     4426   4242   4440    275    132    200       C  
ATOM   8466  CD2 LEU B 354       3.946  12.542 -13.282  1.00 34.68           C  
ANISOU 8466  CD2 LEU B 354     4408   4288   4481    250    136    181       C  
ATOM   8467  N   THR B 355       1.659   8.418 -14.695  1.00 36.41           N  
ANISOU 8467  N   THR B 355     4654   4499   4679    281     68    199       N  
ATOM   8468  CA  THR B 355       1.705   7.288 -13.779  1.00 36.99           C  
ANISOU 8468  CA  THR B 355     4705   4593   4757    271     61    201       C  
ATOM   8469  C   THR B 355       3.166   7.029 -13.392  1.00 36.10           C  
ANISOU 8469  C   THR B 355     4581   4490   4645    263     81    209       C  
ATOM   8470  O   THR B 355       4.033   6.830 -14.248  1.00 35.39           O  
ANISOU 8470  O   THR B 355     4510   4387   4547    271     93    217       O  
ATOM   8471  CB  THR B 355       1.059   6.020 -14.403  1.00 38.28           C  
ANISOU 8471  CB  THR B 355     4881   4749   4914    281     42    206       C  
ATOM   8472  OG1 THR B 355      -0.349   6.224 -14.583  1.00 38.50           O  
ANISOU 8472  OG1 THR B 355     4912   4771   4943    286     21    199       O  
ATOM   8473  CG2 THR B 355       1.275   4.795 -13.522  1.00 37.17           C  
ANISOU 8473  CG2 THR B 355     4718   4627   4776    271     38    211       C  
ATOM   8474  N   LEU B 356       3.428   7.077 -12.095  1.00 35.83           N  
ANISOU 8474  N   LEU B 356     4516   4478   4618    247     85    206       N  
ATOM   8475  CA  LEU B 356       4.697   6.659 -11.536  1.00 35.87           C  
ANISOU 8475  CA  LEU B 356     4505   4498   4623    239    101    212       C  
ATOM   8476  C   LEU B 356       4.332   5.772 -10.351  1.00 36.81           C  
ANISOU 8476  C   LEU B 356     4596   4640   4747    229     90    213       C  
ATOM   8477  O   LEU B 356       3.905   6.257  -9.306  1.00 36.88           O  
ANISOU 8477  O   LEU B 356     4582   4665   4763    217     86    204       O  
ATOM   8478  CB  LEU B 356       5.505   7.864 -11.076  1.00 35.23           C  
ANISOU 8478  CB  LEU B 356     4413   4423   4548    228    120    207       C  
ATOM   8479  CG  LEU B 356       7.007   7.723 -10.835  1.00 35.77           C  
ANISOU 8479  CG  LEU B 356     4472   4501   4617    222    140    214       C  
ATOM   8480  CD1 LEU B 356       7.543   9.095 -10.468  1.00 36.33           C  
ANISOU 8480  CD1 LEU B 356     4535   4574   4694    212    157    206       C  
ATOM   8481  CD2 LEU B 356       7.355   6.725  -9.744  1.00 35.78           C  
ANISOU 8481  CD2 LEU B 356     4445   4527   4620    212    137    219       C  
ATOM   8482  N   THR B 357       4.477   4.467 -10.527  1.00 36.02           N  
ANISOU 8482  N   THR B 357     4499   4542   4643    233     84    222       N  
ATOM   8483  CA  THR B 357       3.963   3.540  -9.549  1.00 36.03           C  
ANISOU 8483  CA  THR B 357     4478   4562   4649    226     72    223       C  
ATOM   8484  C   THR B 357       4.873   2.330  -9.334  1.00 36.73           C  
ANISOU 8484  C   THR B 357     4559   4661   4734    226     79    235       C  
ATOM   8485  O   THR B 357       5.691   1.974 -10.196  1.00 35.61           O  
ANISOU 8485  O   THR B 357     4436   4507   4587    235     89    244       O  
ATOM   8486  CB  THR B 357       2.506   3.133  -9.879  1.00 35.62           C  
ANISOU 8486  CB  THR B 357     4435   4501   4597    233     50    219       C  
ATOM   8487  OG1 THR B 357       1.951   2.390  -8.788  1.00 36.93           O  
ANISOU 8487  OG1 THR B 357     4576   4685   4768    225     39    218       O  
ATOM   8488  CG2 THR B 357       2.439   2.304 -11.129  1.00 35.41           C  
ANISOU 8488  CG2 THR B 357     4437   4454   4563    247     44    226       C  
ATOM   8489  N   MET B 358       4.728   1.732  -8.152  1.00 36.90           N  
ANISOU 8489  N   MET B 358     4554   4705   4761    217     75    236       N  
ATOM   8490  CA  MET B 358       5.493   0.565  -7.723  1.00 37.78           C  
ANISOU 8490  CA  MET B 358     4654   4829   4870    215     80    248       C  
ATOM   8491  C   MET B 358       7.003   0.740  -7.882  1.00 38.21           C  
ANISOU 8491  C   MET B 358     4708   4887   4922    215    101    256       C  
ATOM   8492  O   MET B 358       7.730  -0.221  -8.149  1.00 38.13           O  
ANISOU 8492  O   MET B 358     4701   4876   4908    220    108    268       O  
ATOM   8493  CB  MET B 358       5.006  -0.709  -8.417  1.00 37.60           C  
ANISOU 8493  CB  MET B 358     4647   4793   4843    226     70    255       C  
ATOM   8494  CG  MET B 358       3.500  -0.829  -8.506  1.00 38.30           C  
ANISOU 8494  CG  MET B 358     4741   4875   4936    228     49    247       C  
ATOM   8495  SD  MET B 358       3.054  -2.393  -9.271  1.00 40.54           S  
ANISOU 8495  SD  MET B 358     5043   5144   5215    239     37    255       S  
ATOM   8496  CE  MET B 358       3.250  -3.484  -7.861  1.00 40.46           C  
ANISOU 8496  CE  MET B 358     5001   5160   5210    229     39    263       C  
ATOM   8497  N   ASN B 359       7.465   1.972  -7.700  1.00 39.62           N  
ANISOU 8497  N   ASN B 359     4881   5068   5103    208    112    249       N  
ATOM   8498  CA  ASN B 359       8.888   2.267  -7.713  1.00 42.69           C  
ANISOU 8498  CA  ASN B 359     5265   5462   5491    205    132    254       C  
ATOM   8499  C   ASN B 359       9.611   1.427  -6.669  1.00 43.80           C  
ANISOU 8499  C   ASN B 359     5378   5628   5633    198    136    263       C  
ATOM   8500  O   ASN B 359       9.069   1.165  -5.599  1.00 42.39           O  
ANISOU 8500  O   ASN B 359     5178   5469   5457    190    127    259       O  
ATOM   8501  CB  ASN B 359       9.134   3.754  -7.462  1.00 42.35           C  
ANISOU 8501  CB  ASN B 359     5216   5421   5453    196    141    243       C  
ATOM   8502  CG  ASN B 359      10.503   4.205  -7.926  1.00 42.53           C  
ANISOU 8502  CG  ASN B 359     5243   5439   5475    196    163    248       C  
ATOM   8503  OD1 ASN B 359      11.300   4.713  -7.138  1.00 43.54           O  
ANISOU 8503  OD1 ASN B 359     5350   5585   5607    184    173    245       O  
ATOM   8504  ND2 ASN B 359      10.781   4.026  -9.213  1.00 41.99           N  
ANISOU 8504  ND2 ASN B 359     5204   5347   5402    209    169    255       N  
ATOM   8505  N   LYS B 360      10.824   0.999  -7.007  1.00 49.82           N  
ANISOU 8505  N   LYS B 360     6144   6392   6393    202    151    274       N  
ATOM   8506  CA  LYS B 360      11.622   0.089  -6.181  1.00 53.51           C  
ANISOU 8506  CA  LYS B 360     6588   6882   6860    198    157    285       C  
ATOM   8507  C   LYS B 360      12.020   0.692  -4.833  1.00 54.47           C  
ANISOU 8507  C   LYS B 360     6676   7031   6986    182    160    279       C  
ATOM   8508  O   LYS B 360      11.931   0.025  -3.807  1.00 61.79           O  
ANISOU 8508  O   LYS B 360     7582   7981   7914    177    155    282       O  
ATOM   8509  CB  LYS B 360      12.848  -0.405  -6.970  1.00 58.26           C  
ANISOU 8509  CB  LYS B 360     7202   7475   7459    207    173    299       C  
ATOM   8510  CG  LYS B 360      13.972  -1.056  -6.166  1.00 63.71           C  
ANISOU 8510  CG  LYS B 360     7867   8189   8149    202    184    310       C  
ATOM   8511  CD  LYS B 360      15.202  -0.154  -6.060  1.00 63.00           C  
ANISOU 8511  CD  LYS B 360     7767   8107   8063    195    202    309       C  
ATOM   8512  CE  LYS B 360      16.460  -0.941  -5.702  1.00 61.96           C  
ANISOU 8512  CE  LYS B 360     7618   7992   7931    196    214    324       C  
ATOM   8513  NZ  LYS B 360      16.929  -1.810  -6.816  1.00 60.70           N  
ANISOU 8513  NZ  LYS B 360     7482   7813   7766    212    223    338       N  
ATOM   8514  N   GLY B 361      12.429   1.952  -4.830  1.00 54.70           N  
ANISOU 8514  N   GLY B 361     6704   7060   7019    174    169    269       N  
ATOM   8515  CA  GLY B 361      12.902   2.582  -3.607  1.00 58.17           C  
ANISOU 8515  CA  GLY B 361     7113   7526   7463    159    174    262       C  
ATOM   8516  C   GLY B 361      11.843   3.315  -2.807  1.00 62.66           C  
ANISOU 8516  C   GLY B 361     7671   8102   8034    149    162    247       C  
ATOM   8517  O   GLY B 361      10.705   2.851  -2.676  1.00 67.38           O  
ANISOU 8517  O   GLY B 361     8272   8697   8631    152    147    245       O  
ATOM   8518  N   SER B 362      12.240   4.464  -2.265  1.00 61.48           N  
ANISOU 8518  N   SER B 362     7507   7962   7888    136    169    236       N  
ATOM   8519  CA  SER B 362      11.373   5.306  -1.453  1.00 56.28           C  
ANISOU 8519  CA  SER B 362     6838   7312   7233    126    161    221       C  
ATOM   8520  C   SER B 362      11.710   6.766  -1.747  1.00 54.38           C  
ANISOU 8520  C   SER B 362     6603   7061   6996    118    173    209       C  
ATOM   8521  O   SER B 362      12.460   7.424  -1.017  1.00 58.22           O  
ANISOU 8521  O   SER B 362     7070   7564   7486    105    182    203       O  
ATOM   8522  CB  SER B 362      11.536   4.966   0.031  1.00 55.31           C  
ANISOU 8522  CB  SER B 362     6683   7222   7110    114    157    220       C  
ATOM   8523  OG  SER B 362      11.055   6.008   0.859  1.00 57.31           O  
ANISOU 8523  OG  SER B 362     6923   7485   7366    101    155    204       O  
ATOM   8524  N   ILE B 363      11.166   7.251  -2.853  1.00 49.64           N  
ANISOU 8524  N   ILE B 363     6030   6433   6397    128    173    206       N  
ATOM   8525  CA  ILE B 363      11.367   8.631  -3.280  1.00 45.07           C  
ANISOU 8525  CA  ILE B 363     5461   5839   5822    123    184    196       C  
ATOM   8526  C   ILE B 363      10.441   9.559  -2.498  1.00 42.81           C  
ANISOU 8526  C   ILE B 363     5165   5559   5540    113    177    180       C  
ATOM   8527  O   ILE B 363       9.391   9.140  -1.993  1.00 40.49           O  
ANISOU 8527  O   ILE B 363     4866   5272   5245    114    162    178       O  
ATOM   8528  CB  ILE B 363      11.133   8.790  -4.803  1.00 43.43           C  
ANISOU 8528  CB  ILE B 363     5288   5599   5613    139    187    200       C  
ATOM   8529  CG1 ILE B 363       9.805   8.142  -5.223  1.00 43.65           C  
ANISOU 8529  CG1 ILE B 363     5332   5616   5637    151    169    202       C  
ATOM   8530  CG2 ILE B 363      12.267   8.148  -5.575  1.00 43.64           C  
ANISOU 8530  CG2 ILE B 363     5324   5619   5636    147    200    214       C  
ATOM   8531  CD1 ILE B 363       9.381   8.401  -6.656  1.00 43.84           C  
ANISOU 8531  CD1 ILE B 363     5390   5608   5658    166    168    204       C  
ATOM   8532  N   SER B 364      10.835  10.820  -2.395  1.00 41.11           N  
ANISOU 8532  N   SER B 364     4948   5341   5330    104    190    169       N  
ATOM   8533  CA  SER B 364       9.954  11.834  -1.839  1.00 41.93           C  
ANISOU 8533  CA  SER B 364     5047   5445   5437     96    185    153       C  
ATOM   8534  C   SER B 364       9.459  12.778  -2.941  1.00 41.64           C  
ANISOU 8534  C   SER B 364     5039   5378   5403    104    190    149       C  
ATOM   8535  O   SER B 364      10.156  13.010  -3.919  1.00 41.66           O  
ANISOU 8535  O   SER B 364     5059   5363   5405    111    203    154       O  
ATOM   8536  CB  SER B 364      10.660  12.606  -0.737  1.00 39.79           C  
ANISOU 8536  CB  SER B 364     4752   5196   5170     77    195    142       C  
ATOM   8537  OG  SER B 364      11.709  13.357  -1.286  1.00 40.56           O  
ANISOU 8537  OG  SER B 364     4855   5283   5271     73    214    141       O  
ATOM   8538  N   PHE B 365       8.252  13.311  -2.780  1.00 42.40           N  
ANISOU 8538  N   PHE B 365     5139   5467   5501    105    181    139       N  
ATOM   8539  CA  PHE B 365       7.672  14.187  -3.793  1.00 43.11           C  
ANISOU 8539  CA  PHE B 365     5256   5530   5593    115    184    135       C  
ATOM   8540  C   PHE B 365       8.515  15.440  -3.966  1.00 41.94           C  
ANISOU 8540  C   PHE B 365     5111   5374   5450    107    205    128       C  
ATOM   8541  O   PHE B 365       8.978  16.018  -2.997  1.00 42.79           O  
ANISOU 8541  O   PHE B 365     5197   5497   5561     90    212    118       O  
ATOM   8542  CB  PHE B 365       6.224  14.555  -3.446  1.00 41.93           C  
ANISOU 8542  CB  PHE B 365     5107   5378   5446    117    170    127       C  
ATOM   8543  CG  PHE B 365       5.551  15.387  -4.495  1.00 41.84           C  
ANISOU 8543  CG  PHE B 365     5122   5338   5435    128    172    124       C  
ATOM   8544  CD1 PHE B 365       5.065  14.801  -5.662  1.00 42.26           C  
ANISOU 8544  CD1 PHE B 365     5200   5372   5483    147    162    133       C  
ATOM   8545  CD2 PHE B 365       5.418  16.765  -4.329  1.00 40.68           C  
ANISOU 8545  CD2 PHE B 365     4977   5184   5294    122    183    111       C  
ATOM   8546  CE1 PHE B 365       4.454  15.577  -6.643  1.00 40.99           C  
ANISOU 8546  CE1 PHE B 365     5064   5186   5322    159    164    131       C  
ATOM   8547  CE2 PHE B 365       4.810  17.541  -5.301  1.00 39.18           C  
ANISOU 8547  CE2 PHE B 365     4812   4968   5104    134    185    110       C  
ATOM   8548  CZ  PHE B 365       4.330  16.947  -6.459  1.00 39.88           C  
ANISOU 8548  CZ  PHE B 365     4926   5039   5188    153    175    120       C  
ATOM   8549  N   LYS B 366       8.724  15.840  -5.209  1.00 43.79           N  
ANISOU 8549  N   LYS B 366     5372   5582   5684    118    215    132       N  
ATOM   8550  CA  LYS B 366       9.411  17.088  -5.512  1.00 46.07           C  
ANISOU 8550  CA  LYS B 366     5667   5858   5977    113    236    125       C  
ATOM   8551  C   LYS B 366       8.475  17.920  -6.390  1.00 44.84           C  
ANISOU 8551  C   LYS B 366     5539   5675   5823    125    235    121       C  
ATOM   8552  O   LYS B 366       7.921  17.419  -7.369  1.00 46.04           O  
ANISOU 8552  O   LYS B 366     5713   5811   5969    142    226    130       O  
ATOM   8553  CB  LYS B 366      10.751  16.802  -6.202  1.00 48.52           C  
ANISOU 8553  CB  LYS B 366     5985   6163   6287    115    251    135       C  
ATOM   8554  CG  LYS B 366      11.609  18.021  -6.493  1.00 53.66           C  
ANISOU 8554  CG  LYS B 366     6640   6801   6945    108    275    129       C  
ATOM   8555  CD  LYS B 366      12.470  17.792  -7.738  1.00 58.40           C  
ANISOU 8555  CD  LYS B 366     7263   7383   7544    120    289    141       C  
ATOM   8556  CE  LYS B 366      12.891  19.094  -8.421  1.00 57.37           C  
ANISOU 8556  CE  LYS B 366     7149   7229   7419    120    311    136       C  
ATOM   8557  NZ  LYS B 366      11.740  19.886  -8.958  1.00 56.88           N  
ANISOU 8557  NZ  LYS B 366     7109   7145   7355    130    307    130       N  
ATOM   8558  N   LYS B 367       8.280  19.181  -6.021  1.00 44.69           N  
ANISOU 8558  N   LYS B 367     5518   5652   5810    116    245    108       N  
ATOM   8559  CA  LYS B 367       7.335  20.058  -6.714  1.00 45.05           C  
ANISOU 8559  CA  LYS B 367     5585   5673   5856    127    245    104       C  
ATOM   8560  C   LYS B 367       7.588  20.082  -8.228  1.00 44.17           C  
ANISOU 8560  C   LYS B 367     5506   5534   5740    145    253    114       C  
ATOM   8561  O   LYS B 367       8.730  20.184  -8.681  1.00 43.75           O  
ANISOU 8561  O   LYS B 367     5458   5476   5689    144    270    119       O  
ATOM   8562  CB  LYS B 367       7.346  21.444  -6.062  1.00 48.01           C  
ANISOU 8562  CB  LYS B 367     5952   6048   6240    113    259     88       C  
ATOM   8563  CG  LYS B 367       7.163  22.651  -6.968  1.00 51.54           C  
ANISOU 8563  CG  LYS B 367     6425   6467   6691    121    274     85       C  
ATOM   8564  CD  LYS B 367       7.861  23.866  -6.354  1.00 56.74           C  
ANISOU 8564  CD  LYS B 367     7072   7127   7358    103    295     72       C  
ATOM   8565  CE  LYS B 367       9.387  23.736  -6.433  1.00 57.87           C  
ANISOU 8565  CE  LYS B 367     7209   7275   7504     93    312     75       C  
ATOM   8566  NZ  LYS B 367      10.111  24.406  -5.317  1.00 55.74           N  
ANISOU 8566  NZ  LYS B 367     6913   7022   7241     70    325     61       N  
ATOM   8567  N   VAL B 368       6.501  19.960  -8.988  1.00 43.35           N  
ANISOU 8567  N   VAL B 368     5424   5415   5632    163    240    118       N  
ATOM   8568  CA  VAL B 368       6.547  19.771 -10.437  1.00 42.63           C  
ANISOU 8568  CA  VAL B 368     5363   5299   5533    182    242    129       C  
ATOM   8569  C   VAL B 368       5.617  20.772 -11.172  1.00 42.09           C  
ANISOU 8569  C   VAL B 368     5319   5207   5465    196    243    125       C  
ATOM   8570  O   VAL B 368       4.726  21.348 -10.565  1.00 43.21           O  
ANISOU 8570  O   VAL B 368     5452   5353   5612    191    236    116       O  
ATOM   8571  CB  VAL B 368       6.207  18.293 -10.764  1.00 43.07           C  
ANISOU 8571  CB  VAL B 368     5423   5360   5581    193    222    140       C  
ATOM   8572  CG1 VAL B 368       4.727  18.112 -11.103  1.00 41.56           C  
ANISOU 8572  CG1 VAL B 368     5243   5162   5386    207    200    140       C  
ATOM   8573  CG2 VAL B 368       7.113  17.749 -11.856  1.00 41.31           C  
ANISOU 8573  CG2 VAL B 368     5220   5124   5352    204    231    153       C  
ATOM   8574  N   ALA B 369       5.834  20.994 -12.468  1.00 42.86           N  
ANISOU 8574  N   ALA B 369     5446   5280   5557    212    252    133       N  
ATOM   8575  CA  ALA B 369       5.032  21.962 -13.241  1.00 41.36           C  
ANISOU 8575  CA  ALA B 369     5281   5067   5367    226    254    131       C  
ATOM   8576  C   ALA B 369       4.513  21.372 -14.550  1.00 40.76           C  
ANISOU 8576  C   ALA B 369     5234   4972   5278    250    242    142       C  
ATOM   8577  O   ALA B 369       5.221  21.344 -15.564  1.00 40.63           O  
ANISOU 8577  O   ALA B 369     5240   4940   5256    260    254    151       O  
ATOM   8578  CB  ALA B 369       5.827  23.235 -13.509  1.00 40.16           C  
ANISOU 8578  CB  ALA B 369     5137   4898   5220    222    283    127       C  
ATOM   8579  N   LEU B 370       3.265  20.917 -14.519  1.00 40.34           N  
ANISOU 8579  N   LEU B 370     5182   4924   5222    258    217    142       N  
ATOM   8580  CA  LEU B 370       2.681  20.158 -15.622  1.00 39.71           C  
ANISOU 8580  CA  LEU B 370     5125   4830   5130    279    200    151       C  
ATOM   8581  C   LEU B 370       1.314  20.722 -15.951  1.00 39.12           C  
ANISOU 8581  C   LEU B 370     5062   4746   5054    291    186    147       C  
ATOM   8582  O   LEU B 370       0.292  20.208 -15.495  1.00 40.88           O  
ANISOU 8582  O   LEU B 370     5274   4981   5279    291    164    144       O  
ATOM   8583  CB  LEU B 370       2.593  18.666 -15.267  1.00 39.08           C  
ANISOU 8583  CB  LEU B 370     5031   4768   5046    275    181    156       C  
ATOM   8584  CG  LEU B 370       3.917  17.946 -14.977  1.00 39.35           C  
ANISOU 8584  CG  LEU B 370     5055   4815   5081    265    192    161       C  
ATOM   8585  CD1 LEU B 370       3.667  16.614 -14.286  1.00 39.26           C  
ANISOU 8585  CD1 LEU B 370     5023   4825   5069    258    173    163       C  
ATOM   8586  CD2 LEU B 370       4.765  17.764 -16.235  1.00 38.87           C  
ANISOU 8586  CD2 LEU B 370     5021   4733   5011    278    206    172       C  
ATOM   8587  N   PRO B 371       1.288  21.776 -16.774  1.00 39.00           N  
ANISOU 8587  N   PRO B 371     5071   4708   5037    303    200    148       N  
ATOM   8588  CA  PRO B 371       0.095  22.618 -16.900  1.00 38.64           C  
ANISOU 8588  CA  PRO B 371     5033   4654   4994    313    193    143       C  
ATOM   8589  C   PRO B 371      -1.088  21.979 -17.642  1.00 37.53           C  
ANISOU 8589  C   PRO B 371     4907   4507   4843    332    165    148       C  
ATOM   8590  O   PRO B 371      -2.161  22.579 -17.706  1.00 38.38           O  
ANISOU 8590  O   PRO B 371     5019   4611   4953    340    156    144       O  
ATOM   8591  CB  PRO B 371       0.618  23.859 -17.646  1.00 38.38           C  
ANISOU 8591  CB  PRO B 371     5023   4598   4961    321    218    144       C  
ATOM   8592  CG  PRO B 371       2.102  23.679 -17.779  1.00 38.51           C  
ANISOU 8592  CG  PRO B 371     5041   4613   4978    313    240    149       C  
ATOM   8593  CD  PRO B 371       2.348  22.206 -17.699  1.00 38.36           C  
ANISOU 8593  CD  PRO B 371     5013   4608   4952    311    224    155       C  
ATOM   8594  N   SER B 372      -0.899  20.775 -18.170  1.00 36.48           N  
ANISOU 8594  N   SER B 372     4782   4377   4701    338    153    156       N  
ATOM   8595  CA  SER B 372      -1.949  20.087 -18.909  1.00 36.81           C  
ANISOU 8595  CA  SER B 372     4838   4413   4733    355    126    160       C  
ATOM   8596  C   SER B 372      -2.441  18.844 -18.177  1.00 37.36           C  
ANISOU 8596  C   SER B 372     4885   4504   4805    346    103    158       C  
ATOM   8597  O   SER B 372      -3.344  18.152 -18.669  1.00 39.03           O  
ANISOU 8597  O   SER B 372     5104   4714   5011    357     79    161       O  
ATOM   8598  CB  SER B 372      -1.457  19.685 -20.307  1.00 36.82           C  
ANISOU 8598  CB  SER B 372     4873   4396   4721    373    129    170       C  
ATOM   8599  OG  SER B 372      -1.201  20.810 -21.125  1.00 37.39           O  
ANISOU 8599  OG  SER B 372     4970   4447   4789    386    148    173       O  
ATOM   8600  N   LEU B 373      -1.849  18.560 -17.016  1.00 35.64           N  
ANISOU 8600  N   LEU B 373     4638   4305   4596    325    110    155       N  
ATOM   8601  CA  LEU B 373      -2.129  17.323 -16.275  1.00 34.38           C  
ANISOU 8601  CA  LEU B 373     4456   4166   4438    315     92    154       C  
ATOM   8602  C   LEU B 373      -3.574  17.226 -15.830  1.00 33.36           C  
ANISOU 8602  C   LEU B 373     4314   4044   4314    317     68    149       C  
ATOM   8603  O   LEU B 373      -4.109  18.172 -15.261  1.00 33.91           O  
ANISOU 8603  O   LEU B 373     4375   4117   4393    312     72    141       O  
ATOM   8604  CB  LEU B 373      -1.226  17.226 -15.040  1.00 34.41           C  
ANISOU 8604  CB  LEU B 373     4432   4190   4451    294    105    151       C  
ATOM   8605  CG  LEU B 373      -1.040  15.846 -14.412  1.00 33.84           C  
ANISOU 8605  CG  LEU B 373     4340   4136   4379    284     94    154       C  
ATOM   8606  CD1 LEU B 373      -0.402  14.885 -15.409  1.00 32.86           C  
ANISOU 8606  CD1 LEU B 373     4236   4003   4244    295     93    165       C  
ATOM   8607  CD2 LEU B 373      -0.178  15.980 -13.165  1.00 32.97           C  
ANISOU 8607  CD2 LEU B 373     4201   4046   4277    263    108    150       C  
ATOM   8608  N   SER B 374      -4.204  16.084 -16.074  1.00 32.63           N  
ANISOU 8608  N   SER B 374     4223   3956   4217    322     45    152       N  
ATOM   8609  CA  SER B 374      -5.552  15.852 -15.547  1.00 32.14           C  
ANISOU 8609  CA  SER B 374     4145   3904   4162    321     23    147       C  
ATOM   8610  C   SER B 374      -5.669  14.519 -14.792  1.00 31.70           C  
ANISOU 8610  C   SER B 374     4067   3867   4109    310      8    148       C  
ATOM   8611  O   SER B 374      -6.690  14.228 -14.161  1.00 31.60           O  
ANISOU 8611  O   SER B 374     4037   3865   4103    306     -8    143       O  
ATOM   8612  CB  SER B 374      -6.575  15.929 -16.672  1.00 31.21           C  
ANISOU 8612  CB  SER B 374     4051   3770   4037    342      4    149       C  
ATOM   8613  OG  SER B 374      -6.540  14.754 -17.450  1.00 32.12           O  
ANISOU 8613  OG  SER B 374     4180   3881   4142    350     -9    155       O  
ATOM   8614  N   TYR B 375      -4.612  13.717 -14.876  1.00 31.68           N  
ANISOU 8614  N   TYR B 375     4066   3867   4101    306     16    154       N  
ATOM   8615  CA  TYR B 375      -4.569  12.391 -14.282  1.00 32.05           C  
ANISOU 8615  CA  TYR B 375     4096   3930   4150    297      6    156       C  
ATOM   8616  C   TYR B 375      -3.178  12.190 -13.692  1.00 33.19           C  
ANISOU 8616  C   TYR B 375     4229   4086   4296    284     26    159       C  
ATOM   8617  O   TYR B 375      -2.169  12.441 -14.355  1.00 33.71           O  
ANISOU 8617  O   TYR B 375     4312   4140   4355    288     43    164       O  
ATOM   8618  CB  TYR B 375      -4.871  11.327 -15.339  1.00 31.49           C  
ANISOU 8618  CB  TYR B 375     4045   3848   4069    310    -10    163       C  
ATOM   8619  CG  TYR B 375      -4.961   9.912 -14.813  1.00 31.50           C  
ANISOU 8619  CG  TYR B 375     4032   3864   4073    302    -23    165       C  
ATOM   8620  CD1 TYR B 375      -6.193   9.334 -14.525  1.00 31.65           C  
ANISOU 8620  CD1 TYR B 375     4039   3889   4097    302    -46    162       C  
ATOM   8621  CD2 TYR B 375      -3.809   9.138 -14.627  1.00 32.07           C  
ANISOU 8621  CD2 TYR B 375     4099   3942   4141    296    -11    172       C  
ATOM   8622  CE1 TYR B 375      -6.279   8.032 -14.053  1.00 32.38           C  
ANISOU 8622  CE1 TYR B 375     4117   3993   4191    295    -56    165       C  
ATOM   8623  CE2 TYR B 375      -3.882   7.832 -14.155  1.00 31.90           C  
ANISOU 8623  CE2 TYR B 375     4065   3933   4122    290    -21    175       C  
ATOM   8624  CZ  TYR B 375      -5.118   7.287 -13.867  1.00 32.23           C  
ANISOU 8624  CZ  TYR B 375     4096   3980   4168    289    -43    171       C  
ATOM   8625  OH  TYR B 375      -5.193   5.998 -13.400  1.00 32.31           O  
ANISOU 8625  OH  TYR B 375     4093   4001   4181    283    -52    175       O  
ATOM   8626  N   LEU B 376      -3.127  11.761 -12.436  1.00 32.42           N  
ANISOU 8626  N   LEU B 376     4102   4010   4206    268     25    157       N  
ATOM   8627  CA  LEU B 376      -1.857  11.584 -11.759  1.00 32.06           C  
ANISOU 8627  CA  LEU B 376     4042   3977   4161    255     43    159       C  
ATOM   8628  C   LEU B 376      -1.940  10.432 -10.755  1.00 33.00           C  
ANISOU 8628  C   LEU B 376     4135   4118   4284    244     34    161       C  
ATOM   8629  O   LEU B 376      -2.614  10.527  -9.718  1.00 32.59           O  
ANISOU 8629  O   LEU B 376     4061   4081   4241    235     27    155       O  
ATOM   8630  CB  LEU B 376      -1.416  12.891 -11.088  1.00 31.47           C  
ANISOU 8630  CB  LEU B 376     3956   3907   4094    245     62    152       C  
ATOM   8631  CG  LEU B 376      -0.173  12.871 -10.193  1.00 31.23           C  
ANISOU 8631  CG  LEU B 376     3905   3893   4065    229     80    152       C  
ATOM   8632  CD1 LEU B 376       1.077  12.602 -11.014  1.00 32.17           C  
ANISOU 8632  CD1 LEU B 376     4041   4003   4178    234     94    161       C  
ATOM   8633  CD2 LEU B 376      -0.033  14.173  -9.425  1.00 30.32           C  
ANISOU 8633  CD2 LEU B 376     3777   3784   3958    217     94    142       C  
ATOM   8634  N   ASP B 377      -1.270   9.334 -11.100  1.00 33.14           N  
ANISOU 8634  N   ASP B 377     4158   4136   4296    247     34    170       N  
ATOM   8635  CA  ASP B 377      -1.159   8.177 -10.226  1.00 31.88           C  
ANISOU 8635  CA  ASP B 377     3977   3996   4139    238     28    174       C  
ATOM   8636  C   ASP B 377       0.276   8.083  -9.731  1.00 31.41           C  
ANISOU 8636  C   ASP B 377     3907   3948   4079    228     48    179       C  
ATOM   8637  O   ASP B 377       1.218   7.846 -10.499  1.00 30.47           O  
ANISOU 8637  O   ASP B 377     3804   3819   3953    234     59    186       O  
ATOM   8638  CB  ASP B 377      -1.583   6.895 -10.954  1.00 32.14           C  
ANISOU 8638  CB  ASP B 377     4024   4021   4167    248     12    181       C  
ATOM   8639  CG  ASP B 377      -1.475   5.653 -10.077  1.00 32.88           C  
ANISOU 8639  CG  ASP B 377     4096   4132   4263    239      8    186       C  
ATOM   8640  OD1 ASP B 377      -1.822   4.550 -10.552  1.00 32.35           O  
ANISOU 8640  OD1 ASP B 377     4037   4060   4193    246     -4    191       O  
ATOM   8641  OD2 ASP B 377      -1.043   5.776  -8.906  1.00 34.20           O  
ANISOU 8641  OD2 ASP B 377     4238   4320   4436    226     16    184       O  
ATOM   8642  N   LEU B 378       0.422   8.283  -8.431  1.00 31.08           N  
ANISOU 8642  N   LEU B 378     3836   3928   4044    213     53    174       N  
ATOM   8643  CA  LEU B 378       1.706   8.175  -7.755  1.00 30.60           C  
ANISOU 8643  CA  LEU B 378     3759   3882   3983    202     69    178       C  
ATOM   8644  C   LEU B 378       1.619   7.153  -6.610  1.00 30.08           C  
ANISOU 8644  C   LEU B 378     3666   3840   3919    193     62    181       C  
ATOM   8645  O   LEU B 378       2.215   7.356  -5.549  1.00 30.39           O  
ANISOU 8645  O   LEU B 378     3683   3900   3962    180     71    178       O  
ATOM   8646  CB  LEU B 378       2.114   9.546  -7.210  1.00 30.41           C  
ANISOU 8646  CB  LEU B 378     3725   3863   3963    192     84    168       C  
ATOM   8647  CG  LEU B 378       3.063  10.484  -7.961  1.00 30.97           C  
ANISOU 8647  CG  LEU B 378     3814   3920   4033    195    104    168       C  
ATOM   8648  CD1 LEU B 378       3.098  10.240  -9.461  1.00 31.24           C  
ANISOU 8648  CD1 LEU B 378     3880   3929   4059    212    103    176       C  
ATOM   8649  CD2 LEU B 378       2.692  11.923  -7.654  1.00 30.43           C  
ANISOU 8649  CD2 LEU B 378     3742   3847   3970    189    110    156       C  
ATOM   8650  N   SER B 379       0.881   6.065  -6.825  1.00 28.37           N  
ANISOU 8650  N   SER B 379     3454   3621   3702    200     46    186       N  
ATOM   8651  CA  SER B 379       0.627   5.108  -5.757  1.00 29.04           C  
ANISOU 8651  CA  SER B 379     3515   3727   3791    192     39    188       C  
ATOM   8652  C   SER B 379       1.720   4.035  -5.646  1.00 29.85           C  
ANISOU 8652  C   SER B 379     3612   3839   3888    191     47    200       C  
ATOM   8653  O   SER B 379       2.544   3.884  -6.560  1.00 30.61           O  
ANISOU 8653  O   SER B 379     3727   3923   3979    199     56    207       O  
ATOM   8654  CB  SER B 379      -0.769   4.478  -5.903  1.00 29.09           C  
ANISOU 8654  CB  SER B 379     3524   3727   3800    198     18    187       C  
ATOM   8655  OG  SER B 379      -0.881   3.704  -7.083  1.00 28.51           O  
ANISOU 8655  OG  SER B 379     3475   3636   3721    210     10    193       O  
ATOM   8656  N   ARG B 380       1.734   3.318  -4.516  1.00 28.95           N  
ANISOU 8656  N   ARG B 380     3475   3747   3778    183     45    203       N  
ATOM   8657  CA  ARG B 380       2.623   2.162  -4.301  1.00 28.46           C  
ANISOU 8657  CA  ARG B 380     3405   3696   3712    183     51    215       C  
ATOM   8658  C   ARG B 380       4.120   2.484  -4.418  1.00 29.63           C  
ANISOU 8658  C   ARG B 380     3553   3848   3856    181     70    220       C  
ATOM   8659  O   ARG B 380       4.891   1.701  -4.980  1.00 29.98           O  
ANISOU 8659  O   ARG B 380     3607   3887   3896    187     76    231       O  
ATOM   8660  CB  ARG B 380       2.254   1.017  -5.250  1.00 27.40           C  
ANISOU 8660  CB  ARG B 380     3290   3544   3573    195     41    223       C  
ATOM   8661  CG  ARG B 380       0.849   0.482  -5.037  1.00 26.73           C  
ANISOU 8661  CG  ARG B 380     3202   3458   3494    196     22    220       C  
ATOM   8662  CD  ARG B 380       0.356  -0.348  -6.206  1.00 25.23           C  
ANISOU 8662  CD  ARG B 380     3038   3247   3301    209     11    224       C  
ATOM   8663  NE  ARG B 380      -0.963  -0.897  -5.904  1.00 25.55           N  
ANISOU 8663  NE  ARG B 380     3071   3288   3347    208     -6    220       N  
ATOM   8664  CZ  ARG B 380      -2.117  -0.250  -6.074  1.00 25.51           C  
ANISOU 8664  CZ  ARG B 380     3069   3275   3347    209    -19    210       C  
ATOM   8665  NH1 ARG B 380      -3.258  -0.842  -5.755  1.00 25.15           N  
ANISOU 8665  NH1 ARG B 380     3015   3231   3308    208    -34    208       N  
ATOM   8666  NH2 ARG B 380      -2.139   0.988  -6.557  1.00 25.72           N  
ANISOU 8666  NH2 ARG B 380     3107   3292   3372    212    -16    203       N  
ATOM   8667  N   ASN B 381       4.528   3.620  -3.867  1.00 29.46           N  
ANISOU 8667  N   ASN B 381     3519   3835   3836    171     80    212       N  
ATOM   8668  CA  ASN B 381       5.887   4.085  -4.022  1.00 30.02           C  
ANISOU 8668  CA  ASN B 381     3591   3909   3906    168     98    215       C  
ATOM   8669  C   ASN B 381       6.593   4.303  -2.709  1.00 30.45           C  
ANISOU 8669  C   ASN B 381     3615   3991   3962    153    106    213       C  
ATOM   8670  O   ASN B 381       7.770   4.678  -2.696  1.00 30.19           O  
ANISOU 8670  O   ASN B 381     3578   3964   3929    149    121    215       O  
ATOM   8671  CB  ASN B 381       5.886   5.405  -4.788  1.00 32.60           C  
ANISOU 8671  CB  ASN B 381     3935   4216   4233    170    105    206       C  
ATOM   8672  CG  ASN B 381       5.486   5.239  -6.240  1.00 34.23           C  
ANISOU 8672  CG  ASN B 381     4174   4395   4436    185    100    210       C  
ATOM   8673  OD1 ASN B 381       5.986   4.353  -6.943  1.00 35.89           O  
ANISOU 8673  OD1 ASN B 381     4397   4597   4640    194    103    221       O  
ATOM   8674  ND2 ASN B 381       4.590   6.103  -6.704  1.00 33.15           N  
ANISOU 8674  ND2 ASN B 381     4051   4243   4301    189     94    201       N  
ATOM   8675  N   ALA B 382       5.878   4.064  -1.609  1.00 30.78           N  
ANISOU 8675  N   ALA B 382     3636   4051   4007    146     96    209       N  
ATOM   8676  CA  ALA B 382       6.290   4.522  -0.285  1.00 30.89           C  
ANISOU 8676  CA  ALA B 382     3623   4092   4023    132    101    203       C  
ATOM   8677  C   ALA B 382       6.710   6.004  -0.313  1.00 31.75           C  
ANISOU 8677  C   ALA B 382     3732   4196   4133    124    112    191       C  
ATOM   8678  O   ALA B 382       7.712   6.392   0.303  1.00 31.93           O  
ANISOU 8678  O   ALA B 382     3738   4235   4156    113    124    189       O  
ATOM   8679  CB  ALA B 382       7.397   3.646   0.266  1.00 30.43           C  
ANISOU 8679  CB  ALA B 382     3548   4054   3960    129    109    214       C  
ATOM   8680  N   LEU B 383       5.931   6.818  -1.031  1.00 32.36           N  
ANISOU 8680  N   LEU B 383     3829   4253   4214    128    109    183       N  
ATOM   8681  CA  LEU B 383       6.242   8.234  -1.240  1.00 33.51           C  
ANISOU 8681  CA  LEU B 383     3979   4389   4362    122    121    172       C  
ATOM   8682  C   LEU B 383       6.135   9.037   0.036  1.00 34.27           C  
ANISOU 8682  C   LEU B 383     4053   4506   4462    107    123    159       C  
ATOM   8683  O   LEU B 383       5.160   8.881   0.771  1.00 34.00           O  
ANISOU 8683  O   LEU B 383     4007   4480   4429    104    111    155       O  
ATOM   8684  CB  LEU B 383       5.275   8.855  -2.252  1.00 33.90           C  
ANISOU 8684  CB  LEU B 383     4055   4412   4414    133    115    167       C  
ATOM   8685  CG  LEU B 383       5.758   9.402  -3.599  1.00 35.68           C  
ANISOU 8685  CG  LEU B 383     4307   4611   4637    142    126    169       C  
ATOM   8686  CD1 LEU B 383       4.574   9.881  -4.423  1.00 36.97           C  
ANISOU 8686  CD1 LEU B 383     4492   4752   4801    153    116    164       C  
ATOM   8687  CD2 LEU B 383       6.721  10.556  -3.421  1.00 36.56           C  
ANISOU 8687  CD2 LEU B 383     4413   4725   4751    132    144    162       C  
ATOM   8688  N   SER B 384       7.132   9.890   0.295  1.00 34.96           N  
ANISOU 8688  N   SER B 384     4131   4599   4550     96    138    153       N  
ATOM   8689  CA  SER B 384       6.980  11.000   1.242  1.00 35.18           C  
ANISOU 8689  CA  SER B 384     4144   4638   4582     82    142    138       C  
ATOM   8690  C   SER B 384       6.404  12.194   0.487  1.00 36.54           C  
ANISOU 8690  C   SER B 384     4338   4786   4759     86    146    129       C  
ATOM   8691  O   SER B 384       6.788  12.465  -0.663  1.00 36.53           O  
ANISOU 8691  O   SER B 384     4357   4762   4757     94    154    133       O  
ATOM   8692  CB  SER B 384       8.311  11.437   1.852  1.00 35.97           C  
ANISOU 8692  CB  SER B 384     4226   4756   4682     68    156    135       C  
ATOM   8693  OG  SER B 384       9.234  10.374   1.945  1.00 39.91           O  
ANISOU 8693  OG  SER B 384     4717   5270   5177     70    158    148       O  
ATOM   8694  N   PHE B 385       5.496  12.911   1.139  1.00 36.52           N  
ANISOU 8694  N   PHE B 385     4328   4786   4760     80    141    117       N  
ATOM   8695  CA  PHE B 385       4.930  14.116   0.580  1.00 38.02           C  
ANISOU 8695  CA  PHE B 385     4535   4954   4954     82    146    107       C  
ATOM   8696  C   PHE B 385       4.722  15.052   1.737  1.00 37.66           C  
ANISOU 8696  C   PHE B 385     4472   4923   4912     67    150     92       C  
ATOM   8697  O   PHE B 385       3.805  14.850   2.519  1.00 39.15           O  
ANISOU 8697  O   PHE B 385     4649   5123   5102     65    139     88       O  
ATOM   8698  CB  PHE B 385       3.584  13.804  -0.078  1.00 40.96           C  
ANISOU 8698  CB  PHE B 385     4924   5310   5327     97    131    110       C  
ATOM   8699  CG  PHE B 385       3.119  14.839  -1.073  1.00 44.21           C  
ANISOU 8699  CG  PHE B 385     5360   5694   5741    105    135    105       C  
ATOM   8700  CD1 PHE B 385       2.472  14.443  -2.245  1.00 43.69           C  
ANISOU 8700  CD1 PHE B 385     5318   5607   5673    123    126    113       C  
ATOM   8701  CD2 PHE B 385       3.321  16.208  -0.851  1.00 45.99           C  
ANISOU 8701  CD2 PHE B 385     5586   5916   5972     96    150     93       C  
ATOM   8702  CE1 PHE B 385       2.028  15.386  -3.165  1.00 44.33           C  
ANISOU 8702  CE1 PHE B 385     5422   5664   5757    132    130    109       C  
ATOM   8703  CE2 PHE B 385       2.879  17.152  -1.772  1.00 45.99           C  
ANISOU 8703  CE2 PHE B 385     5608   5889   5974    105    155     89       C  
ATOM   8704  CZ  PHE B 385       2.230  16.738  -2.929  1.00 44.49           C  
ANISOU 8704  CZ  PHE B 385     5441   5679   5781    124    145     98       C  
ATOM   8705  N   SER B 386       5.573  16.063   1.874  1.00 39.22           N  
ANISOU 8705  N   SER B 386     4667   5121   5113     56    166     83       N  
ATOM   8706  CA  SER B 386       5.362  17.039   2.942  1.00 41.46           C  
ANISOU 8706  CA  SER B 386     4935   5416   5399     41    171     67       C  
ATOM   8707  C   SER B 386       4.922  18.370   2.365  1.00 41.10           C  
ANISOU 8707  C   SER B 386     4908   5347   5360     43    180     57       C  
ATOM   8708  O   SER B 386       5.657  18.999   1.625  1.00 41.82           O  
ANISOU 8708  O   SER B 386     5012   5423   5453     43    195     56       O  
ATOM   8709  CB  SER B 386       6.599  17.192   3.826  1.00 41.85           C  
ANISOU 8709  CB  SER B 386     4963   5489   5448     24    181     62       C  
ATOM   8710  OG  SER B 386       7.350  18.327   3.463  1.00 45.50           O  
ANISOU 8710  OG  SER B 386     5432   5940   5915     16    199     53       O  
ATOM   8711  N   GLY B 387       3.709  18.784   2.700  1.00 43.04           N  
ANISOU 8711  N   GLY B 387     5154   5588   5608     45    173     50       N  
ATOM   8712  CA  GLY B 387       3.149  20.019   2.166  1.00 46.30           C  
ANISOU 8712  CA  GLY B 387     5585   5978   6027     48    181     41       C  
ATOM   8713  C   GLY B 387       2.062  19.814   1.127  1.00 47.49           C  
ANISOU 8713  C   GLY B 387     5758   6106   6178     68    170     49       C  
ATOM   8714  O   GLY B 387       1.941  20.603   0.193  1.00 52.09           O  
ANISOU 8714  O   GLY B 387     6363   6666   6764     76    178     48       O  
ATOM   8715  N   CYS B 388       1.272  18.758   1.300  1.00 47.81           N  
ANISOU 8715  N   CYS B 388     5792   6154   6216     75    152     56       N  
ATOM   8716  CA  CYS B 388       0.171  18.426   0.405  1.00 48.13           C  
ANISOU 8716  CA  CYS B 388     5852   6178   6258     93    139     63       C  
ATOM   8717  C   CYS B 388      -1.089  19.225   0.752  1.00 48.62           C  
ANISOU 8717  C   CYS B 388     5914   6234   6325     94    135     54       C  
ATOM   8718  O   CYS B 388      -1.452  19.303   1.932  1.00 49.31           O  
ANISOU 8718  O   CYS B 388     5981   6339   6415     84    132     46       O  
ATOM   8719  CB  CYS B 388      -0.153  16.943   0.545  1.00 50.55           C  
ANISOU 8719  CB  CYS B 388     6150   6496   6560     98    121     74       C  
ATOM   8720  SG  CYS B 388      -0.831  16.140  -0.929  1.00 58.41           S  
ANISOU 8720  SG  CYS B 388     7171   7469   7553    120    106     87       S  
ATOM   8721  N   CYS B 389      -1.769  19.815  -0.238  1.00 45.28           N  
ANISOU 8721  N   CYS B 389     5512   5786   5904    108    134     55       N  
ATOM   8722  CA  CYS B 389      -1.330  19.912  -1.635  1.00 47.26           C  
ANISOU 8722  CA  CYS B 389     5788   6014   6151    121    139     62       C  
ATOM   8723  C   CYS B 389      -2.084  21.080  -2.247  1.00 45.68           C  
ANISOU 8723  C   CYS B 389     5607   5792   5956    130    144     57       C  
ATOM   8724  O   CYS B 389      -3.177  21.407  -1.799  1.00 45.51           O  
ANISOU 8724  O   CYS B 389     5580   5771   5939    132    136     51       O  
ATOM   8725  CB  CYS B 389      -1.644  18.650  -2.450  1.00 50.20           C  
ANISOU 8725  CB  CYS B 389     6171   6382   6519    135    122     76       C  
ATOM   8726  SG  CYS B 389      -2.382  17.288  -1.526  1.00 59.97           S  
ANISOU 8726  SG  CYS B 389     7386   7642   7756    132    101     80       S  
ATOM   8727  N   SER B 390      -1.506  21.706  -3.269  1.00 41.86           N  
ANISOU 8727  N   SER B 390     5144   5287   5470    137    157     59       N  
ATOM   8728  CA  SER B 390      -2.092  22.891  -3.870  1.00 40.15           C  
ANISOU 8728  CA  SER B 390     4946   5048   5257    146    165     54       C  
ATOM   8729  C   SER B 390      -1.518  23.109  -5.264  1.00 40.01           C  
ANISOU 8729  C   SER B 390     4957   5007   5235    159    174     62       C  
ATOM   8730  O   SER B 390      -0.668  22.336  -5.709  1.00 40.23           O  
ANISOU 8730  O   SER B 390     4988   5037   5258    161    174     71       O  
ATOM   8731  CB  SER B 390      -1.838  24.119  -2.983  1.00 40.22           C  
ANISOU 8731  CB  SER B 390     4946   5062   5274    131    183     40       C  
ATOM   8732  OG  SER B 390      -0.511  24.599  -3.133  1.00 41.73           O  
ANISOU 8732  OG  SER B 390     5139   5249   5464    121    203     38       O  
ATOM   8733  N   TYR B 391      -1.967  24.168  -5.939  1.00 39.04           N  
ANISOU 8733  N   TYR B 391     4854   4863   5115    170    182     60       N  
ATOM   8734  CA  TYR B 391      -1.524  24.469  -7.304  1.00 38.50           C  
ANISOU 8734  CA  TYR B 391     4814   4771   5042    184    191     68       C  
ATOM   8735  C   TYR B 391      -0.007  24.441  -7.486  1.00 37.72           C  
ANISOU 8735  C   TYR B 391     4717   4673   4942    176    210     70       C  
ATOM   8736  O   TYR B 391       0.482  23.818  -8.423  1.00 37.68           O  
ANISOU 8736  O   TYR B 391     4728   4659   4930    186    208     80       O  
ATOM   8737  CB  TYR B 391      -2.104  25.798  -7.813  1.00 38.11           C  
ANISOU 8737  CB  TYR B 391     4783   4699   4997    194    202     63       C  
ATOM   8738  CG  TYR B 391      -1.633  26.173  -9.206  1.00 36.68           C  
ANISOU 8738  CG  TYR B 391     4632   4493   4810    210    214     71       C  
ATOM   8739  CD1 TYR B 391      -2.256  25.649 -10.338  1.00 35.86           C  
ANISOU 8739  CD1 TYR B 391     4550   4376   4699    231    198     82       C  
ATOM   8740  CD2 TYR B 391      -0.551  27.041  -9.389  1.00 36.90           C  
ANISOU 8740  CD2 TYR B 391     4667   4510   4841    203    240     68       C  
ATOM   8741  CE1 TYR B 391      -1.828  25.983 -11.616  1.00 35.62           C  
ANISOU 8741  CE1 TYR B 391     4549   4323   4663    247    209     90       C  
ATOM   8742  CE2 TYR B 391      -0.108  27.379 -10.661  1.00 36.56           C  
ANISOU 8742  CE2 TYR B 391     4653   4444   4794    218    252     76       C  
ATOM   8743  CZ  TYR B 391      -0.752  26.850 -11.772  1.00 37.08           C  
ANISOU 8743  CZ  TYR B 391     4740   4496   4850    240    236     87       C  
ATOM   8744  OH  TYR B 391      -0.313  27.184 -13.038  1.00 37.27           O  
ANISOU 8744  OH  TYR B 391     4794   4497   4868    255    248     95       O  
ATOM   8745  N   SER B 392       0.726  25.109  -6.598  1.00 38.28           N  
ANISOU 8745  N   SER B 392     4772   4753   5019    156    227     59       N  
ATOM   8746  CA  SER B 392       2.191  25.228  -6.730  1.00 39.46           C  
ANISOU 8746  CA  SER B 392     4921   4902   5169    147    246     60       C  
ATOM   8747  C   SER B 392       2.947  23.895  -6.760  1.00 39.27           C  
ANISOU 8747  C   SER B 392     4888   4892   5138    145    238     70       C  
ATOM   8748  O   SER B 392       4.064  23.830  -7.271  1.00 40.01           O  
ANISOU 8748  O   SER B 392     4989   4981   5231    144    252     75       O  
ATOM   8749  CB  SER B 392       2.783  26.177  -5.679  1.00 39.80           C  
ANISOU 8749  CB  SER B 392     4946   4955   5221    125    264     46       C  
ATOM   8750  OG  SER B 392       1.888  26.371  -4.595  1.00 43.64           O  
ANISOU 8750  OG  SER B 392     5414   5455   5710    117    255     36       O  
ATOM   8751  N   ASP B 393       2.327  22.835  -6.245  1.00 38.34           N  
ANISOU 8751  N   ASP B 393     4756   4792   5017    145    216     73       N  
ATOM   8752  CA  ASP B 393       2.924  21.505  -6.297  1.00 38.62           C  
ANISOU 8752  CA  ASP B 393     4785   4840   5047    146    207     83       C  
ATOM   8753  C   ASP B 393       2.910  20.900  -7.717  1.00 39.63           C  
ANISOU 8753  C   ASP B 393     4941   4950   5168    166    202     97       C  
ATOM   8754  O   ASP B 393       3.808  20.120  -8.072  1.00 39.92           O  
ANISOU 8754  O   ASP B 393     4978   4988   5199    167    205    106       O  
ATOM   8755  CB  ASP B 393       2.246  20.555  -5.293  1.00 38.07           C  
ANISOU 8755  CB  ASP B 393     4692   4794   4976    140    187     83       C  
ATOM   8756  CG  ASP B 393       2.426  20.997  -3.836  1.00 39.30           C  
ANISOU 8756  CG  ASP B 393     4820   4973   5138    119    192     71       C  
ATOM   8757  OD1 ASP B 393       3.566  21.336  -3.444  1.00 38.71           O  
ANISOU 8757  OD1 ASP B 393     4736   4906   5066    106    208     67       O  
ATOM   8758  OD2 ASP B 393       1.421  21.002  -3.078  1.00 39.23           O  
ANISOU 8758  OD2 ASP B 393     4798   4973   5131    117    181     65       O  
ATOM   8759  N   LEU B 394       1.915  21.269  -8.528  1.00 37.89           N  
ANISOU 8759  N   LEU B 394     4741   4709   4945    182    195     98       N  
ATOM   8760  CA  LEU B 394       1.705  20.624  -9.828  1.00 38.08           C  
ANISOU 8760  CA  LEU B 394     4791   4717   4961    202    186    110       C  
ATOM   8761  C   LEU B 394       1.703  21.560 -11.037  1.00 39.64           C  
ANISOU 8761  C   LEU B 394     5019   4886   5156    217    198    113       C  
ATOM   8762  O   LEU B 394       2.096  21.159 -12.134  1.00 40.32           O  
ANISOU 8762  O   LEU B 394     5127   4958   5234    231    200    123       O  
ATOM   8763  CB  LEU B 394       0.417  19.800  -9.805  1.00 38.72           C  
ANISOU 8763  CB  LEU B 394     4869   4802   5038    211    159    113       C  
ATOM   8764  CG  LEU B 394       0.326  18.758  -8.677  1.00 39.53           C  
ANISOU 8764  CG  LEU B 394     4943   4931   5143    199    145    112       C  
ATOM   8765  CD1 LEU B 394      -1.119  18.396  -8.387  1.00 40.12           C  
ANISOU 8765  CD1 LEU B 394     5012   5010   5219    204    123    110       C  
ATOM   8766  CD2 LEU B 394       1.148  17.512  -8.983  1.00 38.16           C  
ANISOU 8766  CD2 LEU B 394     4771   4764   4963    200    143    123       C  
ATOM   8767  N   GLY B 395       1.249  22.796 -10.834  1.00 40.14           N  
ANISOU 8767  N   GLY B 395     5084   4941   5225    216    207    104       N  
ATOM   8768  CA  GLY B 395       1.147  23.780 -11.907  1.00 37.50           C  
ANISOU 8768  CA  GLY B 395     4778   4579   4889    230    220    105       C  
ATOM   8769  C   GLY B 395       0.125  23.435 -12.974  1.00 37.37           C  
ANISOU 8769  C   GLY B 395     4785   4548   4864    254    202    113       C  
ATOM   8770  O   GLY B 395       0.311  23.787 -14.137  1.00 38.59           O  
ANISOU 8770  O   GLY B 395     4968   4681   5013    269    210    120       O  
ATOM   8771  N   THR B 396      -0.944  22.749 -12.569  1.00 36.42           N  
ANISOU 8771  N   THR B 396     4653   4440   4744    256    177    112       N  
ATOM   8772  CA  THR B 396      -2.096  22.448 -13.432  1.00 36.83           C  
ANISOU 8772  CA  THR B 396     4723   4480   4788    276    156    118       C  
ATOM   8773  C   THR B 396      -3.402  23.034 -12.864  1.00 37.04           C  
ANISOU 8773  C   THR B 396     4739   4510   4822    277    146    110       C  
ATOM   8774  O   THR B 396      -3.565  23.134 -11.649  1.00 35.95           O  
ANISOU 8774  O   THR B 396     4575   4389   4692    261    145    102       O  
ATOM   8775  CB  THR B 396      -2.289  20.920 -13.642  1.00 36.33           C  
ANISOU 8775  CB  THR B 396     4658   4427   4719    280    134    125       C  
ATOM   8776  OG1 THR B 396      -3.447  20.690 -14.446  1.00 34.84           O  
ANISOU 8776  OG1 THR B 396     4485   4227   4524    299    113    129       O  
ATOM   8777  CG2 THR B 396      -2.472  20.177 -12.307  1.00 35.01           C  
ANISOU 8777  CG2 THR B 396     4457   4285   4557    263    123    121       C  
ATOM   8778  N   ASN B 397      -4.326  23.409 -13.748  1.00 37.58           N  
ANISOU 8778  N   ASN B 397     4829   4562   4887    296    136    113       N  
ATOM   8779  CA  ASN B 397      -5.684  23.796 -13.335  1.00 38.21           C  
ANISOU 8779  CA  ASN B 397     4899   4644   4972    300    122    108       C  
ATOM   8780  C   ASN B 397      -6.693  22.702 -13.687  1.00 38.30           C  
ANISOU 8780  C   ASN B 397     4911   4661   4979    311     92    113       C  
ATOM   8781  O   ASN B 397      -7.880  22.843 -13.395  1.00 38.42           O  
ANISOU 8781  O   ASN B 397     4917   4679   4999    315     77    110       O  
ATOM   8782  CB  ASN B 397      -6.125  25.126 -13.979  1.00 38.09           C  
ANISOU 8782  CB  ASN B 397     4905   4609   4958    314    134    107       C  
ATOM   8783  CG  ASN B 397      -5.225  26.307 -13.608  1.00 40.02           C  
ANISOU 8783  CG  ASN B 397     5150   4847   5209    303    165    101       C  
ATOM   8784  OD1 ASN B 397      -4.515  26.851 -14.465  1.00 38.88           O  
ANISOU 8784  OD1 ASN B 397     5027   4683   5060    311    182    105       O  
ATOM   8785  ND2 ASN B 397      -5.261  26.719 -12.333  1.00 38.98           N  
ANISOU 8785  ND2 ASN B 397     4992   4729   5088    284    171     90       N  
ATOM   8786  N   SER B 398      -6.209  21.610 -14.287  1.00 37.42           N  
ANISOU 8786  N   SER B 398     4808   4549   4858    315     84    121       N  
ATOM   8787  CA  SER B 398      -7.074  20.609 -14.930  1.00 37.84           C  
ANISOU 8787  CA  SER B 398     4869   4602   4905    328     57    126       C  
ATOM   8788  C   SER B 398      -7.136  19.229 -14.277  1.00 38.26           C  
ANISOU 8788  C   SER B 398     4901   4675   4960    317     40    127       C  
ATOM   8789  O   SER B 398      -7.703  18.302 -14.867  1.00 38.59           O  
ANISOU 8789  O   SER B 398     4950   4715   4995    327     19    132       O  
ATOM   8790  CB  SER B 398      -6.655  20.411 -16.390  1.00 38.61           C  
ANISOU 8790  CB  SER B 398     5000   4681   4989    346     57    135       C  
ATOM   8791  OG  SER B 398      -6.762  21.618 -17.113  1.00 43.05           O  
ANISOU 8791  OG  SER B 398     5583   5223   5548    360     70    136       O  
ATOM   8792  N   LEU B 399      -6.568  19.085 -13.081  1.00 37.28           N  
ANISOU 8792  N   LEU B 399     4751   4568   4842    297     49    122       N  
ATOM   8793  CA  LEU B 399      -6.435  17.771 -12.456  1.00 36.93           C  
ANISOU 8793  CA  LEU B 399     4688   4542   4799    287     38    124       C  
ATOM   8794  C   LEU B 399      -7.763  17.206 -11.917  1.00 37.98           C  
ANISOU 8794  C   LEU B 399     4804   4687   4939    286     14    121       C  
ATOM   8795  O   LEU B 399      -8.407  17.839 -11.076  1.00 37.82           O  
ANISOU 8795  O   LEU B 399     4767   4674   4927    280     14    114       O  
ATOM   8796  CB  LEU B 399      -5.389  17.836 -11.347  1.00 34.83           C  
ANISOU 8796  CB  LEU B 399     4400   4293   4538    267     56    121       C  
ATOM   8797  CG  LEU B 399      -4.986  16.533 -10.671  1.00 33.39           C  
ANISOU 8797  CG  LEU B 399     4200   4131   4357    255     48    124       C  
ATOM   8798  CD1 LEU B 399      -3.966  15.790 -11.521  1.00 32.03           C  
ANISOU 8798  CD1 LEU B 399     4044   3951   4174    261     53    133       C  
ATOM   8799  CD2 LEU B 399      -4.421  16.856  -9.300  1.00 33.52           C  
ANISOU 8799  CD2 LEU B 399     4188   4166   4380    235     62    117       C  
ATOM   8800  N   ARG B 400      -8.146  16.015 -12.396  1.00 39.41           N  
ANISOU 8800  N   ARG B 400     4989   4868   5114    293     -5    127       N  
ATOM   8801  CA  ARG B 400      -9.405  15.343 -12.002  1.00 41.73           C  
ANISOU 8801  CA  ARG B 400     5268   5172   5414    293    -29    125       C  
ATOM   8802  C   ARG B 400      -9.195  14.069 -11.178  1.00 40.35           C  
ANISOU 8802  C   ARG B 400     5071   5015   5242    280    -36    127       C  
ATOM   8803  O   ARG B 400     -10.101  13.646 -10.440  1.00 38.86           O  
ANISOU 8803  O   ARG B 400     4862   4838   5062    275    -50    124       O  
ATOM   8804  CB  ARG B 400     -10.274  14.991 -13.223  1.00 46.25           C  
ANISOU 8804  CB  ARG B 400     5862   5729   5980    312    -50    129       C  
ATOM   8805  CG  ARG B 400     -10.114  15.928 -14.403  1.00 53.48           C  
ANISOU 8805  CG  ARG B 400     6808   6624   6887    328    -42    131       C  
ATOM   8806  CD  ARG B 400     -11.415  16.189 -15.140  1.00 60.01           C  
ANISOU 8806  CD  ARG B 400     7646   7440   7713    345    -63    130       C  
ATOM   8807  NE  ARG B 400     -11.349  17.509 -15.773  1.00 68.72           N  
ANISOU 8807  NE  ARG B 400     8769   8527   8812    357    -49    131       N  
ATOM   8808  CZ  ARG B 400     -11.845  18.632 -15.250  1.00 70.90           C  
ANISOU 8808  CZ  ARG B 400     9036   8803   9097    356    -41    125       C  
ATOM   8809  NH1 ARG B 400     -12.479  18.613 -14.082  1.00 70.68           N  
ANISOU 8809  NH1 ARG B 400     8980   8792   9082    344    -46    119       N  
ATOM   8810  NH2 ARG B 400     -11.716  19.782 -15.902  1.00 72.68           N  
ANISOU 8810  NH2 ARG B 400     9281   9012   9319    368    -28    126       N  
ATOM   8811  N   HIS B 401      -8.007  13.470 -11.313  1.00 37.69           N  
ANISOU 8811  N   HIS B 401     4739   4681   4899    276    -25    132       N  
ATOM   8812  CA  HIS B 401      -7.670  12.194 -10.681  1.00 34.99           C  
ANISOU 8812  CA  HIS B 401     4380   4354   4558    265    -30    136       C  
ATOM   8813  C   HIS B 401      -6.346  12.287  -9.974  1.00 34.31           C  
ANISOU 8813  C   HIS B 401     4283   4280   4471    252     -9    136       C  
ATOM   8814  O   HIS B 401      -5.317  12.546 -10.618  1.00 33.84           O  
ANISOU 8814  O   HIS B 401     4241   4211   4405    255      5    140       O  
ATOM   8815  CB  HIS B 401      -7.635  11.107 -11.751  1.00 35.84           C  
ANISOU 8815  CB  HIS B 401     4508   4451   4656    277    -43    143       C  
ATOM   8816  CG  HIS B 401      -7.357   9.713 -11.222  1.00 37.84           C  
ANISOU 8816  CG  HIS B 401     4746   4718   4910    268    -49    148       C  
ATOM   8817  ND1 HIS B 401      -8.328   8.786 -11.063  1.00 37.69           N  
ANISOU 8817  ND1 HIS B 401     4719   4705   4895    268    -70    147       N  
ATOM   8818  CD2 HIS B 401      -6.163   9.098 -10.840  1.00 38.10           C  
ANISOU 8818  CD2 HIS B 401     4773   4761   4940    259    -36    153       C  
ATOM   8819  CE1 HIS B 401      -7.786   7.648 -10.592  1.00 37.04           C  
ANISOU 8819  CE1 HIS B 401     4625   4633   4813    260    -68    153       C  
ATOM   8820  NE2 HIS B 401      -6.462   7.840 -10.460  1.00 38.32           N  
ANISOU 8820  NE2 HIS B 401     4789   4799   4970    255    -48    156       N  
ATOM   8821  N   LEU B 402      -6.364  12.075  -8.650  1.00 32.43           N  
ANISOU 8821  N   LEU B 402     4016   4062   4241    237     -7    133       N  
ATOM   8822  CA  LEU B 402      -5.156  12.067  -7.809  1.00 31.24           C  
ANISOU 8822  CA  LEU B 402     3851   3927   4091    222     10    133       C  
ATOM   8823  C   LEU B 402      -5.068  10.829  -6.914  1.00 32.19           C  
ANISOU 8823  C   LEU B 402     3949   4068   4213    213      3    137       C  
ATOM   8824  O   LEU B 402      -5.825  10.673  -5.942  1.00 32.26           O  
ANISOU 8824  O   LEU B 402     3936   4090   4229    205     -4    133       O  
ATOM   8825  CB  LEU B 402      -5.057  13.341  -6.962  1.00 31.06           C  
ANISOU 8825  CB  LEU B 402     3815   3911   4075    212     24    124       C  
ATOM   8826  CG  LEU B 402      -3.829  13.594  -6.068  1.00 30.74           C  
ANISOU 8826  CG  LEU B 402     3758   3886   4034    196     43    122       C  
ATOM   8827  CD1 LEU B 402      -2.521  13.465  -6.833  1.00 31.31           C  
ANISOU 8827  CD1 LEU B 402     3846   3950   4099    199     57    128       C  
ATOM   8828  CD2 LEU B 402      -3.891  14.963  -5.406  1.00 29.40           C  
ANISOU 8828  CD2 LEU B 402     3581   3719   3871    188     56    111       C  
ATOM   8829  N   ASP B 403      -4.132   9.948  -7.253  1.00 32.77           N  
ANISOU 8829  N   ASP B 403     4028   4142   4280    214      7    145       N  
ATOM   8830  CA  ASP B 403      -3.937   8.714  -6.516  1.00 31.85           C  
ANISOU 8830  CA  ASP B 403     3893   4042   4164    206      2    151       C  
ATOM   8831  C   ASP B 403      -2.604   8.763  -5.787  1.00 31.24           C  
ANISOU 8831  C   ASP B 403     3802   3981   4086    194     21    153       C  
ATOM   8832  O   ASP B 403      -1.532   8.770  -6.408  1.00 29.44           O  
ANISOU 8832  O   ASP B 403     3587   3746   3851    197     33    158       O  
ATOM   8833  CB  ASP B 403      -4.016   7.498  -7.454  1.00 33.47           C  
ANISOU 8833  CB  ASP B 403     4115   4237   4364    217     -8    160       C  
ATOM   8834  CG  ASP B 403      -4.136   6.157  -6.697  1.00 35.69           C  
ANISOU 8834  CG  ASP B 403     4377   4534   4647    211    -16    165       C  
ATOM   8835  OD1 ASP B 403      -4.665   5.196  -7.296  1.00 36.39           O  
ANISOU 8835  OD1 ASP B 403     4476   4615   4734    218    -31    169       O  
ATOM   8836  OD2 ASP B 403      -3.703   6.050  -5.518  1.00 36.27           O  
ANISOU 8836  OD2 ASP B 403     4427   4629   4724    198     -8    165       O  
ATOM   8837  N   LEU B 404      -2.691   8.798  -4.459  1.00 30.63           N  
ANISOU 8837  N   LEU B 404     3697   3924   4013    181     23    148       N  
ATOM   8838  CA  LEU B 404      -1.515   8.799  -3.594  1.00 29.99           C  
ANISOU 8838  CA  LEU B 404     3599   3862   3931    169     38    149       C  
ATOM   8839  C   LEU B 404      -1.637   7.683  -2.569  1.00 29.70           C  
ANISOU 8839  C   LEU B 404     3540   3847   3896    162     31    154       C  
ATOM   8840  O   LEU B 404      -1.259   7.851  -1.403  1.00 29.71           O  
ANISOU 8840  O   LEU B 404     3519   3870   3900    150     38    151       O  
ATOM   8841  CB  LEU B 404      -1.370  10.147  -2.878  1.00 29.51           C  
ANISOU 8841  CB  LEU B 404     3528   3809   3875    158     50    138       C  
ATOM   8842  CG  LEU B 404      -1.226  11.416  -3.719  1.00 30.05           C  
ANISOU 8842  CG  LEU B 404     3616   3857   3943    163     60    133       C  
ATOM   8843  CD1 LEU B 404      -1.289  12.663  -2.849  1.00 29.93           C  
ANISOU 8843  CD1 LEU B 404     3588   3849   3933    152     70    121       C  
ATOM   8844  CD2 LEU B 404       0.068  11.384  -4.517  1.00 30.67           C  
ANISOU 8844  CD2 LEU B 404     3709   3926   4015    166     74    139       C  
ATOM   8845  N   SER B 405      -2.181   6.549  -2.999  1.00 29.07           N  
ANISOU 8845  N   SER B 405     3467   3763   3816    170     17    161       N  
ATOM   8846  CA  SER B 405      -2.404   5.434  -2.085  1.00 29.35           C  
ANISOU 8846  CA  SER B 405     3481   3815   3853    165     11    166       C  
ATOM   8847  C   SER B 405      -1.151   4.555  -1.890  1.00 28.72           C  
ANISOU 8847  C   SER B 405     3396   3747   3767    162     20    177       C  
ATOM   8848  O   SER B 405      -0.222   4.591  -2.702  1.00 27.91           O  
ANISOU 8848  O   SER B 405     3309   3635   3659    167     30    182       O  
ATOM   8849  CB  SER B 405      -3.622   4.607  -2.520  1.00 29.00           C  
ANISOU 8849  CB  SER B 405     3444   3761   3813    173     -7    168       C  
ATOM   8850  OG  SER B 405      -3.471   4.130  -3.838  1.00 28.78           O  
ANISOU 8850  OG  SER B 405     3441   3713   3779    185    -12    174       O  
ATOM   8851  N   PHE B 406      -1.138   3.789  -0.797  1.00 28.05           N  
ANISOU 8851  N   PHE B 406     3289   3684   3685    155     19    180       N  
ATOM   8852  CA  PHE B 406      -0.026   2.902  -0.468  1.00 28.11           C  
ANISOU 8852  CA  PHE B 406     3287   3704   3686    153     28    191       C  
ATOM   8853  C   PHE B 406       1.325   3.645  -0.517  1.00 28.54           C  
ANISOU 8853  C   PHE B 406     3342   3763   3737    148     45    191       C  
ATOM   8854  O   PHE B 406       2.235   3.275  -1.269  1.00 29.00           O  
ANISOU 8854  O   PHE B 406     3413   3814   3790    154     53    199       O  
ATOM   8855  CB  PHE B 406      -0.012   1.683  -1.401  1.00 26.85           C  
ANISOU 8855  CB  PHE B 406     3145   3531   3524    164     22    202       C  
ATOM   8856  CG  PHE B 406      -1.283   0.867  -1.373  1.00 27.02           C  
ANISOU 8856  CG  PHE B 406     3165   3548   3550    168      5    203       C  
ATOM   8857  CD1 PHE B 406      -2.289   1.067  -2.342  1.00 27.30           C  
ANISOU 8857  CD1 PHE B 406     3221   3562   3589    176     -7    198       C  
ATOM   8858  CD2 PHE B 406      -1.472  -0.134  -0.408  1.00 25.66           C  
ANISOU 8858  CD2 PHE B 406     2974   3394   3382    164      2    208       C  
ATOM   8859  CE1 PHE B 406      -3.458   0.300  -2.327  1.00 26.32           C  
ANISOU 8859  CE1 PHE B 406     3095   3434   3471    179    -23    198       C  
ATOM   8860  CE2 PHE B 406      -2.633  -0.896  -0.392  1.00 25.33           C  
ANISOU 8860  CE2 PHE B 406     2931   3346   3345    167    -11    209       C  
ATOM   8861  CZ  PHE B 406      -3.626  -0.679  -1.346  1.00 25.96           C  
ANISOU 8861  CZ  PHE B 406     3028   3404   3428    174    -24    203       C  
ATOM   8862  N   ASN B 407       1.443   4.703   0.275  1.00 27.80           N  
ANISOU 8862  N   ASN B 407     3234   3681   3645    138     52    180       N  
ATOM   8863  CA  ASN B 407       2.673   5.486   0.325  1.00 27.89           C  
ANISOU 8863  CA  ASN B 407     3244   3699   3655    131     68    178       C  
ATOM   8864  C   ASN B 407       3.125   5.757   1.757  1.00 27.68           C  
ANISOU 8864  C   ASN B 407     3189   3700   3628    117     74    174       C  
ATOM   8865  O   ASN B 407       2.494   5.294   2.715  1.00 27.57           O  
ANISOU 8865  O   ASN B 407     3157   3701   3615    113     66    173       O  
ATOM   8866  CB  ASN B 407       2.500   6.802  -0.447  1.00 28.00           C  
ANISOU 8866  CB  ASN B 407     3276   3693   3671    133     73    169       C  
ATOM   8867  CG  ASN B 407       2.459   6.593  -1.948  1.00 28.52           C  
ANISOU 8867  CG  ASN B 407     3370   3731   3733    147     71    174       C  
ATOM   8868  OD1 ASN B 407       3.291   5.872  -2.504  1.00 29.59           O  
ANISOU 8868  OD1 ASN B 407     3514   3864   3864    153     76    185       O  
ATOM   8869  ND2 ASN B 407       1.498   7.228  -2.615  1.00 27.71           N  
ANISOU 8869  ND2 ASN B 407     3285   3610   3633    154     63    168       N  
ATOM   8870  N   GLY B 408       4.214   6.512   1.899  1.00 27.22           N  
ANISOU 8870  N   GLY B 408     3125   3647   3567    109     88    170       N  
ATOM   8871  CA  GLY B 408       4.748   6.862   3.216  1.00 27.31           C  
ANISOU 8871  CA  GLY B 408     3111   3686   3578     95     94    164       C  
ATOM   8872  C   GLY B 408       3.936   7.899   3.975  1.00 27.42           C  
ANISOU 8872  C   GLY B 408     3116   3705   3597     86     92    149       C  
ATOM   8873  O   GLY B 408       2.700   7.812   4.062  1.00 27.69           O  
ANISOU 8873  O   GLY B 408     3152   3733   3634     90     81    146       O  
ATOM   8874  N   ALA B 409       4.636   8.876   4.543  1.00 27.18           N  
ANISOU 8874  N   ALA B 409     3075   3686   3566     74    103    139       N  
ATOM   8875  CA  ALA B 409       3.995   9.923   5.317  1.00 27.60           C  
ANISOU 8875  CA  ALA B 409     3119   3744   3622     64    103    124       C  
ATOM   8876  C   ALA B 409       3.608  11.081   4.403  1.00 28.69           C  
ANISOU 8876  C   ALA B 409     3279   3856   3766     67    108    115       C  
ATOM   8877  O   ALA B 409       4.468  11.671   3.743  1.00 28.89           O  
ANISOU 8877  O   ALA B 409     3314   3870   3790     66    120    114       O  
ATOM   8878  CB  ALA B 409       4.911  10.398   6.431  1.00 26.69           C  
ANISOU 8878  CB  ALA B 409     2982   3654   3504     48    112    117       C  
ATOM   8879  N   ILE B 410       2.310  11.384   4.360  1.00 28.91           N  
ANISOU 8879  N   ILE B 410     3313   3873   3798     72     99    110       N  
ATOM   8880  CA  ILE B 410       1.801  12.526   3.614  1.00 29.58           C  
ANISOU 8880  CA  ILE B 410     3416   3934   3887     75    102    101       C  
ATOM   8881  C   ILE B 410       1.266  13.590   4.559  1.00 31.31           C  
ANISOU 8881  C   ILE B 410     3624   4160   4110     64    106     86       C  
ATOM   8882  O   ILE B 410       0.231  13.424   5.221  1.00 32.30           O  
ANISOU 8882  O   ILE B 410     3740   4292   4237     64     96     83       O  
ATOM   8883  CB  ILE B 410       0.744  12.111   2.577  1.00 29.99           C  
ANISOU 8883  CB  ILE B 410     3489   3964   3942     91     90    107       C  
ATOM   8884  CG1 ILE B 410       1.408  11.223   1.509  1.00 29.88           C  
ANISOU 8884  CG1 ILE B 410     3489   3939   3923    102     89    121       C  
ATOM   8885  CG2 ILE B 410       0.113  13.351   1.951  1.00 28.92           C  
ANISOU 8885  CG2 ILE B 410     3370   3807   3811     95     93     98       C  
ATOM   8886  CD1 ILE B 410       0.450  10.374   0.710  1.00 31.02           C  
ANISOU 8886  CD1 ILE B 410     3648   4069   4068    116     74    129       C  
ATOM   8887  N   ILE B 411       1.999  14.690   4.629  1.00 33.30           N  
ANISOU 8887  N   ILE B 411     3876   4411   4363     55    120     77       N  
ATOM   8888  CA  ILE B 411       1.702  15.729   5.590  1.00 34.02           C  
ANISOU 8888  CA  ILE B 411     3956   4511   4457     43    126     61       C  
ATOM   8889  C   ILE B 411       0.844  16.805   4.934  1.00 35.04           C  
ANISOU 8889  C   ILE B 411     4104   4615   4593     49    128     54       C  
ATOM   8890  O   ILE B 411       1.277  17.485   4.005  1.00 35.06           O  
ANISOU 8890  O   ILE B 411     4125   4599   4598     52    139     53       O  
ATOM   8891  CB  ILE B 411       2.995  16.323   6.184  1.00 34.02           C  
ANISOU 8891  CB  ILE B 411     3944   4526   4455     27    141     54       C  
ATOM   8892  CG1 ILE B 411       3.927  15.195   6.642  1.00 33.64           C  
ANISOU 8892  CG1 ILE B 411     3879   4501   4401     23    138     64       C  
ATOM   8893  CG2 ILE B 411       2.661  17.270   7.329  1.00 33.60           C  
ANISOU 8893  CG2 ILE B 411     3877   4485   4404     13    145     37       C  
ATOM   8894  CD1 ILE B 411       5.324  15.650   7.005  1.00 35.07           C  
ANISOU 8894  CD1 ILE B 411     4049   4695   4579     10    152     59       C  
ATOM   8895  N   MET B 412      -0.382  16.922   5.431  1.00 35.75           N  
ANISOU 8895  N   MET B 412     4190   4706   4686     51    120     49       N  
ATOM   8896  CA  MET B 412      -1.342  17.903   4.976  1.00 35.29           C  
ANISOU 8896  CA  MET B 412     4146   4628   4635     57    121     42       C  
ATOM   8897  C   MET B 412      -1.028  19.258   5.578  1.00 35.60           C  
ANISOU 8897  C   MET B 412     4181   4668   4676     44    137     26       C  
ATOM   8898  O   MET B 412      -1.030  19.420   6.800  1.00 35.10           O  
ANISOU 8898  O   MET B 412     4098   4624   4611     31    138     18       O  
ATOM   8899  CB  MET B 412      -2.751  17.474   5.403  1.00 36.07           C  
ANISOU 8899  CB  MET B 412     4238   4728   4736     63    106     43       C  
ATOM   8900  CG  MET B 412      -3.207  16.135   4.836  1.00 37.58           C  
ANISOU 8900  CG  MET B 412     4433   4918   4926     76     90     57       C  
ATOM   8901  SD  MET B 412      -3.075  16.009   3.035  1.00 40.15           S  
ANISOU 8901  SD  MET B 412     4788   5214   5251     93     87     67       S  
ATOM   8902  CE  MET B 412      -4.176  17.320   2.505  1.00 39.42           C  
ANISOU 8902  CE  MET B 412     4712   5098   5165    101     89     58       C  
ATOM   8903  N   SER B 413      -0.767  20.234   4.717  1.00 37.19           N  
ANISOU 8903  N   SER B 413     4401   4848   4881     47    148     22       N  
ATOM   8904  CA  SER B 413      -0.535  21.610   5.163  1.00 37.35           C  
ANISOU 8904  CA  SER B 413     4420   4865   4904     35    165      7       C  
ATOM   8905  C   SER B 413      -1.368  22.650   4.395  1.00 37.92           C  
ANISOU 8905  C   SER B 413     4513   4909   4983     45    170      3       C  
ATOM   8906  O   SER B 413      -1.513  23.788   4.848  1.00 38.25           O  
ANISOU 8906  O   SER B 413     4554   4948   5029     37    181     -9       O  
ATOM   8907  CB  SER B 413       0.950  21.946   5.069  1.00 37.72           C  
ANISOU 8907  CB  SER B 413     4466   4915   4949     23    180      4       C  
ATOM   8908  OG  SER B 413       1.374  21.933   3.723  1.00 39.34           O  
ANISOU 8908  OG  SER B 413     4693   5099   5155     35    184     13       O  
ATOM   8909  N   ALA B 414      -1.906  22.250   3.243  1.00 37.82           N  
ANISOU 8909  N   ALA B 414     4519   4879   4971     63    160     14       N  
ATOM   8910  CA  ALA B 414      -2.725  23.121   2.390  1.00 37.84           C  
ANISOU 8910  CA  ALA B 414     4542   4855   4978     76    163     13       C  
ATOM   8911  C   ALA B 414      -3.979  22.389   1.914  1.00 36.70           C  
ANISOU 8911  C   ALA B 414     4404   4705   4835     92    143     22       C  
ATOM   8912  O   ALA B 414      -3.907  21.223   1.523  1.00 38.06           O  
ANISOU 8912  O   ALA B 414     4577   4881   5003     99    130     33       O  
ATOM   8913  CB  ALA B 414      -1.913  23.619   1.198  1.00 37.98           C  
ANISOU 8913  CB  ALA B 414     4583   4852   4995     82    176     16       C  
ATOM   8914  N   ASN B 415      -5.125  23.064   1.942  1.00 35.02           N  
ANISOU 8914  N   ASN B 415     4195   4481   4627     99    141     17       N  
ATOM   8915  CA  ASN B 415      -6.385  22.405   1.602  1.00 34.44           C  
ANISOU 8915  CA  ASN B 415     4124   4404   4556    113    121     25       C  
ATOM   8916  C   ASN B 415      -6.771  22.484   0.127  1.00 34.57           C  
ANISOU 8916  C   ASN B 415     4167   4395   4572    133    115     33       C  
ATOM   8917  O   ASN B 415      -7.883  22.882  -0.209  1.00 33.33           O  
ANISOU 8917  O   ASN B 415     4017   4226   4419    144    109     33       O  
ATOM   8918  CB  ASN B 415      -7.522  22.904   2.488  1.00 34.83           C  
ANISOU 8918  CB  ASN B 415     4161   4458   4612    111    118     17       C  
ATOM   8919  CG  ASN B 415      -7.540  24.411   2.634  1.00 35.46           C  
ANISOU 8919  CG  ASN B 415     4249   4526   4697    107    137      5       C  
ATOM   8920  OD1 ASN B 415      -6.871  25.138   1.894  1.00 36.68           O  
ANISOU 8920  OD1 ASN B 415     4420   4665   4851    109    151      4       O  
ATOM   8921  ND2 ASN B 415      -8.316  24.890   3.596  1.00 35.45           N  
ANISOU 8921  ND2 ASN B 415     4235   4533   4701    102    138     -3       N  
ATOM   8922  N   PHE B 416      -5.830  22.105  -0.739  1.00 34.95           N  
ANISOU 8922  N   PHE B 416     4228   4436   4614    137    119     40       N  
ATOM   8923  CA  PHE B 416      -6.049  21.962  -2.191  1.00 34.44           C  
ANISOU 8923  CA  PHE B 416     4189   4349   4546    155    112     50       C  
ATOM   8924  C   PHE B 416      -6.462  23.246  -2.934  1.00 34.40           C  
ANISOU 8924  C   PHE B 416     4205   4321   4544    166    122     46       C  
ATOM   8925  O   PHE B 416      -7.141  23.168  -3.956  1.00 34.43           O  
ANISOU 8925  O   PHE B 416     4226   4309   4546    184    112     53       O  
ATOM   8926  CB  PHE B 416      -7.043  20.819  -2.500  1.00 33.97           C  
ANISOU 8926  CB  PHE B 416     4128   4292   4486    167     88     58       C  
ATOM   8927  CG  PHE B 416      -6.614  19.468  -1.995  1.00 33.38           C  
ANISOU 8927  CG  PHE B 416     4037   4236   4406    160     78     64       C  
ATOM   8928  CD1 PHE B 416      -6.900  19.071  -0.694  1.00 33.70           C  
ANISOU 8928  CD1 PHE B 416     4052   4299   4450    147     74     60       C  
ATOM   8929  CD2 PHE B 416      -5.952  18.577  -2.827  1.00 33.37           C  
ANISOU 8929  CD2 PHE B 416     4047   4231   4398    166     74     74       C  
ATOM   8930  CE1 PHE B 416      -6.516  17.823  -0.225  1.00 33.58           C  
ANISOU 8930  CE1 PHE B 416     4022   4302   4432    142     66     66       C  
ATOM   8931  CE2 PHE B 416      -5.564  17.328  -2.364  1.00 33.21           C  
ANISOU 8931  CE2 PHE B 416     4014   4229   4376    160     66     80       C  
ATOM   8932  CZ  PHE B 416      -5.839  16.952  -1.057  1.00 32.94           C  
ANISOU 8932  CZ  PHE B 416     3953   4216   4344    148     62     76       C  
ATOM   8933  N   MET B 417      -6.058  24.417  -2.440  1.00 35.24           N  
ANISOU 8933  N   MET B 417     4309   4425   4654    156    142     36       N  
ATOM   8934  CA  MET B 417      -6.302  25.659  -3.181  1.00 36.38           C  
ANISOU 8934  CA  MET B 417     4474   4546   4802    166    155     33       C  
ATOM   8935  C   MET B 417      -5.749  25.509  -4.596  1.00 36.72           C  
ANISOU 8935  C   MET B 417     4542   4569   4837    180    157     43       C  
ATOM   8936  O   MET B 417      -4.558  25.224  -4.787  1.00 36.23           O  
ANISOU 8936  O   MET B 417     4483   4510   4772    173    166     46       O  
ATOM   8937  CB  MET B 417      -5.658  26.887  -2.524  1.00 38.75           C  
ANISOU 8937  CB  MET B 417     4770   4845   5106    151    179     21       C  
ATOM   8938  CG  MET B 417      -5.721  26.946  -1.004  1.00 43.15           C  
ANISOU 8938  CG  MET B 417     5300   5424   5667    132    181     10       C  
ATOM   8939  SD  MET B 417      -4.392  26.021  -0.191  1.00 46.74           S  
ANISOU 8939  SD  MET B 417     5734   5906   6117    112    182      9       S  
ATOM   8940  CE  MET B 417      -2.935  26.965  -0.651  1.00 41.66           C  
ANISOU 8940  CE  MET B 417     5103   5249   5474    104    209      4       C  
ATOM   8941  N   GLY B 418      -6.624  25.676  -5.583  1.00 36.47           N  
ANISOU 8941  N   GLY B 418     4530   4520   4804    200    148     49       N  
ATOM   8942  CA  GLY B 418      -6.205  25.676  -6.973  1.00 36.32           C  
ANISOU 8942  CA  GLY B 418     4539   4482   4779    215    151     58       C  
ATOM   8943  C   GLY B 418      -6.501  24.379  -7.680  1.00 36.29           C  
ANISOU 8943  C   GLY B 418     4541   4479   4768    227    128     69       C  
ATOM   8944  O   GLY B 418      -6.323  24.282  -8.894  1.00 37.77           O  
ANISOU 8944  O   GLY B 418     4752   4650   4948    242    127     78       O  
ATOM   8945  N   LEU B 419      -6.944  23.381  -6.921  1.00 35.69           N  
ANISOU 8945  N   LEU B 419     4444   4423   4693    220    111     70       N  
ATOM   8946  CA  LEU B 419      -7.193  22.050  -7.466  1.00 36.26           C  
ANISOU 8946  CA  LEU B 419     4519   4498   4759    229     90     79       C  
ATOM   8947  C   LEU B 419      -8.663  21.644  -7.348  1.00 37.47           C  
ANISOU 8947  C   LEU B 419     4664   4654   4916    237     67     80       C  
ATOM   8948  O   LEU B 419      -8.973  20.469  -7.189  1.00 37.64           O  
ANISOU 8948  O   LEU B 419     4676   4687   4936    236     49     84       O  
ATOM   8949  CB  LEU B 419      -6.304  21.005  -6.785  1.00 34.68           C  
ANISOU 8949  CB  LEU B 419     4301   4317   4556    214     89     81       C  
ATOM   8950  CG  LEU B 419      -4.781  21.173  -6.750  1.00 35.25           C  
ANISOU 8950  CG  LEU B 419     4374   4391   4626    204    110     81       C  
ATOM   8951  CD1 LEU B 419      -4.153  20.144  -5.807  1.00 34.62           C  
ANISOU 8951  CD1 LEU B 419     4271   4336   4545    188    107     82       C  
ATOM   8952  CD2 LEU B 419      -4.159  21.091  -8.141  1.00 33.39           C  
ANISOU 8952  CD2 LEU B 419     4167   4136   4382    217    115     90       C  
ATOM   8953  N   GLU B 420      -9.566  22.612  -7.457  1.00 39.74           N  
ANISOU 8953  N   GLU B 420     4957   4931   5209    245     67     76       N  
ATOM   8954  CA  GLU B 420     -10.995  22.345  -7.294  1.00 41.07           C  
ANISOU 8954  CA  GLU B 420     5117   5103   5382    253     47     76       C  
ATOM   8955  C   GLU B 420     -11.649  21.514  -8.402  1.00 41.34           C  
ANISOU 8955  C   GLU B 420     5166   5129   5411    271     24     85       C  
ATOM   8956  O   GLU B 420     -12.791  21.092  -8.255  1.00 43.72           O  
ANISOU 8956  O   GLU B 420     5458   5435   5717    275      5     85       O  
ATOM   8957  CB  GLU B 420     -11.791  23.627  -7.005  1.00 43.08           C  
ANISOU 8957  CB  GLU B 420     5371   5350   5645    257     55     69       C  
ATOM   8958  CG  GLU B 420     -11.357  24.870  -7.763  1.00 48.15           C  
ANISOU 8958  CG  GLU B 420     6037   5972   6285    265     74     69       C  
ATOM   8959  CD  GLU B 420     -10.095  25.515  -7.211  1.00 51.38           C  
ANISOU 8959  CD  GLU B 420     6442   6382   6694    249    101     62       C  
ATOM   8960  OE1 GLU B 420      -9.886  25.488  -5.975  1.00 54.54           O  
ANISOU 8960  OE1 GLU B 420     6820   6801   7100    230    106     54       O  
ATOM   8961  OE2 GLU B 420      -9.311  26.057  -8.025  1.00 53.65           O  
ANISOU 8961  OE2 GLU B 420     6751   6654   6977    254    116     65       O  
ATOM   8962  N   GLU B 421     -10.925  21.239  -9.483  1.00 41.95           N  
ANISOU 8962  N   GLU B 421     5266   5194   5478    279     26     92       N  
ATOM   8963  CA  GLU B 421     -11.427  20.319 -10.514  1.00 42.82           C  
ANISOU 8963  CA  GLU B 421     5390   5297   5581    294      4    100       C  
ATOM   8964  C   GLU B 421     -11.425  18.830 -10.115  1.00 40.56           C  
ANISOU 8964  C   GLU B 421     5089   5027   5295    286    -11    103       C  
ATOM   8965  O   GLU B 421     -12.047  18.008 -10.801  1.00 39.03           O  
ANISOU 8965  O   GLU B 421     4902   4829   5096    297    -32    107       O  
ATOM   8966  CB  GLU B 421     -10.669  20.498 -11.840  1.00 46.88           C  
ANISOU 8966  CB  GLU B 421     5935   5792   6083    308     12    106       C  
ATOM   8967  CG  GLU B 421     -10.796  21.871 -12.494  1.00 52.11           C  
ANISOU 8967  CG  GLU B 421     6618   6435   6745    320     25    105       C  
ATOM   8968  CD  GLU B 421     -12.226  22.403 -12.562  1.00 54.66           C  
ANISOU 8968  CD  GLU B 421     6940   6754   7074    332     11    104       C  
ATOM   8969  OE1 GLU B 421     -13.162  21.619 -12.859  1.00 51.70           O  
ANISOU 8969  OE1 GLU B 421     6562   6382   6698    340    -13    106       O  
ATOM   8970  OE2 GLU B 421     -12.404  23.623 -12.319  1.00 56.08           O  
ANISOU 8970  OE2 GLU B 421     7120   6927   7259    333     26     99       O  
ATOM   8971  N   LEU B 422     -10.728  18.496  -9.023  1.00 38.14           N  
ANISOU 8971  N   LEU B 422     4761   4738   4992    268     -2    100       N  
ATOM   8972  CA  LEU B 422     -10.548  17.108  -8.568  1.00 36.66           C  
ANISOU 8972  CA  LEU B 422     4558   4565   4803    260    -13    103       C  
ATOM   8973  C   LEU B 422     -11.838  16.341  -8.366  1.00 36.98           C  
ANISOU 8973  C   LEU B 422     4587   4613   4850    263    -37    104       C  
ATOM   8974  O   LEU B 422     -12.738  16.815  -7.683  1.00 37.38           O  
ANISOU 8974  O   LEU B 422     4623   4669   4910    260    -41     98       O  
ATOM   8975  CB  LEU B 422      -9.762  17.055  -7.252  1.00 35.13           C  
ANISOU 8975  CB  LEU B 422     4340   4391   4613    239      0     99       C  
ATOM   8976  CG  LEU B 422      -8.353  16.457  -7.219  1.00 34.29           C  
ANISOU 8976  CG  LEU B 422     4235   4292   4501    231     12    103       C  
ATOM   8977  CD1 LEU B 422      -8.019  16.083  -5.783  1.00 34.43           C  
ANISOU 8977  CD1 LEU B 422     4224   4334   4524    213     17     99       C  
ATOM   8978  CD2 LEU B 422      -8.205  15.240  -8.120  1.00 33.18           C  
ANISOU 8978  CD2 LEU B 422     4108   4146   4352    240      0    113       C  
ATOM   8979  N   GLN B 423     -11.900  15.138  -8.938  1.00 37.73           N  
ANISOU 8979  N   GLN B 423     4687   4707   4939    268    -53    110       N  
ATOM   8980  CA  GLN B 423     -13.055  14.243  -8.792  1.00 36.43           C  
ANISOU 8980  CA  GLN B 423     4511   4548   4780    270    -76    110       C  
ATOM   8981  C   GLN B 423     -12.727  12.985  -8.000  1.00 35.47           C  
ANISOU 8981  C   GLN B 423     4370   4444   4661    257    -80    113       C  
ATOM   8982  O   GLN B 423     -13.594  12.407  -7.345  1.00 35.17           O  
ANISOU 8982  O   GLN B 423     4313   4416   4632    253    -93    112       O  
ATOM   8983  CB  GLN B 423     -13.574  13.830 -10.162  1.00 37.01           C  
ANISOU 8983  CB  GLN B 423     4608   4606   4847    287    -95    115       C  
ATOM   8984  CG  GLN B 423     -14.164  14.977 -10.963  1.00 39.56           C  
ANISOU 8984  CG  GLN B 423     4949   4913   5169    302    -96    113       C  
ATOM   8985  CD  GLN B 423     -14.731  14.526 -12.294  1.00 41.64           C  
ANISOU 8985  CD  GLN B 423     5235   5162   5424    320   -116    118       C  
ATOM   8986  OE1 GLN B 423     -15.852  14.894 -12.655  1.00 42.95           O  
ANISOU 8986  OE1 GLN B 423     5402   5322   5594    331   -130    116       O  
ATOM   8987  NE2 GLN B 423     -13.965  13.709 -13.029  1.00 40.41           N  
ANISOU 8987  NE2 GLN B 423     5095   5000   5257    323   -117    123       N  
ATOM   8988  N   HIS B 424     -11.462  12.574  -8.070  1.00 34.73           N  
ANISOU 8988  N   HIS B 424     4282   4352   4559    252    -68    117       N  
ATOM   8989  CA  HIS B 424     -10.996  11.327  -7.483  1.00 32.84           C  
ANISOU 8989  CA  HIS B 424     4029   4128   4320    242    -70    121       C  
ATOM   8990  C   HIS B 424      -9.764  11.573  -6.648  1.00 31.43           C  
ANISOU 8990  C   HIS B 424     3839   3962   4140    228    -48    121       C  
ATOM   8991  O   HIS B 424      -8.731  11.995  -7.164  1.00 32.02           O  
ANISOU 8991  O   HIS B 424     3928   4029   4207    230    -34    123       O  
ATOM   8992  CB  HIS B 424     -10.705  10.337  -8.604  1.00 33.09           C  
ANISOU 8992  CB  HIS B 424     4081   4149   4343    251    -79    129       C  
ATOM   8993  CG  HIS B 424     -10.637   8.895  -8.156  1.00 34.34           C  
ANISOU 8993  CG  HIS B 424     4226   4319   4503    245    -88    134       C  
ATOM   8994  ND1 HIS B 424      -9.469   8.272  -7.874  1.00 35.23           N  
ANISOU 8994  ND1 HIS B 424     4336   4439   4610    237    -76    139       N  
ATOM   8995  CD2 HIS B 424     -11.636   7.950  -7.975  1.00 33.48           C  
ANISOU 8995  CD2 HIS B 424     4106   4214   4400    245   -107    134       C  
ATOM   8996  CE1 HIS B 424      -9.715   7.001  -7.525  1.00 33.18           C  
ANISOU 8996  CE1 HIS B 424     4065   4188   4353    233    -86    143       C  
ATOM   8997  NE2 HIS B 424     -11.038   6.807  -7.576  1.00 33.15           N  
ANISOU 8997  NE2 HIS B 424     4056   4182   4356    237   -105    140       N  
ATOM   8998  N   LEU B 425      -9.873  11.332  -5.344  1.00 29.55           N  
ANISOU 8998  N   LEU B 425     3574   3744   3909    215    -46    118       N  
ATOM   8999  CA  LEU B 425      -8.748  11.468  -4.429  1.00 28.88           C  
ANISOU 8999  CA  LEU B 425     3475   3674   3822    201    -28    117       C  
ATOM   9000  C   LEU B 425      -8.596  10.205  -3.570  1.00 28.92           C  
ANISOU 9000  C   LEU B 425     3460   3698   3829    192    -33    122       C  
ATOM   9001  O   LEU B 425      -9.532   9.796  -2.874  1.00 27.43           O  
ANISOU 9001  O   LEU B 425     3254   3518   3647    189    -43    120       O  
ATOM   9002  CB  LEU B 425      -8.908  12.722  -3.565  1.00 28.09           C  
ANISOU 9002  CB  LEU B 425     3364   3581   3729    193    -16    107       C  
ATOM   9003  CG  LEU B 425      -7.764  13.133  -2.632  1.00 28.05           C  
ANISOU 9003  CG  LEU B 425     3345   3590   3722    178      2    104       C  
ATOM   9004  CD1 LEU B 425      -6.398  13.132  -3.301  1.00 27.74           C  
ANISOU 9004  CD1 LEU B 425     3320   3545   3674    179     16    109       C  
ATOM   9005  CD2 LEU B 425      -8.036  14.499  -2.051  1.00 28.08           C  
ANISOU 9005  CD2 LEU B 425     3343   3594   3731    173     13     93       C  
ATOM   9006  N   ASP B 426      -7.415   9.584  -3.648  1.00 30.34           N  
ANISOU 9006  N   ASP B 426     3642   3882   4001    189    -24    128       N  
ATOM   9007  CA  ASP B 426      -7.176   8.264  -3.035  1.00 30.91           C  
ANISOU 9007  CA  ASP B 426     3700   3970   4074    183    -28    135       C  
ATOM   9008  C   ASP B 426      -5.882   8.237  -2.248  1.00 30.40           C  
ANISOU 9008  C   ASP B 426     3622   3922   4005    171    -11    137       C  
ATOM   9009  O   ASP B 426      -4.793   8.366  -2.826  1.00 30.11           O  
ANISOU 9009  O   ASP B 426     3598   3880   3961    173      0    140       O  
ATOM   9010  CB  ASP B 426      -7.160   7.158  -4.104  1.00 33.32           C  
ANISOU 9010  CB  ASP B 426     4022   4262   4373    193    -39    144       C  
ATOM   9011  CG  ASP B 426      -7.250   5.748  -3.507  1.00 35.78           C  
ANISOU 9011  CG  ASP B 426     4318   4587   4687    189    -46    150       C  
ATOM   9012  OD1 ASP B 426      -7.239   5.603  -2.257  1.00 35.95           O  
ANISOU 9012  OD1 ASP B 426     4316   4629   4713    178    -42    149       O  
ATOM   9013  OD2 ASP B 426      -7.335   4.778  -4.301  1.00 36.65           O  
ANISOU 9013  OD2 ASP B 426     4442   4687   4794    197    -56    157       O  
ATOM   9014  N   PHE B 427      -6.031   8.068  -0.932  1.00 30.20           N  
ANISOU 9014  N   PHE B 427     3571   3918   3984    160    -10    134       N  
ATOM   9015  CA  PHE B 427      -4.924   8.009   0.036  1.00 29.93           C  
ANISOU 9015  CA  PHE B 427     3521   3905   3947    148      3    135       C  
ATOM   9016  C   PHE B 427      -4.846   6.667   0.774  1.00 29.40           C  
ANISOU 9016  C   PHE B 427     3435   3854   3879    144      0    143       C  
ATOM   9017  O   PHE B 427      -4.041   6.529   1.694  1.00 30.38           O  
ANISOU 9017  O   PHE B 427     3544   3999   4001    135      8    145       O  
ATOM   9018  CB  PHE B 427      -5.093   9.067   1.137  1.00 30.07           C  
ANISOU 9018  CB  PHE B 427     3520   3934   3968    137     11    124       C  
ATOM   9019  CG  PHE B 427      -4.912  10.480   0.690  1.00 31.35           C  
ANISOU 9019  CG  PHE B 427     3695   4084   4131    138     21    116       C  
ATOM   9020  CD1 PHE B 427      -5.992  11.356   0.684  1.00 32.41           C  
ANISOU 9020  CD1 PHE B 427     3831   4209   4271    140     17    108       C  
ATOM   9021  CD2 PHE B 427      -3.660  10.964   0.333  1.00 32.01           C  
ANISOU 9021  CD2 PHE B 427     3786   4165   4208    135     37    116       C  
ATOM   9022  CE1 PHE B 427      -5.826  12.682   0.301  1.00 32.13           C  
ANISOU 9022  CE1 PHE B 427     3809   4162   4237    141     28    100       C  
ATOM   9023  CE2 PHE B 427      -3.493  12.285  -0.060  1.00 31.27           C  
ANISOU 9023  CE2 PHE B 427     3705   4059   4116    135     47    108       C  
ATOM   9024  CZ  PHE B 427      -4.576  13.142  -0.078  1.00 31.28           C  
ANISOU 9024  CZ  PHE B 427     3710   4051   4124    138     43    100       C  
ATOM   9025  N   GLN B 428      -5.691   5.698   0.426  1.00 28.54           N  
ANISOU 9025  N   GLN B 428     3331   3739   3774    152    -15    149       N  
ATOM   9026  CA  GLN B 428      -5.791   4.478   1.236  1.00 28.54           C  
ANISOU 9026  CA  GLN B 428     3313   3755   3775    148    -19    156       C  
ATOM   9027  C   GLN B 428      -4.406   3.895   1.548  1.00 28.81           C  
ANISOU 9027  C   GLN B 428     3341   3803   3801    143     -7    164       C  
ATOM   9028  O   GLN B 428      -3.518   3.864   0.684  1.00 27.61           O  
ANISOU 9028  O   GLN B 428     3205   3641   3643    148     -1    169       O  
ATOM   9029  CB  GLN B 428      -6.754   3.427   0.626  1.00 27.90           C  
ANISOU 9029  CB  GLN B 428     3239   3661   3698    156    -36    161       C  
ATOM   9030  CG  GLN B 428      -6.208   2.615  -0.544  1.00 27.66           C  
ANISOU 9030  CG  GLN B 428     3230   3617   3662    165    -38    169       C  
ATOM   9031  CD  GLN B 428      -7.011   1.363  -0.855  1.00 27.24           C  
ANISOU 9031  CD  GLN B 428     3180   3558   3613    171    -53    175       C  
ATOM   9032  OE1 GLN B 428      -7.544   0.711   0.037  1.00 28.27           O  
ANISOU 9032  OE1 GLN B 428     3291   3700   3749    166    -57    177       O  
ATOM   9033  NE2 GLN B 428      -7.080   1.011  -2.127  1.00 26.48           N  
ANISOU 9033  NE2 GLN B 428     3106   3440   3512    181    -61    178       N  
ATOM   9034  N   HIS B 429      -4.228   3.493   2.806  1.00 29.56           N  
ANISOU 9034  N   HIS B 429     3413   3921   3897    135     -3    166       N  
ATOM   9035  CA  HIS B 429      -2.997   2.841   3.299  1.00 30.15           C  
ANISOU 9035  CA  HIS B 429     3478   4013   3965    131      6    175       C  
ATOM   9036  C   HIS B 429      -1.763   3.681   3.409  1.00 31.36           C  
ANISOU 9036  C   HIS B 429     3630   4173   4112    124     21    171       C  
ATOM   9037  O   HIS B 429      -0.732   3.178   3.845  1.00 33.45           O  
ANISOU 9037  O   HIS B 429     3884   4453   4371    121     29    179       O  
ATOM   9038  CB  HIS B 429      -2.695   1.553   2.545  1.00 29.53           C  
ANISOU 9038  CB  HIS B 429     3410   3925   3883    139      2    187       C  
ATOM   9039  CG  HIS B 429      -3.568   0.396   2.965  1.00 30.79           C  
ANISOU 9039  CG  HIS B 429     3561   4089   4048    141     -7    193       C  
ATOM   9040  ND1 HIS B 429      -3.317  -0.339   4.065  1.00 30.43           N  
ANISOU 9040  ND1 HIS B 429     3495   4065   4002    136     -3    199       N  
ATOM   9041  CD2 HIS B 429      -4.731  -0.121   2.406  1.00 30.67           C  
ANISOU 9041  CD2 HIS B 429     3555   4058   4040    148    -22    193       C  
ATOM   9042  CE1 HIS B 429      -4.260  -1.286   4.190  1.00 30.03           C  
ANISOU 9042  CE1 HIS B 429     3441   4010   3957    139    -13    203       C  
ATOM   9043  NE2 HIS B 429      -5.124  -1.148   3.178  1.00 30.57           N  
ANISOU 9043  NE2 HIS B 429     3527   4057   4030    146    -25    199       N  
ATOM   9044  N   SER B 430      -1.850   4.957   3.025  1.00 31.34           N  
ANISOU 9044  N   SER B 430     3637   4160   4111    123     24    161       N  
ATOM   9045  CA  SER B 430      -0.765   5.913   3.238  1.00 30.91           C  
ANISOU 9045  CA  SER B 430     3579   4112   4053    115     39    156       C  
ATOM   9046  C   SER B 430      -0.862   6.481   4.647  1.00 31.19           C  
ANISOU 9046  C   SER B 430     3591   4170   4089    102     43    147       C  
ATOM   9047  O   SER B 430      -1.872   6.325   5.307  1.00 32.29           O  
ANISOU 9047  O   SER B 430     3720   4315   4233    101     35    144       O  
ATOM   9048  CB  SER B 430      -0.831   7.039   2.208  1.00 31.27           C  
ANISOU 9048  CB  SER B 430     3646   4135   4099    120     43    149       C  
ATOM   9049  OG  SER B 430      -0.769   6.533   0.886  1.00 31.75           O  
ANISOU 9049  OG  SER B 430     3730   4175   4158    132     39    156       O  
ATOM   9050  N   THR B 431       0.188   7.132   5.117  1.00 32.30           N  
ANISOU 9050  N   THR B 431     3722   4322   4225     93     56    143       N  
ATOM   9051  CA  THR B 431       0.166   7.703   6.454  1.00 33.20           C  
ANISOU 9051  CA  THR B 431     3815   4459   4339     80     60    133       C  
ATOM   9052  C   THR B 431      -0.236   9.167   6.360  1.00 33.89           C  
ANISOU 9052  C   THR B 431     3909   4535   4431     76     65    119       C  
ATOM   9053  O   THR B 431       0.603  10.026   6.099  1.00 34.91           O  
ANISOU 9053  O   THR B 431     4043   4661   4559     71     76    113       O  
ATOM   9054  CB  THR B 431       1.544   7.590   7.149  1.00 33.32           C  
ANISOU 9054  CB  THR B 431     3814   4496   4347     71     71    136       C  
ATOM   9055  OG1 THR B 431       2.093   6.278   6.944  1.00 32.05           O  
ANISOU 9055  OG1 THR B 431     3652   4341   4182     77     69    151       O  
ATOM   9056  CG2 THR B 431       1.407   7.864   8.642  1.00 33.25           C  
ANISOU 9056  CG2 THR B 431     3781   4513   4336     59     72    128       C  
ATOM   9057  N   LEU B 432      -1.518   9.443   6.554  1.00 34.46           N  
ANISOU 9057  N   LEU B 432     3981   4601   4509     78     56    113       N  
ATOM   9058  CA  LEU B 432      -2.012  10.815   6.543  1.00 36.61           C  
ANISOU 9058  CA  LEU B 432     4259   4863   4786     75     61     99       C  
ATOM   9059  C   LEU B 432      -1.782  11.515   7.876  1.00 38.34           C  
ANISOU 9059  C   LEU B 432     4458   5103   5003     60     69     88       C  
ATOM   9060  O   LEU B 432      -2.284  11.081   8.918  1.00 38.75           O  
ANISOU 9060  O   LEU B 432     4493   5173   5055     56     64     88       O  
ATOM   9061  CB  LEU B 432      -3.507  10.867   6.228  1.00 35.78           C  
ANISOU 9061  CB  LEU B 432     4162   4744   4689     83     49     97       C  
ATOM   9062  CG  LEU B 432      -3.963  10.768   4.785  1.00 35.76           C  
ANISOU 9062  CG  LEU B 432     4183   4713   4688     97     42    102       C  
ATOM   9063  CD1 LEU B 432      -5.478  10.895   4.751  1.00 34.49           C  
ANISOU 9063  CD1 LEU B 432     4024   4544   4536    104     30     99       C  
ATOM   9064  CD2 LEU B 432      -3.296  11.834   3.924  1.00 36.81           C  
ANISOU 9064  CD2 LEU B 432     4335   4831   4821     98     53     97       C  
ATOM   9065  N   LYS B 433      -1.058  12.624   7.819  1.00 38.31           N  
ANISOU 9065  N   LYS B 433     4458   5097   4999     52     82     79       N  
ATOM   9066  CA  LYS B 433      -0.775  13.414   8.998  1.00 39.19           C  
ANISOU 9066  CA  LYS B 433     4553   5227   5109     37     90     66       C  
ATOM   9067  C   LYS B 433      -1.486  14.755   8.942  1.00 38.15           C  
ANISOU 9067  C   LYS B 433     4430   5081   4983     35     95     52       C  
ATOM   9068  O   LYS B 433      -1.586  15.370   7.889  1.00 38.94           O  
ANISOU 9068  O   LYS B 433     4549   5157   5087     42     99     51       O  
ATOM   9069  CB  LYS B 433       0.737  13.637   9.134  1.00 39.82           C  
ANISOU 9069  CB  LYS B 433     4627   5318   5182     27    102     65       C  
ATOM   9070  CG  LYS B 433       1.387  12.895  10.280  1.00 39.59           C  
ANISOU 9070  CG  LYS B 433     4575   5320   5146     19    101     68       C  
ATOM   9071  CD  LYS B 433       1.999  11.572   9.873  1.00 39.30           C  
ANISOU 9071  CD  LYS B 433     4538   5289   5106     27     97     85       C  
ATOM   9072  CE  LYS B 433       1.949  10.574  11.032  1.00 42.73           C  
ANISOU 9072  CE  LYS B 433     4950   5750   5534     24     90     91       C  
ATOM   9073  NZ  LYS B 433       1.968  11.154  12.414  1.00 42.10           N  
ANISOU 9073  NZ  LYS B 433     4851   5693   5450     11     94     80       N  
ATOM   9074  N   ARG B 434      -1.961  15.199  10.099  1.00 39.09           N  
ANISOU 9074  N   ARG B 434     4535   5214   5103     26     97     42       N  
ATOM   9075  CA  ARG B 434      -2.487  16.549  10.295  1.00 40.19           C  
ANISOU 9075  CA  ARG B 434     4678   5343   5246     21    105     28       C  
ATOM   9076  C   ARG B 434      -3.836  16.788   9.619  1.00 40.28           C  
ANISOU 9076  C   ARG B 434     4703   5332   5266     34     97     29       C  
ATOM   9077  O   ARG B 434      -4.322  17.916   9.572  1.00 40.69           O  
ANISOU 9077  O   ARG B 434     4763   5372   5323     33    104     18       O  
ATOM   9078  CB  ARG B 434      -1.459  17.608   9.862  1.00 41.85           C  
ANISOU 9078  CB  ARG B 434     4897   5545   5456     14    120     19       C  
ATOM   9079  CG  ARG B 434      -0.037  17.306  10.308  1.00 44.29           C  
ANISOU 9079  CG  ARG B 434     5194   5874   5758      3    126     20       C  
ATOM   9080  CD  ARG B 434       0.590  18.466  11.054  1.00 45.61           C  
ANISOU 9080  CD  ARG B 434     5353   6051   5925    -13    140      3       C  
ATOM   9081  NE  ARG B 434       0.835  19.602  10.176  1.00 49.86           N  
ANISOU 9081  NE  ARG B 434     5909   6565   6468    -13    152     -3       N  
ATOM   9082  CZ  ARG B 434       2.029  19.939   9.696  1.00 50.44           C  
ANISOU 9082  CZ  ARG B 434     5986   6635   6541    -19    163     -4       C  
ATOM   9083  NH1 ARG B 434       3.108  19.230  10.014  1.00 50.05           N  
ANISOU 9083  NH1 ARG B 434     5924   6606   6485    -25    163      1       N  
ATOM   9084  NH2 ARG B 434       2.145  20.997   8.903  1.00 49.97           N  
ANISOU 9084  NH2 ARG B 434     5945   6553   6488    -18    175    -10       N  
ATOM   9085  N   VAL B 435      -4.456  15.725   9.120  1.00 39.51           N  
ANISOU 9085  N   VAL B 435     4609   5230   5171     46     84     41       N  
ATOM   9086  CA  VAL B 435      -5.682  15.866   8.346  1.00 39.16           C  
ANISOU 9086  CA  VAL B 435     4579   5165   5135     59     75     43       C  
ATOM   9087  C   VAL B 435      -6.877  16.280   9.218  1.00 40.32           C  
ANISOU 9087  C   VAL B 435     4716   5316   5288     58     72     35       C  
ATOM   9088  O   VAL B 435      -7.883  16.775   8.721  1.00 40.88           O  
ANISOU 9088  O   VAL B 435     4796   5369   5365     66     69     33       O  
ATOM   9089  CB  VAL B 435      -5.965  14.586   7.527  1.00 37.74           C  
ANISOU 9089  CB  VAL B 435     4406   4977   4955     72     60     58       C  
ATOM   9090  CG1 VAL B 435      -6.856  13.627   8.294  1.00 38.11           C  
ANISOU 9090  CG1 VAL B 435     4437   5037   5004     73     49     63       C  
ATOM   9091  CG2 VAL B 435      -6.596  14.930   6.188  1.00 37.80           C  
ANISOU 9091  CG2 VAL B 435     4436   4957   4967     86     55     60       C  
ATOM   9092  N   THR B 436      -6.754  16.062  10.521  1.00 43.00           N  
ANISOU 9092  N   THR B 436     5035   5678   5623     47     75     32       N  
ATOM   9093  CA  THR B 436      -7.796  16.402  11.475  1.00 44.68           C  
ANISOU 9093  CA  THR B 436     5236   5898   5840     44     74     25       C  
ATOM   9094  C   THR B 436      -7.520  17.792  12.041  1.00 45.03           C  
ANISOU 9094  C   THR B 436     5280   5943   5884     33     89      9       C  
ATOM   9095  O   THR B 436      -8.306  18.335  12.812  1.00 43.71           O  
ANISOU 9095  O   THR B 436     5106   5780   5721     30     92      1       O  
ATOM   9096  CB  THR B 436      -7.843  15.376  12.624  1.00 48.59           C  
ANISOU 9096  CB  THR B 436     5710   6418   6331     39     69     30       C  
ATOM   9097  OG1 THR B 436      -9.001  15.611  13.430  1.00 51.77           O  
ANISOU 9097  OG1 THR B 436     6103   6824   6740     39     68     25       O  
ATOM   9098  CG2 THR B 436      -6.582  15.463  13.507  1.00 47.65           C  
ANISOU 9098  CG2 THR B 436     5579   6322   6202     25     79     25       C  
ATOM   9099  N   GLU B 437      -6.382  18.350  11.649  1.00 46.63           N  
ANISOU 9099  N   GLU B 437     5490   6143   6082     27    100      5       N  
ATOM   9100  CA  GLU B 437      -5.903  19.604  12.188  1.00 47.44           C  
ANISOU 9100  CA  GLU B 437     5592   6248   6184     14    115    -10       C  
ATOM   9101  C   GLU B 437      -6.808  20.736  11.717  1.00 49.05           C  
ANISOU 9101  C   GLU B 437     5810   6429   6397     20    120    -17       C  
ATOM   9102  O   GLU B 437      -7.048  21.697  12.450  1.00 54.30           O  
ANISOU 9102  O   GLU B 437     6471   7096   7063     12    130    -30       O  
ATOM   9103  CB  GLU B 437      -4.468  19.848  11.722  1.00 48.07           C  
ANISOU 9103  CB  GLU B 437     5677   6327   6258      7    124    -11       C  
ATOM   9104  CG  GLU B 437      -3.475  20.173  12.826  1.00 51.62           C  
ANISOU 9104  CG  GLU B 437     6111   6801   6701    -10    134    -21       C  
ATOM   9105  CD  GLU B 437      -2.784  18.941  13.390  1.00 53.57           C  
ANISOU 9105  CD  GLU B 437     6341   7072   6939    -13    127    -12       C  
ATOM   9106  OE1 GLU B 437      -1.551  19.006  13.576  1.00 55.13           O  
ANISOU 9106  OE1 GLU B 437     6533   7282   7130    -23    133    -15       O  
ATOM   9107  OE2 GLU B 437      -3.456  17.911  13.648  1.00 53.58           O  
ANISOU 9107  OE2 GLU B 437     6335   7081   6939     -5    115     -2       O  
ATOM   9108  N   PHE B 438      -7.323  20.604  10.497  1.00 46.42           N  
ANISOU 9108  N   PHE B 438     5493   6073   6069     35    113     -9       N  
ATOM   9109  CA  PHE B 438      -8.105  21.655   9.858  1.00 44.56           C  
ANISOU 9109  CA  PHE B 438     5273   5814   5841     44    118    -14       C  
ATOM   9110  C   PHE B 438      -9.005  21.076   8.763  1.00 42.99           C  
ANISOU 9110  C   PHE B 438     5087   5598   5648     62    103     -2       C  
ATOM   9111  O   PHE B 438      -9.040  19.857   8.564  1.00 42.35           O  
ANISOU 9111  O   PHE B 438     5001   5523   5564     67     89      9       O  
ATOM   9112  CB  PHE B 438      -7.170  22.728   9.285  1.00 44.58           C  
ANISOU 9112  CB  PHE B 438     5291   5804   5843     39    134    -21       C  
ATOM   9113  CG  PHE B 438      -6.324  22.251   8.136  1.00 44.15           C  
ANISOU 9113  CG  PHE B 438     5249   5739   5785     45    132    -11       C  
ATOM   9114  CD1 PHE B 438      -6.545  22.735   6.851  1.00 44.13           C  
ANISOU 9114  CD1 PHE B 438     5270   5711   5787     58    133     -8       C  
ATOM   9115  CD2 PHE B 438      -5.296  21.328   8.336  1.00 43.83           C  
ANISOU 9115  CD2 PHE B 438     5199   5715   5737     38    129     -5       C  
ATOM   9116  CE1 PHE B 438      -5.757  22.311   5.788  1.00 45.18           C  
ANISOU 9116  CE1 PHE B 438     5416   5834   5916     64    132      0       C  
ATOM   9117  CE2 PHE B 438      -4.506  20.897   7.278  1.00 44.19           C  
ANISOU 9117  CE2 PHE B 438     5257   5751   5779     44    129      3       C  
ATOM   9118  CZ  PHE B 438      -4.736  21.388   6.000  1.00 44.97           C  
ANISOU 9118  CZ  PHE B 438     5379   5824   5882     57    130      6       C  
ATOM   9119  N   SER B 439      -9.742  21.950   8.070  1.00 40.71           N  
ANISOU 9119  N   SER B 439     4813   5287   5366     72    105     -4       N  
ATOM   9120  CA  SER B 439     -10.604  21.529   6.972  1.00 38.47           C  
ANISOU 9120  CA  SER B 439     4542   4986   5086     90     91      5       C  
ATOM   9121  C   SER B 439      -9.735  21.277   5.753  1.00 37.29           C  
ANISOU 9121  C   SER B 439     4410   4824   4932     96     91     12       C  
ATOM   9122  O   SER B 439      -9.612  22.111   4.861  1.00 37.91           O  
ANISOU 9122  O   SER B 439     4508   4883   5012    102     98     11       O  
ATOM   9123  CB  SER B 439     -11.703  22.560   6.689  1.00 37.37           C  
ANISOU 9123  CB  SER B 439     4412   4829   4956     99     93      0       C  
ATOM   9124  OG  SER B 439     -12.753  22.458   7.638  1.00 35.59           O  
ANISOU 9124  OG  SER B 439     4170   4614   4737     98     89     -1       O  
ATOM   9125  N   ALA B 440      -9.146  20.093   5.734  1.00 36.73           N  
ANISOU 9125  N   ALA B 440     4333   4766   4855     94     82     21       N  
ATOM   9126  CA  ALA B 440      -8.086  19.765   4.799  1.00 35.74           C  
ANISOU 9126  CA  ALA B 440     4221   4633   4723     97     85     28       C  
ATOM   9127  C   ALA B 440      -8.575  19.560   3.370  1.00 34.04           C  
ANISOU 9127  C   ALA B 440     4027   4395   4509    115     74     36       C  
ATOM   9128  O   ALA B 440      -7.767  19.578   2.438  1.00 32.73           O  
ANISOU 9128  O   ALA B 440     3877   4218   4338    119     79     41       O  
ATOM   9129  CB  ALA B 440      -7.333  18.535   5.291  1.00 35.81           C  
ANISOU 9129  CB  ALA B 440     4217   4663   4727     90     79     34       C  
ATOM   9130  N   PHE B 441      -9.883  19.352   3.208  1.00 32.06           N  
ANISOU 9130  N   PHE B 441     3777   4138   4265    125     60     39       N  
ATOM   9131  CA  PHE B 441     -10.462  19.074   1.895  1.00 32.08           C  
ANISOU 9131  CA  PHE B 441     3798   4122   4268    142     48     47       C  
ATOM   9132  C   PHE B 441     -11.401  20.177   1.427  1.00 33.07           C  
ANISOU 9132  C   PHE B 441     3936   4229   4400    153     49     43       C  
ATOM   9133  O   PHE B 441     -12.210  19.958   0.534  1.00 35.09           O  
ANISOU 9133  O   PHE B 441     4202   4470   4657    168     35     49       O  
ATOM   9134  CB  PHE B 441     -11.216  17.737   1.900  1.00 30.12           C  
ANISOU 9134  CB  PHE B 441     3541   3881   4022    148     27     56       C  
ATOM   9135  CG  PHE B 441     -10.390  16.581   2.359  1.00 29.62           C  
ANISOU 9135  CG  PHE B 441     3466   3835   3953    139     25     61       C  
ATOM   9136  CD1 PHE B 441      -9.383  16.064   1.552  1.00 29.63           C  
ANISOU 9136  CD1 PHE B 441     3480   3831   3946    142     27     68       C  
ATOM   9137  CD2 PHE B 441     -10.603  16.015   3.607  1.00 29.41           C  
ANISOU 9137  CD2 PHE B 441     3416   3829   3928    129     23     60       C  
ATOM   9138  CE1 PHE B 441      -8.609  15.004   1.982  1.00 28.53           C  
ANISOU 9138  CE1 PHE B 441     3329   3707   3801    135     26     74       C  
ATOM   9139  CE2 PHE B 441      -9.837  14.953   4.039  1.00 29.05           C  
ANISOU 9139  CE2 PHE B 441     3360   3800   3877    122     22     66       C  
ATOM   9140  CZ  PHE B 441      -8.840  14.446   3.225  1.00 28.82           C  
ANISOU 9140  CZ  PHE B 441     3343   3766   3841    125     23     73       C  
ATOM   9141  N   LEU B 442     -11.275  21.360   2.014  1.00 33.73           N  
ANISOU 9141  N   LEU B 442     4017   4312   4487    145     66     32       N  
ATOM   9142  CA  LEU B 442     -12.240  22.448   1.824  1.00 34.05           C  
ANISOU 9142  CA  LEU B 442     4064   4337   4533    154     69     28       C  
ATOM   9143  C   LEU B 442     -12.499  22.847   0.371  1.00 34.34           C  
ANISOU 9143  C   LEU B 442     4127   4350   4570    172     66     33       C  
ATOM   9144  O   LEU B 442     -13.635  23.116  -0.005  1.00 35.52           O  
ANISOU 9144  O   LEU B 442     4280   4489   4724    184     56     35       O  
ATOM   9145  CB  LEU B 442     -11.792  23.671   2.620  1.00 34.20           C  
ANISOU 9145  CB  LEU B 442     4080   4359   4555    141     91     15       C  
ATOM   9146  CG  LEU B 442     -12.796  24.791   2.872  1.00 32.97           C  
ANISOU 9146  CG  LEU B 442     3925   4193   4407    146     97      8       C  
ATOM   9147  CD1 LEU B 442     -13.975  24.288   3.680  1.00 31.44           C  
ANISOU 9147  CD1 LEU B 442     3713   4012   4221    146     84      9       C  
ATOM   9148  CD2 LEU B 442     -12.069  25.909   3.592  1.00 33.30           C  
ANISOU 9148  CD2 LEU B 442     3965   4237   4449    131    120     -4       C  
ATOM   9149  N   SER B 443     -11.445  22.871  -0.434  1.00 34.01           N  
ANISOU 9149  N   SER B 443     4101   4299   4520    173     73     36       N  
ATOM   9150  CA  SER B 443     -11.521  23.290  -1.817  1.00 33.90           C  
ANISOU 9150  CA  SER B 443     4113   4262   4503    190     72     42       C  
ATOM   9151  C   SER B 443     -12.176  22.262  -2.740  1.00 35.90           C  
ANISOU 9151  C   SER B 443     4375   4510   4754    205     49     53       C  
ATOM   9152  O   SER B 443     -12.393  22.549  -3.921  1.00 38.43           O  
ANISOU 9152  O   SER B 443     4716   4811   5071    221     46     57       O  
ATOM   9153  CB  SER B 443     -10.113  23.589  -2.348  1.00 33.47           C  
ANISOU 9153  CB  SER B 443     4073   4200   4442    186     89     42       C  
ATOM   9154  OG  SER B 443      -9.517  24.675  -1.667  1.00 33.13           O  
ANISOU 9154  OG  SER B 443     4025   4158   4401    173    111     32       O  
ATOM   9155  N   LEU B 444     -12.479  21.068  -2.247  1.00 34.63           N  
ANISOU 9155  N   LEU B 444     4197   4365   4594    201     34     56       N  
ATOM   9156  CA  LEU B 444     -12.841  19.996  -3.175  1.00 35.50           C  
ANISOU 9156  CA  LEU B 444     4317   4470   4701    213     13     66       C  
ATOM   9157  C   LEU B 444     -14.349  19.898  -3.397  1.00 38.95           C  
ANISOU 9157  C   LEU B 444     4751   4902   5145    225     -5     67       C  
ATOM   9158  O   LEU B 444     -14.964  18.828  -3.265  1.00 40.80           O  
ANISOU 9158  O   LEU B 444     4974   5145   5382    226    -23     71       O  
ATOM   9159  CB  LEU B 444     -12.185  18.659  -2.791  1.00 32.63           C  
ANISOU 9159  CB  LEU B 444     3942   4123   4333    203      7     71       C  
ATOM   9160  CG  LEU B 444     -10.651  18.650  -2.654  1.00 30.81           C  
ANISOU 9160  CG  LEU B 444     3712   3897   4094    193     24     70       C  
ATOM   9161  CD1 LEU B 444     -10.152  17.241  -2.411  1.00 29.90           C  
ANISOU 9161  CD1 LEU B 444     3587   3796   3975    187     16     77       C  
ATOM   9162  CD2 LEU B 444      -9.925  19.245  -3.850  1.00 29.73           C  
ANISOU 9162  CD2 LEU B 444     3603   3741   3952    202     34     73       C  
ATOM   9163  N   GLU B 445     -14.925  21.036  -3.766  1.00 41.46           N  
ANISOU 9163  N   GLU B 445     5080   5206   5467    235      0     64       N  
ATOM   9164  CA  GLU B 445     -16.352  21.173  -4.010  1.00 43.21           C  
ANISOU 9164  CA  GLU B 445     5299   5421   5695    247    -15     65       C  
ATOM   9165  C   GLU B 445     -16.879  20.145  -5.026  1.00 41.77           C  
ANISOU 9165  C   GLU B 445     5126   5234   5510    261    -39     74       C  
ATOM   9166  O   GLU B 445     -18.033  19.728  -4.945  1.00 40.03           O  
ANISOU 9166  O   GLU B 445     4895   5016   5296    266    -57     75       O  
ATOM   9167  CB  GLU B 445     -16.644  22.612  -4.450  1.00 48.82           C  
ANISOU 9167  CB  GLU B 445     6025   6116   6408    258     -3     62       C  
ATOM   9168  CG  GLU B 445     -18.095  22.921  -4.801  1.00 58.95           C  
ANISOU 9168  CG  GLU B 445     7308   7390   7698    273    -17     64       C  
ATOM   9169  CD  GLU B 445     -18.293  24.353  -5.289  1.00 65.34           C  
ANISOU 9169  CD  GLU B 445     8134   8183   8509    285     -3     62       C  
ATOM   9170  OE1 GLU B 445     -18.106  25.295  -4.479  1.00 68.47           O  
ANISOU 9170  OE1 GLU B 445     8524   8580   8910    275     15     55       O  
ATOM   9171  OE2 GLU B 445     -18.642  24.534  -6.479  1.00 64.42           O  
ANISOU 9171  OE2 GLU B 445     8038   8050   8388    303    -12     68       O  
ATOM   9172  N   LYS B 446     -16.024  19.717  -5.953  1.00 40.36           N  
ANISOU 9172  N   LYS B 446     4967   5048   5321    265    -40     79       N  
ATOM   9173  CA  LYS B 446     -16.439  18.816  -7.034  1.00 40.08           C  
ANISOU 9173  CA  LYS B 446     4944   5004   5280    278    -61     86       C  
ATOM   9174  C   LYS B 446     -16.012  17.358  -6.862  1.00 38.19           C  
ANISOU 9174  C   LYS B 446     4696   4777   5037    270    -71     90       C  
ATOM   9175  O   LYS B 446     -16.186  16.554  -7.782  1.00 38.95           O  
ANISOU 9175  O   LYS B 446     4804   4866   5127    279    -88     96       O  
ATOM   9176  CB  LYS B 446     -15.907  19.322  -8.373  1.00 41.68           C  
ANISOU 9176  CB  LYS B 446     5177   5187   5471    293    -56     90       C  
ATOM   9177  CG  LYS B 446     -16.455  20.668  -8.794  1.00 44.43           C  
ANISOU 9177  CG  LYS B 446     5537   5520   5821    305    -49     88       C  
ATOM   9178  CD  LYS B 446     -15.659  21.218  -9.964  1.00 45.42           C  
ANISOU 9178  CD  LYS B 446     5694   5628   5936    317    -39     92       C  
ATOM   9179  CE  LYS B 446     -15.930  22.697 -10.159  1.00 47.30           C  
ANISOU 9179  CE  LYS B 446     5942   5852   6176    325    -24     90       C  
ATOM   9180  NZ  LYS B 446     -14.960  23.279 -11.125  1.00 50.47           N  
ANISOU 9180  NZ  LYS B 446     6371   6237   6567    334     -8     93       N  
ATOM   9181  N   LEU B 447     -15.455  17.011  -5.705  1.00 35.41           N  
ANISOU 9181  N   LEU B 447     4323   4441   4687    253    -62     88       N  
ATOM   9182  CA  LEU B 447     -14.953  15.658  -5.501  1.00 33.65           C  
ANISOU 9182  CA  LEU B 447     4093   4230   4461    245    -69     92       C  
ATOM   9183  C   LEU B 447     -16.081  14.651  -5.418  1.00 32.04           C  
ANISOU 9183  C   LEU B 447     3877   4031   4264    248    -92     95       C  
ATOM   9184  O   LEU B 447     -17.050  14.861  -4.696  1.00 31.02           O  
ANISOU 9184  O   LEU B 447     3730   3909   4146    245    -96     91       O  
ATOM   9185  CB  LEU B 447     -14.072  15.566  -4.246  1.00 34.59           C  
ANISOU 9185  CB  LEU B 447     4193   4368   4582    227    -52     89       C  
ATOM   9186  CG  LEU B 447     -13.182  14.311  -4.168  1.00 33.94           C  
ANISOU 9186  CG  LEU B 447     4108   4295   4493    220    -54     95       C  
ATOM   9187  CD1 LEU B 447     -11.970  14.437  -5.079  1.00 33.35           C  
ANISOU 9187  CD1 LEU B 447     4055   4209   4407    224    -43     99       C  
ATOM   9188  CD2 LEU B 447     -12.744  14.049  -2.740  1.00 33.82           C  
ANISOU 9188  CD2 LEU B 447     4066   4301   4480    203    -44     93       C  
ATOM   9189  N   LEU B 448     -15.940  13.552  -6.154  1.00 31.22           N  
ANISOU 9189  N   LEU B 448     3782   3923   4154    253   -105    101       N  
ATOM   9190  CA  LEU B 448     -16.940  12.489  -6.141  1.00 30.71           C  
ANISOU 9190  CA  LEU B 448     3708   3864   4097    254   -127    103       C  
ATOM   9191  C   LEU B 448     -16.532  11.295  -5.294  1.00 30.52           C  
ANISOU 9191  C   LEU B 448     3666   3855   4075    241   -127    106       C  
ATOM   9192  O   LEU B 448     -17.395  10.596  -4.750  1.00 30.94           O  
ANISOU 9192  O   LEU B 448     3700   3916   4137    237   -139    105       O  
ATOM   9193  CB  LEU B 448     -17.278  12.034  -7.564  1.00 30.60           C  
ANISOU 9193  CB  LEU B 448     3716   3834   4076    269   -145    107       C  
ATOM   9194  CG  LEU B 448     -17.891  13.053  -8.537  1.00 30.31           C  
ANISOU 9194  CG  LEU B 448     3698   3781   4038    286   -150    105       C  
ATOM   9195  CD1 LEU B 448     -18.237  12.381  -9.855  1.00 29.22           C  
ANISOU 9195  CD1 LEU B 448     3579   3629   3891    299   -171    109       C  
ATOM   9196  CD2 LEU B 448     -19.119  13.740  -7.948  1.00 29.96           C  
ANISOU 9196  CD2 LEU B 448     3637   3739   4006    287   -155    101       C  
ATOM   9197  N   TYR B 449     -15.220  11.094  -5.161  1.00 29.92           N  
ANISOU 9197  N   TYR B 449     3593   3783   3989    234   -112    108       N  
ATOM   9198  CA  TYR B 449     -14.645   9.882  -4.567  1.00 29.23           C  
ANISOU 9198  CA  TYR B 449     3494   3710   3901    224   -111    113       C  
ATOM   9199  C   TYR B 449     -13.493  10.212  -3.600  1.00 29.33           C  
ANISOU 9199  C   TYR B 449     3496   3737   3911    211    -89    112       C  
ATOM   9200  O   TYR B 449     -12.475  10.794  -4.010  1.00 29.20           O  
ANISOU 9200  O   TYR B 449     3493   3714   3886    211    -75    112       O  
ATOM   9201  CB  TYR B 449     -14.142   8.985  -5.701  1.00 28.82           C  
ANISOU 9201  CB  TYR B 449     3462   3647   3839    232   -118    119       C  
ATOM   9202  CG  TYR B 449     -13.637   7.622  -5.282  1.00 29.62           C  
ANISOU 9202  CG  TYR B 449     3554   3759   3939    224   -119    125       C  
ATOM   9203  CD1 TYR B 449     -12.348   7.460  -4.774  1.00 29.83           C  
ANISOU 9203  CD1 TYR B 449     3577   3795   3959    215   -102    129       C  
ATOM   9204  CD2 TYR B 449     -14.440   6.485  -5.417  1.00 29.57           C  
ANISOU 9204  CD2 TYR B 449     3543   3752   3938    225   -137    128       C  
ATOM   9205  CE1 TYR B 449     -11.878   6.215  -4.394  1.00 29.56           C  
ANISOU 9205  CE1 TYR B 449     3534   3771   3924    209   -102    135       C  
ATOM   9206  CE2 TYR B 449     -13.979   5.236  -5.039  1.00 29.49           C  
ANISOU 9206  CE2 TYR B 449     3525   3752   3928    219   -137    134       C  
ATOM   9207  CZ  TYR B 449     -12.695   5.108  -4.530  1.00 29.97           C  
ANISOU 9207  CZ  TYR B 449     3582   3822   3981    211   -119    138       C  
ATOM   9208  OH  TYR B 449     -12.209   3.877  -4.149  1.00 29.88           O  
ANISOU 9208  OH  TYR B 449     3563   3820   3969    205   -118    145       O  
ATOM   9209  N   LEU B 450     -13.652   9.851  -2.324  1.00 28.45           N  
ANISOU 9209  N   LEU B 450     3359   3643   3806    199    -86    110       N  
ATOM   9210  CA  LEU B 450     -12.572  10.039  -1.339  1.00 28.55           C  
ANISOU 9210  CA  LEU B 450     3360   3673   3815    186    -68    109       C  
ATOM   9211  C   LEU B 450     -12.256   8.761  -0.556  1.00 28.90           C  
ANISOU 9211  C   LEU B 450     3386   3733   3859    177    -69    115       C  
ATOM   9212  O   LEU B 450     -13.146   8.172   0.077  1.00 30.21           O  
ANISOU 9212  O   LEU B 450     3536   3907   4034    175    -78    115       O  
ATOM   9213  CB  LEU B 450     -12.869  11.193  -0.369  1.00 27.47           C  
ANISOU 9213  CB  LEU B 450     3208   3543   3684    179    -57    100       C  
ATOM   9214  CG  LEU B 450     -11.753  11.509   0.644  1.00 26.91           C  
ANISOU 9214  CG  LEU B 450     3125   3489   3608    165    -38     98       C  
ATOM   9215  CD1 LEU B 450     -10.456  11.889  -0.050  1.00 26.82           C  
ANISOU 9215  CD1 LEU B 450     3132   3470   3587    166    -25     99       C  
ATOM   9216  CD2 LEU B 450     -12.138  12.582   1.656  1.00 25.92           C  
ANISOU 9216  CD2 LEU B 450     2986   3372   3489    157    -28     88       C  
ATOM   9217  N   ASP B 451     -10.993   8.340  -0.602  1.00 27.92           N  
ANISOU 9217  N   ASP B 451     3266   3614   3726    174    -59    120       N  
ATOM   9218  CA  ASP B 451     -10.566   7.147   0.122  1.00 28.07           C  
ANISOU 9218  CA  ASP B 451     3270   3649   3744    166    -58    127       C  
ATOM   9219  C   ASP B 451      -9.460   7.445   1.124  1.00 28.11           C  
ANISOU 9219  C   ASP B 451     3262   3673   3745    154    -41    126       C  
ATOM   9220  O   ASP B 451      -8.315   7.709   0.744  1.00 27.90           O  
ANISOU 9220  O   ASP B 451     3245   3645   3710    154    -29    127       O  
ATOM   9221  CB  ASP B 451     -10.112   6.069  -0.845  1.00 28.34           C  
ANISOU 9221  CB  ASP B 451     3320   3675   3773    173    -64    136       C  
ATOM   9222  CG  ASP B 451     -10.104   4.684  -0.223  1.00 28.21           C  
ANISOU 9222  CG  ASP B 451     3289   3671   3758    169    -69    143       C  
ATOM   9223  OD1 ASP B 451     -10.126   4.571   1.016  1.00 27.12           O  
ANISOU 9223  OD1 ASP B 451     3129   3552   3623    159    -63    143       O  
ATOM   9224  OD2 ASP B 451     -10.071   3.701  -0.998  1.00 29.56           O  
ANISOU 9224  OD2 ASP B 451     3472   3832   3926    175    -77    150       O  
ATOM   9225  N   ILE B 452      -9.815   7.414   2.404  1.00 27.78           N  
ANISOU 9225  N   ILE B 452     3197   3649   3708    145    -38    123       N  
ATOM   9226  CA  ILE B 452      -8.853   7.675   3.475  1.00 28.41           C  
ANISOU 9226  CA  ILE B 452     3261   3749   3783    133    -23    121       C  
ATOM   9227  C   ILE B 452      -8.811   6.469   4.425  1.00 29.13           C  
ANISOU 9227  C   ILE B 452     3334   3860   3875    128    -25    128       C  
ATOM   9228  O   ILE B 452      -8.456   6.580   5.604  1.00 29.73           O  
ANISOU 9228  O   ILE B 452     3391   3955   3948    118    -17    126       O  
ATOM   9229  CB  ILE B 452      -9.152   9.003   4.219  1.00 27.90           C  
ANISOU 9229  CB  ILE B 452     3189   3690   3722    127    -15    109       C  
ATOM   9230  CG1 ILE B 452     -10.561   8.988   4.835  1.00 27.89           C  
ANISOU 9230  CG1 ILE B 452     3174   3691   3730    127    -24    106       C  
ATOM   9231  CG2 ILE B 452      -8.985  10.183   3.269  1.00 27.35           C  
ANISOU 9231  CG2 ILE B 452     3139   3602   3651    132    -10    103       C  
ATOM   9232  CD1 ILE B 452     -10.758   9.942   6.003  1.00 27.54           C  
ANISOU 9232  CD1 ILE B 452     3114   3660   3689    118    -14     96       C  
ATOM   9233  N   SER B 453      -9.188   5.316   3.881  1.00 28.89           N  
ANISOU 9233  N   SER B 453     3308   3822   3845    135    -37    136       N  
ATOM   9234  CA  SER B 453      -9.146   4.057   4.590  1.00 29.14           C  
ANISOU 9234  CA  SER B 453     3325   3868   3878    132    -39    145       C  
ATOM   9235  C   SER B 453      -7.719   3.663   4.952  1.00 30.07           C  
ANISOU 9235  C   SER B 453     3438   4000   3985    127    -26    151       C  
ATOM   9236  O   SER B 453      -6.790   3.874   4.161  1.00 30.90           O  
ANISOU 9236  O   SER B 453     3558   4098   4084    130    -21    153       O  
ATOM   9237  CB  SER B 453      -9.796   2.971   3.737  1.00 29.12           C  
ANISOU 9237  CB  SER B 453     3332   3851   3880    141    -53    152       C  
ATOM   9238  OG  SER B 453     -11.154   3.284   3.459  1.00 28.73           O  
ANISOU 9238  OG  SER B 453     3285   3790   3841    145    -66    146       O  
ATOM   9239  N   TYR B 454      -7.562   3.080   6.144  1.00 30.48           N  
ANISOU 9239  N   TYR B 454     3470   4074   4037    120    -22    155       N  
ATOM   9240  CA  TYR B 454      -6.266   2.621   6.694  1.00 30.44           C  
ANISOU 9240  CA  TYR B 454     3455   4086   4022    115    -11    162       C  
ATOM   9241  C   TYR B 454      -5.174   3.676   6.586  1.00 31.05           C  
ANISOU 9241  C   TYR B 454     3538   4167   4093    110      0    156       C  
ATOM   9242  O   TYR B 454      -4.065   3.387   6.149  1.00 31.52           O  
ANISOU 9242  O   TYR B 454     3603   4227   4145    112      7    162       O  
ATOM   9243  CB  TYR B 454      -5.828   1.287   6.075  1.00 30.23           C  
ANISOU 9243  CB  TYR B 454     3437   4055   3993    122    -14    175       C  
ATOM   9244  CG  TYR B 454      -6.992   0.368   5.849  1.00 31.27           C  
ANISOU 9244  CG  TYR B 454     3569   4177   4133    128    -27    179       C  
ATOM   9245  CD1 TYR B 454      -7.643   0.342   4.610  1.00 32.71           C  
ANISOU 9245  CD1 TYR B 454     3771   4335   4320    136    -38    177       C  
ATOM   9246  CD2 TYR B 454      -7.485  -0.438   6.872  1.00 31.17           C  
ANISOU 9246  CD2 TYR B 454     3539   4179   4125    124    -28    184       C  
ATOM   9247  CE1 TYR B 454      -8.740  -0.467   4.389  1.00 32.81           C  
ANISOU 9247  CE1 TYR B 454     3784   4338   4341    140    -51    180       C  
ATOM   9248  CE2 TYR B 454      -8.592  -1.256   6.659  1.00 32.44           C  
ANISOU 9248  CE2 TYR B 454     3699   4329   4295    129    -40    186       C  
ATOM   9249  CZ  TYR B 454      -9.210  -1.264   5.413  1.00 33.12           C  
ANISOU 9249  CZ  TYR B 454     3805   4392   4386    136    -52    184       C  
ATOM   9250  OH  TYR B 454     -10.314  -2.050   5.166  1.00 35.45           O  
ANISOU 9250  OH  TYR B 454     4100   4677   4691    140    -64    186       O  
ATOM   9251  N   THR B 455      -5.512   4.906   6.967  1.00 31.29           N  
ANISOU 9251  N   THR B 455     3564   4198   4125    105      4    144       N  
ATOM   9252  CA  THR B 455      -4.548   5.994   6.994  1.00 32.35           C  
ANISOU 9252  CA  THR B 455     3700   4335   4254     98     16    137       C  
ATOM   9253  C   THR B 455      -4.212   6.364   8.422  1.00 34.43           C  
ANISOU 9253  C   THR B 455     3942   4625   4514     86     24    131       C  
ATOM   9254  O   THR B 455      -3.468   7.321   8.662  1.00 35.56           O  
ANISOU 9254  O   THR B 455     4083   4773   4653     78     35    123       O  
ATOM   9255  CB  THR B 455      -5.069   7.261   6.295  1.00 31.59           C  
ANISOU 9255  CB  THR B 455     3619   4220   4162    101     16    126       C  
ATOM   9256  OG1 THR B 455      -6.304   7.683   6.911  1.00 30.35           O  
ANISOU 9256  OG1 THR B 455     3453   4064   4013     99     10    119       O  
ATOM   9257  CG2 THR B 455      -5.231   7.022   4.785  1.00 30.16           C  
ANISOU 9257  CG2 THR B 455     3463   4013   3982    113      9    131       C  
ATOM   9258  N   ASN B 456      -4.779   5.620   9.369  1.00 35.76           N  
ANISOU 9258  N   ASN B 456     4094   4808   4685     85     20    135       N  
ATOM   9259  CA  ASN B 456      -4.574   5.899  10.781  1.00 37.89           C  
ANISOU 9259  CA  ASN B 456     4343   5103   4950     74     26    130       C  
ATOM   9260  C   ASN B 456      -4.973   7.283  11.227  1.00 36.64           C  
ANISOU 9260  C   ASN B 456     4182   4944   4794     67     31    115       C  
ATOM   9261  O   ASN B 456      -4.244   7.940  11.957  1.00 37.21           O  
ANISOU 9261  O   ASN B 456     4244   5031   4860     57     41    108       O  
ATOM   9262  CB  ASN B 456      -3.121   5.680  11.156  1.00 42.54           C  
ANISOU 9262  CB  ASN B 456     4923   5709   5528     68     36    134       C  
ATOM   9263  CG  ASN B 456      -2.945   4.462  12.003  1.00 48.96           C  
ANISOU 9263  CG  ASN B 456     5720   6543   6337     69     34    146       C  
ATOM   9264  OD1 ASN B 456      -2.578   4.567  13.179  1.00 52.90           O  
ANISOU 9264  OD1 ASN B 456     6202   7067   6830     61     39    143       O  
ATOM   9265  ND2 ASN B 456      -3.253   3.287  11.430  1.00 47.86           N  
ANISOU 9265  ND2 ASN B 456     5587   6394   6201     78     27    158       N  
ATOM   9266  N   THR B 457      -6.128   7.735  10.785  1.00 35.07           N  
ANISOU 9266  N   THR B 457     3992   4727   4604     72     25    110       N  
ATOM   9267  CA  THR B 457      -6.564   9.048  11.151  1.00 35.18           C  
ANISOU 9267  CA  THR B 457     4005   4738   4621     67     30     96       C  
ATOM   9268  C   THR B 457      -7.470   8.897  12.357  1.00 36.42           C  
ANISOU 9268  C   THR B 457     4144   4910   4782     63     28     93       C  
ATOM   9269  O   THR B 457      -8.422   8.113  12.321  1.00 37.86           O  
ANISOU 9269  O   THR B 457     4324   5088   4971     70     18    100       O  
ATOM   9270  CB  THR B 457      -7.266   9.714   9.965  1.00 34.93           C  
ANISOU 9270  CB  THR B 457     3994   4680   4598     75     25     92       C  
ATOM   9271  OG1 THR B 457      -6.368   9.715   8.846  1.00 35.02           O  
ANISOU 9271  OG1 THR B 457     4021   4678   4604     79     28     96       O  
ATOM   9272  CG2 THR B 457      -7.676  11.137  10.297  1.00 34.09           C  
ANISOU 9272  CG2 THR B 457     3887   4569   4494     70     32     78       C  
ATOM   9273  N   LYS B 458      -7.137   9.596  13.439  1.00 34.89           N  
ANISOU 9273  N   LYS B 458     3939   4734   4584     52     37     84       N  
ATOM   9274  CA  LYS B 458      -8.023   9.674  14.580  1.00 36.27           C  
ANISOU 9274  CA  LYS B 458     4098   4920   4760     49     37     80       C  
ATOM   9275  C   LYS B 458      -8.926  10.906  14.391  1.00 37.31           C  
ANISOU 9275  C   LYS B 458     4237   5036   4900     49     39     68       C  
ATOM   9276  O   LYS B 458      -8.480  12.052  14.549  1.00 38.03           O  
ANISOU 9276  O   LYS B 458     4332   5128   4989     42     49     56       O  
ATOM   9277  CB  LYS B 458      -7.222   9.733  15.886  1.00 36.78           C  
ANISOU 9277  CB  LYS B 458     4146   5013   4814     38     46     76       C  
ATOM   9278  CG  LYS B 458      -7.972  10.330  17.077  1.00 38.84           C  
ANISOU 9278  CG  LYS B 458     4395   5285   5076     32     50     66       C  
ATOM   9279  CD  LYS B 458      -9.010   9.378  17.652  1.00 39.33           C  
ANISOU 9279  CD  LYS B 458     4446   5353   5144     37     44     75       C  
ATOM   9280  CE  LYS B 458      -8.390   8.434  18.675  1.00 42.25           C  
ANISOU 9280  CE  LYS B 458     4800   5750   5504     34     46     83       C  
ATOM   9281  NZ  LYS B 458      -7.855   9.169  19.863  1.00 42.41           N  
ANISOU 9281  NZ  LYS B 458     4809   5792   5513     23     55     72       N  
ATOM   9282  N   ILE B 459     -10.188  10.668  14.029  1.00 36.45           N  
ANISOU 9282  N   ILE B 459     4131   4913   4803     58     30     71       N  
ATOM   9283  CA  ILE B 459     -11.103  11.767  13.730  1.00 36.42           C  
ANISOU 9283  CA  ILE B 459     4135   4893   4807     61     31     61       C  
ATOM   9284  C   ILE B 459     -11.440  12.480  15.024  1.00 36.68           C  
ANISOU 9284  C   ILE B 459     4155   4940   4840     52     40     51       C  
ATOM   9285  O   ILE B 459     -11.912  11.884  15.989  1.00 34.46           O  
ANISOU 9285  O   ILE B 459     3858   4673   4559     51     38     54       O  
ATOM   9286  CB  ILE B 459     -12.388  11.323  13.006  1.00 36.34           C  
ANISOU 9286  CB  ILE B 459     4131   4865   4810     73     18     67       C  
ATOM   9287  CG1 ILE B 459     -12.100  10.226  11.963  1.00 36.04           C  
ANISOU 9287  CG1 ILE B 459     4103   4818   4772     81      7     79       C  
ATOM   9288  CG2 ILE B 459     -13.116  12.527  12.423  1.00 35.56           C  
ANISOU 9288  CG2 ILE B 459     4045   4747   4720     77     18     58       C  
ATOM   9289  CD1 ILE B 459     -11.458  10.683  10.675  1.00 36.23           C  
ANISOU 9289  CD1 ILE B 459     4147   4824   4793     86      7     78       C  
ATOM   9290  N   ASP B 460     -11.199  13.780  14.998  1.00 39.46           N  
ANISOU 9290  N   ASP B 460     4514   5286   5190     47     50     38       N  
ATOM   9291  CA  ASP B 460     -10.986  14.573  16.185  1.00 40.99           C  
ANISOU 9291  CA  ASP B 460     4698   5496   5379     36     61     26       C  
ATOM   9292  C   ASP B 460     -11.682  15.921  16.002  1.00 37.91           C  
ANISOU 9292  C   ASP B 460     4317   5089   4997     36     68     15       C  
ATOM   9293  O   ASP B 460     -11.736  16.723  16.921  1.00 37.32           O  
ANISOU 9293  O   ASP B 460     4236   5023   4920     28     78      3       O  
ATOM   9294  CB  ASP B 460      -9.474  14.800  16.298  1.00 47.38           C  
ANISOU 9294  CB  ASP B 460     5507   6317   6176     25     70     23       C  
ATOM   9295  CG  ASP B 460      -8.992  14.881  17.724  1.00 58.96           C  
ANISOU 9295  CG  ASP B 460     6958   7811   7634     13     77     16       C  
ATOM   9296  OD1 ASP B 460      -9.854  15.053  18.632  1.00 63.54           O  
ANISOU 9296  OD1 ASP B 460     7528   8397   8216     12     79     12       O  
ATOM   9297  OD2 ASP B 460      -7.744  14.770  17.925  1.00 58.54           O  
ANISOU 9297  OD2 ASP B 460     6900   7772   7570      5     82     15       O  
ATOM   9298  N   PHE B 461     -12.211  16.145  14.801  1.00 35.70           N  
ANISOU 9298  N   PHE B 461     4052   4785   4725     47     62     18       N  
ATOM   9299  CA  PHE B 461     -12.661  17.459  14.342  1.00 36.03           C  
ANISOU 9299  CA  PHE B 461     4106   4808   4773     50     69      8       C  
ATOM   9300  C   PHE B 461     -13.919  17.339  13.462  1.00 36.35           C  
ANISOU 9300  C   PHE B 461     4156   4829   4827     64     57     14       C  
ATOM   9301  O   PHE B 461     -13.918  16.681  12.415  1.00 37.10           O  
ANISOU 9301  O   PHE B 461     4260   4913   4924     74     46     24       O  
ATOM   9302  CB  PHE B 461     -11.492  18.164  13.612  1.00 34.55           C  
ANISOU 9302  CB  PHE B 461     3933   4612   4580     46     77      3       C  
ATOM   9303  CG  PHE B 461     -11.864  19.434  12.887  1.00 33.01           C  
ANISOU 9303  CG  PHE B 461     3756   4395   4392     50     84     -4       C  
ATOM   9304  CD1 PHE B 461     -11.444  19.634  11.572  1.00 32.84           C  
ANISOU 9304  CD1 PHE B 461     3752   4354   4370     58     83      0       C  
ATOM   9305  CD2 PHE B 461     -12.604  20.436  13.510  1.00 33.07           C  
ANISOU 9305  CD2 PHE B 461     3760   4398   4404     48     93    -14       C  
ATOM   9306  CE1 PHE B 461     -11.772  20.797  10.886  1.00 32.05           C  
ANISOU 9306  CE1 PHE B 461     3669   4233   4276     63     90     -6       C  
ATOM   9307  CE2 PHE B 461     -12.933  21.602  12.828  1.00 33.21           C  
ANISOU 9307  CE2 PHE B 461     3793   4394   4428     53    100    -21       C  
ATOM   9308  CZ  PHE B 461     -12.515  21.782  11.516  1.00 32.17           C  
ANISOU 9308  CZ  PHE B 461     3681   4245   4297     61     99    -16       C  
ATOM   9309  N   ASP B 462     -14.997  17.975  13.900  1.00 36.80           N  
ANISOU 9309  N   ASP B 462     4209   4881   4892     67     60      8       N  
ATOM   9310  CA  ASP B 462     -16.280  17.863  13.214  1.00 36.57           C  
ANISOU 9310  CA  ASP B 462     4183   4835   4875     81     49     14       C  
ATOM   9311  C   ASP B 462     -16.318  18.488  11.828  1.00 34.95           C  
ANISOU 9311  C   ASP B 462     3999   4605   4673     91     46     14       C  
ATOM   9312  O   ASP B 462     -17.219  18.198  11.051  1.00 34.37           O  
ANISOU 9312  O   ASP B 462     3930   4518   4608    103     34     21       O  
ATOM   9313  CB  ASP B 462     -17.395  18.440  14.079  1.00 39.56           C  
ANISOU 9313  CB  ASP B 462     4552   5215   5263     81     54      8       C  
ATOM   9314  CG  ASP B 462     -17.756  17.538  15.256  1.00 43.72           C  
ANISOU 9314  CG  ASP B 462     5058   5763   5790     76     52     12       C  
ATOM   9315  OD1 ASP B 462     -16.957  16.651  15.641  1.00 44.60           O  
ANISOU 9315  OD1 ASP B 462     5163   5890   5892     70     50     17       O  
ATOM   9316  OD2 ASP B 462     -18.858  17.725  15.808  1.00 48.37           O  
ANISOU 9316  OD2 ASP B 462     5638   6350   6388     79     52     10       O  
ATOM   9317  N   GLY B 463     -15.346  19.342  11.516  1.00 34.56           N  
ANISOU 9317  N   GLY B 463     3962   4551   4617     86     58      7       N  
ATOM   9318  CA  GLY B 463     -15.259  19.948  10.184  1.00 33.66           C  
ANISOU 9318  CA  GLY B 463     3869   4414   4505     95     57      8       C  
ATOM   9319  C   GLY B 463     -14.278  19.277   9.231  1.00 32.76           C  
ANISOU 9319  C   GLY B 463     3766   4296   4383     98     52     16       C  
ATOM   9320  O   GLY B 463     -13.904  19.855   8.226  1.00 36.19           O  
ANISOU 9320  O   GLY B 463     4220   4714   4817    103     55     16       O  
ATOM   9321  N   ILE B 464     -13.851  18.062   9.544  1.00 31.32           N  
ANISOU 9321  N   ILE B 464     3574   4130   4196     94     44     23       N  
ATOM   9322  CA  ILE B 464     -12.911  17.327   8.706  1.00 30.56           C  
ANISOU 9322  CA  ILE B 464     3486   4030   4092     96     40     32       C  
ATOM   9323  C   ILE B 464     -13.385  17.222   7.238  1.00 30.95           C  
ANISOU 9323  C   ILE B 464     3556   4058   4146    112     28     38       C  
ATOM   9324  O   ILE B 464     -12.588  17.393   6.316  1.00 30.08           O  
ANISOU 9324  O   ILE B 464     3462   3937   4030    115     31     40       O  
ATOM   9325  CB  ILE B 464     -12.584  15.937   9.319  1.00 30.58           C  
ANISOU 9325  CB  ILE B 464     3474   4053   4091     91     32     40       C  
ATOM   9326  CG1 ILE B 464     -11.395  15.283   8.605  1.00 30.04           C  
ANISOU 9326  CG1 ILE B 464     3415   3985   4014     91     32     47       C  
ATOM   9327  CG2 ILE B 464     -13.822  15.024   9.360  1.00 30.07           C  
ANISOU 9327  CG2 ILE B 464     3400   3988   4035     99     17     47       C  
ATOM   9328  CD1 ILE B 464     -10.941  13.978   9.234  1.00 29.47           C  
ANISOU 9328  CD1 ILE B 464     3328   3933   3937     86     27     55       C  
ATOM   9329  N   PHE B 465     -14.678  16.979   7.024  1.00 30.85           N  
ANISOU 9329  N   PHE B 465     3541   4037   4143    121     15     42       N  
ATOM   9330  CA  PHE B 465     -15.198  16.808   5.666  1.00 32.00           C  
ANISOU 9330  CA  PHE B 465     3703   4162   4291    137      2     48       C  
ATOM   9331  C   PHE B 465     -15.869  18.054   5.057  1.00 33.86           C  
ANISOU 9331  C   PHE B 465     3952   4379   4532    146      6     43       C  
ATOM   9332  O   PHE B 465     -16.503  17.972   3.999  1.00 34.50           O  
ANISOU 9332  O   PHE B 465     4047   4445   4617    160     -6     48       O  
ATOM   9333  CB  PHE B 465     -16.100  15.566   5.575  1.00 31.63           C  
ANISOU 9333  CB  PHE B 465     3648   4119   4251    143    -16     57       C  
ATOM   9334  CG  PHE B 465     -15.392  14.271   5.925  1.00 31.83           C  
ANISOU 9334  CG  PHE B 465     3664   4159   4270    136    -19     64       C  
ATOM   9335  CD1 PHE B 465     -16.014  13.311   6.725  1.00 30.63           C  
ANISOU 9335  CD1 PHE B 465     3493   4020   4123    133    -27     68       C  
ATOM   9336  CD2 PHE B 465     -14.085  14.017   5.473  1.00 30.71           C  
ANISOU 9336  CD2 PHE B 465     3532   4018   4117    133    -13     67       C  
ATOM   9337  CE1 PHE B 465     -15.356  12.127   7.047  1.00 29.64           C  
ANISOU 9337  CE1 PHE B 465     3360   3908   3992    127    -29     75       C  
ATOM   9338  CE2 PHE B 465     -13.428  12.839   5.803  1.00 28.83           C  
ANISOU 9338  CE2 PHE B 465     3286   3793   3873    128    -16     74       C  
ATOM   9339  CZ  PHE B 465     -14.066  11.895   6.590  1.00 28.96           C  
ANISOU 9339  CZ  PHE B 465     3284   3823   3895    125    -24     78       C  
ATOM   9340  N   LEU B 466     -15.683  19.207   5.697  1.00 35.04           N  
ANISOU 9340  N   LEU B 466     4101   4531   4683    139     22     33       N  
ATOM   9341  CA  LEU B 466     -16.254  20.465   5.228  1.00 36.49           C  
ANISOU 9341  CA  LEU B 466     4296   4696   4871    147     29     28       C  
ATOM   9342  C   LEU B 466     -15.774  20.795   3.817  1.00 37.66           C  
ANISOU 9342  C   LEU B 466     4469   4824   5014    158     28     31       C  
ATOM   9343  O   LEU B 466     -14.572  20.786   3.544  1.00 39.97           O  
ANISOU 9343  O   LEU B 466     4770   5117   5298    152     37     31       O  
ATOM   9344  CB  LEU B 466     -15.864  21.587   6.187  1.00 38.73           C  
ANISOU 9344  CB  LEU B 466     4575   4986   5154    135     49     16       C  
ATOM   9345  CG  LEU B 466     -16.892  22.620   6.676  1.00 39.28           C  
ANISOU 9345  CG  LEU B 466     4640   5049   5233    138     56      9       C  
ATOM   9346  CD1 LEU B 466     -18.133  21.967   7.280  1.00 38.16           C  
ANISOU 9346  CD1 LEU B 466     4481   4916   5101    141     44     12       C  
ATOM   9347  CD2 LEU B 466     -16.207  23.505   7.703  1.00 38.18           C  
ANISOU 9347  CD2 LEU B 466     4496   4919   5091    123     77     -3       C  
ATOM   9348  N   GLY B 467     -16.712  21.073   2.918  1.00 36.70           N  
ANISOU 9348  N   GLY B 467     4358   4685   4897    174     19     35       N  
ATOM   9349  CA  GLY B 467     -16.359  21.449   1.551  1.00 34.56           C  
ANISOU 9349  CA  GLY B 467     4113   4395   4621    186     18     39       C  
ATOM   9350  C   GLY B 467     -16.613  20.347   0.544  1.00 34.60           C  
ANISOU 9350  C   GLY B 467     4126   4395   4624    197     -1     49       C  
ATOM   9351  O   GLY B 467     -16.542  20.575  -0.659  1.00 34.45           O  
ANISOU 9351  O   GLY B 467     4129   4359   4601    210     -5     53       O  
ATOM   9352  N   LEU B 468     -16.925  19.149   1.028  1.00 35.36           N  
ANISOU 9352  N   LEU B 468     4206   4506   4723    193    -15     53       N  
ATOM   9353  CA  LEU B 468     -17.169  18.001   0.140  1.00 33.78           C  
ANISOU 9353  CA  LEU B 468     4013   4301   4520    202    -35     62       C  
ATOM   9354  C   LEU B 468     -18.647  17.826  -0.231  1.00 33.83           C  
ANISOU 9354  C   LEU B 468     4015   4300   4536    214    -54     65       C  
ATOM   9355  O   LEU B 468     -19.230  16.774   0.000  1.00 34.24           O  
ANISOU 9355  O   LEU B 468     4054   4360   4593    213    -69     69       O  
ATOM   9356  CB  LEU B 468     -16.581  16.713   0.742  1.00 31.74           C  
ANISOU 9356  CB  LEU B 468     3740   4060   4258    191    -39     66       C  
ATOM   9357  CG  LEU B 468     -15.077  16.717   1.036  1.00 31.04           C  
ANISOU 9357  CG  LEU B 468     3653   3979   4159    179    -22     65       C  
ATOM   9358  CD1 LEU B 468     -14.607  15.371   1.550  1.00 30.42           C  
ANISOU 9358  CD1 LEU B 468     3562   3917   4078    171    -28     71       C  
ATOM   9359  CD2 LEU B 468     -14.276  17.108  -0.192  1.00 31.49           C  
ANISOU 9359  CD2 LEU B 468     3736   4019   4207    187    -17     68       C  
ATOM   9360  N   THR B 469     -19.239  18.849  -0.840  1.00 34.68           N  
ANISOU 9360  N   THR B 469     4135   4392   4646    226    -53     63       N  
ATOM   9361  CA  THR B 469     -20.677  18.827  -1.134  1.00 35.11           C  
ANISOU 9361  CA  THR B 469     4186   4442   4711    238    -70     65       C  
ATOM   9362  C   THR B 469     -21.101  17.969  -2.337  1.00 33.99           C  
ANISOU 9362  C   THR B 469     4055   4290   4566    251    -93     72       C  
ATOM   9363  O   THR B 469     -22.284  17.682  -2.489  1.00 35.06           O  
ANISOU 9363  O   THR B 469     4183   4425   4712    259   -110     74       O  
ATOM   9364  CB  THR B 469     -21.252  20.250  -1.276  1.00 36.44           C  
ANISOU 9364  CB  THR B 469     4361   4598   4884    247    -61     61       C  
ATOM   9365  OG1 THR B 469     -20.601  20.922  -2.359  1.00 38.22           O  
ANISOU 9365  OG1 THR B 469     4613   4807   5100    257    -54     62       O  
ATOM   9366  CG2 THR B 469     -21.025  21.050   0.000  1.00 37.13           C  
ANISOU 9366  CG2 THR B 469     4434   4695   4976    234    -40     53       C  
ATOM   9367  N   SER B 470     -20.160  17.558  -3.180  1.00 33.23           N  
ANISOU 9367  N   SER B 470     3977   4188   4458    253    -93     76       N  
ATOM   9368  CA  SER B 470     -20.492  16.706  -4.337  1.00 34.28           C  
ANISOU 9368  CA  SER B 470     4123   4312   4587    265   -115     82       C  
ATOM   9369  C   SER B 470     -20.237  15.222  -4.101  1.00 34.60           C  
ANISOU 9369  C   SER B 470     4154   4365   4628    256   -126     86       C  
ATOM   9370  O   SER B 470     -20.615  14.390  -4.928  1.00 35.41           O  
ANISOU 9370  O   SER B 470     4264   4461   4728    264   -145     90       O  
ATOM   9371  CB  SER B 470     -19.692  17.108  -5.585  1.00 34.71           C  
ANISOU 9371  CB  SER B 470     4208   4351   4629    275   -111     85       C  
ATOM   9372  OG  SER B 470     -19.898  18.454  -5.951  1.00 35.67           O  
ANISOU 9372  OG  SER B 470     4341   4459   4750    285   -101     83       O  
ATOM   9373  N   LEU B 471     -19.574  14.901  -2.990  1.00 34.70           N  
ANISOU 9373  N   LEU B 471     4151   4393   4641    241   -113     84       N  
ATOM   9374  CA  LEU B 471     -19.048  13.555  -2.725  1.00 32.41           C  
ANISOU 9374  CA  LEU B 471     3853   4113   4348    232   -118     89       C  
ATOM   9375  C   LEU B 471     -20.121  12.458  -2.734  1.00 31.09           C  
ANISOU 9375  C   LEU B 471     3673   3949   4189    234   -139     92       C  
ATOM   9376  O   LEU B 471     -21.156  12.599  -2.095  1.00 29.92           O  
ANISOU 9376  O   LEU B 471     3508   3806   4054    233   -144     89       O  
ATOM   9377  CB  LEU B 471     -18.282  13.570  -1.394  1.00 31.76           C  
ANISOU 9377  CB  LEU B 471     3753   4048   4264    215   -100     86       C  
ATOM   9378  CG  LEU B 471     -17.314  12.439  -1.027  1.00 31.32           C  
ANISOU 9378  CG  LEU B 471     3692   4004   4203    205    -97     91       C  
ATOM   9379  CD1 LEU B 471     -16.152  12.389  -1.995  1.00 31.74           C  
ANISOU 9379  CD1 LEU B 471     3767   4048   4243    209    -91     94       C  
ATOM   9380  CD2 LEU B 471     -16.800  12.624   0.395  1.00 30.70           C  
ANISOU 9380  CD2 LEU B 471     3592   3944   4125    190    -80     87       C  
ATOM   9381  N   ASN B 472     -19.856  11.378  -3.468  1.00 30.16           N  
ANISOU 9381  N   ASN B 472     3566   3827   4066    237   -151     97       N  
ATOM   9382  CA  ASN B 472     -20.746  10.212  -3.513  1.00 30.71           C  
ANISOU 9382  CA  ASN B 472     3624   3899   4143    237   -172    100       C  
ATOM   9383  C   ASN B 472     -20.193   9.036  -2.756  1.00 31.00           C  
ANISOU 9383  C   ASN B 472     3648   3950   4180    225   -168    103       C  
ATOM   9384  O   ASN B 472     -20.940   8.307  -2.104  1.00 31.76           O  
ANISOU 9384  O   ASN B 472     3724   4054   4287    219   -176    104       O  
ATOM   9385  CB  ASN B 472     -20.983   9.742  -4.944  1.00 30.85           C  
ANISOU 9385  CB  ASN B 472     3664   3902   4156    250   -190    103       C  
ATOM   9386  CG  ASN B 472     -21.582  10.810  -5.806  1.00 31.94           C  
ANISOU 9386  CG  ASN B 472     3817   4026   4293    264   -196    100       C  
ATOM   9387  OD1 ASN B 472     -22.606  11.408  -5.450  1.00 32.77           O  
ANISOU 9387  OD1 ASN B 472     3909   4132   4409    267   -200     97       O  
ATOM   9388  ND2 ASN B 472     -20.946  11.073  -6.947  1.00 31.83           N  
ANISOU 9388  ND2 ASN B 472     3829   3998   4264    274   -195    102       N  
ATOM   9389  N   THR B 473     -18.881   8.841  -2.877  1.00 31.22           N  
ANISOU 9389  N   THR B 473     3687   3979   4196    221   -156    106       N  
ATOM   9390  CA  THR B 473     -18.187   7.726  -2.243  1.00 30.61           C  
ANISOU 9390  CA  THR B 473     3598   3914   4116    210   -151    111       C  
ATOM   9391  C   THR B 473     -17.208   8.204  -1.171  1.00 29.80           C  
ANISOU 9391  C   THR B 473     3486   3827   4010    199   -129    110       C  
ATOM   9392  O   THR B 473     -16.308   9.001  -1.442  1.00 30.26           O  
ANISOU 9392  O   THR B 473     3557   3881   4060    200   -116    108       O  
ATOM   9393  CB  THR B 473     -17.444   6.880  -3.281  1.00 30.75           C  
ANISOU 9393  CB  THR B 473     3636   3922   4123    215   -156    117       C  
ATOM   9394  OG1 THR B 473     -18.237   6.786  -4.472  1.00 32.10           O  
ANISOU 9394  OG1 THR B 473     3824   4078   4295    228   -175    116       O  
ATOM   9395  CG2 THR B 473     -17.214   5.487  -2.739  1.00 31.93           C  
ANISOU 9395  CG2 THR B 473     3774   4083   4275    207   -158    122       C  
ATOM   9396  N   LEU B 474     -17.405   7.725   0.051  1.00 29.10           N  
ANISOU 9396  N   LEU B 474     3373   3754   3928    189   -125    110       N  
ATOM   9397  CA  LEU B 474     -16.497   8.038   1.143  1.00 28.81           C  
ANISOU 9397  CA  LEU B 474     3324   3734   3887    177   -106    109       C  
ATOM   9398  C   LEU B 474     -16.057   6.751   1.810  1.00 29.24           C  
ANISOU 9398  C   LEU B 474     3366   3802   3940    169   -105    115       C  
ATOM   9399  O   LEU B 474     -16.812   6.157   2.597  1.00 28.39           O  
ANISOU 9399  O   LEU B 474     3240   3704   3842    165   -110    116       O  
ATOM   9400  CB  LEU B 474     -17.137   9.002   2.147  1.00 28.03           C  
ANISOU 9400  CB  LEU B 474     3209   3643   3796    172    -99    101       C  
ATOM   9401  CG  LEU B 474     -16.291   9.490   3.329  1.00 28.98           C  
ANISOU 9401  CG  LEU B 474     3317   3780   3912    160    -79     98       C  
ATOM   9402  CD1 LEU B 474     -14.866   9.862   2.926  1.00 28.87           C  
ANISOU 9402  CD1 LEU B 474     3317   3765   3885    158    -67     98       C  
ATOM   9403  CD2 LEU B 474     -16.975  10.654   4.034  1.00 28.91           C  
ANISOU 9403  CD2 LEU B 474     3299   3774   3910    158    -73     90       C  
ATOM   9404  N   LYS B 475     -14.836   6.326   1.466  1.00 29.32           N  
ANISOU 9404  N   LYS B 475     3386   3813   3939    168    -98    120       N  
ATOM   9405  CA  LYS B 475     -14.210   5.142   2.045  1.00 29.00           C  
ANISOU 9405  CA  LYS B 475     3336   3786   3896    162    -94    128       C  
ATOM   9406  C   LYS B 475     -13.271   5.571   3.169  1.00 29.55           C  
ANISOU 9406  C   LYS B 475     3392   3875   3960    151    -76    126       C  
ATOM   9407  O   LYS B 475     -12.294   6.290   2.941  1.00 29.74           O  
ANISOU 9407  O   LYS B 475     3426   3898   3976    150    -65    124       O  
ATOM   9408  CB  LYS B 475     -13.437   4.366   0.978  1.00 29.34           C  
ANISOU 9408  CB  LYS B 475     3397   3818   3929    168    -98    135       C  
ATOM   9409  CG  LYS B 475     -14.310   3.616  -0.020  1.00 29.79           C  
ANISOU 9409  CG  LYS B 475     3467   3861   3992    177   -117    137       C  
ATOM   9410  CD  LYS B 475     -13.509   2.984  -1.152  1.00 28.87           C  
ANISOU 9410  CD  LYS B 475     3371   3731   3864    183   -118    143       C  
ATOM   9411  CE  LYS B 475     -14.456   2.231  -2.074  1.00 30.47           C  
ANISOU 9411  CE  LYS B 475     3585   3920   4072    191   -138    144       C  
ATOM   9412  NZ  LYS B 475     -13.912   1.862  -3.419  1.00 30.40           N  
ANISOU 9412  NZ  LYS B 475     3603   3894   4053    200   -143    148       N  
ATOM   9413  N   MET B 476     -13.570   5.143   4.388  1.00 29.62           N  
ANISOU 9413  N   MET B 476     3378   3900   3973    143    -74    127       N  
ATOM   9414  CA  MET B 476     -12.728   5.511   5.518  1.00 31.08           C  
ANISOU 9414  CA  MET B 476     3549   4105   4152    133    -58    125       C  
ATOM   9415  C   MET B 476     -12.649   4.402   6.555  1.00 31.27           C  
ANISOU 9415  C   MET B 476     3554   4148   4177    127    -56    132       C  
ATOM   9416  O   MET B 476     -12.705   4.656   7.765  1.00 30.93           O  
ANISOU 9416  O   MET B 476     3494   4122   4135    119    -48    129       O  
ATOM   9417  CB  MET B 476     -13.188   6.829   6.145  1.00 31.92           C  
ANISOU 9417  CB  MET B 476     3649   4215   4262    129    -51    115       C  
ATOM   9418  CG  MET B 476     -14.640   6.828   6.571  1.00 34.23           C  
ANISOU 9418  CG  MET B 476     3929   4506   4568    131    -60    112       C  
ATOM   9419  SD  MET B 476     -15.109   8.358   7.381  1.00 39.29           S  
ANISOU 9419  SD  MET B 476     4562   5151   5213    126    -50    100       S  
ATOM   9420  CE  MET B 476     -14.133   8.313   8.887  1.00 38.74           C  
ANISOU 9420  CE  MET B 476     4474   5109   5135    112    -34     99       C  
ATOM   9421  N   ALA B 477     -12.516   3.169   6.068  1.00 31.13           N  
ANISOU 9421  N   ALA B 477     3542   4127   4159    131    -63    142       N  
ATOM   9422  CA  ALA B 477     -12.364   2.016   6.942  1.00 32.41           C  
ANISOU 9422  CA  ALA B 477     3688   4305   4322    127    -60    150       C  
ATOM   9423  C   ALA B 477     -10.998   2.028   7.634  1.00 33.77           C  
ANISOU 9423  C   ALA B 477     3853   4494   4481    120    -46    153       C  
ATOM   9424  O   ALA B 477     -10.042   2.627   7.136  1.00 33.96           O  
ANISOU 9424  O   ALA B 477     3889   4516   4497    120    -39    151       O  
ATOM   9425  CB  ALA B 477     -12.559   0.729   6.157  1.00 32.35           C  
ANISOU 9425  CB  ALA B 477     3689   4285   4317    133    -71    159       C  
ATOM   9426  N   GLY B 478     -10.911   1.388   8.794  1.00 34.08           N  
ANISOU 9426  N   GLY B 478     3873   4553   4520    115    -40    158       N  
ATOM   9427  CA  GLY B 478      -9.621   1.196   9.444  1.00 33.57           C  
ANISOU 9427  CA  GLY B 478     3801   4508   4444    110    -28    163       C  
ATOM   9428  C   GLY B 478      -9.203   2.323  10.366  1.00 34.44           C  
ANISOU 9428  C   GLY B 478     3900   4634   4548    101    -17    154       C  
ATOM   9429  O   GLY B 478      -8.208   2.199  11.073  1.00 35.67           O  
ANISOU 9429  O   GLY B 478     4047   4809   4695     96     -8    157       O  
ATOM   9430  N   ASN B 479      -9.957   3.419  10.382  1.00 32.49           N  
ANISOU 9430  N   ASN B 479     3656   4381   4308    100    -19    143       N  
ATOM   9431  CA  ASN B 479      -9.564   4.559  11.205  1.00 31.46           C  
ANISOU 9431  CA  ASN B 479     3516   4262   4171     91     -8    133       C  
ATOM   9432  C   ASN B 479     -10.209   4.525  12.577  1.00 31.32           C  
ANISOU 9432  C   ASN B 479     3479   4263   4157     86     -5    130       C  
ATOM   9433  O   ASN B 479     -10.580   3.449  13.041  1.00 32.60           O  
ANISOU 9433  O   ASN B 479     3630   4431   4322     87     -9    139       O  
ATOM   9434  CB  ASN B 479      -9.820   5.862  10.463  1.00 31.15           C  
ANISOU 9434  CB  ASN B 479     3492   4207   4136     92     -8    122       C  
ATOM   9435  CG  ASN B 479      -8.999   5.957   9.197  1.00 31.18           C  
ANISOU 9435  CG  ASN B 479     3516   4195   4135     97     -8    124       C  
ATOM   9436  OD1 ASN B 479      -7.772   6.042   9.247  1.00 30.73           O  
ANISOU 9436  OD1 ASN B 479     3460   4147   4069     93      0    125       O  
ATOM   9437  ND2 ASN B 479      -9.670   5.913   8.049  1.00 31.57           N  
ANISOU 9437  ND2 ASN B 479     3582   4222   4190    107    -18    125       N  
ATOM   9438  N   SER B 480     -10.317   5.673  13.241  1.00 30.02           N  
ANISOU 9438  N   SER B 480     3309   4105   3991     79      1    119       N  
ATOM   9439  CA  SER B 480     -10.918   5.718  14.572  1.00 30.79           C  
ANISOU 9439  CA  SER B 480     3387   4219   4090     74      5    116       C  
ATOM   9440  C   SER B 480     -11.460   7.113  14.898  1.00 30.96           C  
ANISOU 9440  C   SER B 480     3410   4238   4116     70      9    102       C  
ATOM   9441  O   SER B 480     -11.234   8.054  14.137  1.00 30.79           O  
ANISOU 9441  O   SER B 480     3402   4202   4094     70     11     94       O  
ATOM   9442  CB  SER B 480      -9.929   5.220  15.641  1.00 30.54           C  
ANISOU 9442  CB  SER B 480     3341   4214   4047     67     13    121       C  
ATOM   9443  OG  SER B 480      -8.895   6.157  15.885  1.00 32.32           O  
ANISOU 9443  OG  SER B 480     3568   4449   4262     59     22    112       O  
ATOM   9444  N   PHE B 481     -12.176   7.240  16.017  1.00 31.17           N  
ANISOU 9444  N   PHE B 481     3421   4276   4145     66     13     98       N  
ATOM   9445  CA  PHE B 481     -12.833   8.504  16.391  1.00 31.91           C  
ANISOU 9445  CA  PHE B 481     3515   4366   4244     63     18     85       C  
ATOM   9446  C   PHE B 481     -12.555   8.871  17.829  1.00 32.47           C  
ANISOU 9446  C   PHE B 481     3570   4459   4306     54     29     79       C  
ATOM   9447  O   PHE B 481     -12.433   7.985  18.664  1.00 33.36           O  
ANISOU 9447  O   PHE B 481     3670   4590   4414     52     30     87       O  
ATOM   9448  CB  PHE B 481     -14.348   8.386  16.192  1.00 32.10           C  
ANISOU 9448  CB  PHE B 481     3537   4375   4283     70     10     87       C  
ATOM   9449  CG  PHE B 481     -14.786   8.585  14.772  1.00 32.15           C  
ANISOU 9449  CG  PHE B 481     3560   4356   4297     79      0     87       C  
ATOM   9450  CD1 PHE B 481     -14.658   7.562  13.839  1.00 31.72           C  
ANISOU 9450  CD1 PHE B 481     3513   4292   4244     86    -10     97       C  
ATOM   9451  CD2 PHE B 481     -15.313   9.802  14.364  1.00 32.13           C  
ANISOU 9451  CD2 PHE B 481     3567   4339   4301     81      1     77       C  
ATOM   9452  CE1 PHE B 481     -15.043   7.754  12.528  1.00 32.23           C  
ANISOU 9452  CE1 PHE B 481     3594   4334   4315     94    -19     97       C  
ATOM   9453  CE2 PHE B 481     -15.705   9.998  13.053  1.00 32.60           C  
ANISOU 9453  CE2 PHE B 481     3643   4377   4367     90     -7     78       C  
ATOM   9454  CZ  PHE B 481     -15.567   8.975  12.135  1.00 32.77           C  
ANISOU 9454  CZ  PHE B 481     3671   4389   4389     97    -18     88       C  
ATOM   9455  N   LYS B 482     -12.474  10.167  18.132  1.00 33.74           N  
ANISOU 9455  N   LYS B 482     3734   4620   4465     47     37     66       N  
ATOM   9456  CA  LYS B 482     -12.282  10.597  19.519  1.00 35.20           C  
ANISOU 9456  CA  LYS B 482     3906   4827   4642     38     48     58       C  
ATOM   9457  C   LYS B 482     -13.364   9.973  20.390  1.00 36.37           C  
ANISOU 9457  C   LYS B 482     4040   4983   4796     41     46     63       C  
ATOM   9458  O   LYS B 482     -14.529   9.899  19.978  1.00 35.01           O  
ANISOU 9458  O   LYS B 482     3870   4794   4638     49     40     65       O  
ATOM   9459  CB  LYS B 482     -12.295  12.117  19.666  1.00 36.18           C  
ANISOU 9459  CB  LYS B 482     4035   4945   4764     32     57     42       C  
ATOM   9460  CG  LYS B 482     -11.815  12.587  21.046  1.00 40.19           C  
ANISOU 9460  CG  LYS B 482     4531   5477   5261     20     68     32       C  
ATOM   9461  CD  LYS B 482     -12.073  14.069  21.319  1.00 41.70           C  
ANISOU 9461  CD  LYS B 482     4727   5662   5454     14     78     16       C  
ATOM   9462  CE  LYS B 482     -13.567  14.386  21.295  1.00 44.62           C  
ANISOU 9462  CE  LYS B 482     5098   6016   5838     21     77     15       C  
ATOM   9463  NZ  LYS B 482     -13.925  15.780  21.694  1.00 46.59           N  
ANISOU 9463  NZ  LYS B 482     5351   6260   6088     16     88      0       N  
ATOM   9464  N   ASP B 483     -12.955   9.501  21.572  1.00 37.96           N  
ANISOU 9464  N   ASP B 483     4227   5208   4987     36     51     66       N  
ATOM   9465  CA  ASP B 483     -13.838   8.817  22.535  1.00 38.77           C  
ANISOU 9465  CA  ASP B 483     4315   5320   5093     39     52     72       C  
ATOM   9466  C   ASP B 483     -14.660   7.688  21.901  1.00 38.20           C  
ANISOU 9466  C   ASP B 483     4244   5236   5035     49     41     85       C  
ATOM   9467  O   ASP B 483     -15.711   7.317  22.426  1.00 39.80           O  
ANISOU 9467  O   ASP B 483     4437   5438   5247     52     41     89       O  
ATOM   9468  CB  ASP B 483     -14.779   9.815  23.242  1.00 40.01           C  
ANISOU 9468  CB  ASP B 483     4469   5476   5255     36     59     60       C  
ATOM   9469  CG  ASP B 483     -14.028  10.926  23.983  1.00 44.88           C  
ANISOU 9469  CG  ASP B 483     5085   6106   5859     25     70     46       C  
ATOM   9470  OD1 ASP B 483     -13.203  10.627  24.883  1.00 44.86           O  
ANISOU 9470  OD1 ASP B 483     5074   6128   5842     19     75     46       O  
ATOM   9471  OD2 ASP B 483     -14.288  12.113  23.680  1.00 47.22           O  
ANISOU 9471  OD2 ASP B 483     5391   6390   6160     23     74     33       O  
ATOM   9472  N   ASN B 484     -14.187   7.156  20.773  1.00 36.14           N  
ANISOU 9472  N   ASN B 484     3992   4963   4774     53     33     92       N  
ATOM   9473  CA  ASN B 484     -14.909   6.127  20.016  1.00 34.10           C  
ANISOU 9473  CA  ASN B 484     3737   4690   4529     62     22    103       C  
ATOM   9474  C   ASN B 484     -16.386   6.460  19.720  1.00 33.56           C  
ANISOU 9474  C   ASN B 484     3669   4604   4478     67     17    100       C  
ATOM   9475  O   ASN B 484     -17.230   5.566  19.608  1.00 33.23           O  
ANISOU 9475  O   ASN B 484     3621   4555   4447     73     10    109       O  
ATOM   9476  CB  ASN B 484     -14.773   4.756  20.698  1.00 34.77           C  
ANISOU 9476  CB  ASN B 484     3808   4790   4610     64     23    117       C  
ATOM   9477  CG  ASN B 484     -13.341   4.221  20.686  1.00 34.56           C  
ANISOU 9477  CG  ASN B 484     3784   4778   4569     61     25    123       C  
ATOM   9478  OD1 ASN B 484     -12.891   3.624  21.660  1.00 33.44           O  
ANISOU 9478  OD1 ASN B 484     3629   4657   4417     59     31    129       O  
ATOM   9479  ND2 ASN B 484     -12.633   4.412  19.579  1.00 33.69           N  
ANISOU 9479  ND2 ASN B 484     3688   4656   4457     62     21    122       N  
ATOM   9480  N   THR B 485     -16.684   7.750  19.587  1.00 31.92           N  
ANISOU 9480  N   THR B 485     3467   4387   4272     66     21     88       N  
ATOM   9481  CA  THR B 485     -18.015   8.217  19.228  1.00 30.33           C  
ANISOU 9481  CA  THR B 485     3267   4168   4087     71     16     85       C  
ATOM   9482  C   THR B 485     -18.008   8.755  17.796  1.00 29.63           C  
ANISOU 9482  C   THR B 485     3196   4057   4003     77      8     81       C  
ATOM   9483  O   THR B 485     -17.168   9.578  17.449  1.00 30.69           O  
ANISOU 9483  O   THR B 485     3341   4189   4129     73     13     74       O  
ATOM   9484  CB  THR B 485     -18.478   9.336  20.185  1.00 30.25           C  
ANISOU 9484  CB  THR B 485     3251   4164   4077     67     27     73       C  
ATOM   9485  OG1 THR B 485     -18.339   8.902  21.542  1.00 29.07           O  
ANISOU 9485  OG1 THR B 485     3087   4038   3921     62     36     75       O  
ATOM   9486  CG2 THR B 485     -19.939   9.716  19.919  1.00 30.53           C  
ANISOU 9486  CG2 THR B 485     3286   4183   4131     74     23     71       C  
ATOM   9487  N   LEU B 486     -18.941   8.296  16.967  1.00 29.23           N  
ANISOU 9487  N   LEU B 486     3149   3990   3966     85     -4     87       N  
ATOM   9488  CA  LEU B 486     -19.084   8.813  15.609  1.00 29.35           C  
ANISOU 9488  CA  LEU B 486     3181   3983   3986     92    -12     84       C  
ATOM   9489  C   LEU B 486     -19.767  10.165  15.663  1.00 29.23           C  
ANISOU 9489  C   LEU B 486     3169   3959   3978     93     -7     73       C  
ATOM   9490  O   LEU B 486     -20.924  10.259  16.067  1.00 28.82           O  
ANISOU 9490  O   LEU B 486     3107   3905   3938     96     -9     73       O  
ATOM   9491  CB  LEU B 486     -19.915   7.855  14.759  1.00 30.80           C  
ANISOU 9491  CB  LEU B 486     3366   4153   4182    100    -28     93       C  
ATOM   9492  CG  LEU B 486     -20.173   8.177  13.283  1.00 31.15           C  
ANISOU 9492  CG  LEU B 486     3428   4174   4231    109    -40     91       C  
ATOM   9493  CD1 LEU B 486     -18.901   8.020  12.461  1.00 30.52           C  
ANISOU 9493  CD1 LEU B 486     3364   4092   4139    109    -40     94       C  
ATOM   9494  CD2 LEU B 486     -21.255   7.243  12.763  1.00 31.47           C  
ANISOU 9494  CD2 LEU B 486     3465   4205   4287    116    -55     98       C  
ATOM   9495  N   SER B 487     -19.047  11.206  15.250  1.00 29.70           N  
ANISOU 9495  N   SER B 487     3242   4014   4029     91     -1     65       N  
ATOM   9496  CA  SER B 487     -19.482  12.596  15.436  1.00 29.66           C  
ANISOU 9496  CA  SER B 487     3239   4001   4026     91      7     54       C  
ATOM   9497  C   SER B 487     -20.114  13.213  14.183  1.00 29.96           C  
ANISOU 9497  C   SER B 487     3292   4016   4074    101     -1     53       C  
ATOM   9498  O   SER B 487     -20.091  12.606  13.114  1.00 29.10           O  
ANISOU 9498  O   SER B 487     3192   3895   3966    108    -13     59       O  
ATOM   9499  CB  SER B 487     -18.300  13.437  15.890  1.00 29.27           C  
ANISOU 9499  CB  SER B 487     3195   3962   3964     81     21     45       C  
ATOM   9500  OG  SER B 487     -17.151  13.090  15.142  1.00 29.91           O  
ANISOU 9500  OG  SER B 487     3286   4042   4035     80     18     48       O  
ATOM   9501  N   ASN B 488     -20.666  14.423  14.329  1.00 31.57           N  
ANISOU 9501  N   ASN B 488     3499   4212   4283    102      6     44       N  
ATOM   9502  CA  ASN B 488     -21.390  15.124  13.252  1.00 31.54           C  
ANISOU 9502  CA  ASN B 488     3508   4186   4288    113      0     42       C  
ATOM   9503  C   ASN B 488     -20.463  15.575  12.115  1.00 31.71           C  
ANISOU 9503  C   ASN B 488     3551   4196   4302    116      0     41       C  
ATOM   9504  O   ASN B 488     -20.368  16.769  11.795  1.00 32.51           O  
ANISOU 9504  O   ASN B 488     3662   4286   4401    118      8     33       O  
ATOM   9505  CB  ASN B 488     -22.189  16.306  13.826  1.00 32.55           C  
ANISOU 9505  CB  ASN B 488     3632   4310   4423    114     10     34       C  
ATOM   9506  CG  ASN B 488     -23.305  16.785  12.899  1.00 34.87           C  
ANISOU 9506  CG  ASN B 488     3933   4584   4730    128      1     35       C  
ATOM   9507  OD1 ASN B 488     -23.964  15.989  12.221  1.00 38.42           O  
ANISOU 9507  OD1 ASN B 488     4381   5027   5189    136    -15     43       O  
ATOM   9508  ND2 ASN B 488     -23.534  18.095  12.881  1.00 33.98           N  
ANISOU 9508  ND2 ASN B 488     3828   4462   4620    130     11     27       N  
ATOM   9509  N   VAL B 489     -19.789  14.607  11.499  1.00 30.06           N  
ANISOU 9509  N   VAL B 489     3346   3987   4085    117     -9     48       N  
ATOM   9510  CA  VAL B 489     -18.811  14.897  10.464  1.00 30.53           C  
ANISOU 9510  CA  VAL B 489     3425   4036   4136    119     -8     48       C  
ATOM   9511  C   VAL B 489     -19.435  14.890   9.070  1.00 31.28           C  
ANISOU 9511  C   VAL B 489     3536   4110   4238    133    -22     53       C  
ATOM   9512  O   VAL B 489     -18.788  15.280   8.088  1.00 31.39           O  
ANISOU 9512  O   VAL B 489     3568   4112   4245    137    -22     52       O  
ATOM   9513  CB  VAL B 489     -17.628  13.910  10.512  1.00 29.87           C  
ANISOU 9513  CB  VAL B 489     3341   3965   4042    112     -8     54       C  
ATOM   9514  CG1 VAL B 489     -16.932  13.985  11.863  1.00 28.99           C  
ANISOU 9514  CG1 VAL B 489     3215   3875   3922     99      4     50       C  
ATOM   9515  CG2 VAL B 489     -18.095  12.491  10.207  1.00 28.88           C  
ANISOU 9515  CG2 VAL B 489     3211   3841   3922    117    -24     65       C  
ATOM   9516  N   PHE B 490     -20.689  14.445   8.999  1.00 31.61           N  
ANISOU 9516  N   PHE B 490     3569   4148   4292    140    -35     56       N  
ATOM   9517  CA  PHE B 490     -21.383  14.245   7.728  1.00 31.84           C  
ANISOU 9517  CA  PHE B 490     3610   4159   4327    153    -52     61       C  
ATOM   9518  C   PHE B 490     -22.448  15.299   7.400  1.00 32.76           C  
ANISOU 9518  C   PHE B 490     3730   4262   4454    163    -53     57       C  
ATOM   9519  O   PHE B 490     -23.072  15.228   6.346  1.00 33.48           O  
ANISOU 9519  O   PHE B 490     3830   4338   4550    174    -67     60       O  
ATOM   9520  CB  PHE B 490     -22.020  12.848   7.686  1.00 30.27           C  
ANISOU 9520  CB  PHE B 490     3400   3964   4136    155    -68     70       C  
ATOM   9521  CG  PHE B 490     -21.041  11.724   7.868  1.00 29.40           C  
ANISOU 9521  CG  PHE B 490     3288   3865   4016    148    -68     75       C  
ATOM   9522  CD1 PHE B 490     -19.949  11.584   7.018  1.00 28.61           C  
ANISOU 9522  CD1 PHE B 490     3205   3759   3905    149    -68     78       C  
ATOM   9523  CD2 PHE B 490     -21.224  10.783   8.881  1.00 29.11           C  
ANISOU 9523  CD2 PHE B 490     3232   3844   3984    141    -68     79       C  
ATOM   9524  CE1 PHE B 490     -19.043  10.543   7.188  1.00 28.44           C  
ANISOU 9524  CE1 PHE B 490     3182   3749   3875    143    -67     84       C  
ATOM   9525  CE2 PHE B 490     -20.320   9.736   9.050  1.00 29.13           C  
ANISOU 9525  CE2 PHE B 490     3233   3857   3978    135    -67     86       C  
ATOM   9526  CZ  PHE B 490     -19.226   9.619   8.206  1.00 28.30           C  
ANISOU 9526  CZ  PHE B 490     3145   3747   3861    136    -67     88       C  
ATOM   9527  N   ALA B 491     -22.648  16.275   8.282  1.00 35.18           N  
ANISOU 9527  N   ALA B 491     4029   4573   4763    158    -38     50       N  
ATOM   9528  CA  ALA B 491     -23.759  17.236   8.147  1.00 36.02           C  
ANISOU 9528  CA  ALA B 491     4136   4668   4881    167    -38     46       C  
ATOM   9529  C   ALA B 491     -23.942  17.765   6.719  1.00 38.20           C  
ANISOU 9529  C   ALA B 491     4432   4924   5156    181    -47     48       C  
ATOM   9530  O   ALA B 491     -25.065  17.777   6.209  1.00 40.62           O  
ANISOU 9530  O   ALA B 491     4738   5221   5474    193    -60     51       O  
ATOM   9531  CB  ALA B 491     -23.615  18.388   9.136  1.00 34.28           C  
ANISOU 9531  CB  ALA B 491     3912   4453   4659    160    -17     37       C  
ATOM   9532  N   ASN B 492     -22.845  18.167   6.080  1.00 38.03           N  
ANISOU 9532  N   ASN B 492     4429   4895   5122    181    -40     46       N  
ATOM   9533  CA  ASN B 492     -22.888  18.794   4.769  1.00 40.35           C  
ANISOU 9533  CA  ASN B 492     4745   5170   5414    194    -44     47       C  
ATOM   9534  C   ASN B 492     -22.449  17.905   3.586  1.00 40.73           C  
ANISOU 9534  C   ASN B 492     4807   5211   5455    200    -60     55       C  
ATOM   9535  O   ASN B 492     -22.222  18.407   2.474  1.00 41.63           O  
ANISOU 9535  O   ASN B 492     4943   5310   5564    210    -61     56       O  
ATOM   9536  CB  ASN B 492     -22.075  20.102   4.797  1.00 44.92           C  
ANISOU 9536  CB  ASN B 492     5337   5742   5985    191    -23     40       C  
ATOM   9537  CG  ASN B 492     -22.882  21.294   5.316  1.00 50.49           C  
ANISOU 9537  CG  ASN B 492     6039   6444   6700    194    -12     33       C  
ATOM   9538  OD1 ASN B 492     -23.991  21.137   5.845  1.00 52.03           O  
ANISOU 9538  OD1 ASN B 492     6218   6643   6907    196    -18     34       O  
ATOM   9539  ND2 ASN B 492     -22.329  22.497   5.157  1.00 50.06           N  
ANISOU 9539  ND2 ASN B 492     5998   6379   6641    194      4     27       N  
ATOM   9540  N   THR B 493     -22.320  16.598   3.816  1.00 38.91           N  
ANISOU 9540  N   THR B 493     4566   4991   5224    194    -70     60       N  
ATOM   9541  CA  THR B 493     -21.952  15.668   2.734  1.00 37.58           C  
ANISOU 9541  CA  THR B 493     4412   4817   5050    200    -85     67       C  
ATOM   9542  C   THR B 493     -23.205  14.980   2.184  1.00 36.66           C  
ANISOU 9542  C   THR B 493     4290   4694   4944    210   -107     71       C  
ATOM   9543  O   THR B 493     -23.379  13.762   2.268  1.00 35.34           O  
ANISOU 9543  O   THR B 493     4113   4533   4779    207   -119     76       O  
ATOM   9544  CB  THR B 493     -20.835  14.671   3.137  1.00 36.81           C  
ANISOU 9544  CB  THR B 493     4310   4732   4943    189    -81     70       C  
ATOM   9545  OG1 THR B 493     -21.295  13.803   4.175  1.00 36.64           O  
ANISOU 9545  OG1 THR B 493     4265   4726   4928    180    -84     71       O  
ATOM   9546  CG2 THR B 493     -19.614  15.412   3.611  1.00 36.63           C  
ANISOU 9546  CG2 THR B 493     4292   4715   4910    179    -59     64       C  
ATOM   9547  N   THR B 494     -24.050  15.819   1.600  1.00 36.73           N  
ANISOU 9547  N   THR B 494     4305   4690   4958    222   -112     70       N  
ATOM   9548  CA  THR B 494     -25.421  15.521   1.217  1.00 35.59           C  
ANISOU 9548  CA  THR B 494     4154   4541   4826    232   -131     73       C  
ATOM   9549  C   THR B 494     -25.540  14.493   0.109  1.00 35.03           C  
ANISOU 9549  C   THR B 494     4093   4462   4752    239   -153     78       C  
ATOM   9550  O   THR B 494     -26.517  13.763   0.048  1.00 35.85           O  
ANISOU 9550  O   THR B 494     4185   4568   4867    242   -170     81       O  
ATOM   9551  CB  THR B 494     -26.081  16.843   0.808  1.00 36.87           C  
ANISOU 9551  CB  THR B 494     4325   4691   4993    245   -128     70       C  
ATOM   9552  OG1 THR B 494     -26.457  17.533   2.002  1.00 39.30           O  
ANISOU 9552  OG1 THR B 494     4615   5006   5309    238   -113     65       O  
ATOM   9553  CG2 THR B 494     -27.302  16.656  -0.091  1.00 37.57           C  
ANISOU 9553  CG2 THR B 494     4413   4769   5089    259   -151     73       C  
ATOM   9554  N   ASN B 495     -24.533  14.418  -0.748  1.00 33.96           N  
ANISOU 9554  N   ASN B 495     3980   4320   4603    242   -152     80       N  
ATOM   9555  CA  ASN B 495     -24.600  13.572  -1.926  1.00 33.82           C  
ANISOU 9555  CA  ASN B 495     3976   4293   4580    250   -171     85       C  
ATOM   9556  C   ASN B 495     -24.046  12.143  -1.793  1.00 34.43           C  
ANISOU 9556  C   ASN B 495     4048   4378   4654    241   -177     88       C  
ATOM   9557  O   ASN B 495     -23.979  11.394  -2.787  1.00 33.92           O  
ANISOU 9557  O   ASN B 495     3997   4306   4584    247   -192     92       O  
ATOM   9558  CB  ASN B 495     -23.954  14.303  -3.092  1.00 34.31           C  
ANISOU 9558  CB  ASN B 495     4065   4339   4628    261   -168     85       C  
ATOM   9559  CG  ASN B 495     -24.881  15.321  -3.700  1.00 34.24           C  
ANISOU 9559  CG  ASN B 495     4064   4318   4624    276   -174     84       C  
ATOM   9560  OD1 ASN B 495     -25.992  14.984  -4.090  1.00 33.72           O  
ANISOU 9560  OD1 ASN B 495     3993   4251   4568    284   -194     85       O  
ATOM   9561  ND2 ASN B 495     -24.438  16.579  -3.772  1.00 34.54           N  
ANISOU 9561  ND2 ASN B 495     4114   4350   4658    280   -157     81       N  
ATOM   9562  N   LEU B 496     -23.664  11.771  -0.570  1.00 33.61           N  
ANISOU 9562  N   LEU B 496     3927   4291   4553    227   -165     88       N  
ATOM   9563  CA  LEU B 496     -23.136  10.442  -0.284  1.00 32.86           C  
ANISOU 9563  CA  LEU B 496     3825   4204   4455    218   -167     92       C  
ATOM   9564  C   LEU B 496     -24.107   9.347  -0.660  1.00 32.94           C  
ANISOU 9564  C   LEU B 496     3828   4212   4475    221   -189     95       C  
ATOM   9565  O   LEU B 496     -25.260   9.356  -0.228  1.00 31.83           O  
ANISOU 9565  O   LEU B 496     3670   4074   4348    222   -197     94       O  
ATOM   9566  CB  LEU B 496     -22.757  10.312   1.192  1.00 32.47           C  
ANISOU 9566  CB  LEU B 496     3755   4173   4408    204   -151     91       C  
ATOM   9567  CG  LEU B 496     -21.257  10.263   1.516  1.00 32.21           C  
ANISOU 9567  CG  LEU B 496     3728   4147   4361    195   -134     92       C  
ATOM   9568  CD1 LEU B 496     -20.393  10.929   0.455  1.00 30.98           C  
ANISOU 9568  CD1 LEU B 496     3598   3979   4193    202   -129     92       C  
ATOM   9569  CD2 LEU B 496     -20.993  10.864   2.884  1.00 31.77           C  
ANISOU 9569  CD2 LEU B 496     3655   4107   4307    184   -116     88       C  
ATOM   9570  N   THR B 497     -23.628   8.416  -1.480  1.00 32.86           N  
ANISOU 9570  N   THR B 497     3831   4195   4456    223   -199     99       N  
ATOM   9571  CA  THR B 497     -24.391   7.212  -1.809  1.00 33.41           C  
ANISOU 9571  CA  THR B 497     3895   4263   4534    224   -219    102       C  
ATOM   9572  C   THR B 497     -23.755   5.961  -1.183  1.00 32.90           C  
ANISOU 9572  C   THR B 497     3821   4209   4468    213   -214    107       C  
ATOM   9573  O   THR B 497     -24.428   4.940  -0.993  1.00 33.14           O  
ANISOU 9573  O   THR B 497     3839   4242   4509    209   -225    108       O  
ATOM   9574  CB  THR B 497     -24.569   7.040  -3.334  1.00 34.02           C  
ANISOU 9574  CB  THR B 497     3996   4325   4606    237   -237    102       C  
ATOM   9575  OG1 THR B 497     -23.302   7.179  -3.991  1.00 35.31           O  
ANISOU 9575  OG1 THR B 497     4182   4482   4751    239   -228    104       O  
ATOM   9576  CG2 THR B 497     -25.531   8.079  -3.885  1.00 32.38           C  
ANISOU 9576  CG2 THR B 497     3792   4108   4403    249   -247     99       C  
ATOM   9577  N   PHE B 498     -22.471   6.072  -0.829  1.00 31.79           N  
ANISOU 9577  N   PHE B 498     3686   4075   4316    207   -196    108       N  
ATOM   9578  CA  PHE B 498     -21.665   4.961  -0.311  1.00 29.68           C  
ANISOU 9578  CA  PHE B 498     3413   3817   4044    198   -189    114       C  
ATOM   9579  C   PHE B 498     -20.811   5.453   0.859  1.00 29.36           C  
ANISOU 9579  C   PHE B 498     3362   3793   3999    188   -167    113       C  
ATOM   9580  O   PHE B 498     -20.007   6.378   0.691  1.00 29.43           O  
ANISOU 9580  O   PHE B 498     3383   3800   3998    189   -155    111       O  
ATOM   9581  CB  PHE B 498     -20.774   4.435  -1.435  1.00 28.84           C  
ANISOU 9581  CB  PHE B 498     3331   3701   3924    203   -192    118       C  
ATOM   9582  CG  PHE B 498     -19.994   3.197  -1.090  1.00 29.52           C  
ANISOU 9582  CG  PHE B 498     3414   3794   4006    195   -187    124       C  
ATOM   9583  CD1 PHE B 498     -20.468   1.937  -1.449  1.00 29.21           C  
ANISOU 9583  CD1 PHE B 498     3374   3751   3972    195   -202    127       C  
ATOM   9584  CD2 PHE B 498     -18.749   3.286  -0.445  1.00 29.23           C  
ANISOU 9584  CD2 PHE B 498     3375   3769   3959    188   -168    127       C  
ATOM   9585  CE1 PHE B 498     -19.734   0.791  -1.149  1.00 29.45           C  
ANISOU 9585  CE1 PHE B 498     3402   3787   3998    189   -196    134       C  
ATOM   9586  CE2 PHE B 498     -18.017   2.142  -0.142  1.00 28.42           C  
ANISOU 9586  CE2 PHE B 498     3270   3675   3854    183   -163    134       C  
ATOM   9587  CZ  PHE B 498     -18.507   0.893  -0.495  1.00 28.50           C  
ANISOU 9587  CZ  PHE B 498     3280   3679   3869    183   -176    138       C  
ATOM   9588  N   LEU B 499     -20.981   4.835   2.033  1.00 28.55           N  
ANISOU 9588  N   LEU B 499     3237   3705   3903    178   -161    116       N  
ATOM   9589  CA  LEU B 499     -20.193   5.175   3.227  1.00 28.24           C  
ANISOU 9589  CA  LEU B 499     3187   3683   3860    169   -142    115       C  
ATOM   9590  C   LEU B 499     -19.669   3.945   3.988  1.00 28.51           C  
ANISOU 9590  C   LEU B 499     3208   3731   3892    161   -136    122       C  
ATOM   9591  O   LEU B 499     -20.445   3.171   4.571  1.00 27.84           O  
ANISOU 9591  O   LEU B 499     3106   3651   3818    157   -142    125       O  
ATOM   9592  CB  LEU B 499     -20.992   6.097   4.153  1.00 28.14           C  
ANISOU 9592  CB  LEU B 499     3157   3677   3856    166   -136    109       C  
ATOM   9593  CG  LEU B 499     -20.329   6.691   5.400  1.00 28.18           C  
ANISOU 9593  CG  LEU B 499     3151   3700   3857    157   -116    107       C  
ATOM   9594  CD1 LEU B 499     -19.137   7.553   5.031  1.00 28.48           C  
ANISOU 9594  CD1 LEU B 499     3205   3735   3880    156   -104    103       C  
ATOM   9595  CD2 LEU B 499     -21.331   7.511   6.197  1.00 27.79           C  
ANISOU 9595  CD2 LEU B 499     3086   3653   3818    155   -112    101       C  
ATOM   9596  N   ASP B 500     -18.347   3.772   3.961  1.00 28.45           N  
ANISOU 9596  N   ASP B 500     3209   3729   3871    157   -126    126       N  
ATOM   9597  CA  ASP B 500     -17.665   2.676   4.656  1.00 28.61           C  
ANISOU 9597  CA  ASP B 500     3219   3762   3887    151   -119    133       C  
ATOM   9598  C   ASP B 500     -16.986   3.181   5.932  1.00 29.00           C  
ANISOU 9598  C   ASP B 500     3254   3831   3931    142   -101    132       C  
ATOM   9599  O   ASP B 500     -16.003   3.917   5.879  1.00 29.34           O  
ANISOU 9599  O   ASP B 500     3306   3878   3964    140    -90    129       O  
ATOM   9600  CB  ASP B 500     -16.638   1.991   3.738  1.00 28.59           C  
ANISOU 9600  CB  ASP B 500     3236   3753   3874    154   -119    139       C  
ATOM   9601  CG  ASP B 500     -16.177   0.638   4.275  1.00 29.80           C  
ANISOU 9601  CG  ASP B 500     3379   3916   4025    149   -116    149       C  
ATOM   9602  OD1 ASP B 500     -16.276   0.426   5.501  1.00 30.47           O  
ANISOU 9602  OD1 ASP B 500     3444   4018   4114    142   -108    150       O  
ATOM   9603  OD2 ASP B 500     -15.732  -0.227   3.476  1.00 29.96           O  
ANISOU 9603  OD2 ASP B 500     3412   3928   4040    153   -120    155       O  
ATOM   9604  N   LEU B 501     -17.527   2.766   7.070  1.00 29.62           N  
ANISOU 9604  N   LEU B 501     3311   3923   4017    136    -98    133       N  
ATOM   9605  CA  LEU B 501     -17.014   3.125   8.381  1.00 30.59           C  
ANISOU 9605  CA  LEU B 501     3419   4066   4135    128    -82    132       C  
ATOM   9606  C   LEU B 501     -16.622   1.869   9.155  1.00 31.58           C  
ANISOU 9606  C   LEU B 501     3532   4207   4259    123    -78    142       C  
ATOM   9607  O   LEU B 501     -16.624   1.868  10.399  1.00 32.07           O  
ANISOU 9607  O   LEU B 501     3576   4286   4320    117    -68    142       O  
ATOM   9608  CB  LEU B 501     -18.091   3.867   9.173  1.00 30.45           C  
ANISOU 9608  CB  LEU B 501     3387   4053   4128    126    -81    125       C  
ATOM   9609  CG  LEU B 501     -18.323   5.335   8.858  1.00 30.51           C  
ANISOU 9609  CG  LEU B 501     3403   4052   4136    128    -79    115       C  
ATOM   9610  CD1 LEU B 501     -19.638   5.768   9.482  1.00 29.66           C  
ANISOU 9610  CD1 LEU B 501     3281   3944   4042    128    -81    111       C  
ATOM   9611  CD2 LEU B 501     -17.151   6.162   9.378  1.00 30.25           C  
ANISOU 9611  CD2 LEU B 501     3372   4031   4090    121    -63    111       C  
ATOM   9612  N   SER B 502     -16.302   0.802   8.426  1.00 31.58           N  
ANISOU 9612  N   SER B 502     3542   4200   4257    127    -84    149       N  
ATOM   9613  CA  SER B 502     -15.914  -0.461   9.051  1.00 32.71           C  
ANISOU 9613  CA  SER B 502     3675   4355   4399    124    -80    160       C  
ATOM   9614  C   SER B 502     -14.530  -0.395   9.684  1.00 32.93           C  
ANISOU 9614  C   SER B 502     3699   4400   4411    119    -65    163       C  
ATOM   9615  O   SER B 502     -13.661   0.346   9.224  1.00 33.48           O  
ANISOU 9615  O   SER B 502     3780   4468   4471    119    -60    159       O  
ATOM   9616  CB  SER B 502     -15.986  -1.621   8.048  1.00 33.38           C  
ANISOU 9616  CB  SER B 502     3771   4425   4486    129    -90    167       C  
ATOM   9617  OG  SER B 502     -15.128  -1.393   6.951  1.00 34.00           O  
ANISOU 9617  OG  SER B 502     3870   4492   4554    134    -92    167       O  
ATOM   9618  N   LYS B 503     -14.351  -1.166  10.754  1.00 33.77           N  
ANISOU 9618  N   LYS B 503     3790   4524   4517    115    -58    170       N  
ATOM   9619  CA  LYS B 503     -13.069  -1.307  11.446  1.00 34.07           C  
ANISOU 9619  CA  LYS B 503     3821   4581   4540    111    -44    175       C  
ATOM   9620  C   LYS B 503     -12.545  -0.004  12.026  1.00 34.03           C  
ANISOU 9620  C   LYS B 503     3812   4587   4527    105    -35    166       C  
ATOM   9621  O   LYS B 503     -11.335   0.220  12.038  1.00 35.29           O  
ANISOU 9621  O   LYS B 503     3976   4756   4675    103    -27    167       O  
ATOM   9622  CB  LYS B 503     -12.017  -1.929  10.524  1.00 34.89           C  
ANISOU 9622  CB  LYS B 503     3941   4678   4636    115    -45    183       C  
ATOM   9623  CG  LYS B 503     -12.180  -3.422  10.319  1.00 37.42           C  
ANISOU 9623  CG  LYS B 503     4262   4994   4961    119    -49    194       C  
ATOM   9624  CD  LYS B 503     -11.205  -3.942   9.282  1.00 39.77           C  
ANISOU 9624  CD  LYS B 503     4577   5282   5251    124    -49    201       C  
ATOM   9625  CE  LYS B 503     -11.459  -5.409   8.979  1.00 43.07           C  
ANISOU 9625  CE  LYS B 503     4998   5693   5674    128    -53    211       C  
ATOM   9626  NZ  LYS B 503     -10.522  -5.912   7.932  1.00 46.60           N  
ANISOU 9626  NZ  LYS B 503     5463   6129   6113    133    -53    217       N  
ATOM   9627  N   CYS B 504     -13.451   0.856  12.495  1.00 33.32           N  
ANISOU 9627  N   CYS B 504     3716   4498   4445    103    -36    157       N  
ATOM   9628  CA  CYS B 504     -13.064   2.143  13.087  1.00 32.43           C  
ANISOU 9628  CA  CYS B 504     3600   4396   4326     96    -26    146       C  
ATOM   9629  C   CYS B 504     -13.228   2.165  14.607  1.00 31.93           C  
ANISOU 9629  C   CYS B 504     3516   4354   4260     90    -17    146       C  
ATOM   9630  O   CYS B 504     -13.290   3.239  15.214  1.00 32.05           O  
ANISOU 9630  O   CYS B 504     3526   4376   4273     85    -11    136       O  
ATOM   9631  CB  CYS B 504     -13.855   3.304  12.460  1.00 32.76           C  
ANISOU 9631  CB  CYS B 504     3651   4420   4375     99    -32    135       C  
ATOM   9632  SG  CYS B 504     -13.563   3.595  10.699  1.00 34.17           S  
ANISOU 9632  SG  CYS B 504     3855   4573   4553    106    -40    134       S  
ATOM   9633  N   GLN B 505     -13.327   0.979  15.210  1.00 31.75           N  
ANISOU 9633  N   GLN B 505     3482   4342   4239     91    -17    156       N  
ATOM   9634  CA  GLN B 505     -13.409   0.832  16.670  1.00 31.48           C  
ANISOU 9634  CA  GLN B 505     3428   4329   4200     86     -8    158       C  
ATOM   9635  C   GLN B 505     -14.587   1.605  17.294  1.00 32.80           C  
ANISOU 9635  C   GLN B 505     3588   4496   4378     84     -7    149       C  
ATOM   9636  O   GLN B 505     -14.494   2.115  18.429  1.00 31.72           O  
ANISOU 9636  O   GLN B 505     3439   4377   4235     79      1    144       O  
ATOM   9637  CB  GLN B 505     -12.099   1.273  17.322  1.00 29.94           C  
ANISOU 9637  CB  GLN B 505     3230   4156   3989     80      2    156       C  
ATOM   9638  CG  GLN B 505     -10.860   0.518  16.888  1.00 29.49           C  
ANISOU 9638  CG  GLN B 505     3178   4103   3922     82      3    165       C  
ATOM   9639  CD  GLN B 505      -9.602   1.151  17.457  1.00 30.64           C  
ANISOU 9639  CD  GLN B 505     3320   4269   4052     75     13    161       C  
ATOM   9640  OE1 GLN B 505      -8.682   1.498  16.720  1.00 29.74           O  
ANISOU 9640  OE1 GLN B 505     3216   4149   3932     74     14    159       O  
ATOM   9641  NE2 GLN B 505      -9.568   1.325  18.780  1.00 31.44           N  
ANISOU 9641  NE2 GLN B 505     3405   4392   4147     69     20    159       N  
ATOM   9642  N   LEU B 506     -15.689   1.689  16.549  1.00 32.80           N  
ANISOU 9642  N   LEU B 506     3593   4475   4392     89    -17    146       N  
ATOM   9643  CA  LEU B 506     -16.841   2.473  16.976  1.00 33.38           C  
ANISOU 9643  CA  LEU B 506     3660   4545   4476     88    -17    138       C  
ATOM   9644  C   LEU B 506     -17.597   1.831  18.122  1.00 33.05           C  
ANISOU 9644  C   LEU B 506     3600   4515   4441     88    -12    143       C  
ATOM   9645  O   LEU B 506     -17.876   0.648  18.092  1.00 33.14           O  
ANISOU 9645  O   LEU B 506     3607   4525   4459     91    -16    154       O  
ATOM   9646  CB  LEU B 506     -17.775   2.745  15.796  1.00 33.91           C  
ANISOU 9646  CB  LEU B 506     3737   4587   4557     95    -30    135       C  
ATOM   9647  CG  LEU B 506     -17.262   3.756  14.758  1.00 33.91           C  
ANISOU 9647  CG  LEU B 506     3756   4575   4552     96    -32    127       C  
ATOM   9648  CD1 LEU B 506     -18.221   3.835  13.574  1.00 34.83           C  
ANISOU 9648  CD1 LEU B 506     3884   4668   4682    104    -46    125       C  
ATOM   9649  CD2 LEU B 506     -17.032   5.133  15.369  1.00 32.19           C  
ANISOU 9649  CD2 LEU B 506     3537   4365   4328     91    -21    115       C  
ATOM   9650  N   GLU B 507     -17.916   2.628  19.135  1.00 35.60           N  
ANISOU 9650  N   GLU B 507     3913   4849   4763     83     -4    136       N  
ATOM   9651  CA  GLU B 507     -18.614   2.146  20.332  1.00 37.24           C  
ANISOU 9651  CA  GLU B 507     4104   5070   4976     83      2    140       C  
ATOM   9652  C   GLU B 507     -19.971   2.814  20.552  1.00 38.93           C  
ANISOU 9652  C   GLU B 507     4312   5274   5204     84      1    134       C  
ATOM   9653  O   GLU B 507     -20.823   2.264  21.242  1.00 39.90           O  
ANISOU 9653  O   GLU B 507     4422   5401   5337     85      4    139       O  
ATOM   9654  CB  GLU B 507     -17.742   2.354  21.561  1.00 38.15           C  
ANISOU 9654  CB  GLU B 507     4210   5209   5073     77     15    139       C  
ATOM   9655  CG  GLU B 507     -16.794   1.207  21.847  1.00 40.13           C  
ANISOU 9655  CG  GLU B 507     4458   5476   5314     77     18    152       C  
ATOM   9656  CD  GLU B 507     -15.772   1.545  22.919  1.00 44.35           C  
ANISOU 9656  CD  GLU B 507     4985   6035   5829     71     29    149       C  
ATOM   9657  OE1 GLU B 507     -16.048   2.399  23.790  1.00 41.48           O  
ANISOU 9657  OE1 GLU B 507     4616   5681   5462     67     36    140       O  
ATOM   9658  OE2 GLU B 507     -14.672   0.948  22.888  1.00 52.84           O  
ANISOU 9658  OE2 GLU B 507     6062   7122   6892     71     30    156       O  
ATOM   9659  N   GLN B 508     -20.153   3.992  19.947  1.00 41.34           N  
ANISOU 9659  N   GLN B 508     4627   5567   5512     84      0    123       N  
ATOM   9660  CA  GLN B 508     -21.325   4.850  20.127  1.00 41.82           C  
ANISOU 9660  CA  GLN B 508     4683   5619   5585     86      0    115       C  
ATOM   9661  C   GLN B 508     -21.542   5.749  18.900  1.00 41.35           C  
ANISOU 9661  C   GLN B 508     4639   5539   5531     90     -8    108       C  
ATOM   9662  O   GLN B 508     -20.579   6.231  18.295  1.00 40.05           O  
ANISOU 9662  O   GLN B 508     4488   5373   5356     88     -8    104       O  
ATOM   9663  CB  GLN B 508     -21.163   5.720  21.381  1.00 44.34           C  
ANISOU 9663  CB  GLN B 508     4995   5955   5895     80     14    107       C  
ATOM   9664  CG  GLN B 508     -21.456   4.986  22.681  1.00 49.93           C  
ANISOU 9664  CG  GLN B 508     5686   6680   6602     78     23    114       C  
ATOM   9665  CD  GLN B 508     -21.174   5.821  23.921  1.00 56.01           C  
ANISOU 9665  CD  GLN B 508     6450   7468   7360     72     37    106       C  
ATOM   9666  OE1 GLN B 508     -20.130   6.477  24.023  1.00 55.15           O  
ANISOU 9666  OE1 GLN B 508     6348   7368   7236     67     42     98       O  
ATOM   9667  NE2 GLN B 508     -22.101   5.785  24.885  1.00 56.56           N  
ANISOU 9667  NE2 GLN B 508     6507   7543   7438     73     45    107       N  
ATOM   9668  N   ILE B 509     -22.809   5.972  18.546  1.00 39.86           N  
ANISOU 9668  N   ILE B 509     4447   5335   5359     95    -15    106       N  
ATOM   9669  CA  ILE B 509     -23.178   6.825  17.412  1.00 37.88           C  
ANISOU 9669  CA  ILE B 509     4210   5066   5115    101    -24    100       C  
ATOM   9670  C   ILE B 509     -23.949   8.037  17.923  1.00 37.34           C  
ANISOU 9670  C   ILE B 509     4138   4995   5053    101    -16     90       C  
ATOM   9671  O   ILE B 509     -24.897   7.883  18.676  1.00 39.32           O  
ANISOU 9671  O   ILE B 509     4374   5250   5315    102    -13     92       O  
ATOM   9672  CB  ILE B 509     -24.042   6.063  16.384  1.00 37.04           C  
ANISOU 9672  CB  ILE B 509     4106   4942   5024    108    -41    106       C  
ATOM   9673  CG1 ILE B 509     -23.350   4.766  15.952  1.00 36.33           C  
ANISOU 9673  CG1 ILE B 509     4020   4854   4929    108    -47    115       C  
ATOM   9674  CG2 ILE B 509     -24.356   6.949  15.183  1.00 37.33           C  
ANISOU 9674  CG2 ILE B 509     4157   4959   5064    115    -50    100       C  
ATOM   9675  CD1 ILE B 509     -23.988   4.064  14.767  1.00 35.93           C  
ANISOU 9675  CD1 ILE B 509     3975   4785   4890    114    -65    120       C  
ATOM   9676  N   SER B 510     -23.539   9.239  17.525  1.00 37.36           N  
ANISOU 9676  N   SER B 510     4153   4992   5049    101    -12     81       N  
ATOM   9677  CA  SER B 510     -24.168  10.470  18.013  1.00 36.97           C  
ANISOU 9677  CA  SER B 510     4101   4940   5004    101     -3     72       C  
ATOM   9678  C   SER B 510     -25.517  10.735  17.379  1.00 37.66           C  
ANISOU 9678  C   SER B 510     4188   5010   5111    110    -12     72       C  
ATOM   9679  O   SER B 510     -25.740  10.406  16.219  1.00 38.83           O  
ANISOU 9679  O   SER B 510     4344   5143   5264    117    -27     76       O  
ATOM   9680  CB  SER B 510     -23.266  11.669  17.770  1.00 36.04           C  
ANISOU 9680  CB  SER B 510     3998   4820   4874     98      5     62       C  
ATOM   9681  OG  SER B 510     -22.342  11.795  18.818  1.00 37.27           O  
ANISOU 9681  OG  SER B 510     4149   4995   5015     88     18     58       O  
ATOM   9682  N   TRP B 511     -26.406  11.362  18.139  1.00 38.32           N  
ANISOU 9682  N   TRP B 511     4261   5094   5202    111     -4     68       N  
ATOM   9683  CA  TRP B 511     -27.753  11.641  17.661  1.00 38.91           C  
ANISOU 9683  CA  TRP B 511     4332   5154   5297    120    -12     69       C  
ATOM   9684  C   TRP B 511     -27.694  12.617  16.524  1.00 37.67           C  
ANISOU 9684  C   TRP B 511     4192   4980   5139    127    -17     63       C  
ATOM   9685  O   TRP B 511     -27.092  13.677  16.654  1.00 39.18           O  
ANISOU 9685  O   TRP B 511     4394   5172   5320    124     -6     55       O  
ATOM   9686  CB  TRP B 511     -28.625  12.156  18.808  1.00 41.56           C  
ANISOU 9686  CB  TRP B 511     4653   5495   5640    120      0     66       C  
ATOM   9687  CG  TRP B 511     -30.093  11.786  18.686  1.00 45.78           C  
ANISOU 9687  CG  TRP B 511     5174   6021   6197    127     -8     71       C  
ATOM   9688  CD1 TRP B 511     -30.665  10.503  18.707  1.00 45.72           C  
ANISOU 9688  CD1 TRP B 511     5154   6015   6201    128    -18     81       C  
ATOM   9689  CD2 TRP B 511     -31.233  12.708  18.529  1.00 46.05           C  
ANISOU 9689  CD2 TRP B 511     5206   6044   6247    135     -7     68       C  
ATOM   9690  NE1 TRP B 511     -32.036  10.572  18.579  1.00 47.03           N  
ANISOU 9690  NE1 TRP B 511     5308   6171   6387    135    -23     83       N  
ATOM   9691  CE2 TRP B 511     -32.440  11.865  18.465  1.00 47.97           C  
ANISOU 9691  CE2 TRP B 511     5433   6282   6510    140    -18     76       C  
ATOM   9692  CE3 TRP B 511     -31.369  14.089  18.443  1.00 48.92           C  
ANISOU 9692  CE3 TRP B 511     5578   6399   6609    139      1     59       C  
ATOM   9693  CZ2 TRP B 511     -33.713  12.413  18.315  1.00 53.79           C  
ANISOU 9693  CZ2 TRP B 511     6163   7009   7266    149    -20     75       C  
ATOM   9694  CZ3 TRP B 511     -32.661  14.634  18.296  1.00 54.88           C  
ANISOU 9694  CZ3 TRP B 511     6326   7143   7382    148      0     59       C  
ATOM   9695  CH2 TRP B 511     -33.805  13.815  18.233  1.00 54.82           C  
ANISOU 9695  CH2 TRP B 511     6303   7133   7394    153    -11     67       C  
ATOM   9696  N   GLY B 512     -28.273  12.248  15.385  1.00 35.77           N  
ANISOU 9696  N   GLY B 512     3956   4724   4908    135    -35     68       N  
ATOM   9697  CA  GLY B 512     -28.367  13.153  14.228  1.00 36.14           C  
ANISOU 9697  CA  GLY B 512     4019   4754   4956    144    -41     64       C  
ATOM   9698  C   GLY B 512     -27.355  12.940  13.106  1.00 36.39           C  
ANISOU 9698  C   GLY B 512     4070   4779   4975    145    -49     65       C  
ATOM   9699  O   GLY B 512     -27.437  13.577  12.050  1.00 35.97           O  
ANISOU 9699  O   GLY B 512     4032   4711   4922    153    -56     63       O  
ATOM   9700  N   VAL B 513     -26.420  12.025  13.334  1.00 35.06           N  
ANISOU 9700  N   VAL B 513     3902   4622   4797    138    -49     69       N  
ATOM   9701  CA  VAL B 513     -25.253  11.848  12.482  1.00 34.74           C  
ANISOU 9701  CA  VAL B 513     3878   4578   4742    137    -52     70       C  
ATOM   9702  C   VAL B 513     -25.579  11.567  11.015  1.00 33.75           C  
ANISOU 9702  C   VAL B 513     3766   4435   4621    147    -71     74       C  
ATOM   9703  O   VAL B 513     -24.876  12.030  10.134  1.00 34.60           O  
ANISOU 9703  O   VAL B 513     3892   4533   4719    150    -72     72       O  
ATOM   9704  CB  VAL B 513     -24.317  10.770  13.091  1.00 36.43           C  
ANISOU 9704  CB  VAL B 513     4087   4809   4946    128    -49     75       C  
ATOM   9705  CG1 VAL B 513     -23.433  10.122  12.043  1.00 37.43           C  
ANISOU 9705  CG1 VAL B 513     4228   4929   5063    129    -58     80       C  
ATOM   9706  CG2 VAL B 513     -23.464  11.381  14.192  1.00 34.55           C  
ANISOU 9706  CG2 VAL B 513     3845   4586   4695    118    -30     69       C  
ATOM   9707  N   PHE B 514     -26.648  10.827  10.751  1.00 33.98           N  
ANISOU 9707  N   PHE B 514     3787   4459   4665    152    -85     79       N  
ATOM   9708  CA  PHE B 514     -27.008  10.481   9.376  1.00 32.98           C  
ANISOU 9708  CA  PHE B 514     3672   4317   4542    162   -104     82       C  
ATOM   9709  C   PHE B 514     -28.190  11.288   8.803  1.00 33.75           C  
ANISOU 9709  C   PHE B 514     3769   4400   4652    173   -113     80       C  
ATOM   9710  O   PHE B 514     -28.547  11.108   7.633  1.00 34.48           O  
ANISOU 9710  O   PHE B 514     3872   4479   4747    182   -130     82       O  
ATOM   9711  CB  PHE B 514     -27.285   8.970   9.250  1.00 32.35           C  
ANISOU 9711  CB  PHE B 514     3583   4239   4468    160   -118     90       C  
ATOM   9712  CG  PHE B 514     -26.168   8.091   9.758  1.00 32.66           C  
ANISOU 9712  CG  PHE B 514     3621   4291   4495    151   -110     94       C  
ATOM   9713  CD1 PHE B 514     -26.370   7.253  10.854  1.00 31.65           C  
ANISOU 9713  CD1 PHE B 514     3474   4177   4373    144   -105     98       C  
ATOM   9714  CD2 PHE B 514     -24.912   8.100   9.146  1.00 31.74           C  
ANISOU 9714  CD2 PHE B 514     3523   4173   4363    150   -108     94       C  
ATOM   9715  CE1 PHE B 514     -25.348   6.448  11.326  1.00 31.23           C  
ANISOU 9715  CE1 PHE B 514     3420   4135   4308    137    -97    103       C  
ATOM   9716  CE2 PHE B 514     -23.889   7.297   9.617  1.00 31.05           C  
ANISOU 9716  CE2 PHE B 514     3433   4097   4264    142   -101     99       C  
ATOM   9717  CZ  PHE B 514     -24.106   6.470  10.710  1.00 31.47           C  
ANISOU 9717  CZ  PHE B 514     3467   4165   4323    136    -96    103       C  
ATOM   9718  N   ASP B 515     -28.774  12.175   9.612  1.00 33.46           N  
ANISOU 9718  N   ASP B 515     3722   4367   4622    173   -101     75       N  
ATOM   9719  CA  ASP B 515     -30.051  12.844   9.296  1.00 34.14           C  
ANISOU 9719  CA  ASP B 515     3804   4442   4723    183   -108     74       C  
ATOM   9720  C   ASP B 515     -30.112  13.554   7.948  1.00 34.24           C  
ANISOU 9720  C   ASP B 515     3836   4438   4733    195   -118     72       C  
ATOM   9721  O   ASP B 515     -31.195  13.868   7.445  1.00 36.28           O  
ANISOU 9721  O   ASP B 515     4092   4687   5004    205   -129     73       O  
ATOM   9722  CB  ASP B 515     -30.416  13.849  10.397  1.00 34.99           C  
ANISOU 9722  CB  ASP B 515     3902   4556   4836    180    -90     69       C  
ATOM   9723  CG  ASP B 515     -31.026  13.187  11.635  1.00 36.44           C  
ANISOU 9723  CG  ASP B 515     4062   4753   5030    174    -84     71       C  
ATOM   9724  OD1 ASP B 515     -31.256  11.952  11.632  1.00 35.56           O  
ANISOU 9724  OD1 ASP B 515     3941   4646   4925    171    -95     77       O  
ATOM   9725  OD2 ASP B 515     -31.277  13.915  12.624  1.00 36.87           O  
ANISOU 9725  OD2 ASP B 515     4107   4813   5086    171    -68     67       O  
ATOM   9726  N   THR B 516     -28.949  13.799   7.370  1.00 33.39           N  
ANISOU 9726  N   THR B 516     3749   4327   4609    194   -114     71       N  
ATOM   9727  CA  THR B 516     -28.832  14.566   6.149  1.00 33.04           C  
ANISOU 9727  CA  THR B 516     3727   4268   4560    205   -120     70       C  
ATOM   9728  C   THR B 516     -28.566  13.686   4.936  1.00 34.51           C  
ANISOU 9728  C   THR B 516     3926   4445   4740    210   -138     74       C  
ATOM   9729  O   THR B 516     -28.731  14.113   3.794  1.00 36.25           O  
ANISOU 9729  O   THR B 516     4163   4652   4959    222   -148     75       O  
ATOM   9730  CB  THR B 516     -27.735  15.616   6.331  1.00 32.35           C  
ANISOU 9730  CB  THR B 516     3653   4179   4458    201   -100     64       C  
ATOM   9731  OG1 THR B 516     -28.306  16.754   6.983  1.00 31.62           O  
ANISOU 9731  OG1 THR B 516     3554   4086   4373    203    -86     58       O  
ATOM   9732  CG2 THR B 516     -27.139  16.033   5.022  1.00 32.67           C  
ANISOU 9732  CG2 THR B 516     3718   4205   4488    210   -104     64       C  
ATOM   9733  N   LEU B 517     -28.184  12.444   5.190  1.00 36.21           N  
ANISOU 9733  N   LEU B 517     4133   4669   4953    202   -143     78       N  
ATOM   9734  CA  LEU B 517     -27.739  11.547   4.133  1.00 38.05           C  
ANISOU 9734  CA  LEU B 517     4381   4896   5180    205   -158     83       C  
ATOM   9735  C   LEU B 517     -28.911  10.921   3.350  1.00 39.53           C  
ANISOU 9735  C   LEU B 517     4564   5074   5379    214   -182     86       C  
ATOM   9736  O   LEU B 517     -29.150   9.712   3.401  1.00 39.37           O  
ANISOU 9736  O   LEU B 517     4535   5057   5364    210   -193     89       O  
ATOM   9737  CB  LEU B 517     -26.773  10.506   4.715  1.00 37.25           C  
ANISOU 9737  CB  LEU B 517     4276   4807   5070    193   -152     86       C  
ATOM   9738  CG  LEU B 517     -25.553  11.093   5.452  1.00 36.40           C  
ANISOU 9738  CG  LEU B 517     4171   4708   4949    184   -130     83       C  
ATOM   9739  CD1 LEU B 517     -24.571  10.010   5.889  1.00 34.01           C  
ANISOU 9739  CD1 LEU B 517     3865   4417   4637    174   -125     87       C  
ATOM   9740  CD2 LEU B 517     -24.845  12.152   4.616  1.00 36.08           C  
ANISOU 9740  CD2 LEU B 517     4154   4657   4897    190   -124     79       C  
ATOM   9741  N   HIS B 518     -29.618  11.765   2.605  1.00 41.45           N  
ANISOU 9741  N   HIS B 518     4816   5306   5627    226   -190     84       N  
ATOM   9742  CA  HIS B 518     -30.861  11.362   1.942  1.00 44.56           C  
ANISOU 9742  CA  HIS B 518     5203   5693   6034    235   -213     86       C  
ATOM   9743  C   HIS B 518     -30.663  10.488   0.736  1.00 41.86           C  
ANISOU 9743  C   HIS B 518     4876   5342   5685    240   -232     88       C  
ATOM   9744  O   HIS B 518     -31.565   9.744   0.346  1.00 39.56           O  
ANISOU 9744  O   HIS B 518     4577   5049   5405    242   -252     90       O  
ATOM   9745  CB  HIS B 518     -31.728  12.581   1.621  1.00 50.25           C  
ANISOU 9745  CB  HIS B 518     5924   6404   6761    248   -214     83       C  
ATOM   9746  CG  HIS B 518     -32.339  13.226   2.853  1.00 59.39           C  
ANISOU 9746  CG  HIS B 518     7062   7571   7931    244   -199     81       C  
ATOM   9747  ND1 HIS B 518     -32.243  14.550   3.108  1.00 64.16           N  
ANISOU 9747  ND1 HIS B 518     7672   8172   8533    248   -183     78       N  
ATOM   9748  CD2 HIS B 518     -33.048  12.669   3.924  1.00 60.62           C  
ANISOU 9748  CD2 HIS B 518     7192   7737   8102    236   -197     82       C  
ATOM   9749  CE1 HIS B 518     -32.868  14.829   4.274  1.00 65.27           C  
ANISOU 9749  CE1 HIS B 518     7792   8321   8686    243   -172     76       C  
ATOM   9750  NE2 HIS B 518     -33.358  13.676   4.772  1.00 64.35           N  
ANISOU 9750  NE2 HIS B 518     7656   8213   8580    236   -180     79       N  
ATOM   9751  N   ARG B 519     -29.471  10.546   0.153  1.00 39.80           N  
ANISOU 9751  N   ARG B 519     4637   5077   5406    240   -227     88       N  
ATOM   9752  CA  ARG B 519     -29.188   9.778  -1.049  1.00 39.67           C  
ANISOU 9752  CA  ARG B 519     4638   5051   5381    245   -243     91       C  
ATOM   9753  C   ARG B 519     -28.419   8.480  -0.775  1.00 38.75           C  
ANISOU 9753  C   ARG B 519     4521   4942   5260    234   -242     94       C  
ATOM   9754  O   ARG B 519     -28.143   7.723  -1.705  1.00 38.54           O  
ANISOU 9754  O   ARG B 519     4508   4908   5227    237   -255     96       O  
ATOM   9755  CB  ARG B 519     -28.457  10.644  -2.077  1.00 40.66           C  
ANISOU 9755  CB  ARG B 519     4792   5165   5491    255   -240     90       C  
ATOM   9756  CG  ARG B 519     -29.342  11.648  -2.799  1.00 43.38           C  
ANISOU 9756  CG  ARG B 519     5143   5499   5839    271   -250     88       C  
ATOM   9757  CD  ARG B 519     -28.575  12.384  -3.889  1.00 45.83           C  
ANISOU 9757  CD  ARG B 519     5483   5796   6132    281   -246     89       C  
ATOM   9758  NE  ARG B 519     -28.101  11.452  -4.914  1.00 50.31           N  
ANISOU 9758  NE  ARG B 519     6068   6358   6690    284   -260     91       N  
ATOM   9759  CZ  ARG B 519     -27.045  11.641  -5.706  1.00 49.08           C  
ANISOU 9759  CZ  ARG B 519     5938   6193   6516    289   -255     93       C  
ATOM   9760  NH1 ARG B 519     -26.736  10.697  -6.583  1.00 49.37           N  
ANISOU 9760  NH1 ARG B 519     5989   6224   6544    291   -268     95       N  
ATOM   9761  NH2 ARG B 519     -26.299  12.747  -5.633  1.00 45.06           N  
ANISOU 9761  NH2 ARG B 519     5440   5680   5998    290   -235     91       N  
ATOM   9762  N   LEU B 520     -28.108   8.215   0.496  1.00 38.36           N  
ANISOU 9762  N   LEU B 520     4453   4906   5213    222   -226     95       N  
ATOM   9763  CA  LEU B 520     -27.219   7.099   0.882  1.00 37.03           C  
ANISOU 9763  CA  LEU B 520     4283   4745   5038    211   -221     99       C  
ATOM   9764  C   LEU B 520     -27.814   5.706   0.645  1.00 36.27           C  
ANISOU 9764  C   LEU B 520     4179   4648   4952    209   -238    102       C  
ATOM   9765  O   LEU B 520     -28.938   5.441   1.049  1.00 37.29           O  
ANISOU 9765  O   LEU B 520     4289   4780   5098    208   -246    101       O  
ATOM   9766  CB  LEU B 520     -26.789   7.250   2.347  1.00 35.18           C  
ANISOU 9766  CB  LEU B 520     4032   4528   4806    199   -200     98       C  
ATOM   9767  CG  LEU B 520     -25.704   6.326   2.903  1.00 33.44           C  
ANISOU 9767  CG  LEU B 520     3810   4318   4576    189   -189    103       C  
ATOM   9768  CD1 LEU B 520     -24.319   6.659   2.352  1.00 32.11           C  
ANISOU 9768  CD1 LEU B 520     3663   4146   4389    190   -180    103       C  
ATOM   9769  CD2 LEU B 520     -25.723   6.417   4.420  1.00 32.94           C  
ANISOU 9769  CD2 LEU B 520     3724   4271   4518    179   -173    103       C  
ATOM   9770  N   GLN B 521     -27.037   4.826   0.011  1.00 35.09           N  
ANISOU 9770  N   GLN B 521     4044   4495   4792    208   -242    105       N  
ATOM   9771  CA  GLN B 521     -27.499   3.485  -0.383  1.00 33.45           C  
ANISOU 9771  CA  GLN B 521     3833   4284   4592    206   -259    107       C  
ATOM   9772  C   GLN B 521     -26.828   2.336   0.363  1.00 32.78           C  
ANISOU 9772  C   GLN B 521     3740   4208   4505    195   -249    112       C  
ATOM   9773  O   GLN B 521     -27.495   1.361   0.734  1.00 33.34           O  
ANISOU 9773  O   GLN B 521     3796   4283   4590    189   -256    114       O  
ATOM   9774  CB  GLN B 521     -27.280   3.271  -1.870  1.00 33.36           C  
ANISOU 9774  CB  GLN B 521     3847   4257   4569    215   -275    107       C  
ATOM   9775  CG  GLN B 521     -28.135   4.151  -2.744  1.00 34.45           C  
ANISOU 9775  CG  GLN B 521     3993   4385   4710    227   -290    102       C  
ATOM   9776  CD  GLN B 521     -27.940   3.861  -4.213  1.00 36.07           C  
ANISOU 9776  CD  GLN B 521     4224   4575   4904    237   -306    102       C  
ATOM   9777  OE1 GLN B 521     -28.088   4.749  -5.041  1.00 39.67           O  
ANISOU 9777  OE1 GLN B 521     4696   5023   5354    249   -312    100       O  
ATOM   9778  NE2 GLN B 521     -27.607   2.619  -4.549  1.00 36.52           N  
ANISOU 9778  NE2 GLN B 521     4286   4630   4958    233   -313    104       N  
ATOM   9779  N   LEU B 522     -25.510   2.424   0.541  1.00 31.48           N  
ANISOU 9779  N   LEU B 522     3586   4049   4325    191   -233    115       N  
ATOM   9780  CA  LEU B 522     -24.783   1.433   1.331  1.00 30.72           C  
ANISOU 9780  CA  LEU B 522     3481   3963   4226    182   -222    121       C  
ATOM   9781  C   LEU B 522     -24.110   2.100   2.524  1.00 29.86           C  
ANISOU 9781  C   LEU B 522     3362   3870   4112    175   -200    121       C  
ATOM   9782  O   LEU B 522     -23.495   3.149   2.391  1.00 30.70           O  
ANISOU 9782  O   LEU B 522     3479   3976   4209    178   -190    118       O  
ATOM   9783  CB  LEU B 522     -23.780   0.653   0.466  1.00 30.68           C  
ANISOU 9783  CB  LEU B 522     3497   3951   4207    183   -224    125       C  
ATOM   9784  CG  LEU B 522     -22.929  -0.461   1.106  1.00 31.19           C  
ANISOU 9784  CG  LEU B 522     3556   4026   4267    175   -212    132       C  
ATOM   9785  CD1 LEU B 522     -22.582  -1.559   0.117  1.00 30.78           C  
ANISOU 9785  CD1 LEU B 522     3521   3963   4210    178   -222    135       C  
ATOM   9786  CD2 LEU B 522     -21.657   0.086   1.737  1.00 30.88           C  
ANISOU 9786  CD2 LEU B 522     3518   3998   4214    171   -191    134       C  
ATOM   9787  N   LEU B 523     -24.253   1.496   3.694  1.00 29.14           N  
ANISOU 9787  N   LEU B 523     3250   3793   4029    166   -191    124       N  
ATOM   9788  CA  LEU B 523     -23.631   2.005   4.902  1.00 29.72           C  
ANISOU 9788  CA  LEU B 523     3312   3882   4096    160   -171    125       C  
ATOM   9789  C   LEU B 523     -22.969   0.840   5.620  1.00 30.43           C  
ANISOU 9789  C   LEU B 523     3394   3984   4183    152   -162    132       C  
ATOM   9790  O   LEU B 523     -23.656  -0.056   6.114  1.00 30.31           O  
ANISOU 9790  O   LEU B 523     3363   3971   4180    149   -166    136       O  
ATOM   9791  CB  LEU B 523     -24.654   2.729   5.792  1.00 29.05           C  
ANISOU 9791  CB  LEU B 523     3208   3803   4025    158   -168    120       C  
ATOM   9792  CG  LEU B 523     -24.291   3.126   7.231  1.00 29.79           C  
ANISOU 9792  CG  LEU B 523     3286   3914   4116    150   -148    120       C  
ATOM   9793  CD1 LEU B 523     -23.102   4.070   7.343  1.00 30.08           C  
ANISOU 9793  CD1 LEU B 523     3334   3957   4137    148   -133    117       C  
ATOM   9794  CD2 LEU B 523     -25.495   3.754   7.902  1.00 30.40           C  
ANISOU 9794  CD2 LEU B 523     3346   3994   4208    150   -147    116       C  
ATOM   9795  N   ASN B 524     -21.632   0.833   5.626  1.00 32.06           N  
ANISOU 9795  N   ASN B 524     3611   4196   4374    150   -151    135       N  
ATOM   9796  CA  ASN B 524     -20.866  -0.240   6.264  1.00 32.15           C  
ANISOU 9796  CA  ASN B 524     3615   4219   4380    144   -142    143       C  
ATOM   9797  C   ASN B 524     -20.341   0.174   7.628  1.00 31.54           C  
ANISOU 9797  C   ASN B 524     3523   4162   4298    137   -123    144       C  
ATOM   9798  O   ASN B 524     -19.553   1.110   7.761  1.00 30.87           O  
ANISOU 9798  O   ASN B 524     3443   4082   4201    136   -113    140       O  
ATOM   9799  CB  ASN B 524     -19.722  -0.728   5.368  1.00 33.63           C  
ANISOU 9799  CB  ASN B 524     3823   4400   4554    147   -142    148       C  
ATOM   9800  CG  ASN B 524     -19.226  -2.122   5.746  1.00 36.16           C  
ANISOU 9800  CG  ASN B 524     4138   4727   4872    143   -137    157       C  
ATOM   9801  OD1 ASN B 524     -19.453  -2.599   6.861  1.00 35.48           O  
ANISOU 9801  OD1 ASN B 524     4032   4654   4792    137   -130    161       O  
ATOM   9802  ND2 ASN B 524     -18.539  -2.782   4.805  1.00 39.12           N  
ANISOU 9802  ND2 ASN B 524     4531   5093   5240    147   -141    162       N  
ATOM   9803  N   MET B 525     -20.804  -0.518   8.650  1.00 30.89           N  
ANISOU 9803  N   MET B 525     3421   4090   4223    132   -119    148       N  
ATOM   9804  CA  MET B 525     -20.295  -0.285   9.978  1.00 31.55           C  
ANISOU 9804  CA  MET B 525     3490   4194   4301    125   -103    149       C  
ATOM   9805  C   MET B 525     -19.887  -1.593  10.621  1.00 32.16           C  
ANISOU 9805  C   MET B 525     3559   4283   4377    122    -97    160       C  
ATOM   9806  O   MET B 525     -19.865  -1.717  11.847  1.00 33.24           O  
ANISOU 9806  O   MET B 525     3679   4436   4514    117    -85    162       O  
ATOM   9807  CB  MET B 525     -21.328   0.446  10.813  1.00 31.56           C  
ANISOU 9807  CB  MET B 525     3476   4200   4313    124   -100    144       C  
ATOM   9808  CG  MET B 525     -21.458   1.900  10.419  1.00 32.21           C  
ANISOU 9808  CG  MET B 525     3566   4275   4393    126   -100    134       C  
ATOM   9809  SD  MET B 525     -22.347   2.853  11.647  1.00 33.24           S  
ANISOU 9809  SD  MET B 525     3679   4416   4533    123    -91    127       S  
ATOM   9810  CE  MET B 525     -23.919   1.981  11.597  1.00 33.13           C  
ANISOU 9810  CE  MET B 525     3651   4393   4541    126   -104    131       C  
ATOM   9811  N   SER B 526     -19.551  -2.568   9.780  1.00 32.69           N  
ANISOU 9811  N   SER B 526     3637   4340   4442    125   -104    166       N  
ATOM   9812  CA  SER B 526     -19.136  -3.878  10.257  1.00 33.74           C  
ANISOU 9812  CA  SER B 526     3764   4481   4574    123    -98    176       C  
ATOM   9813  C   SER B 526     -17.809  -3.777  10.996  1.00 33.55           C  
ANISOU 9813  C   SER B 526     3737   4475   4533    119    -82    181       C  
ATOM   9814  O   SER B 526     -17.084  -2.795  10.843  1.00 32.46           O  
ANISOU 9814  O   SER B 526     3607   4341   4385    119    -77    175       O  
ATOM   9815  CB  SER B 526     -19.040  -4.877   9.101  1.00 33.64           C  
ANISOU 9815  CB  SER B 526     3766   4452   4563    127   -108    181       C  
ATOM   9816  OG  SER B 526     -18.143  -4.417   8.115  1.00 35.76           O  
ANISOU 9816  OG  SER B 526     4055   4713   4819    131   -110    179       O  
ATOM   9817  N   HIS B 527     -17.511  -4.784  11.813  1.00 33.47           N  
ANISOU 9817  N   HIS B 527     3716   4478   4522    117    -73    191       N  
ATOM   9818  CA  HIS B 527     -16.245  -4.851  12.535  1.00 33.56           C  
ANISOU 9818  CA  HIS B 527     3723   4508   4518    115    -59    196       C  
ATOM   9819  C   HIS B 527     -15.995  -3.626  13.365  1.00 34.01           C  
ANISOU 9819  C   HIS B 527     3772   4580   4567    110    -51    189       C  
ATOM   9820  O   HIS B 527     -14.901  -3.039  13.313  1.00 35.41           O  
ANISOU 9820  O   HIS B 527     3957   4766   4731    109    -44    187       O  
ATOM   9821  CB  HIS B 527     -15.073  -5.077  11.584  1.00 32.90           C  
ANISOU 9821  CB  HIS B 527     3658   4419   4422    118    -60    200       C  
ATOM   9822  CG  HIS B 527     -15.071  -6.427  10.926  1.00 33.55           C  
ANISOU 9822  CG  HIS B 527     3748   4490   4509    122    -65    209       C  
ATOM   9823  ND1 HIS B 527     -15.526  -6.622   9.672  1.00 34.38           N  
ANISOU 9823  ND1 HIS B 527     3869   4573   4620    126    -78    206       N  
ATOM   9824  CD2 HIS B 527     -14.628  -7.667  11.384  1.00 33.55           C  
ANISOU 9824  CD2 HIS B 527     3742   4498   4506    122    -57    222       C  
ATOM   9825  CE1 HIS B 527     -15.395  -7.927   9.344  1.00 34.48           C  
ANISOU 9825  CE1 HIS B 527     3886   4580   4635    128    -79    216       C  
ATOM   9826  NE2 HIS B 527     -14.844  -8.564  10.394  1.00 34.82           N  
ANISOU 9826  NE2 HIS B 527     3916   4640   4673    126    -66    225       N  
ATOM   9827  N   ASN B 528     -17.003  -3.222  14.129  1.00 31.56           N  
ANISOU 9827  N   ASN B 528     3449   4275   4267    108    -50    184       N  
ATOM   9828  CA  ASN B 528     -16.809  -2.232  15.174  1.00 31.75           C  
ANISOU 9828  CA  ASN B 528     3463   4316   4285    103    -39    178       C  
ATOM   9829  C   ASN B 528     -17.144  -2.830  16.546  1.00 32.34           C  
ANISOU 9829  C   ASN B 528     3517   4407   4361    100    -30    184       C  
ATOM   9830  O   ASN B 528     -17.310  -4.048  16.665  1.00 33.99           O  
ANISOU 9830  O   ASN B 528     3721   4616   4575    103    -30    194       O  
ATOM   9831  CB  ASN B 528     -17.620  -0.977  14.867  1.00 31.68           C  
ANISOU 9831  CB  ASN B 528     3457   4296   4283    103    -45    165       C  
ATOM   9832  CG  ASN B 528     -16.978  -0.121  13.790  1.00 31.49           C  
ANISOU 9832  CG  ASN B 528     3451   4261   4251    105    -49    158       C  
ATOM   9833  OD1 ASN B 528     -16.021   0.613  14.047  1.00 31.27           O  
ANISOU 9833  OD1 ASN B 528     3426   4243   4210    101    -40    154       O  
ATOM   9834  ND2 ASN B 528     -17.509  -0.201  12.582  1.00 31.31           N  
ANISOU 9834  ND2 ASN B 528     3441   4217   4236    110    -62    157       N  
ATOM   9835  N   ASN B 529     -17.227  -1.997  17.577  1.00 32.46           N  
ANISOU 9835  N   ASN B 529     3522   4437   4372     96    -21    178       N  
ATOM   9836  CA  ASN B 529     -17.577  -2.472  18.911  1.00 33.91           C  
ANISOU 9836  CA  ASN B 529     3687   4637   4556     94    -12    183       C  
ATOM   9837  C   ASN B 529     -18.926  -1.936  19.404  1.00 33.69           C  
ANISOU 9837  C   ASN B 529     3650   4606   4544     94    -12    177       C  
ATOM   9838  O   ASN B 529     -19.089  -1.637  20.593  1.00 34.00           O  
ANISOU 9838  O   ASN B 529     3677   4661   4580     91     -2    176       O  
ATOM   9839  CB  ASN B 529     -16.477  -2.134  19.924  1.00 35.89           C  
ANISOU 9839  CB  ASN B 529     3932   4913   4788     90      0    183       C  
ATOM   9840  CG  ASN B 529     -15.093  -2.552  19.457  1.00 39.98           C  
ANISOU 9840  CG  ASN B 529     4460   5437   5293     91      1    189       C  
ATOM   9841  OD1 ASN B 529     -14.898  -3.662  18.958  1.00 41.46           O  
ANISOU 9841  OD1 ASN B 529     4651   5618   5483     95     -1    200       O  
ATOM   9842  ND2 ASN B 529     -14.111  -1.656  19.628  1.00 41.45           N  
ANISOU 9842  ND2 ASN B 529     4648   5634   5464     86      6    183       N  
ATOM   9843  N   LEU B 530     -19.903  -1.824  18.510  1.00 32.40           N  
ANISOU 9843  N   LEU B 530     3491   4421   4395     97    -24    173       N  
ATOM   9844  CA  LEU B 530     -21.221  -1.353  18.936  1.00 33.00           C  
ANISOU 9844  CA  LEU B 530     3557   4493   4487     97    -24    168       C  
ATOM   9845  C   LEU B 530     -21.907  -2.413  19.812  1.00 34.03           C  
ANISOU 9845  C   LEU B 530     3671   4629   4627     97    -19    178       C  
ATOM   9846  O   LEU B 530     -21.869  -3.600  19.486  1.00 35.63           O  
ANISOU 9846  O   LEU B 530     3875   4827   4834     99    -22    187       O  
ATOM   9847  CB  LEU B 530     -22.087  -0.971  17.722  1.00 31.75           C  
ANISOU 9847  CB  LEU B 530     3408   4311   4343    101    -39    162       C  
ATOM   9848  CG  LEU B 530     -21.608   0.161  16.791  1.00 29.51           C  
ANISOU 9848  CG  LEU B 530     3141   4018   4051    102    -44    152       C  
ATOM   9849  CD1 LEU B 530     -22.490   0.231  15.556  1.00 28.67           C  
ANISOU 9849  CD1 LEU B 530     3043   3889   3959    107    -61    149       C  
ATOM   9850  CD2 LEU B 530     -21.553   1.508  17.488  1.00 27.72           C  
ANISOU 9850  CD2 LEU B 530     2912   3801   3819     99    -35    142       C  
ATOM   9851  N   LEU B 531     -22.496  -2.000  20.933  1.00 34.12           N  
ANISOU 9851  N   LEU B 531     3670   4652   4642     96     -9    175       N  
ATOM   9852  CA  LEU B 531     -23.183  -2.952  21.812  1.00 36.79           C  
ANISOU 9852  CA  LEU B 531     3992   4995   4989     96     -2    185       C  
ATOM   9853  C   LEU B 531     -24.666  -3.057  21.490  1.00 38.06           C  
ANISOU 9853  C   LEU B 531     4145   5139   5174     98    -10    183       C  
ATOM   9854  O   LEU B 531     -25.339  -4.018  21.879  1.00 38.08           O  
ANISOU 9854  O   LEU B 531     4138   5141   5191     99     -7    192       O  
ATOM   9855  CB  LEU B 531     -22.984  -2.605  23.294  1.00 38.25           C  
ANISOU 9855  CB  LEU B 531     4165   5202   5163     94     13    185       C  
ATOM   9856  CG  LEU B 531     -21.567  -2.725  23.891  1.00 41.30           C  
ANISOU 9856  CG  LEU B 531     4554   5610   5526     92     22    189       C  
ATOM   9857  CD1 LEU B 531     -21.617  -2.709  25.412  1.00 41.30           C  
ANISOU 9857  CD1 LEU B 531     4540   5631   5519     90     37    191       C  
ATOM   9858  CD2 LEU B 531     -20.792  -3.949  23.398  1.00 41.74           C  
ANISOU 9858  CD2 LEU B 531     4614   5665   5577     94     19    200       C  
ATOM   9859  N   PHE B 532     -25.167  -2.053  20.781  1.00 38.14           N  
ANISOU 9859  N   PHE B 532     4162   5137   5191     99    -19    173       N  
ATOM   9860  CA  PHE B 532     -26.549  -2.018  20.342  1.00 38.40           C  
ANISOU 9860  CA  PHE B 532     4189   5153   5247    102    -28    170       C  
ATOM   9861  C   PHE B 532     -26.709  -1.065  19.164  1.00 38.96           C  
ANISOU 9861  C   PHE B 532     4273   5208   5320    104    -42    161       C  
ATOM   9862  O   PHE B 532     -25.820  -0.270  18.864  1.00 40.11           O  
ANISOU 9862  O   PHE B 532     4432   5358   5451    104    -41    155       O  
ATOM   9863  CB  PHE B 532     -27.488  -1.636  21.498  1.00 37.61           C  
ANISOU 9863  CB  PHE B 532     4072   5060   5156    101    -17    169       C  
ATOM   9864  CG  PHE B 532     -27.268  -0.243  22.047  1.00 37.98           C  
ANISOU 9864  CG  PHE B 532     4121   5116   5192    100     -8    159       C  
ATOM   9865  CD1 PHE B 532     -27.791   0.881  21.389  1.00 36.13           C  
ANISOU 9865  CD1 PHE B 532     3892   4869   4964    102    -16    149       C  
ATOM   9866  CD2 PHE B 532     -26.566  -0.054  23.244  1.00 37.03           C  
ANISOU 9866  CD2 PHE B 532     3996   5016   5055     97      7    160       C  
ATOM   9867  CE1 PHE B 532     -27.596   2.155  21.899  1.00 35.65           C  
ANISOU 9867  CE1 PHE B 532     3834   4816   4895    101     -6    140       C  
ATOM   9868  CE2 PHE B 532     -26.372   1.223  23.760  1.00 36.24           C  
ANISOU 9868  CE2 PHE B 532     3898   4924   4946     95     15    150       C  
ATOM   9869  CZ  PHE B 532     -26.885   2.329  23.087  1.00 35.96           C  
ANISOU 9869  CZ  PHE B 532     3870   4876   4918     97      8    140       C  
ATOM   9870  N   LEU B 533     -27.841  -1.174  18.485  1.00 39.70           N  
ANISOU 9870  N   LEU B 533     4364   5286   5434    107    -54    159       N  
ATOM   9871  CA  LEU B 533     -28.228  -0.213  17.466  1.00 38.36           C  
ANISOU 9871  CA  LEU B 533     4205   5102   5268    111    -66    150       C  
ATOM   9872  C   LEU B 533     -29.382   0.591  17.999  1.00 37.57           C  
ANISOU 9872  C   LEU B 533     4092   5000   5182    113    -63    145       C  
ATOM   9873  O   LEU B 533     -30.105   0.140  18.880  1.00 36.43           O  
ANISOU 9873  O   LEU B 533     3930   4860   5049    112    -55    150       O  
ATOM   9874  CB  LEU B 533     -28.663  -0.918  16.183  1.00 37.28           C  
ANISOU 9874  CB  LEU B 533     4075   4947   5143    115    -85    152       C  
ATOM   9875  CG  LEU B 533     -27.596  -1.681  15.402  1.00 36.20           C  
ANISOU 9875  CG  LEU B 533     3953   4806   4993    114    -91    156       C  
ATOM   9876  CD1 LEU B 533     -28.218  -2.336  14.171  1.00 34.69           C  
ANISOU 9876  CD1 LEU B 533     3768   4597   4815    117   -110    156       C  
ATOM   9877  CD2 LEU B 533     -26.450  -0.754  15.018  1.00 35.59           C  
ANISOU 9877  CD2 LEU B 533     3893   4733   4896    115    -88    150       C  
ATOM   9878  N   ASP B 534     -29.542   1.793  17.469  1.00 38.88           N  
ANISOU 9878  N   ASP B 534     4266   5158   5346    116    -67    136       N  
ATOM   9879  CA  ASP B 534     -30.723   2.587  17.745  1.00 40.63           C  
ANISOU 9879  CA  ASP B 534     4477   5375   5584    120    -66    131       C  
ATOM   9880  C   ASP B 534     -31.332   2.988  16.414  1.00 40.33           C  
ANISOU 9880  C   ASP B 534     4447   5318   5555    126    -84    127       C  
ATOM   9881  O   ASP B 534     -30.714   3.719  15.631  1.00 39.66           O  
ANISOU 9881  O   ASP B 534     4380   5228   5459    129    -89    122       O  
ATOM   9882  CB  ASP B 534     -30.371   3.807  18.584  1.00 42.64           C  
ANISOU 9882  CB  ASP B 534     4732   5640   5827    118    -50    125       C  
ATOM   9883  CG  ASP B 534     -31.589   4.574  19.029  1.00 44.08           C  
ANISOU 9883  CG  ASP B 534     4902   5818   6025    121    -46    121       C  
ATOM   9884  OD1 ASP B 534     -31.447   5.433  19.925  1.00 47.19           O  
ANISOU 9884  OD1 ASP B 534     5294   6222   6411    119    -31    116       O  
ATOM   9885  OD2 ASP B 534     -32.686   4.325  18.485  1.00 43.60           O  
ANISOU 9885  OD2 ASP B 534     4835   5746   5984    126    -58    122       O  
ATOM   9886  N   SER B 535     -32.537   2.484  16.160  1.00 39.41           N  
ANISOU 9886  N   SER B 535     4319   5193   5461    129    -95    130       N  
ATOM   9887  CA  SER B 535     -33.182   2.625  14.856  1.00 38.85           C  
ANISOU 9887  CA  SER B 535     4254   5104   5400    135   -115    127       C  
ATOM   9888  C   SER B 535     -33.325   4.082  14.453  1.00 37.45           C  
ANISOU 9888  C   SER B 535     4087   4922   5220    141   -116    118       C  
ATOM   9889  O   SER B 535     -33.266   4.408  13.272  1.00 36.94           O  
ANISOU 9889  O   SER B 535     4036   4845   5152    147   -130    115       O  
ATOM   9890  CB  SER B 535     -34.560   1.989  14.878  1.00 39.12           C  
ANISOU 9890  CB  SER B 535     4271   5132   5460    136   -124    130       C  
ATOM   9891  OG  SER B 535     -34.715   1.208  16.038  1.00 42.93           O  
ANISOU 9891  OG  SER B 535     4737   5626   5949    130   -111    136       O  
ATOM   9892  N   SER B 536     -33.513   4.953  15.439  1.00 36.98           N  
ANISOU 9892  N   SER B 536     4020   4871   5160    140   -100    115       N  
ATOM   9893  CA  SER B 536     -33.713   6.367  15.174  1.00 37.65           C  
ANISOU 9893  CA  SER B 536     4111   4949   5242    146    -98    108       C  
ATOM   9894  C   SER B 536     -32.537   6.966  14.415  1.00 37.07           C  
ANISOU 9894  C   SER B 536     4061   4873   5148    147    -99    103       C  
ATOM   9895  O   SER B 536     -32.712   7.919  13.655  1.00 37.56           O  
ANISOU 9895  O   SER B 536     4135   4925   5211    154   -104     98       O  
ATOM   9896  CB  SER B 536     -34.026   7.154  16.456  1.00 38.56           C  
ANISOU 9896  CB  SER B 536     4215   5075   5360    144    -78    105       C  
ATOM   9897  OG  SER B 536     -33.358   6.629  17.584  1.00 39.06           O  
ANISOU 9897  OG  SER B 536     4272   5154   5413    136    -63    108       O  
ATOM   9898  N   HIS B 537     -31.355   6.380  14.589  1.00 36.07           N  
ANISOU 9898  N   HIS B 537     3942   4755   5006    141    -94    106       N  
ATOM   9899  CA  HIS B 537     -30.178   6.790  13.831  1.00 35.80           C  
ANISOU 9899  CA  HIS B 537     3930   4719   4954    141    -95    102       C  
ATOM   9900  C   HIS B 537     -30.363   6.674  12.339  1.00 35.52           C  
ANISOU 9900  C   HIS B 537     3908   4666   4920    149   -115    102       C  
ATOM   9901  O   HIS B 537     -29.599   7.259  11.575  1.00 37.71           O  
ANISOU 9901  O   HIS B 537     4204   4938   5185    151   -116     99       O  
ATOM   9902  CB  HIS B 537     -28.942   5.993  14.245  1.00 36.20           C  
ANISOU 9902  CB  HIS B 537     3984   4782   4988    133    -88    107       C  
ATOM   9903  CG  HIS B 537     -28.459   6.270  15.655  1.00 36.28           C  
ANISOU 9903  CG  HIS B 537     3985   4810   4989    126    -67    105       C  
ATOM   9904  ND1 HIS B 537     -27.869   5.320  16.422  1.00 35.50           N  
ANISOU 9904  ND1 HIS B 537     3878   4724   4883    120    -60    112       N  
ATOM   9905  CD2 HIS B 537     -28.483   7.430  16.420  1.00 34.79           C  
ANISOU 9905  CD2 HIS B 537     3794   4627   4797    125    -53     98       C  
ATOM   9906  CE1 HIS B 537     -27.539   5.847  17.609  1.00 34.05           C  
ANISOU 9906  CE1 HIS B 537     3688   4556   4691    115    -43    109       C  
ATOM   9907  NE2 HIS B 537     -27.918   7.137  17.611  1.00 34.94           N  
ANISOU 9907  NE2 HIS B 537     3804   4664   4807    117    -39    100       N  
ATOM   9908  N   TYR B 538     -31.378   5.940  11.897  1.00 34.85           N  
ANISOU 9908  N   TYR B 538     3814   4573   4853    152   -130    106       N  
ATOM   9909  CA  TYR B 538     -31.513   5.652  10.466  1.00 35.40           C  
ANISOU 9909  CA  TYR B 538     3897   4628   4924    159   -151    106       C  
ATOM   9910  C   TYR B 538     -32.820   6.145   9.819  1.00 35.07           C  
ANISOU 9910  C   TYR B 538     3851   4574   4899    168   -165    104       C  
ATOM   9911  O   TYR B 538     -33.041   5.914   8.636  1.00 34.30           O  
ANISOU 9911  O   TYR B 538     3764   4465   4803    174   -183    103       O  
ATOM   9912  CB  TYR B 538     -31.262   4.158  10.191  1.00 35.49           C  
ANISOU 9912  CB  TYR B 538     3908   4639   4936    154   -160    112       C  
ATOM   9913  CG  TYR B 538     -30.072   3.623  10.964  1.00 35.46           C  
ANISOU 9913  CG  TYR B 538     3906   4650   4918    146   -144    116       C  
ATOM   9914  CD1 TYR B 538     -30.231   3.129  12.261  1.00 34.74           C  
ANISOU 9914  CD1 TYR B 538     3796   4572   4831    139   -131    120       C  
ATOM   9915  CD2 TYR B 538     -28.788   3.644  10.414  1.00 34.91           C  
ANISOU 9915  CD2 TYR B 538     3855   4579   4828    145   -143    116       C  
ATOM   9916  CE1 TYR B 538     -29.156   2.667  12.981  1.00 35.20           C  
ANISOU 9916  CE1 TYR B 538     3854   4643   4875    133   -118    124       C  
ATOM   9917  CE2 TYR B 538     -27.699   3.181  11.129  1.00 34.68           C  
ANISOU 9917  CE2 TYR B 538     3826   4564   4786    138   -129    120       C  
ATOM   9918  CZ  TYR B 538     -27.892   2.698  12.411  1.00 35.62           C  
ANISOU 9918  CZ  TYR B 538     3926   4697   4910    132   -117    124       C  
ATOM   9919  OH  TYR B 538     -26.826   2.239  13.141  1.00 36.44           O  
ANISOU 9919  OH  TYR B 538     4030   4816   5000    126   -104    128       O  
ATOM   9920  N   ASN B 539     -33.660   6.855  10.569  1.00 34.71           N  
ANISOU 9920  N   ASN B 539     3790   4531   4864    169   -157    102       N  
ATOM   9921  CA  ASN B 539     -34.985   7.204  10.046  1.00 35.84           C  
ANISOU 9921  CA  ASN B 539     3926   4664   5026    178   -170    101       C  
ATOM   9922  C   ASN B 539     -34.978   8.035   8.771  1.00 35.95           C  
ANISOU 9922  C   ASN B 539     3959   4666   5035    189   -183     97       C  
ATOM   9923  O   ASN B 539     -35.911   7.933   7.977  1.00 36.64           O  
ANISOU 9923  O   ASN B 539     4043   4743   5134    196   -201     97       O  
ATOM   9924  CB  ASN B 539     -35.887   7.856  11.102  1.00 36.04           C  
ANISOU 9924  CB  ASN B 539     3932   4695   5065    178   -158    100       C  
ATOM   9925  CG  ASN B 539     -35.361   9.194  11.576  1.00 36.73           C  
ANISOU 9925  CG  ASN B 539     4027   4785   5140    180   -139     94       C  
ATOM   9926  OD1 ASN B 539     -34.404   9.259  12.349  1.00 37.18           O  
ANISOU 9926  OD1 ASN B 539     4088   4853   5183    172   -123     93       O  
ATOM   9927  ND2 ASN B 539     -35.992  10.270  11.126  1.00 35.89           N  
ANISOU 9927  ND2 ASN B 539     3925   4670   5040    189   -142     91       N  
ATOM   9928  N   GLN B 540     -33.937   8.837   8.562  1.00 35.06           N  
ANISOU 9928  N   GLN B 540     3865   4552   4903    190   -173     93       N  
ATOM   9929  CA  GLN B 540     -33.906   9.720   7.393  1.00 36.63           C  
ANISOU 9929  CA  GLN B 540     4083   4738   5095    201   -182     90       C  
ATOM   9930  C   GLN B 540     -33.261   9.055   6.185  1.00 36.32           C  
ANISOU 9930  C   GLN B 540     4062   4690   5045    203   -198     92       C  
ATOM   9931  O   GLN B 540     -33.023   9.702   5.164  1.00 36.42           O  
ANISOU 9931  O   GLN B 540     4095   4693   5049    212   -205     90       O  
ATOM   9932  CB  GLN B 540     -33.187  11.039   7.702  1.00 37.72           C  
ANISOU 9932  CB  GLN B 540     4233   4877   5221    202   -163     85       C  
ATOM   9933  CG  GLN B 540     -33.685  11.780   8.936  1.00 40.26           C  
ANISOU 9933  CG  GLN B 540     4539   5206   5550    199   -145     83       C  
ATOM   9934  CD  GLN B 540     -35.008  12.506   8.741  1.00 42.09           C  
ANISOU 9934  CD  GLN B 540     4762   5430   5799    210   -151     82       C  
ATOM   9935  OE1 GLN B 540     -35.451  12.758   7.621  1.00 43.05           O  
ANISOU 9935  OE1 GLN B 540     4893   5540   5923    221   -167     83       O  
ATOM   9936  NE2 GLN B 540     -35.636  12.859   9.846  1.00 44.61           N  
ANISOU 9936  NE2 GLN B 540     5063   5756   6129    207   -138     82       N  
ATOM   9937  N   LEU B 541     -32.980   7.765   6.299  1.00 36.70           N  
ANISOU 9937  N   LEU B 541     4107   4744   5094    195   -203     96       N  
ATOM   9938  CA  LEU B 541     -32.208   7.076   5.269  1.00 40.17           C  
ANISOU 9938  CA  LEU B 541     4564   5176   5520    196   -214     97       C  
ATOM   9939  C   LEU B 541     -33.082   6.400   4.202  1.00 42.19           C  
ANISOU 9939  C   LEU B 541     4822   5422   5787    202   -240     98       C  
ATOM   9940  O   LEU B 541     -33.036   5.186   4.030  1.00 44.53           O  
ANISOU 9940  O   LEU B 541     5116   5718   6086    197   -249    101       O  
ATOM   9941  CB  LEU B 541     -31.186   6.115   5.904  1.00 38.20           C  
ANISOU 9941  CB  LEU B 541     4314   4937   5261    185   -203    101       C  
ATOM   9942  CG  LEU B 541     -30.159   6.767   6.853  1.00 37.42           C  
ANISOU 9942  CG  LEU B 541     4217   4850   5149    178   -180     99       C  
ATOM   9943  CD1 LEU B 541     -29.214   5.757   7.489  1.00 37.33           C  
ANISOU 9943  CD1 LEU B 541     4203   4850   5129    168   -170    104       C  
ATOM   9944  CD2 LEU B 541     -29.358   7.854   6.159  1.00 36.91           C  
ANISOU 9944  CD2 LEU B 541     4174   4778   5069    184   -175     95       C  
ATOM   9945  N   TYR B 542     -33.841   7.212   3.467  1.00 43.18           N  
ANISOU 9945  N   TYR B 542     4951   5537   5917    214   -251     95       N  
ATOM   9946  CA  TYR B 542     -34.874   6.738   2.523  1.00 45.21           C  
ANISOU 9946  CA  TYR B 542     5205   5785   6186    221   -277     95       C  
ATOM   9947  C   TYR B 542     -34.378   5.903   1.338  1.00 44.89           C  
ANISOU 9947  C   TYR B 542     5184   5736   6135    223   -294     95       C  
ATOM   9948  O   TYR B 542     -35.176   5.216   0.695  1.00 46.48           O  
ANISOU 9948  O   TYR B 542     5381   5931   6346    225   -315     95       O  
ATOM   9949  CB  TYR B 542     -35.729   7.923   2.025  1.00 48.01           C  
ANISOU 9949  CB  TYR B 542     5561   6133   6547    234   -284     93       C  
ATOM   9950  CG  TYR B 542     -36.235   8.772   3.169  1.00 51.16           C  
ANISOU 9950  CG  TYR B 542     5942   6539   6956    233   -266     92       C  
ATOM   9951  CD1 TYR B 542     -35.785  10.081   3.350  1.00 52.00           C  
ANISOU 9951  CD1 TYR B 542     6059   6644   7053    238   -250     90       C  
ATOM   9952  CD2 TYR B 542     -37.127   8.241   4.110  1.00 53.04           C  
ANISOU 9952  CD2 TYR B 542     6153   6784   7213    226   -264     94       C  
ATOM   9953  CE1 TYR B 542     -36.231  10.846   4.424  1.00 53.77           C  
ANISOU 9953  CE1 TYR B 542     6268   6875   7287    236   -233     89       C  
ATOM   9954  CE2 TYR B 542     -37.576   8.994   5.183  1.00 54.23           C  
ANISOU 9954  CE2 TYR B 542     6288   6941   7373    225   -247     94       C  
ATOM   9955  CZ  TYR B 542     -37.128  10.293   5.336  1.00 54.68           C  
ANISOU 9955  CZ  TYR B 542     6356   6997   7420    230   -232     91       C  
ATOM   9956  OH  TYR B 542     -37.585  11.028   6.409  1.00 58.21           O  
ANISOU 9956  OH  TYR B 542     6789   7451   7876    229   -214     90       O  
ATOM   9957  N   SER B 543     -33.075   5.961   1.058  1.00 42.49           N  
ANISOU 9957  N   SER B 543     4902   5432   5811    221   -284     96       N  
ATOM   9958  CA  SER B 543     -32.489   5.284  -0.104  1.00 39.89           C  
ANISOU 9958  CA  SER B 543     4594   5094   5469    224   -298     97       C  
ATOM   9959  C   SER B 543     -31.641   4.075   0.285  1.00 39.24           C  
ANISOU 9959  C   SER B 543     4510   5016   5380    213   -291    100       C  
ATOM   9960  O   SER B 543     -31.132   3.362  -0.584  1.00 40.83           O  
ANISOU 9960  O   SER B 543     4729   5210   5572    214   -301    101       O  
ATOM   9961  CB  SER B 543     -31.625   6.255  -0.920  1.00 39.99           C  
ANISOU 9961  CB  SER B 543     4633   5098   5462    233   -293     95       C  
ATOM   9962  OG  SER B 543     -32.285   7.479  -1.186  1.00 39.06           O  
ANISOU 9962  OG  SER B 543     4516   4975   5348    244   -295     93       O  
ATOM   9963  N   LEU B 544     -31.489   3.849   1.585  1.00 38.14           N  
ANISOU 9963  N   LEU B 544     4354   4890   5247    202   -274    102       N  
ATOM   9964  CA  LEU B 544     -30.569   2.837   2.106  1.00 37.27           C  
ANISOU 9964  CA  LEU B 544     4243   4787   5130    192   -263    107       C  
ATOM   9965  C   LEU B 544     -30.980   1.424   1.738  1.00 37.15           C  
ANISOU 9965  C   LEU B 544     4223   4767   5123    188   -278    109       C  
ATOM   9966  O   LEU B 544     -31.909   0.881   2.326  1.00 38.08           O  
ANISOU 9966  O   LEU B 544     4320   4889   5260    184   -282    110       O  
ATOM   9967  CB  LEU B 544     -30.497   2.952   3.629  1.00 37.11           C  
ANISOU 9967  CB  LEU B 544     4201   4781   5114    183   -243    109       C  
ATOM   9968  CG  LEU B 544     -29.287   2.361   4.344  1.00 36.65           C  
ANISOU 9968  CG  LEU B 544     4144   4734   5044    174   -225    113       C  
ATOM   9969  CD1 LEU B 544     -28.121   3.330   4.224  1.00 35.94           C  
ANISOU 9969  CD1 LEU B 544     4072   4646   4935    176   -212    111       C  
ATOM   9970  CD2 LEU B 544     -29.610   2.087   5.805  1.00 35.26           C  
ANISOU 9970  CD2 LEU B 544     3944   4572   4879    166   -211    116       C  
ATOM   9971  N   SER B 545     -30.302   0.819   0.769  1.00 37.75           N  
ANISOU 9971  N   SER B 545     4320   4835   5187    190   -287    110       N  
ATOM   9972  CA  SER B 545     -30.586  -0.586   0.459  1.00 37.98           C  
ANISOU 9972  CA  SER B 545     4346   4859   5224    186   -299    111       C  
ATOM   9973  C   SER B 545     -29.698  -1.549   1.248  1.00 39.56           C  
ANISOU 9973  C   SER B 545     4542   5068   5419    176   -283    118       C  
ATOM   9974  O   SER B 545     -30.126  -2.666   1.553  1.00 40.60           O  
ANISOU 9974  O   SER B 545     4662   5200   5563    169   -286    120       O  
ATOM   9975  CB  SER B 545     -30.539  -0.876  -1.045  1.00 36.60           C  
ANISOU 9975  CB  SER B 545     4194   4670   5040    193   -319    109       C  
ATOM   9976  OG  SER B 545     -29.309  -0.492  -1.610  1.00 37.34           O  
ANISOU 9976  OG  SER B 545     4314   4761   5113    198   -311    110       O  
ATOM   9977  N   THR B 546     -28.481  -1.117   1.592  1.00 39.78           N  
ANISOU 9977  N   THR B 546     4580   5104   5431    175   -265    120       N  
ATOM   9978  CA  THR B 546     -27.549  -1.960   2.362  1.00 39.87           C  
ANISOU 9978  CA  THR B 546     4588   5125   5436    166   -249    127       C  
ATOM   9979  C   THR B 546     -27.063  -1.322   3.679  1.00 40.34           C  
ANISOU 9979  C   THR B 546     4635   5201   5492    161   -227    129       C  
ATOM   9980  O   THR B 546     -26.532  -0.203   3.684  1.00 39.57           O  
ANISOU 9980  O   THR B 546     4545   5105   5383    165   -218    126       O  
ATOM   9981  CB  THR B 546     -26.337  -2.391   1.509  1.00 38.77           C  
ANISOU 9981  CB  THR B 546     4473   4979   5278    169   -248    130       C  
ATOM   9982  OG1 THR B 546     -26.798  -3.065   0.334  1.00 37.67           O  
ANISOU 9982  OG1 THR B 546     4346   4824   5141    173   -268    128       O  
ATOM   9983  CG2 THR B 546     -25.424  -3.340   2.291  1.00 39.62           C  
ANISOU 9983  CG2 THR B 546     4575   5096   5379    161   -232    138       C  
ATOM   9984  N   LEU B 547     -27.268  -2.042   4.784  1.00 38.59           N  
ANISOU 9984  N   LEU B 547     4393   4990   5279    153   -217    134       N  
ATOM   9985  CA  LEU B 547     -26.739  -1.660   6.093  1.00 37.66           C  
ANISOU 9985  CA  LEU B 547     4262   4889   5157    148   -196    136       C  
ATOM   9986  C   LEU B 547     -25.967  -2.835   6.674  1.00 38.21           C  
ANISOU 9986  C   LEU B 547     4328   4966   5221    142   -185    145       C  
ATOM   9987  O   LEU B 547     -26.558  -3.846   7.040  1.00 38.80           O  
ANISOU 9987  O   LEU B 547     4390   5041   5309    138   -188    149       O  
ATOM   9988  CB  LEU B 547     -27.864  -1.240   7.050  1.00 37.17           C  
ANISOU 9988  CB  LEU B 547     4177   4833   5111    146   -193    134       C  
ATOM   9989  CG  LEU B 547     -27.521  -0.834   8.497  1.00 37.65           C  
ANISOU 9989  CG  LEU B 547     4223   4911   5169    140   -172    136       C  
ATOM   9990  CD1 LEU B 547     -26.431   0.229   8.580  1.00 35.20           C  
ANISOU 9990  CD1 LEU B 547     3925   4608   4840    141   -160    133       C  
ATOM   9991  CD2 LEU B 547     -28.761  -0.366   9.253  1.00 37.13           C  
ANISOU 9991  CD2 LEU B 547     4136   4849   5121    140   -170    134       C  
ATOM   9992  N   ASP B 548     -24.646  -2.699   6.757  1.00 37.77           N  
ANISOU 9992  N   ASP B 548     4284   4918   5147    141   -173    148       N  
ATOM   9993  CA  ASP B 548     -23.796  -3.762   7.264  1.00 36.07           C  
ANISOU 9993  CA  ASP B 548     4066   4711   4925    136   -163    156       C  
ATOM   9994  C   ASP B 548     -23.376  -3.474   8.693  1.00 36.81           C  
ANISOU 9994  C   ASP B 548     4144   4825   5014    131   -144    159       C  
ATOM   9995  O   ASP B 548     -22.557  -2.596   8.943  1.00 37.16           O  
ANISOU 9995  O   ASP B 548     4194   4878   5046    130   -134    157       O  
ATOM   9996  CB  ASP B 548     -22.568  -3.910   6.378  1.00 36.31           C  
ANISOU 9996  CB  ASP B 548     4119   4736   4938    139   -162    158       C  
ATOM   9997  CG  ASP B 548     -21.900  -5.266   6.522  1.00 37.52           C  
ANISOU 9997  CG  ASP B 548     4274   4893   5088    137   -157    168       C  
ATOM   9998  OD1 ASP B 548     -21.073  -5.593   5.648  1.00 37.98           O  
ANISOU 9998  OD1 ASP B 548     4351   4944   5135    140   -159    170       O  
ATOM   9999  OD2 ASP B 548     -22.197  -6.006   7.491  1.00 37.62           O  
ANISOU 9999  OD2 ASP B 548     4268   4914   5108    132   -149    174       O  
ATOM  10000  N   CYS B 549     -23.944  -4.217   9.631  1.00 38.23           N  
ANISOU10000  N   CYS B 549     4306   5013   5207    126   -138    164       N  
ATOM  10001  CA  CYS B 549     -23.622  -4.051  11.040  1.00 38.76           C  
ANISOU10001  CA  CYS B 549     4356   5099   5269    122   -121    167       C  
ATOM  10002  C   CYS B 549     -23.038  -5.318  11.646  1.00 39.31           C  
ANISOU10002  C   CYS B 549     4420   5178   5335    118   -111    178       C  
ATOM  10003  O   CYS B 549     -23.065  -5.503  12.867  1.00 39.81           O  
ANISOU10003  O   CYS B 549     4468   5257   5400    115    -98    183       O  
ATOM  10004  CB  CYS B 549     -24.869  -3.644  11.808  1.00 39.25           C  
ANISOU10004  CB  CYS B 549     4399   5164   5347    120   -120    164       C  
ATOM  10005  SG  CYS B 549     -25.174  -1.881  11.695  1.00 40.83           S  
ANISOU10005  SG  CYS B 549     4603   5363   5545    123   -121    153       S  
ATOM  10006  N   SER B 550     -22.511  -6.192  10.793  1.00 38.93           N  
ANISOU10006  N   SER B 550     4386   5120   5283    120   -117    183       N  
ATOM  10007  CA  SER B 550     -21.991  -7.471  11.255  1.00 38.87           C  
ANISOU10007  CA  SER B 550     4374   5119   5273    118   -108    194       C  
ATOM  10008  C   SER B 550     -20.691  -7.292  12.021  1.00 37.21           C  
ANISOU10008  C   SER B 550     4164   4929   5045    117    -91    199       C  
ATOM  10009  O   SER B 550     -20.039  -6.250  11.923  1.00 35.58           O  
ANISOU10009  O   SER B 550     3964   4727   4825    118    -89    194       O  
ATOM  10010  CB  SER B 550     -21.803  -8.434  10.084  1.00 40.15           C  
ANISOU10010  CB  SER B 550     4552   5265   5436    121   -118    197       C  
ATOM  10011  OG  SER B 550     -21.167  -7.776   9.009  1.00 43.20           O  
ANISOU10011  OG  SER B 550     4960   5643   5811    125   -125    192       O  
ATOM  10012  N   PHE B 551     -20.338  -8.310  12.798  1.00 36.28           N  
ANISOU10012  N   PHE B 551     4036   4821   4925    116    -80    210       N  
ATOM  10013  CA  PHE B 551     -19.087  -8.332  13.550  1.00 36.19           C  
ANISOU10013  CA  PHE B 551     4023   4829   4896    115    -65    217       C  
ATOM  10014  C   PHE B 551     -18.945  -7.151  14.481  1.00 35.87           C  
ANISOU10014  C   PHE B 551     3973   4806   4849    112    -57    211       C  
ATOM  10015  O   PHE B 551     -17.878  -6.552  14.595  1.00 37.66           O  
ANISOU10015  O   PHE B 551     4205   5043   5059    111    -50    210       O  
ATOM  10016  CB  PHE B 551     -17.878  -8.438  12.624  1.00 35.49           C  
ANISOU10016  CB  PHE B 551     3954   4736   4794    118    -67    219       C  
ATOM  10017  CG  PHE B 551     -17.742  -9.773  11.968  1.00 36.11           C  
ANISOU10017  CG  PHE B 551     4041   4803   4876    121    -70    228       C  
ATOM  10018  CD1 PHE B 551     -18.238  -9.988  10.691  1.00 37.45           C  
ANISOU10018  CD1 PHE B 551     4226   4950   5053    123    -85    223       C  
ATOM  10019  CD2 PHE B 551     -17.122 -10.827  12.631  1.00 36.48           C  
ANISOU10019  CD2 PHE B 551     4082   4861   4917    121    -58    240       C  
ATOM  10020  CE1 PHE B 551     -18.106 -11.235  10.078  1.00 38.23           C  
ANISOU10020  CE1 PHE B 551     4334   5037   5154    125    -88    230       C  
ATOM  10021  CE2 PHE B 551     -16.993 -12.070  12.029  1.00 36.14           C  
ANISOU10021  CE2 PHE B 551     4047   4805   4877    124    -59    248       C  
ATOM  10022  CZ  PHE B 551     -17.483 -12.274  10.749  1.00 36.12           C  
ANISOU10022  CZ  PHE B 551     4061   4780   4883    125    -74    243       C  
ATOM  10023  N   ASN B 552     -20.047  -6.811  15.126  1.00 35.55           N  
ANISOU10023  N   ASN B 552     3919   4767   4821    110    -57    207       N  
ATOM  10024  CA  ASN B 552     -20.031  -5.897  16.233  1.00 36.38           C  
ANISOU10024  CA  ASN B 552     4012   4888   4920    107    -47    202       C  
ATOM  10025  C   ASN B 552     -20.348  -6.748  17.450  1.00 39.63           C  
ANISOU10025  C   ASN B 552     4406   5313   5336    106    -35    212       C  
ATOM  10026  O   ASN B 552     -20.182  -7.965  17.414  1.00 42.01           O  
ANISOU10026  O   ASN B 552     4707   5613   5640    107    -34    222       O  
ATOM  10027  CB  ASN B 552     -21.061  -4.792  16.016  1.00 35.63           C  
ANISOU10027  CB  ASN B 552     3916   4785   4837    107    -54    191       C  
ATOM  10028  CG  ASN B 552     -20.529  -3.661  15.152  1.00 34.88           C  
ANISOU10028  CG  ASN B 552     3837   4683   4732    108    -60    181       C  
ATOM  10029  OD1 ASN B 552     -20.089  -2.630  15.669  1.00 35.77           O  
ANISOU10029  OD1 ASN B 552     3948   4807   4835    105    -52    175       O  
ATOM  10030  ND2 ASN B 552     -20.553  -3.848  13.839  1.00 33.15           N  
ANISOU10030  ND2 ASN B 552     3633   4445   4515    112    -73    180       N  
ATOM  10031  N   ARG B 553     -20.797  -6.126  18.527  1.00 43.19           N  
ANISOU10031  N   ARG B 553     4843   5777   5788    103    -27    208       N  
ATOM  10032  CA  ARG B 553     -21.192  -6.873  19.709  1.00 46.56           C  
ANISOU10032  CA  ARG B 553     5254   6216   6220    103    -16    217       C  
ATOM  10033  C   ARG B 553     -22.630  -6.481  20.078  1.00 45.81           C  
ANISOU10033  C   ARG B 553     5146   6114   6143    102    -18    212       C  
ATOM  10034  O   ARG B 553     -22.971  -6.337  21.258  1.00 44.13           O  
ANISOU10034  O   ARG B 553     4920   5915   5931    101     -6    213       O  
ATOM  10035  CB  ARG B 553     -20.196  -6.625  20.850  1.00 50.66           C  
ANISOU10035  CB  ARG B 553     5767   6761   6720    101     -1    221       C  
ATOM  10036  CG  ARG B 553     -18.836  -7.278  20.629  1.00 60.88           C  
ANISOU10036  CG  ARG B 553     7069   8063   7998    103      1    229       C  
ATOM  10037  CD  ARG B 553     -17.915  -7.165  21.850  1.00 70.91           C  
ANISOU10037  CD  ARG B 553     8331   9360   9249    102     15    234       C  
ATOM  10038  NE  ARG B 553     -16.868  -6.145  21.710  1.00 75.93           N  
ANISOU10038  NE  ARG B 553     8974  10005   9868     99     15    225       N  
ATOM  10039  CZ  ARG B 553     -15.816  -6.014  22.522  1.00 78.01           C  
ANISOU10039  CZ  ARG B 553     9234  10293  10114     98     25    228       C  
ATOM  10040  NH1 ARG B 553     -15.650  -6.835  23.552  1.00 78.53           N  
ANISOU10040  NH1 ARG B 553     9288  10375  10174    100     35    240       N  
ATOM  10041  NH2 ARG B 553     -14.916  -5.059  22.301  1.00 76.20           N  
ANISOU10041  NH2 ARG B 553     9011  10070   9871     94     24    220       N  
ATOM  10042  N   ILE B 554     -23.453  -6.311  19.037  1.00 44.45           N  
ANISOU10042  N   ILE B 554     4980   5921   5986    103    -32    206       N  
ATOM  10043  CA  ILE B 554     -24.842  -5.828  19.141  1.00 43.89           C  
ANISOU10043  CA  ILE B 554     4899   5841   5934    103    -37    199       C  
ATOM  10044  C   ILE B 554     -25.737  -6.794  19.925  1.00 44.42           C  
ANISOU10044  C   ILE B 554     4949   5909   6017    102    -30    208       C  
ATOM  10045  O   ILE B 554     -25.862  -7.972  19.570  1.00 43.32           O  
ANISOU10045  O   ILE B 554     4809   5761   5886    103    -33    216       O  
ATOM  10046  CB  ILE B 554     -25.437  -5.543  17.732  1.00 43.63           C  
ANISOU10046  CB  ILE B 554     4877   5786   5913    105    -55    192       C  
ATOM  10047  CG1 ILE B 554     -24.812  -4.271  17.134  1.00 43.77           C  
ANISOU10047  CG1 ILE B 554     4909   5804   5918    106    -60    182       C  
ATOM  10048  CG2 ILE B 554     -26.964  -5.444  17.764  1.00 43.63           C  
ANISOU10048  CG2 ILE B 554     4864   5776   5936    105    -62    188       C  
ATOM  10049  CD1 ILE B 554     -24.791  -4.231  15.617  1.00 42.30           C  
ANISOU10049  CD1 ILE B 554     4740   5598   5733    109    -77    178       C  
ATOM  10050  N   GLU B 555     -26.342  -6.281  20.996  1.00 44.59           N  
ANISOU10050  N   GLU B 555     4956   5941   6043    101    -20    206       N  
ATOM  10051  CA  GLU B 555     -27.245  -7.059  21.847  1.00 47.34           C  
ANISOU10051  CA  GLU B 555     5288   6291   6407    101    -11    214       C  
ATOM  10052  C   GLU B 555     -28.703  -6.970  21.373  1.00 47.55           C  
ANISOU10052  C   GLU B 555     5307   6300   6460    101    -21    209       C  
ATOM  10053  O   GLU B 555     -29.373  -7.996  21.216  1.00 48.79           O  
ANISOU10053  O   GLU B 555     5456   6446   6634    101    -24    215       O  
ATOM  10054  CB  GLU B 555     -27.127  -6.613  23.306  1.00 49.41           C  
ANISOU10054  CB  GLU B 555     5539   6573   6660    101      6    216       C  
ATOM  10055  CG  GLU B 555     -25.883  -7.116  24.026  1.00 49.29           C  
ANISOU10055  CG  GLU B 555     5526   6577   6623    101     18    224       C  
ATOM  10056  CD  GLU B 555     -25.649  -6.404  25.346  1.00 50.43           C  
ANISOU10056  CD  GLU B 555     5663   6744   6754    100     33    222       C  
ATOM  10057  OE1 GLU B 555     -26.484  -5.566  25.745  1.00 53.14           O  
ANISOU10057  OE1 GLU B 555     5998   7085   7105    100     36    215       O  
ATOM  10058  OE2 GLU B 555     -24.623  -6.673  25.992  1.00 52.23           O  
ANISOU10058  OE2 GLU B 555     5891   6989   6962    100     43    228       O  
ATOM  10059  N   THR B 556     -29.194  -5.747  21.171  1.00 45.64           N  
ANISOU10059  N   THR B 556     5065   6054   6220    102    -27    198       N  
ATOM  10060  CA  THR B 556     -30.441  -5.528  20.442  1.00 45.83           C  
ANISOU10060  CA  THR B 556     5084   6060   6267    103    -40    193       C  
ATOM  10061  C   THR B 556     -30.422  -4.249  19.656  1.00 43.86           C  
ANISOU10061  C   THR B 556     4846   5804   6013    105    -51    181       C  
ATOM  10062  O   THR B 556     -29.371  -3.661  19.401  1.00 43.08           O  
ANISOU10062  O   THR B 556     4761   5711   5894    105    -50    177       O  
ATOM  10063  CB  THR B 556     -31.677  -5.417  21.358  1.00 49.20           C  
ANISOU10063  CB  THR B 556     5492   6489   6713    103    -32    194       C  
ATOM  10064  OG1 THR B 556     -31.378  -4.583  22.487  1.00 49.65           O  
ANISOU10064  OG1 THR B 556     5544   6563   6757    103    -16    192       O  
ATOM  10065  CG2 THR B 556     -32.134  -6.777  21.807  1.00 52.06           C  
ANISOU10065  CG2 THR B 556     5841   6848   7089    101    -26    205       C  
ATOM  10066  N   SER B 557     -31.627  -3.836  19.286  1.00 43.78           N  
ANISOU10066  N   SER B 557     4828   5781   6022    107    -60    176       N  
ATOM  10067  CA  SER B 557     -31.879  -2.546  18.710  1.00 42.52           C  
ANISOU10067  CA  SER B 557     4676   5616   5862    110    -68    166       C  
ATOM  10068  C   SER B 557     -32.895  -1.833  19.576  1.00 41.48           C  
ANISOU10068  C   SER B 557     4529   5488   5743    111    -59    163       C  
ATOM  10069  O   SER B 557     -34.001  -2.326  19.762  1.00 43.06           O  
ANISOU10069  O   SER B 557     4714   5682   5965    112    -61    166       O  
ATOM  10070  CB  SER B 557     -32.410  -2.701  17.296  1.00 41.61           C  
ANISOU10070  CB  SER B 557     4568   5481   5758    113    -90    162       C  
ATOM  10071  OG  SER B 557     -32.668  -1.431  16.744  1.00 44.67           O  
ANISOU10071  OG  SER B 557     4962   5863   6145    118    -97    153       O  
ATOM  10072  N   LYS B 558     -32.490  -0.694  20.136  1.00 41.34           N  
ANISOU10072  N   LYS B 558     4514   5480   5712    112    -48    157       N  
ATOM  10073  CA  LYS B 558     -33.397   0.243  20.795  1.00 39.97           C  
ANISOU10073  CA  LYS B 558     4329   5307   5548    114    -40    153       C  
ATOM  10074  C   LYS B 558     -34.110   1.053  19.725  1.00 39.48           C  
ANISOU10074  C   LYS B 558     4272   5230   5498    119    -56    145       C  
ATOM  10075  O   LYS B 558     -33.793   0.927  18.539  1.00 39.05           O  
ANISOU10075  O   LYS B 558     4231   5165   5440    121    -72    143       O  
ATOM  10076  CB  LYS B 558     -32.624   1.222  21.678  1.00 39.52           C  
ANISOU10076  CB  LYS B 558     4277   5265   5471    112    -24    148       C  
ATOM  10077  CG  LYS B 558     -31.945   0.637  22.899  1.00 39.76           C  
ANISOU10077  CG  LYS B 558     4302   5315   5489    108     -7    155       C  
ATOM  10078  CD  LYS B 558     -31.108   1.728  23.548  1.00 41.05           C  
ANISOU10078  CD  LYS B 558     4473   5492   5631    106      4    147       C  
ATOM  10079  CE  LYS B 558     -29.964   1.167  24.377  1.00 41.60           C  
ANISOU10079  CE  LYS B 558     4544   5581   5680    102     16    153       C  
ATOM  10080  NZ  LYS B 558     -30.402   0.600  25.683  1.00 43.38           N  
ANISOU10080  NZ  LYS B 558     4754   5818   5910    102     31    160       N  
ATOM  10081  N   GLY B 559     -35.043   1.904  20.157  1.00 39.18           N  
ANISOU10081  N   GLY B 559     4224   5190   5471    122    -51    142       N  
ATOM  10082  CA  GLY B 559     -35.768   2.810  19.267  1.00 37.49           C  
ANISOU10082  CA  GLY B 559     4013   4962   5267    129    -63    135       C  
ATOM  10083  C   GLY B 559     -37.053   2.208  18.719  1.00 37.27           C  
ANISOU10083  C   GLY B 559     3972   4921   5266    131    -78    138       C  
ATOM  10084  O   GLY B 559     -37.402   1.081  19.057  1.00 38.89           O  
ANISOU10084  O   GLY B 559     4164   5127   5482    128    -77    145       O  
ATOM  10085  N   ILE B 560     -37.757   2.973  17.884  1.00 35.41           N  
ANISOU10085  N   ILE B 560     3739   4675   5041    138    -91    132       N  
ATOM  10086  CA  ILE B 560     -38.915   2.489  17.142  1.00 33.41           C  
ANISOU10086  CA  ILE B 560     3474   4408   4811    141   -109    134       C  
ATOM  10087  C   ILE B 560     -38.421   1.689  15.935  1.00 33.25           C  
ANISOU10087  C   ILE B 560     3468   4380   4786    140   -128    134       C  
ATOM  10088  O   ILE B 560     -37.855   2.249  14.992  1.00 32.90           O  
ANISOU10088  O   ILE B 560     3442   4330   4728    144   -138    129       O  
ATOM  10089  CB  ILE B 560     -39.802   3.664  16.651  1.00 33.59           C  
ANISOU10089  CB  ILE B 560     3495   4422   4844    149   -116    128       C  
ATOM  10090  CG1 ILE B 560     -40.298   4.551  17.819  1.00 33.14           C  
ANISOU10090  CG1 ILE B 560     3426   4372   4791    151    -96    127       C  
ATOM  10091  CG2 ILE B 560     -40.928   3.182  15.728  1.00 33.48           C  
ANISOU10091  CG2 ILE B 560     3471   4395   4853    153   -138    129       C  
ATOM  10092  CD1 ILE B 560     -41.225   3.895  18.822  1.00 32.93           C  
ANISOU10092  CD1 ILE B 560     3375   4350   4785    148    -85    134       C  
ATOM  10093  N   LEU B 561     -38.655   0.380  15.962  1.00 33.19           N  
ANISOU10093  N   LEU B 561     3451   4371   4789    135   -133    140       N  
ATOM  10094  CA  LEU B 561     -38.146  -0.538  14.936  1.00 33.27           C  
ANISOU10094  CA  LEU B 561     3473   4373   4793    133   -149    141       C  
ATOM  10095  C   LEU B 561     -38.636  -0.231  13.520  1.00 33.25           C  
ANISOU10095  C   LEU B 561     3479   4355   4796    139   -173    135       C  
ATOM  10096  O   LEU B 561     -38.110  -0.736  12.531  1.00 32.81           O  
ANISOU10096  O   LEU B 561     3439   4293   4733    139   -187    134       O  
ATOM  10097  CB  LEU B 561     -38.440  -1.982  15.349  1.00 33.77           C  
ANISOU10097  CB  LEU B 561     3523   4436   4870    126   -147    148       C  
ATOM  10098  CG  LEU B 561     -37.832  -2.324  16.726  1.00 35.64           C  
ANISOU10098  CG  LEU B 561     3754   4689   5098    121   -122    155       C  
ATOM  10099  CD1 LEU B 561     -38.305  -3.680  17.234  1.00 34.55           C  
ANISOU10099  CD1 LEU B 561     3600   4550   4976    115   -118    163       C  
ATOM  10100  CD2 LEU B 561     -36.300  -2.245  16.717  1.00 34.79           C  
ANISOU10100  CD2 LEU B 561     3666   4589   4961    120   -115    155       C  
ATOM  10101  N   GLN B 562     -39.634   0.633  13.440  1.00 36.16           N  
ANISOU10101  N   GLN B 562     3838   4720   5179    145   -177    132       N  
ATOM  10102  CA  GLN B 562     -40.226   1.028  12.178  1.00 37.08           C  
ANISOU10102  CA  GLN B 562     3961   4825   5303    152   -200    127       C  
ATOM  10103  C   GLN B 562     -39.457   2.190  11.552  1.00 36.33           C  
ANISOU10103  C   GLN B 562     3888   4727   5186    159   -201    121       C  
ATOM  10104  O   GLN B 562     -39.741   2.590  10.423  1.00 36.29           O  
ANISOU10104  O   GLN B 562     3893   4712   5181    166   -220    117       O  
ATOM  10105  CB  GLN B 562     -41.691   1.390  12.391  1.00 38.85           C  
ANISOU10105  CB  GLN B 562     4163   5045   5553    156   -204    126       C  
ATOM  10106  CG  GLN B 562     -42.581   1.075  11.195  1.00 43.44           C  
ANISOU10106  CG  GLN B 562     4741   5614   6149    160   -231    123       C  
ATOM  10107  CD  GLN B 562     -42.820  -0.407  10.999  1.00 43.86           C  
ANISOU10107  CD  GLN B 562     4787   5664   6215    152   -241    126       C  
ATOM  10108  OE1 GLN B 562     -42.810  -0.903   9.875  1.00 43.62           O  
ANISOU10108  OE1 GLN B 562     4765   5624   6183    152   -262    123       O  
ATOM  10109  NE2 GLN B 562     -43.038  -1.122  12.097  1.00 47.29           N  
ANISOU10109  NE2 GLN B 562     5203   6104   6660    144   -225    132       N  
ATOM  10110  N   HIS B 563     -38.477   2.714  12.287  1.00 35.32           N  
ANISOU10110  N   HIS B 563     3768   4609   5040    157   -182    121       N  
ATOM  10111  CA  HIS B 563     -37.553   3.716  11.760  1.00 35.67           C  
ANISOU10111  CA  HIS B 563     3836   4653   5063    162   -180    116       C  
ATOM  10112  C   HIS B 563     -36.528   3.159  10.808  1.00 35.35           C  
ANISOU10112  C   HIS B 563     3817   4608   5006    160   -190    116       C  
ATOM  10113  O   HIS B 563     -35.828   3.919  10.133  1.00 34.03           O  
ANISOU10113  O   HIS B 563     3670   4437   4823    165   -192    113       O  
ATOM  10114  CB  HIS B 563     -36.843   4.452  12.891  1.00 36.22           C  
ANISOU10114  CB  HIS B 563     3907   4735   5120    158   -156    116       C  
ATOM  10115  CG  HIS B 563     -37.671   5.537  13.522  1.00 37.03           C  
ANISOU10115  CG  HIS B 563     3998   4839   5233    163   -146    113       C  
ATOM  10116  ND1 HIS B 563     -37.496   5.928  14.796  1.00 36.88           N  
ANISOU10116  ND1 HIS B 563     3971   4831   5209    159   -124    113       N  
ATOM  10117  CD2 HIS B 563     -38.710   6.315  13.007  1.00 36.84           C  
ANISOU10117  CD2 HIS B 563     3969   4804   5221    172   -155    110       C  
ATOM  10118  CE1 HIS B 563     -38.374   6.907  15.084  1.00 37.04           C  
ANISOU10118  CE1 HIS B 563     3982   4848   5240    165   -119    110       C  
ATOM  10119  NE2 HIS B 563     -39.116   7.139  13.987  1.00 37.08           N  
ANISOU10119  NE2 HIS B 563     3989   4841   5257    173   -138    109       N  
ATOM  10120  N   PHE B 564     -36.406   1.833  10.761  1.00 36.56           N  
ANISOU10120  N   PHE B 564     3966   4761   5163    154   -195    121       N  
ATOM  10121  CA  PHE B 564     -35.509   1.198   9.803  1.00 37.87           C  
ANISOU10121  CA  PHE B 564     4152   4922   5315    154   -206    121       C  
ATOM  10122  C   PHE B 564     -36.072   1.397   8.390  1.00 38.19           C  
ANISOU10122  C   PHE B 564     4202   4947   5359    162   -230    117       C  
ATOM  10123  O   PHE B 564     -37.256   1.154   8.145  1.00 38.06           O  
ANISOU10123  O   PHE B 564     4171   4924   5363    164   -243    116       O  
ATOM  10124  CB  PHE B 564     -35.259  -0.285  10.135  1.00 37.73           C  
ANISOU10124  CB  PHE B 564     4128   4907   5300    145   -204    128       C  
ATOM  10125  CG  PHE B 564     -34.266  -0.505  11.247  1.00 37.34           C  
ANISOU10125  CG  PHE B 564     4077   4871   5237    139   -182    132       C  
ATOM  10126  CD1 PHE B 564     -34.655  -1.105  12.439  1.00 39.41           C  
ANISOU10126  CD1 PHE B 564     4319   5143   5510    133   -168    138       C  
ATOM  10127  CD2 PHE B 564     -32.941  -0.111  11.110  1.00 36.51           C  
ANISOU10127  CD2 PHE B 564     3991   4771   5108    139   -174    132       C  
ATOM  10128  CE1 PHE B 564     -33.735  -1.304  13.476  1.00 39.92           C  
ANISOU10128  CE1 PHE B 564     4383   5222   5562    128   -149    142       C  
ATOM  10129  CE2 PHE B 564     -32.024  -0.309  12.138  1.00 37.20           C  
ANISOU10129  CE2 PHE B 564     4077   4874   5184    133   -155    136       C  
ATOM  10130  CZ  PHE B 564     -32.419  -0.902  13.326  1.00 36.60           C  
ANISOU10130  CZ  PHE B 564     3981   4807   5117    128   -142    141       C  
ATOM  10131  N   PRO B 565     -35.227   1.880   7.469  1.00 39.53           N  
ANISOU10131  N   PRO B 565     4397   5112   5511    167   -235    114       N  
ATOM  10132  CA  PRO B 565     -35.660   2.286   6.135  1.00 41.38           C  
ANISOU10132  CA  PRO B 565     4643   5333   5746    176   -256    110       C  
ATOM  10133  C   PRO B 565     -36.429   1.205   5.397  1.00 43.76           C  
ANISOU10133  C   PRO B 565     4939   5625   6061    176   -278    110       C  
ATOM  10134  O   PRO B 565     -36.016   0.043   5.378  1.00 44.77           O  
ANISOU10134  O   PRO B 565     5069   5753   6187    168   -279    113       O  
ATOM  10135  CB  PRO B 565     -34.343   2.573   5.419  1.00 41.75           C  
ANISOU10135  CB  PRO B 565     4718   5377   5768    179   -254    109       C  
ATOM  10136  CG  PRO B 565     -33.419   2.983   6.515  1.00 40.78           C  
ANISOU10136  CG  PRO B 565     4594   5266   5633    173   -230    110       C  
ATOM  10137  CD  PRO B 565     -33.782   2.093   7.665  1.00 38.89           C  
ANISOU10137  CD  PRO B 565     4331   5036   5406    164   -220    115       C  
ATOM  10138  N   LYS B 566     -37.546   1.591   4.792  1.00 46.81           N  
ANISOU10138  N   LYS B 566     5319   6004   6461    183   -295    106       N  
ATOM  10139  CA  LYS B 566     -38.359   0.643   4.042  1.00 49.62           C  
ANISOU10139  CA  LYS B 566     5669   6351   6831    182   -318    105       C  
ATOM  10140  C   LYS B 566     -37.663   0.166   2.757  1.00 47.24           C  
ANISOU10140  C   LYS B 566     5393   6041   6513    185   -334    103       C  
ATOM  10141  O   LYS B 566     -38.077  -0.812   2.143  1.00 47.76           O  
ANISOU10141  O   LYS B 566     5458   6100   6587    182   -351    102       O  
ATOM  10142  CB  LYS B 566     -39.754   1.224   3.767  1.00 53.80           C  
ANISOU10142  CB  LYS B 566     6183   6877   7380    189   -333    102       C  
ATOM  10143  CG  LYS B 566     -40.689   1.128   4.968  1.00 57.02           C  
ANISOU10143  CG  LYS B 566     6561   7292   7810    184   -322    105       C  
ATOM  10144  CD  LYS B 566     -41.984   1.904   4.766  1.00 63.13           C  
ANISOU10144  CD  LYS B 566     7320   8063   8602    193   -333    103       C  
ATOM  10145  CE  LYS B 566     -43.025   1.143   3.946  1.00 64.21           C  
ANISOU10145  CE  LYS B 566     7447   8192   8757    193   -360    100       C  
ATOM  10146  NZ  LYS B 566     -44.289   1.926   3.828  1.00 61.39           N  
ANISOU10146  NZ  LYS B 566     7073   7834   8418    202   -370     99       N  
ATOM  10147  N   SER B 567     -36.590   0.854   2.379  1.00 45.63           N  
ANISOU10147  N   SER B 567     5212   5835   6286    190   -327    103       N  
ATOM  10148  CA  SER B 567     -35.812   0.518   1.189  1.00 43.34           C  
ANISOU10148  CA  SER B 567     4949   5537   5979    193   -338    101       C  
ATOM  10149  C   SER B 567     -34.762  -0.545   1.488  1.00 42.98           C  
ANISOU10149  C   SER B 567     4911   5495   5924    184   -327    105       C  
ATOM  10150  O   SER B 567     -34.084  -1.031   0.583  1.00 43.67           O  
ANISOU10150  O   SER B 567     5019   5574   5997    185   -335    105       O  
ATOM  10151  CB  SER B 567     -35.125   1.768   0.666  1.00 41.62           C  
ANISOU10151  CB  SER B 567     4753   5316   5742    203   -333     99       C  
ATOM  10152  OG  SER B 567     -34.475   2.427   1.736  1.00 41.94           O  
ANISOU10152  OG  SER B 567     4789   5367   5777    200   -308    102       O  
ATOM  10153  N   LEU B 568     -34.643  -0.908   2.758  1.00 42.33           N  
ANISOU10153  N   LEU B 568     4811   5423   5848    175   -309    110       N  
ATOM  10154  CA  LEU B 568     -33.630  -1.847   3.212  1.00 43.16           C  
ANISOU10154  CA  LEU B 568     4920   5533   5944    166   -296    115       C  
ATOM  10155  C   LEU B 568     -33.789  -3.227   2.574  1.00 43.18           C  
ANISOU10155  C   LEU B 568     4925   5527   5951    162   -310    115       C  
ATOM  10156  O   LEU B 568     -34.844  -3.845   2.687  1.00 45.73           O  
ANISOU10156  O   LEU B 568     5231   5847   6295    158   -320    114       O  
ATOM  10157  CB  LEU B 568     -33.685  -1.955   4.737  1.00 42.66           C  
ANISOU10157  CB  LEU B 568     4835   5484   5889    159   -275    119       C  
ATOM  10158  CG  LEU B 568     -32.402  -2.224   5.515  1.00 41.95           C  
ANISOU10158  CG  LEU B 568     4750   5405   5784    153   -253    125       C  
ATOM  10159  CD1 LEU B 568     -31.322  -1.199   5.208  1.00 40.05           C  
ANISOU10159  CD1 LEU B 568     4530   5166   5521    158   -245    123       C  
ATOM  10160  CD2 LEU B 568     -32.735  -2.221   6.996  1.00 41.71           C  
ANISOU10160  CD2 LEU B 568     4696   5388   5763    147   -235    129       C  
ATOM  10161  N   ALA B 569     -32.734  -3.697   1.907  1.00 42.25           N  
ANISOU10161  N   ALA B 569     4831   5405   5817    163   -310    117       N  
ATOM  10162  CA  ALA B 569     -32.737  -4.993   1.224  1.00 41.06           C  
ANISOU10162  CA  ALA B 569     4686   5244   5667    159   -323    117       C  
ATOM  10163  C   ALA B 569     -31.734  -5.968   1.829  1.00 42.22           C  
ANISOU10163  C   ALA B 569     4837   5398   5808    151   -306    124       C  
ATOM  10164  O   ALA B 569     -31.972  -7.177   1.854  1.00 43.52           O  
ANISOU10164  O   ALA B 569     4995   5557   5982    145   -309    126       O  
ATOM  10165  CB  ALA B 569     -32.463  -4.814  -0.260  1.00 38.97           C  
ANISOU10165  CB  ALA B 569     4449   4967   5389    167   -341    112       C  
ATOM  10166  N   PHE B 570     -30.605  -5.445   2.302  1.00 42.31           N  
ANISOU10166  N   PHE B 570     4856   5418   5802    152   -287    128       N  
ATOM  10167  CA  PHE B 570     -29.581  -6.275   2.936  1.00 41.60           C  
ANISOU10167  CA  PHE B 570     4767   5335   5703    146   -270    136       C  
ATOM  10168  C   PHE B 570     -29.098  -5.633   4.233  1.00 39.57           C  
ANISOU10168  C   PHE B 570     4497   5094   5441    143   -247    140       C  
ATOM  10169  O   PHE B 570     -28.236  -4.749   4.229  1.00 40.29           O  
ANISOU10169  O   PHE B 570     4600   5191   5517    147   -238    140       O  
ATOM  10170  CB  PHE B 570     -28.417  -6.571   1.974  1.00 44.60           C  
ANISOU10170  CB  PHE B 570     5174   5707   6062    150   -271    137       C  
ATOM  10171  CG  PHE B 570     -28.854  -7.092   0.630  1.00 47.15           C  
ANISOU10171  CG  PHE B 570     5512   6013   6387    153   -293    132       C  
ATOM  10172  CD1 PHE B 570     -29.009  -6.221  -0.454  1.00 48.83           C  
ANISOU10172  CD1 PHE B 570     5742   6218   6593    163   -308    126       C  
ATOM  10173  CD2 PHE B 570     -29.126  -8.442   0.444  1.00 47.50           C  
ANISOU10173  CD2 PHE B 570     5554   6050   6441    148   -300    134       C  
ATOM  10174  CE1 PHE B 570     -29.422  -6.692  -1.699  1.00 49.70           C  
ANISOU10174  CE1 PHE B 570     5866   6312   6703    166   -330    120       C  
ATOM  10175  CE2 PHE B 570     -29.534  -8.919  -0.796  1.00 48.02           C  
ANISOU10175  CE2 PHE B 570     5636   6102   6508    151   -321    128       C  
ATOM  10176  CZ  PHE B 570     -29.685  -8.045  -1.868  1.00 48.82           C  
ANISOU10176  CZ  PHE B 570     5752   6194   6600    160   -337    121       C  
ATOM  10177  N   PHE B 571     -29.712  -6.067   5.328  1.00 37.49           N  
ANISOU10177  N   PHE B 571     4210   4839   5193    137   -239    143       N  
ATOM  10178  CA  PHE B 571     -29.355  -5.667   6.678  1.00 36.84           C  
ANISOU10178  CA  PHE B 571     4114   4774   5108    134   -217    148       C  
ATOM  10179  C   PHE B 571     -28.557  -6.851   7.214  1.00 37.06           C  
ANISOU10179  C   PHE B 571     4142   4808   5131    128   -205    157       C  
ATOM  10180  O   PHE B 571     -29.109  -7.929   7.431  1.00 37.78           O  
ANISOU10180  O   PHE B 571     4221   4895   5236    124   -206    160       O  
ATOM  10181  CB  PHE B 571     -30.637  -5.473   7.505  1.00 36.19           C  
ANISOU10181  CB  PHE B 571     4006   4695   5047    131   -217    146       C  
ATOM  10182  CG  PHE B 571     -30.454  -4.708   8.797  1.00 34.21           C  
ANISOU10182  CG  PHE B 571     3742   4460   4793    129   -197    148       C  
ATOM  10183  CD1 PHE B 571     -29.190  -4.440   9.319  1.00 33.75           C  
ANISOU10183  CD1 PHE B 571     3692   4414   4715    128   -181    152       C  
ATOM  10184  CD2 PHE B 571     -31.570  -4.281   9.512  1.00 33.16           C  
ANISOU10184  CD2 PHE B 571     3589   4331   4678    129   -195    146       C  
ATOM  10185  CE1 PHE B 571     -29.049  -3.738  10.508  1.00 33.47           C  
ANISOU10185  CE1 PHE B 571     3645   4394   4677    126   -163    152       C  
ATOM  10186  CE2 PHE B 571     -31.438  -3.583  10.705  1.00 32.94           C  
ANISOU10186  CE2 PHE B 571     3550   4318   4647    127   -177    148       C  
ATOM  10187  CZ  PHE B 571     -30.176  -3.310  11.206  1.00 33.46           C  
ANISOU10187  CZ  PHE B 571     3624   4395   4692    126   -161    150       C  
ATOM  10188  N   ASN B 572     -27.253  -6.661   7.386  1.00 37.73           N  
ANISOU10188  N   ASN B 572     4237   4901   5195    129   -192    160       N  
ATOM  10189  CA  ASN B 572     -26.373  -7.732   7.834  1.00 38.50           C  
ANISOU10189  CA  ASN B 572     4336   5005   5286    125   -179    170       C  
ATOM  10190  C   ASN B 572     -26.126  -7.578   9.327  1.00 38.12           C  
ANISOU10190  C   ASN B 572     4270   4976   5236    121   -159    175       C  
ATOM  10191  O   ASN B 572     -25.502  -6.612   9.769  1.00 37.69           O  
ANISOU10191  O   ASN B 572     4217   4933   5169    122   -149    174       O  
ATOM  10192  CB  ASN B 572     -25.057  -7.746   7.026  1.00 41.53           C  
ANISOU10192  CB  ASN B 572     4744   5385   5649    129   -178    171       C  
ATOM  10193  CG  ASN B 572     -24.285  -9.064   7.159  1.00 44.86           C  
ANISOU10193  CG  ASN B 572     5170   5809   6066    126   -170    181       C  
ATOM  10194  OD1 ASN B 572     -24.418  -9.766   8.169  1.00 45.05           O  
ANISOU10194  OD1 ASN B 572     5177   5842   6096    122   -158    188       O  
ATOM  10195  ND2 ASN B 572     -23.479  -9.416   6.139  1.00 45.78           N  
ANISOU10195  ND2 ASN B 572     5307   5915   6169    130   -174    182       N  
ATOM  10196  N   LEU B 573     -26.656  -8.519  10.103  1.00 37.96           N  
ANISOU10196  N   LEU B 573     4233   4959   5229    117   -153    181       N  
ATOM  10197  CA  LEU B 573     -26.484  -8.504  11.548  1.00 37.72           C  
ANISOU10197  CA  LEU B 573     4186   4947   5197    113   -134    187       C  
ATOM  10198  C   LEU B 573     -25.801  -9.772  12.065  1.00 38.98           C  
ANISOU10198  C   LEU B 573     4343   5113   5352    111   -122    199       C  
ATOM  10199  O   LEU B 573     -25.769 -10.014  13.274  1.00 39.38           O  
ANISOU10199  O   LEU B 573     4379   5178   5405    109   -106    205       O  
ATOM  10200  CB  LEU B 573     -27.834  -8.306  12.243  1.00 38.28           C  
ANISOU10200  CB  LEU B 573     4235   5018   5289    111   -134    185       C  
ATOM  10201  CG  LEU B 573     -28.502  -6.932  12.364  1.00 36.55           C  
ANISOU10201  CG  LEU B 573     4011   4801   5074    113   -138    176       C  
ATOM  10202  CD1 LEU B 573     -29.780  -7.096  13.160  1.00 36.93           C  
ANISOU10202  CD1 LEU B 573     4036   4851   5144    111   -135    177       C  
ATOM  10203  CD2 LEU B 573     -27.608  -5.920  13.054  1.00 36.10           C  
ANISOU10203  CD2 LEU B 573     3956   4759   4998    114   -123    175       C  
ATOM  10204  N   THR B 574     -25.248 -10.572  11.149  1.00 39.87           N  
ANISOU10204  N   THR B 574     4472   5214   5460    112   -128    202       N  
ATOM  10205  CA  THR B 574     -24.530 -11.807  11.506  1.00 39.88           C  
ANISOU10205  CA  THR B 574     4474   5220   5457    111   -116    213       C  
ATOM  10206  C   THR B 574     -23.361 -11.531  12.445  1.00 39.46           C  
ANISOU10206  C   THR B 574     4419   5188   5385    112    -98    220       C  
ATOM  10207  O   THR B 574     -22.885 -10.398  12.521  1.00 39.19           O  
ANISOU10207  O   THR B 574     4388   5162   5338    113    -96    215       O  
ATOM  10208  CB  THR B 574     -23.961 -12.528  10.262  1.00 40.96           C  
ANISOU10208  CB  THR B 574     4632   5341   5587    113   -125    214       C  
ATOM  10209  OG1 THR B 574     -22.935 -11.727   9.655  1.00 42.68           O  
ANISOU10209  OG1 THR B 574     4868   5562   5786    118   -127    211       O  
ATOM  10210  CG2 THR B 574     -25.051 -12.835   9.244  1.00 41.24           C  
ANISOU10210  CG2 THR B 574     4671   5356   5639    113   -145    207       C  
ATOM  10211  N   ASN B 575     -22.889 -12.569  13.139  1.00 40.07           N  
ANISOU10211  N   ASN B 575     4491   5273   5460    111    -84    232       N  
ATOM  10212  CA  ASN B 575     -21.693 -12.470  13.993  1.00 39.61           C  
ANISOU10212  CA  ASN B 575     4430   5235   5382    112    -68    240       C  
ATOM  10213  C   ASN B 575     -21.772 -11.338  15.013  1.00 38.92           C  
ANISOU10213  C   ASN B 575     4330   5165   5290    111    -60    235       C  
ATOM  10214  O   ASN B 575     -20.773 -10.641  15.285  1.00 37.76           O  
ANISOU10214  O   ASN B 575     4187   5033   5125    112    -53    235       O  
ATOM  10215  CB  ASN B 575     -20.430 -12.305  13.142  1.00 40.33           C  
ANISOU10215  CB  ASN B 575     4542   5326   5456    116    -70    240       C  
ATOM  10216  CG  ASN B 575     -20.058 -13.565  12.405  1.00 43.23           C  
ANISOU10216  CG  ASN B 575     4921   5680   5823    118    -72    247       C  
ATOM  10217  OD1 ASN B 575     -19.353 -14.415  12.948  1.00 45.04           O  
ANISOU10217  OD1 ASN B 575     5148   5918   6046    119    -58    259       O  
ATOM  10218  ND2 ASN B 575     -20.507 -13.686  11.146  1.00 44.36           N  
ANISOU10218  ND2 ASN B 575     5078   5802   5973    119    -88    241       N  
ATOM  10219  N   ASN B 576     -22.968 -11.131  15.550  1.00 36.93           N  
ANISOU10219  N   ASN B 576     4064   4913   5055    109    -61    232       N  
ATOM  10220  CA  ASN B 576     -23.124 -10.203  16.654  1.00 36.49           C  
ANISOU10220  CA  ASN B 576     3995   4874   4996    107    -51    229       C  
ATOM  10221  C   ASN B 576     -23.252 -10.958  17.971  1.00 36.83           C  
ANISOU10221  C   ASN B 576     4021   4931   5041    106    -35    240       C  
ATOM  10222  O   ASN B 576     -22.673 -12.031  18.102  1.00 39.18           O  
ANISOU10222  O   ASN B 576     4321   5231   5335    108    -28    250       O  
ATOM  10223  CB  ASN B 576     -24.244  -9.210  16.375  1.00 33.93           C  
ANISOU10223  CB  ASN B 576     3666   4541   4684    106    -62    217       C  
ATOM  10224  CG  ASN B 576     -23.737  -7.991  15.636  1.00 32.51           C  
ANISOU10224  CG  ASN B 576     3501   4359   4493    108    -70    207       C  
ATOM  10225  OD1 ASN B 576     -23.185  -7.079  16.236  1.00 32.48           O  
ANISOU10225  OD1 ASN B 576     3495   4369   4476    107    -61    204       O  
ATOM  10226  ND2 ASN B 576     -23.899  -7.982  14.328  1.00 32.69           N  
ANISOU10226  ND2 ASN B 576     3538   4363   4519    110    -85    202       N  
ATOM  10227  N   SER B 577     -23.962 -10.423  18.951  1.00 37.43           N  
ANISOU10227  N   SER B 577     4082   5016   5124    105    -28    237       N  
ATOM  10228  CA  SER B 577     -24.151 -11.161  20.200  1.00 37.14           C  
ANISOU10228  CA  SER B 577     4029   4991   5089    105    -12    248       C  
ATOM  10229  C   SER B 577     -25.471 -10.777  20.863  1.00 36.97           C  
ANISOU10229  C   SER B 577     3991   4969   5086    103    -10    244       C  
ATOM  10230  O   SER B 577     -25.515 -10.037  21.854  1.00 34.34           O  
ANISOU10230  O   SER B 577     3650   4651   4747    103      0    242       O  
ATOM  10231  CB  SER B 577     -22.953 -10.985  21.131  1.00 35.87           C  
ANISOU10231  CB  SER B 577     3867   4854   4905    106      1    254       C  
ATOM  10232  OG  SER B 577     -22.876  -9.656  21.571  1.00 36.90           O  
ANISOU10232  OG  SER B 577     3995   4996   5026    105      3    244       O  
ATOM  10233  N   VAL B 578     -26.543 -11.297  20.269  1.00 38.58           N  
ANISOU10233  N   VAL B 578     4191   5153   5311    102    -20    243       N  
ATOM  10234  CA  VAL B 578     -27.911 -10.956  20.625  1.00 39.72           C  
ANISOU10234  CA  VAL B 578     4321   5293   5477    100    -21    238       C  
ATOM  10235  C   VAL B 578     -28.296 -11.521  21.986  1.00 42.00           C  
ANISOU10235  C   VAL B 578     4593   5593   5772    100     -3    248       C  
ATOM  10236  O   VAL B 578     -27.966 -12.669  22.310  1.00 44.25           O  
ANISOU10236  O   VAL B 578     4876   5880   6056    101      6    259       O  
ATOM  10237  CB  VAL B 578     -28.897 -11.465  19.555  1.00 39.05           C  
ANISOU10237  CB  VAL B 578     4236   5184   5414     99    -37    234       C  
ATOM  10238  CG1 VAL B 578     -30.346 -11.312  20.018  1.00 39.28           C  
ANISOU10238  CG1 VAL B 578     4247   5208   5468     97    -37    232       C  
ATOM  10239  CG2 VAL B 578     -28.661 -10.741  18.239  1.00 37.28           C  
ANISOU10239  CG2 VAL B 578     4029   4949   5185    100    -56    224       C  
ATOM  10240  N   ALA B 579     -28.990 -10.695  22.767  1.00 42.69           N  
ANISOU10240  N   ALA B 579     4668   5687   5864    100      3    243       N  
ATOM  10241  CA  ALA B 579     -29.534 -11.080  24.059  1.00 45.35           C  
ANISOU10241  CA  ALA B 579     4989   6034   6209    101     20    251       C  
ATOM  10242  C   ALA B 579     -30.997 -11.543  23.946  1.00 49.04           C  
ANISOU10242  C   ALA B 579     5442   6485   6706     99     17    252       C  
ATOM  10243  O   ALA B 579     -31.933 -10.728  23.908  1.00 48.29           O  
ANISOU10243  O   ALA B 579     5340   6385   6624     98     12    243       O  
ATOM  10244  CB  ALA B 579     -29.399  -9.932  25.054  1.00 46.54           C  
ANISOU10244  CB  ALA B 579     5134   6202   6345    102     31    247       C  
ATOM  10245  N   CYS B 580     -31.182 -12.860  23.899  1.00 49.70           N  
ANISOU10245  N   CYS B 580     5521   6560   6800     98     20    261       N  
ATOM  10246  CA  CYS B 580     -32.512 -13.457  23.826  1.00 51.54           C  
ANISOU10246  CA  CYS B 580     5740   6777   7063     95     18    262       C  
ATOM  10247  C   CYS B 580     -33.206 -13.502  25.189  1.00 50.67           C  
ANISOU10247  C   CYS B 580     5612   6677   6963     96     37    269       C  
ATOM  10248  O   CYS B 580     -33.540 -14.575  25.678  1.00 50.24           O  
ANISOU10248  O   CYS B 580     5548   6619   6920     95     49    279       O  
ATOM  10249  CB  CYS B 580     -32.426 -14.847  23.189  1.00 51.66           C  
ANISOU10249  CB  CYS B 580     5760   6779   7089     93     14    269       C  
ATOM  10250  SG  CYS B 580     -31.666 -14.777  21.551  1.00 58.17           S  
ANISOU10250  SG  CYS B 580     6607   7592   7902     92     -7    261       S  
ATOM  10251  N   ILE B 581     -33.401 -12.331  25.793  1.00 52.81           N  
ANISOU10251  N   ILE B 581     5878   6958   7227     98     42    263       N  
ATOM  10252  CA  ILE B 581     -34.178 -12.179  27.031  1.00 57.60           C  
ANISOU10252  CA  ILE B 581     6468   7573   7843     99     59    267       C  
ATOM  10253  C   ILE B 581     -35.561 -11.666  26.658  1.00 60.14           C  
ANISOU10253  C   ILE B 581     6777   7879   8191     97     50    259       C  
ATOM  10254  O   ILE B 581     -35.744 -11.153  25.553  1.00 58.94           O  
ANISOU10254  O   ILE B 581     6633   7717   8044     96     30    249       O  
ATOM  10255  CB  ILE B 581     -33.565 -11.117  27.974  1.00 59.97           C  
ANISOU10255  CB  ILE B 581     6770   7894   8119    102     71    265       C  
ATOM  10256  CG1 ILE B 581     -32.039 -11.096  27.887  1.00 58.03           C  
ANISOU10256  CG1 ILE B 581     6541   7662   7844    104     71    266       C  
ATOM  10257  CG2 ILE B 581     -34.063 -11.294  29.414  1.00 63.00           C  
ANISOU10257  CG2 ILE B 581     7140   8289   8507    105     93    273       C  
ATOM  10258  CD1 ILE B 581     -31.448  -9.756  28.269  1.00 57.20           C  
ANISOU10258  CD1 ILE B 581     6442   7573   7717    105     73    257       C  
ATOM  10259  N   CYS B 582     -36.521 -11.780  27.581  1.00 66.78           N  
ANISOU10259  N   CYS B 582     7601   8721   9049     98     64    264       N  
ATOM  10260  CA  CYS B 582     -37.844 -11.155  27.420  1.00 72.15           C  
ANISOU10260  CA  CYS B 582     8267   9390   9753     97     58    257       C  
ATOM  10261  C   CYS B 582     -37.751  -9.629  27.450  1.00 71.31           C  
ANISOU10261  C   CYS B 582     8166   9291   9634    100     55    246       C  
ATOM  10262  O   CYS B 582     -38.601  -8.936  26.881  1.00 67.31           O  
ANISOU10262  O   CYS B 582     7655   8774   9143    100     43    237       O  
ATOM  10263  CB  CYS B 582     -38.834 -11.651  28.479  1.00 80.15           C  
ANISOU10263  CB  CYS B 582     9261  10404  10787     98     77    266       C  
ATOM  10264  SG  CYS B 582     -39.574 -13.268  28.122  1.00 93.67           S  
ANISOU10264  SG  CYS B 582    10963  12098  12529     93     76    274       S  
ATOM  10265  N   GLU B 583     -36.711  -9.131  28.121  1.00 71.41           N  
ANISOU10265  N   GLU B 583     8189   9323   9619    102     65    246       N  
ATOM  10266  CA  GLU B 583     -36.315  -7.721  28.115  1.00 69.74           C  
ANISOU10266  CA  GLU B 583     7986   9120   9391    104     62    236       C  
ATOM  10267  C   GLU B 583     -36.287  -7.128  26.698  1.00 67.76           C  
ANISOU10267  C   GLU B 583     7747   8856   9142    103     39    225       C  
ATOM  10268  O   GLU B 583     -36.557  -5.943  26.511  1.00 69.16           O  
ANISOU10268  O   GLU B 583     7926   9033   9319    105     34    215       O  
ATOM  10269  CB  GLU B 583     -34.942  -7.592  28.792  1.00 77.95           C  
ANISOU10269  CB  GLU B 583     9038  10181  10399    105     73    238       C  
ATOM  10270  CG  GLU B 583     -34.208  -6.268  28.607  1.00 82.38           C  
ANISOU10270  CG  GLU B 583     9611  10749  10937    105     69    227       C  
ATOM  10271  CD  GLU B 583     -34.645  -5.185  29.577  1.00 88.44           C  
ANISOU10271  CD  GLU B 583    10373  11526  11703    107     82    222       C  
ATOM  10272  OE1 GLU B 583     -35.707  -5.335  30.223  1.00 92.33           O  
ANISOU10272  OE1 GLU B 583    10850  12016  12213    109     92    226       O  
ATOM  10273  OE2 GLU B 583     -33.917  -4.173  29.690  1.00 89.94           O  
ANISOU10273  OE2 GLU B 583    10573  11727  11872    107     82    213       O  
ATOM  10274  N   HIS B 584     -35.971  -7.961  25.708  1.00 62.92           N  
ANISOU10274  N   HIS B 584     7141   8233   8532    101     25    226       N  
ATOM  10275  CA  HIS B 584     -35.937  -7.536  24.310  1.00 58.06           C  
ANISOU10275  CA  HIS B 584     6537   7603   7918    100      2    217       C  
ATOM  10276  C   HIS B 584     -36.932  -8.282  23.460  1.00 58.21           C  
ANISOU10276  C   HIS B 584     6548   7603   7964     98    -11    217       C  
ATOM  10277  O   HIS B 584     -36.628  -8.637  22.318  1.00 56.09           O  
ANISOU10277  O   HIS B 584     6291   7324   7695     97    -28    214       O  
ATOM  10278  CB  HIS B 584     -34.543  -7.742  23.720  1.00 54.73           C  
ANISOU10278  CB  HIS B 584     6136   7187   7473    100     -2    217       C  
ATOM  10279  CG  HIS B 584     -33.415  -7.173  24.556  1.00 53.16           C  
ANISOU10279  CG  HIS B 584     5943   7007   7245    101     11    218       C  
ATOM  10280  ND1 HIS B 584     -33.465  -5.954  25.112  1.00 53.75           N  
ANISOU10280  ND1 HIS B 584     6017   7091   7312    103     17    211       N  
ATOM  10281  CD2 HIS B 584     -32.165  -7.697  24.875  1.00 52.62           C  
ANISOU10281  CD2 HIS B 584     5885   6953   7156    101     18    224       C  
ATOM  10282  CE1 HIS B 584     -32.320  -5.715  25.772  1.00 52.18           C  
ANISOU10282  CE1 HIS B 584     5827   6911   7088    102     28    212       C  
ATOM  10283  NE2 HIS B 584     -31.525  -6.784  25.624  1.00 52.34           N  
ANISOU10283  NE2 HIS B 584     5853   6934   7100    102     29    221       N  
ATOM  10284  N   GLN B 585     -38.131  -8.521  23.992  1.00 61.52           N  
ANISOU10284  N   GLN B 585     6948   8018   8408     98     -5    220       N  
ATOM  10285  CA  GLN B 585     -39.134  -9.327  23.287  1.00 60.83           C  
ANISOU10285  CA  GLN B 585     6851   7913   8348     94    -17    220       C  
ATOM  10286  C   GLN B 585     -39.505  -8.742  21.920  1.00 60.38           C  
ANISOU10286  C   GLN B 585     6800   7842   8297     95    -43    209       C  
ATOM  10287  O   GLN B 585     -39.642  -9.488  20.944  1.00 61.82           O  
ANISOU10287  O   GLN B 585     6986   8011   8489     92    -59    208       O  
ATOM  10288  CB  GLN B 585     -40.369  -9.623  24.172  1.00 67.27           C  
ANISOU10288  CB  GLN B 585     7642   8726   9189     94     -4    226       C  
ATOM  10289  CG  GLN B 585     -41.470  -8.558  24.246  1.00 75.06           C  
ANISOU10289  CG  GLN B 585     8616   9709  10192     96     -7    219       C  
ATOM  10290  CD  GLN B 585     -42.743  -8.924  23.469  1.00 82.96           C  
ANISOU10290  CD  GLN B 585     9603  10693  11225     94    -24    216       C  
ATOM  10291  OE1 GLN B 585     -43.065 -10.101  23.283  1.00 89.43           O  
ANISOU10291  OE1 GLN B 585    10414  11502  12060     89    -26    221       O  
ATOM  10292  NE2 GLN B 585     -43.481  -7.908  23.031  1.00 78.90           N  
ANISOU10292  NE2 GLN B 585     9084  10174  10721     97    -35    208       N  
ATOM  10293  N   LYS B 586     -39.622  -7.416  21.836  1.00 57.88           N  
ANISOU10293  N   LYS B 586     6486   7528   7974     99    -46    201       N  
ATOM  10294  CA  LYS B 586     -40.049  -6.774  20.580  1.00 54.89           C  
ANISOU10294  CA  LYS B 586     6113   7137   7602    101    -70    192       C  
ATOM  10295  C   LYS B 586     -39.008  -6.887  19.458  1.00 49.21           C  
ANISOU10295  C   LYS B 586     5418   6415   6865    101    -85    188       C  
ATOM  10296  O   LYS B 586     -39.362  -7.204  18.313  1.00 45.82           O  
ANISOU10296  O   LYS B 586     4992   5971   6445    101   -105    183       O  
ATOM  10297  CB  LYS B 586     -40.529  -5.330  20.799  1.00 56.86           C  
ANISOU10297  CB  LYS B 586     6360   7391   7853    107    -68    185       C  
ATOM  10298  CG  LYS B 586     -41.864  -5.251  21.523  1.00 56.34           C  
ANISOU10298  CG  LYS B 586     6270   7323   7813    107    -59    187       C  
ATOM  10299  CD  LYS B 586     -42.618  -3.964  21.244  1.00 61.47           C  
ANISOU10299  CD  LYS B 586     6915   7968   8470    113    -66    180       C  
ATOM  10300  CE  LYS B 586     -44.097  -4.134  21.590  1.00 66.94           C  
ANISOU10300  CE  LYS B 586     7583   8654   9195    114    -64    182       C  
ATOM  10301  NZ  LYS B 586     -44.960  -3.017  21.106  1.00 67.64           N  
ANISOU10301  NZ  LYS B 586     7667   8738   9296    120    -75    175       N  
ATOM  10302  N   PHE B 587     -37.738  -6.649  19.794  1.00 44.76           N  
ANISOU10302  N   PHE B 587     4868   5863   6273    102    -75    189       N  
ATOM  10303  CA  PHE B 587     -36.653  -6.819  18.829  1.00 41.99           C  
ANISOU10303  CA  PHE B 587     4539   5509   5903    102    -86    187       C  
ATOM  10304  C   PHE B 587     -36.656  -8.226  18.246  1.00 41.95           C  
ANISOU10304  C   PHE B 587     4536   5494   5908     98    -94    192       C  
ATOM  10305  O   PHE B 587     -36.570  -8.409  17.020  1.00 40.74           O  
ANISOU10305  O   PHE B 587     4395   5329   5755     98   -113    187       O  
ATOM  10306  CB  PHE B 587     -35.284  -6.507  19.448  1.00 40.93           C  
ANISOU10306  CB  PHE B 587     4417   5391   5741    103    -71    189       C  
ATOM  10307  CG  PHE B 587     -34.128  -6.818  18.535  1.00 39.71           C  
ANISOU10307  CG  PHE B 587     4283   5234   5567    103    -81    189       C  
ATOM  10308  CD1 PHE B 587     -33.918  -6.079  17.385  1.00 38.37           C  
ANISOU10308  CD1 PHE B 587     4130   5056   5392    106    -97    180       C  
ATOM  10309  CD2 PHE B 587     -33.268  -7.875  18.811  1.00 40.74           C  
ANISOU10309  CD2 PHE B 587     4419   5370   5688    100    -72    198       C  
ATOM  10310  CE1 PHE B 587     -32.874  -6.373  16.533  1.00 37.78           C  
ANISOU10310  CE1 PHE B 587     4075   4978   5301    106   -105    180       C  
ATOM  10311  CE2 PHE B 587     -32.214  -8.174  17.967  1.00 39.01           C  
ANISOU10311  CE2 PHE B 587     4219   5149   5453    101    -80    198       C  
ATOM  10312  CZ  PHE B 587     -32.017  -7.419  16.826  1.00 38.98           C  
ANISOU10312  CZ  PHE B 587     4231   5136   5443    103    -96    189       C  
ATOM  10313  N   LEU B 588     -36.782  -9.212  19.135  1.00 41.29           N  
ANISOU10313  N   LEU B 588     4440   5414   5832     95    -79    201       N  
ATOM  10314  CA  LEU B 588     -36.758 -10.624  18.757  1.00 40.78           C  
ANISOU10314  CA  LEU B 588     4376   5340   5776     90    -83    207       C  
ATOM  10315  C   LEU B 588     -37.896 -11.004  17.820  1.00 39.98           C  
ANISOU10315  C   LEU B 588     4267   5220   5700     88   -102    201       C  
ATOM  10316  O   LEU B 588     -37.702 -11.784  16.885  1.00 40.00           O  
ANISOU10316  O   LEU B 588     4280   5212   5705     85   -116    200       O  
ATOM  10317  CB  LEU B 588     -36.747 -11.510  20.007  1.00 41.27           C  
ANISOU10317  CB  LEU B 588     4425   5411   5842     88    -60    219       C  
ATOM  10318  CG  LEU B 588     -35.456 -11.372  20.827  1.00 42.02           C  
ANISOU10318  CG  LEU B 588     4529   5524   5909     91    -43    225       C  
ATOM  10319  CD1 LEU B 588     -35.606 -11.956  22.228  1.00 41.75           C  
ANISOU10319  CD1 LEU B 588     4481   5501   5880     90    -19    236       C  
ATOM  10320  CD2 LEU B 588     -34.263 -11.966  20.084  1.00 40.26           C  
ANISOU10320  CD2 LEU B 588     4326   5300   5668     90    -49    227       C  
ATOM  10321  N   GLN B 589     -39.077 -10.443  18.079  1.00 41.10           N  
ANISOU10321  N   GLN B 589     4392   5360   5863     88   -104    198       N  
ATOM  10322  CA  GLN B 589     -40.222 -10.581  17.187  1.00 39.97           C  
ANISOU10322  CA  GLN B 589     4240   5201   5743     86   -125    191       C  
ATOM  10323  C   GLN B 589     -39.894  -9.944  15.840  1.00 40.61           C  
ANISOU10323  C   GLN B 589     4340   5276   5813     90   -148    182       C  
ATOM  10324  O   GLN B 589     -40.045 -10.581  14.784  1.00 39.42           O  
ANISOU10324  O   GLN B 589     4195   5111   5668     88   -166    178       O  
ATOM  10325  CB  GLN B 589     -41.475  -9.944  17.810  1.00 40.05           C  
ANISOU10325  CB  GLN B 589     4228   5213   5775     88   -120    190       C  
ATOM  10326  CG  GLN B 589     -42.782 -10.244  17.078  1.00 39.84           C  
ANISOU10326  CG  GLN B 589     4187   5172   5779     85   -139    185       C  
ATOM  10327  CD  GLN B 589     -42.945 -11.713  16.703  1.00 40.68           C  
ANISOU10327  CD  GLN B 589     4290   5266   5898     77   -145    188       C  
ATOM  10328  OE1 GLN B 589     -43.195 -12.051  15.539  1.00 39.30           O  
ANISOU10328  OE1 GLN B 589     4122   5079   5731     75   -167    181       O  
ATOM  10329  NE2 GLN B 589     -42.784 -12.595  17.683  1.00 41.67           N  
ANISOU10329  NE2 GLN B 589     4407   5396   6028     73   -123    198       N  
ATOM  10330  N   TRP B 590     -39.406  -8.702  15.894  1.00 39.00           N  
ANISOU10330  N   TRP B 590     4146   5080   5591     96   -146    178       N  
ATOM  10331  CA  TRP B 590     -39.034  -7.953  14.700  1.00 39.56           C  
ANISOU10331  CA  TRP B 590     4235   5144   5648    101   -165    169       C  
ATOM  10332  C   TRP B 590     -38.099  -8.727  13.792  1.00 40.69           C  
ANISOU10332  C   TRP B 590     4400   5282   5778     99   -174    169       C  
ATOM  10333  O   TRP B 590     -38.162  -8.581  12.559  1.00 39.81           O  
ANISOU10333  O   TRP B 590     4300   5159   5664    102   -195    162       O  
ATOM  10334  CB  TRP B 590     -38.469  -6.578  15.089  1.00 40.76           C  
ANISOU10334  CB  TRP B 590     4395   5308   5781    107   -155    166       C  
ATOM  10335  CG  TRP B 590     -37.835  -5.815  13.951  1.00 40.19           C  
ANISOU10335  CG  TRP B 590     4345   5231   5692    112   -170    159       C  
ATOM  10336  CD1 TRP B 590     -38.436  -4.886  13.108  1.00 41.63           C  
ANISOU10336  CD1 TRP B 590     4532   5406   5880    118   -187    151       C  
ATOM  10337  CD2 TRP B 590     -36.450  -5.919  13.480  1.00 40.59           C  
ANISOU10337  CD2 TRP B 590     4420   5285   5718    112   -170    159       C  
ATOM  10338  NE1 TRP B 590     -37.541  -4.417  12.174  1.00 42.00           N  
ANISOU10338  NE1 TRP B 590     4602   5450   5906    122   -196    147       N  
ATOM  10339  CE2 TRP B 590     -36.330  -4.996  12.344  1.00 41.41           C  
ANISOU10339  CE2 TRP B 590     4540   5381   5813    119   -186    151       C  
ATOM  10340  CE3 TRP B 590     -35.336  -6.661  13.868  1.00 41.00           C  
ANISOU10340  CE3 TRP B 590     4480   5343   5753    109   -157    166       C  
ATOM  10341  CZ2 TRP B 590     -35.137  -4.834  11.650  1.00 41.11           C  
ANISOU10341  CZ2 TRP B 590     4525   5342   5751    121   -189    150       C  
ATOM  10342  CZ3 TRP B 590     -34.135  -6.484  13.164  1.00 41.33           C  
ANISOU10342  CZ3 TRP B 590     4544   5385   5772    111   -161    165       C  
ATOM  10343  CH2 TRP B 590     -34.042  -5.594  12.081  1.00 41.27           C  
ANISOU10343  CH2 TRP B 590     4552   5369   5757    117   -176    157       C  
ATOM  10344  N   VAL B 591     -37.228  -9.551  14.389  1.00 40.15           N  
ANISOU10344  N   VAL B 591     4334   5220   5698     96   -158    178       N  
ATOM  10345  CA  VAL B 591     -36.351 -10.441  13.626  1.00 39.74           C  
ANISOU10345  CA  VAL B 591     4301   5162   5635     94   -165    179       C  
ATOM  10346  C   VAL B 591     -37.161 -11.482  12.847  1.00 41.57           C  
ANISOU10346  C   VAL B 591     4529   5377   5888     89   -181    177       C  
ATOM  10347  O   VAL B 591     -36.915 -11.690  11.643  1.00 40.42           O  
ANISOU10347  O   VAL B 591     4399   5221   5736     90   -199    172       O  
ATOM  10348  CB  VAL B 591     -35.283 -11.121  14.512  1.00 39.40           C  
ANISOU10348  CB  VAL B 591     4262   5131   5577     92   -143    190       C  
ATOM  10349  CG1 VAL B 591     -34.336 -11.970  13.673  1.00 38.57           C  
ANISOU10349  CG1 VAL B 591     4176   5018   5458     91   -149    192       C  
ATOM  10350  CG2 VAL B 591     -34.484 -10.078  15.273  1.00 38.31           C  
ANISOU10350  CG2 VAL B 591     4127   5009   5417     96   -128    191       C  
ATOM  10351  N   LYS B 592     -38.127 -12.122  13.518  1.00 42.63           N  
ANISOU10351  N   LYS B 592     4640   5509   6045     84   -174    181       N  
ATOM  10352  CA  LYS B 592     -39.054 -13.045  12.840  1.00 45.31           C  
ANISOU10352  CA  LYS B 592     4973   5833   6409     78   -190    177       C  
ATOM  10353  C   LYS B 592     -39.806 -12.309  11.721  1.00 46.33           C  
ANISOU10353  C   LYS B 592     5104   5953   6546     82   -216    166       C  
ATOM  10354  O   LYS B 592     -39.922 -12.791  10.594  1.00 45.58           O  
ANISOU10354  O   LYS B 592     5018   5845   6453     80   -235    160       O  
ATOM  10355  CB  LYS B 592     -40.062 -13.635  13.833  1.00 46.95           C  
ANISOU10355  CB  LYS B 592     5153   6041   6642     73   -177    183       C  
ATOM  10356  CG  LYS B 592     -39.561 -14.786  14.688  1.00 47.95           C  
ANISOU10356  CG  LYS B 592     5278   6171   6769     68   -155    194       C  
ATOM  10357  CD  LYS B 592     -40.519 -15.024  15.844  1.00 48.10           C  
ANISOU10357  CD  LYS B 592     5270   6194   6811     65   -139    200       C  
ATOM  10358  CE  LYS B 592     -40.020 -16.098  16.794  1.00 49.33           C  
ANISOU10358  CE  LYS B 592     5423   6354   6966     62   -115    213       C  
ATOM  10359  NZ  LYS B 592     -38.783 -15.707  17.527  1.00 52.10           N  
ANISOU10359  NZ  LYS B 592     5785   6721   7287     68    -98    220       N  
ATOM  10360  N   GLU B 593     -40.298 -11.125  12.063  1.00 48.48           N  
ANISOU10360  N   GLU B 593     5366   6231   6820     87   -215    163       N  
ATOM  10361  CA  GLU B 593     -41.016 -10.246  11.157  1.00 52.42           C  
ANISOU10361  CA  GLU B 593     5866   6724   7325     92   -237    154       C  
ATOM  10362  C   GLU B 593     -40.223  -9.899   9.884  1.00 52.80           C  
ANISOU10362  C   GLU B 593     5941   6766   7351     97   -254    147       C  
ATOM  10363  O   GLU B 593     -40.789  -9.893   8.792  1.00 49.20           O  
ANISOU10363  O   GLU B 593     5490   6300   6903     98   -277    140       O  
ATOM  10364  CB  GLU B 593     -41.377  -8.963  11.916  1.00 56.94           C  
ANISOU10364  CB  GLU B 593     6427   7307   7898     98   -227    154       C  
ATOM  10365  CG  GLU B 593     -42.636  -8.251  11.451  1.00 65.86           C  
ANISOU10365  CG  GLU B 593     7544   8431   9047    102   -243    147       C  
ATOM  10366  CD  GLU B 593     -43.906  -8.778  12.109  1.00 71.00           C  
ANISOU10366  CD  GLU B 593     8166   9080   9730     96   -240    150       C  
ATOM  10367  OE1 GLU B 593     -44.989  -8.224  11.810  1.00 73.47           O  
ANISOU10367  OE1 GLU B 593     8465   9390  10061     99   -252    145       O  
ATOM  10368  OE2 GLU B 593     -43.832  -9.736  12.918  1.00 68.71           O  
ANISOU10368  OE2 GLU B 593     7866   8792   9447     89   -223    157       O  
ATOM  10369  N   GLN B 594     -38.925  -9.612  10.029  1.00 53.48           N  
ANISOU10369  N   GLN B 594     6046   6860   7411    100   -242    151       N  
ATOM  10370  CA  GLN B 594     -38.118  -9.081   8.914  1.00 55.20           C  
ANISOU10370  CA  GLN B 594     6291   7075   7607    106   -255    145       C  
ATOM  10371  C   GLN B 594     -37.086 -10.068   8.380  1.00 58.49           C  
ANISOU10371  C   GLN B 594     6727   7486   8009    103   -255    148       C  
ATOM  10372  O   GLN B 594     -36.111  -9.663   7.735  1.00 59.45           O  
ANISOU10372  O   GLN B 594     6872   7608   8108    108   -258    146       O  
ATOM  10373  CB  GLN B 594     -37.401  -7.776   9.306  1.00 51.14           C  
ANISOU10373  CB  GLN B 594     5785   6571   7072    113   -243    145       C  
ATOM  10374  CG  GLN B 594     -38.265  -6.704   9.946  1.00 48.95           C  
ANISOU10374  CG  GLN B 594     5490   6300   6806    116   -239    143       C  
ATOM  10375  CD  GLN B 594     -39.288  -6.114   9.003  1.00 48.60           C  
ANISOU10375  CD  GLN B 594     5444   6247   6775    122   -262    135       C  
ATOM  10376  OE1 GLN B 594     -39.082  -6.060   7.792  1.00 46.90           O  
ANISOU10376  OE1 GLN B 594     5246   6022   6551    125   -280    130       O  
ATOM  10377  NE2 GLN B 594     -40.405  -5.663   9.561  1.00 48.66           N  
ANISOU10377  NE2 GLN B 594     5428   6255   6802    122   -260    135       N  
ATOM  10378  N   LYS B 595     -37.302 -11.356   8.629  1.00 60.84           N  
ANISOU10378  N   LYS B 595     7017   7779   8320     95   -252    152       N  
ATOM  10379  CA  LYS B 595     -36.319 -12.370   8.255  1.00 63.42           C  
ANISOU10379  CA  LYS B 595     7360   8101   8633     93   -249    156       C  
ATOM  10380  C   LYS B 595     -36.060 -12.444   6.738  1.00 66.37           C  
ANISOU10380  C   LYS B 595     7758   8462   8997     96   -271    148       C  
ATOM  10381  O   LYS B 595     -35.043 -12.982   6.294  1.00 69.92           O  
ANISOU10381  O   LYS B 595     8227   8909   9430     96   -269    151       O  
ATOM  10382  CB  LYS B 595     -36.646 -13.732   8.900  1.00 60.67           C  
ANISOU10382  CB  LYS B 595     6998   7750   8302     84   -238    163       C  
ATOM  10383  CG  LYS B 595     -37.663 -14.619   8.203  1.00 60.08           C  
ANISOU10383  CG  LYS B 595     6916   7660   8250     78   -256    157       C  
ATOM  10384  CD  LYS B 595     -37.997 -15.806   9.105  1.00 59.22           C  
ANISOU10384  CD  LYS B 595     6791   7550   8160     69   -240    165       C  
ATOM  10385  CE  LYS B 595     -38.336 -17.071   8.331  1.00 59.63           C  
ANISOU10385  CE  LYS B 595     6846   7585   8224     62   -252    162       C  
ATOM  10386  NZ  LYS B 595     -39.621 -16.948   7.588  1.00 61.59           N  
ANISOU10386  NZ  LYS B 595     7083   7822   8494     59   -276    151       N  
ATOM  10387  N   GLN B 596     -36.965 -11.858   5.962  1.00 66.89           N  
ANISOU10387  N   GLN B 596     7821   8521   9073     99   -293    139       N  
ATOM  10388  CA  GLN B 596     -36.802 -11.715   4.520  1.00 69.86           C  
ANISOU10388  CA  GLN B 596     8219   8885   9438    104   -315    131       C  
ATOM  10389  C   GLN B 596     -35.615 -10.808   4.146  1.00 67.91           C  
ANISOU10389  C   GLN B 596     7996   8643   9163    112   -311    132       C  
ATOM  10390  O   GLN B 596     -34.980 -11.007   3.105  1.00 65.48           O  
ANISOU10390  O   GLN B 596     7712   8327   8840    115   -321    129       O  
ATOM  10391  CB  GLN B 596     -38.122 -11.196   3.917  1.00 78.05           C  
ANISOU10391  CB  GLN B 596     9246   9917  10493    106   -338    122       C  
ATOM  10392  CG  GLN B 596     -38.043 -10.519   2.550  1.00 86.09           C  
ANISOU10392  CG  GLN B 596    10285  10927  11498    115   -361    114       C  
ATOM  10393  CD  GLN B 596     -37.969 -11.491   1.382  1.00 90.97           C  
ANISOU10393  CD  GLN B 596    10920  11531  12113    112   -379    109       C  
ATOM  10394  OE1 GLN B 596     -38.943 -11.664   0.648  1.00 91.30           O  
ANISOU10394  OE1 GLN B 596    10957  11564  12169    111   -402    101       O  
ATOM  10395  NE2 GLN B 596     -36.807 -12.118   1.195  1.00 92.46           N  
ANISOU10395  NE2 GLN B 596    11128  11717  12284    111   -370    113       N  
ATOM  10396  N   PHE B 597     -35.313  -9.840   5.013  1.00 68.75           N  
ANISOU10396  N   PHE B 597     8096   8763   9262    115   -295    135       N  
ATOM  10397  CA  PHE B 597     -34.373  -8.748   4.707  1.00 67.22           C  
ANISOU10397  CA  PHE B 597     7922   8574   9045    123   -291    134       C  
ATOM  10398  C   PHE B 597     -33.060  -8.794   5.502  1.00 63.04           C  
ANISOU10398  C   PHE B 597     7398   8055   8496    122   -267    142       C  
ATOM  10399  O   PHE B 597     -32.100  -8.089   5.173  1.00 60.53           O  
ANISOU10399  O   PHE B 597     7098   7741   8158    128   -263    142       O  
ATOM  10400  CB  PHE B 597     -35.055  -7.390   4.914  1.00 72.09           C  
ANISOU10400  CB  PHE B 597     8527   9195   9666    129   -294    130       C  
ATOM  10401  CG  PHE B 597     -36.436  -7.303   4.320  1.00 79.66           C  
ANISOU10401  CG  PHE B 597     9475  10145  10645    131   -315    123       C  
ATOM  10402  CD1 PHE B 597     -36.615  -6.957   2.979  1.00 80.92           C  
ANISOU10402  CD1 PHE B 597     9651  10293  10799    138   -338    116       C  
ATOM  10403  CD2 PHE B 597     -37.564  -7.562   5.103  1.00 81.41           C  
ANISOU10403  CD2 PHE B 597     9669  10369  10892    126   -313    124       C  
ATOM  10404  CE1 PHE B 597     -37.887  -6.869   2.432  1.00 81.82           C  
ANISOU10404  CE1 PHE B 597     9754  10400  10931    140   -359    110       C  
ATOM  10405  CE2 PHE B 597     -38.838  -7.482   4.559  1.00 84.16           C  
ANISOU10405  CE2 PHE B 597    10005  10710  11259    127   -334    118       C  
ATOM  10406  CZ  PHE B 597     -39.000  -7.131   3.224  1.00 86.22           C  
ANISOU10406  CZ  PHE B 597    10283  10961  11515    134   -357    111       C  
ATOM  10407  N   LEU B 598     -33.030  -9.602   6.557  1.00 56.57           N  
ANISOU10407  N   LEU B 598     6564   7244   7686    115   -251    150       N  
ATOM  10408  CA  LEU B 598     -31.798  -9.868   7.287  1.00 53.94           C  
ANISOU10408  CA  LEU B 598     6236   6922   7336    114   -230    158       C  
ATOM  10409  C   LEU B 598     -31.056 -10.975   6.560  1.00 54.77           C  
ANISOU10409  C   LEU B 598     6359   7018   7432    113   -233    161       C  
ATOM  10410  O   LEU B 598     -31.686 -11.878   6.012  1.00 57.47           O  
ANISOU10410  O   LEU B 598     6700   7348   7788    109   -245    159       O  
ATOM  10411  CB  LEU B 598     -32.100 -10.275   8.733  1.00 49.74           C  
ANISOU10411  CB  LEU B 598     5680   6401   6814    108   -211    166       C  
ATOM  10412  CG  LEU B 598     -32.983  -9.301   9.522  1.00 48.47           C  
ANISOU10412  CG  LEU B 598     5501   6249   6666    109   -207    163       C  
ATOM  10413  CD1 LEU B 598     -33.692  -9.994  10.674  1.00 46.83           C  
ANISOU10413  CD1 LEU B 598     5269   6047   6477    103   -194    169       C  
ATOM  10414  CD2 LEU B 598     -32.196  -8.097  10.017  1.00 47.66           C  
ANISOU10414  CD2 LEU B 598     5403   6159   6544    113   -194    163       C  
ATOM  10415  N   VAL B 599     -29.726 -10.906   6.530  1.00 58.96           N  
ANISOU10415  N   VAL B 599     6906   7554   7940    115   -222    166       N  
ATOM  10416  CA  VAL B 599     -28.947 -11.915   5.795  1.00 61.47           C  
ANISOU10416  CA  VAL B 599     7242   7863   8248    115   -224    169       C  
ATOM  10417  C   VAL B 599     -28.344 -12.993   6.710  1.00 59.21           C  
ANISOU10417  C   VAL B 599     6949   7585   7962    110   -204    181       C  
ATOM  10418  O   VAL B 599     -27.890 -12.699   7.825  1.00 53.94           O  
ANISOU10418  O   VAL B 599     6271   6934   7289    110   -186    187       O  
ATOM  10419  CB  VAL B 599     -27.920 -11.284   4.809  1.00 64.60           C  
ANISOU10419  CB  VAL B 599     7665   8256   8623    122   -229    166       C  
ATOM  10420  CG1 VAL B 599     -26.603 -10.954   5.493  1.00 61.60           C  
ANISOU10420  CG1 VAL B 599     7289   7891   8223    123   -208    174       C  
ATOM  10421  CG2 VAL B 599     -27.699 -12.197   3.603  1.00 68.13           C  
ANISOU10421  CG2 VAL B 599     8132   8686   9066    123   -241    165       C  
ATOM  10422  N   ASN B 600     -28.378 -14.235   6.212  1.00 58.54           N  
ANISOU10422  N   ASN B 600     6871   7488   7883    107   -209    183       N  
ATOM  10423  CA  ASN B 600     -28.039 -15.457   6.962  1.00 58.27           C  
ANISOU10423  CA  ASN B 600     6830   7457   7852    103   -192    194       C  
ATOM  10424  C   ASN B 600     -28.791 -15.545   8.296  1.00 59.72           C  
ANISOU10424  C   ASN B 600     6986   7651   8052     98   -180    198       C  
ATOM  10425  O   ASN B 600     -28.208 -15.804   9.357  1.00 60.21           O  
ANISOU10425  O   ASN B 600     7040   7727   8108     98   -159    208       O  
ATOM  10426  CB  ASN B 600     -26.517 -15.632   7.119  1.00 57.70           C  
ANISOU10426  CB  ASN B 600     6772   7394   7758    107   -176    203       C  
ATOM  10427  CG  ASN B 600     -25.785 -15.676   5.779  1.00 57.79           C  
ANISOU10427  CG  ASN B 600     6810   7392   7753    111   -187    199       C  
ATOM  10428  OD1 ASN B 600     -24.591 -15.406   5.710  1.00 57.47           O  
ANISOU10428  OD1 ASN B 600     6782   7358   7693    116   -178    204       O  
ATOM  10429  ND2 ASN B 600     -26.502 -16.009   4.712  1.00 57.41           N  
ANISOU10429  ND2 ASN B 600     6771   7326   7715    110   -207    191       N  
ATOM  10430  N   VAL B 601     -30.104 -15.339   8.206  1.00 59.68           N  
ANISOU10430  N   VAL B 601     6967   7639   8067     95   -192    191       N  
ATOM  10431  CA  VAL B 601     -30.972 -15.176   9.367  1.00 62.77           C  
ANISOU10431  CA  VAL B 601     7333   8040   8476     92   -183    193       C  
ATOM  10432  C   VAL B 601     -30.942 -16.376  10.298  1.00 66.73           C  
ANISOU10432  C   VAL B 601     7822   8544   8986     87   -165    204       C  
ATOM  10433  O   VAL B 601     -30.661 -16.225  11.487  1.00 65.74           O  
ANISOU10433  O   VAL B 601     7685   8435   8857     88   -146    212       O  
ATOM  10434  CB  VAL B 601     -32.436 -14.931   8.959  1.00 62.56           C  
ANISOU10434  CB  VAL B 601     7294   8003   8473     89   -201    184       C  
ATOM  10435  CG1 VAL B 601     -33.033 -13.826   9.819  1.00 59.11           C  
ANISOU10435  CG1 VAL B 601     6838   7578   8041     91   -195    182       C  
ATOM  10436  CG2 VAL B 601     -32.533 -14.588   7.480  1.00 66.37           C  
ANISOU10436  CG2 VAL B 601     7794   8472   8950     93   -225    173       C  
ATOM  10437  N   GLU B 602     -31.230 -17.559   9.749  1.00 70.99           N  
ANISOU10437  N   GLU B 602     8365   9069   9537     83   -171    205       N  
ATOM  10438  CA  GLU B 602     -31.298 -18.802  10.526  1.00 72.95           C  
ANISOU10438  CA  GLU B 602     8603   9316   9797     78   -154    215       C  
ATOM  10439  C   GLU B 602     -29.964 -19.143  11.171  1.00 69.58           C  
ANISOU10439  C   GLU B 602     8184   8902   9349     82   -133    227       C  
ATOM  10440  O   GLU B 602     -29.920 -19.735  12.251  1.00 71.74           O  
ANISOU10440  O   GLU B 602     8444   9184   9627     81   -114    238       O  
ATOM  10441  CB  GLU B 602     -31.743 -19.982   9.656  1.00 79.11           C  
ANISOU10441  CB  GLU B 602     9390  10077  10592     72   -165    212       C  
ATOM  10442  CG  GLU B 602     -33.098 -19.818   8.984  1.00 84.30           C  
ANISOU10442  CG  GLU B 602    10038  10721  11271     68   -187    199       C  
ATOM  10443  CD  GLU B 602     -33.010 -19.086   7.656  1.00 87.11           C  
ANISOU10443  CD  GLU B 602    10412  11069  11616     72   -211    187       C  
ATOM  10444  OE1 GLU B 602     -31.881 -18.772   7.210  1.00 90.26           O  
ANISOU10444  OE1 GLU B 602    10832  11470  11990     78   -209    189       O  
ATOM  10445  OE2 GLU B 602     -34.074 -18.820   7.057  1.00 90.55           O  
ANISOU10445  OE2 GLU B 602    10841  11495  12066     69   -231    177       O  
ATOM  10446  N   GLN B 603     -28.884 -18.759  10.500  1.00 66.02           N  
ANISOU10446  N   GLN B 603     7754   8453   8876     87   -137    226       N  
ATOM  10447  CA  GLN B 603     -27.534 -19.008  10.979  1.00 62.72           C  
ANISOU10447  CA  GLN B 603     7344   8047   8437     91   -119    238       C  
ATOM  10448  C   GLN B 603     -27.247 -18.237  12.272  1.00 61.08           C  
ANISOU10448  C   GLN B 603     7123   7863   8221     94   -103    243       C  
ATOM  10449  O   GLN B 603     -26.419 -18.666  13.077  1.00 61.65           O  
ANISOU10449  O   GLN B 603     7193   7948   8282     96    -84    255       O  
ATOM  10450  CB  GLN B 603     -26.512 -18.662   9.886  1.00 67.16           C  
ANISOU10450  CB  GLN B 603     7932   8605   8978     96   -128    234       C  
ATOM  10451  CG  GLN B 603     -26.501 -19.611   8.686  1.00 71.78           C  
ANISOU10451  CG  GLN B 603     8535   9170   9567     95   -139    231       C  
ATOM  10452  CD  GLN B 603     -27.644 -19.390   7.691  1.00 75.17           C  
ANISOU10452  CD  GLN B 603     8965   9582  10011     92   -163    217       C  
ATOM  10453  OE1 GLN B 603     -28.827 -19.386   8.052  1.00 75.48           O  
ANISOU10453  OE1 GLN B 603     8987   9620  10072     87   -168    213       O  
ATOM  10454  NE2 GLN B 603     -27.288 -19.225   6.424  1.00 77.67           N  
ANISOU10454  NE2 GLN B 603     9305   9888  10318     95   -179    210       N  
ATOM  10455  N   MET B 604     -27.942 -17.114  12.476  1.00 56.20           N  
ANISOU10455  N   MET B 604     6494   7249   7608     93   -109    235       N  
ATOM  10456  CA  MET B 604     -27.763 -16.293  13.679  1.00 52.57           C  
ANISOU10456  CA  MET B 604     6021   6810   7140     95    -95    238       C  
ATOM  10457  C   MET B 604     -28.072 -17.095  14.928  1.00 49.93           C  
ANISOU10457  C   MET B 604     5669   6484   6817     93    -76    249       C  
ATOM  10458  O   MET B 604     -28.931 -17.964  14.898  1.00 52.65           O  
ANISOU10458  O   MET B 604     6005   6816   7182     89    -78    251       O  
ATOM  10459  CB  MET B 604     -28.657 -15.056  13.641  1.00 51.43           C  
ANISOU10459  CB  MET B 604     5868   6666   7004     95   -106    227       C  
ATOM  10460  CG  MET B 604     -28.153 -13.938  12.746  1.00 52.05           C  
ANISOU10460  CG  MET B 604     5963   6743   7067     99   -119    218       C  
ATOM  10461  SD  MET B 604     -29.369 -12.623  12.524  1.00 53.37           S  
ANISOU10461  SD  MET B 604     6122   6907   7248     99   -133    205       S  
ATOM  10462  CE  MET B 604     -29.648 -12.123  14.224  1.00 52.31           C  
ANISOU10462  CE  MET B 604     5965   6793   7117     98   -113    210       C  
ATOM  10463  N   THR B 605     -27.363 -16.809  16.017  1.00 48.02           N  
ANISOU10463  N   THR B 605     5421   6262   6560     96    -59    257       N  
ATOM  10464  CA  THR B 605     -27.566 -17.511  17.283  1.00 47.87           C  
ANISOU10464  CA  THR B 605     5387   6253   6548     95    -39    269       C  
ATOM  10465  C   THR B 605     -27.443 -16.563  18.474  1.00 47.17           C  
ANISOU10465  C   THR B 605     5286   6186   6449     97    -27    270       C  
ATOM  10466  O   THR B 605     -26.652 -15.628  18.452  1.00 45.64           O  
ANISOU10466  O   THR B 605     5099   6003   6236    100    -28    266       O  
ATOM  10467  CB  THR B 605     -26.557 -18.672  17.491  1.00 49.09           C  
ANISOU10467  CB  THR B 605     5548   6411   6691     98    -26    282       C  
ATOM  10468  OG1 THR B 605     -25.538 -18.266  18.413  1.00 51.72           O  
ANISOU10468  OG1 THR B 605     5880   6767   7003    103    -11    290       O  
ATOM  10469  CG2 THR B 605     -25.905 -19.128  16.174  1.00 46.88           C  
ANISOU10469  CG2 THR B 605     5290   6116   6404     99    -37    280       C  
ATOM  10470  N   CYS B 606     -28.206 -16.833  19.527  1.00 50.81           N  
ANISOU10470  N   CYS B 606     5729   6652   6924     96    -15    275       N  
ATOM  10471  CA  CYS B 606     -28.124 -16.055  20.761  1.00 53.01           C  
ANISOU10471  CA  CYS B 606     5995   6951   7192     98     -1    277       C  
ATOM  10472  C   CYS B 606     -26.730 -16.156  21.373  1.00 52.81           C  
ANISOU10472  C   CYS B 606     5977   6946   7142    103     12    286       C  
ATOM  10473  O   CYS B 606     -25.994 -17.100  21.111  1.00 51.69           O  
ANISOU10473  O   CYS B 606     5844   6802   6993    104     15    295       O  
ATOM  10474  CB  CYS B 606     -29.164 -16.537  21.783  1.00 54.33           C  
ANISOU10474  CB  CYS B 606     6142   7119   7379     97     11    283       C  
ATOM  10475  SG  CYS B 606     -30.880 -16.636  21.204  1.00 58.92           S  
ANISOU10475  SG  CYS B 606     6712   7678   7995     91     -2    275       S  
ATOM  10476  N   ALA B 607     -26.375 -15.174  22.190  1.00 55.64           N  
ANISOU10476  N   ALA B 607     6330   7323   7484    104     19    284       N  
ATOM  10477  CA  ALA B 607     -25.147 -15.241  22.961  1.00 57.46           C  
ANISOU10477  CA  ALA B 607     6564   7575   7691    108     33    293       C  
ATOM  10478  C   ALA B 607     -25.403 -15.132  24.475  1.00 61.31           C  
ANISOU10478  C   ALA B 607     7036   8082   8177    110     51    299       C  
ATOM  10479  O   ALA B 607     -24.462 -15.196  25.267  1.00 59.33           O  
ANISOU10479  O   ALA B 607     6785   7851   7906    113     63    307       O  
ATOM  10480  CB  ALA B 607     -24.172 -14.177  22.489  1.00 54.06           C  
ANISOU10480  CB  ALA B 607     6146   7153   7240    109     25    284       C  
ATOM  10481  N   THR B 608     -26.670 -14.980  24.871  1.00 66.12           N  
ANISOU10481  N   THR B 608     7631   8683   8805    108     52    296       N  
ATOM  10482  CA  THR B 608     -27.037 -14.930  26.298  1.00 76.56           C  
ANISOU10482  CA  THR B 608     8938  10021  10127    110     70    302       C  
ATOM  10483  C   THR B 608     -27.715 -16.213  26.845  1.00 87.63           C  
ANISOU10483  C   THR B 608    10330  11418  11547    111     83    315       C  
ATOM  10484  O   THR B 608     -27.701 -17.256  26.179  1.00 91.46           O  
ANISOU10484  O   THR B 608    10819  11888  12042    110     80    321       O  
ATOM  10485  CB  THR B 608     -27.871 -13.687  26.634  1.00 73.53           C  
ANISOU10485  CB  THR B 608     8547   9640   9750    108     68    291       C  
ATOM  10486  OG1 THR B 608     -28.884 -13.534  25.636  1.00 77.63           O  
ANISOU10486  OG1 THR B 608     9065  10137  10292    104     52    282       O  
ATOM  10487  CG2 THR B 608     -26.989 -12.444  26.710  1.00 68.11           C  
ANISOU10487  CG2 THR B 608     7869   8969   9040    108     65    282       C  
ATOM  10488  N   PRO B 609     -28.378 -16.121  28.021  1.00 91.10           N  
ANISOU10488  N   PRO B 609    10755  11866  11993    112     98    320       N  
ATOM  10489  CA  PRO B 609     -28.385 -17.141  29.065  1.00 95.23           C  
ANISOU10489  CA  PRO B 609    11269  12397  12516    117    118    335       C  
ATOM  10490  C   PRO B 609     -27.236 -18.176  29.039  1.00 99.21           C  
ANISOU10490  C   PRO B 609    11783  12907  13005    121    125    349       C  
ATOM  10491  O   PRO B 609     -26.286 -18.043  28.265  1.00 91.12           O  
ANISOU10491  O   PRO B 609    10772  11884  11966    121    115    346       O  
ATOM  10492  CB  PRO B 609     -29.765 -17.788  28.876  1.00 92.06           C  
ANISOU10492  CB  PRO B 609    10856  11974  12147    113    119    337       C  
ATOM  10493  CG  PRO B 609     -30.623 -16.674  28.335  1.00 83.37           C  
ANISOU10493  CG  PRO B 609     9752  10864  11059    108    104    321       C  
ATOM  10494  CD  PRO B 609     -29.721 -15.520  27.957  1.00 87.39           C  
ANISOU10494  CD  PRO B 609    10274  11384  11545    109     93    310       C  
ATOM  10495  N   ASN B 613     -27.514 -20.959  23.798  1.00 81.84           N  
ANISOU10495  N   ASN B 613     9624  10616  10855    107     71    338       N  
ATOM  10496  CA  ASN B 613     -26.281 -20.695  23.089  1.00 72.22           C  
ANISOU10496  CA  ASN B 613     8422   9402   9614    109     63    336       C  
ATOM  10497  C   ASN B 613     -26.496 -21.180  21.654  1.00 68.02           C  
ANISOU10497  C   ASN B 613     7902   8845   9094    105     46    329       C  
ATOM  10498  O   ASN B 613     -25.572 -21.198  20.839  1.00 58.95           O  
ANISOU10498  O   ASN B 613     6771   7695   7932    107     38    328       O  
ATOM  10499  CB  ASN B 613     -25.157 -21.457  23.761  1.00 75.97           C  
ANISOU10499  CB  ASN B 613     8900   9892  10070    116     80    352       C  
ATOM  10500  CG  ASN B 613     -23.836 -20.738  23.678  1.00 77.75           C  
ANISOU10500  CG  ASN B 613     9137  10135  10268    120     78    351       C  
ATOM  10501  OD1 ASN B 613     -23.490 -20.143  22.650  1.00 83.73           O  
ANISOU10501  OD1 ASN B 613     9907  10885  11020    118     62    341       O  
ATOM  10502  ND2 ASN B 613     -23.077 -20.796  24.764  1.00 72.60           N  
ANISOU10502  ND2 ASN B 613     8480   9506   9598    126     94    362       N  
ATOM  10503  N   THR B 614     -27.744 -21.595  21.400  1.00 66.97           N  
ANISOU10503  N   THR B 614     7761   8694   8988     99     41    325       N  
ATOM  10504  CA  THR B 614     -28.356 -21.786  20.074  1.00 65.57           C  
ANISOU10504  CA  THR B 614     7591   8493   8827     94     21    314       C  
ATOM  10505  C   THR B 614     -29.901 -21.834  20.260  1.00 65.40           C  
ANISOU10505  C   THR B 614     7552   8460   8835     88     18    309       C  
ATOM  10506  O   THR B 614     -30.370 -22.300  21.305  1.00 64.36           O  
ANISOU10506  O   THR B 614     7406   8334   8714     88     35    318       O  
ATOM  10507  CB  THR B 614     -27.843 -23.071  19.398  0.00 20.00           C  
ATOM  10508  OG1 THR B 614     -28.114 -24.197  20.239  0.00 20.00           O  
ATOM  10509  CG2 THR B 614     -26.324 -23.058  19.309  0.00 20.00           C  
ATOM  10510  N   SER B 615     -30.712 -21.337  19.316  1.00 62.82           N  
ANISOU10510  N   SER B 615     7226   8119   8523     83     -2    295       N  
ATOM  10511  CA  SER B 615     -30.319 -20.600  18.107  1.00 63.61           C  
ANISOU10511  CA  SER B 615     7343   8213   8611     83    -24    283       C  
ATOM  10512  C   SER B 615     -30.822 -19.157  18.250  1.00 66.50           C  
ANISOU10512  C   SER B 615     7702   8588   8977     84    -32    272       C  
ATOM  10513  O   SER B 615     -30.247 -18.426  19.053  1.00 70.37           O  
ANISOU10513  O   SER B 615     8190   9097   9450     88    -22    275       O  
ATOM  10514  CB  SER B 615     -30.878 -21.269  16.841  1.00 63.64           C  
ANISOU10514  CB  SER B 615     7354   8193   8631     78    -41    275       C  
ATOM  10515  OG  SER B 615     -30.502 -20.574  15.662  1.00 57.60           O  
ANISOU10515  OG  SER B 615     6606   7422   7855     79    -62    264       O  
ATOM  10516  N   LEU B 616     -31.874 -18.744  17.519  1.00 59.37           N  
ANISOU10516  N   LEU B 616     6794   7671   8091     80    -51    260       N  
ATOM  10517  CA  LEU B 616     -32.359 -17.342  17.612  1.00 57.81           C  
ANISOU10517  CA  LEU B 616     6590   7480   7894     81    -59    251       C  
ATOM  10518  C   LEU B 616     -33.760 -16.998  17.048  1.00 58.91           C  
ANISOU10518  C   LEU B 616     6719   7605   8058     77    -76    240       C  
ATOM  10519  O   LEU B 616     -34.578 -16.384  17.749  1.00 57.42           O  
ANISOU10519  O   LEU B 616     6514   7423   7881     77    -71    238       O  
ATOM  10520  CB  LEU B 616     -31.323 -16.362  17.040  1.00 54.56           C  
ANISOU10520  CB  LEU B 616     6197   7076   7456     86    -67    245       C  
ATOM  10521  CG  LEU B 616     -31.385 -14.922  17.568  1.00 53.87           C  
ANISOU10521  CG  LEU B 616     6104   7002   7360     89    -65    239       C  
ATOM  10522  CD1 LEU B 616     -30.010 -14.278  17.475  1.00 52.05           C  
ANISOU10522  CD1 LEU B 616     5891   6785   7101     93    -62    239       C  
ATOM  10523  CD2 LEU B 616     -32.432 -14.070  16.855  1.00 52.11           C  
ANISOU10523  CD2 LEU B 616     5877   6768   7152     88    -84    226       C  
ATOM  10524  N   VAL B 617     -34.020 -17.333  15.782  1.00 55.42           N  
ANISOU10524  N   VAL B 617     6286   7145   7623     75    -96    232       N  
ATOM  10525  CA  VAL B 617     -35.371 -17.200  15.229  1.00 52.46           C  
ANISOU10525  CA  VAL B 617     5900   6757   7274     70   -113    223       C  
ATOM  10526  C   VAL B 617     -36.329 -18.062  16.060  1.00 54.47           C  
ANISOU10526  C   VAL B 617     6133   7008   7554     65   -101    229       C  
ATOM  10527  O   VAL B 617     -37.552 -17.986  15.928  1.00 59.27           O  
ANISOU10527  O   VAL B 617     6725   7607   8186     61   -110    223       O  
ATOM  10528  CB  VAL B 617     -35.451 -17.552  13.720  1.00 51.11           C  
ANISOU10528  CB  VAL B 617     5744   6568   7105     68   -137    213       C  
ATOM  10529  CG1 VAL B 617     -35.832 -16.340  12.880  1.00 48.59           C  
ANISOU10529  CG1 VAL B 617     5430   6246   6784     72   -158    201       C  
ATOM  10530  CG2 VAL B 617     -34.162 -18.152  13.203  1.00 52.75           C  
ANISOU10530  CG2 VAL B 617     5975   6774   7292     70   -135    218       C  
ATOM  10531  N   LEU B 618     -35.742 -18.845  16.956  1.00 53.28           N  
ANISOU10531  N   LEU B 618     5980   6864   7397     65    -79    242       N  
ATOM  10532  CA  LEU B 618     -36.445 -19.819  17.767  1.00 50.16           C  
ANISOU10532  CA  LEU B 618     5567   6465   7024     61    -63    250       C  
ATOM  10533  C   LEU B 618     -36.759 -19.311  19.179  1.00 50.31           C  
ANISOU10533  C   LEU B 618     5568   6500   7044     64    -43    257       C  
ATOM  10534  O   LEU B 618     -37.168 -20.097  20.028  1.00 51.85           O  
ANISOU10534  O   LEU B 618     5750   6695   7254     62    -25    266       O  
ATOM  10535  CB  LEU B 618     -35.610 -21.110  17.837  1.00 49.28           C  
ANISOU10535  CB  LEU B 618     5466   6351   6905     60    -50    261       C  
ATOM  10536  CG  LEU B 618     -35.534 -22.110  16.663  1.00 50.11           C  
ANISOU10536  CG  LEU B 618     5584   6436   7016     55    -64    257       C  
ATOM  10537  CD1 LEU B 618     -35.830 -21.527  15.284  1.00 50.12           C  
ANISOU10537  CD1 LEU B 618     5597   6426   7019     54    -92    242       C  
ATOM  10538  CD2 LEU B 618     -34.199 -22.849  16.658  1.00 49.78           C  
ANISOU10538  CD2 LEU B 618     5561   6398   6954     59    -52    267       C  
ATOM  10539  N   ASP B 619     -36.571 -18.013  19.441  1.00 51.24           N  
ANISOU10539  N   ASP B 619     5687   6631   7148     69    -45    252       N  
ATOM  10540  CA  ASP B 619     -36.942 -17.439  20.747  1.00 53.13           C  
ANISOU10540  CA  ASP B 619     5911   6886   7390     72    -27    257       C  
ATOM  10541  C   ASP B 619     -38.442 -17.617  20.904  1.00 58.27           C  
ANISOU10541  C   ASP B 619     6539   7525   8074     67    -28    255       C  
ATOM  10542  O   ASP B 619     -39.176 -17.496  19.924  1.00 57.42           O  
ANISOU10542  O   ASP B 619     6430   7404   7982     63    -49    245       O  
ATOM  10543  CB  ASP B 619     -36.569 -15.952  20.853  1.00 50.56           C  
ANISOU10543  CB  ASP B 619     5590   6574   7046     77    -30    250       C  
ATOM  10544  CG  ASP B 619     -37.005 -15.312  22.191  1.00 49.87           C  
ANISOU10544  CG  ASP B 619     5487   6501   6960     80    -12    254       C  
ATOM  10545  OD1 ASP B 619     -36.383 -15.592  23.234  1.00 49.66           O  
ANISOU10545  OD1 ASP B 619     5458   6488   6919     83      8    264       O  
ATOM  10546  OD2 ASP B 619     -37.960 -14.507  22.207  1.00 46.92           O  
ANISOU10546  OD2 ASP B 619     5101   6124   6600     80    -18    247       O  
ATOM  10547  N   PHE B 620     -38.898 -17.916  22.119  1.00 66.72           N  
ANISOU10547  N   PHE B 620     7593   8602   9155     67     -7    264       N  
ATOM  10548  CA  PHE B 620     -40.322 -18.140  22.329  1.00 73.14           C  
ANISOU10548  CA  PHE B 620     8384   9405  10001     63     -6    263       C  
ATOM  10549  C   PHE B 620     -41.124 -16.868  22.625  1.00 78.31           C  
ANISOU10549  C   PHE B 620     9026  10065  10662     66    -10    256       C  
ATOM  10550  O   PHE B 620     -41.640 -16.246  21.687  1.00 79.48           O  
ANISOU10550  O   PHE B 620     9174  10204  10818     65    -32    245       O  
ATOM  10551  CB  PHE B 620     -40.590 -19.248  23.344  1.00 80.40           C  
ANISOU10551  CB  PHE B 620     9290  10323  10933     61     17    277       C  
ATOM  10552  CG  PHE B 620     -41.568 -20.276  22.849  1.00 89.14           C  
ANISOU10552  CG  PHE B 620    10386  11410  12072     53     11    275       C  
ATOM  10553  CD1 PHE B 620     -42.937 -20.008  22.831  1.00 92.95           C  
ANISOU10553  CD1 PHE B 620    10847  11883  12584     49      5    270       C  
ATOM  10554  CD2 PHE B 620     -41.121 -21.507  22.371  1.00 92.38           C  
ANISOU10554  CD2 PHE B 620    10806  11809  12484     48     11    279       C  
ATOM  10555  CE1 PHE B 620     -43.841 -20.955  22.364  1.00 97.55           C  
ANISOU10555  CE1 PHE B 620    11418  12448  13197     40     -1    268       C  
ATOM  10556  CE2 PHE B 620     -42.021 -22.458  21.902  1.00 95.85           C  
ANISOU10556  CE2 PHE B 620    11235  12229  12953     39      5    277       C  
ATOM  10557  CZ  PHE B 620     -43.382 -22.182  21.900  1.00 96.65           C  
ANISOU10557  CZ  PHE B 620    11315  12323  13084     35      0    271       C  
ATOM  10558  N   ASN B 621     -41.238 -16.476  23.896  1.00 78.27           N  
ANISOU10558  N   ASN B 621     9010  10073  10653     70     11    263       N  
ATOM  10559  CA  ASN B 621     -42.103 -15.347  24.281  1.00 80.92           C  
ANISOU10559  CA  ASN B 621     9333  10413  11000     72     11    258       C  
ATOM  10560  C   ASN B 621     -42.985 -15.710  25.480  1.00 84.02           C  
ANISOU10560  C   ASN B 621     9703  10807  11412     72     33    267       C  
ATOM  10561  O   ASN B 621     -44.203 -15.567  25.405  1.00 88.42           O  
ANISOU10561  O   ASN B 621    10242  11354  11996     70     29    263       O  
ATOM  10562  CB  ASN B 621     -43.005 -14.938  23.089  1.00 77.66           C  
ANISOU10562  CB  ASN B 621     8915   9985  10606     69    -15    245       C  
ATOM  10563  CG  ASN B 621     -43.363 -13.457  23.072  1.00 76.53           C  
ANISOU10563  CG  ASN B 621     8770   9848  10459     75    -21    237       C  
ATOM  10564  OD1 ASN B 621     -42.965 -12.688  23.948  1.00 78.78           O  
ANISOU10564  OD1 ASN B 621     9056  10148  10728     80     -6    239       O  
ATOM  10565  ND2 ASN B 621     -44.119 -13.049  22.052  1.00 70.40           N  
ANISOU10565  ND2 ASN B 621     7989   9059   9698     73    -44    227       N  
ATOM  10566  N   ASN B 622     -42.387 -16.178  26.579  1.00 90.86           N  
ANISOU10566  N   ASN B 622    10570  11685  12265     75     58    279       N  
ATOM  10567  CA  ASN B 622     -43.174 -16.681  27.726  1.00 91.82           C  
ANISOU10567  CA  ASN B 622    10673  11807  12406     75     81    289       C  
ATOM  10568  C   ASN B 622     -42.624 -16.463  29.140  1.00 94.54           C  
ANISOU10568  C   ASN B 622    11018  12171  12730     82    108    299       C  
ATOM  10569  O   ASN B 622     -43.385 -16.490  30.106  1.00 91.79           O  
ANISOU10569  O   ASN B 622    10653  11824  12395     84    126    306       O  
ATOM  10570  CB  ASN B 622     -43.522 -18.163  27.529  1.00 85.01           C  
ANISOU10570  CB  ASN B 622     9804  10930  11565     69     85    296       C  
ATOM  10571  CG  ASN B 622     -44.627 -18.367  26.514  1.00 78.13           C  
ANISOU10571  CG  ASN B 622     8920  10038  10725     61     64    287       C  
ATOM  10572  OD1 ASN B 622     -44.418 -18.969  25.463  1.00 76.48           O  
ANISOU10572  OD1 ASN B 622     8721   9818  10520     56     47    282       O  
ATOM  10573  ND2 ASN B 622     -45.805 -17.840  26.811  1.00 76.50           N  
ANISOU10573  ND2 ASN B 622     8695   9829  10542     61     66    284       N  
ATOM  10574  N   SER B 623     -41.317 -16.250  29.260  1.00108.00           N  
ANISOU10574  N   SER B 623    12742  13891  14402     86    109    301       N  
ATOM  10575  CA  SER B 623     -40.680 -16.010  30.563  1.00123.91           C  
ANISOU10575  CA  SER B 623    14759  15926  16394     93    132    309       C  
ATOM  10576  C   SER B 623     -41.043 -14.630  31.141  1.00132.26           C  
ANISOU10576  C   SER B 623    15812  16995  17446     97    136    303       C  
ATOM  10577  O   SER B 623     -40.249 -13.685  31.070  1.00135.62           O  
ANISOU10577  O   SER B 623    16250  17432  17846    100    130    296       O  
ATOM  10578  CB  SER B 623     -39.155 -16.178  30.457  1.00124.50           C  
ANISOU10578  CB  SER B 623    14854  16014  16436     96    131    312       C  
ATOM  10579  OG  SER B 623     -38.808 -17.453  29.943  1.00120.22           O  
ANISOU10579  OG  SER B 623    14317  15462  15899     93    129    319       O  
ATOM  10580  N   THR B 624     -42.243 -14.543  31.724  1.00136.82           N  
ANISOU10580  N   THR B 624    16370  17566  18047     97    147    305       N  
ATOM  10581  CA  THR B 624     -42.864 -13.287  32.204  1.00136.62           C  
ANISOU10581  CA  THR B 624    16338  17547  18025    101    151    298       C  
ATOM  10582  C   THR B 624     -43.455 -12.468  31.051  1.00132.05           C  
ANISOU10582  C   THR B 624    15757  16956  17459     98    126    284       C  
ATOM  10583  O   THR B 624     -44.543 -11.901  31.181  1.00131.05           O  
ANISOU10583  O   THR B 624    15615  16822  17352     99    127    281       O  
ATOM  10584  CB  THR B 624     -41.915 -12.408  33.065  1.00139.89           C  
ANISOU10584  CB  THR B 624    16763  17983  18404    107    162    297       C  
ATOM  10585  OG1 THR B 624     -41.254 -13.219  34.043  1.00143.58           O  
ANISOU10585  OG1 THR B 624    17233  18462  18856    110    183    311       O  
ATOM  10586  CG2 THR B 624     -42.690 -11.293  33.777  1.00133.96           C  
ANISOU10586  CG2 THR B 624    16002  17237  17658    110    172    293       C  
ATOM  10587  N   CYS B 625     -42.737 -12.421  29.929  1.00126.53           N  
ANISOU10587  N   CYS B 625    15074  16253  16748     95    104    277       N  
ATOM  10588  CA  CYS B 625     -43.176 -11.671  28.751  1.00128.22           C  
ANISOU10588  CA  CYS B 625    15289  16456  16972     94     80    264       C  
ATOM  10589  C   CYS B 625     -44.359 -12.345  28.048  1.00128.49           C  
ANISOU10589  C   CYS B 625    15307  16470  17041     88     68    263       C  
ATOM  10590  O   CYS B 625     -44.471 -13.572  28.032  1.00130.20           O  
ANISOU10590  O   CYS B 625    15519  16679  17270     84     72    270       O  
ATOM  10591  CB  CYS B 625     -42.006 -11.424  27.778  1.00118.25           C  
ANISOU10591  CB  CYS B 625    14049  15195  15684     93     62    257       C  
ATOM  10592  SG  CYS B 625     -41.247 -12.883  27.009  1.00100.69           S  
ANISOU10592  SG  CYS B 625    11837  12964  13457     88     53    262       S  
TER   10593      CYS B 625                                                      
ATOM  10594  N   GLN D  21      12.286 -35.479  -0.639  1.00 74.21           N  
ANISOU10594  N   GLN D  21    10971   8069   9155     72     27    164       N  
ATOM  10595  CA  GLN D  21      11.510 -36.297  -1.618  1.00 79.13           C  
ANISOU10595  CA  GLN D  21    11649   8651   9764     46     15    139       C  
ATOM  10596  C   GLN D  21      11.770 -35.907  -3.079  1.00 79.64           C  
ANISOU10596  C   GLN D  21    11678   8746   9835     99     18    117       C  
ATOM  10597  O   GLN D  21      12.238 -36.730  -3.867  1.00 84.27           O  
ANISOU10597  O   GLN D  21    12321   9293  10402    152      2    104       O  
ATOM  10598  CB  GLN D  21      10.007 -36.246  -1.309  1.00 81.27           C  
ANISOU10598  CB  GLN D  21    11913   8926  10038    -59     21    131       C  
ATOM  10599  CG  GLN D  21       9.595 -36.996  -0.047  1.00 85.16           C  
ANISOU10599  CG  GLN D  21    12466   9373  10515   -120     16    152       C  
ATOM  10600  CD  GLN D  21       8.128 -37.396  -0.046  1.00 85.23           C  
ANISOU10600  CD  GLN D  21    12496   9369  10519   -222     16    139       C  
ATOM  10601  OE1 GLN D  21       7.445 -37.282   0.971  1.00 82.31           O  
ANISOU10601  OE1 GLN D  21    12114   9011  10146   -291     26    155       O  
ATOM  10602  NE2 GLN D  21       7.638 -37.872  -1.189  1.00 82.72           N  
ANISOU10602  NE2 GLN D  21    12203   9029  10196   -232      5    110       N  
ATOM  10603  N   GLN D  22      11.472 -34.658  -3.436  1.00 79.64           N  
ANISOU10603  N   GLN D  22    11585   8814   9859     90     38    113       N  
ATOM  10604  CA  GLN D  22      11.606 -34.194  -4.824  1.00 79.77           C  
ANISOU10604  CA  GLN D  22    11562   8864   9880    135     44     95       C  
ATOM  10605  C   GLN D  22      13.017 -33.727  -5.166  1.00 80.22           C  
ANISOU10605  C   GLN D  22    11584   8952   9943    228     52    109       C  
ATOM  10606  O   GLN D  22      13.556 -34.091  -6.214  1.00 82.59           O  
ANISOU10606  O   GLN D  22    11901   9248  10229    291     46     98       O  
ATOM  10607  CB  GLN D  22      10.612 -33.069  -5.137  1.00 77.45           C  
ANISOU10607  CB  GLN D  22    11189   8628   9607     86     62     86       C  
ATOM  10608  CG  GLN D  22       9.159 -33.351  -4.782  1.00 78.78           C  
ANISOU10608  CG  GLN D  22    11374   8786   9771     -7     59     72       C  
ATOM  10609  CD  GLN D  22       8.594 -34.574  -5.474  1.00 82.47           C  
ANISOU10609  CD  GLN D  22    11919   9200  10214    -28     38     46       C  
ATOM  10610  OE1 GLN D  22       8.830 -34.807  -6.663  1.00 81.32           O  
ANISOU10610  OE1 GLN D  22    11785   9051  10059     20     31     26       O  
ATOM  10611  NE2 GLN D  22       7.829 -35.362  -4.729  1.00 85.63           N  
ANISOU10611  NE2 GLN D  22    12372   9559  10604   -102     28     45       N  
ATOM  10612  N   TRP D  23      13.594 -32.913  -4.282  1.00 77.50           N  
ANISOU10612  N   TRP D  23    11185   8641   9618    234     64    132       N  
ATOM  10613  CA  TRP D  23      14.901 -32.283  -4.492  1.00 79.90           C  
ANISOU10613  CA  TRP D  23    11439   8985   9933    309     74    147       C  
ATOM  10614  C   TRP D  23      15.541 -31.976  -3.167  1.00 81.75           C  
ANISOU10614  C   TRP D  23    11654   9227  10178    309     74    170       C  
ATOM  10615  O   TRP D  23      14.849 -31.701  -2.183  1.00 82.82           O  
ANISOU10615  O   TRP D  23    11781   9362  10323    245     76    175       O  
ATOM  10616  CB  TRP D  23      14.744 -31.020  -5.358  1.00 82.47           C  
ANISOU10616  CB  TRP D  23    11678   9371  10282    313     96    146       C  
ATOM  10617  CG  TRP D  23      15.832 -29.958  -5.257  1.00 81.82           C  
ANISOU10617  CG  TRP D  23    11521   9341  10224    357    112    167       C  
ATOM  10618  CD1 TRP D  23      15.793 -28.762  -4.529  1.00 80.40           C  
ANISOU10618  CD1 TRP D  23    11272   9199  10076    325    126    181       C  
ATOM  10619  CD2 TRP D  23      17.138 -29.944  -5.934  1.00 78.32           C  
ANISOU10619  CD2 TRP D  23    11060   8922   9776    440    117    177       C  
ATOM  10620  NE1 TRP D  23      16.954 -28.043  -4.694  1.00 77.16           N  
ANISOU10620  NE1 TRP D  23    10806   8828   9683    375    138    198       N  
ATOM  10621  CE2 TRP D  23      17.803 -28.693  -5.522  1.00 79.20           C  
ANISOU10621  CE2 TRP D  23    11087   9084   9919    444    134    197       C  
ATOM  10622  CE3 TRP D  23      17.803 -30.811  -6.798  1.00 79.30           C  
ANISOU10622  CE3 TRP D  23    11226   9034   9871    510    109    169       C  
ATOM  10623  CZ2 TRP D  23      19.074 -28.353  -5.970  1.00 80.29           C  
ANISOU10623  CZ2 TRP D  23    11183   9260  10061    510    144    212       C  
ATOM  10624  CZ3 TRP D  23      19.087 -30.458  -7.242  1.00 82.85           C  
ANISOU10624  CZ3 TRP D  23    11631   9526  10321    582    119    184       C  
ATOM  10625  CH2 TRP D  23      19.705 -29.259  -6.837  1.00 83.95           C  
ANISOU10625  CH2 TRP D  23    11687   9716  10492    580    138    206       C  
ATOM  10626  N   PHE D  24      16.869 -32.052  -3.127  1.00 79.72           N  
ANISOU10626  N   PHE D  24    11390   8982   9917    382     72    182       N  
ATOM  10627  CA  PHE D  24      17.642 -31.698  -1.943  1.00 78.18           C  
ANISOU10627  CA  PHE D  24    11169   8804   9731    393     71    201       C  
ATOM  10628  C   PHE D  24      18.961 -31.066  -2.386  1.00 77.10           C  
ANISOU10628  C   PHE D  24    10969   8718   9605    465     80    210       C  
ATOM  10629  O   PHE D  24      19.479 -31.382  -3.462  1.00 81.54           O  
ANISOU10629  O   PHE D  24    11539   9287  10154    523     81    205       O  
ATOM  10630  CB  PHE D  24      17.882 -32.932  -1.043  1.00 81.04           C  
ANISOU10630  CB  PHE D  24    11618   9110  10062    403     48    206       C  
ATOM  10631  CG  PHE D  24      19.167 -33.674  -1.334  1.00 87.17           C  
ANISOU10631  CG  PHE D  24    12430   9877  10814    496     35    209       C  
ATOM  10632  CD1 PHE D  24      19.276 -34.515  -2.445  1.00 86.73           C  
ANISOU10632  CD1 PHE D  24    12426   9791  10734    542     26    193       C  
ATOM  10633  CD2 PHE D  24      20.275 -33.532  -0.495  1.00 88.66           C  
ANISOU10633  CD2 PHE D  24    12596  10087  11001    542     30    224       C  
ATOM  10634  CE1 PHE D  24      20.463 -35.188  -2.716  1.00 86.23           C  
ANISOU10634  CE1 PHE D  24    12394   9724  10645    634     13    194       C  
ATOM  10635  CE2 PHE D  24      21.463 -34.206  -0.763  1.00 88.31           C  
ANISOU10635  CE2 PHE D  24    12579  10041  10930    632     17    224       C  
ATOM  10636  CZ  PHE D  24      21.556 -35.035  -1.874  1.00 86.71           C  
ANISOU10636  CZ  PHE D  24    12430   9811  10703    680      9    210       C  
ATOM  10637  N   CYS D  25      19.484 -30.162  -1.566  1.00 70.47           N  
ANISOU10637  N   CYS D  25    10067   7918   8790    460     87    224       N  
ATOM  10638  CA  CYS D  25      20.839 -29.644  -1.733  1.00 68.16           C  
ANISOU10638  CA  CYS D  25     9716   7672   8507    522     93    235       C  
ATOM  10639  C   CYS D  25      21.287 -29.130  -0.389  1.00 63.57           C  
ANISOU10639  C   CYS D  25     9100   7110   7941    508     88    245       C  
ATOM  10640  O   CYS D  25      20.455 -28.899   0.495  1.00 58.96           O  
ANISOU10640  O   CYS D  25     8523   6513   7366    446     86    244       O  
ATOM  10641  CB  CYS D  25      20.917 -28.519  -2.782  1.00 71.00           C  
ANISOU10641  CB  CYS D  25     9999   8083   8895    525    117    238       C  
ATOM  10642  SG  CYS D  25      20.142 -26.939  -2.328  1.00 81.40           S  
ANISOU10642  SG  CYS D  25    11239   9431  10259    448    134    242       S  
ATOM  10643  N   ASN D  26      22.596 -28.952  -0.237  1.00 62.71           N  
ANISOU10643  N   ASN D  26     8954   7038   7834    565     86    254       N  
ATOM  10644  CA  ASN D  26      23.134 -28.304   0.950  1.00 66.26           C  
ANISOU10644  CA  ASN D  26     9357   7517   8302    555     81    261       C  
ATOM  10645  C   ASN D  26      24.208 -27.269   0.624  1.00 65.88           C  
ANISOU10645  C   ASN D  26     9216   7532   8282    584     94    269       C  
ATOM  10646  O   ASN D  26      25.154 -27.538  -0.120  1.00 65.10           O  
ANISOU10646  O   ASN D  26     9105   7459   8171    647     98    272       O  
ATOM  10647  CB  ASN D  26      23.589 -29.329   2.018  1.00 70.10           C  
ANISOU10647  CB  ASN D  26     9904   7975   8754    586     57    263       C  
ATOM  10648  CG  ASN D  26      24.988 -29.875   1.774  1.00 72.72           C  
ANISOU10648  CG  ASN D  26    10236   8330   9063    676     48    266       C  
ATOM  10649  OD1 ASN D  26      25.257 -30.500   0.751  1.00 75.01           O  
ANISOU10649  OD1 ASN D  26    10555   8611   9332    725     49    262       O  
ATOM  10650  ND2 ASN D  26      25.881 -29.654   2.734  1.00 74.71           N  
ANISOU10650  ND2 ASN D  26    10455   8614   9315    701     36    270       N  
ATOM  10651  N   SER D  27      24.015 -26.067   1.156  1.00 65.10           N  
ANISOU10651  N   SER D  27     9053   7459   8221    534    102    270       N  
ATOM  10652  CA  SER D  27      25.015 -25.014   1.079  1.00 65.12           C  
ANISOU10652  CA  SER D  27     8968   7519   8256    548    111    278       C  
ATOM  10653  C   SER D  27      25.785 -24.993   2.392  1.00 62.98           C  
ANISOU10653  C   SER D  27     8680   7266   7984    560     92    276       C  
ATOM  10654  O   SER D  27      25.448 -25.734   3.315  1.00 64.01           O  
ANISOU10654  O   SER D  27     8868   7363   8089    556     74    271       O  
ATOM  10655  CB  SER D  27      24.357 -23.658   0.805  1.00 64.45           C  
ANISOU10655  CB  SER D  27     8825   7447   8214    488    130    280       C  
ATOM  10656  OG  SER D  27      23.505 -23.274   1.866  1.00 61.76           O  
ANISOU10656  OG  SER D  27     8492   7088   7886    431    121    271       O  
ATOM  10657  N   SER D  28      26.805 -24.140   2.475  1.00 62.54           N  
ANISOU10657  N   SER D  28     8545   7262   7955    573     96    280       N  
ATOM  10658  CA  SER D  28      27.684 -24.063   3.650  1.00 61.88           C  
ANISOU10658  CA  SER D  28     8435   7206   7870    590     76    276       C  
ATOM  10659  C   SER D  28      26.991 -23.669   4.964  1.00 63.23           C  
ANISOU10659  C   SER D  28     8613   7359   8052    537     61    265       C  
ATOM  10660  O   SER D  28      27.622 -23.703   6.022  1.00 61.28           O  
ANISOU10660  O   SER D  28     8352   7131   7798    553     42    259       O  
ATOM  10661  CB  SER D  28      28.855 -23.118   3.376  1.00 60.49           C  
ANISOU10661  CB  SER D  28     8165   7093   7726    604     84    281       C  
ATOM  10662  OG  SER D  28      28.390 -21.835   2.991  1.00 60.97           O  
ANISOU10662  OG  SER D  28     8172   7160   7833    545    103    285       O  
ATOM  10663  N   ASP D  29      25.709 -23.301   4.897  1.00 65.54           N  
ANISOU10663  N   ASP D  29     8923   7618   8357    478     71    262       N  
ATOM  10664  CA  ASP D  29      24.956 -22.873   6.087  1.00 67.15           C  
ANISOU10664  CA  ASP D  29     9132   7811   8570    427     59    252       C  
ATOM  10665  C   ASP D  29      23.495 -23.341   6.138  1.00 66.52           C  
ANISOU10665  C   ASP D  29     9115   7685   8472    384     63    249       C  
ATOM  10666  O   ASP D  29      22.765 -23.002   7.073  1.00 68.04           O  
ANISOU10666  O   ASP D  29     9312   7871   8668    341     56    241       O  
ATOM  10667  CB  ASP D  29      25.034 -21.345   6.263  1.00 70.04           C  
ANISOU10667  CB  ASP D  29     9417   8208   8986    386     65    245       C  
ATOM  10668  CG  ASP D  29      24.223 -20.571   5.215  1.00 70.87           C  
ANISOU10668  CG  ASP D  29     9503   8303   9119    348     88    249       C  
ATOM  10669  OD1 ASP D  29      23.702 -21.173   4.253  1.00 70.04           O  
ANISOU10669  OD1 ASP D  29     9438   8176   8997    356    101    256       O  
ATOM  10670  OD2 ASP D  29      24.108 -19.337   5.362  1.00 71.24           O  
ANISOU10670  OD2 ASP D  29     9497   8365   9206    312     92    244       O  
ATOM  10671  N   ALA D  30      23.073 -24.116   5.140  1.00 63.45           N  
ANISOU10671  N   ALA D  30     8775   7268   8064    396     73    255       N  
ATOM  10672  CA  ALA D  30      21.699 -24.612   5.080  1.00 62.80           C  
ANISOU10672  CA  ALA D  30     8751   7144   7965    352     77    251       C  
ATOM  10673  C   ALA D  30      21.589 -25.958   4.372  1.00 64.77           C  
ANISOU10673  C   ALA D  30     9076   7355   8177    383     75    256       C  
ATOM  10674  O   ALA D  30      22.363 -26.247   3.456  1.00 64.58           O  
ANISOU10674  O   ALA D  30     9049   7340   8148    434     79    260       O  
ATOM  10675  CB  ALA D  30      20.797 -23.593   4.395  1.00 59.02           C  
ANISOU10675  CB  ALA D  30     8233   6674   7518    305     95    246       C  
ATOM  10676  N   ILE D  31      20.635 -26.781   4.809  1.00 66.13           N  
ANISOU10676  N   ILE D  31     9318   7485   8322    351     68    254       N  
ATOM  10677  CA  ILE D  31      20.145 -27.883   3.978  1.00 68.63           C  
ANISOU10677  CA  ILE D  31     9706   7758   8611    358     69    253       C  
ATOM  10678  C   ILE D  31      18.744 -27.507   3.486  1.00 68.50           C  
ANISOU10678  C   ILE D  31     9687   7732   8607    293     82    245       C  
ATOM  10679  O   ILE D  31      17.926 -26.991   4.257  1.00 66.90           O  
ANISOU10679  O   ILE D  31     9468   7537   8413    238     84    241       O  
ATOM  10680  CB  ILE D  31      20.194 -29.281   4.670  1.00 70.95           C  
ANISOU10680  CB  ILE D  31    10091   8003   8862    375     50    260       C  
ATOM  10681  CG1 ILE D  31      19.140 -29.427   5.773  1.00 73.16           C  
ANISOU10681  CG1 ILE D  31    10403   8262   9132    310     46    262       C  
ATOM  10682  CG2 ILE D  31      21.586 -29.594   5.209  1.00 70.49           C  
ANISOU10682  CG2 ILE D  31    10032   7960   8789    446     35    267       C  
ATOM  10683  CD1 ILE D  31      17.907 -30.205   5.351  1.00 75.92           C  
ANISOU10683  CD1 ILE D  31    10817   8564   9463    261     50    259       C  
ATOM  10684  N   ILE D  32      18.489 -27.733   2.197  1.00 68.26           N  
ANISOU10684  N   ILE D  32     9668   7692   8575    304     91    239       N  
ATOM  10685  CA  ILE D  32      17.225 -27.338   1.570  1.00 68.76           C  
ANISOU10685  CA  ILE D  32     9722   7755   8648    250    104    229       C  
ATOM  10686  C   ILE D  32      16.595 -28.508   0.827  1.00 70.60           C  
ANISOU10686  C   ILE D  32    10029   7943   8852    246     98    220       C  
ATOM  10687  O   ILE D  32      17.238 -29.132  -0.021  1.00 74.75           O  
ANISOU10687  O   ILE D  32    10583   8456   9363    300     95    220       O  
ATOM  10688  CB  ILE D  32      17.408 -26.134   0.608  1.00 65.55           C  
ANISOU10688  CB  ILE D  32     9240   7390   8273    261    122    228       C  
ATOM  10689  CG1 ILE D  32      17.800 -24.881   1.397  1.00 64.89           C  
ANISOU10689  CG1 ILE D  32     9086   7345   8224    249    126    233       C  
ATOM  10690  CG2 ILE D  32      16.139 -25.879  -0.197  1.00 61.95           C  
ANISOU10690  CG2 ILE D  32     8783   6933   7821    219    133    216       C  
ATOM  10691  CD1 ILE D  32      18.384 -23.764   0.564  1.00 66.89           C  
ANISOU10691  CD1 ILE D  32     9268   7635   8509    270    142    239       C  
ATOM  10692  N   SER D  33      15.340 -28.803   1.159  1.00 67.55           N  
ANISOU10692  N   SER D  33     9674   7536   8456    181     97    213       N  
ATOM  10693  CA  SER D  33      14.576 -29.814   0.438  1.00 66.67           C  
ANISOU10693  CA  SER D  33     9628   7382   8321    163     92    201       C  
ATOM  10694  C   SER D  33      13.135 -29.356   0.250  1.00 65.17           C  
ANISOU10694  C   SER D  33     9415   7206   8138     92    101    187       C  
ATOM  10695  O   SER D  33      12.658 -28.486   0.987  1.00 64.99           O  
ANISOU10695  O   SER D  33     9344   7216   8132     53    109    189       O  
ATOM  10696  CB  SER D  33      14.613 -31.163   1.171  1.00 65.77           C  
ANISOU10696  CB  SER D  33     9603   7211   8174    159     74    208       C  
ATOM  10697  OG  SER D  33      13.393 -31.423   1.849  1.00 63.40           O  
ANISOU10697  OG  SER D  33     9329   6895   7865     80     74    206       O  
ATOM  10698  N   TYR D  34      12.457 -29.940  -0.741  1.00 60.08           N  
ANISOU10698  N   TYR D  34     8805   6541   7480     79     99    171       N  
ATOM  10699  CA  TYR D  34      11.020 -29.748  -0.919  1.00 57.09           C  
ANISOU10699  CA  TYR D  34     8416   6173   7102     10    105    155       C  
ATOM  10700  C   TYR D  34      10.307 -31.041  -1.312  1.00 57.38           C  
ANISOU10700  C   TYR D  34     8530   6159   7110    -21     91    142       C  
ATOM  10701  O   TYR D  34      10.913 -31.959  -1.864  1.00 56.15           O  
ANISOU10701  O   TYR D  34     8433   5962   6939     21     79    139       O  
ATOM  10702  CB  TYR D  34      10.718 -28.621  -1.918  1.00 55.65           C  
ANISOU10702  CB  TYR D  34     8163   6040   6940     20    119    144       C  
ATOM  10703  CG  TYR D  34      10.731 -29.006  -3.391  1.00 56.52           C  
ANISOU10703  CG  TYR D  34     8291   6142   7040     54    118    129       C  
ATOM  10704  CD1 TYR D  34      11.913 -28.989  -4.131  1.00 56.27           C  
ANISOU10704  CD1 TYR D  34     8254   6113   7010    130    120    137       C  
ATOM  10705  CD2 TYR D  34       9.551 -29.358  -4.050  1.00 55.58           C  
ANISOU10705  CD2 TYR D  34     8190   6019   6908     12    114    106       C  
ATOM  10706  CE1 TYR D  34      11.919 -29.330  -5.478  1.00 57.34           C  
ANISOU10706  CE1 TYR D  34     8406   6246   7133    166    119    123       C  
ATOM  10707  CE2 TYR D  34       9.549 -29.698  -5.394  1.00 56.14           C  
ANISOU10707  CE2 TYR D  34     8276   6085   6967     46    111     90       C  
ATOM  10708  CZ  TYR D  34      10.733 -29.684  -6.105  1.00 56.53           C  
ANISOU10708  CZ  TYR D  34     8324   6137   7018    125    113     98       C  
ATOM  10709  OH  TYR D  34      10.729 -30.024  -7.441  1.00 54.97           O  
ANISOU10709  OH  TYR D  34     8142   5938   6804    163    110     81       O  
ATOM  10710  N   SER D  35       9.018 -31.094  -0.998  1.00 57.80           N  
ANISOU10710  N   SER D  35     8584   6218   7158    -98     93    131       N  
ATOM  10711  CA  SER D  35       8.123 -32.149  -1.446  1.00 57.77           C  
ANISOU10711  CA  SER D  35     8641   6175   7133   -144     82    114       C  
ATOM  10712  C   SER D  35       6.859 -31.445  -1.898  1.00 58.55           C  
ANISOU10712  C   SER D  35     8683   6322   7238   -196     92     93       C  
ATOM  10713  O   SER D  35       6.722 -30.244  -1.682  1.00 61.38           O  
ANISOU10713  O   SER D  35     8968   6736   7616   -195    107     96       O  
ATOM  10714  CB  SER D  35       7.814 -33.107  -0.301  1.00 58.40           C  
ANISOU10714  CB  SER D  35     8785   6209   7193   -197     74    129       C  
ATOM  10715  OG  SER D  35       7.126 -32.449   0.750  1.00 57.75           O  
ANISOU10715  OG  SER D  35     8657   6167   7116   -253     86    137       O  
ATOM  10716  N   TYR D  36       5.941 -32.166  -2.530  1.00 59.00           N  
ANISOU10716  N   TYR D  36     8775   6361   7280   -240     83     71       N  
ATOM  10717  CA  TYR D  36       4.651 -31.580  -2.870  1.00 60.79           C  
ANISOU10717  CA  TYR D  36     8949   6639   7510   -294     91     49       C  
ATOM  10718  C   TYR D  36       3.785 -31.445  -1.616  1.00 60.78           C  
ANISOU10718  C   TYR D  36     8930   6658   7503   -370     99     58       C  
ATOM  10719  O   TYR D  36       4.078 -32.053  -0.590  1.00 61.11           O  
ANISOU10719  O   TYR D  36     9017   6664   7537   -390     95     79       O  
ATOM  10720  CB  TYR D  36       3.929 -32.400  -3.942  1.00 64.13           C  
ANISOU10720  CB  TYR D  36     9410   7039   7915   -318     77     18       C  
ATOM  10721  CG  TYR D  36       4.688 -32.572  -5.244  1.00 66.48           C  
ANISOU10721  CG  TYR D  36     9726   7321   8212   -241     69      6       C  
ATOM  10722  CD1 TYR D  36       4.960 -33.847  -5.748  1.00 68.22           C  
ANISOU10722  CD1 TYR D  36    10029   7475   8413   -230     48     -5       C  
ATOM  10723  CD2 TYR D  36       5.127 -31.467  -5.981  1.00 66.86           C  
ANISOU10723  CD2 TYR D  36     9709   7419   8275   -180     82      6       C  
ATOM  10724  CE1 TYR D  36       5.644 -34.020  -6.941  1.00 66.77           C  
ANISOU10724  CE1 TYR D  36     9862   7282   8224   -155     40    -18       C  
ATOM  10725  CE2 TYR D  36       5.817 -31.634  -7.175  1.00 67.65           C  
ANISOU10725  CE2 TYR D  36     9823   7511   8370   -109     77     -2       C  
ATOM  10726  CZ  TYR D  36       6.073 -32.914  -7.645  1.00 68.72           C  
ANISOU10726  CZ  TYR D  36    10040   7586   8484    -95     56    -16       C  
ATOM  10727  OH  TYR D  36       6.754 -33.095  -8.824  1.00 70.78           O  
ANISOU10727  OH  TYR D  36    10313   7842   8735    -20     51    -26       O  
ATOM  10728  N   CYS D  37       2.734 -30.633  -1.699  1.00 63.97           N  
ANISOU10728  N   CYS D  37     9269   7124   7911   -409    109     41       N  
ATOM  10729  CA  CYS D  37       1.820 -30.421  -0.576  1.00 66.58           C  
ANISOU10729  CA  CYS D  37     9573   7488   8234   -480    118     46       C  
ATOM  10730  C   CYS D  37       0.879 -31.605  -0.415  1.00 67.36           C  
ANISOU10730  C   CYS D  37     9725   7558   8310   -562    110     39       C  
ATOM  10731  O   CYS D  37       0.610 -32.327  -1.374  1.00 68.11           O  
ANISOU10731  O   CYS D  37     9857   7624   8397   -572     97     18       O  
ATOM  10732  CB  CYS D  37       1.019 -29.122  -0.757  1.00 68.71           C  
ANISOU10732  CB  CYS D  37     9753   7839   8513   -485    130     29       C  
ATOM  10733  SG  CYS D  37       2.035 -27.625  -0.677  1.00 76.31           S  
ANISOU10733  SG  CYS D  37    10653   8834   9505   -403    141     43       S  
ATOM  10734  N   ASP D  38       0.388 -31.799   0.805  1.00 71.81           N  
ANISOU10734  N   ASP D  38    10292   8129   8861   -623    117     56       N  
ATOM  10735  CA  ASP D  38      -0.583 -32.852   1.101  1.00 75.32           C  
ANISOU10735  CA  ASP D  38    10781   8553   9284   -714    113     53       C  
ATOM  10736  C   ASP D  38      -1.886 -32.668   0.317  1.00 78.00           C  
ANISOU10736  C   ASP D  38    11073   8944   9616   -765    113     17       C  
ATOM  10737  O   ASP D  38      -2.506 -33.646  -0.099  1.00 76.84           O  
ANISOU10737  O   ASP D  38    10972   8766   9457   -823    102      3       O  
ATOM  10738  CB  ASP D  38      -0.877 -32.902   2.605  1.00 76.35           C  
ANISOU10738  CB  ASP D  38    10910   8698   9401   -766    125     81       C  
ATOM  10739  CG  ASP D  38       0.309 -33.405   3.428  1.00 76.76           C  
ANISOU10739  CG  ASP D  38    11025   8689   9451   -727    121    117       C  
ATOM  10740  OD1 ASP D  38       1.447 -33.441   2.906  1.00 74.75           O  
ANISOU10740  OD1 ASP D  38    10797   8395   9210   -649    111    119       O  
ATOM  10741  OD2 ASP D  38       0.097 -33.761   4.610  1.00 76.74           O  
ANISOU10741  OD2 ASP D  38    11044   8681   9431   -772    128    143       O  
ATOM  10742  N   HIS D  39      -2.286 -31.414   0.111  1.00 82.94           N  
ANISOU10742  N   HIS D  39    11612   9648  10251   -743    124      2       N  
ATOM  10743  CA  HIS D  39      -3.525 -31.094  -0.602  1.00 83.62           C  
ANISOU10743  CA  HIS D  39    11644   9797  10329   -782    124    -33       C  
ATOM  10744  C   HIS D  39      -3.409 -31.088  -2.107  1.00 77.27           C  
ANISOU10744  C   HIS D  39    10842   8985   9531   -737    111    -62       C  
ATOM  10745  O   HIS D  39      -4.413 -31.237  -2.801  1.00 77.63           O  
ANISOU10745  O   HIS D  39    10866   9063   9564   -777    105    -94       O  
ATOM  10746  CB  HIS D  39      -4.100 -29.764  -0.111  1.00 94.31           C  
ANISOU10746  CB  HIS D  39    12907  11241  11685   -777    140    -38       C  
ATOM  10747  CG  HIS D  39      -4.596 -29.801   1.323  1.00106.82           C  
ANISOU10747  CG  HIS D  39    14479  12853  13254   -837    153    -18       C  
ATOM  10748  ND1 HIS D  39      -4.228 -28.886   2.242  1.00109.51           N  
ANISOU10748  ND1 HIS D  39    14781  13226  13601   -804    165      0       N  
ATOM  10749  CD2 HIS D  39      -5.451 -30.692   1.977  1.00109.32           C  
ANISOU10749  CD2 HIS D  39    14818  13169  13547   -931    156    -12       C  
ATOM  10750  CE1 HIS D  39      -4.818 -29.171   3.421  1.00106.95           C  
ANISOU10750  CE1 HIS D  39    14454  12925  13256   -869    175     14       C  
ATOM  10751  NE2 HIS D  39      -5.565 -30.276   3.258  1.00108.76           N  
ANISOU10751  NE2 HIS D  39    14721  13136  13467   -948    171      9       N  
ATOM  10752  N   LEU D  40      -2.198 -30.919  -2.633  1.00 72.96           N  
ANISOU10752  N   LEU D  40    10318   8400   9000   -652    107    -52       N  
ATOM  10753  CA  LEU D  40      -2.011 -30.746  -4.078  1.00 72.74           C  
ANISOU10753  CA  LEU D  40    10284   8375   8977   -597     98    -77       C  
ATOM  10754  C   LEU D  40      -0.666 -31.284  -4.578  1.00 74.88           C  
ANISOU10754  C   LEU D  40    10617   8576   9256   -527     89    -63       C  
ATOM  10755  O   LEU D  40       0.377 -31.046  -3.959  1.00 75.17           O  
ANISOU10755  O   LEU D  40    10664   8591   9305   -483     95    -34       O  
ATOM  10756  CB  LEU D  40      -2.160 -29.268  -4.450  1.00 69.85           C  
ANISOU10756  CB  LEU D  40     9832   8082   8622   -549    111    -84       C  
ATOM  10757  CG  LEU D  40      -2.688 -28.922  -5.841  1.00 71.59           C  
ANISOU10757  CG  LEU D  40    10021   8342   8837   -523    105   -118       C  
ATOM  10758  CD1 LEU D  40      -4.200 -29.110  -5.918  1.00 72.99           C  
ANISOU10758  CD1 LEU D  40    10168   8571   8994   -599    101   -150       C  
ATOM  10759  CD2 LEU D  40      -2.301 -27.495  -6.208  1.00 70.89           C  
ANISOU10759  CD2 LEU D  40     9870   8300   8764   -449    119   -111       C  
ATOM  10760  N   LYS D  41      -0.694 -31.991  -5.710  1.00 73.80           N  
ANISOU10760  N   LYS D  41    10521   8410   9110   -514     72    -88       N  
ATOM  10761  CA  LYS D  41       0.494 -32.689  -6.214  1.00 72.15           C  
ANISOU10761  CA  LYS D  41    10378   8133   8901   -450     60    -80       C  
ATOM  10762  C   LYS D  41       0.795 -32.526  -7.716  1.00 73.51           C  
ANISOU10762  C   LYS D  41    10544   8315   9070   -381     53   -104       C  
ATOM  10763  O   LYS D  41       1.311 -33.451  -8.344  1.00 77.78           O  
ANISOU10763  O   LYS D  41    11150   8800   9600   -352     35   -114       O  
ATOM  10764  CB  LYS D  41       0.424 -34.176  -5.843  1.00 70.30           C  
ANISOU10764  CB  LYS D  41    10237   7819   8651   -502     42    -80       C  
ATOM  10765  CG  LYS D  41       0.869 -34.489  -4.424  1.00 71.80           C  
ANISOU10765  CG  LYS D  41    10461   7974   8844   -526     48    -42       C  
ATOM  10766  CD  LYS D  41       1.322 -35.937  -4.294  1.00 76.15           C  
ANISOU10766  CD  LYS D  41    11119   8430   9381   -535     28    -36       C  
ATOM  10767  CE  LYS D  41       2.225 -36.158  -3.084  1.00 75.36           C  
ANISOU10767  CE  LYS D  41    11057   8292   9282   -517     33      4       C  
ATOM  10768  NZ  LYS D  41       1.521 -35.944  -1.787  1.00 72.44           N  
ANISOU10768  NZ  LYS D  41    10663   7949   8910   -593     48     25       N  
ATOM  10769  N   PHE D  42       0.498 -31.358  -8.285  1.00 73.37           N  
ANISOU10769  N   PHE D  42    10450   8367   9059   -351     65   -112       N  
ATOM  10770  CA  PHE D  42       0.841 -31.076  -9.685  1.00 70.41           C  
ANISOU10770  CA  PHE D  42    10063   8008   8679   -279     62   -129       C  
ATOM  10771  C   PHE D  42       2.357 -30.920  -9.874  1.00 68.95           C  
ANISOU10771  C   PHE D  42     9895   7795   8505   -191     69   -101       C  
ATOM  10772  O   PHE D  42       3.006 -30.253  -9.071  1.00 68.59           O  
ANISOU10772  O   PHE D  42     9822   7757   8478   -173     84    -70       O  
ATOM  10773  CB  PHE D  42       0.100 -29.834 -10.180  1.00 71.54           C  
ANISOU10773  CB  PHE D  42    10123   8232   8826   -271     75   -142       C  
ATOM  10774  CG  PHE D  42      -1.391 -30.011 -10.259  1.00 76.04           C  
ANISOU10774  CG  PHE D  42    10672   8840   9380   -346     66   -176       C  
ATOM  10775  CD1 PHE D  42      -2.240 -29.231  -9.485  1.00 78.04           C  
ANISOU10775  CD1 PHE D  42    10864   9150   9637   -392     79   -174       C  
ATOM  10776  CD2 PHE D  42      -1.950 -30.963 -11.104  1.00 80.22           C  
ANISOU10776  CD2 PHE D  42    11239   9352   9888   -369     44   -213       C  
ATOM  10777  CE1 PHE D  42      -3.616 -29.390  -9.554  1.00 79.21           C  
ANISOU10777  CE1 PHE D  42    10985   9341   9768   -460     71   -207       C  
ATOM  10778  CE2 PHE D  42      -3.326 -31.129 -11.182  1.00 83.56           C  
ANISOU10778  CE2 PHE D  42    11637   9815  10297   -442     35   -247       C  
ATOM  10779  CZ  PHE D  42      -4.160 -30.342 -10.403  1.00 83.48           C  
ANISOU10779  CZ  PHE D  42    11561   9867  10290   -488     50   -243       C  
ATOM  10780  N   PRO D  43       2.927 -31.530 -10.937  1.00 69.17           N  
ANISOU10780  N   PRO D  43     9965   7796   8520   -135     56   -115       N  
ATOM  10781  CA  PRO D  43       4.396 -31.606 -11.045  1.00 67.62           C  
ANISOU10781  CA  PRO D  43     9792   7570   8328    -55     61    -89       C  
ATOM  10782  C   PRO D  43       5.120 -30.308 -11.449  1.00 61.86           C  
ANISOU10782  C   PRO D  43     8995   6894   7615     12     84    -66       C  
ATOM  10783  O   PRO D  43       4.705 -29.625 -12.382  1.00 61.04           O  
ANISOU10783  O   PRO D  43     8847   6838   7508     35     91    -79       O  
ATOM  10784  CB  PRO D  43       4.618 -32.709 -12.094  1.00 66.53           C  
ANISOU10784  CB  PRO D  43     9721   7392   8165    -19     38   -116       C  
ATOM  10785  CG  PRO D  43       3.386 -32.694 -12.932  1.00 66.54           C  
ANISOU10785  CG  PRO D  43     9703   7425   8152    -55     29   -156       C  
ATOM  10786  CD  PRO D  43       2.253 -32.193 -12.073  1.00 68.11           C  
ANISOU10786  CD  PRO D  43     9857   7658   8362   -141     37   -156       C  
ATOM  10787  N   ILE D  44       6.187 -29.990 -10.717  1.00 58.49           N  
ANISOU10787  N   ILE D  44     8561   6456   7206     43     96    -32       N  
ATOM  10788  CA  ILE D  44       7.129 -28.926 -11.064  1.00 57.52           C  
ANISOU10788  CA  ILE D  44     8383   6369   7099    109    117     -6       C  
ATOM  10789  C   ILE D  44       8.526 -29.421 -10.745  1.00 56.27           C  
ANISOU10789  C   ILE D  44     8260   6176   6943    162    115     16       C  
ATOM  10790  O   ILE D  44       8.750 -30.057  -9.716  1.00 58.71           O  
ANISOU10790  O   ILE D  44     8609   6445   7253    135    105     24       O  
ATOM  10791  CB  ILE D  44       6.951 -27.633 -10.218  1.00 58.44           C  
ANISOU10791  CB  ILE D  44     8433   6527   7245     83    136     14       C  
ATOM  10792  CG1 ILE D  44       5.567 -27.543  -9.590  1.00 60.22           C  
ANISOU10792  CG1 ILE D  44     8644   6765   7468      3    131     -3       C  
ATOM  10793  CG2 ILE D  44       7.319 -26.377 -11.005  1.00 55.21           C  
ANISOU10793  CG2 ILE D  44     7960   6166   6849    135    156     29       C  
ATOM  10794  CD1 ILE D  44       5.535 -28.068  -8.172  1.00 62.40           C  
ANISOU10794  CD1 ILE D  44     8950   7008   7749    -49    125      7       C  
ATOM  10795  N   SER D  45       9.470 -29.117 -11.620  1.00 55.39           N  
ANISOU10795  N   SER D  45     8131   6085   6829    237    125     27       N  
ATOM  10796  CA  SER D  45      10.863 -29.312 -11.301  1.00 55.57           C  
ANISOU10796  CA  SER D  45     8165   6092   6855    292    128     52       C  
ATOM  10797  C   SER D  45      11.453 -27.941 -11.049  1.00 57.78           C  
ANISOU10797  C   SER D  45     8369   6419   7166    309    153     83       C  
ATOM  10798  O   SER D  45      11.663 -27.158 -11.983  1.00 57.68           O  
ANISOU10798  O   SER D  45     8311   6448   7157    348    170     91       O  
ATOM  10799  CB  SER D  45      11.596 -30.024 -12.437  1.00 56.11           C  
ANISOU10799  CB  SER D  45     8269   6152   6896    368    121     42       C  
ATOM  10800  OG  SER D  45      10.947 -31.238 -12.777  1.00 58.88           O  
ANISOU10800  OG  SER D  45     8692   6458   7220    350     95      8       O  
ATOM  10801  N   ILE D  46      11.674 -27.637  -9.775  1.00 58.49           N  
ANISOU10801  N   ILE D  46     8445   6502   7277    277    155    100       N  
ATOM  10802  CA  ILE D  46      12.368 -26.416  -9.392  1.00 57.52           C  
ANISOU10802  CA  ILE D  46     8254   6414   7184    291    175    129       C  
ATOM  10803  C   ILE D  46      13.697 -26.747  -8.709  1.00 58.76           C  
ANISOU10803  C   ILE D  46     8422   6556   7346    328    172    149       C  
ATOM  10804  O   ILE D  46      13.802 -27.719  -7.956  1.00 61.02           O  
ANISOU10804  O   ILE D  46     8762   6801   7618    316    154    144       O  
ATOM  10805  CB  ILE D  46      11.478 -25.473  -8.545  1.00 56.50           C  
ANISOU10805  CB  ILE D  46     8084   6303   7080    227    180    129       C  
ATOM  10806  CG1 ILE D  46      12.157 -24.113  -8.363  1.00 58.46           C  
ANISOU10806  CG1 ILE D  46     8264   6586   7361    245    200    155       C  
ATOM  10807  CG2 ILE D  46      11.136 -26.095  -7.202  1.00 58.56           C  
ANISOU10807  CG2 ILE D  46     8379   6530   7337    175    166    125       C  
ATOM  10808  CD1 ILE D  46      11.235 -22.994  -7.930  1.00 61.95           C  
ANISOU10808  CD1 ILE D  46     8660   7053   7824    198    207    153       C  
ATOM  10809  N   SER D  47      14.706 -25.928  -8.994  1.00 59.13           N  
ANISOU10809  N   SER D  47     8417   6639   7411    372    189    172       N  
ATOM  10810  CA  SER D  47      16.078 -26.156  -8.564  1.00 57.40           C  
ANISOU10810  CA  SER D  47     8195   6419   7193    417    188    191       C  
ATOM  10811  C   SER D  47      16.828 -24.819  -8.535  1.00 60.61           C  
ANISOU10811  C   SER D  47     8523   6871   7633    429    210    218       C  
ATOM  10812  O   SER D  47      16.465 -23.886  -9.256  1.00 62.67           O  
ANISOU10812  O   SER D  47     8742   7161   7908    424    228    224       O  
ATOM  10813  CB  SER D  47      16.746 -27.130  -9.538  1.00 57.12           C  
ANISOU10813  CB  SER D  47     8201   6377   7125    486    182    185       C  
ATOM  10814  OG  SER D  47      18.151 -26.971  -9.575  1.00 61.11           O  
ANISOU10814  OG  SER D  47     8676   6909   7633    545    191    206       O  
ATOM  10815  N   SER D  48      17.865 -24.722  -7.704  1.00 60.33           N  
ANISOU10815  N   SER D  48     8470   6841   7612    444    208    233       N  
ATOM  10816  CA  SER D  48      18.662 -23.503  -7.628  1.00 60.55           C  
ANISOU10816  CA  SER D  48     8424   6909   7673    452    227    258       C  
ATOM  10817  C   SER D  48      20.150 -23.808  -7.650  1.00 64.22           C  
ANISOU10817  C   SER D  48     8874   7394   8131    511    228    273       C  
ATOM  10818  O   SER D  48      20.649 -24.583  -6.835  1.00 66.64           O  
ANISOU10818  O   SER D  48     9211   7682   8424    525    210    268       O  
ATOM  10819  CB  SER D  48      18.294 -22.663  -6.395  1.00 60.36           C  
ANISOU10819  CB  SER D  48     8369   6882   7681    394    223    259       C  
ATOM  10820  OG  SER D  48      19.052 -23.027  -5.253  1.00 62.46           O  
ANISOU10820  OG  SER D  48     8643   7140   7949    398    209    262       O  
ATOM  10821  N   GLU D  49      20.846 -23.191  -8.595  1.00 65.93           N  
ANISOU10821  N   GLU D  49     9042   7653   8355    547    250    293       N  
ATOM  10822  CA  GLU D  49      22.282 -23.333  -8.719  1.00 66.56           C  
ANISOU10822  CA  GLU D  49     9093   7765   8428    603    256    309       C  
ATOM  10823  C   GLU D  49      22.937 -21.968  -8.471  1.00 67.18           C  
ANISOU10823  C   GLU D  49     9090   7882   8550    582    275    335       C  
ATOM  10824  O   GLU D  49      22.651 -21.002  -9.187  1.00 65.47           O  
ANISOU10824  O   GLU D  49     8837   7686   8353    566    296    350       O  
ATOM  10825  CB  GLU D  49      22.631 -23.883 -10.104  1.00 70.75           C  
ANISOU10825  CB  GLU D  49     9637   8318   8925    668    267    311       C  
ATOM  10826  CG  GLU D  49      24.083 -23.714 -10.516  1.00 76.15           C  
ANISOU10826  CG  GLU D  49    10271   9056   9606    726    282    334       C  
ATOM  10827  CD  GLU D  49      24.211 -23.051 -11.874  1.00 83.22           C  
ANISOU10827  CD  GLU D  49    11125   9994  10499    750    313    355       C  
ATOM  10828  OE1 GLU D  49      23.647 -23.578 -12.858  1.00 88.34           O  
ANISOU10828  OE1 GLU D  49    11811  10636  11116    777    313    342       O  
ATOM  10829  OE2 GLU D  49      24.869 -21.992 -11.956  1.00 87.64           O  
ANISOU10829  OE2 GLU D  49    11614  10596  11088    740    335    384       O  
ATOM  10830  N   PRO D  50      23.800 -21.877  -7.439  1.00 66.94           N  
ANISOU10830  N   PRO D  50     9036   7863   8535    581    265    340       N  
ATOM  10831  CA  PRO D  50      24.093 -22.963  -6.501  1.00 66.35           C  
ANISOU10831  CA  PRO D  50     9008   7764   8437    600    238    323       C  
ATOM  10832  C   PRO D  50      23.017 -23.100  -5.433  1.00 65.89           C  
ANISOU10832  C   PRO D  50     8990   7659   8385    542    219    305       C  
ATOM  10833  O   PRO D  50      22.020 -22.377  -5.462  1.00 66.90           O  
ANISOU10833  O   PRO D  50     9108   7776   8533    490    226    302       O  
ATOM  10834  CB  PRO D  50      25.423 -22.537  -5.870  1.00 63.46           C  
ANISOU10834  CB  PRO D  50     8583   7438   8088    617    239    337       C  
ATOM  10835  CG  PRO D  50      25.425 -21.059  -5.957  1.00 64.25           C  
ANISOU10835  CG  PRO D  50     8613   7563   8236    572    259    355       C  
ATOM  10836  CD  PRO D  50      24.658 -20.701  -7.202  1.00 65.83           C  
ANISOU10836  CD  PRO D  50     8816   7761   8433    566    280    363       C  
ATOM  10837  N   CYS D  51      23.217 -24.041  -4.515  1.00 66.89           N  
ANISOU10837  N   CYS D  51     9163   7760   8490    553    196    294       N  
ATOM  10838  CA  CYS D  51      22.318 -24.229  -3.386  1.00 67.49           C  
ANISOU10838  CA  CYS D  51     9276   7797   8568    501    179    280       C  
ATOM  10839  C   CYS D  51      22.295 -22.954  -2.557  1.00 66.01           C  
ANISOU10839  C   CYS D  51     9027   7629   8423    453    183    285       C  
ATOM  10840  O   CYS D  51      23.345 -22.386  -2.250  1.00 69.65           O  
ANISOU10840  O   CYS D  51     9434   8124   8903    469    185    296       O  
ATOM  10841  CB  CYS D  51      22.769 -25.413  -2.527  1.00 70.87           C  
ANISOU10841  CB  CYS D  51     9760   8199   8965    530    154    273       C  
ATOM  10842  SG  CYS D  51      21.566 -25.910  -1.274  1.00 70.82           S  
ANISOU10842  SG  CYS D  51     9815   8141   8949    468    135    259       S  
ATOM  10843  N   ILE D  52      21.095 -22.506  -2.213  1.00 61.86           N  
ANISOU10843  N   ILE D  52     8509   7084   7910    394    182    276       N  
ATOM  10844  CA  ILE D  52      20.913 -21.250  -1.491  1.00 62.82           C  
ANISOU10844  CA  ILE D  52     8577   7220   8070    349    185    277       C  
ATOM  10845  C   ILE D  52      21.651 -21.181  -0.138  1.00 63.96           C  
ANISOU10845  C   ILE D  52     8705   7372   8222    348    167    275       C  
ATOM  10846  O   ILE D  52      21.432 -22.008   0.754  1.00 62.04           O  
ANISOU10846  O   ILE D  52     8509   7106   7955    345    149    266       O  
ATOM  10847  CB  ILE D  52      19.407 -20.893  -1.376  1.00 59.82           C  
ANISOU10847  CB  ILE D  52     8212   6820   7694    294    186    264       C  
ATOM  10848  CG1 ILE D  52      18.929 -20.311  -2.706  1.00 58.36           C  
ANISOU10848  CG1 ILE D  52     8008   6646   7518    294    206    269       C  
ATOM  10849  CG2 ILE D  52      19.150 -19.899  -0.252  1.00 58.98           C  
ANISOU10849  CG2 ILE D  52     8070   6720   7616    250    179    258       C  
ATOM  10850  CD1 ILE D  52      17.480 -20.581  -3.027  1.00 61.09           C  
ANISOU10850  CD1 ILE D  52     8390   6972   7846    262    206    253       C  
ATOM  10851  N   ARG D  53      22.561 -20.212  -0.034  1.00 66.03           N  
ANISOU10851  N   ARG D  53     8902   7669   8518    352    173    285       N  
ATOM  10852  CA  ARG D  53      23.150 -19.801   1.238  1.00 68.14           C  
ANISOU10852  CA  ARG D  53     9139   7949   8802    341    156    279       C  
ATOM  10853  C   ARG D  53      22.259 -18.718   1.813  1.00 68.35           C  
ANISOU10853  C   ARG D  53     9143   7968   8858    283    155    269       C  
ATOM  10854  O   ARG D  53      21.931 -17.761   1.110  1.00 70.41           O  
ANISOU10854  O   ARG D  53     9371   8233   9146    263    171    275       O  
ATOM  10855  CB  ARG D  53      24.519 -19.160   1.025  1.00 72.32           C  
ANISOU10855  CB  ARG D  53     9600   8520   9356    365    162    292       C  
ATOM  10856  CG  ARG D  53      25.648 -20.066   0.578  1.00 76.43           C  
ANISOU10856  CG  ARG D  53    10125   9063   9849    430    162    301       C  
ATOM  10857  CD  ARG D  53      26.918 -19.243   0.409  1.00 77.07           C  
ANISOU10857  CD  ARG D  53    10127   9194   9960    442    171    314       C  
ATOM  10858  NE  ARG D  53      27.131 -18.342   1.542  1.00 75.95           N  
ANISOU10858  NE  ARG D  53     9943   9062   9852    403    156    304       N  
ATOM  10859  CZ  ARG D  53      28.169 -17.520   1.670  1.00 79.14           C  
ANISOU10859  CZ  ARG D  53    10274   9505  10287    398    158    311       C  
ATOM  10860  NH1 ARG D  53      29.108 -17.473   0.735  1.00 77.75           N  
ANISOU10860  NH1 ARG D  53    10058   9369  10113    430    176    330       N  
ATOM  10861  NH2 ARG D  53      28.269 -16.743   2.741  1.00 78.53           N  
ANISOU10861  NH2 ARG D  53    10165   9431  10239    362    141    297       N  
ATOM  10862  N   LEU D  54      21.890 -18.833   3.086  1.00 65.94           N  
ANISOU10862  N   LEU D  54     8855   7652   8546    261    136    254       N  
ATOM  10863  CA  LEU D  54      21.065 -17.793   3.707  1.00 64.55           C  
ANISOU10863  CA  LEU D  54     8656   7473   8395    211    132    241       C  
ATOM  10864  C   LEU D  54      21.864 -16.516   4.013  1.00 63.64           C  
ANISOU10864  C   LEU D  54     8474   7382   8325    201    130    241       C  
ATOM  10865  O   LEU D  54      21.290 -15.483   4.364  1.00 67.38           O  
ANISOU10865  O   LEU D  54     8924   7851   8824    165    128    230       O  
ATOM  10866  CB  LEU D  54      20.313 -18.325   4.937  1.00 64.47           C  
ANISOU10866  CB  LEU D  54     8687   7448   8359    190    115    225       C  
ATOM  10867  CG  LEU D  54      19.296 -19.457   4.692  1.00 65.95           C  
ANISOU10867  CG  LEU D  54     8942   7608   8507    182    118    224       C  
ATOM  10868  CD1 LEU D  54      18.641 -19.890   5.990  1.00 65.81           C  
ANISOU10868  CD1 LEU D  54     8957   7581   8464    157    102    213       C  
ATOM  10869  CD2 LEU D  54      18.216 -19.083   3.685  1.00 68.82           C  
ANISOU10869  CD2 LEU D  54     9307   7964   8877    157    135    223       C  
ATOM  10870  N   ARG D  55      23.182 -16.588   3.850  1.00 62.70           N  
ANISOU10870  N   ARG D  55     8323   7287   8214    233    129    252       N  
ATOM  10871  CA  ARG D  55      24.052 -15.426   4.006  1.00 64.05           C  
ANISOU10871  CA  ARG D  55     8425   7481   8428    221    128    254       C  
ATOM  10872  C   ARG D  55      24.123 -14.605   2.726  1.00 61.42           C  
ANISOU10872  C   ARG D  55     8059   7152   8124    213    154    274       C  
ATOM  10873  O   ARG D  55      24.387 -13.408   2.778  1.00 60.99           O  
ANISOU10873  O   ARG D  55     7958   7103   8112    185    156    276       O  
ATOM  10874  CB  ARG D  55      25.464 -15.852   4.412  1.00 72.10           C  
ANISOU10874  CB  ARG D  55     9418   8533   9441    258    116    256       C  
ATOM  10875  CG  ARG D  55      25.577 -16.420   5.821  1.00 82.48           C  
ANISOU10875  CG  ARG D  55    10755   9849  10733    266     88    237       C  
ATOM  10876  CD  ARG D  55      26.774 -17.357   5.942  1.00 87.99           C  
ANISOU10876  CD  ARG D  55    11452  10576  11404    321     79    242       C  
ATOM  10877  NE  ARG D  55      26.916 -17.903   7.293  1.00 90.27           N  
ANISOU10877  NE  ARG D  55    11764  10866  11667    334     51    225       N  
ATOM  10878  CZ  ARG D  55      27.683 -18.941   7.616  1.00 89.52           C  
ANISOU10878  CZ  ARG D  55    11690  10786  11535    387     39    227       C  
ATOM  10879  NH1 ARG D  55      28.389 -19.576   6.684  1.00 88.00           N  
ANISOU10879  NH1 ARG D  55    11499  10608  11327    434     50    242       N  
ATOM  10880  NH2 ARG D  55      27.737 -19.351   8.879  1.00 85.21           N  
ANISOU10880  NH2 ARG D  55    11166  10241  10965    397     14    213       N  
ATOM  10881  N   GLY D  56      23.908 -15.250   1.581  1.00 59.88           N  
ANISOU10881  N   GLY D  56     7891   6954   7906    239    174    290       N  
ATOM  10882  CA  GLY D  56      23.969 -14.569   0.285  1.00 60.74           C  
ANISOU10882  CA  GLY D  56     7972   7069   8034    238    200    313       C  
ATOM  10883  C   GLY D  56      24.290 -15.499  -0.869  1.00 61.28           C  
ANISOU10883  C   GLY D  56     8061   7150   8071    285    218    329       C  
ATOM  10884  O   GLY D  56      25.180 -16.346  -0.768  1.00 64.73           O  
ANISOU10884  O   GLY D  56     8501   7608   8486    325    212    331       O  
ATOM  10885  N   THR D  57      23.568 -15.343  -1.973  1.00 59.14           N  
ANISOU10885  N   THR D  57     7805   6870   7796    284    238    340       N  
ATOM  10886  CA  THR D  57      23.739 -16.232  -3.117  1.00 61.37           C  
ANISOU10886  CA  THR D  57     8110   7162   8043    330    253    352       C  
ATOM  10887  C   THR D  57      23.481 -15.506  -4.424  1.00 61.38           C  
ANISOU10887  C   THR D  57     8093   7172   8057    330    281    374       C  
ATOM  10888  O   THR D  57      22.528 -14.740  -4.526  1.00 65.16           O  
ANISOU10888  O   THR D  57     8573   7630   8552    295    285    371       O  
ATOM  10889  CB  THR D  57      22.786 -17.447  -3.045  1.00 60.69           C  
ANISOU10889  CB  THR D  57     8096   7046   7914    341    241    332       C  
ATOM  10890  OG1 THR D  57      22.662 -17.891  -1.689  1.00 60.50           O  
ANISOU10890  OG1 THR D  57     8097   7006   7884    325    215    312       O  
ATOM  10891  CG2 THR D  57      23.317 -18.595  -3.894  1.00 62.13           C  
ANISOU10891  CG2 THR D  57     8308   7240   8059    399    246    338       C  
ATOM  10892  N   ASN D  58      24.345 -15.743  -5.409  1.00 61.93           N  
ANISOU10892  N   ASN D  58     8142   7274   8115    371    300    396       N  
ATOM  10893  CA  ASN D  58      24.105 -15.335  -6.794  1.00 60.55           C  
ANISOU10893  CA  ASN D  58     7958   7110   7937    384    328    419       C  
ATOM  10894  C   ASN D  58      23.972 -16.573  -7.652  1.00 55.33           C  
ANISOU10894  C   ASN D  58     7341   6453   7225    437    331    414       C  
ATOM  10895  O   ASN D  58      24.891 -17.383  -7.723  1.00 56.27           O  
ANISOU10895  O   ASN D  58     7460   6596   7321    482    328    415       O  
ATOM  10896  CB  ASN D  58      25.258 -14.489  -7.345  1.00 64.65           C  
ANISOU10896  CB  ASN D  58     8411   7669   8482    388    352    453       C  
ATOM  10897  CG  ASN D  58      25.408 -13.158  -6.639  1.00 71.79           C  
ANISOU10897  CG  ASN D  58     9271   8564   9440    333    350    460       C  
ATOM  10898  OD1 ASN D  58      24.793 -12.909  -5.598  1.00 74.54           O  
ANISOU10898  OD1 ASN D  58     9635   8882   9804    297    327    436       O  
ATOM  10899  ND2 ASN D  58      26.239 -12.290  -7.205  1.00 73.60           N  
ANISOU10899  ND2 ASN D  58     9446   8822   9696    325    373    493       N  
ATOM  10900  N   GLY D  59      22.838 -16.727  -8.313  1.00 50.49           N  
ANISOU10900  N   GLY D  59     6767   5820   6594    434    335    405       N  
ATOM  10901  CA  GLY D  59      22.690 -17.849  -9.208  1.00 50.04           C  
ANISOU10901  CA  GLY D  59     6753   5767   6492    483    336    398       C  
ATOM  10902  C   GLY D  59      21.385 -17.836  -9.948  1.00 49.13           C  
ANISOU10902  C   GLY D  59     6672   5634   6362    474    340    387       C  
ATOM  10903  O   GLY D  59      20.814 -16.780 -10.193  1.00 49.18           O  
ANISOU10903  O   GLY D  59     6656   5638   6391    444    352    398       O  
ATOM  10904  N   PHE D  60      20.920 -19.025 -10.304  1.00 49.68           N  
ANISOU10904  N   PHE D  60     6797   5687   6389    501    328    365       N  
ATOM  10905  CA  PHE D  60      19.707 -19.168 -11.088  1.00 49.65           C  
ANISOU10905  CA  PHE D  60     6826   5671   6366    496    329    351       C  
ATOM  10906  C   PHE D  60      18.760 -20.134 -10.409  1.00 49.62           C  
ANISOU10906  C   PHE D  60     6882   5628   6342    471    302    316       C  
ATOM  10907  O   PHE D  60      19.186 -21.068  -9.730  1.00 50.88           O  
ANISOU10907  O   PHE D  60     7072   5769   6488    481    284    305       O  
ATOM  10908  CB  PHE D  60      20.015 -19.679 -12.499  1.00 50.09           C  
ANISOU10908  CB  PHE D  60     6892   5753   6386    557    343    358       C  
ATOM  10909  CG  PHE D  60      20.995 -18.829 -13.264  1.00 50.75           C  
ANISOU10909  CG  PHE D  60     6918   5882   6482    585    374    396       C  
ATOM  10910  CD1 PHE D  60      22.365 -18.923 -13.019  1.00 51.07           C  
ANISOU10910  CD1 PHE D  60     6925   5949   6528    612    380    415       C  
ATOM  10911  CD2 PHE D  60      20.551 -17.958 -14.250  1.00 50.86           C  
ANISOU10911  CD2 PHE D  60     6910   5914   6500    585    396    415       C  
ATOM  10912  CE1 PHE D  60      23.267 -18.144 -13.722  1.00 51.30           C  
ANISOU10912  CE1 PHE D  60     6897   6024   6569    632    410    452       C  
ATOM  10913  CE2 PHE D  60      21.450 -17.180 -14.963  1.00 51.81           C  
ANISOU10913  CE2 PHE D  60     6978   6074   6630    607    427    455       C  
ATOM  10914  CZ  PHE D  60      22.809 -17.273 -14.698  1.00 52.92           C  
ANISOU10914  CZ  PHE D  60     7084   6244   6779    628    434    474       C  
ATOM  10915  N   VAL D  61      17.472 -19.874 -10.582  1.00 49.70           N  
ANISOU10915  N   VAL D  61     6906   5625   6350    437    299    300       N  
ATOM  10916  CA  VAL D  61      16.429 -20.818 -10.246  1.00 49.36           C  
ANISOU10916  CA  VAL D  61     6919   5551   6283    412    277    267       C  
ATOM  10917  C   VAL D  61      16.047 -21.459 -11.580  1.00 50.72           C  
ANISOU10917  C   VAL D  61     7121   5729   6420    449    280    256       C  
ATOM  10918  O   VAL D  61      15.616 -20.772 -12.509  1.00 50.99           O  
ANISOU10918  O   VAL D  61     7132   5787   6454    458    295    262       O  
ATOM  10919  CB  VAL D  61      15.221 -20.108  -9.584  1.00 47.86           C  
ANISOU10919  CB  VAL D  61     6719   5353   6113    351    272    254       C  
ATOM  10920  CG1 VAL D  61      14.023 -21.036  -9.462  1.00 46.78           C  
ANISOU10920  CG1 VAL D  61     6634   5192   5948    322    254    222       C  
ATOM  10921  CG2 VAL D  61      15.608 -19.570  -8.221  1.00 46.73           C  
ANISOU10921  CG2 VAL D  61     6551   5202   6000    319    266    261       C  
ATOM  10922  N   HIS D  62      16.255 -22.764 -11.695  1.00 50.55           N  
ANISOU10922  N   HIS D  62     7152   5686   6366    476    264    239       N  
ATOM  10923  CA  HIS D  62      15.854 -23.482 -12.894  1.00 50.61           C  
ANISOU10923  CA  HIS D  62     7195   5695   6337    510    261    221       C  
ATOM  10924  C   HIS D  62      14.479 -24.043 -12.678  1.00 49.87           C  
ANISOU10924  C   HIS D  62     7145   5571   6230    462    241    187       C  
ATOM  10925  O   HIS D  62      14.216 -24.675 -11.661  1.00 50.35           O  
ANISOU10925  O   HIS D  62     7240   5597   6291    424    222    174       O  
ATOM  10926  CB  HIS D  62      16.865 -24.570 -13.232  1.00 52.47           C  
ANISOU10926  CB  HIS D  62     7466   5925   6544    572    253    219       C  
ATOM  10927  CG  HIS D  62      18.270 -24.048 -13.462  1.00 54.55           C  
ANISOU10927  CG  HIS D  62     7680   6227   6817    621    274    252       C  
ATOM  10928  ND1 HIS D  62      19.237 -24.117 -12.522  1.00 55.94           N  
ANISOU10928  ND1 HIS D  62     7844   6402   7008    626    270    265       N  
ATOM  10929  CD2 HIS D  62      18.846 -23.429 -14.570  1.00 54.52           C  
ANISOU10929  CD2 HIS D  62     7633   6270   6809    667    300    276       C  
ATOM  10930  CE1 HIS D  62      20.374 -23.569 -13.003  1.00 54.11           C  
ANISOU10930  CE1 HIS D  62     7560   6215   6782    670    292    294       C  
ATOM  10931  NE2 HIS D  62      20.133 -23.147 -14.256  1.00 53.72           N  
ANISOU10931  NE2 HIS D  62     7492   6195   6722    693    312    303       N  
ATOM  10932  N   VAL D  63      13.573 -23.776 -13.612  1.00 50.89           N  
ANISOU10932  N   VAL D  63     7270   5718   6347    459    245    174       N  
ATOM  10933  CA  VAL D  63      12.194 -24.242 -13.503  1.00 53.92           C  
ANISOU10933  CA  VAL D  63     7686   6083   6717    410    227    140       C  
ATOM  10934  C   VAL D  63      11.784 -24.932 -14.792  1.00 57.33           C  
ANISOU10934  C   VAL D  63     8149   6520   7111    444    220    116       C  
ATOM  10935  O   VAL D  63      12.001 -24.392 -15.886  1.00 60.21           O  
ANISOU10935  O   VAL D  63     8487   6921   7468    491    236    126       O  
ATOM  10936  CB  VAL D  63      11.220 -23.083 -13.203  1.00 53.62           C  
ANISOU10936  CB  VAL D  63     7603   6068   6701    363    236    141       C  
ATOM  10937  CG1 VAL D  63       9.771 -23.549 -13.289  1.00 52.27           C  
ANISOU10937  CG1 VAL D  63     7457   5891   6511    317    219    104       C  
ATOM  10938  CG2 VAL D  63      11.500 -22.507 -11.827  1.00 54.79           C  
ANISOU10938  CG2 VAL D  63     7726   6206   6883    324    238    158       C  
ATOM  10939  N   GLU D  64      11.193 -26.119 -14.659  1.00 57.91           N  
ANISOU10939  N   GLU D  64     8283   6556   7162    421    194     83       N  
ATOM  10940  CA  GLU D  64      10.750 -26.898 -15.814  1.00 60.10           C  
ANISOU10940  CA  GLU D  64     8599   6832   7404    448    181     52       C  
ATOM  10941  C   GLU D  64       9.451 -27.621 -15.476  1.00 57.15           C  
ANISOU10941  C   GLU D  64     8265   6429   7019    381    157     14       C  
ATOM  10942  O   GLU D  64       9.453 -28.591 -14.719  1.00 57.65           O  
ANISOU10942  O   GLU D  64     8381   6444   7080    351    138      4       O  
ATOM  10943  CB  GLU D  64      11.846 -27.887 -16.249  1.00 65.84           C  
ANISOU10943  CB  GLU D  64     9370   7537   8106    514    173     51       C  
ATOM  10944  CG  GLU D  64      11.621 -28.555 -17.604  1.00 76.17           C  
ANISOU10944  CG  GLU D  64    10712   8853   9376    562    161     22       C  
ATOM  10945  CD  GLU D  64      12.524 -29.770 -17.854  1.00 84.20           C  
ANISOU10945  CD  GLU D  64    11790   9836  10365    620    144     11       C  
ATOM  10946  OE1 GLU D  64      12.944 -30.437 -16.878  1.00 87.76           O  
ANISOU10946  OE1 GLU D  64    12280  10242  10822    605    131     14       O  
ATOM  10947  OE2 GLU D  64      12.806 -30.075 -19.038  1.00 82.28           O  
ANISOU10947  OE2 GLU D  64    11558   9613  10090    686    143     -1       O  
ATOM  10948  N   PHE D  65       8.340 -27.138 -16.026  1.00 53.28           N  
ANISOU10948  N   PHE D  65     7749   5971   6523    357    157     -4       N  
ATOM  10949  CA  PHE D  65       7.036 -27.756 -15.781  1.00 53.11           C  
ANISOU10949  CA  PHE D  65     7755   5933   6491    289    136    -41       C  
ATOM  10950  C   PHE D  65       6.010 -27.439 -16.859  1.00 53.46           C  
ANISOU10950  C   PHE D  65     7777   6020   6515    291    133    -69       C  
ATOM  10951  O   PHE D  65       6.284 -26.668 -17.780  1.00 56.14           O  
ANISOU10951  O   PHE D  65     8079   6401   6849    347    150    -57       O  
ATOM  10952  CB  PHE D  65       6.503 -27.378 -14.389  1.00 54.38           C  
ANISOU10952  CB  PHE D  65     7896   6086   6677    214    138    -32       C  
ATOM  10953  CG  PHE D  65       5.916 -25.986 -14.288  1.00 55.33           C  
ANISOU10953  CG  PHE D  65     7946   6259   6816    199    156    -21       C  
ATOM  10954  CD1 PHE D  65       4.601 -25.807 -13.863  1.00 55.95           C  
ANISOU10954  CD1 PHE D  65     8008   6357   6894    133    149    -44       C  
ATOM  10955  CD2 PHE D  65       6.682 -24.853 -14.571  1.00 55.07           C  
ANISOU10955  CD2 PHE D  65     7865   6256   6801    248    180     11       C  
ATOM  10956  CE1 PHE D  65       4.059 -24.532 -13.744  1.00 57.42           C  
ANISOU10956  CE1 PHE D  65     8132   6589   7093    125    164    -36       C  
ATOM  10957  CE2 PHE D  65       6.141 -23.579 -14.464  1.00 54.51           C  
ANISOU10957  CE2 PHE D  65     7737   6225   6747    236    195     21       C  
ATOM  10958  CZ  PHE D  65       4.827 -23.418 -14.052  1.00 55.53           C  
ANISOU10958  CZ  PHE D  65     7852   6372   6872    178    186     -3       C  
ATOM  10959  N   ILE D  66       4.835 -28.052 -16.751  1.00 52.94           N  
ANISOU10959  N   ILE D  66     7733   5945   6436    230    112   -107       N  
ATOM  10960  CA  ILE D  66       3.731 -27.728 -17.639  1.00 56.79           C  
ANISOU10960  CA  ILE D  66     8193   6478   6904    224    106   -138       C  
ATOM  10961  C   ILE D  66       2.604 -27.124 -16.808  1.00 57.10           C  
ANISOU10961  C   ILE D  66     8192   6544   6958    151    109   -144       C  
ATOM  10962  O   ILE D  66       1.848 -27.861 -16.180  1.00 58.21           O  
ANISOU10962  O   ILE D  66     8358   6662   7095     80     91   -167       O  
ATOM  10963  CB  ILE D  66       3.226 -28.952 -18.430  1.00 58.19           C  
ANISOU10963  CB  ILE D  66     8426   6634   7049    219     77   -185       C  
ATOM  10964  CG1 ILE D  66       4.358 -29.571 -19.251  1.00 58.42           C  
ANISOU10964  CG1 ILE D  66     8497   6639   7060    300     73   -181       C  
ATOM  10965  CG2 ILE D  66       2.078 -28.557 -19.351  1.00 57.25           C  
ANISOU10965  CG2 ILE D  66     8271   6571   6908    215     71   -218       C  
ATOM  10966  CD1 ILE D  66       4.101 -31.010 -19.652  1.00 59.13           C  
ANISOU10966  CD1 ILE D  66     8662   6681   7123    289     39   -225       C  
ATOM  10967  N   PRO D  67       2.507 -25.776 -16.786  1.00 59.22           N  
ANISOU10967  N   PRO D  67     8398   6860   7242    168    131   -121       N  
ATOM  10968  CA  PRO D  67       1.501 -25.056 -15.999  1.00 59.77           C  
ANISOU10968  CA  PRO D  67     8423   6962   7324    111    135   -126       C  
ATOM  10969  C   PRO D  67       0.073 -25.506 -16.252  1.00 61.74           C  
ANISOU10969  C   PRO D  67     8670   7238   7549     58    115   -172       C  
ATOM  10970  O   PRO D  67      -0.325 -25.722 -17.398  1.00 63.08           O  
ANISOU10970  O   PRO D  67     8842   7431   7691     87    104   -200       O  
ATOM  10971  CB  PRO D  67       1.684 -23.592 -16.426  1.00 58.23           C  
ANISOU10971  CB  PRO D  67     8171   6813   7139    162    158   -100       C  
ATOM  10972  CG  PRO D  67       2.679 -23.601 -17.540  1.00 59.82           C  
ANISOU10972  CG  PRO D  67     8385   7012   7331    240    167    -83       C  
ATOM  10973  CD  PRO D  67       3.488 -24.844 -17.362  1.00 58.48           C  
ANISOU10973  CD  PRO D  67     8274   6787   7158    243    155    -85       C  
ATOM  10974  N   ARG D  68      -0.678 -25.645 -15.164  1.00 63.74           N  
ANISOU10974  N   ARG D  68     8915   7491   7810    -17    110   -181       N  
ATOM  10975  CA  ARG D  68      -2.059 -26.119 -15.202  1.00 64.43           C  
ANISOU10975  CA  ARG D  68     8996   7606   7876    -81     92   -224       C  
ATOM  10976  C   ARG D  68      -3.052 -24.976 -15.446  1.00 61.34           C  
ANISOU10976  C   ARG D  68     8535   7292   7477    -77     99   -236       C  
ATOM  10977  O   ARG D  68      -4.265 -25.186 -15.503  1.00 59.76           O  
ANISOU10977  O   ARG D  68     8315   7131   7258   -126     86   -273       O  
ATOM  10978  CB  ARG D  68      -2.386 -26.872 -13.904  1.00 68.53           C  
ANISOU10978  CB  ARG D  68     9542   8091   8404   -167     85   -224       C  
ATOM  10979  CG  ARG D  68      -1.520 -28.106 -13.657  1.00 73.59           C  
ANISOU10979  CG  ARG D  68    10259   8653   9048   -173     74   -215       C  
ATOM  10980  CD  ARG D  68      -2.068 -29.348 -14.353  1.00 77.70           C  
ANISOU10980  CD  ARG D  68    10830   9149   9544   -204     46   -257       C  
ATOM  10981  NE  ARG D  68      -1.121 -30.469 -14.342  1.00 80.82           N  
ANISOU10981  NE  ARG D  68    11304   9465   9938   -188     34   -250       N  
ATOM  10982  CZ  ARG D  68      -1.470 -31.757 -14.396  1.00 82.13           C  
ANISOU10982  CZ  ARG D  68    11533   9582  10090   -237      9   -277       C  
ATOM  10983  NH1 ARG D  68      -2.753 -32.111 -14.450  1.00 81.19           N  
ANISOU10983  NH1 ARG D  68    11403   9486   9958   -312     -4   -313       N  
ATOM  10984  NH2 ARG D  68      -0.532 -32.697 -14.383  1.00 78.99           N  
ANISOU10984  NH2 ARG D  68    11209   9110   9691   -211     -1   -268       N  
ATOM  10985  N   GLY D  69      -2.520 -23.766 -15.584  1.00 58.71           N  
ANISOU10985  N   GLY D  69     8167   6980   7159    -17    119   -205       N  
ATOM  10986  CA  GLY D  69      -3.311 -22.582 -15.904  1.00 55.90           C  
ANISOU10986  CA  GLY D  69     7752   6692   6796      3    127   -212       C  
ATOM  10987  C   GLY D  69      -2.412 -21.581 -16.596  1.00 54.70           C  
ANISOU10987  C   GLY D  69     7586   6544   6654     87    146   -178       C  
ATOM  10988  O   GLY D  69      -1.205 -21.807 -16.729  1.00 52.98           O  
ANISOU10988  O   GLY D  69     7398   6281   6450    122    155   -149       O  
ATOM  10989  N   ASN D  70      -2.990 -20.473 -17.045  1.00 53.99           N  
ANISOU10989  N   ASN D  70     7449   6507   6555    121    153   -179       N  
ATOM  10990  CA  ASN D  70      -2.186 -19.410 -17.638  1.00 53.83           C  
ANISOU10990  CA  ASN D  70     7415   6490   6546    195    174   -141       C  
ATOM  10991  C   ASN D  70      -1.332 -18.690 -16.580  1.00 52.14           C  
ANISOU10991  C   ASN D  70     7194   6243   6373    190    192    -99       C  
ATOM  10992  O   ASN D  70      -1.728 -18.572 -15.414  1.00 49.31           O  
ANISOU10992  O   ASN D  70     6822   5883   6029    139    189   -104       O  
ATOM  10993  CB  ASN D  70      -3.067 -18.445 -18.442  1.00 54.27           C  
ANISOU10993  CB  ASN D  70     7432   6609   6579    235    175   -154       C  
ATOM  10994  CG  ASN D  70      -3.881 -19.155 -19.523  1.00 56.18           C  
ANISOU10994  CG  ASN D  70     7679   6888   6779    243    156   -199       C  
ATOM  10995  OD1 ASN D  70      -3.338 -19.894 -20.352  1.00 56.19           O  
ANISOU10995  OD1 ASN D  70     7714   6869   6766    271    151   -202       O  
ATOM  10996  ND2 ASN D  70      -5.191 -18.931 -19.517  1.00 56.01           N  
ANISOU10996  ND2 ASN D  70     7622   6923   6734    220    142   -236       N  
ATOM  10997  N   LEU D  71      -0.150 -18.241 -16.990  1.00 50.15           N  
ANISOU10997  N   LEU D  71     6948   5966   6138    243    210    -59       N  
ATOM  10998  CA  LEU D  71       0.796 -17.596 -16.078  1.00 49.15           C  
ANISOU10998  CA  LEU D  71     6815   5807   6051    241    225    -19       C  
ATOM  10999  C   LEU D  71       0.864 -16.058 -16.215  1.00 48.62           C  
ANISOU10999  C   LEU D  71     6711   5759   6000    279    242      7       C  
ATOM  11000  O   LEU D  71       1.807 -15.429 -15.727  1.00 48.79           O  
ANISOU11000  O   LEU D  71     6728   5753   6055    287    256     44       O  
ATOM  11001  CB  LEU D  71       2.187 -18.229 -16.243  1.00 48.90           C  
ANISOU11001  CB  LEU D  71     6816   5731   6031    264    233      7       C  
ATOM  11002  CG  LEU D  71       2.693 -19.304 -15.262  1.00 49.62           C  
ANISOU11002  CG  LEU D  71     6941   5777   6134    220    223      4       C  
ATOM  11003  CD1 LEU D  71       1.616 -20.297 -14.836  1.00 49.18           C  
ANISOU11003  CD1 LEU D  71     6904   5722   6057    159    200    -38       C  
ATOM  11004  CD2 LEU D  71       3.900 -20.026 -15.842  1.00 46.48           C  
ANISOU11004  CD2 LEU D  71     6577   5349   5733    261    227     21       C  
ATOM  11005  N   LYS D  72      -0.136 -15.462 -16.868  1.00 46.63           N  
ANISOU11005  N   LYS D  72     6437   5554   5724    301    239    -10       N  
ATOM  11006  CA  LYS D  72      -0.193 -14.009 -17.072  1.00 46.54           C  
ANISOU11006  CA  LYS D  72     6398   5559   5724    340    253     13       C  
ATOM  11007  C   LYS D  72      -0.231 -13.211 -15.763  1.00 45.68           C  
ANISOU11007  C   LYS D  72     6270   5436   5648    309    253     22       C  
ATOM  11008  O   LYS D  72       0.319 -12.110 -15.693  1.00 44.81           O  
ANISOU11008  O   LYS D  72     6151   5311   5564    336    267     55       O  
ATOM  11009  CB  LYS D  72      -1.389 -13.624 -17.956  1.00 47.53           C  
ANISOU11009  CB  LYS D  72     6504   5741   5811    371    245    -13       C  
ATOM  11010  CG  LYS D  72      -1.261 -12.266 -18.642  1.00 46.03           C  
ANISOU11010  CG  LYS D  72     6300   5564   5623    433    261     18       C  
ATOM  11011  CD  LYS D  72      -2.619 -11.611 -18.836  1.00 47.18           C  
ANISOU11011  CD  LYS D  72     6420   5765   5741    449    249    -12       C  
ATOM  11012  CE  LYS D  72      -3.264 -11.967 -20.161  1.00 50.00           C  
ANISOU11012  CE  LYS D  72     6777   6170   6050    490    242    -35       C  
ATOM  11013  NZ  LYS D  72      -2.836 -11.018 -21.226  1.00 50.01           N  
ANISOU11013  NZ  LYS D  72     6781   6174   6043    564    260      2       N  
ATOM  11014  N   TYR D  73      -0.880 -13.773 -14.743  1.00 44.31           N  
ANISOU11014  N   TYR D  73     6093   5269   5472    251    238     -7       N  
ATOM  11015  CA  TYR D  73      -0.974 -13.152 -13.429  1.00 43.35           C  
ANISOU11015  CA  TYR D  73     5955   5138   5376    219    237     -5       C  
ATOM  11016  C   TYR D  73      -0.492 -14.092 -12.340  1.00 44.67           C  
ANISOU11016  C   TYR D  73     6141   5271   5559    165    231     -6       C  
ATOM  11017  O   TYR D  73      -1.219 -14.349 -11.378  1.00 44.98           O  
ANISOU11017  O   TYR D  73     6171   5326   5592    117    220    -30       O  
ATOM  11018  CB  TYR D  73      -2.415 -12.750 -13.127  1.00 42.93           C  
ANISOU11018  CB  TYR D  73     5872   5139   5299    205    224    -42       C  
ATOM  11019  CG  TYR D  73      -3.004 -11.771 -14.106  1.00 44.77           C  
ANISOU11019  CG  TYR D  73     6086   5410   5513    262    227    -44       C  
ATOM  11020  CD1 TYR D  73      -3.736 -12.214 -15.204  1.00 45.80           C  
ANISOU11020  CD1 TYR D  73     6214   5583   5604    283    220    -69       C  
ATOM  11021  CD2 TYR D  73      -2.833 -10.397 -13.938  1.00 45.17           C  
ANISOU11021  CD2 TYR D  73     6125   5454   5584    298    234    -21       C  
ATOM  11022  CE1 TYR D  73      -4.284 -11.320 -16.107  1.00 45.76           C  
ANISOU11022  CE1 TYR D  73     6193   5615   5576    341    221    -70       C  
ATOM  11023  CE2 TYR D  73      -3.377  -9.494 -14.838  1.00 44.82           C  
ANISOU11023  CE2 TYR D  73     6069   5441   5520    355    236    -21       C  
ATOM  11024  CZ  TYR D  73      -4.097  -9.963 -15.920  1.00 45.72           C  
ANISOU11024  CZ  TYR D  73     6179   5599   5591    378    230    -44       C  
ATOM  11025  OH  TYR D  73      -4.642  -9.077 -16.820  1.00 49.03           O  
ANISOU11025  OH  TYR D  73     6589   6053   5987    439    231    -43       O  
ATOM  11026  N   LEU D  74       0.730 -14.599 -12.480  1.00 45.20           N  
ANISOU11026  N   LEU D  74     6234   5295   5643    174    239     20       N  
ATOM  11027  CA  LEU D  74       1.280 -15.531 -11.493  1.00 46.41           C  
ANISOU11027  CA  LEU D  74     6410   5413   5808    130    233     21       C  
ATOM  11028  C   LEU D  74       1.699 -14.805 -10.218  1.00 46.61           C  
ANISOU11028  C   LEU D  74     6420   5420   5866    112    236     37       C  
ATOM  11029  O   LEU D  74       2.427 -13.810 -10.271  1.00 48.71           O  
ANISOU11029  O   LEU D  74     6672   5672   6160    143    247     65       O  
ATOM  11030  CB  LEU D  74       2.466 -16.313 -12.078  1.00 47.80           C  
ANISOU11030  CB  LEU D  74     6619   5553   5988    155    239     43       C  
ATOM  11031  CG  LEU D  74       3.277 -17.263 -11.176  1.00 49.32           C  
ANISOU11031  CG  LEU D  74     6841   5703   6193    125    234     50       C  
ATOM  11032  CD1 LEU D  74       2.545 -18.570 -10.908  1.00 48.37           C  
ANISOU11032  CD1 LEU D  74     6751   5579   6046     78    217     19       C  
ATOM  11033  CD2 LEU D  74       4.645 -17.549 -11.784  1.00 49.59           C  
ANISOU11033  CD2 LEU D  74     6894   5710   6237    168    245     80       C  
ATOM  11034  N   TYR D  75       1.216 -15.298  -9.079  1.00 46.15           N  
ANISOU11034  N   TYR D  75     6364   5364   5804     60    225     18       N  
ATOM  11035  CA  TYR D  75       1.712 -14.857  -7.774  1.00 45.02           C  
ANISOU11035  CA  TYR D  75     6213   5203   5689     40    224     31       C  
ATOM  11036  C   TYR D  75       1.830 -15.993  -6.767  1.00 46.32           C  
ANISOU11036  C   TYR D  75     6403   5347   5848     -8    216     24       C  
ATOM  11037  O   TYR D  75       1.207 -17.048  -6.916  1.00 47.31           O  
ANISOU11037  O   TYR D  75     6550   5479   5947    -39    208      5       O  
ATOM  11038  CB  TYR D  75       0.885 -13.698  -7.210  1.00 42.92           C  
ANISOU11038  CB  TYR D  75     5911   4969   5425     38    221     17       C  
ATOM  11039  CG  TYR D  75      -0.452 -14.061  -6.611  1.00 42.17           C  
ANISOU11039  CG  TYR D  75     5803   4917   5301     -4    211    -17       C  
ATOM  11040  CD1 TYR D  75      -1.616 -14.031  -7.382  1.00 42.23           C  
ANISOU11040  CD1 TYR D  75     5795   4973   5278      1    207    -44       C  
ATOM  11041  CD2 TYR D  75      -0.563 -14.393  -5.258  1.00 42.70           C  
ANISOU11041  CD2 TYR D  75     5871   4983   5370    -49    205    -24       C  
ATOM  11042  CE1 TYR D  75      -2.848 -14.337  -6.827  1.00 42.57           C  
ANISOU11042  CE1 TYR D  75     5819   5062   5292    -40    198    -76       C  
ATOM  11043  CE2 TYR D  75      -1.790 -14.711  -4.689  1.00 41.11           C  
ANISOU11043  CE2 TYR D  75     5653   4826   5138    -91    198    -53       C  
ATOM  11044  CZ  TYR D  75      -2.925 -14.679  -5.475  1.00 43.26           C  
ANISOU11044  CZ  TYR D  75     5906   5148   5382    -88    195    -79       C  
ATOM  11045  OH  TYR D  75      -4.139 -14.992  -4.916  1.00 44.44           O  
ANISOU11045  OH  TYR D  75     6034   5349   5501   -133    189   -109       O  
ATOM  11046  N   PHE D  76       2.645 -15.776  -5.745  1.00 47.25           N  
ANISOU11046  N   PHE D  76     6522   5439   5991    -15    216     42       N  
ATOM  11047  CA  PHE D  76       2.891 -16.793  -4.737  1.00 47.52           C  
ANISOU11047  CA  PHE D  76     6583   5451   6020    -55    208     41       C  
ATOM  11048  C   PHE D  76       2.353 -16.390  -3.378  1.00 47.31           C  
ANISOU11048  C   PHE D  76     6537   5444   5994    -89    202     30       C  
ATOM  11049  O   PHE D  76       2.496 -15.237  -2.952  1.00 47.11           O  
ANISOU11049  O   PHE D  76     6482   5427   5990    -72    204     34       O  
ATOM  11050  CB  PHE D  76       4.392 -17.085  -4.621  1.00 49.57           C  
ANISOU11050  CB  PHE D  76     6864   5667   6302    -31    211     70       C  
ATOM  11051  CG  PHE D  76       4.886 -18.118  -5.592  1.00 52.67           C  
ANISOU11051  CG  PHE D  76     7293   6037   6681    -12    212     76       C  
ATOM  11052  CD1 PHE D  76       5.468 -17.738  -6.797  1.00 53.94           C  
ANISOU11052  CD1 PHE D  76     7447   6196   6849     37    223     91       C  
ATOM  11053  CD2 PHE D  76       4.764 -19.477  -5.307  1.00 54.61           C  
ANISOU11053  CD2 PHE D  76     7583   6261   6905    -42    203     67       C  
ATOM  11054  CE1 PHE D  76       5.918 -18.694  -7.700  1.00 56.61           C  
ANISOU11054  CE1 PHE D  76     7819   6518   7172     60    223     93       C  
ATOM  11055  CE2 PHE D  76       5.218 -20.438  -6.204  1.00 56.78           C  
ANISOU11055  CE2 PHE D  76     7895   6511   7165    -20    201     69       C  
ATOM  11056  CZ  PHE D  76       5.793 -20.046  -7.405  1.00 56.96           C  
ANISOU11056  CZ  PHE D  76     7909   6539   7195     33    211     80       C  
ATOM  11057  N   ASN D  77       1.723 -17.343  -2.706  1.00 46.03           N  
ANISOU11057  N   ASN D  77     6392   5287   5807   -138    196     17       N  
ATOM  11058  CA  ASN D  77       1.499 -17.225  -1.280  1.00 47.06           C  
ANISOU11058  CA  ASN D  77     6513   5429   5936   -171    192     13       C  
ATOM  11059  C   ASN D  77       2.649 -17.949  -0.604  1.00 47.93           C  
ANISOU11059  C   ASN D  77     6659   5493   6057   -174    189     36       C  
ATOM  11060  O   ASN D  77       2.863 -19.129  -0.865  1.00 52.94           O  
ANISOU11060  O   ASN D  77     7336   6100   6679   -188    187     41       O  
ATOM  11061  CB  ASN D  77       0.176 -17.880  -0.881  1.00 47.65           C  
ANISOU11061  CB  ASN D  77     6587   5540   5976   -226    188     -9       C  
ATOM  11062  CG  ASN D  77      -1.033 -17.115  -1.373  1.00 46.91           C  
ANISOU11062  CG  ASN D  77     6452   5504   5867   -223    189    -35       C  
ATOM  11063  OD1 ASN D  77      -1.102 -15.893  -1.265  1.00 46.49           O  
ANISOU11063  OD1 ASN D  77     6364   5472   5828   -191    190    -38       O  
ATOM  11064  ND2 ASN D  77      -2.005 -17.841  -1.906  1.00 47.54           N  
ANISOU11064  ND2 ASN D  77     6535   5610   5918   -255    188    -54       N  
ATOM  11065  N   LEU D  78       3.408 -17.255   0.236  1.00 45.23           N  
ANISOU11065  N   LEU D  78     6302   5142   5739   -158    187     47       N  
ATOM  11066  CA  LEU D  78       4.444 -17.923   1.017  1.00 45.37           C  
ANISOU11066  CA  LEU D  78     6351   5125   5764   -160    182     66       C  
ATOM  11067  C   LEU D  78       4.051 -18.045   2.487  1.00 47.30           C  
ANISOU11067  C   LEU D  78     6593   5384   5993   -196    176     60       C  
ATOM  11068  O   LEU D  78       3.944 -17.036   3.197  1.00 47.82           O  
ANISOU11068  O   LEU D  78     6623   5473   6070   -190    174     53       O  
ATOM  11069  CB  LEU D  78       5.788 -17.201   0.898  1.00 43.54           C  
ANISOU11069  CB  LEU D  78     6105   4870   5568   -114    183     85       C  
ATOM  11070  CG  LEU D  78       6.404 -16.912  -0.470  1.00 42.46           C  
ANISOU11070  CG  LEU D  78     5963   4719   5447    -73    192     98       C  
ATOM  11071  CD1 LEU D  78       7.702 -16.145  -0.263  1.00 41.32           C  
ANISOU11071  CD1 LEU D  78     5799   4559   5339    -41    193    117       C  
ATOM  11072  CD2 LEU D  78       6.656 -18.187  -1.256  1.00 40.64           C  
ANISOU11072  CD2 LEU D  78     5776   4465   5198    -67    194    104       C  
ATOM  11073  N   PHE D  79       3.837 -19.279   2.945  1.00 47.94           N  
ANISOU11073  N   PHE D  79     6714   5451   6048   -232    174     64       N  
ATOM  11074  CA  PHE D  79       3.562 -19.524   4.362  1.00 46.53           C  
ANISOU11074  CA  PHE D  79     6540   5286   5852   -266    170     65       C  
ATOM  11075  C   PHE D  79       4.834 -20.019   5.020  1.00 46.44           C  
ANISOU11075  C   PHE D  79     6560   5234   5848   -247    164     87       C  
ATOM  11076  O   PHE D  79       5.271 -21.136   4.763  1.00 52.06           O  
ANISOU11076  O   PHE D  79     7321   5908   6550   -249    162    100       O  
ATOM  11077  CB  PHE D  79       2.406 -20.511   4.547  1.00 46.27           C  
ANISOU11077  CB  PHE D  79     6529   5268   5781   -325    173     57       C  
ATOM  11078  CG  PHE D  79       1.127 -20.077   3.878  1.00 45.72           C  
ANISOU11078  CG  PHE D  79     6424   5245   5700   -343    178     32       C  
ATOM  11079  CD1 PHE D  79       0.829 -20.491   2.580  1.00 44.74           C  
ANISOU11079  CD1 PHE D  79     6312   5112   5573   -342    180     25       C  
ATOM  11080  CD2 PHE D  79       0.232 -19.238   4.534  1.00 45.03           C  
ANISOU11080  CD2 PHE D  79     6290   5215   5602   -357    180     15       C  
ATOM  11081  CE1 PHE D  79      -0.338 -20.078   1.956  1.00 45.06           C  
ANISOU11081  CE1 PHE D  79     6317   5201   5600   -355    183      0       C  
ATOM  11082  CE2 PHE D  79      -0.941 -18.828   3.916  1.00 44.28           C  
ANISOU11082  CE2 PHE D  79     6160   5169   5494   -368    184     -9       C  
ATOM  11083  CZ  PHE D  79      -1.226 -19.248   2.626  1.00 44.44           C  
ANISOU11083  CZ  PHE D  79     6191   5180   5511   -368    185    -16       C  
ATOM  11084  N   ILE D  80       5.444 -19.167   5.839  1.00 44.81           N  
ANISOU11084  N   ILE D  80     6326   5037   5661   -225    158     88       N  
ATOM  11085  CA  ILE D  80       6.736 -19.472   6.444  1.00 44.81           C  
ANISOU11085  CA  ILE D  80     6346   5006   5671   -199    150    106       C  
ATOM  11086  C   ILE D  80       6.609 -19.626   7.954  1.00 45.96           C  
ANISOU11086  C   ILE D  80     6498   5167   5797   -220    143    107       C  
ATOM  11087  O   ILE D  80       5.833 -18.918   8.588  1.00 46.93           O  
ANISOU11087  O   ILE D  80     6587   5330   5913   -237    143     91       O  
ATOM  11088  CB  ILE D  80       7.806 -18.412   6.080  1.00 44.26           C  
ANISOU11088  CB  ILE D  80     6242   4930   5642   -152    147    109       C  
ATOM  11089  CG1 ILE D  80       7.940 -18.306   4.554  1.00 46.36           C  
ANISOU11089  CG1 ILE D  80     6506   5185   5924   -129    157    113       C  
ATOM  11090  CG2 ILE D  80       9.157 -18.763   6.689  1.00 42.13           C  
ANISOU11090  CG2 ILE D  80     5988   4636   5381   -125    138    125       C  
ATOM  11091  CD1 ILE D  80       8.910 -17.257   4.055  1.00 46.11           C  
ANISOU11091  CD1 ILE D  80     6439   5148   5932    -89    158    119       C  
ATOM  11092  N   SER D  81       7.361 -20.578   8.507  1.00 47.75           N  
ANISOU11092  N   SER D  81     6767   5364   6010   -215    137    125       N  
ATOM  11093  CA  SER D  81       7.482 -20.777   9.948  1.00 48.48           C  
ANISOU11093  CA  SER D  81     6870   5467   6083   -225    130    131       C  
ATOM  11094  C   SER D  81       8.945 -20.937  10.322  1.00 48.21           C  
ANISOU11094  C   SER D  81     6848   5406   6061   -181    118    145       C  
ATOM  11095  O   SER D  81       9.721 -21.524   9.567  1.00 46.74           O  
ANISOU11095  O   SER D  81     6690   5185   5883   -155    117    157       O  
ATOM  11096  CB  SER D  81       6.733 -22.032  10.388  1.00 49.72           C  
ANISOU11096  CB  SER D  81     7077   5615   6198   -271    135    143       C  
ATOM  11097  OG  SER D  81       5.370 -21.947  10.034  1.00 58.42           O  
ANISOU11097  OG  SER D  81     8163   6748   7286   -316    146    129       O  
ATOM  11098  N   VAL D  82       9.310 -20.416  11.490  1.00 49.86           N  
ANISOU11098  N   VAL D  82     7036   5636   6270   -170    108    140       N  
ATOM  11099  CA  VAL D  82      10.619 -20.672  12.086  1.00 53.18           C  
ANISOU11099  CA  VAL D  82     7470   6040   6694   -131     94    152       C  
ATOM  11100  C   VAL D  82      10.398 -21.363  13.426  1.00 54.48           C  
ANISOU11100  C   VAL D  82     7667   6212   6817   -148     89    162       C  
ATOM  11101  O   VAL D  82       9.781 -20.791  14.325  1.00 54.94           O  
ANISOU11101  O   VAL D  82     7700   6309   6865   -166     87    149       O  
ATOM  11102  CB  VAL D  82      11.450 -19.387  12.309  1.00 56.10           C  
ANISOU11102  CB  VAL D  82     7783   6428   7101    -98     82    137       C  
ATOM  11103  CG1 VAL D  82      12.890 -19.749  12.645  1.00 58.08           C  
ANISOU11103  CG1 VAL D  82     8045   6662   7358    -56     69    149       C  
ATOM  11104  CG2 VAL D  82      11.407 -18.473  11.089  1.00 56.36           C  
ANISOU11104  CG2 VAL D  82     7778   6460   7173    -91     90    128       C  
ATOM  11105  N   ASN D  83      10.896 -22.595  13.539  1.00 55.58           N  
ANISOU11105  N   ASN D  83     7867   6317   6933   -139     86    185       N  
ATOM  11106  CA  ASN D  83      10.690 -23.443  14.715  1.00 55.45           C  
ANISOU11106  CA  ASN D  83     7894   6299   6873   -155     83    201       C  
ATOM  11107  C   ASN D  83       9.269 -23.359  15.247  1.00 56.64           C  
ANISOU11107  C   ASN D  83     8038   6483   6998   -212     95    196       C  
ATOM  11108  O   ASN D  83       9.044 -23.006  16.402  1.00 57.82           O  
ANISOU11108  O   ASN D  83     8171   6670   7129   -217     92    192       O  
ATOM  11109  CB  ASN D  83      11.719 -23.130  15.807  1.00 54.11           C  
ANISOU11109  CB  ASN D  83     7712   6145   6702   -113     65    201       C  
ATOM  11110  CG  ASN D  83      13.144 -23.298  15.322  1.00 54.50           C  
ANISOU11110  CG  ASN D  83     7766   6168   6772    -57     53    206       C  
ATOM  11111  OD1 ASN D  83      13.469 -24.261  14.627  1.00 54.77           O  
ANISOU11111  OD1 ASN D  83     7849   6161   6799    -45     55    223       O  
ATOM  11112  ND2 ASN D  83      14.001 -22.354  15.675  1.00 53.29           N  
ANISOU11112  ND2 ASN D  83     7562   6040   6645    -23     39    190       N  
ATOM  11113  N   SER D  84       8.318 -23.667  14.368  1.00 61.12           N  
ANISOU11113  N   SER D  84     8615   7044   7564   -252    110    195       N  
ATOM  11114  CA  SER D  84       6.876 -23.645  14.666  1.00 64.40           C  
ANISOU11114  CA  SER D  84     9019   7496   7954   -311    124    189       C  
ATOM  11115  C   SER D  84       6.251 -22.256  14.862  1.00 62.44           C  
ANISOU11115  C   SER D  84     8697   7306   7720   -312    125    160       C  
ATOM  11116  O   SER D  84       5.028 -22.114  14.784  1.00 62.42           O  
ANISOU11116  O   SER D  84     8675   7339   7702   -354    138    149       O  
ATOM  11117  CB  SER D  84       6.530 -24.580  15.829  1.00 68.48           C  
ANISOU11117  CB  SER D  84     9581   8013   8423   -342    128    213       C  
ATOM  11118  OG  SER D  84       6.721 -25.928  15.442  1.00 76.05           O  
ANISOU11118  OG  SER D  84    10614   8913   9366   -356    129    239       O  
ATOM  11119  N   ILE D  85       7.075 -21.240  15.110  1.00 60.66           N  
ANISOU11119  N   ILE D  85     8432   7092   7524   -266    112    145       N  
ATOM  11120  CA  ILE D  85       6.589 -19.860  15.123  1.00 59.40           C  
ANISOU11120  CA  ILE D  85     8209   6977   7384   -259    110    115       C  
ATOM  11121  C   ILE D  85       6.331 -19.448  13.675  1.00 56.55           C  
ANISOU11121  C   ILE D  85     7828   6603   7053   -258    117    104       C  
ATOM  11122  O   ILE D  85       7.242 -19.497  12.848  1.00 53.84           O  
ANISOU11122  O   ILE D  85     7493   6222   6739   -229    114    111       O  
ATOM  11123  CB  ILE D  85       7.594 -18.874  15.769  1.00 60.39           C  
ANISOU11123  CB  ILE D  85     8300   7111   7534   -213     91    100       C  
ATOM  11124  CG1 ILE D  85       8.228 -19.439  17.063  1.00 61.96           C  
ANISOU11124  CG1 ILE D  85     8526   7311   7704   -200     80    114       C  
ATOM  11125  CG2 ILE D  85       6.944 -17.508  15.968  1.00 58.67           C  
ANISOU11125  CG2 ILE D  85     8025   6937   7329   -210     87     68       C  
ATOM  11126  CD1 ILE D  85       7.263 -19.831  18.172  1.00 65.42           C  
ANISOU11126  CD1 ILE D  85     8975   7789   8092   -234     88    119       C  
ATOM  11127  N   GLU D  86       5.094 -19.061  13.369  1.00 55.27           N  
ANISOU11127  N   GLU D  86     7640   6478   6882   -288    128     88       N  
ATOM  11128  CA  GLU D  86       4.718 -18.777  11.978  1.00 55.60           C  
ANISOU11128  CA  GLU D  86     7667   6511   6946   -288    135     79       C  
ATOM  11129  C   GLU D  86       4.566 -17.305  11.612  1.00 51.76           C  
ANISOU11129  C   GLU D  86     7126   6050   6490   -261    131     53       C  
ATOM  11130  O   GLU D  86       3.873 -16.537  12.278  1.00 50.48           O  
ANISOU11130  O   GLU D  86     6930   5933   6317   -265    129     33       O  
ATOM  11131  CB  GLU D  86       3.484 -19.581  11.540  1.00 59.76           C  
ANISOU11131  CB  GLU D  86     8210   7051   7441   -340    150     80       C  
ATOM  11132  CG  GLU D  86       2.195 -19.285  12.291  1.00 64.36           C  
ANISOU11132  CG  GLU D  86     8763   7699   7992   -376    157     65       C  
ATOM  11133  CD  GLU D  86       1.075 -20.242  11.915  1.00 71.01           C  
ANISOU11133  CD  GLU D  86     9623   8552   8802   -434    171     69       C  
ATOM  11134  OE1 GLU D  86      -0.072 -20.037  12.380  1.00 71.45           O  
ANISOU11134  OE1 GLU D  86     9649   8669   8830   -467    179     56       O  
ATOM  11135  OE2 GLU D  86       1.339 -21.200  11.150  1.00 71.89           O  
ANISOU11135  OE2 GLU D  86     9780   8617   8917   -447    173     84       O  
ATOM  11136  N   LEU D  87       5.242 -16.935  10.530  1.00 51.26           N  
ANISOU11136  N   LEU D  87     7058   5955   6463   -232    130     56       N  
ATOM  11137  CA  LEU D  87       5.164 -15.597   9.970  1.00 49.84           C  
ANISOU11137  CA  LEU D  87     6835   5786   6314   -205    128     38       C  
ATOM  11138  C   LEU D  87       3.820 -15.406   9.281  1.00 46.87           C  
ANISOU11138  C   LEU D  87     6441   5443   5922   -225    138     22       C  
ATOM  11139  O   LEU D  87       3.231 -16.383   8.817  1.00 45.97           O  
ANISOU11139  O   LEU D  87     6352   5330   5784   -256    148     29       O  
ATOM  11140  CB  LEU D  87       6.302 -15.377   8.971  1.00 48.70           C  
ANISOU11140  CB  LEU D  87     6693   5599   6209   -172    127     51       C  
ATOM  11141  CG  LEU D  87       7.687 -15.042   9.523  1.00 51.93           C  
ANISOU11141  CG  LEU D  87     7097   5986   6646   -142    114     59       C  
ATOM  11142  CD1 LEU D  87       8.335 -16.253  10.184  1.00 55.73           C  
ANISOU11142  CD1 LEU D  87     7619   6450   7106   -147    110     78       C  
ATOM  11143  CD2 LEU D  87       8.571 -14.547   8.395  1.00 51.97           C  
ANISOU11143  CD2 LEU D  87     7091   5963   6692   -113    118     70       C  
ATOM  11144  N   PRO D  88       3.329 -14.149   9.208  1.00 46.81           N  
ANISOU11144  N   PRO D  88     6394   5464   5926   -207    134      0       N  
ATOM  11145  CA  PRO D  88       2.106 -13.918   8.434  1.00 46.04           C  
ANISOU11145  CA  PRO D  88     6278   5401   5814   -217    143    -16       C  
ATOM  11146  C   PRO D  88       2.286 -14.282   6.956  1.00 45.45           C  
ANISOU11146  C   PRO D  88     6218   5295   5753   -210    152     -3       C  
ATOM  11147  O   PRO D  88       3.412 -14.259   6.427  1.00 44.34           O  
ANISOU11147  O   PRO D  88     6091   5111   5643   -185    151     14       O  
ATOM  11148  CB  PRO D  88       1.857 -12.407   8.583  1.00 43.69           C  
ANISOU11148  CB  PRO D  88     5940   5125   5533   -184    134    -40       C  
ATOM  11149  CG  PRO D  88       2.681 -11.982   9.747  1.00 44.61           C  
ANISOU11149  CG  PRO D  88     6054   5231   5663   -170    120    -41       C  
ATOM  11150  CD  PRO D  88       3.864 -12.897   9.781  1.00 45.34           C  
ANISOU11150  CD  PRO D  88     6180   5278   5768   -174    120    -13       C  
ATOM  11151  N   LYS D  89       1.173 -14.629   6.315  1.00 44.16           N  
ANISOU11151  N   LYS D  89     6051   5162   5565   -232    161    -14       N  
ATOM  11152  CA  LYS D  89       1.130 -14.894   4.886  1.00 43.20           C  
ANISOU11152  CA  LYS D  89     5939   5023   5450   -223    168     -9       C  
ATOM  11153  C   LYS D  89       1.887 -13.798   4.145  1.00 43.96           C  
ANISOU11153  C   LYS D  89     6021   5095   5586   -173    166     -3       C  
ATOM  11154  O   LYS D  89       1.828 -12.622   4.496  1.00 43.66           O  
ANISOU11154  O   LYS D  89     5954   5070   5563   -150    160    -16       O  
ATOM  11155  CB  LYS D  89      -0.326 -14.997   4.417  1.00 43.92           C  
ANISOU11155  CB  LYS D  89     6011   5165   5509   -247    173    -31       C  
ATOM  11156  CG  LYS D  89      -0.552 -15.057   2.915  1.00 46.43           C  
ANISOU11156  CG  LYS D  89     6332   5478   5831   -231    179    -33       C  
ATOM  11157  CD  LYS D  89      -2.006 -14.730   2.590  1.00 48.93           C  
ANISOU11157  CD  LYS D  89     6614   5858   6119   -242    180    -61       C  
ATOM  11158  CE  LYS D  89      -2.158 -14.104   1.209  1.00 50.48           C  
ANISOU11158  CE  LYS D  89     6798   6057   6325   -202    182    -67       C  
ATOM  11159  NZ  LYS D  89      -3.555 -13.651   0.949  1.00 50.79           N  
ANISOU11159  NZ  LYS D  89     6799   6163   6334   -203    181    -97       N  
ATOM  11160  N   ARG D  90       2.609 -14.210   3.119  1.00 45.84           N  
ANISOU11160  N   ARG D  90     6281   5296   5840   -157    172     14       N  
ATOM  11161  CA  ARG D  90       3.459 -13.332   2.361  1.00 44.42           C  
ANISOU11161  CA  ARG D  90     6090   5089   5696   -115    174     27       C  
ATOM  11162  C   ARG D  90       3.104 -13.492   0.878  1.00 44.58           C  
ANISOU11162  C   ARG D  90     6116   5112   5711   -100    184     29       C  
ATOM  11163  O   ARG D  90       3.315 -14.556   0.293  1.00 47.60           O  
ANISOU11163  O   ARG D  90     6527   5478   6081   -108    188     39       O  
ATOM  11164  CB  ARG D  90       4.901 -13.744   2.629  1.00 42.67           C  
ANISOU11164  CB  ARG D  90     5889   4825   5498   -104    172     51       C  
ATOM  11165  CG  ARG D  90       5.895 -12.636   2.457  1.00 45.00           C  
ANISOU11165  CG  ARG D  90     6163   5098   5834    -71    171     63       C  
ATOM  11166  CD  ARG D  90       7.306 -13.133   2.679  1.00 47.66           C  
ANISOU11166  CD  ARG D  90     6516   5403   6190    -61    169     85       C  
ATOM  11167  NE  ARG D  90       8.084 -12.124   3.388  1.00 52.74           N  
ANISOU11167  NE  ARG D  90     7134   6036   6866    -49    159     86       N  
ATOM  11168  CZ  ARG D  90       8.392 -10.926   2.898  1.00 53.56           C  
ANISOU11168  CZ  ARG D  90     7214   6131   7004    -29    161     90       C  
ATOM  11169  NH1 ARG D  90       7.997 -10.565   1.678  1.00 50.43           N  
ANISOU11169  NH1 ARG D  90     6814   5736   6609    -13    174     96       N  
ATOM  11170  NH2 ARG D  90       9.105 -10.088   3.639  1.00 55.75           N  
ANISOU11170  NH2 ARG D  90     7471   6397   7311    -24    149     87       N  
ATOM  11171  N   LYS D  91       2.541 -12.445   0.280  1.00 43.50           N  
ANISOU11171  N   LYS D  91     5952   4995   5578    -75    186     19       N  
ATOM  11172  CA  LYS D  91       2.175 -12.472  -1.137  1.00 42.52           C  
ANISOU11172  CA  LYS D  91     5830   4878   5446    -55    194     20       C  
ATOM  11173  C   LYS D  91       3.289 -11.887  -2.017  1.00 42.83           C  
ANISOU11173  C   LYS D  91     5871   4881   5518    -14    202     47       C  
ATOM  11174  O   LYS D  91       3.729 -10.772  -1.800  1.00 40.97           O  
ANISOU11174  O   LYS D  91     5618   4634   5312      6    201     55       O  
ATOM  11175  CB  LYS D  91       0.844 -11.749  -1.361  1.00 42.31           C  
ANISOU11175  CB  LYS D  91     5775   4900   5398    -48    192     -5       C  
ATOM  11176  CG  LYS D  91       0.296 -11.856  -2.774  1.00 44.64           C  
ANISOU11176  CG  LYS D  91     6071   5212   5677    -28    198     -9       C  
ATOM  11177  CD  LYS D  91      -0.993 -11.067  -2.961  1.00 44.55           C  
ANISOU11177  CD  LYS D  91     6029   5253   5643    -15    194    -37       C  
ATOM  11178  CE  LYS D  91      -1.394 -11.051  -4.430  1.00 45.15           C  
ANISOU11178  CE  LYS D  91     6106   5344   5705     14    200    -38       C  
ATOM  11179  NZ  LYS D  91      -2.748 -10.476  -4.664  1.00 47.40           N  
ANISOU11179  NZ  LYS D  91     6361   5689   5960     27    195    -68       N  
ATOM  11180  N   GLU D  92       3.748 -12.669  -2.994  1.00 46.28           N  
ANISOU11180  N   GLU D  92     6329   5302   5951     -4    211     63       N  
ATOM  11181  CA  GLU D  92       4.792 -12.245  -3.936  1.00 47.21           C  
ANISOU11181  CA  GLU D  92     6448   5393   6094     34    222     91       C  
ATOM  11182  C   GLU D  92       4.325 -12.364  -5.393  1.00 46.93           C  
ANISOU11182  C   GLU D  92     6417   5373   6039     60    231     92       C  
ATOM  11183  O   GLU D  92       3.980 -13.456  -5.861  1.00 45.20           O  
ANISOU11183  O   GLU D  92     6219   5161   5792     49    230     82       O  
ATOM  11184  CB  GLU D  92       6.073 -13.068  -3.742  1.00 49.51           C  
ANISOU11184  CB  GLU D  92     6760   5651   6397     33    224    113       C  
ATOM  11185  CG  GLU D  92       6.710 -12.972  -2.363  1.00 53.99           C  
ANISOU11185  CG  GLU D  92     7324   6204   6984     14    214    115       C  
ATOM  11186  CD  GLU D  92       7.015 -11.549  -1.922  1.00 58.30           C  
ANISOU11186  CD  GLU D  92     7840   6746   7565     25    211    118       C  
ATOM  11187  OE1 GLU D  92       7.438 -10.722  -2.760  1.00 58.11           O  
ANISOU11187  OE1 GLU D  92     7803   6713   7563     53    221    136       O  
ATOM  11188  OE2 GLU D  92       6.838 -11.259  -0.716  1.00 64.24           O  
ANISOU11188  OE2 GLU D  92     8582   7503   8320      5    199    103       O  
ATOM  11189  N   VAL D  93       4.327 -11.244  -6.109  1.00 45.09           N  
ANISOU11189  N   VAL D  93     6167   5143   5820     94    239    103       N  
ATOM  11190  CA  VAL D  93       3.851 -11.233  -7.484  1.00 46.37           C  
ANISOU11190  CA  VAL D  93     6331   5325   5961    125    247    104       C  
ATOM  11191  C   VAL D  93       5.017 -11.273  -8.474  1.00 49.96           C  
ANISOU11191  C   VAL D  93     6795   5756   6430    159    263    139       C  
ATOM  11192  O   VAL D  93       5.995 -10.540  -8.330  1.00 51.86           O  
ANISOU11192  O   VAL D  93     7026   5972   6705    170    271    167       O  
ATOM  11193  CB  VAL D  93       2.916 -10.038  -7.756  1.00 44.46           C  
ANISOU11193  CB  VAL D  93     6068   5108   5714    146    246     93       C  
ATOM  11194  CG1 VAL D  93       2.388 -10.083  -9.182  1.00 45.82           C  
ANISOU11194  CG1 VAL D  93     6243   5305   5859    181    254     92       C  
ATOM  11195  CG2 VAL D  93       1.750 -10.054  -6.787  1.00 42.98           C  
ANISOU11195  CG2 VAL D  93     5868   4955   5508    116    231     56       C  
ATOM  11196  N   LEU D  94       4.906 -12.141  -9.476  1.00 52.52           N  
ANISOU11196  N   LEU D  94     7136   6090   6726    174    268    137       N  
ATOM  11197  CA  LEU D  94       5.947 -12.282 -10.495  1.00 52.23           C  
ANISOU11197  CA  LEU D  94     7108   6041   6695    211    284    168       C  
ATOM  11198  C   LEU D  94       5.494 -11.762 -11.853  1.00 50.57           C  
ANISOU11198  C   LEU D  94     6893   5854   6467    253    295    175       C  
ATOM  11199  O   LEU D  94       6.299 -11.242 -12.629  1.00 49.57           O  
ANISOU11199  O   LEU D  94     6761   5720   6352    288    312    209       O  
ATOM  11200  CB  LEU D  94       6.401 -13.739 -10.589  1.00 52.10           C  
ANISOU11200  CB  LEU D  94     7121   6014   6661    204    279    162       C  
ATOM  11201  CG  LEU D  94       7.229 -14.150  -9.371  1.00 50.37           C  
ANISOU11201  CG  LEU D  94     6907   5765   6463    176    273    168       C  
ATOM  11202  CD1 LEU D  94       7.170 -15.649  -9.170  1.00 50.93           C  
ANISOU11202  CD1 LEU D  94     7015   5826   6508    157    261    151       C  
ATOM  11203  CD2 LEU D  94       8.669 -13.673  -9.496  1.00 49.82           C  
ANISOU11203  CD2 LEU D  94     6825   5678   6425    201    287    206       C  
ATOM  11204  N   CYS D  95       4.203 -11.915 -12.128  1.00 49.45           N  
ANISOU11204  N   CYS D  95     6750   5744   6293    249    284    142       N  
ATOM  11205  CA  CYS D  95       3.599 -11.380 -13.332  1.00 50.75           C  
ANISOU11205  CA  CYS D  95     6908   5938   6435    291    291    143       C  
ATOM  11206  C   CYS D  95       2.373 -10.568 -12.944  1.00 52.36           C  
ANISOU11206  C   CYS D  95     7093   6169   6631    285    281    118       C  
ATOM  11207  O   CYS D  95       1.399 -11.114 -12.414  1.00 53.45           O  
ANISOU11207  O   CYS D  95     7228   6331   6748    252    265     81       O  
ATOM  11208  CB  CYS D  95       3.207 -12.496 -14.308  1.00 51.44           C  
ANISOU11208  CB  CYS D  95     7015   6047   6482    303    287    123       C  
ATOM  11209  SG  CYS D  95       4.416 -13.829 -14.487  1.00 54.56           S  
ANISOU11209  SG  CYS D  95     7439   6412   6877    303    291    136       S  
ATOM  11210  N   HIS D  96       2.432  -9.262 -13.194  1.00 50.32           N  
ANISOU11210  N   HIS D  96     6822   5906   6388    316    289    140       N  
ATOM  11211  CA  HIS D  96       1.305  -8.374 -12.925  1.00 47.26           C  
ANISOU11211  CA  HIS D  96     6419   5546   5992    323    279    117       C  
ATOM  11212  C   HIS D  96       0.345  -8.361 -14.075  1.00 47.70           C  
ANISOU11212  C   HIS D  96     6471   5645   6004    361    278    101       C  
ATOM  11213  O   HIS D  96      -0.792  -7.925 -13.922  1.00 49.25           O  
ANISOU11213  O   HIS D  96     6652   5878   6180    367    266     72       O  
ATOM  11214  CB  HIS D  96       1.788  -6.965 -12.626  1.00 45.92           C  
ANISOU11214  CB  HIS D  96     6243   5345   5857    341    286    146       C  
ATOM  11215  CG  HIS D  96       2.789  -6.894 -11.501  1.00 45.34           C  
ANISOU11215  CG  HIS D  96     6169   5229   5826    305    285    160       C  
ATOM  11216  ND1 HIS D  96       2.452  -6.506 -10.254  1.00 43.71           N  
ANISOU11216  ND1 HIS D  96     5953   5018   5634    278    270    139       N  
ATOM  11217  CD2 HIS D  96       4.155  -7.179 -11.472  1.00 45.35           C  
ANISOU11217  CD2 HIS D  96     6178   5196   5858    296    297    193       C  
ATOM  11218  CE1 HIS D  96       3.546  -6.548  -9.464  1.00 44.86           C  
ANISOU11218  CE1 HIS D  96     6100   5126   5817    252    271    157       C  
ATOM  11219  NE2 HIS D  96       4.587  -6.963 -10.213  1.00 46.13           N  
ANISOU11219  NE2 HIS D  96     6269   5269   5987    263    288    190       N  
ATOM  11220  N   GLY D  97       0.799  -8.828 -15.239  1.00 46.11           N  
ANISOU11220  N   GLY D  97     6284   5447   5788    391    290    119       N  
ATOM  11221  CA  GLY D  97      -0.060  -8.948 -16.419  1.00 47.23           C  
ANISOU11221  CA  GLY D  97     6424   5634   5885    430    287    101       C  
ATOM  11222  C   GLY D  97       0.106  -7.878 -17.484  1.00 47.68           C  
ANISOU11222  C   GLY D  97     6483   5694   5937    493    303    135       C  
ATOM  11223  O   GLY D  97      -0.758  -7.712 -18.341  1.00 48.57           O  
ANISOU11223  O   GLY D  97     6592   5850   6013    531    299    119       O  
ATOM  11224  N   HIS D  98       1.219  -7.155 -17.427  1.00 49.36           N  
ANISOU11224  N   HIS D  98     6702   5863   6188    502    322    183       N  
ATOM  11225  CA  HIS D  98       1.505  -6.061 -18.349  1.00 49.55           C  
ANISOU11225  CA  HIS D  98     6731   5880   6213    555    340    225       C  
ATOM  11226  C   HIS D  98       2.977  -5.835 -18.350  1.00 48.25           C  
ANISOU11226  C   HIS D  98     6573   5670   6088    549    362    276       C  
ATOM  11227  O   HIS D  98       3.548  -5.468 -17.329  1.00 50.30           O  
ANISOU11227  O   HIS D  98     6829   5892   6390    513    361    286       O  
ATOM  11228  CB  HIS D  98       0.776  -4.782 -17.925  1.00 51.97           C  
ANISOU11228  CB  HIS D  98     7032   6184   6527    570    331    220       C  
ATOM  11229  CG  HIS D  98       1.306  -3.523 -18.583  1.00 55.09           C  
ANISOU11229  CG  HIS D  98     7441   6552   6939    613    351    272       C  
ATOM  11230  ND1 HIS D  98       0.813  -3.048 -19.747  1.00 55.05           N  
ANISOU11230  ND1 HIS D  98     7444   6574   6899    672    358    284       N  
ATOM  11231  CD2 HIS D  98       2.322  -2.640 -18.194  1.00 57.03           C  
ANISOU11231  CD2 HIS D  98     7693   6742   7233    600    365    316       C  
ATOM  11232  CE1 HIS D  98       1.478  -1.924 -20.090  1.00 58.32           C  
ANISOU11232  CE1 HIS D  98     7872   6947   7337    696    378    337       C  
ATOM  11233  NE2 HIS D  98       2.403  -1.677 -19.139  1.00 58.77           N  
ANISOU11233  NE2 HIS D  98     7928   6953   7447    649    381    356       N  
ATOM  11234  N   ASP D  99       3.603  -6.062 -19.499  1.00 48.66           N  
ANISOU11234  N   ASP D  99     6633   5731   6125    585    383    308       N  
ATOM  11235  CA  ASP D  99       5.037  -5.850 -19.681  1.00 49.00           C  
ANISOU11235  CA  ASP D  99     6676   5740   6198    584    408    361       C  
ATOM  11236  C   ASP D  99       5.865  -6.448 -18.544  1.00 49.24           C  
ANISOU11236  C   ASP D  99     6701   5741   6266    531    402    356       C  
ATOM  11237  O   ASP D  99       6.619  -5.747 -17.866  1.00 50.05           O  
ANISOU11237  O   ASP D  99     6796   5807   6413    507    409    382       O  
ATOM  11238  CB  ASP D  99       5.342  -4.357 -19.868  1.00 50.10           C  
ANISOU11238  CB  ASP D  99     6817   5851   6365    603    424    407       C  
ATOM  11239  CG  ASP D  99       4.982  -3.847 -21.264  1.00 51.92           C  
ANISOU11239  CG  ASP D  99     7059   6109   6558    666    440    432       C  
ATOM  11240  OD1 ASP D  99       5.037  -2.614 -21.475  1.00 49.92           O  
ANISOU11240  OD1 ASP D  99     6814   5833   6320    685    451    468       O  
ATOM  11241  OD2 ASP D  99       4.653  -4.669 -22.154  1.00 53.01           O  
ANISOU11241  OD2 ASP D  99     7200   6290   6651    698    440    416       O  
ATOM  11242  N   ASP D 100       5.714  -7.754 -18.350  1.00 51.36           N  
ANISOU11242  N   ASP D 100     6974   6025   6514    513    389    321       N  
ATOM  11243  CA  ASP D 100       6.410  -8.478 -17.278  1.00 51.91           C  
ANISOU11243  CA  ASP D 100     7043   6070   6611    467    381    312       C  
ATOM  11244  C   ASP D 100       7.869  -8.838 -17.586  1.00 50.13           C  
ANISOU11244  C   ASP D 100     6815   5830   6400    476    401    350       C  
ATOM  11245  O   ASP D 100       8.262  -8.974 -18.747  1.00 47.92           O  
ANISOU11245  O   ASP D 100     6539   5569   6098    518    419    374       O  
ATOM  11246  CB  ASP D 100       5.620  -9.727 -16.895  1.00 51.23           C  
ANISOU11246  CB  ASP D 100     6967   6000   6495    442    357    260       C  
ATOM  11247  CG  ASP D 100       4.421  -9.402 -16.050  1.00 52.95           C  
ANISOU11247  CG  ASP D 100     7178   6228   6712    414    336    223       C  
ATOM  11248  OD1 ASP D 100       4.593  -8.659 -15.055  1.00 53.50           O  
ANISOU11248  OD1 ASP D 100     7237   6273   6816    389    333    229       O  
ATOM  11249  OD2 ASP D 100       3.314  -9.892 -16.369  1.00 54.93           O  
ANISOU11249  OD2 ASP D 100     7432   6513   6926    416    323    185       O  
ATOM  11250  N   ASP D 101       8.657  -9.007 -16.530  1.00 48.56           N  
ANISOU11250  N   ASP D 101     6610   5603   6236    438    396    354       N  
ATOM  11251  CA  ASP D 101      10.098  -9.166 -16.663  1.00 50.12           C  
ANISOU11251  CA  ASP D 101     6798   5791   6453    443    415    391       C  
ATOM  11252  C   ASP D 101      10.528 -10.533 -17.184  1.00 49.91           C  
ANISOU11252  C   ASP D 101     6786   5781   6395    464    415    382       C  
ATOM  11253  O   ASP D 101      11.674 -10.706 -17.608  1.00 50.49           O  
ANISOU11253  O   ASP D 101     6850   5859   6473    485    434    413       O  
ATOM  11254  CB  ASP D 101      10.787  -8.888 -15.322  1.00 52.58           C  
ANISOU11254  CB  ASP D 101     7095   6070   6810    398    407    395       C  
ATOM  11255  CG  ASP D 101      10.661  -7.448 -14.884  1.00 54.26           C  
ANISOU11255  CG  ASP D 101     7295   6261   7060    382    409    411       C  
ATOM  11256  OD1 ASP D 101      10.402  -6.583 -15.750  1.00 57.65           O  
ANISOU11256  OD1 ASP D 101     7724   6694   7484    410    424    436       O  
ATOM  11257  OD2 ASP D 101      10.829  -7.181 -13.672  1.00 54.56           O  
ANISOU11257  OD2 ASP D 101     7324   6274   7130    344    395    399       O  
ATOM  11258  N   TYR D 102       9.620 -11.504 -17.149  1.00 50.30           N  
ANISOU11258  N   TYR D 102     6858   5841   6412    459    394    337       N  
ATOM  11259  CA  TYR D 102       9.986 -12.889 -17.447  1.00 49.54           C  
ANISOU11259  CA  TYR D 102     6783   5751   6288    473    388    321       C  
ATOM  11260  C   TYR D 102       9.253 -13.445 -18.655  1.00 50.47           C  
ANISOU11260  C   TYR D 102     6920   5899   6358    511    386    301       C  
ATOM  11261  O   TYR D 102       8.099 -13.085 -18.916  1.00 50.48           O  
ANISOU11261  O   TYR D 102     6920   5917   6342    511    377    280       O  
ATOM  11262  CB  TYR D 102       9.741 -13.779 -16.235  1.00 47.82           C  
ANISOU11262  CB  TYR D 102     6582   5510   6075    427    363    285       C  
ATOM  11263  CG  TYR D 102      10.282 -13.210 -14.945  1.00 48.69           C  
ANISOU11263  CG  TYR D 102     6674   5595   6230    388    361    298       C  
ATOM  11264  CD1 TYR D 102       9.440 -12.545 -14.052  1.00 47.55           C  
ANISOU11264  CD1 TYR D 102     6521   5443   6103    351    348    280       C  
ATOM  11265  CD2 TYR D 102      11.634 -13.322 -14.622  1.00 48.28           C  
ANISOU11265  CD2 TYR D 102     6612   5531   6201    392    370    325       C  
ATOM  11266  CE1 TYR D 102       9.929 -12.012 -12.877  1.00 47.85           C  
ANISOU11266  CE1 TYR D 102     6542   5457   6179    318    344    288       C  
ATOM  11267  CE2 TYR D 102      12.132 -12.791 -13.447  1.00 48.37           C  
ANISOU11267  CE2 TYR D 102     6605   5521   6252    357    366    333       C  
ATOM  11268  CZ  TYR D 102      11.274 -12.142 -12.580  1.00 48.62           C  
ANISOU11268  CZ  TYR D 102     6631   5541   6300    320    352    314       C  
ATOM  11269  OH  TYR D 102      11.757 -11.618 -11.409  1.00 50.25           O  
ANISOU11269  OH  TYR D 102     6820   5727   6543    289    346    318       O  
ATOM  11270  N   SER D 103       9.940 -14.323 -19.385  1.00 50.44           N  
ANISOU11270  N   SER D 103     6930   5906   6329    548    391    305       N  
ATOM  11271  CA  SER D 103       9.398 -14.932 -20.597  1.00 51.21           C  
ANISOU11271  CA  SER D 103     7046   6032   6378    590    388    285       C  
ATOM  11272  C   SER D 103       8.234 -15.872 -20.314  1.00 51.23           C  
ANISOU11272  C   SER D 103     7076   6031   6357    561    356    228       C  
ATOM  11273  O   SER D 103       7.390 -16.081 -21.186  1.00 51.56           O  
ANISOU11273  O   SER D 103     7127   6100   6362    584    349    203       O  
ATOM  11274  CB  SER D 103      10.495 -15.655 -21.395  1.00 51.68           C  
ANISOU11274  CB  SER D 103     7116   6104   6416    639    400    302       C  
ATOM  11275  OG  SER D 103      11.100 -16.695 -20.645  1.00 48.91           O  
ANISOU11275  OG  SER D 103     6784   5725   6071    621    386    286       O  
ATOM  11276  N   PHE D 104       8.186 -16.426 -19.101  1.00 51.41           N  
ANISOU11276  N   PHE D 104     7111   6023   6399    509    339    208       N  
ATOM  11277  CA  PHE D 104       7.158 -17.415 -18.748  1.00 52.81           C  
ANISOU11277  CA  PHE D 104     7315   6194   6556    472    310    157       C  
ATOM  11278  C   PHE D 104       5.789 -16.837 -18.395  1.00 54.50           C  
ANISOU11278  C   PHE D 104     7512   6424   6768    437    299    132       C  
ATOM  11279  O   PHE D 104       4.807 -17.578 -18.321  1.00 58.42           O  
ANISOU11279  O   PHE D 104     8026   6927   7242    409    278     90       O  
ATOM  11280  CB  PHE D 104       7.639 -18.365 -17.649  1.00 50.84           C  
ANISOU11280  CB  PHE D 104     7091   5905   6321    434    296    147       C  
ATOM  11281  CG  PHE D 104       8.065 -17.677 -16.389  1.00 50.19           C  
ANISOU11281  CG  PHE D 104     6986   5801   6280    398    301    169       C  
ATOM  11282  CD1 PHE D 104       9.413 -17.441 -16.140  1.00 49.98           C  
ANISOU11282  CD1 PHE D 104     6949   5762   6279    416    316    205       C  
ATOM  11283  CD2 PHE D 104       7.125 -17.278 -15.444  1.00 48.62           C  
ANISOU11283  CD2 PHE D 104     6776   5601   6094    347    290    150       C  
ATOM  11284  CE1 PHE D 104       9.816 -16.813 -14.972  1.00 50.44           C  
ANISOU11284  CE1 PHE D 104     6985   5802   6375    382    318    221       C  
ATOM  11285  CE2 PHE D 104       7.521 -16.647 -14.277  1.00 49.26           C  
ANISOU11285  CE2 PHE D 104     6838   5665   6212    317    293    167       C  
ATOM  11286  CZ  PHE D 104       8.869 -16.414 -14.039  1.00 49.93           C  
ANISOU11286  CZ  PHE D 104     6914   5733   6324    334    306    202       C  
ATOM  11287  N   CYS D 105       5.721 -15.525 -18.186  1.00 54.69           N  
ANISOU11287  N   CYS D 105     7505   6457   6817    439    313    157       N  
ATOM  11288  CA  CYS D 105       4.447 -14.856 -17.926  1.00 56.52           C  
ANISOU11288  CA  CYS D 105     7718   6711   7044    418    304    134       C  
ATOM  11289  C   CYS D 105       3.500 -14.916 -19.135  1.00 59.97           C  
ANISOU11289  C   CYS D 105     8156   7191   7438    452    298    110       C  
ATOM  11290  O   CYS D 105       2.284 -14.818 -18.976  1.00 60.04           O  
ANISOU11290  O   CYS D 105     8154   7225   7431    431    283     76       O  
ATOM  11291  CB  CYS D 105       4.674 -13.406 -17.483  1.00 57.42           C  
ANISOU11291  CB  CYS D 105     7804   6819   7192    420    319    167       C  
ATOM  11292  SG  CYS D 105       5.665 -13.222 -15.974  1.00 59.25           S  
ANISOU11292  SG  CYS D 105     8030   7007   7475    376    320    188       S  
ATOM  11293  N   ARG D 106       4.052 -15.085 -20.337  1.00 62.37           N  
ANISOU11293  N   ARG D 106     8468   7507   7720    507    311    127       N  
ATOM  11294  CA  ARG D 106       3.219 -15.242 -21.534  1.00 61.98           C  
ANISOU11294  CA  ARG D 106     8422   7500   7625    545    304    102       C  
ATOM  11295  C   ARG D 106       2.829 -16.695 -21.794  1.00 62.54           C  
ANISOU11295  C   ARG D 106     8523   7573   7665    531    280     56       C  
ATOM  11296  O   ARG D 106       1.917 -16.963 -22.584  1.00 63.08           O  
ANISOU11296  O   ARG D 106     8593   7678   7696    547    266     21       O  
ATOM  11297  CB  ARG D 106       3.884 -14.637 -22.771  1.00 63.67           C  
ANISOU11297  CB  ARG D 106     8631   7733   7825    616    329    142       C  
ATOM  11298  CG  ARG D 106       5.114 -15.374 -23.273  1.00 66.63           C  
ANISOU11298  CG  ARG D 106     9025   8096   8195    647    340    163       C  
ATOM  11299  CD  ARG D 106       5.768 -14.667 -24.455  1.00 70.30           C  
ANISOU11299  CD  ARG D 106     9480   8586   8645    715    369    208       C  
ATOM  11300  NE  ARG D 106       5.863 -13.218 -24.262  1.00 74.07           N  
ANISOU11300  NE  ARG D 106     9931   9060   9151    717    390    251       N  
ATOM  11301  CZ  ARG D 106       5.367 -12.311 -25.101  1.00 75.13           C  
ANISOU11301  CZ  ARG D 106    10055   9224   9264    758    402    268       C  
ATOM  11302  NH1 ARG D 106       4.758 -12.699 -26.214  1.00 77.68           N  
ANISOU11302  NH1 ARG D 106    10387   9588   9537    804    394    244       N  
ATOM  11303  NH2 ARG D 106       5.494 -11.013 -24.837  1.00 71.01           N  
ANISOU11303  NH2 ARG D 106     9517   8691   8773    756    419    307       N  
ATOM  11304  N   ALA D 107       3.512 -17.623 -21.124  1.00 61.02           N  
ANISOU11304  N   ALA D 107     8355   7340   7488    501    273     53       N  
ATOM  11305  CA  ALA D 107       3.271 -19.052 -21.311  1.00 58.23           C  
ANISOU11305  CA  ALA D 107     8039   6976   7109    486    249     12       C  
ATOM  11306  C   ALA D 107       1.871 -19.451 -20.861  1.00 57.49           C  
ANISOU11306  C   ALA D 107     7944   6895   7002    428    224    -36       C  
ATOM  11307  O   ALA D 107       1.428 -19.078 -19.772  1.00 58.77           O  
ANISOU11307  O   ALA D 107     8090   7052   7188    376    222    -38       O  
ATOM  11308  CB  ALA D 107       4.324 -19.871 -20.592  1.00 57.88           C  
ANISOU11308  CB  ALA D 107     8025   6882   7085    468    248     24       C  
ATOM  11309  N   LEU D 108       1.191 -20.213 -21.713  1.00 57.14           N  
ANISOU11309  N   LEU D 108     7917   6873   6920    437    205    -78       N  
ATOM  11310  CA  LEU D 108      -0.219 -20.549 -21.526  1.00 56.86           C  
ANISOU11310  CA  LEU D 108     7873   6863   6866    386    181   -127       C  
ATOM  11311  C   LEU D 108      -0.425 -21.830 -20.734  1.00 56.95           C  
ANISOU11311  C   LEU D 108     7921   6834   6881    317    158   -157       C  
ATOM  11312  O   LEU D 108       0.541 -22.519 -20.392  1.00 56.84           O  
ANISOU11312  O   LEU D 108     7944   6770   6881    315    159   -142       O  
ATOM  11313  CB  LEU D 108      -0.923 -20.656 -22.884  1.00 55.86           C  
ANISOU11313  CB  LEU D 108     7742   6785   6695    430    169   -160       C  
ATOM  11314  CG  LEU D 108      -0.912 -19.410 -23.777  1.00 55.52           C  
ANISOU11314  CG  LEU D 108     7667   6788   6640    501    189   -133       C  
ATOM  11315  CD1 LEU D 108      -1.874 -19.584 -24.939  1.00 52.71           C  
ANISOU11315  CD1 LEU D 108     7304   6487   6235    532    171   -175       C  
ATOM  11316  CD2 LEU D 108      -1.240 -18.141 -22.996  1.00 53.88           C  
ANISOU11316  CD2 LEU D 108     7419   6592   6458    485    203   -108       C  
ATOM  11317  N   LYS D 109      -1.690 -22.135 -20.437  1.00 56.77           N  
ANISOU11317  N   LYS D 109     7886   6835   6845    260    139   -199       N  
ATOM  11318  CA  LYS D 109      -2.054 -23.402 -19.813  1.00 56.30           C  
ANISOU11318  CA  LYS D 109     7863   6741   6784    188    116   -231       C  
ATOM  11319  C   LYS D 109      -1.667 -24.559 -20.722  1.00 59.16           C  
ANISOU11319  C   LYS D 109     8278   7076   7123    213     98   -254       C  
ATOM  11320  O   LYS D 109      -1.977 -24.550 -21.915  1.00 61.43           O  
ANISOU11320  O   LYS D 109     8560   7399   7379    259     91   -277       O  
ATOM  11321  CB  LYS D 109      -3.549 -23.463 -19.497  1.00 54.05           C  
ANISOU11321  CB  LYS D 109     7549   6500   6485    123     99   -273       C  
ATOM  11322  CG  LYS D 109      -4.046 -24.875 -19.198  1.00 55.49           C  
ANISOU11322  CG  LYS D 109     7773   6652   6657     51     73   -311       C  
ATOM  11323  CD  LYS D 109      -5.278 -24.910 -18.309  1.00 54.75           C  
ANISOU11323  CD  LYS D 109     7648   6589   6563    -34     64   -336       C  
ATOM  11324  CE  LYS D 109      -6.569 -24.771 -19.090  1.00 55.30           C  
ANISOU11324  CE  LYS D 109     7678   6731   6599    -40     48   -384       C  
ATOM  11325  NZ  LYS D 109      -7.727 -24.746 -18.156  1.00 57.99           N  
ANISOU11325  NZ  LYS D 109     7982   7110   6939   -122     43   -405       N  
ATOM  11326  N   GLY D 110      -0.985 -25.546 -20.148  1.00 60.66           N  
ANISOU11326  N   GLY D 110     8519   7203   7325    188     91   -248       N  
ATOM  11327  CA  GLY D 110      -0.622 -26.757 -20.870  1.00 61.56           C  
ANISOU11327  CA  GLY D 110     8691   7280   7417    208     71   -274       C  
ATOM  11328  C   GLY D 110       0.539 -26.564 -21.822  1.00 62.71           C  
ANISOU11328  C   GLY D 110     8847   7424   7552    303     84   -249       C  
ATOM  11329  O   GLY D 110       0.723 -27.361 -22.742  1.00 64.01           O  
ANISOU11329  O   GLY D 110     9050   7579   7689    340     68   -275       O  
ATOM  11330  N   GLU D 111       1.314 -25.502 -21.600  1.00 61.79           N  
ANISOU11330  N   GLU D 111     8697   7320   7458    341    115   -199       N  
ATOM  11331  CA  GLU D 111       2.489 -25.195 -22.409  1.00 60.88           C  
ANISOU11331  CA  GLU D 111     8583   7210   7337    427    134   -166       C  
ATOM  11332  C   GLU D 111       3.736 -25.619 -21.644  1.00 61.99           C  
ANISOU11332  C   GLU D 111     8753   7297   7501    431    142   -135       C  
ATOM  11333  O   GLU D 111       3.755 -25.596 -20.413  1.00 63.78           O  
ANISOU11333  O   GLU D 111     8980   7495   7758    375    143   -122       O  
ATOM  11334  CB  GLU D 111       2.537 -23.698 -22.741  1.00 61.19           C  
ANISOU11334  CB  GLU D 111     8564   7300   7385    467    163   -130       C  
ATOM  11335  CG  GLU D 111       3.588 -23.304 -23.773  1.00 64.24           C  
ANISOU11335  CG  GLU D 111     8945   7705   7758    555    185    -97       C  
ATOM  11336  CD  GLU D 111       3.750 -21.800 -23.950  1.00 63.56           C  
ANISOU11336  CD  GLU D 111     8807   7656   7686    586    216    -52       C  
ATOM  11337  OE1 GLU D 111       4.906 -21.332 -24.017  1.00 65.39           O  
ANISOU11337  OE1 GLU D 111     9030   7882   7933    626    241     -5       O  
ATOM  11338  OE2 GLU D 111       2.731 -21.083 -24.034  1.00 64.85           O  
ANISOU11338  OE2 GLU D 111     8939   7855   7844    572    214    -63       O  
ATOM  11339  N   THR D 112       4.769 -26.021 -22.374  1.00 62.27           N  
ANISOU11339  N   THR D 112     8813   7323   7520    499    146   -123       N  
ATOM  11340  CA  THR D 112       6.023 -26.441 -21.762  1.00 63.31           C  
ANISOU11340  CA  THR D 112     8971   7412   7669    515    153    -95       C  
ATOM  11341  C   THR D 112       6.874 -25.212 -21.421  1.00 62.63           C  
ANISOU11341  C   THR D 112     8834   7347   7613    538    187    -39       C  
ATOM  11342  O   THR D 112       7.184 -24.394 -22.296  1.00 62.83           O  
ANISOU11342  O   THR D 112     8825   7416   7631    593    209    -16       O  
ATOM  11343  CB  THR D 112       6.790 -27.419 -22.683  1.00 66.88           C  
ANISOU11343  CB  THR D 112     9472   7851   8089    583    142   -109       C  
ATOM  11344  OG1 THR D 112       5.933 -28.513 -23.042  1.00 70.15           O  
ANISOU11344  OG1 THR D 112     9935   8242   8475    558    107   -165       O  
ATOM  11345  CG2 THR D 112       8.044 -27.966 -21.999  1.00 67.22           C  
ANISOU11345  CG2 THR D 112     9544   7849   8144    600    144    -85       C  
ATOM  11346  N   VAL D 113       7.224 -25.085 -20.142  1.00 59.85           N  
ANISOU11346  N   VAL D 113     8478   6965   7297    494    192    -18       N  
ATOM  11347  CA  VAL D 113       8.063 -23.988 -19.659  1.00 59.05           C  
ANISOU11347  CA  VAL D 113     8331   6875   7228    507    220     30       C  
ATOM  11348  C   VAL D 113       9.411 -24.549 -19.244  1.00 59.40           C  
ANISOU11348  C   VAL D 113     8399   6890   7281    534    223     52       C  
ATOM  11349  O   VAL D 113       9.486 -25.454 -18.412  1.00 62.99           O  
ANISOU11349  O   VAL D 113     8894   7299   7738    502    204     38       O  
ATOM  11350  CB  VAL D 113       7.432 -23.259 -18.444  1.00 58.84           C  
ANISOU11350  CB  VAL D 113     8275   6844   7236    437    222     37       C  
ATOM  11351  CG1 VAL D 113       8.368 -22.189 -17.898  1.00 56.11           C  
ANISOU11351  CG1 VAL D 113     7888   6504   6926    448    248     85       C  
ATOM  11352  CG2 VAL D 113       6.096 -22.642 -18.817  1.00 59.29           C  
ANISOU11352  CG2 VAL D 113     8305   6938   7283    415    220     15       C  
ATOM  11353  N   ASN D 114      10.471 -24.019 -19.839  1.00 59.89           N  
ANISOU11353  N   ASN D 114     8433   6978   7343    595    248     87       N  
ATOM  11354  CA  ASN D 114      11.825 -24.357 -19.436  1.00 62.52           C  
ANISOU11354  CA  ASN D 114     8773   7295   7685    626    254    112       C  
ATOM  11355  C   ASN D 114      12.640 -23.078 -19.372  1.00 59.63           C  
ANISOU11355  C   ASN D 114     8346   6962   7348    642    287    162       C  
ATOM  11356  O   ASN D 114      12.906 -22.446 -20.393  1.00 58.65           O  
ANISOU11356  O   ASN D 114     8193   6879   7213    688    309    183       O  
ATOM  11357  CB  ASN D 114      12.458 -25.382 -20.391  1.00 66.79           C  
ANISOU11357  CB  ASN D 114     9354   7837   8185    696    246     98       C  
ATOM  11358  CG  ASN D 114      13.582 -26.180 -19.739  1.00 71.83           C  
ANISOU11358  CG  ASN D 114    10022   8445   8826    717    238    105       C  
ATOM  11359  OD1 ASN D 114      13.765 -26.153 -18.515  1.00 73.29           O  
ANISOU11359  OD1 ASN D 114    10205   8600   9039    672    234    115       O  
ATOM  11360  ND2 ASN D 114      14.340 -26.907 -20.560  1.00 72.74           N  
ANISOU11360  ND2 ASN D 114    10162   8568   8906    789    236     99       N  
ATOM  11361  N   THR D 115      13.008 -22.687 -18.158  1.00 57.43           N  
ANISOU11361  N   THR D 115     8049   6663   7106    602    290    180       N  
ATOM  11362  CA  THR D 115      13.640 -21.397 -17.943  1.00 55.14           C  
ANISOU11362  CA  THR D 115     7701   6397   6850    601    317    224       C  
ATOM  11363  C   THR D 115      14.556 -21.389 -16.727  1.00 53.82           C  
ANISOU11363  C   THR D 115     7524   6209   6714    581    316    242       C  
ATOM  11364  O   THR D 115      14.364 -22.161 -15.790  1.00 52.55           O  
ANISOU11364  O   THR D 115     7397   6012   6555    548    294    220       O  
ATOM  11365  CB  THR D 115      12.588 -20.268 -17.818  1.00 54.21           C  
ANISOU11365  CB  THR D 115     7553   6290   6753    559    323    226       C  
ATOM  11366  OG1 THR D 115      13.243 -18.999 -17.896  1.00 55.23           O  
ANISOU11366  OG1 THR D 115     7631   6441   6911    569    351    269       O  
ATOM  11367  CG2 THR D 115      11.793 -20.366 -16.502  1.00 50.78           C  
ANISOU11367  CG2 THR D 115     7130   5824   6339    489    303    203       C  
ATOM  11368  N   SER D 116      15.556 -20.511 -16.775  1.00 54.69           N  
ANISOU11368  N   SER D 116     7586   6344   6848    599    341    282       N  
ATOM  11369  CA  SER D 116      16.456 -20.254 -15.660  1.00 55.46           C  
ANISOU11369  CA  SER D 116     7661   6432   6979    579    342    301       C  
ATOM  11370  C   SER D 116      16.302 -18.788 -15.267  1.00 55.60           C  
ANISOU11370  C   SER D 116     7629   6458   7039    541    358    326       C  
ATOM  11371  O   SER D 116      16.494 -17.896 -16.096  1.00 56.04           O  
ANISOU11371  O   SER D 116     7650   6542   7099    561    383    354       O  
ATOM  11372  CB  SER D 116      17.903 -20.534 -16.063  1.00 55.80           C  
ANISOU11372  CB  SER D 116     7688   6501   7013    636    356    325       C  
ATOM  11373  OG  SER D 116      17.982 -21.666 -16.912  1.00 59.11           O  
ANISOU11373  OG  SER D 116     8149   6923   7386    690    347    305       O  
ATOM  11374  N   ILE D 117      15.948 -18.541 -14.009  1.00 54.02           N  
ANISOU11374  N   ILE D 117     7427   6231   6866    487    344    316       N  
ATOM  11375  CA  ILE D 117      15.724 -17.178 -13.545  1.00 51.33           C  
ANISOU11375  CA  ILE D 117     7044   5892   6564    450    354    333       C  
ATOM  11376  C   ILE D 117      16.850 -16.754 -12.624  1.00 50.39           C  
ANISOU11376  C   ILE D 117     6893   5770   6480    437    357    354       C  
ATOM  11377  O   ILE D 117      16.993 -17.302 -11.534  1.00 51.10           O  
ANISOU11377  O   ILE D 117     6999   5840   6575    415    338    338       O  
ATOM  11378  CB  ILE D 117      14.379 -17.027 -12.816  1.00 49.88           C  
ANISOU11378  CB  ILE D 117     6876   5688   6385    399    336    303       C  
ATOM  11379  CG1 ILE D 117      13.235 -17.526 -13.699  1.00 50.43           C  
ANISOU11379  CG1 ILE D 117     6976   5765   6418    408    330    277       C  
ATOM  11380  CG2 ILE D 117      14.153 -15.575 -12.430  1.00 49.32           C  
ANISOU11380  CG2 ILE D 117     6766   5619   6351    370    345    320       C  
ATOM  11381  CD1 ILE D 117      12.165 -18.269 -12.931  1.00 50.98           C  
ANISOU11381  CD1 ILE D 117     7080   5813   6475    364    304    238       C  
ATOM  11382  N   PRO D 118      17.655 -15.772 -13.065  1.00 50.73           N  
ANISOU11382  N   PRO D 118     6891   5837   6547    449    382    392       N  
ATOM  11383  CA  PRO D 118      18.747 -15.252 -12.243  1.00 50.73           C  
ANISOU11383  CA  PRO D 118     6852   5838   6583    433    385    412       C  
ATOM  11384  C   PRO D 118      18.222 -14.475 -11.032  1.00 51.17           C  
ANISOU11384  C   PRO D 118     6898   5868   6675    377    370    400       C  
ATOM  11385  O   PRO D 118      17.128 -13.907 -11.085  1.00 50.61           O  
ANISOU11385  O   PRO D 118     6834   5785   6607    354    368    389       O  
ATOM  11386  CB  PRO D 118      19.499 -14.321 -13.202  1.00 50.02           C  
ANISOU11386  CB  PRO D 118     6718   5779   6507    454    417    455       C  
ATOM  11387  CG  PRO D 118      18.482 -13.908 -14.216  1.00 48.64           C  
ANISOU11387  CG  PRO D 118     6557   5608   6315    464    428    457       C  
ATOM  11388  CD  PRO D 118      17.559 -15.082 -14.368  1.00 49.50           C  
ANISOU11388  CD  PRO D 118     6717   5706   6383    477    407    417       C  
ATOM  11389  N   PHE D 119      19.005 -14.471  -9.956  1.00 52.60           N  
ANISOU11389  N   PHE D 119     7061   6043   6879    359    359    400       N  
ATOM  11390  CA  PHE D 119      18.657 -13.778  -8.717  1.00 52.99           C  
ANISOU11390  CA  PHE D 119     7101   6071   6962    310    343    387       C  
ATOM  11391  C   PHE D 119      19.898 -13.540  -7.857  1.00 54.66           C  
ANISOU11391  C   PHE D 119     7276   6288   7202    301    339    397       C  
ATOM  11392  O   PHE D 119      20.951 -14.153  -8.078  1.00 56.07           O  
ANISOU11392  O   PHE D 119     7445   6489   7369    333    344    409       O  
ATOM  11393  CB  PHE D 119      17.618 -14.581  -7.921  1.00 53.25           C  
ANISOU11393  CB  PHE D 119     7177   6081   6972    289    318    349       C  
ATOM  11394  CG  PHE D 119      18.189 -15.771  -7.198  1.00 52.90           C  
ANISOU11394  CG  PHE D 119     7157   6031   6909    300    301    336       C  
ATOM  11395  CD1 PHE D 119      18.631 -15.659  -5.877  1.00 53.08           C  
ANISOU11395  CD1 PHE D 119     7168   6046   6953    276    285    329       C  
ATOM  11396  CD2 PHE D 119      18.283 -17.006  -7.831  1.00 52.64           C  
ANISOU11396  CD2 PHE D 119     7162   6000   6838    337    300    330       C  
ATOM  11397  CE1 PHE D 119      19.160 -16.752  -5.209  1.00 53.24           C  
ANISOU11397  CE1 PHE D 119     7213   6060   6952    290    269    319       C  
ATOM  11398  CE2 PHE D 119      18.811 -18.103  -7.166  1.00 52.86           C  
ANISOU11398  CE2 PHE D 119     7219   6017   6847    351    283    319       C  
ATOM  11399  CZ  PHE D 119      19.252 -17.975  -5.857  1.00 53.62           C  
ANISOU11399  CZ  PHE D 119     7303   6107   6962    328    268    315       C  
ATOM  11400  N   SER D 120      19.758 -12.655  -6.873  1.00 54.39           N  
ANISOU11400  N   SER D 120     7223   6239   7203    260    327    390       N  
ATOM  11401  CA  SER D 120      20.803 -12.392  -5.889  1.00 53.69           C  
ANISOU11401  CA  SER D 120     7101   6154   7143    245    317    393       C  
ATOM  11402  C   SER D 120      20.155 -11.883  -4.612  1.00 53.42           C  
ANISOU11402  C   SER D 120     7071   6096   7129    202    293    366       C  
ATOM  11403  O   SER D 120      19.034 -11.363  -4.642  1.00 54.26           O  
ANISOU11403  O   SER D 120     7192   6186   7237    183    291    355       O  
ATOM  11404  CB  SER D 120      21.783 -11.335  -6.396  1.00 55.60           C  
ANISOU11404  CB  SER D 120     7290   6413   7421    240    338    427       C  
ATOM  11405  OG  SER D 120      21.466 -10.918  -7.710  1.00 63.29           O  
ANISOU11405  OG  SER D 120     8263   7393   8388    256    364    452       O  
ATOM  11406  N   PHE D 121      20.849 -12.032  -3.490  1.00 52.60           N  
ANISOU11406  N   PHE D 121     6953   5995   7037    192    275    355       N  
ATOM  11407  CA  PHE D 121      20.397 -11.415  -2.245  1.00 54.74           C  
ANISOU11407  CA  PHE D 121     7220   6248   7329    155    253    331       C  
ATOM  11408  C   PHE D 121      21.501 -11.244  -1.200  1.00 55.05           C  
ANISOU11408  C   PHE D 121     7226   6296   7391    145    237    327       C  
ATOM  11409  O   PHE D 121      22.377 -12.096  -1.054  1.00 53.90           O  
ANISOU11409  O   PHE D 121     7078   6170   7229    171    233    330       O  
ATOM  11410  CB  PHE D 121      19.158 -12.124  -1.671  1.00 53.21           C  
ANISOU11410  CB  PHE D 121     7073   6039   7103    146    237    302       C  
ATOM  11411  CG  PHE D 121      19.427 -13.494  -1.135  1.00 51.70           C  
ANISOU11411  CG  PHE D 121     6914   5852   6878    164    224    292       C  
ATOM  11412  CD1 PHE D 121      19.308 -14.604  -1.955  1.00 50.59           C  
ANISOU11412  CD1 PHE D 121     6808   5713   6701    194    233    297       C  
ATOM  11413  CD2 PHE D 121      19.777 -13.675   0.204  1.00 52.06           C  
ANISOU11413  CD2 PHE D 121     6956   5896   6925    153    202    275       C  
ATOM  11414  CE1 PHE D 121      19.545 -15.870  -1.455  1.00 53.61           C  
ANISOU11414  CE1 PHE D 121     7227   6091   7051    212    220    287       C  
ATOM  11415  CE2 PHE D 121      20.016 -14.937   0.714  1.00 51.81           C  
ANISOU11415  CE2 PHE D 121     6960   5866   6860    172    190    268       C  
ATOM  11416  CZ  PHE D 121      19.896 -16.038  -0.118  1.00 54.15           C  
ANISOU11416  CZ  PHE D 121     7294   6157   7121    201    199    275       C  
ATOM  11417  N   GLU D 122      21.421 -10.135  -0.472  1.00 58.61           N  
ANISOU11417  N   GLU D 122     7654   6735   7880    111    224    316       N  
ATOM  11418  CA  GLU D 122      22.500  -9.668   0.389  1.00 62.79           C  
ANISOU11418  CA  GLU D 122     8141   7274   8439     96    209    312       C  
ATOM  11419  C   GLU D 122      22.637 -10.387   1.723  1.00 59.96           C  
ANISOU11419  C   GLU D 122     7796   6923   8063     99    181    284       C  
ATOM  11420  O   GLU D 122      23.743 -10.454   2.264  1.00 66.25           O  
ANISOU11420  O   GLU D 122     8561   7740   8870    104    170    283       O  
ATOM  11421  CB  GLU D 122      22.386  -8.151   0.619  1.00 72.67           C  
ANISOU11421  CB  GLU D 122     9366   8506   9740     58    205    310       C  
ATOM  11422  CG  GLU D 122      23.247  -7.293  -0.306  1.00 78.63           C  
ANISOU11422  CG  GLU D 122    10079   9265  10529     49    227    345       C  
ATOM  11423  CD  GLU D 122      24.724  -7.268   0.095  1.00 86.11           C  
ANISOU11423  CD  GLU D 122    10977  10241  11499     44    221    351       C  
ATOM  11424  OE1 GLU D 122      25.270  -6.156   0.290  1.00 85.64           O  
ANISOU11424  OE1 GLU D 122    10879  10173  11486      9    218    357       O  
ATOM  11425  OE2 GLU D 122      25.343  -8.353   0.218  1.00 85.04           O  
ANISOU11425  OE2 GLU D 122    10840  10137  11335     75    219    350       O  
ATOM  11426  N   GLY D 123      21.533 -10.899   2.263  1.00 52.72           N  
ANISOU11426  N   GLY D 123     6922   5991   7116     96    170    262       N  
ATOM  11427  CA  GLY D 123      21.577 -11.677   3.505  1.00 50.79           C  
ANISOU11427  CA  GLY D 123     6697   5752   6847    101    146    240       C  
ATOM  11428  C   GLY D 123      21.413 -10.892   4.800  1.00 50.93           C  
ANISOU11428  C   GLY D 123     6698   5765   6885     73    121    213       C  
ATOM  11429  O   GLY D 123      22.109  -9.903   5.051  1.00 51.39           O  
ANISOU11429  O   GLY D 123     6714   5827   6984     57    113    211       O  
ATOM  11430  N   ILE D 124      20.488 -11.363   5.628  1.00 51.14           N  
ANISOU11430  N   ILE D 124     6761   5787   6883     67    107    191       N  
ATOM  11431  CA  ILE D 124      20.116 -10.746   6.904  1.00 48.77           C  
ANISOU11431  CA  ILE D 124     6453   5486   6590     46     83    162       C  
ATOM  11432  C   ILE D 124      20.476 -11.776   7.972  1.00 46.50           C  
ANISOU11432  C   ILE D 124     6185   5213   6268     62     65    152       C  
ATOM  11433  O   ILE D 124      20.911 -12.878   7.630  1.00 46.79           O  
ANISOU11433  O   ILE D 124     6243   5255   6278     88     72    168       O  
ATOM  11434  CB  ILE D 124      18.593 -10.422   6.886  1.00 51.27           C  
ANISOU11434  CB  ILE D 124     6795   5789   6894     27     86    148       C  
ATOM  11435  CG1 ILE D 124      18.349  -9.057   6.258  1.00 52.00           C  
ANISOU11435  CG1 ILE D 124     6863   5867   7027     11     94    150       C  
ATOM  11436  CG2 ILE D 124      17.937 -10.460   8.255  1.00 49.53           C  
ANISOU11436  CG2 ILE D 124     6588   5577   6653     16     64    119       C  
ATOM  11437  CD1 ILE D 124      17.981  -9.137   4.799  1.00 56.05           C  
ANISOU11437  CD1 ILE D 124     7387   6371   7537     20    121    175       C  
ATOM  11438  N   LEU D 125      20.328 -11.428   9.249  1.00 45.11           N  
ANISOU11438  N   LEU D 125     6003   5044   6091     51     41    126       N  
ATOM  11439  CA  LEU D 125      20.478 -12.417  10.317  1.00 43.77           C  
ANISOU11439  CA  LEU D 125     5859   4888   5882     67     25    117       C  
ATOM  11440  C   LEU D 125      19.198 -13.230  10.467  1.00 43.60           C  
ANISOU11440  C   LEU D 125     5889   4859   5817     59     32    117       C  
ATOM  11441  O   LEU D 125      18.127 -12.676  10.687  1.00 43.24           O  
ANISOU11441  O   LEU D 125     5847   4811   5771     36     32    102       O  
ATOM  11442  CB  LEU D 125      20.863 -11.768  11.652  1.00 42.30           C  
ANISOU11442  CB  LEU D 125     5645   4718   5708     61     -4     89       C  
ATOM  11443  CG  LEU D 125      21.421 -12.723  12.726  1.00 41.37           C  
ANISOU11443  CG  LEU D 125     5544   4621   5553     87    -22     84       C  
ATOM  11444  CD1 LEU D 125      22.736 -13.364  12.296  1.00 39.07           C  
ANISOU11444  CD1 LEU D 125     5240   4342   5262    119    -21    103       C  
ATOM  11445  CD2 LEU D 125      21.592 -12.021  14.064  1.00 39.15           C  
ANISOU11445  CD2 LEU D 125     5237   4357   5278     81    -52     52       C  
ATOM  11446  N   PHE D 126      19.321 -14.545  10.325  1.00 46.47           N  
ANISOU11446  N   PHE D 126     6293   5219   6143     79     38    133       N  
ATOM  11447  CA  PHE D 126      18.208 -15.470  10.532  1.00 48.10           C  
ANISOU11447  CA  PHE D 126     6552   5416   6305     67     44    135       C  
ATOM  11448  C   PHE D 126      18.492 -16.335  11.754  1.00 47.90           C  
ANISOU11448  C   PHE D 126     6556   5400   6244     81     27    132       C  
ATOM  11449  O   PHE D 126      19.619 -16.792  11.934  1.00 50.31           O  
ANISOU11449  O   PHE D 126     6858   5710   6545    113     17    140       O  
ATOM  11450  CB  PHE D 126      18.008 -16.377   9.313  1.00 47.86           C  
ANISOU11450  CB  PHE D 126     6557   5366   6259     77     64    156       C  
ATOM  11451  CG  PHE D 126      17.740 -15.638   8.041  1.00 48.24           C  
ANISOU11451  CG  PHE D 126     6582   5409   6338     69     83    162       C  
ATOM  11452  CD1 PHE D 126      16.468 -15.177   7.745  1.00 50.84           C  
ANISOU11452  CD1 PHE D 126     6914   5734   6666     40     92    153       C  
ATOM  11453  CD2 PHE D 126      18.761 -15.413   7.128  1.00 50.08           C  
ANISOU11453  CD2 PHE D 126     6787   5642   6595     92     92    178       C  
ATOM  11454  CE1 PHE D 126      16.220 -14.492   6.563  1.00 52.82           C  
ANISOU11454  CE1 PHE D 126     7146   5980   6941     38    108    159       C  
ATOM  11455  CE2 PHE D 126      18.521 -14.733   5.944  1.00 51.08           C  
ANISOU11455  CE2 PHE D 126     6895   5764   6747     87    110    186       C  
ATOM  11456  CZ  PHE D 126      17.247 -14.272   5.660  1.00 51.31           C  
ANISOU11456  CZ  PHE D 126     6932   5787   6775     61    118    177       C  
ATOM  11457  N   PRO D 127      17.473 -16.570  12.596  1.00 48.04           N  
ANISOU11457  N   PRO D 127     6600   5422   6231     59     23    123       N  
ATOM  11458  CA  PRO D 127      17.662 -17.475  13.732  1.00 49.63           C  
ANISOU11458  CA  PRO D 127     6836   5629   6392     71      9    126       C  
ATOM  11459  C   PRO D 127      17.986 -18.888  13.254  1.00 53.51           C  
ANISOU11459  C   PRO D 127     7381   6096   6852     93     17    151       C  
ATOM  11460  O   PRO D 127      17.411 -19.344  12.258  1.00 56.47           O  
ANISOU11460  O   PRO D 127     7782   6449   7222     81     35    163       O  
ATOM  11461  CB  PRO D 127      16.304 -17.444  14.442  1.00 48.80           C  
ANISOU11461  CB  PRO D 127     6748   5534   6259     36     12    116       C  
ATOM  11462  CG  PRO D 127      15.333 -16.949  13.422  1.00 47.49           C  
ANISOU11462  CG  PRO D 127     6571   5360   6110      8     31    113       C  
ATOM  11463  CD  PRO D 127      16.105 -16.022  12.536  1.00 47.35           C  
ANISOU11463  CD  PRO D 127     6510   5338   6143     23     32    111       C  
ATOM  11464  N   LYS D 128      18.912 -19.563  13.933  1.00 55.32           N  
ANISOU11464  N   LYS D 128     7628   6329   7060    128      2    158       N  
ATOM  11465  CA  LYS D 128      19.259 -20.948  13.594  1.00 56.62           C  
ANISOU11465  CA  LYS D 128     7852   6468   7192    156      5    180       C  
ATOM  11466  C   LYS D 128      18.095 -21.886  13.929  1.00 55.83           C  
ANISOU11466  C   LYS D 128     7817   6345   7049    125     13    191       C  
ATOM  11467  O   LYS D 128      17.387 -21.670  14.914  1.00 53.77           O  
ANISOU11467  O   LYS D 128     7557   6100   6772     98      9    184       O  
ATOM  11468  CB  LYS D 128      20.535 -21.378  14.318  1.00 58.94           C  
ANISOU11468  CB  LYS D 128     8148   6776   7470    206    -15    183       C  
ATOM  11469  CG  LYS D 128      21.806 -20.695  13.812  1.00 62.76           C  
ANISOU11469  CG  LYS D 128     8570   7282   7992    238    -21    176       C  
ATOM  11470  CD  LYS D 128      22.795 -20.428  14.948  1.00 64.37           C  
ANISOU11470  CD  LYS D 128     8743   7520   8193    268    -47    163       C  
ATOM  11471  CE  LYS D 128      22.358 -19.241  15.809  1.00 63.57           C  
ANISOU11471  CE  LYS D 128     8597   7443   8113    234    -58    138       C  
ATOM  11472  NZ  LYS D 128      23.201 -18.979  17.013  1.00 59.81           N  
ANISOU11472  NZ  LYS D 128     8093   7001   7630    260    -86    120       N  
ATOM  11473  N   GLY D 129      17.881 -22.903  13.095  1.00 56.75           N  
ANISOU11473  N   GLY D 129     7986   6426   7148    127     24    208       N  
ATOM  11474  CA  GLY D 129      16.800 -23.863  13.326  1.00 61.46           C  
ANISOU11474  CA  GLY D 129     8648   6997   7707     92     31    220       C  
ATOM  11475  C   GLY D 129      16.042 -24.349  12.100  1.00 67.51           C  
ANISOU11475  C   GLY D 129     9444   7733   8474     67     48    226       C  
ATOM  11476  O   GLY D 129      16.551 -24.311  10.976  1.00 70.41           O  
ANISOU11476  O   GLY D 129     9801   8090   8861     92     53    226       O  
ATOM  11477  N   HIS D 130      14.810 -24.796  12.335  1.00 71.26           N  
ANISOU11477  N   HIS D 130     9953   8197   8924     16     57    229       N  
ATOM  11478  CA  HIS D 130      13.973 -25.464  11.334  1.00 72.95           C  
ANISOU11478  CA  HIS D 130    10206   8380   9130    -13     70    233       C  
ATOM  11479  C   HIS D 130      13.005 -24.497  10.696  1.00 69.10           C  
ANISOU11479  C   HIS D 130     9668   7919   8667    -51     84    215       C  
ATOM  11480  O   HIS D 130      12.249 -23.820  11.392  1.00 69.14           O  
ANISOU11480  O   HIS D 130     9641   7956   8671    -84     87    205       O  
ATOM  11481  CB  HIS D 130      13.244 -26.628  12.020  1.00 80.42           C  
ANISOU11481  CB  HIS D 130    11224   9299  10032    -49     71    250       C  
ATOM  11482  CG  HIS D 130      12.199 -27.316  11.166  1.00 88.52           C  
ANISOU11482  CG  HIS D 130    12290  10296  11048    -95     82    251       C  
ATOM  11483  ND1 HIS D 130      12.473 -28.407  10.425  1.00 92.97           N  
ANISOU11483  ND1 HIS D 130    12917  10808  11598    -79     79    261       N  
ATOM  11484  CD2 HIS D 130      10.837 -27.054  10.992  1.00 91.15           C  
ANISOU11484  CD2 HIS D 130    12606  10648  11379   -158     96    241       C  
ATOM  11485  CE1 HIS D 130      11.352 -28.813   9.792  1.00 94.11           C  
ANISOU11485  CE1 HIS D 130    13083  10937  11736   -132     89    256       C  
ATOM  11486  NE2 HIS D 130      10.353 -27.982  10.139  1.00 94.23           N  
ANISOU11486  NE2 HIS D 130    13047  10998  11758   -181    100    244       N  
ATOM  11487  N   TYR D 131      13.031 -24.419   9.365  1.00 65.17           N  
ANISOU11487  N   TYR D 131     9162   7409   8189    -41     92    211       N  
ATOM  11488  CA  TYR D 131      12.118 -23.558   8.603  1.00 63.81           C  
ANISOU11488  CA  TYR D 131     8947   7259   8038    -70    105    195       C  
ATOM  11489  C   TYR D 131      11.196 -24.370   7.705  1.00 64.21           C  
ANISOU11489  C   TYR D 131     9038   7286   8071   -101    114    194       C  
ATOM  11490  O   TYR D 131      11.655 -25.201   6.917  1.00 65.26           O  
ANISOU11490  O   TYR D 131     9213   7384   8197    -77    112    202       O  
ATOM  11491  CB  TYR D 131      12.884 -22.574   7.711  1.00 61.79           C  
ANISOU11491  CB  TYR D 131     8638   7016   7821    -32    108    190       C  
ATOM  11492  CG  TYR D 131      13.682 -21.523   8.431  1.00 61.45           C  
ANISOU11492  CG  TYR D 131     8542   7000   7805    -10     99    185       C  
ATOM  11493  CD1 TYR D 131      14.887 -21.845   9.053  1.00 61.99           C  
ANISOU11493  CD1 TYR D 131     8618   7063   7869     27     86    194       C  
ATOM  11494  CD2 TYR D 131      13.253 -20.198   8.464  1.00 60.43           C  
ANISOU11494  CD2 TYR D 131     8355   6900   7703    -25    103    169       C  
ATOM  11495  CE1 TYR D 131      15.631 -20.885   9.712  1.00 59.62           C  
ANISOU11495  CE1 TYR D 131     8267   6789   7594     44     76    186       C  
ATOM  11496  CE2 TYR D 131      13.999 -19.227   9.113  1.00 59.68           C  
ANISOU11496  CE2 TYR D 131     8215   6825   7634     -8     92    162       C  
ATOM  11497  CZ  TYR D 131      15.185 -19.583   9.736  1.00 59.56           C  
ANISOU11497  CZ  TYR D 131     8206   6807   7616     24     79    170       C  
ATOM  11498  OH  TYR D 131      15.940 -18.647  10.388  1.00 60.33           O  
ANISOU11498  OH  TYR D 131     8257   6925   7740     38     66    160       O  
ATOM  11499  N   ARG D 132       9.900 -24.105   7.817  1.00 63.41           N  
ANISOU11499  N   ARG D 132     8923   7208   7962   -153    122    183       N  
ATOM  11500  CA  ARG D 132       8.901 -24.667   6.920  1.00 65.06           C  
ANISOU11500  CA  ARG D 132     9156   7405   8158   -188    130    176       C  
ATOM  11501  C   ARG D 132       8.399 -23.538   6.025  1.00 62.51           C  
ANISOU11501  C   ARG D 132     8773   7116   7860   -187    139    158       C  
ATOM  11502  O   ARG D 132       7.913 -22.512   6.513  1.00 61.29           O  
ANISOU11502  O   ARG D 132     8569   7001   7715   -200    142    146       O  
ATOM  11503  CB  ARG D 132       7.732 -25.259   7.729  1.00 69.81           C  
ANISOU11503  CB  ARG D 132     9784   8014   8727   -252    133    177       C  
ATOM  11504  CG  ARG D 132       6.803 -26.215   6.983  1.00 72.55           C  
ANISOU11504  CG  ARG D 132    10172   8338   9053   -296    137    173       C  
ATOM  11505  CD  ARG D 132       7.103 -27.672   7.326  1.00 80.51           C  
ANISOU11505  CD  ARG D 132    11264   9289  10033   -306    129    194       C  
ATOM  11506  NE  ARG D 132       6.018 -28.590   6.958  1.00 87.07           N  
ANISOU11506  NE  ARG D 132    12137  10102  10842   -368    133    190       N  
ATOM  11507  CZ  ARG D 132       6.071 -29.919   7.079  1.00 91.63           C  
ANISOU11507  CZ  ARG D 132    12796  10623  11396   -388    126    205       C  
ATOM  11508  NH1 ARG D 132       7.162 -30.508   7.560  1.00 88.40           N  
ANISOU11508  NH1 ARG D 132    12436  10171  10979   -344    115    226       N  
ATOM  11509  NH2 ARG D 132       5.028 -30.668   6.717  1.00 88.28           N  
ANISOU11509  NH2 ARG D 132    12403  10182  10954   -451    128    199       N  
ATOM  11510  N   CYS D 133       8.536 -23.707   4.716  1.00 58.90           N  
ANISOU11510  N   CYS D 133     8324   6643   7412   -166    142    155       N  
ATOM  11511  CA  CYS D 133       7.854 -22.812   3.795  1.00 55.07           C  
ANISOU11511  CA  CYS D 133     7792   6188   6942   -169    152    138       C  
ATOM  11512  C   CYS D 133       6.951 -23.592   2.872  1.00 51.87           C  
ANISOU11512  C   CYS D 133     7418   5773   6517   -197    154    128       C  
ATOM  11513  O   CYS D 133       7.420 -24.401   2.068  1.00 51.95           O  
ANISOU11513  O   CYS D 133     7469   5748   6521   -175    151    132       O  
ATOM  11514  CB  CYS D 133       8.821 -21.967   2.966  1.00 56.97           C  
ANISOU11514  CB  CYS D 133     7998   6432   7216   -115    155    143       C  
ATOM  11515  SG  CYS D 133       7.945 -20.877   1.804  1.00 61.66           S  
ANISOU11515  SG  CYS D 133     8543   7060   7825   -116    167    126       S  
ATOM  11516  N   VAL D 134       5.654 -23.356   3.002  1.00 49.19           N  
ANISOU11516  N   VAL D 134     7057   5466   6164   -245    159    111       N  
ATOM  11517  CA  VAL D 134       4.711 -23.821   1.994  1.00 51.00           C  
ANISOU11517  CA  VAL D 134     7299   5699   6380   -270    161     95       C  
ATOM  11518  C   VAL D 134       4.422 -22.665   1.029  1.00 49.24           C  
ANISOU11518  C   VAL D 134     7020   5512   6175   -243    168     81       C  
ATOM  11519  O   VAL D 134       4.001 -21.580   1.441  1.00 50.65           O  
ANISOU11519  O   VAL D 134     7149   5732   6364   -246    173     73       O  
ATOM  11520  CB  VAL D 134       3.443 -24.530   2.586  1.00 51.82           C  
ANISOU11520  CB  VAL D 134     7421   5816   6453   -343    161     86       C  
ATOM  11521  CG1 VAL D 134       3.248 -24.230   4.070  1.00 50.86           C  
ANISOU11521  CG1 VAL D 134     7282   5718   6323   -370    163     94       C  
ATOM  11522  CG2 VAL D 134       2.186 -24.216   1.779  1.00 51.19           C  
ANISOU11522  CG2 VAL D 134     7308   5777   6364   -371    166     60       C  
ATOM  11523  N   ALA D 135       4.706 -22.909  -0.247  1.00 47.69           N  
ANISOU11523  N   ALA D 135     6837   5299   5981   -213    169     79       N  
ATOM  11524  CA  ALA D 135       4.600 -21.912  -1.304  1.00 46.25           C  
ANISOU11524  CA  ALA D 135     6612   5145   5815   -178    176     71       C  
ATOM  11525  C   ALA D 135       3.541 -22.314  -2.328  1.00 47.47           C  
ANISOU11525  C   ALA D 135     6773   5315   5948   -198    176     48       C  
ATOM  11526  O   ALA D 135       3.760 -23.227  -3.129  1.00 45.86           O  
ANISOU11526  O   ALA D 135     6609   5081   5732   -188    171     46       O  
ATOM  11527  CB  ALA D 135       5.950 -21.740  -1.983  1.00 44.75           C  
ANISOU11527  CB  ALA D 135     6426   4930   5645   -117    179     89       C  
ATOM  11528  N   GLU D 136       2.392 -21.642  -2.284  1.00 49.18           N  
ANISOU11528  N   GLU D 136     6948   5580   6158   -223    179     29       N  
ATOM  11529  CA  GLU D 136       1.326 -21.853  -3.259  1.00 52.47           C  
ANISOU11529  CA  GLU D 136     7357   6022   6553   -239    177      4       C  
ATOM  11530  C   GLU D 136       1.476 -20.894  -4.426  1.00 52.29           C  
ANISOU11530  C   GLU D 136     7302   6021   6543   -184    183      2       C  
ATOM  11531  O   GLU D 136       1.638 -19.692  -4.230  1.00 54.38           O  
ANISOU11531  O   GLU D 136     7527   6307   6828   -157    190      9       O  
ATOM  11532  CB  GLU D 136      -0.048 -21.639  -2.629  1.00 57.44           C  
ANISOU11532  CB  GLU D 136     7955   6703   7164   -293    177    -17       C  
ATOM  11533  CG  GLU D 136      -0.461 -22.697  -1.622  1.00 65.28           C  
ANISOU11533  CG  GLU D 136     8981   7682   8137   -359    172    -16       C  
ATOM  11534  CD  GLU D 136      -1.932 -22.612  -1.244  1.00 70.43           C  
ANISOU11534  CD  GLU D 136     9598   8394   8765   -416    174    -40       C  
ATOM  11535  OE1 GLU D 136      -2.593 -21.607  -1.597  1.00 70.45           O  
ANISOU11535  OE1 GLU D 136     9548   8451   8767   -398    177    -57       O  
ATOM  11536  OE2 GLU D 136      -2.429 -23.556  -0.586  1.00 73.84           O  
ANISOU11536  OE2 GLU D 136    10058   8820   9177   -479    172    -40       O  
ATOM  11537  N   ALA D 137       1.416 -21.433  -5.638  1.00 51.86           N  
ANISOU11537  N   ALA D 137     7268   5959   6476   -166    181     -7       N  
ATOM  11538  CA  ALA D 137       1.432 -20.624  -6.846  1.00 48.80           C  
ANISOU11538  CA  ALA D 137     6853   5594   6092   -114    187     -9       C  
ATOM  11539  C   ALA D 137       0.004 -20.428  -7.325  1.00 48.10           C  
ANISOU11539  C   ALA D 137     6737   5558   5980   -137    183    -41       C  
ATOM  11540  O   ALA D 137      -0.696 -21.395  -7.601  1.00 48.26           O  
ANISOU11540  O   ALA D 137     6779   5580   5976   -174    173    -64       O  
ATOM  11541  CB  ALA D 137       2.260 -21.308  -7.915  1.00 49.16           C  
ANISOU11541  CB  ALA D 137     6936   5608   6135    -73    186     -1       C  
ATOM  11542  N   ILE D 138      -0.427 -19.175  -7.419  1.00 49.14           N  
ANISOU11542  N   ILE D 138     6820   5731   6118   -114    190    -44       N  
ATOM  11543  CA  ILE D 138      -1.797 -18.855  -7.825  1.00 49.46           C  
ANISOU11543  CA  ILE D 138     6827   5830   6134   -128    185    -76       C  
ATOM  11544  C   ILE D 138      -1.841 -18.209  -9.212  1.00 51.27           C  
ANISOU11544  C   ILE D 138     7041   6080   6358    -68    189    -78       C  
ATOM  11545  O   ILE D 138      -0.948 -17.441  -9.576  1.00 52.96           O  
ANISOU11545  O   ILE D 138     7251   6277   6594    -16    200    -51       O  
ATOM  11546  CB  ILE D 138      -2.473 -17.917  -6.801  1.00 48.13           C  
ANISOU11546  CB  ILE D 138     6615   5701   5968   -145    187    -82       C  
ATOM  11547  CG1 ILE D 138      -2.154 -18.350  -5.362  1.00 49.05           C  
ANISOU11547  CG1 ILE D 138     6747   5794   6093   -190    186    -71       C  
ATOM  11548  CG2 ILE D 138      -3.977 -17.801  -7.046  1.00 47.22           C  
ANISOU11548  CG2 ILE D 138     6465   5653   5821   -169    181   -119       C  
ATOM  11549  CD1 ILE D 138      -2.756 -19.677  -4.939  1.00 50.93           C  
ANISOU11549  CD1 ILE D 138     7012   6029   6307   -258    179    -85       C  
ATOM  11550  N   ALA D 139      -2.866 -18.556  -9.990  1.00 53.36           N  
ANISOU11550  N   ALA D 139     7297   6384   6592    -78    181   -110       N  
ATOM  11551  CA  ALA D 139      -3.210 -17.817 -11.202  1.00 55.62           C  
ANISOU11551  CA  ALA D 139     7560   6706   6866    -23    183   -117       C  
ATOM  11552  C   ALA D 139      -4.224 -16.749 -10.824  1.00 58.76           C  
ANISOU11552  C   ALA D 139     7908   7162   7255    -22    183   -133       C  
ATOM  11553  O   ALA D 139      -5.424 -17.024 -10.730  1.00 60.06           O  
ANISOU11553  O   ALA D 139     8050   7376   7392    -58    173   -168       O  
ATOM  11554  CB  ALA D 139      -3.783 -18.746 -12.259  1.00 57.28           C  
ANISOU11554  CB  ALA D 139     7786   6933   7044    -29    171   -147       C  
ATOM  11555  N   GLY D 140      -3.727 -15.532 -10.607  1.00 60.49           N  
ANISOU11555  N   GLY D 140     8110   7374   7498     19    193   -109       N  
ATOM  11556  CA  GLY D 140      -4.525 -14.405 -10.109  1.00 60.31           C  
ANISOU11556  CA  GLY D 140     8045   7396   7471     29    192   -121       C  
ATOM  11557  C   GLY D 140      -5.793 -14.053 -10.869  1.00 61.13           C  
ANISOU11557  C   GLY D 140     8117   7569   7540     48    185   -154       C  
ATOM  11558  O   GLY D 140      -6.669 -13.372 -10.333  1.00 60.63           O  
ANISOU11558  O   GLY D 140     8018   7553   7464     46    180   -173       O  
ATOM  11559  N   ASP D 141      -5.890 -14.503 -12.117  1.00 61.61           N  
ANISOU11559  N   ASP D 141     8189   7638   7580     72    182   -162       N  
ATOM  11560  CA  ASP D 141      -7.106 -14.323 -12.907  1.00 65.61           C  
ANISOU11560  CA  ASP D 141     8666   8215   8048     90    172   -198       C  
ATOM  11561  C   ASP D 141      -8.207 -15.292 -12.460  1.00 68.86           C  
ANISOU11561  C   ASP D 141     9061   8669   8432     19    158   -240       C  
ATOM  11562  O   ASP D 141      -9.304 -14.860 -12.089  1.00 70.88           O  
ANISOU11562  O   ASP D 141     9274   8990   8666      7    152   -268       O  
ATOM  11563  CB  ASP D 141      -6.824 -14.442 -14.415  1.00 66.61           C  
ANISOU11563  CB  ASP D 141     8809   8338   8159    143    173   -194       C  
ATOM  11564  CG  ASP D 141      -5.910 -15.614 -14.762  1.00 69.54           C  
ANISOU11564  CG  ASP D 141     9226   8655   8540    126    174   -182       C  
ATOM  11565  OD1 ASP D 141      -4.852 -15.773 -14.111  1.00 73.52           O  
ANISOU11565  OD1 ASP D 141     9755   9101   9077    114    183   -150       O  
ATOM  11566  OD2 ASP D 141      -6.241 -16.372 -15.698  1.00 68.62           O  
ANISOU11566  OD2 ASP D 141     9119   8555   8396    129    164   -206       O  
ATOM  11567  N   THR D 142      -7.897 -16.589 -12.474  1.00 68.31           N  
ANISOU11567  N   THR D 142     9026   8565   8363    -29    153   -243       N  
ATOM  11568  CA  THR D 142      -8.841 -17.631 -12.065  1.00 67.96           C  
ANISOU11568  CA  THR D 142     8974   8550   8295   -106    140   -278       C  
ATOM  11569  C   THR D 142      -8.887 -17.783 -10.544  1.00 68.23           C  
ANISOU11569  C   THR D 142     9004   8575   8343   -167    145   -269       C  
ATOM  11570  O   THR D 142      -9.881 -18.257  -9.988  1.00 66.66           O  
ANISOU11570  O   THR D 142     8782   8422   8124   -229    139   -296       O  
ATOM  11571  CB  THR D 142      -8.498 -18.998 -12.696  1.00 67.62           C  
ANISOU11571  CB  THR D 142     8979   8466   8248   -134    131   -286       C  
ATOM  11572  OG1 THR D 142      -7.259 -19.484 -12.162  1.00 68.38           O  
ANISOU11572  OG1 THR D 142     9123   8482   8374   -143    139   -250       O  
ATOM  11573  CG2 THR D 142      -8.396 -18.888 -14.213  1.00 66.04           C  
ANISOU11573  CG2 THR D 142     8784   8275   8030    -70    126   -295       C  
ATOM  11574  N   GLU D 143      -7.804 -17.371  -9.886  1.00 69.28           N  
ANISOU11574  N   GLU D 143     9158   8654   8511   -148    157   -232       N  
ATOM  11575  CA  GLU D 143      -7.625 -17.529  -8.440  1.00 68.87           C  
ANISOU11575  CA  GLU D 143     9109   8585   8474   -197    161   -219       C  
ATOM  11576  C   GLU D 143      -7.574 -18.995  -8.037  1.00 68.00           C  
ANISOU11576  C   GLU D 143     9036   8440   8358   -269    156   -221       C  
ATOM  11577  O   GLU D 143      -8.087 -19.375  -6.987  1.00 70.64           O  
ANISOU11577  O   GLU D 143     9362   8792   8684   -331    156   -227       O  
ATOM  11578  CB  GLU D 143      -8.707 -16.773  -7.652  1.00 72.00           C  
ANISOU11578  CB  GLU D 143     9451   9053   8852   -211    161   -240       C  
ATOM  11579  CG  GLU D 143      -8.518 -15.260  -7.630  1.00 75.72           C  
ANISOU11579  CG  GLU D 143     9896   9537   9337   -141    166   -229       C  
ATOM  11580  CD  GLU D 143      -7.311 -14.814  -6.814  1.00 75.31           C  
ANISOU11580  CD  GLU D 143     9866   9422   9323   -126    175   -192       C  
ATOM  11581  OE1 GLU D 143      -7.161 -15.280  -5.664  1.00 76.85           O  
ANISOU11581  OE1 GLU D 143    10070   9602   9524   -175    176   -186       O  
ATOM  11582  OE2 GLU D 143      -6.517 -13.987  -7.315  1.00 73.18           O  
ANISOU11582  OE2 GLU D 143     9607   9120   9078    -67    180   -169       O  
ATOM  11583  N   GLU D 144      -6.944 -19.812  -8.880  1.00 67.46           N  
ANISOU11583  N   GLU D 144     9013   8323   8293   -260    152   -216       N  
ATOM  11584  CA  GLU D 144      -6.823 -21.244  -8.629  1.00 66.46           C  
ANISOU11584  CA  GLU D 144     8934   8153   8162   -322    144   -218       C  
ATOM  11585  C   GLU D 144      -5.377 -21.705  -8.469  1.00 62.51           C  
ANISOU11585  C   GLU D 144     8491   7571   7689   -301    148   -183       C  
ATOM  11586  O   GLU D 144      -4.481 -21.210  -9.153  1.00 60.21           O  
ANISOU11586  O   GLU D 144     8208   7256   7414   -234    154   -164       O  
ATOM  11587  CB  GLU D 144      -7.547 -22.039  -9.716  1.00 70.48           C  
ANISOU11587  CB  GLU D 144     9451   8681   8644   -340    129   -253       C  
ATOM  11588  CG  GLU D 144      -8.998 -22.330  -9.354  1.00 78.96           C  
ANISOU11588  CG  GLU D 144    10487   9823   9691   -411    121   -289       C  
ATOM  11589  CD  GLU D 144      -9.738 -23.108 -10.425  1.00 85.58           C  
ANISOU11589  CD  GLU D 144    11329  10682  10502   -434    104   -328       C  
ATOM  11590  OE1 GLU D 144      -9.782 -24.356 -10.328  1.00 90.09           O  
ANISOU11590  OE1 GLU D 144    11944  11214  11069   -496     93   -336       O  
ATOM  11591  OE2 GLU D 144     -10.271 -22.475 -11.365  1.00 83.19           O  
ANISOU11591  OE2 GLU D 144    10989  10435  10182   -388     99   -352       O  
ATOM  11592  N   LYS D 145      -5.160 -22.645  -7.549  0.50 59.56           N  
ANISOU11592  N   LYS D 145     8154   7156   7318   -357    146   -172       N  
ATOM  11593  CA  LYS D 145      -3.825 -23.158  -7.268  0.50 56.68           C  
ANISOU11593  CA  LYS D 145     7843   6716   6974   -339    148   -140       C  
ATOM  11594  C   LYS D 145      -3.228 -23.755  -8.527  0.50 53.96           C  
ANISOU11594  C   LYS D 145     7539   6335   6627   -298    141   -144       C  
ATOM  11595  O   LYS D 145      -3.844 -24.603  -9.171  0.50 52.81           O  
ANISOU11595  O   LYS D 145     7413   6190   6460   -327    127   -172       O  
ATOM  11596  CB  LYS D 145      -3.861 -24.231  -6.182  0.50 58.50           C  
ANISOU11596  CB  LYS D 145     8114   6911   7200   -409    144   -133       C  
ATOM  11597  CG  LYS D 145      -5.107 -24.229  -5.315  0.50 62.09           C  
ANISOU11597  CG  LYS D 145     8534   7419   7637   -480    146   -149       C  
ATOM  11598  CD  LYS D 145      -4.976 -23.311  -4.113  1.00 62.75           C  
ANISOU11598  CD  LYS D 145     8582   7527   7732   -475    158   -130       C  
ATOM  11599  CE  LYS D 145      -6.193 -23.448  -3.210  0.50 62.20           C  
ANISOU11599  CE  LYS D 145     8481   7513   7639   -548    160   -145       C  
ATOM  11600  NZ  LYS D 145      -6.278 -22.343  -2.216  1.00 62.37           N  
ANISOU11600  NZ  LYS D 145     8455   7575   7665   -532    170   -136       N  
ATOM  11601  N   LEU D 146      -2.036 -23.287  -8.876  1.00 52.39           N  
ANISOU11601  N   LEU D 146     7348   6106   6448   -230    149   -117       N  
ATOM  11602  CA  LEU D 146      -1.266 -23.830  -9.990  1.00 55.24           C  
ANISOU11602  CA  LEU D 146     7748   6432   6806   -182    144   -115       C  
ATOM  11603  C   LEU D 146      -0.428 -25.021  -9.546  1.00 56.64           C  
ANISOU11603  C   LEU D 146     7992   6541   6988   -197    137   -102       C  
ATOM  11604  O   LEU D 146      -0.447 -26.080 -10.182  1.00 55.47           O  
ANISOU11604  O   LEU D 146     7890   6361   6822   -203    122   -119       O  
ATOM  11605  CB  LEU D 146      -0.363 -22.756 -10.595  1.00 55.79           C  
ANISOU11605  CB  LEU D 146     7793   6508   6894   -103    159    -90       C  
ATOM  11606  CG  LEU D 146      -1.073 -21.839 -11.588  1.00 58.69           C  
ANISOU11606  CG  LEU D 146     8115   6932   7250    -69    163   -106       C  
ATOM  11607  CD1 LEU D 146      -0.377 -20.491 -11.662  1.00 60.11           C  
ANISOU11607  CD1 LEU D 146     8261   7122   7454    -12    181    -75       C  
ATOM  11608  CD2 LEU D 146      -1.157 -22.487 -12.960  1.00 57.08           C  
ANISOU11608  CD2 LEU D 146     7936   6729   7021    -39    153   -127       C  
ATOM  11609  N   PHE D 147       0.326 -24.823  -8.468  1.00 56.09           N  
ANISOU11609  N   PHE D 147     7926   6445   6938   -199    145    -72       N  
ATOM  11610  CA  PHE D 147       1.005 -25.908  -7.778  1.00 56.10           C  
ANISOU11610  CA  PHE D 147     7987   6385   6940   -219    137    -58       C  
ATOM  11611  C   PHE D 147       1.227 -25.535  -6.324  1.00 56.92           C  
ANISOU11611  C   PHE D 147     8078   6488   7060   -245    145    -35       C  
ATOM  11612  O   PHE D 147       0.856 -24.437  -5.913  1.00 57.89           O  
ANISOU11612  O   PHE D 147     8146   6656   7193   -246    155    -33       O  
ATOM  11613  CB  PHE D 147       2.311 -26.305  -8.472  1.00 53.53           C  
ANISOU11613  CB  PHE D 147     7701   6017   6620   -152    136    -42       C  
ATOM  11614  CG  PHE D 147       3.271 -25.174  -8.704  1.00 52.38           C  
ANISOU11614  CG  PHE D 147     7515   5889   6497    -85    152    -16       C  
ATOM  11615  CD1 PHE D 147       3.288 -24.501  -9.922  1.00 54.67           C  
ANISOU11615  CD1 PHE D 147     7775   6210   6785    -34    160    -21       C  
ATOM  11616  CD2 PHE D 147       4.201 -24.820  -7.736  1.00 53.01           C  
ANISOU11616  CD2 PHE D 147     7589   5951   6599    -73    160     12       C  
ATOM  11617  CE1 PHE D 147       4.195 -23.480 -10.162  1.00 52.95           C  
ANISOU11617  CE1 PHE D 147     7523   6005   6589     21    176      6       C  
ATOM  11618  CE2 PHE D 147       5.115 -23.802  -7.966  1.00 52.51           C  
ANISOU11618  CE2 PHE D 147     7489   5903   6559    -18    174     36       C  
ATOM  11619  CZ  PHE D 147       5.111 -23.130  -9.180  1.00 54.19           C  
ANISOU11619  CZ  PHE D 147     7673   6145   6772     26    183     34       C  
ATOM  11620  N   CYS D 148       1.814 -26.451  -5.555  1.00 58.99           N  
ANISOU11620  N   CYS D 148     8394   6698   7321   -263    139    -19       N  
ATOM  11621  CA  CYS D 148       2.070 -26.232  -4.131  1.00 59.71           C  
ANISOU11621  CA  CYS D 148     8478   6785   7421   -286    144      2       C  
ATOM  11622  C   CYS D 148       3.303 -27.000  -3.656  1.00 56.87           C  
ANISOU11622  C   CYS D 148     8175   6365   7066   -261    139     26       C  
ATOM  11623  O   CYS D 148       3.372 -28.213  -3.803  1.00 58.60           O  
ANISOU11623  O   CYS D 148     8459   6537   7269   -277    127     23       O  
ATOM  11624  CB  CYS D 148       0.843 -26.635  -3.309  1.00 64.79           C  
ANISOU11624  CB  CYS D 148     9122   7448   8047   -369    142    -10       C  
ATOM  11625  SG  CYS D 148       0.922 -26.153  -1.568  1.00 77.41           S  
ANISOU11625  SG  CYS D 148    10698   9061   9652   -397    151     12       S  
ATOM  11626  N   LEU D 149       4.265 -26.294  -3.070  1.00 55.55           N  
ANISOU11626  N   LEU D 149     7985   6200   6920   -222    146     49       N  
ATOM  11627  CA  LEU D 149       5.514 -26.916  -2.626  1.00 53.62           C  
ANISOU11627  CA  LEU D 149     7785   5907   6678   -188    141     72       C  
ATOM  11628  C   LEU D 149       5.704 -26.813  -1.130  1.00 52.71           C  
ANISOU11628  C   LEU D 149     7669   5791   6567   -213    142     90       C  
ATOM  11629  O   LEU D 149       5.325 -25.816  -0.527  1.00 54.63           O  
ANISOU11629  O   LEU D 149     7858   6076   6821   -228    150     89       O  
ATOM  11630  CB  LEU D 149       6.713 -26.293  -3.348  1.00 53.71           C  
ANISOU11630  CB  LEU D 149     7773   5922   6709   -111    147     84       C  
ATOM  11631  CG  LEU D 149       6.761 -26.554  -4.855  1.00 53.81           C  
ANISOU11631  CG  LEU D 149     7798   5933   6713    -73    146     71       C  
ATOM  11632  CD1 LEU D 149       8.084 -26.098  -5.441  1.00 52.53           C  
ANISOU11632  CD1 LEU D 149     7618   5772   6566      1    153     89       C  
ATOM  11633  CD2 LEU D 149       6.529 -28.029  -5.143  1.00 54.15           C  
ANISOU11633  CD2 LEU D 149     7917   5928   6730    -92    129     57       C  
ATOM  11634  N   ASN D 150       6.294 -27.845  -0.533  1.00 54.47           N  
ANISOU11634  N   ASN D 150     7954   5965   6777   -213    132    104       N  
ATOM  11635  CA  ASN D 150       6.528 -27.871   0.913  1.00 54.63           C  
ANISOU11635  CA  ASN D 150     7980   5981   6795   -233    132    123       C  
ATOM  11636  C   ASN D 150       8.028 -27.889   1.242  1.00 55.26           C  
ANISOU11636  C   ASN D 150     8073   6038   6885   -169    127    143       C  
ATOM  11637  O   ASN D 150       8.617 -28.943   1.502  1.00 57.00           O  
ANISOU11637  O   ASN D 150     8357   6210   7089   -155    116    155       O  
ATOM  11638  CB  ASN D 150       5.765 -29.036   1.571  1.00 53.31           C  
ANISOU11638  CB  ASN D 150     7873   5782   6599   -299    125    125       C  
ATOM  11639  CG  ASN D 150       5.738 -28.946   3.093  1.00 55.77           C  
ANISOU11639  CG  ASN D 150     8182   6102   6903   -328    128    143       C  
ATOM  11640  OD1 ASN D 150       6.355 -28.063   3.686  1.00 56.54           O  
ANISOU11640  OD1 ASN D 150     8237   6227   7018   -295    132    151       O  
ATOM  11641  ND2 ASN D 150       5.016 -29.868   3.734  1.00 55.16           N  
ANISOU11641  ND2 ASN D 150     8152   6003   6801   -390    126    149       N  
ATOM  11642  N   PHE D 151       8.633 -26.702   1.224  1.00 53.34           N  
ANISOU11642  N   PHE D 151     7766   5830   6668   -131    135    147       N  
ATOM  11643  CA  PHE D 151      10.062 -26.539   1.478  1.00 51.59           C  
ANISOU11643  CA  PHE D 151     7541   5600   6460    -71    132    164       C  
ATOM  11644  C   PHE D 151      10.443 -26.736   2.948  1.00 53.83           C  
ANISOU11644  C   PHE D 151     7839   5876   6736    -81    125    179       C  
ATOM  11645  O   PHE D 151       9.691 -26.367   3.859  1.00 53.74           O  
ANISOU11645  O   PHE D 151     7808   5887   6721   -127    127    176       O  
ATOM  11646  CB  PHE D 151      10.523 -25.160   1.014  1.00 48.68           C  
ANISOU11646  CB  PHE D 151     7099   5272   6124    -38    142    164       C  
ATOM  11647  CG  PHE D 151      10.737 -25.055  -0.463  1.00 47.69           C  
ANISOU11647  CG  PHE D 151     6965   5149   6005      0    149    159       C  
ATOM  11648  CD1 PHE D 151       9.704 -24.656  -1.304  1.00 49.08           C  
ANISOU11648  CD1 PHE D 151     7120   5346   6180    -23    156    143       C  
ATOM  11649  CD2 PHE D 151      11.976 -25.340  -1.018  1.00 48.82           C  
ANISOU11649  CD2 PHE D 151     7119   5279   6151     60    148    171       C  
ATOM  11650  CE1 PHE D 151       9.895 -24.555  -2.673  1.00 47.37           C  
ANISOU11650  CE1 PHE D 151     6896   5135   5965     14    163    139       C  
ATOM  11651  CE2 PHE D 151      12.178 -25.242  -2.388  1.00 50.08           C  
ANISOU11651  CE2 PHE D 151     7270   5446   6312     97    155    168       C  
ATOM  11652  CZ  PHE D 151      11.135 -24.846  -3.216  1.00 49.60           C  
ANISOU11652  CZ  PHE D 151     7190   5403   6250     74    163    153       C  
ATOM  11653  N   THR D 152      11.620 -27.323   3.156  1.00 53.73           N  
ANISOU11653  N   THR D 152     7859   5836   6717    -33    115    193       N  
ATOM  11654  CA  THR D 152      12.239 -27.440   4.473  1.00 53.49           C  
ANISOU11654  CA  THR D 152     7839   5803   6680    -24    107    208       C  
ATOM  11655  C   THR D 152      13.595 -26.751   4.398  1.00 53.89           C  
ANISOU11655  C   THR D 152     7845   5874   6754     38    105    214       C  
ATOM  11656  O   THR D 152      14.363 -26.985   3.457  1.00 55.16           O  
ANISOU11656  O   THR D 152     8012   6025   6918     87    105    216       O  
ATOM  11657  CB  THR D 152      12.445 -28.918   4.882  1.00 55.30           C  
ANISOU11657  CB  THR D 152     8157   5977   6874    -21     94    220       C  
ATOM  11658  OG1 THR D 152      11.195 -29.614   4.844  1.00 54.85           O  
ANISOU11658  OG1 THR D 152     8144   5898   6798    -85     95    215       O  
ATOM  11659  CG2 THR D 152      13.045 -29.029   6.289  1.00 56.01           C  
ANISOU11659  CG2 THR D 152     8258   6068   6953    -10     85    236       C  
ATOM  11660  N   ILE D 153      13.885 -25.889   5.370  1.00 52.94           N  
ANISOU11660  N   ILE D 153     7678   5785   6650     36    104    216       N  
ATOM  11661  CA  ILE D 153      15.209 -25.270   5.462  1.00 52.95           C  
ANISOU11661  CA  ILE D 153     7637   5808   6673     89    100    221       C  
ATOM  11662  C   ILE D 153      15.737 -25.496   6.865  1.00 51.57           C  
ANISOU11662  C   ILE D 153     7475   5635   6485     97     87    229       C  
ATOM  11663  O   ILE D 153      15.138 -25.044   7.838  1.00 53.90           O  
ANISOU11663  O   ILE D 153     7753   5947   6779     60     85    224       O  
ATOM  11664  CB  ILE D 153      15.214 -23.740   5.163  1.00 52.01           C  
ANISOU11664  CB  ILE D 153     7436   5729   6594     84    111    213       C  
ATOM  11665  CG1 ILE D 153      14.235 -23.346   4.042  1.00 53.13           C  
ANISOU11665  CG1 ILE D 153     7563   5876   6745     59    125    203       C  
ATOM  11666  CG2 ILE D 153      16.626 -23.239   4.883  1.00 47.60           C  
ANISOU11666  CG2 ILE D 153     6836   5189   6059    137    109    220       C  
ATOM  11667  CD1 ILE D 153      14.644 -23.751   2.642  1.00 55.38           C  
ANISOU11667  CD1 ILE D 153     7862   6150   7030     96    132    207       C  
ATOM  11668  N   ILE D 154      16.846 -26.209   6.971  0.50 49.90           N  
ANISOU11668  N   ILE D 154     7292   5407   6258    150     75    239       N  
ATOM  11669  CA  ILE D 154      17.502 -26.362   8.253  0.50 50.38           C  
ANISOU11669  CA  ILE D 154     7360   5476   6306    169     60    246       C  
ATOM  11670  C   ILE D 154      18.758 -25.508   8.213  0.50 52.39           C  
ANISOU11670  C   ILE D 154     7548   5768   6589    215     56    243       C  
ATOM  11671  O   ILE D 154      19.634 -25.710   7.368  0.50 50.05           O  
ANISOU11671  O   ILE D 154     7246   5471   6297    262     57    247       O  
ATOM  11672  CB  ILE D 154      17.751 -27.846   8.595  0.50 49.46           C  
ANISOU11672  CB  ILE D 154     7331   5314   6146    192     48    260       C  
ATOM  11673  CG1 ILE D 154      16.440 -28.478   9.081  1.00 48.54           C  
ANISOU11673  CG1 ILE D 154     7270   5168   6004    129     51    265       C  
ATOM  11674  CG2 ILE D 154      18.844 -28.001   9.646  1.00 48.06           C  
ANISOU11674  CG2 ILE D 154     7155   5149   5955    239     31    268       C  
ATOM  11675  CD1 ILE D 154      16.330 -29.971   8.839  0.50 49.79           C  
ANISOU11675  CD1 ILE D 154     7525   5266   6127    136     44    277       C  
ATOM  11676  N   HIS D 155      18.805 -24.529   9.116  1.00 56.30           N  
ANISOU11676  N   HIS D 155     7991   6296   7103    198     52    235       N  
ATOM  11677  CA  HIS D 155      19.827 -23.488   9.100  1.00 60.96           C  
ANISOU11677  CA  HIS D 155     8508   6924   7727    224     48    229       C  
ATOM  11678  C   HIS D 155      20.834 -23.633  10.203  1.00 67.61           C  
ANISOU11678  C   HIS D 155     9344   7785   8558    260     28    229       C  
ATOM  11679  O   HIS D 155      20.495 -23.546  11.390  1.00 69.63           O  
ANISOU11679  O   HIS D 155     9607   8049   8801    241     18    224       O  
ATOM  11680  CB  HIS D 155      19.181 -22.107   9.160  1.00 58.75           C  
ANISOU11680  CB  HIS D 155     8168   6669   7484    181     56    214       C  
ATOM  11681  CG  HIS D 155      20.176 -20.971   9.131  1.00 58.13           C  
ANISOU11681  CG  HIS D 155     8016   6624   7446    198     52    208       C  
ATOM  11682  ND1 HIS D 155      20.400 -20.180  10.194  1.00 59.01           N  
ANISOU11682  ND1 HIS D 155     8088   6760   7571    189     38    195       N  
ATOM  11683  CD2 HIS D 155      21.027 -20.526   8.121  1.00 56.53           C  
ANISOU11683  CD2 HIS D 155     7772   6435   7272    224     62    214       C  
ATOM  11684  CE1 HIS D 155      21.336 -19.266   9.877  1.00 59.00           C  
ANISOU11684  CE1 HIS D 155     8025   6783   7609    203     37    191       C  
ATOM  11685  NE2 HIS D 155      21.716 -19.481   8.606  1.00 55.10           N  
ANISOU11685  NE2 HIS D 155     7529   6283   7123    224     53    205       N  
TER   11686      HIS D 155                                                      
HETATM11687  C1  NAG E   1      33.510  25.920  35.406  1.00 46.85           C  
HETATM11688  C2  NAG E   1      33.709  24.424  35.576  1.00 47.71           C  
HETATM11689  C3  NAG E   1      32.500  23.816  34.894  1.00 46.50           C  
HETATM11690  C4  NAG E   1      31.237  24.342  35.569  1.00 48.69           C  
HETATM11691  C5  NAG E   1      31.308  25.837  35.951  1.00 46.93           C  
HETATM11692  C6  NAG E   1      30.381  26.071  37.127  1.00 47.45           C  
HETATM11693  C7  NAG E   1      36.082  23.930  35.774  1.00 51.29           C  
HETATM11694  C8  NAG E   1      37.353  23.560  35.058  1.00 47.15           C  
HETATM11695  N2  NAG E   1      34.992  24.048  35.013  1.00 49.59           N  
HETATM11696  O3  NAG E   1      32.500  22.418  34.984  1.00 49.42           O  
HETATM11697  O4  NAG E   1      30.170  24.131  34.668  1.00 53.74           O  
HETATM11698  O5  NAG E   1      32.607  26.319  36.307  1.00 48.47           O  
HETATM11699  O6  NAG E   1      29.189  26.631  36.643  1.00 49.64           O  
HETATM11700  O7  NAG E   1      36.071  24.101  36.998  1.00 52.53           O  
HETATM11701  C1  NAG E   2      29.237  23.143  35.136  1.00 54.25           C  
HETATM11702  C2  NAG E   2      27.984  23.167  34.266  1.00 53.37           C  
HETATM11703  C3  NAG E   2      26.951  22.229  34.883  1.00 56.98           C  
HETATM11704  C4  NAG E   2      27.530  20.816  34.799  1.00 56.98           C  
HETATM11705  C5  NAG E   2      28.862  20.781  35.562  1.00 58.70           C  
HETATM11706  C6  NAG E   2      29.499  19.395  35.454  1.00 56.96           C  
HETATM11707  C7  NAG E   2      27.515  25.090  32.832  1.00 49.37           C  
HETATM11708  C8  NAG E   2      26.773  26.390  32.701  1.00 50.76           C  
HETATM11709  N2  NAG E   2      27.364  24.456  34.002  1.00 50.07           N  
HETATM11710  O3  NAG E   2      25.698  22.339  34.225  1.00 56.07           O  
HETATM11711  O4  NAG E   2      26.608  19.862  35.290  1.00 58.83           O  
HETATM11712  O5  NAG E   2      29.748  21.810  35.087  1.00 61.22           O  
HETATM11713  O6  NAG E   2      30.885  19.495  35.192  1.00 58.85           O  
HETATM11714  O7  NAG E   2      28.232  24.691  31.903  1.00 41.80           O  
HETATM11715  C1  NAG F   1      -0.776   2.741  31.951  1.00 40.88           C  
HETATM11716  C2  NAG F   1      -0.079   3.692  32.925  1.00 41.27           C  
HETATM11717  C3  NAG F   1      -0.965   4.926  33.162  1.00 40.71           C  
HETATM11718  C4  NAG F   1      -1.253   5.733  31.899  1.00 43.60           C  
HETATM11719  C5  NAG F   1      -1.570   4.807  30.730  1.00 42.83           C  
HETATM11720  C6  NAG F   1      -1.048   5.545  29.505  1.00 44.23           C  
HETATM11721  C7  NAG F   1       1.094   3.464  35.097  1.00 45.96           C  
HETATM11722  C8  NAG F   1       1.144   2.706  36.388  1.00 47.40           C  
HETATM11723  N2  NAG F   1       0.148   3.093  34.231  1.00 46.64           N  
HETATM11724  O3  NAG F   1      -0.355   5.805  34.075  1.00 39.31           O  
HETATM11725  O4  NAG F   1      -2.346   6.638  32.032  1.00 47.69           O  
HETATM11726  O5  NAG F   1      -0.959   3.511  30.753  1.00 42.39           O  
HETATM11727  O6  NAG F   1      -2.083   5.692  28.569  1.00 50.30           O  
HETATM11728  O7  NAG F   1       1.894   4.370  34.885  1.00 49.07           O  
HETATM11729  C1  NAG F   2      -2.049   7.949  32.570  1.00 56.17           C  
HETATM11730  C2  NAG F   2      -2.776   9.055  31.787  1.00 58.16           C  
HETATM11731  C3  NAG F   2      -2.673  10.418  32.469  1.00 58.53           C  
HETATM11732  C4  NAG F   2      -2.946  10.378  33.965  1.00 65.84           C  
HETATM11733  C5  NAG F   2      -2.240   9.208  34.637  1.00 67.48           C  
HETATM11734  C6  NAG F   2      -2.781   9.048  36.053  1.00 71.60           C  
HETATM11735  C7  NAG F   2      -2.989   9.022  29.313  1.00 58.27           C  
HETATM11736  C8  NAG F   2      -2.244   9.235  28.030  1.00 54.30           C  
HETATM11737  N2  NAG F   2      -2.266   9.204  30.430  1.00 61.34           N  
HETATM11738  O3  NAG F   2      -3.662  11.246  31.932  1.00 55.67           O  
HETATM11739  O4  NAG F   2      -2.551  11.605  34.549  1.00 72.01           O  
HETATM11740  O5  NAG F   2      -2.470   8.001  33.923  1.00 65.00           O  
HETATM11741  O6  NAG F   2      -1.824   9.485  36.995  1.00 83.48           O  
HETATM11742  O7  NAG F   2      -4.181   8.695  29.281  1.00 56.51           O  
HETATM11743  C1  NAG G   1     -18.002  -4.111   4.993  1.00 35.15           C  
HETATM11744  C2  NAG G   1     -18.236  -4.856   3.685  1.00 36.94           C  
HETATM11745  C3  NAG G   1     -17.730  -6.291   3.824  1.00 39.92           C  
HETATM11746  C4  NAG G   1     -16.290  -6.410   4.349  1.00 43.64           C  
HETATM11747  C5  NAG G   1     -15.989  -5.416   5.483  1.00 40.08           C  
HETATM11748  C6  NAG G   1     -14.494  -5.193   5.465  1.00 38.84           C  
HETATM11749  C7  NAG G   1     -20.188  -4.746   2.191  1.00 36.19           C  
HETATM11750  C8  NAG G   1     -21.679  -4.873   2.128  1.00 35.00           C  
HETATM11751  N2  NAG G   1     -19.659  -4.921   3.398  1.00 35.26           N  
HETATM11752  O3  NAG G   1     -17.835  -6.938   2.582  1.00 40.40           O  
HETATM11753  O4  NAG G   1     -16.066  -7.722   4.855  1.00 48.52           O  
HETATM11754  O5  NAG G   1     -16.630  -4.145   5.384  1.00 38.41           O  
HETATM11755  O6  NAG G   1     -14.159  -4.017   6.147  1.00 41.28           O  
HETATM11756  O7  NAG G   1     -19.537  -4.493   1.168  1.00 37.54           O  
HETATM11757  C1  NAG G   2     -15.425  -8.594   3.908  1.00 53.86           C  
HETATM11758  C2  NAG G   2     -14.157  -9.140   4.586  1.00 58.70           C  
HETATM11759  C3  NAG G   2     -13.654 -10.505   4.073  1.00 58.78           C  
HETATM11760  C4  NAG G   2     -14.832 -11.422   3.733  1.00 61.19           C  
HETATM11761  C5  NAG G   2     -15.609 -10.607   2.706  1.00 63.95           C  
HETATM11762  C6  NAG G   2     -16.497 -11.408   1.755  1.00 67.89           C  
HETATM11763  C7  NAG G   2     -12.449  -7.635   5.527  1.00 52.45           C  
HETATM11764  C8  NAG G   2     -12.740  -8.216   6.889  1.00 49.72           C  
HETATM11765  N2  NAG G   2     -13.135  -8.108   4.481  1.00 56.34           N  
HETATM11766  O3  NAG G   2     -12.835 -11.087   5.058  1.00 57.62           O  
HETATM11767  O4  NAG G   2     -14.455 -12.700   3.250  1.00 62.93           O  
HETATM11768  O5  NAG G   2     -16.302  -9.613   3.445  1.00 60.06           O  
HETATM11769  O6  NAG G   2     -15.667 -12.004   0.771  1.00 63.45           O  
HETATM11770  O7  NAG G   2     -11.601  -6.750   5.396  1.00 46.74           O  
HETATM11771  C1  NAG A 705      -2.887   3.797  38.969  1.00 66.57           C  
HETATM11772  C2  NAG A 705      -2.828   4.883  37.891  1.00 64.51           C  
HETATM11773  C3  NAG A 705      -1.364   5.217  37.605  1.00 66.64           C  
HETATM11774  C4  NAG A 705      -0.551   5.500  38.868  1.00 71.56           C  
HETATM11775  C5  NAG A 705      -0.802   4.443  39.960  1.00 80.29           C  
HETATM11776  C6  NAG A 705      -0.182   4.854  41.301  1.00 86.39           C  
HETATM11777  C7  NAG A 705      -4.284   5.207  35.894  1.00 57.58           C  
HETATM11778  C8  NAG A 705      -4.849   4.605  34.645  1.00 50.88           C  
HETATM11779  N2  NAG A 705      -3.477   4.446  36.656  1.00 59.48           N  
HETATM11780  O3  NAG A 705      -1.283   6.332  36.757  1.00 67.31           O  
HETATM11781  O4  NAG A 705       0.819   5.526  38.519  1.00 64.48           O  
HETATM11782  O5  NAG A 705      -2.193   4.193  40.143  1.00 73.31           O  
HETATM11783  O6  NAG A 705       1.232   4.770  41.250  1.00 87.93           O  
HETATM11784  O7  NAG A 705      -4.596   6.366  36.146  1.00 61.51           O  
HETATM11785  C1  LP4 C 300       7.087  30.873   6.463  1.00 48.82           C  
HETATM11786  C2  LP4 C 300       7.215  30.959   7.966  1.00 48.60           C  
HETATM11787  N2  LP4 C 300       5.868  31.172   8.525  1.00 52.03           N  
HETATM11788  C3  LP4 C 300       8.172  32.122   8.303  1.00 49.20           C  
HETATM11789  O3  LP4 C 300       8.521  32.128   9.687  1.00 50.97           O  
HETATM11790  C4  LP4 C 300       9.482  31.926   7.543  1.00 48.27           C  
HETATM11791  O4  LP4 C 300      10.406  32.950   7.873  1.00 48.45           O  
HETATM11792  C5  LP4 C 300       9.228  31.825   6.033  1.00 49.61           C  
HETATM11793  O5  LP4 C 300       8.394  30.666   5.841  1.00 50.80           O  
HETATM11794  C6  LP4 C 300      10.532  31.752   5.205  1.00 49.97           C  
HETATM11795  O6  LP4 C 300      11.203  30.488   5.358  1.00 50.85           O  
HETATM11796  C7  LP4 C 300       5.081  30.173   8.984  1.00 55.71           C  
HETATM11797  O7  LP4 C 300       5.404  28.985   8.980  1.00 58.90           O  
HETATM11798  C8  LP4 C 300       3.689  30.594   9.511  1.00 56.15           C  
HETATM11799  C16 LP4 C 300       3.786  31.585  10.683  1.00 57.99           C  
HETATM11800  C17 LP4 C 300       2.408  31.765  11.349  1.00 54.94           C  
HETATM11801  C18 LP4 C 300       2.421  32.964  12.316  1.00 54.29           C  
HETATM11802  C19 LP4 C 300       0.985  33.445  12.606  1.00 53.61           C  
HETATM11803  C20 LP4 C 300       0.972  34.936  12.981  1.00 50.86           C  
HETATM11804  C21 LP4 C 300       0.517  35.118  14.436  1.00 52.65           C  
HETATM11805  C22 LP4 C 300      -0.531  36.247  14.506  1.00 55.06           C  
HETATM11806  C23 LP4 C 300      -0.678  36.808  15.938  1.00 54.30           C  
HETATM11807  C24 LP4 C 300      -1.247  38.238  15.874  1.00 54.29           C  
HETATM11808  C25 LP4 C 300      -2.146  38.538  17.076  1.00 51.80           C  
HETATM11809  C28 LP4 C 300       7.620  32.670  10.539  1.00 53.28           C  
HETATM11810  C29 LP4 C 300       7.884  32.327  12.001  1.00 56.17           C  
HETATM11811  C30 LP4 C 300       8.245  33.599  12.763  1.00 58.53           C  
HETATM11812  C31 LP4 C 300       6.971  34.298  13.222  1.00 55.74           C  
HETATM11813  C32 LP4 C 300       5.951  33.293  13.762  1.00 56.82           C  
HETATM11814  C33 LP4 C 300       5.952  33.306  15.293  1.00 57.81           C  
HETATM11815  C34 LP4 C 300       5.794  34.737  15.812  1.00 56.04           C  
HETATM11816  C35 LP4 C 300       4.407  34.914  16.429  1.00 57.07           C  
HETATM11817  C36 LP4 C 300       4.447  36.052  17.459  1.00 55.66           C  
HETATM11818  C37 LP4 C 300       4.448  35.484  18.884  1.00 51.07           C  
HETATM11819  C38 LP4 C 300       3.678  36.434  19.812  1.00 48.23           C  
HETATM11820  C39 LP4 C 300       3.752  35.916  21.254  1.00 45.47           C  
HETATM11821  C40 LP4 C 300       4.590  36.870  22.121  1.00 43.07           C  
HETATM11822  C41 LP4 C 300       4.584  36.405  23.581  1.00 37.38           C  
HETATM11823  O42 LP4 C 300       6.661  33.362  10.202  1.00 56.26           O  
HETATM11824  O43 LP4 C 300       9.029  33.270  13.913  1.00 63.68           O  
HETATM11825  O44 LP4 C 300       4.731  31.084  11.637  1.00 63.63           O  
HETATM11826  P45 LP4 C 300      11.709  32.462   8.653  1.00 51.71           P  
HETATM11827  O46 LP4 C 300      11.326  32.356  10.079  1.00 50.72           O  
HETATM11828  O47 LP4 C 300      12.797  33.644   8.478  1.00 51.89           O  
HETATM11829  O48 LP4 C 300      12.234  31.267   7.950  1.00 49.73           O  
HETATM11830  O48 LP5 C 301       2.462  24.590   3.220  1.00 52.89           O  
HETATM11831  P45 LP5 C 301       3.869  24.891   3.564  1.00 53.21           P  
HETATM11832  O46 LP5 C 301       4.533  23.838   4.611  1.00 54.33           O  
HETATM11833  O47 LP5 C 301       4.864  24.952   2.283  1.00 54.48           O  
HETATM11834  O1  LP5 C 301       4.020  26.323   4.230  1.00 52.83           O  
HETATM11835  C1  LP5 C 301       4.390  26.513   5.593  1.00 54.90           C  
HETATM11836  C2  LP5 C 301       3.199  27.030   6.385  1.00 56.03           C  
HETATM11837  N2  LP5 C 301       2.214  25.944   6.558  1.00 60.17           N  
HETATM11838  C7  LP5 C 301       1.256  25.897   7.505  1.00 61.86           C  
HETATM11839  C8  LP5 C 301       0.426  24.615   7.470  1.00 65.40           C  
HETATM11840  C16 LP5 C 301      -0.555  24.542   8.637  1.00 66.21           C  
HETATM11841  O44 LP5 C 301      -0.634  23.180   9.080  1.00 67.67           O  
HETATM11842  C17 LP5 C 301      -1.919  25.065   8.151  1.00 68.51           C  
HETATM11843  C18 LP5 C 301      -3.091  24.459   8.940  1.00 69.39           C  
HETATM11844  C19 LP5 C 301      -3.278  25.207  10.263  1.00 68.22           C  
HETATM11845  C20 LP5 C 301      -4.337  26.291  10.099  1.00 67.54           C  
HETATM11846  C21 LP5 C 301      -5.052  26.465  11.432  1.00 67.76           C  
HETATM11847  C22 LP5 C 301      -6.518  26.786  11.163  1.00 67.27           C  
HETATM11848  C23 LP5 C 301      -7.038  27.739  12.244  1.00 74.66           C  
HETATM11849  C24 LP5 C 301      -6.910  29.191  11.765  1.00 77.67           C  
HETATM11850  C25 LP5 C 301      -7.943  30.074  12.467  1.00 79.34           C  
HETATM11851  C26 LP5 C 301      -7.288  31.391  12.885  1.00 79.73           C  
HETATM11852  C27 LP5 C 301      -7.110  31.405  14.407  1.00 82.57           C  
HETATM11853  O7  LP5 C 301       1.012  26.787   8.318  1.00 62.72           O  
HETATM11854  C3  LP5 C 301       2.606  28.229   5.653  1.00 54.19           C  
HETATM11855  C4  LP5 C 301       3.677  29.298   5.417  1.00 52.46           C  
HETATM11856  C5  LP5 C 301       4.928  28.675   4.788  1.00 51.91           C  
HETATM11857  O5  LP5 C 301       5.381  27.532   5.560  1.00 55.53           O  
HETATM11858  C6  LP5 C 301       6.044  29.706   4.754  1.00 51.39           C  
HETATM11859  O6  LP5 C 301       6.856  29.554   5.922  1.00 50.97           O  
HETATM11860  O4  LP5 C 301       3.164  30.289   4.531  1.00 49.46           O  
HETATM11861  O3  LP5 C 301       1.602  28.771   6.468  1.00 53.82           O  
HETATM11862  C28 LP5 C 301       0.487  29.143   5.798  1.00 55.91           C  
HETATM11863  O42 LP5 C 301       0.173  28.794   4.656  1.00 62.04           O  
HETATM11864  C29 LP5 C 301      -0.383  30.080   6.603  1.00 51.33           C  
HETATM11865  C30 LP5 C 301      -1.380  29.237   7.352  1.00 46.12           C  
HETATM11866  O43 LP5 C 301      -2.612  29.359   6.640  1.00 46.48           O  
HETATM11867  C31 LP5 C 301      -1.462  29.761   8.789  1.00 43.65           C  
HETATM11868  C32 LP5 C 301      -2.815  30.399   9.090  1.00 44.71           C  
HETATM11869  C33 LP5 C 301      -2.617  31.867   9.462  1.00 46.44           C  
HETATM11870  C34 LP5 C 301      -3.195  32.076  10.859  1.00 51.12           C  
HETATM11871  C35 LP5 C 301      -2.813  33.464  11.375  1.00 55.76           C  
HETATM11872  C36 LP5 C 301      -4.051  34.129  11.982  1.00 58.80           C  
HETATM11873  C37 LP5 C 301      -3.644  35.441  12.653  1.00 62.01           C  
HETATM11874  C38 LP5 C 301      -4.749  35.903  13.605  1.00 66.23           C  
HETATM11875  C39 LP5 C 301      -4.285  35.726  15.055  1.00 69.99           C  
HETATM11876  C40 LP5 C 301      -5.451  35.238  15.922  1.00 70.54           C  
HETATM11877  C41 LP5 C 301      -4.952  34.120  16.847  1.00 73.28           C  
HETATM11878  C1  NAG B 802     -23.214  -8.687   4.907  1.00 46.18           C  
HETATM11879  C2  NAG B 802     -21.759  -9.046   4.555  1.00 50.12           C  
HETATM11880  C3  NAG B 802     -21.300  -8.517   3.197  1.00 49.06           C  
HETATM11881  C4  NAG B 802     -22.328  -8.783   2.107  1.00 49.81           C  
HETATM11882  C5  NAG B 802     -23.689  -8.280   2.607  1.00 49.43           C  
HETATM11883  C6  NAG B 802     -24.774  -8.406   1.543  1.00 50.47           C  
HETATM11884  C7  NAG B 802     -19.874  -9.276   6.058  1.00 55.75           C  
HETATM11885  C8  NAG B 802     -19.014  -8.632   7.105  1.00 50.55           C  
HETATM11886  N2  NAG B 802     -20.858  -8.529   5.569  1.00 53.14           N  
HETATM11887  O3  NAG B 802     -20.066  -9.093   2.835  1.00 51.70           O  
HETATM11888  O4  NAG B 802     -21.905  -8.162   0.902  1.00 52.32           O  
HETATM11889  O5  NAG B 802     -24.057  -8.985   3.797  1.00 48.98           O  
HETATM11890  O6  NAG B 802     -25.267  -9.725   1.590  1.00 51.76           O  
HETATM11891  O7  NAG B 802     -19.661 -10.434   5.685  1.00 59.56           O  
HETATM11892  C1  LP4 D 300      19.117  -7.246  -4.886  1.00 69.97           C  
HETATM11893  C2  LP4 D 300      17.782  -7.807  -5.356  1.00 68.91           C  
HETATM11894  N2  LP4 D 300      17.409  -8.983  -4.541  1.00 63.02           N  
HETATM11895  C3  LP4 D 300      17.891  -8.197  -6.845  1.00 72.46           C  
HETATM11896  O3  LP4 D 300      16.587  -8.545  -7.341  1.00 73.28           O  
HETATM11897  C4  LP4 D 300      18.511  -7.070  -7.706  1.00 70.51           C  
HETATM11898  O4  LP4 D 300      18.817  -7.591  -9.016  1.00 68.89           O  
HETATM11899  C5  LP4 D 300      19.799  -6.559  -7.038  1.00 71.91           C  
HETATM11900  O5  LP4 D 300      19.494  -6.123  -5.717  1.00 69.13           O  
HETATM11901  C6  LP4 D 300      20.406  -5.376  -7.794  1.00 72.91           C  
HETATM11902  O6  LP4 D 300      19.623  -4.206  -7.553  1.00 75.23           O  
HETATM11903  C7  LP4 D 300      16.335  -8.997  -3.733  1.00 58.51           C  
HETATM11904  O7  LP4 D 300      15.598  -8.030  -3.571  1.00 56.83           O  
HETATM11905  C8  LP4 D 300      16.089 -10.300  -2.950  1.00 58.75           C  
HETATM11906  C16 LP4 D 300      15.546 -11.450  -3.830  1.00 62.44           C  
HETATM11907  C17 LP4 D 300      14.988 -12.573  -2.939  1.00 61.50           C  
HETATM11908  C18 LP4 D 300      15.576 -13.929  -3.364  1.00 62.90           C  
HETATM11909  C19 LP4 D 300      14.453 -14.905  -3.741  1.00 63.01           C  
HETATM11910  C20 LP4 D 300      15.044 -16.285  -4.069  1.00 64.84           C  
HETATM11911  C21 LP4 D 300      13.911 -17.274  -4.381  1.00 63.52           C  
HETATM11912  C22 LP4 D 300      14.438 -18.710  -4.274  1.00 62.47           C  
HETATM11913  C23 LP4 D 300      13.652 -19.635  -5.215  1.00 59.10           C  
HETATM11914  C24 LP4 D 300      13.449 -21.004  -4.559  1.00 60.52           C  
HETATM11915  C25 LP4 D 300      14.427 -22.039  -5.136  1.00 63.60           C  
HETATM11916  C28 LP4 D 300      16.531  -9.851  -7.702  1.00 73.08           C  
HETATM11917  C29 LP4 D 300      15.618 -10.116  -8.894  1.00 73.25           C  
HETATM11918  C30 LP4 D 300      15.426 -11.616  -9.119  1.00 73.97           C  
HETATM11919  C31 LP4 D 300      14.602 -12.225  -7.960  1.00 72.03           C  
HETATM11920  C32 LP4 D 300      13.115 -12.373  -8.304  1.00 73.96           C  
HETATM11921  C33 LP4 D 300      12.806 -13.760  -8.897  1.00 74.62           C  
HETATM11922  C34 LP4 D 300      13.572 -14.876  -8.170  1.00 72.42           C  
HETATM11923  C35 LP4 D 300      12.601 -15.997  -7.782  1.00 70.88           C  
HETATM11924  C36 LP4 D 300      12.590 -17.079  -8.865  1.00 64.96           C  
HETATM11925  C37 LP4 D 300      11.155 -17.294  -9.332  1.00 57.88           C  
HETATM11926  C38 LP4 D 300      10.825 -18.784  -9.279  1.00 54.28           C  
HETATM11927  C39 LP4 D 300       9.361 -18.953  -9.680  1.00 55.85           C  
HETATM11928  C40 LP4 D 300       9.139 -20.311 -10.343  1.00 55.49           C  
HETATM11929  C41 LP4 D 300       8.386 -20.127 -11.669  1.00 56.24           C  
HETATM11930  O42 LP4 D 300      17.134 -10.762  -7.131  1.00 77.72           O  
HETATM11931  O43 LP4 D 300      14.805 -11.818 -10.394  1.00 73.46           O  
HETATM11932  O44 LP4 D 300      14.509 -11.000  -4.718  1.00 60.43           O  
HETATM11933  P45 LP4 D 300      18.157  -6.946 -10.315  1.00 70.59           P  
HETATM11934  O46 LP4 D 300      16.727  -7.317 -10.319  1.00 71.55           O  
HETATM11935  O47 LP4 D 300      18.897  -7.705 -11.536  1.00 72.49           O  
HETATM11936  O48 LP4 D 300      18.527  -5.517 -10.379  1.00 67.59           O  
HETATM11937  O48 LP5 D 301      17.596  -3.092   2.218  1.00 63.95           O  
HETATM11938  P45 LP5 D 301      18.022  -3.590   0.889  1.00 67.96           P  
HETATM11939  O46 LP5 D 301      17.384  -2.816  -0.382  1.00 67.17           O  
HETATM11940  O47 LP5 D 301      19.638  -3.515   0.647  1.00 63.79           O  
HETATM11941  O1  LP5 D 301      17.626  -5.130   0.729  1.00 67.50           O  
HETATM11942  C1  LP5 D 301      16.742  -5.639  -0.277  1.00 69.67           C  
HETATM11943  C2  LP5 D 301      16.606  -7.129  -0.015  1.00 70.78           C  
HETATM11944  N2  LP5 D 301      16.159  -7.310   1.368  1.00 67.83           N  
HETATM11945  C7  LP5 D 301      14.993  -7.869   1.685  1.00 68.89           C  
HETATM11946  C8  LP5 D 301      14.737  -7.962   3.193  1.00 67.43           C  
HETATM11947  C16 LP5 D 301      13.261  -8.228   3.493  1.00 65.27           C  
HETATM11948  O44 LP5 D 301      12.464  -7.132   3.031  1.00 66.90           O  
HETATM11949  C17 LP5 D 301      13.088  -8.412   5.005  1.00 63.81           C  
HETATM11950  C18 LP5 D 301      12.053  -9.504   5.298  1.00 63.03           C  
HETATM11951  C19 LP5 D 301      12.507 -10.860   4.740  1.00 66.33           C  
HETATM11952  C20 LP5 D 301      12.639 -11.877   5.872  1.00 66.07           C  
HETATM11953  C21 LP5 D 301      11.888 -13.164   5.515  1.00 67.77           C  
HETATM11954  C22 LP5 D 301      12.037 -14.152   6.676  1.00 70.06           C  
HETATM11955  C23 LP5 D 301      11.891 -15.579   6.153  1.00 73.22           C  
HETATM11956  C24 LP5 D 301      13.219 -16.328   6.289  1.00 71.08           C  
HETATM11957  C25 LP5 D 301      13.037 -17.773   5.805  1.00 75.37           C  
HETATM11958  C26 LP5 D 301      13.663 -17.968   4.422  1.00 73.76           C  
HETATM11959  C27 LP5 D 301      12.555 -18.148   3.379  1.00 74.04           C  
HETATM11960  O7  LP5 D 301      14.181  -8.278   0.855  1.00 75.59           O  
HETATM11961  C3  LP5 D 301      17.980  -7.785  -0.124  1.00 75.17           C  
HETATM11962  C4  LP5 D 301      18.695  -7.450  -1.445  1.00 74.14           C  
HETATM11963  C5  LP5 D 301      18.634  -5.922  -1.710  1.00 71.50           C  
HETATM11964  O5  LP5 D 301      17.271  -5.439  -1.606  1.00 70.37           O  
HETATM11965  C6  LP5 D 301      19.170  -5.561  -3.093  1.00 69.29           C  
HETATM11966  O6  LP5 D 301      18.420  -6.247  -4.101  1.00 72.26           O  
HETATM11967  O4  LP5 D 301      20.066  -7.872  -1.364  1.00 70.16           O  
HETATM11968  O3  LP5 D 301      17.842  -9.204   0.055  1.00 81.62           O  
HETATM11969  C28 LP5 D 301      18.383  -9.566   1.260  1.00 85.53           C  
HETATM11970  O42 LP5 D 301      19.026  -8.810   1.993  1.00 89.10           O  
HETATM11971  C29 LP5 D 301      18.179 -11.034   1.646  1.00 77.99           C  
HETATM11972  C30 LP5 D 301      16.713 -11.315   1.942  1.00 72.29           C  
HETATM11973  O43 LP5 D 301      16.586 -11.471   3.351  1.00 78.26           O  
HETATM11974  C31 LP5 D 301      16.259 -12.593   1.219  1.00 68.68           C  
HETATM11975  C32 LP5 D 301      16.591 -13.838   2.051  1.00 64.59           C  
HETATM11976  C33 LP5 D 301      15.476 -14.868   1.913  1.00 64.54           C  
HETATM11977  C34 LP5 D 301      16.085 -16.254   1.696  1.00 66.01           C  
HETATM11978  C35 LP5 D 301      15.325 -16.966   0.572  1.00 69.85           C  
HETATM11979  C36 LP5 D 301      15.394 -18.483   0.785  1.00 71.41           C  
HETATM11980  C37 LP5 D 301      15.092 -19.217  -0.530  1.00 72.65           C  
HETATM11981  C38 LP5 D 301      14.835 -20.710  -0.258  1.00 74.28           C  
HETATM11982  C39 LP5 D 301      13.454 -21.129  -0.785  1.00 76.57           C  
HETATM11983  C40 LP5 D 301      12.371 -20.846   0.272  1.00 78.48           C  
HETATM11984  C41 LP5 D 301      11.015 -20.653  -0.413  1.00 75.62           C  
HETATM11985  O   HOH A 801       7.438  -9.983  38.197  1.00 29.06           O  
HETATM11986  O   HOH A 802      10.728   6.627  24.812  1.00 22.22           O  
HETATM11987  O   HOH A 803      32.403   9.234  13.816  1.00 19.37           O  
HETATM11988  O   HOH A 804      10.977   9.836  22.059  1.00 16.43           O  
HETATM11989  O   HOH A 805      21.955  34.627  53.473  1.00 49.39           O  
HETATM11990  O   HOH A 806       6.402   6.218  25.265  1.00 33.14           O  
HETATM11991  O   HOH A 807      35.534  13.904  13.728  1.00 37.52           O  
HETATM11992  O   HOH A 808      -5.214  -6.035  19.633  1.00 39.23           O  
HETATM11993  O   HOH A 809      13.556  -9.506  16.795  1.00 33.05           O  
HETATM11994  O   HOH A 810      17.538  20.502  12.560  1.00 44.17           O  
HETATM11995  O   HOH A 811      -6.816  -9.022  13.549  1.00 38.93           O  
HETATM11996  O   HOH A 812      14.074 -13.636  36.313  1.00 41.10           O  
HETATM11997  O   HOH A 813      18.409  30.424  17.555  1.00 38.21           O  
HETATM11998  O   HOH A 814      14.925  -9.622  28.513  1.00 45.35           O  
HETATM11999  O   HOH A 815      18.290  -7.217  24.670  1.00 40.72           O  
HETATM12000  O   HOH C 401       9.763  36.765   8.708  1.00 25.99           O  
HETATM12001  O   HOH C 402      -4.581  37.384  30.871  1.00 37.83           O  
HETATM12002  O   HOH C 403       8.819  29.263  31.307  1.00 35.59           O  
HETATM12003  O   HOH C 404      11.311  31.860  14.539  1.00 41.28           O  
HETATM12004  O   HOH B 901     -17.138  17.181  -2.962  1.00 18.60           O  
HETATM12005  O   HOH B 902     -21.546  15.065  -0.647  1.00 27.51           O  
HETATM12006  O   HOH B 903       1.540  18.963 -18.702  1.00 31.32           O  
HETATM12007  O   HOH B 904     -26.986  11.309   1.041  1.00 28.17           O  
HETATM12008  O   HOH B 905     -12.329  19.544   4.555  1.00 30.53           O  
HETATM12009  O   HOH B 906     -20.370  17.344   6.860  1.00 30.07           O  
HETATM12010  O   HOH B 907     -27.231   2.844  15.618  1.00 34.22           O  
HETATM12011  O   HOH B 908      -7.551   5.317  -7.093  1.00 35.94           O  
HETATM12012  O   HOH B 909     -12.764  -1.818  14.696  1.00 28.28           O  
HETATM12013  O   HOH B 910     -13.114  19.131  -6.156  1.00 35.12           O  
HETATM12014  O   HOH B 911     -16.911  17.437   8.477  1.00 24.79           O  
HETATM12015  O   HOH B 912     -31.541 -17.527  13.947  1.00 42.73           O  
HETATM12016  O   HOH B 913     -13.386   5.197  17.348  1.00 44.85           O  
HETATM12017  O   HOH B 914     -10.180   9.001  21.843  1.00 40.89           O  
HETATM12018  O   HOH B 915      10.510 -14.239 -48.629  1.00 43.64           O  
HETATM12019  O   HOH B 916     -30.530   7.398   2.555  1.00 48.61           O  
HETATM12020  O   HOH B 917      -5.777   2.659  -3.736  1.00 35.42           O  
HETATM12021  O   HOH D 401      21.937  -8.649  -4.700  1.00 56.94           O  
CONECT   13  101                                                                
CONECT  101   13                                                                
CONECT 141511687                                                                
CONECT 2021 2224                                                                
CONECT 2224 2021                                                                
CONECT 2877 2883                                                                
CONECT 2883 2877                                                                
CONECT 395911715                                                                
CONECT 4407 4632                                                                
CONECT 4421 4749                                                                
CONECT 4632 4407                                                                
CONECT 4749 4421                                                                
CONECT 4799 4999                                                                
CONECT 4890 5782                                                                
CONECT 4999 4799                                                                
CONECT 5366 5449                                                                
CONECT 5449 5366                                                                
CONECT 5782 4890                                                                
CONECT 5856 5944                                                                
CONECT 5944 5856                                                                
CONECT 7864 8067                                                                
CONECT 8067 7864                                                                
CONECT 8720 8726                                                                
CONECT 8726 8720                                                                
CONECT 980211743                                                                
CONECT1019511878                                                                
CONECT1025010475                                                                
CONECT1026410592                                                                
CONECT1047510250                                                                
CONECT1059210264                                                                
CONECT1064210842                                                                
CONECT1073311625                                                                
CONECT1084210642                                                                
CONECT1120911292                                                                
CONECT1129211209                                                                
CONECT1162510733                                                                
CONECT11687 14151168811698                                                      
CONECT11688116871168911695                                                      
CONECT11689116881169011696                                                      
CONECT11690116891169111697                                                      
CONECT11691116901169211698                                                      
CONECT116921169111699                                                           
CONECT11693116941169511700                                                      
CONECT1169411693                                                                
CONECT116951168811693                                                           
CONECT1169611689                                                                
CONECT116971169011701                                                           
CONECT116981168711691                                                           
CONECT1169911692                                                                
CONECT1170011693                                                                
CONECT11701116971170211712                                                      
CONECT11702117011170311709                                                      
CONECT11703117021170411710                                                      
CONECT11704117031170511711                                                      
CONECT11705117041170611712                                                      
CONECT117061170511713                                                           
CONECT11707117081170911714                                                      
CONECT1170811707                                                                
CONECT117091170211707                                                           
CONECT1171011703                                                                
CONECT1171111704                                                                
CONECT117121170111705                                                           
CONECT1171311706                                                                
CONECT1171411707                                                                
CONECT11715 39591171611726                                                      
CONECT11716117151171711723                                                      
CONECT11717117161171811724                                                      
CONECT11718117171171911725                                                      
CONECT11719117181172011726                                                      
CONECT117201171911727                                                           
CONECT11721117221172311728                                                      
CONECT1172211721                                                                
CONECT117231171611721                                                           
CONECT1172411717                                                                
CONECT117251171811729                                                           
CONECT117261171511719                                                           
CONECT1172711720                                                                
CONECT1172811721                                                                
CONECT11729117251173011740                                                      
CONECT11730117291173111737                                                      
CONECT11731117301173211738                                                      
CONECT11732117311173311739                                                      
CONECT11733117321173411740                                                      
CONECT117341173311741                                                           
CONECT11735117361173711742                                                      
CONECT1173611735                                                                
CONECT117371173011735                                                           
CONECT1173811731                                                                
CONECT1173911732                                                                
CONECT117401172911733                                                           
CONECT1174111734                                                                
CONECT1174211735                                                                
CONECT11743 98021174411754                                                      
CONECT11744117431174511751                                                      
CONECT11745117441174611752                                                      
CONECT11746117451174711753                                                      
CONECT11747117461174811754                                                      
CONECT117481174711755                                                           
CONECT11749117501175111756                                                      
CONECT1175011749                                                                
CONECT117511174411749                                                           
CONECT1175211745                                                                
CONECT117531174611757                                                           
CONECT117541174311747                                                           
CONECT1175511748                                                                
CONECT1175611749                                                                
CONECT11757117531175811768                                                      
CONECT11758117571175911765                                                      
CONECT11759117581176011766                                                      
CONECT11760117591176111767                                                      
CONECT11761117601176211768                                                      
CONECT117621176111769                                                           
CONECT11763117641176511770                                                      
CONECT1176411763                                                                
CONECT117651175811763                                                           
CONECT1176611759                                                                
CONECT1176711760                                                                
CONECT117681175711761                                                           
CONECT1176911762                                                                
CONECT1177011763                                                                
CONECT117711177211782                                                           
CONECT11772117711177311779                                                      
CONECT11773117721177411780                                                      
CONECT11774117731177511781                                                      
CONECT11775117741177611782                                                      
CONECT117761177511783                                                           
CONECT11777117781177911784                                                      
CONECT1177811777                                                                
CONECT117791177211777                                                           
CONECT1178011773                                                                
CONECT1178111774                                                                
CONECT117821177111775                                                           
CONECT1178311776                                                                
CONECT1178411777                                                                
CONECT11785117861179311859                                                      
CONECT11786117851178711788                                                      
CONECT117871178611796                                                           
CONECT11788117861178911790                                                      
CONECT117891178811809                                                           
CONECT11790117881179111792                                                      
CONECT117911179011826                                                           
CONECT11792117901179311794                                                      
CONECT117931178511792                                                           
CONECT117941179211795                                                           
CONECT1179511794                                                                
CONECT11796117871179711798                                                      
CONECT1179711796                                                                
CONECT117981179611799                                                           
CONECT11799117981180011825                                                      
CONECT118001179911801                                                           
CONECT118011180011802                                                           
CONECT118021180111803                                                           
CONECT118031180211804                                                           
CONECT118041180311805                                                           
CONECT118051180411806                                                           
CONECT118061180511807                                                           
CONECT118071180611808                                                           
CONECT1180811807                                                                
CONECT11809117891181011823                                                      
CONECT118101180911811                                                           
CONECT11811118101181211824                                                      
CONECT118121181111813                                                           
CONECT118131181211814                                                           
CONECT118141181311815                                                           
CONECT118151181411816                                                           
CONECT118161181511817                                                           
CONECT118171181611818                                                           
CONECT118181181711819                                                           
CONECT118191181811820                                                           
CONECT118201181911821                                                           
CONECT118211182011822                                                           
CONECT1182211821                                                                
CONECT1182311809                                                                
CONECT1182411811                                                                
CONECT1182511799                                                                
CONECT1182611791118271182811829                                                 
CONECT1182711826                                                                
CONECT1182811826                                                                
CONECT1182911826                                                                
CONECT1183011831                                                                
CONECT1183111830118321183311834                                                 
CONECT1183211831                                                                
CONECT1183311831                                                                
CONECT118341183111835                                                           
CONECT11835118341183611857                                                      
CONECT11836118351183711854                                                      
CONECT118371183611838                                                           
CONECT11838118371183911853                                                      
CONECT118391183811840                                                           
CONECT11840118391184111842                                                      
CONECT1184111840                                                                
CONECT118421184011843                                                           
CONECT118431184211844                                                           
CONECT118441184311845                                                           
CONECT118451184411846                                                           
CONECT118461184511847                                                           
CONECT118471184611848                                                           
CONECT118481184711849                                                           
CONECT118491184811850                                                           
CONECT118501184911851                                                           
CONECT118511185011852                                                           
CONECT1185211851                                                                
CONECT1185311838                                                                
CONECT11854118361185511861                                                      
CONECT11855118541185611860                                                      
CONECT11856118551185711858                                                      
CONECT118571183511856                                                           
CONECT118581185611859                                                           
CONECT118591178511858                                                           
CONECT1186011855                                                                
CONECT118611185411862                                                           
CONECT11862118611186311864                                                      
CONECT1186311862                                                                
CONECT118641186211865                                                           
CONECT11865118641186611867                                                      
CONECT1186611865                                                                
CONECT118671186511868                                                           
CONECT118681186711869                                                           
CONECT118691186811870                                                           
CONECT118701186911871                                                           
CONECT118711187011872                                                           
CONECT118721187111873                                                           
CONECT118731187211874                                                           
CONECT118741187311875                                                           
CONECT118751187411876                                                           
CONECT118761187511877                                                           
CONECT1187711876                                                                
CONECT11878101951187911889                                                      
CONECT11879118781188011886                                                      
CONECT11880118791188111887                                                      
CONECT11881118801188211888                                                      
CONECT11882118811188311889                                                      
CONECT118831188211890                                                           
CONECT11884118851188611891                                                      
CONECT1188511884                                                                
CONECT118861187911884                                                           
CONECT1188711880                                                                
CONECT1188811881                                                                
CONECT118891187811882                                                           
CONECT1189011883                                                                
CONECT1189111884                                                                
CONECT11892118931190011966                                                      
CONECT11893118921189411895                                                      
CONECT118941189311903                                                           
CONECT11895118931189611897                                                      
CONECT118961189511916                                                           
CONECT11897118951189811899                                                      
CONECT118981189711933                                                           
CONECT11899118971190011901                                                      
CONECT119001189211899                                                           
CONECT119011189911902                                                           
CONECT1190211901                                                                
CONECT11903118941190411905                                                      
CONECT1190411903                                                                
CONECT119051190311906                                                           
CONECT11906119051190711932                                                      
CONECT119071190611908                                                           
CONECT119081190711909                                                           
CONECT119091190811910                                                           
CONECT119101190911911                                                           
CONECT119111191011912                                                           
CONECT119121191111913                                                           
CONECT119131191211914                                                           
CONECT119141191311915                                                           
CONECT1191511914                                                                
CONECT11916118961191711930                                                      
CONECT119171191611918                                                           
CONECT11918119171191911931                                                      
CONECT119191191811920                                                           
CONECT119201191911921                                                           
CONECT119211192011922                                                           
CONECT119221192111923                                                           
CONECT119231192211924                                                           
CONECT119241192311925                                                           
CONECT119251192411926                                                           
CONECT119261192511927                                                           
CONECT119271192611928                                                           
CONECT119281192711929                                                           
CONECT1192911928                                                                
CONECT1193011916                                                                
CONECT1193111918                                                                
CONECT1193211906                                                                
CONECT1193311898119341193511936                                                 
CONECT1193411933                                                                
CONECT1193511933                                                                
CONECT1193611933                                                                
CONECT1193711938                                                                
CONECT1193811937119391194011941                                                 
CONECT1193911938                                                                
CONECT1194011938                                                                
CONECT119411193811942                                                           
CONECT11942119411194311964                                                      
CONECT11943119421194411961                                                      
CONECT119441194311945                                                           
CONECT11945119441194611960                                                      
CONECT119461194511947                                                           
CONECT11947119461194811949                                                      
CONECT1194811947                                                                
CONECT119491194711950                                                           
CONECT119501194911951                                                           
CONECT119511195011952                                                           
CONECT119521195111953                                                           
CONECT119531195211954                                                           
CONECT119541195311955                                                           
CONECT119551195411956                                                           
CONECT119561195511957                                                           
CONECT119571195611958                                                           
CONECT119581195711959                                                           
CONECT1195911958                                                                
CONECT1196011945                                                                
CONECT11961119431196211968                                                      
CONECT11962119611196311967                                                      
CONECT11963119621196411965                                                      
CONECT119641194211963                                                           
CONECT119651196311966                                                           
CONECT119661189211965                                                           
CONECT1196711962                                                                
CONECT119681196111969                                                           
CONECT11969119681197011971                                                      
CONECT1197011969                                                                
CONECT119711196911972                                                           
CONECT11972119711197311974                                                      
CONECT1197311972                                                                
CONECT119741197211975                                                           
CONECT119751197411976                                                           
CONECT119761197511977                                                           
CONECT119771197611978                                                           
CONECT119781197711979                                                           
CONECT119791197811980                                                           
CONECT119801197911981                                                           
CONECT119811198011982                                                           
CONECT119821198111983                                                           
CONECT119831198211984                                                           
CONECT1198411983                                                                
MASTER      478    0   12   26  105    0    0    612017    4  334  118          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.