CNRS Nantes University US2B US2B
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***  CELL ADHESION 14-DEC-19 6TPW  ***

elNémo ID: 2403161612103502452

Job options:

ID        	=	 2403161612103502452
JOBID     	=	 CELL ADHESION 14-DEC-19 6TPW
USERID    	=	 unknown
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    CELL ADHESION                           14-DEC-19   6TPW              
TITLE     CRYSTAL STRUCTURES OF FNIII DOMAIN ONE THROUGH FOUR OF THE HUMAN      
TITLE    2 LEUCOCYTE COMMON ANTIGEN-RELATED PROTEIN ( LAR)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE F;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LEUKOCYTE COMMON ANTIGEN RELATED,LAR;                       
COMPND   5 EC: 3.1.3.48;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PTPRF, LAR;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FIBRONECTIN TYPE-III, ADHESION PROTEIN, CELL ADHESION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.VILSTRUP,S.S.THIRUP,A.SIMONSEN,T.BIRKEFELDT,D.STRANDBYGAARD       
REVDAT   2   24-JAN-24 6TPW    1       REMARK                                   
REVDAT   1   13-MAY-20 6TPW    0                                                
JRNL        AUTH   J.VILSTRUP,A.SIMONSEN,T.BIRKEFELDT,D.STRANDBYGARD,J.LYNGSO,  
JRNL        AUTH 2 J.S.PEDERSEN,S.THIRUP                                        
JRNL        TITL   CRYSTAL AND SOLUTION STRUCTURES OF FRAGMENTS OF THE HUMAN    
JRNL        TITL 2 LEUCOCYTE COMMON ANTIGEN-RELATED PROTEIN.                    
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  76   406 2020              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   32355037                                                     
JRNL        DOI    10.1107/S2059798320003885                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15102                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.282                           
REMARK   3   R VALUE            (WORKING SET) : 0.281                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 751                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.9850 -  4.9562    0.99     3069   163  0.2554 0.2525        
REMARK   3     2  4.9562 -  3.9351    0.99     2884   152  0.2618 0.3073        
REMARK   3     3  3.9351 -  3.4380    0.99     2839   146  0.3111 0.3561        
REMARK   3     4  3.4380 -  3.1238    0.98     2782   147  0.3350 0.3703        
REMARK   3     5  3.1238 -  2.9000    0.98     2777   143  0.4166 0.4344        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.510            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 164.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.7064 -21.4442-111.7377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3788 T22:   3.2233                                     
REMARK   3      T33:   1.0356 T12:  -0.4205                                     
REMARK   3      T13:  -0.1308 T23:  -0.2168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6316 L22:   4.9938                                     
REMARK   3      L33:   6.9512 L12:   0.5519                                     
REMARK   3      L13:   3.1138 L23:   3.2203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5460 S12:  -1.1829 S13:   0.1129                       
REMARK   3      S21:  -0.5710 S22:  -0.2333 S23:   0.5853                       
REMARK   3      S31:  -0.8112 S32:  -0.6182 S33:  -0.3093                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 600 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7406  -3.0716 -58.4703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7018 T22:   3.0263                                     
REMARK   3      T33:   0.7763 T12:  -0.0462                                     
REMARK   3      T13:   0.0068 T23:   0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9018 L22:   1.1218                                     
REMARK   3      L33:   1.1752 L12:   0.4625                                     
REMARK   3      L13:  -0.6969 L23:  -0.2467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2204 S12:   0.6963 S13:  -0.0221                       
REMARK   3      S21:   0.0797 S22:   0.0773 S23:   0.1680                       
REMARK   3      S31:  -0.0388 S32:  -0.2712 S33:  -0.0848                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 601 THROUGH 704 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1077 -13.9126  -2.8242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6098 T22:   2.7042                                     
REMARK   3      T33:   0.9101 T12:   0.3607                                     
REMARK   3      T13:   0.1747 T23:   0.1896                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1938 L22:   0.7319                                     
REMARK   3      L33:   2.5907 L12:  -1.2403                                     
REMARK   3      L13:  -2.3920 L23:   1.3615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1898 S12:   0.0922 S13:  -0.8803                       
REMARK   3      S21:   1.3369 S22:   0.2837 S23:   0.6931                       
REMARK   3      S31:   0.5374 S32:   0.4226 S33:  -0.0486                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6TPW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292105870.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15285                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 8.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
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: PHASER                                                
REMARK 200 STARTING MODEL: 6TPV, 6TPU                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE AND 30%           
REMARK 280  PEG8000, EVAPORATION, TEMPERATURE 277K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       37.43000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       37.43000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      230.52000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      115.26000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.43000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      345.78000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      345.78000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.43000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      115.26000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       37.43000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      230.52000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       37.43000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      230.52000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       37.43000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      345.78000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      115.26000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       37.43000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      115.26000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      345.78000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       37.43000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       37.43000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      230.52000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 310 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 21310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     MET A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     TYR A   315                                                      
REMARK 465     PHE A   316                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     GLY A   318                                                      
REMARK 465     ASP A   340                                                      
REMARK 465     SER A   341                                                      
REMARK 465     GLY A   342                                                      
REMARK 465     ASN A   343                                                      
REMARK 465     SER A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     ASP A   653                                                      
REMARK 465     ARG A   654                                                      
REMARK 465     GLY A   655                                                      
REMARK 465     ARG A   656                                                      
REMARK 465     HIS A   657                                                      
REMARK 465     GLU A   705                                                      
REMARK 465     ASP A   706                                                      
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    ASP A 324       46.06    -91.21                                   
REMARK 500    THR A 331     -165.36   -120.23                                   
REMARK 500    THR A 359     -144.09    -98.39                                   
REMARK 500    GLN A 509      -70.02    -60.03                                   
REMARK 500    SER A 524     -162.30   -160.39                                   
REMARK 500    ARG A 539       69.07    -68.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802                 
DBREF  6TPW A  319   706  UNP    P10586   PTPRF_HUMAN    319    706             
SEQADV 6TPW MET A  305  UNP  P10586              INITIATING METHIONINE          
SEQADV 6TPW HIS A  306  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW HIS A  307  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW HIS A  308  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW HIS A  309  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW HIS A  310  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW HIS A  311  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW GLU A  312  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW ASN A  313  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW LEU A  314  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW TYR A  315  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW PHE A  316  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW GLN A  317  UNP  P10586              EXPRESSION TAG                 
SEQADV 6TPW GLY A  318  UNP  P10586              EXPRESSION TAG                 
SEQRES   1 A  402  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 A  402  GLY PRO LYS PRO PRO ILE ASP LEU VAL VAL THR GLU THR          
SEQRES   3 A  402  THR ALA THR SER VAL THR LEU THR TRP ASP SER GLY ASN          
SEQRES   4 A  402  SER GLU PRO VAL THR TYR TYR GLY ILE GLN TYR ARG ALA          
SEQRES   5 A  402  ALA GLY THR GLU GLY PRO PHE GLN GLU VAL ASP GLY VAL          
SEQRES   6 A  402  ALA THR THR ARG TYR SER ILE GLY GLY LEU SER PRO PHE          
SEQRES   7 A  402  SER GLU TYR ALA PHE ARG VAL LEU ALA VAL ASN SER ILE          
SEQRES   8 A  402  GLY ARG GLY PRO PRO SER GLU ALA VAL ARG ALA ARG THR          
SEQRES   9 A  402  GLY GLU GLN ALA PRO SER SER PRO PRO ARG ARG VAL GLN          
SEQRES  10 A  402  ALA ARG MET LEU SER ALA SER THR MET LEU VAL GLN TRP          
SEQRES  11 A  402  GLU PRO PRO GLU GLU PRO ASN GLY LEU VAL ARG GLY TYR          
SEQRES  12 A  402  ARG VAL TYR TYR THR PRO ASP SER ARG ARG PRO PRO ASN          
SEQRES  13 A  402  ALA TRP HIS LYS HIS ASN THR ASP ALA GLY LEU LEU THR          
SEQRES  14 A  402  THR VAL GLY SER LEU LEU PRO GLY ILE THR TYR SER LEU          
SEQRES  15 A  402  ARG VAL LEU ALA PHE THR ALA VAL GLY ASP GLY PRO PRO          
SEQRES  16 A  402  SER PRO THR ILE GLN VAL LYS THR GLN GLN GLY VAL PRO          
SEQRES  17 A  402  ALA GLN PRO ALA ASP PHE GLN ALA GLU VAL GLU SER ASP          
SEQRES  18 A  402  THR ARG ILE GLN LEU SER TRP LEU LEU PRO PRO GLN GLU          
SEQRES  19 A  402  ARG ILE ILE MET TYR GLU LEU VAL TYR TRP ALA ALA GLU          
SEQRES  20 A  402  ASP GLU ASP GLN GLN HIS LYS VAL THR PHE ASP PRO THR          
SEQRES  21 A  402  SER SER TYR THR LEU GLU ASP LEU LYS PRO ASP THR LEU          
SEQRES  22 A  402  TYR ARG PHE GLN LEU ALA ALA ARG SER ASP MET GLY VAL          
SEQRES  23 A  402  GLY VAL PHE THR PRO THR ILE GLU ALA ARG THR ALA GLN          
SEQRES  24 A  402  SER THR PRO SER ALA PRO PRO GLN LYS VAL MET CYS VAL          
SEQRES  25 A  402  SER MET GLY SER THR THR VAL ARG VAL SER TRP VAL PRO          
SEQRES  26 A  402  PRO PRO ALA ASP SER ARG ASN GLY VAL ILE THR GLN TYR          
SEQRES  27 A  402  SER VAL ALA TYR GLU ALA VAL ASP GLY GLU ASP ARG GLY          
SEQRES  28 A  402  ARG HIS VAL VAL ASP GLY ILE SER ARG GLU HIS SER SER          
SEQRES  29 A  402  TRP ASP LEU VAL GLY LEU GLU LYS TRP THR GLU TYR ARG          
SEQRES  30 A  402  VAL TRP VAL ARG ALA HIS THR ASP VAL GLY PRO GLY PRO          
SEQRES  31 A  402  GLU SER SER PRO VAL LEU VAL ARG THR ASP GLU ASP              
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  HOH   *(H2 O)                                                       
HELIX    1 AA1 PRO A  458  TRP A  462  5                                   5    
HELIX    2 AA2 PRO A  631  ARG A  635  5                                   5    
SHEET    1 AA1 3 VAL A 326  THR A 330  0                                        
SHEET    2 AA1 3 VAL A 335  THR A 338 -1  O  THR A 336   N  THR A 328           
SHEET    3 AA1 3 ARG A 373  ILE A 376 -1  O  TYR A 374   N  LEU A 337           
SHEET    1 AA2 4 GLN A 364  VAL A 369  0                                        
SHEET    2 AA2 4 TYR A 349  ARG A 355 -1  N  TYR A 354   O  GLN A 364           
SHEET    3 AA2 4 GLU A 384  VAL A 392 -1  O  ALA A 386   N  ARG A 355           
SHEET    4 AA2 4 ARG A 397  PRO A 400 -1  O  GLY A 398   N  ALA A 391           
SHEET    1 AA3 4 GLN A 364  VAL A 369  0                                        
SHEET    2 AA3 4 TYR A 349  ARG A 355 -1  N  TYR A 354   O  GLN A 364           
SHEET    3 AA3 4 GLU A 384  VAL A 392 -1  O  ALA A 386   N  ARG A 355           
SHEET    4 AA3 4 VAL A 404  ARG A 407 -1  O  ALA A 406   N  TYR A 385           
SHEET    1 AA4 3 ARG A 418  MET A 424  0                                        
SHEET    2 AA4 3 MET A 430  GLU A 435 -1  O  GLU A 435   N  ARG A 418           
SHEET    3 AA4 3 LEU A 472  VAL A 475 -1  O  THR A 473   N  VAL A 432           
SHEET    1 AA5 4 HIS A 463  THR A 467  0                                        
SHEET    2 AA5 4 VAL A 444  THR A 452 -1  N  VAL A 449   O  HIS A 465           
SHEET    3 AA5 4 SER A 485  THR A 492 -1  O  ARG A 487   N  TYR A 450           
SHEET    4 AA5 4 ILE A 503  GLN A 504 -1  O  ILE A 503   N  LEU A 486           
SHEET    1 AA6 3 ALA A 516  VAL A 522  0                                        
SHEET    2 AA6 3 ILE A 528  LEU A 533 -1  O  SER A 531   N  GLN A 519           
SHEET    3 AA6 3 SER A 566  LEU A 569 -1  O  TYR A 567   N  LEU A 530           
SHEET    1 AA7 4 GLN A 556  PHE A 561  0                                        
SHEET    2 AA7 4 MET A 542  ALA A 549 -1  N  TYR A 547   O  HIS A 557           
SHEET    3 AA7 4 LEU A 577  SER A 586 -1  O  GLN A 581   N  VAL A 546           
SHEET    4 AA7 4 GLY A 589  VAL A 590 -1  O  GLY A 589   N  SER A 586           
SHEET    1 AA8 4 GLN A 556  PHE A 561  0                                        
SHEET    2 AA8 4 MET A 542  ALA A 549 -1  N  TYR A 547   O  HIS A 557           
SHEET    3 AA8 4 LEU A 577  SER A 586 -1  O  GLN A 581   N  VAL A 546           
SHEET    4 AA8 4 ILE A 597  ARG A 600 -1  O  ALA A 599   N  TYR A 578           
SHEET    1 AA9 3 GLN A 611  VAL A 616  0                                        
SHEET    2 AA9 3 THR A 622  VAL A 628 -1  O  ARG A 624   N  VAL A 616           
SHEET    3 AA9 3 SER A 668  VAL A 672 -1  O  LEU A 671   N  VAL A 623           
SHEET    1 AB1 4 VAL A 659  SER A 663  0                                        
SHEET    2 AB1 4 GLN A 641  ALA A 648 -1  N  VAL A 644   O  VAL A 659           
SHEET    3 AB1 4 GLU A 679  HIS A 687 -1  O  ARG A 681   N  GLU A 647           
SHEET    4 AB1 4 PRO A 692  GLU A 695 -1  O  GLY A 693   N  ALA A 686           
SHEET    1 AB2 4 VAL A 659  SER A 663  0                                        
SHEET    2 AB2 4 GLN A 641  ALA A 648 -1  N  VAL A 644   O  VAL A 659           
SHEET    3 AB2 4 GLU A 679  HIS A 687 -1  O  ARG A 681   N  GLU A 647           
SHEET    4 AB2 4 VAL A 699  ARG A 702 -1  O  VAL A 701   N  TYR A 680           
SITE     1 AC1  3 PRO A 453  ARG A 457  HIS A 463                               
SITE     1 AC2  3 PRO A 459  ARG A 487  ARG A 579                               
CRYST1   74.860   74.860  461.040  90.00  90.00  90.00 I 41 2 2     16          
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      0.013358  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002169        0.00000                         
ATOM      1  N   PRO A 319     -48.704 -21.941-126.548  1.00184.46           N  
ANISOU    1  N   PRO A 319    29797  27788  12501   -610  -5125  -1986       N  
ATOM      2  CA  PRO A 319     -49.413 -22.902-125.697  1.00183.79           C  
ANISOU    2  CA  PRO A 319    28768  28317  12749   -690  -5232  -1882       C  
ATOM      3  C   PRO A 319     -50.150 -22.221-124.553  1.00185.95           C  
ANISOU    3  C   PRO A 319    28458  29057  13136   -610  -5145  -2143       C  
ATOM      4  O   PRO A 319     -49.926 -21.040-124.288  1.00187.06           O  
ANISOU    4  O   PRO A 319    28903  29081  13091   -521  -4960  -2386       O  
ATOM      5  CB  PRO A 319     -48.290 -23.796-125.149  1.00180.35           C  
ANISOU    5  CB  PRO A 319    28030  28252  12243  -1168  -4877  -1614       C  
ATOM      6  CG  PRO A 319     -47.066 -23.443-125.929  1.00179.31           C  
ANISOU    6  CG  PRO A 319    28643  27696  11793  -1282  -4633  -1595       C  
ATOM      7  CD  PRO A 319     -47.247 -22.038-126.383  1.00181.91           C  
ANISOU    7  CD  PRO A 319    29639  27558  11922  -1045  -4636  -1857       C  
ATOM      8  N   LYS A 320     -51.020 -22.966-123.887  1.00186.45           N  
ANISOU    8  N   LYS A 320    27710  29650  13482   -661  -5278  -2103       N  
ATOM      9  CA  LYS A 320     -51.696 -22.461-122.707  1.00201.96           C  
ANISOU    9  CA  LYS A 320    29013  32184  15538   -645  -5135  -2357       C  
ATOM     10  C   LYS A 320     -50.789 -22.595-121.485  1.00199.20           C  
ANISOU   10  C   LYS A 320    28302  32351  15036  -1124  -4619  -2230       C  
ATOM     11  O   LYS A 320     -49.979 -23.522-121.404  1.00189.64           O  
ANISOU   11  O   LYS A 320    27050  31229  13774  -1489  -4486  -1908       O  
ATOM     12  CB  LYS A 320     -52.995 -23.223-122.470  1.00209.05           C  
ANISOU   12  CB  LYS A 320    29159  33500  16770   -588  -5440  -2384       C  
ATOM     13  CG  LYS A 320     -52.808 -24.727-122.361  1.00211.28           C  
ANISOU   13  CG  LYS A 320    29092  34030  17156  -1017  -5471  -1965       C  
ATOM     14  CD  LYS A 320     -54.064 -25.413-121.860  1.00211.72           C  
ANISOU   14  CD  LYS A 320    28321  34625  17496  -1110  -5672  -2000       C  
ATOM     15  CE  LYS A 320     -53.823 -26.898-121.659  1.00203.19           C  
ANISOU   15  CE  LYS A 320    26978  33759  16467  -1601  -5718  -1559       C  
ATOM     16  NZ  LYS A 320     -55.007 -27.582-121.076  1.00201.37           N  
ANISOU   16  NZ  LYS A 320    25943  34102  16467  -1827  -5857  -1570       N  
ATOM     17  N   PRO A 321     -50.900 -21.675-120.524  1.00187.77           N  
ANISOU   17  N   PRO A 321    26610  31229  13504  -1096  -4361  -2503       N  
ATOM     18  CA  PRO A 321     -50.098 -21.795-119.311  1.00191.61           C  
ANISOU   18  CA  PRO A 321    26747  32213  13844  -1535  -3905  -2399       C  
ATOM     19  C   PRO A 321     -50.527 -23.003-118.499  1.00199.45           C  
ANISOU   19  C   PRO A 321    26972  33825  14984  -1888  -3889  -2176       C  
ATOM     20  O   PRO A 321     -51.714 -23.372-118.490  1.00207.00           O  
ANISOU   20  O   PRO A 321    27463  35027  16159  -1777  -4136  -2249       O  
ATOM     21  CB  PRO A 321     -50.393 -20.484-118.561  1.00195.07           C  
ANISOU   21  CB  PRO A 321    27109  32827  14182  -1326  -3730  -2799       C  
ATOM     22  CG  PRO A 321     -51.715 -20.041-119.086  1.00192.41           C  
ANISOU   22  CG  PRO A 321    26716  32352  14037   -807  -4138  -3115       C  
ATOM     23  CD  PRO A 321     -51.736 -20.463-120.523  1.00191.61           C  
ANISOU   23  CD  PRO A 321    27181  31611  14012   -623  -4518  -2948       C  
ATOM     24  N   PRO A 322     -49.594 -23.664-117.814  1.00183.13           N  
ANISOU   24  N   PRO A 322    24772  32017  12792  -2336  -3628  -1911       N  
ATOM     25  CA  PRO A 322     -49.982 -24.729-116.884  1.00183.63           C  
ANISOU   25  CA  PRO A 322    24184  32667  12921  -2730  -3606  -1700       C  
ATOM     26  C   PRO A 322     -50.854 -24.167-115.772  1.00186.99           C  
ANISOU   26  C   PRO A 322    24010  33693  13344  -2744  -3409  -1977       C  
ATOM     27  O   PRO A 322     -50.816 -22.978-115.458  1.00188.11           O  
ANISOU   27  O   PRO A 322    24244  33845  13384  -2507  -3217  -2305       O  
ATOM     28  CB  PRO A 322     -48.641 -25.241-116.343  1.00180.55           C  
ANISOU   28  CB  PRO A 322    23916  32345  12338  -3121  -3373  -1452       C  
ATOM     29  CG  PRO A 322     -47.622 -24.794-117.350  1.00178.23           C  
ANISOU   29  CG  PRO A 322    24306  31460  11954  -2934  -3358  -1477       C  
ATOM     30  CD  PRO A 322     -48.133 -23.494-117.885  1.00180.12           C  
ANISOU   30  CD  PRO A 322    24850  31394  12193  -2516  -3374  -1811       C  
ATOM     31  N   ILE A 323     -51.661 -25.041-115.175  1.00189.06           N  
ANISOU   31  N   ILE A 323    23666  34470  13699  -3042  -3461  -1856       N  
ATOM     32  CA  ILE A 323     -52.648 -24.581-114.205  1.00193.16           C  
ANISOU   32  CA  ILE A 323    23541  35628  14223  -3058  -3275  -2162       C  
ATOM     33  C   ILE A 323     -52.484 -25.297-112.871  1.00193.72           C  
ANISOU   33  C   ILE A 323    23171  36325  14107  -3661  -2987  -1948       C  
ATOM     34  O   ILE A 323     -52.793 -24.735-111.814  1.00196.26           O  
ANISOU   34  O   ILE A 323    23096  37180  14292  -3742  -2671  -2193       O  
ATOM     35  CB  ILE A 323     -54.078 -24.754-114.753  1.00197.02           C  
ANISOU   35  CB  ILE A 323    23626  36236  14998  -2822  -3598  -2354       C  
ATOM     36  CG1 ILE A 323     -54.330 -26.207-115.162  1.00196.60           C  
ANISOU   36  CG1 ILE A 323    23461  36155  15082  -3180  -3885  -1944       C  
ATOM     37  CG2 ILE A 323     -54.314 -23.819-115.932  1.00197.39           C  
ANISOU   37  CG2 ILE A 323    24143  35672  15184  -2156  -3896  -2656       C  
ATOM     38  CD1 ILE A 323     -55.737 -26.462-115.662  1.00200.76           C  
ANISOU   38  CD1 ILE A 323    23530  36841  15908  -3016  -4212  -2129       C  
ATOM     39  N   ASP A 324     -51.995 -26.532-112.901  1.00191.72           N  
ANISOU   39  N   ASP A 324    23032  35993  13820  -4076  -3119  -1503       N  
ATOM     40  CA  ASP A 324     -51.868 -27.336-111.683  1.00200.89           C  
ANISOU   40  CA  ASP A 324    23881  37676  14773  -4686  -2932  -1256       C  
ATOM     41  C   ASP A 324     -50.505 -27.161-111.023  1.00196.40           C  
ANISOU   41  C   ASP A 324    23650  37031  13943  -4840  -2696  -1152       C  
ATOM     42  O   ASP A 324     -49.858 -28.126-110.620  1.00188.99           O  
ANISOU   42  O   ASP A 324    22844  36099  12867  -5240  -2771   -811       O  
ATOM     43  CB  ASP A 324     -52.140 -28.801-112.000  1.00201.06           C  
ANISOU   43  CB  ASP A 324    23877  37641  14876  -5066  -3276   -844       C  
ATOM     44  CG  ASP A 324     -53.619 -29.098-112.184  1.00197.50           C  
ANISOU   44  CG  ASP A 324    22886  37524  14632  -5130  -3424   -949       C  
ATOM     45  OD1 ASP A 324     -54.434 -28.151-112.147  1.00200.30           O  
ANISOU   45  OD1 ASP A 324    22872  38142  15092  -4802  -3287  -1383       O  
ATOM     46  OD2 ASP A 324     -53.970 -30.283-112.358  1.00198.58           O  
ANISOU   46  OD2 ASP A 324    22962  37665  14825  -5507  -3702   -623       O  
ATOM     47  N   LEU A 325     -50.060 -25.912-110.899  1.00188.92           N  
ANISOU   47  N   LEU A 325    22863  35995  12922  -4514  -2447  -1470       N  
ATOM     48  CA  LEU A 325     -48.795 -25.622-110.236  1.00186.56           C  
ANISOU   48  CA  LEU A 325    22833  35660  12391  -4651  -2211  -1435       C  
ATOM     49  C   LEU A 325     -48.953 -25.815-108.733  1.00189.00           C  
ANISOU   49  C   LEU A 325    22751  36607  12452  -5084  -1939  -1411       C  
ATOM     50  O   LEU A 325     -49.816 -25.189-108.108  1.00192.39           O  
ANISOU   50  O   LEU A 325    22768  37498  12833  -5038  -1717  -1693       O  
ATOM     51  CB  LEU A 325     -48.348 -24.201-110.560  1.00185.58           C  
ANISOU   51  CB  LEU A 325    23018  35242  12251  -4220  -2041  -1786       C  
ATOM     52  CG  LEU A 325     -47.025 -23.732-109.952  1.00183.45           C  
ANISOU   52  CG  LEU A 325    23024  34912  11768  -4337  -1791  -1815       C  
ATOM     53  CD1 LEU A 325     -45.889 -24.671-110.327  1.00180.28           C  
ANISOU   53  CD1 LEU A 325    22933  34210  11356  -4543  -1948  -1503       C  
ATOM     54  CD2 LEU A 325     -46.711 -22.310-110.389  1.00183.16           C  
ANISOU   54  CD2 LEU A 325    23341  34537  11714  -3945  -1662  -2157       C  
ATOM     55  N   VAL A 326     -48.128 -26.686-108.154  1.00193.18           N  
ANISOU   55  N   VAL A 326    23428  37165  12805  -5488  -1979  -1098       N  
ATOM     56  CA  VAL A 326     -48.241 -27.070-106.750  1.00190.29           C  
ANISOU   56  CA  VAL A 326    22800  37349  12153  -5971  -1784  -1000       C  
ATOM     57  C   VAL A 326     -46.853 -27.091-106.124  1.00187.97           C  
ANISOU   57  C   VAL A 326    22847  36927  11649  -6102  -1725   -917       C  
ATOM     58  O   VAL A 326     -45.891 -27.571-106.734  1.00184.93           O  
ANISOU   58  O   VAL A 326    22833  36094  11336  -6036  -1969   -755       O  
ATOM     59  CB  VAL A 326     -48.929 -28.445-106.594  1.00192.67           C  
ANISOU   59  CB  VAL A 326    22927  37856  12423  -6459  -2016   -640       C  
ATOM     60  CG1 VAL A 326     -48.901 -28.903-105.143  1.00195.56           C  
ANISOU   60  CG1 VAL A 326    23166  38721  12415  -7030  -1831   -492       C  
ATOM     61  CG2 VAL A 326     -50.362 -28.394-107.106  1.00195.74           C  
ANISOU   61  CG2 VAL A 326    22878  38467  13028  -6368  -2051   -776       C  
ATOM     62  N   VAL A 327     -46.750 -26.569-104.904  1.00210.38           N  
ANISOU   62  N   VAL A 327    25536  40176  14223  -6270  -1411  -1063       N  
ATOM     63  CA  VAL A 327     -45.524 -26.649-104.117  1.00189.19           C  
ANISOU   63  CA  VAL A 327    23123  37445  11313  -6443  -1376   -997       C  
ATOM     64  C   VAL A 327     -45.537 -27.964-103.348  1.00190.39           C  
ANISOU   64  C   VAL A 327    23314  37794  11232  -6989  -1571   -623       C  
ATOM     65  O   VAL A 327     -46.458 -28.227-102.567  1.00194.25           O  
ANISOU   65  O   VAL A 327    23513  38768  11523  -7353  -1423   -563       O  
ATOM     66  CB  VAL A 327     -45.393 -25.453-103.162  1.00189.73           C  
ANISOU   66  CB  VAL A 327    23077  37823  11188  -6355   -984  -1334       C  
ATOM     67  CG1 VAL A 327     -44.136 -25.586-102.314  1.00188.70           C  
ANISOU   67  CG1 VAL A 327    23217  37649  10830  -6547   -989  -1272       C  
ATOM     68  CG2 VAL A 327     -45.383 -24.146-103.940  1.00188.31           C  
ANISOU   68  CG2 VAL A 327    22962  37378  11209  -5830   -854  -1695       C  
ATOM     69  N   THR A 328     -44.516 -28.792-103.564  1.00188.24           N  
ANISOU   69  N   THR A 328    23416  37149  10959  -7056  -1915   -395       N  
ATOM     70  CA  THR A 328     -44.469 -30.121-102.968  1.00191.55           C  
ANISOU   70  CA  THR A 328    24006  37619  11154  -7539  -2226    -21       C  
ATOM     71  C   THR A 328     -43.493 -30.236-101.807  1.00190.91           C  
ANISOU   71  C   THR A 328    24169  37613  10754  -7752  -2245     -2       C  
ATOM     72  O   THR A 328     -43.761 -30.984-100.862  1.00210.36           O  
ANISOU   72  O   THR A 328    26707  40223  12998  -8197  -2315    240       O  
ATOM     73  CB  THR A 328     -44.104 -31.169-104.026  1.00222.50           C  
ANISOU   73  CB  THR A 328    28215  41042  15281  -7450  -2730    227       C  
ATOM     74  OG1 THR A 328     -42.818 -30.864-104.578  1.00230.24           O  
ANISOU   74  OG1 THR A 328    29445  41630  16406  -7063  -2830     60       O  
ATOM     75  CG2 THR A 328     -45.139 -31.181-105.137  1.00232.35           C  
ANISOU   75  CG2 THR A 328    29257  42205  16822  -7280  -2770    242       C  
ATOM     76  N   GLU A 329     -42.366 -29.528-101.854  1.00190.95           N  
ANISOU   76  N   GLU A 329    24302  37382  10868  -7411  -2170   -251       N  
ATOM     77  CA  GLU A 329     -41.369 -29.592-100.796  1.00215.79           C  
ANISOU   77  CA  GLU A 329    27641  40402  13946  -7475  -2193   -274       C  
ATOM     78  C   GLU A 329     -40.809 -28.201-100.541  1.00217.72           C  
ANISOU   78  C   GLU A 329    27785  40741  14198  -7200  -1823   -664       C  
ATOM     79  O   GLU A 329     -40.731 -27.369-101.448  1.00227.34           O  
ANISOU   79  O   GLU A 329    28934  41889  15554  -6884  -1678   -899       O  
ATOM     80  CB  GLU A 329     -40.226 -30.558-101.144  1.00214.71           C  
ANISOU   80  CB  GLU A 329    27848  39729  14001  -7347  -2678   -147       C  
ATOM     81  CG  GLU A 329     -40.653 -32.011-101.275  1.00220.23           C  
ANISOU   81  CG  GLU A 329    28754  40221  14703  -7606  -3118    248       C  
ATOM     82  CD  GLU A 329     -39.513 -32.919-101.692  1.00228.11           C  
ANISOU   82  CD  GLU A 329    30091  40670  15909  -7366  -3630    298       C  
ATOM     83  OE1 GLU A 329     -38.354 -32.628-101.329  1.00224.49           O  
ANISOU   83  OE1 GLU A 329    29726  40080  15491  -7153  -3669     70       O  
ATOM     84  OE2 GLU A 329     -39.777 -33.921-102.388  1.00239.34           O  
ANISOU   84  OE2 GLU A 329    31674  41808  17457  -7373  -4009    532       O  
ATOM     85  N   THR A 330     -40.416 -27.960 -99.291  1.00205.13           N  
ANISOU   85  N   THR A 330    26234  39267  12439  -7336  -1694   -728       N  
ATOM     86  CA  THR A 330     -39.846 -26.681 -98.890  1.00199.12           C  
ANISOU   86  CA  THR A 330    25413  38568  11675  -7112  -1378  -1084       C  
ATOM     87  C   THR A 330     -38.769 -26.916 -97.844  1.00192.59           C  
ANISOU   87  C   THR A 330    24804  37590  10782  -7188  -1528  -1093       C  
ATOM     88  O   THR A 330     -39.025 -27.554 -96.818  1.00192.87           O  
ANISOU   88  O   THR A 330    24941  37739  10601  -7499  -1610   -891       O  
ATOM     89  CB  THR A 330     -40.919 -25.740 -98.330  1.00205.98           C  
ANISOU   89  CB  THR A 330    25998  39919  12347  -7158   -939  -1259       C  
ATOM     90  OG1 THR A 330     -41.985 -25.604 -99.276  1.00204.89           O  
ANISOU   90  OG1 THR A 330    25644  39961  12242  -7077   -862  -1277       O  
ATOM     91  CG2 THR A 330     -40.324 -24.367 -98.047  1.00204.87           C  
ANISOU   91  CG2 THR A 330    25851  39754  12237  -6878   -661  -1638       C  
ATOM     92  N   THR A 331     -37.574 -26.403 -98.107  1.00187.64           N  
ANISOU   92  N   THR A 331    24260  36717  10316  -6929  -1572  -1342       N  
ATOM     93  CA  THR A 331     -36.478 -26.404 -97.149  1.00188.68           C  
ANISOU   93  CA  THR A 331    24554  36743  10392  -6940  -1706  -1452       C  
ATOM     94  C   THR A 331     -36.064 -24.959 -96.877  1.00188.14           C  
ANISOU   94  C   THR A 331    24382  36774  10330  -6773  -1346  -1822       C  
ATOM     95  O   THR A 331     -36.782 -24.011 -97.209  1.00187.69           O  
ANISOU   95  O   THR A 331    24166  36880  10270  -6675   -998  -1960       O  
ATOM     96  CB  THR A 331     -35.302 -27.242 -97.659  1.00191.79           C  
ANISOU   96  CB  THR A 331    25124  36777  10970  -6804  -2163  -1453       C  
ATOM     97  OG1 THR A 331     -34.730 -26.617 -98.815  1.00184.50           O  
ANISOU   97  OG1 THR A 331    24091  35738  10271  -6548  -2058  -1711       O  
ATOM     98  CG2 THR A 331     -35.762 -28.646 -98.023  1.00188.46           C  
ANISOU   98  CG2 THR A 331    24855  36186  10564  -6927  -2555  -1090       C  
ATOM     99  N   ALA A 332     -34.891 -24.794 -96.265  1.00188.57           N  
ANISOU   99  N   ALA A 332    24549  36709  10389  -6726  -1474  -2003       N  
ATOM    100  CA  ALA A 332     -34.392 -23.451 -95.997  1.00188.59           C  
ANISOU  100  CA  ALA A 332    24490  36762  10405  -6599  -1178  -2354       C  
ATOM    101  C   ALA A 332     -33.903 -22.771 -97.268  1.00185.60           C  
ANISOU  101  C   ALA A 332    24048  36218  10252  -6407  -1058  -2586       C  
ATOM    102  O   ALA A 332     -33.907 -21.536 -97.347  1.00185.38           O  
ANISOU  102  O   ALA A 332    23994  36211  10232  -6314   -747  -2834       O  
ATOM    103  CB  ALA A 332     -33.272 -23.502 -94.959  1.00189.98           C  
ANISOU  103  CB  ALA A 332    24798  36877  10511  -6630  -1381  -2495       C  
ATOM    104  N   THR A 333     -33.484 -23.549 -98.270  1.00183.89           N  
ANISOU  104  N   THR A 333    23849  35819  10202  -6352  -1308  -2516       N  
ATOM    105  CA  THR A 333     -32.881 -22.970 -99.464  1.00194.04           C  
ANISOU  105  CA  THR A 333    25111  36948  11668  -6220  -1190  -2751       C  
ATOM    106  C   THR A 333     -33.400 -23.571-100.766  1.00180.00           C  
ANISOU  106  C   THR A 333    23345  35045  10001  -6143  -1282  -2576       C  
ATOM    107  O   THR A 333     -32.824 -23.290-101.824  1.00178.59           O  
ANISOU  107  O   THR A 333    23188  34716   9951  -6056  -1224  -2750       O  
ATOM    108  CB  THR A 333     -31.352 -23.121 -99.423  1.00203.53           C  
ANISOU  108  CB  THR A 333    26294  38067  12972  -6206  -1388  -3017       C  
ATOM    109  OG1 THR A 333     -31.015 -24.503 -99.270  1.00205.17           O  
ANISOU  109  OG1 THR A 333    26539  38208  13208  -6195  -1856  -2853       O  
ATOM    110  CG2 THR A 333     -30.750 -22.321 -98.274  1.00204.06           C  
ANISOU  110  CG2 THR A 333    26355  38233  12944  -6269  -1279  -3253       C  
ATOM    111  N   SER A 334     -34.454 -24.385-100.738  1.00180.30           N  
ANISOU  111  N   SER A 334    23381  35145   9980  -6201  -1419  -2247       N  
ATOM    112  CA  SER A 334     -34.919 -25.031-101.957  1.00178.74           C  
ANISOU  112  CA  SER A 334    23211  34810   9891  -6125  -1567  -2075       C  
ATOM    113  C   SER A 334     -36.431 -25.206-101.918  1.00179.45           C  
ANISOU  113  C   SER A 334    23232  35073   9877  -6205  -1495  -1821       C  
ATOM    114  O   SER A 334     -37.031 -25.338-100.848  1.00181.59           O  
ANISOU  114  O   SER A 334    23436  35578   9981  -6383  -1445  -1698       O  
ATOM    115  CB  SER A 334     -34.243 -26.392-102.168  1.00178.71           C  
ANISOU  115  CB  SER A 334    23288  34629   9986  -6113  -2040  -1939       C  
ATOM    116  OG  SER A 334     -34.708 -27.346-101.230  1.00188.93           O  
ANISOU  116  OG  SER A 334    24652  35971  11164  -6285  -2304  -1643       O  
ATOM    117  N   VAL A 335     -37.035 -25.208-103.106  1.00178.03           N  
ANISOU  117  N   VAL A 335    23064  34801   9779  -6088  -1490  -1768       N  
ATOM    118  CA  VAL A 335     -38.466 -25.442-103.280  1.00178.87           C  
ANISOU  118  CA  VAL A 335    23060  35084   9819  -6143  -1472  -1566       C  
ATOM    119  C   VAL A 335     -38.655 -26.358-104.481  1.00181.77           C  
ANISOU  119  C   VAL A 335    23510  35157  10399  -6046  -1772  -1358       C  
ATOM    120  O   VAL A 335     -38.168 -26.059-105.577  1.00190.07           O  
ANISOU  120  O   VAL A 335    24680  35894  11643  -5816  -1759  -1485       O  
ATOM    121  CB  VAL A 335     -39.253 -24.130-103.480  1.00179.23           C  
ANISOU  121  CB  VAL A 335    23007  35195   9898  -5952  -1101  -1787       C  
ATOM    122  CG1 VAL A 335     -40.697 -24.430-103.858  1.00180.33           C  
ANISOU  122  CG1 VAL A 335    22967  35448  10102  -5928  -1124  -1629       C  
ATOM    123  CG2 VAL A 335     -39.199 -23.272-102.225  1.00198.25           C  
ANISOU  123  CG2 VAL A 335    25334  37921  12071  -6037   -829  -1991       C  
ATOM    124  N   THR A 336     -39.358 -27.469-104.279  1.00190.17           N  
ANISOU  124  N   THR A 336    24541  36316  11400  -6250  -2040  -1039       N  
ATOM    125  CA  THR A 336     -39.640 -28.426-105.341  1.00179.01           C  
ANISOU  125  CA  THR A 336    23221  34625  10169  -6178  -2375   -816       C  
ATOM    126  C   THR A 336     -41.054 -28.203-105.863  1.00189.64           C  
ANISOU  126  C   THR A 336    24392  36042  11622  -6129  -2257   -740       C  
ATOM    127  O   THR A 336     -42.003 -28.109-105.078  1.00208.46           O  
ANISOU  127  O   THR A 336    26549  38796  13859  -6345  -2102   -684       O  
ATOM    128  CB  THR A 336     -39.480 -29.863-104.841  1.00179.24           C  
ANISOU  128  CB  THR A 336    23388  34613  10103  -6432  -2820   -506       C  
ATOM    129  OG1 THR A 336     -38.133 -30.069-104.398  1.00178.98           O  
ANISOU  129  OG1 THR A 336    23498  34385  10123  -6348  -2964   -630       O  
ATOM    130  CG2 THR A 336     -39.799 -30.856-105.950  1.00178.50           C  
ANISOU  130  CG2 THR A 336    23421  34231  10168  -6356  -3208   -281       C  
ATOM    131  N   LEU A 337     -41.189 -28.120-107.185  1.00178.58           N  
ANISOU  131  N   LEU A 337    23085  34304  10464  -5845  -2335   -767       N  
ATOM    132  CA  LEU A 337     -42.462 -27.835-107.831  1.00177.37           C  
ANISOU  132  CA  LEU A 337    22787  34153  10454  -5713  -2279   -756       C  
ATOM    133  C   LEU A 337     -42.836 -28.958-108.787  1.00176.93           C  
ANISOU  133  C   LEU A 337    22835  33828  10562  -5695  -2684   -487       C  
ATOM    134  O   LEU A 337     -41.970 -29.584-109.405  1.00175.24           O  
ANISOU  134  O   LEU A 337    22876  33293  10412  -5604  -2946   -417       O  
ATOM    135  CB  LEU A 337     -42.408 -26.508-108.597  1.00176.17           C  
ANISOU  135  CB  LEU A 337    22733  33782  10423  -5344  -2017  -1071       C  
ATOM    136  CG  LEU A 337     -42.086 -25.258-107.778  1.00176.79           C  
ANISOU  136  CG  LEU A 337    22762  34059  10353  -5317  -1639  -1369       C  
ATOM    137  CD1 LEU A 337     -41.962 -24.044-108.684  1.00180.69           C  
ANISOU  137  CD1 LEU A 337    23490  34218  10944  -4978  -1470  -1644       C  
ATOM    138  CD2 LEU A 337     -43.150 -25.033-106.718  1.00179.74           C  
ANISOU  138  CD2 LEU A 337    22781  34924  10588  -5465  -1468  -1400       C  
ATOM    139  N   THR A 338     -44.140 -29.209-108.900  1.00178.85           N  
ANISOU  139  N   THR A 338    22855  34226  10873  -5775  -2743   -368       N  
ATOM    140  CA  THR A 338     -44.676 -30.168-109.855  1.00181.92           C  
ANISOU  140  CA  THR A 338    23325  34357  11439  -5747  -3129   -131       C  
ATOM    141  C   THR A 338     -45.907 -29.572-110.523  1.00179.90           C  
ANISOU  141  C   THR A 338    22860  34119  11376  -5522  -3051   -264       C  
ATOM    142  O   THR A 338     -46.615 -28.751-109.934  1.00181.89           O  
ANISOU  142  O   THR A 338    22798  34731  11582  -5521  -2750   -472       O  
ATOM    143  CB  THR A 338     -45.051 -31.508-109.198  1.00213.57           C  
ANISOU  143  CB  THR A 338    27288  38545  15314  -6212  -3434    228       C  
ATOM    144  OG1 THR A 338     -46.055 -31.291-108.199  1.00247.49           O  
ANISOU  144  OG1 THR A 338    31203  43368  19463  -6543  -3180    223       O  
ATOM    145  CG2 THR A 338     -43.832 -32.168-108.564  1.00200.32           C  
ANISOU  145  CG2 THR A 338    25885  36786  13442  -6382  -3624    343       C  
ATOM    146  N   TRP A 339     -46.155 -29.995-111.759  1.00178.92           N  
ANISOU  146  N   TRP A 339    22916  33601  11464  -5298  -3356   -175       N  
ATOM    147  CA  TRP A 339     -47.319 -29.528-112.507  1.00180.21           C  
ANISOU  147  CA  TRP A 339    22923  33714  11835  -5038  -3387   -308       C  
ATOM    148  C   TRP A 339     -47.728 -30.532-113.582  1.00180.03           C  
ANISOU  148  C   TRP A 339    23054  33345  12006  -4979  -3845    -73       C  
ATOM    149  O   TRP A 339     -47.468 -31.729-113.460  1.00180.05           O  
ANISOU  149  O   TRP A 339    23157  33294  11959  -5259  -4142    234       O  
ATOM    150  CB  TRP A 339     -47.038 -28.165-113.144  1.00178.85           C  
ANISOU  150  CB  TRP A 339    22966  33272  11717  -4583  -3165   -652       C  
ATOM    151  CG  TRP A 339     -45.890 -28.177-114.104  1.00175.80           C  
ANISOU  151  CG  TRP A 339    23086  32369  11342  -4375  -3253   -641       C  
ATOM    152  CD1 TRP A 339     -45.938 -28.470-115.436  1.00174.78           C  
ANISOU  152  CD1 TRP A 339    23279  31769  11361  -4114  -3531   -582       C  
ATOM    153  CD2 TRP A 339     -44.519 -27.881-113.808  1.00179.11           C  
ANISOU  153  CD2 TRP A 339    23723  32727  11606  -4427  -3046   -722       C  
ATOM    154  NE1 TRP A 339     -44.683 -28.377-115.986  1.00172.49           N  
ANISOU  154  NE1 TRP A 339    23386  31158  10995  -4018  -3474   -628       N  
ATOM    155  CE2 TRP A 339     -43.795 -28.016-115.008  1.00175.27           C  
ANISOU  155  CE2 TRP A 339    23652  31766  11176  -4211  -3178   -726       C  
ATOM    156  CE3 TRP A 339     -43.835 -27.515-112.644  1.00173.91           C  
ANISOU  156  CE3 TRP A 339    22935  32381  10760  -4639  -2765   -813       C  
ATOM    157  CZ2 TRP A 339     -42.420 -27.800-115.079  1.00180.85           C  
ANISOU  157  CZ2 TRP A 339    24589  32354  11771  -4225  -3012   -844       C  
ATOM    158  CZ3 TRP A 339     -42.470 -27.301-112.717  1.00179.11           C  
ANISOU  158  CZ3 TRP A 339    23840  32883  11332  -4630  -2645   -920       C  
ATOM    159  CH2 TRP A 339     -41.778 -27.443-113.926  1.00176.15           C  
ANISOU  159  CH2 TRP A 339    23820  32082  11028  -4436  -2755   -946       C  
ATOM    160  N   PRO A 346     -50.062 -30.116-125.554  1.00177.73           N  
ANISOU  160  N   PRO A 346    26802  27914  12813  -1396  -6714   -318       N  
ATOM    161  CA  PRO A 346     -48.862 -30.823-126.012  1.00175.20           C  
ANISOU  161  CA  PRO A 346    26557  27721  12288  -1660  -6430   -197       C  
ATOM    162  C   PRO A 346     -47.692 -29.867-126.151  1.00174.27           C  
ANISOU  162  C   PRO A 346    26653  27643  11917  -1697  -5886   -420       C  
ATOM    163  O   PRO A 346     -47.548 -29.247-127.197  1.00175.18           O  
ANISOU  163  O   PRO A 346    27246  27397  11918  -1449  -5800   -619       O  
ATOM    164  CB  PRO A 346     -49.284 -31.340-127.373  1.00 30.00           C  
ATOM    165  CG  PRO A 346     -50.753 -31.581-127.230  1.00 30.00           C  
ATOM    166  CD  PRO A 346     -51.282 -30.612-126.210  1.00 30.00           C  
ATOM    167  N   VAL A 347     -46.869 -29.758-125.110  1.00172.80           N  
ANISOU  167  N   VAL A 347    26152  27873  11633  -2022  -5553   -387       N  
ATOM    168  CA  VAL A 347     -45.743 -28.832-125.133  1.00172.05           C  
ANISOU  168  CA  VAL A 347    26171  27889  11313  -2131  -5034   -592       C  
ATOM    169  C   VAL A 347     -44.411 -29.503-125.157  1.00170.33           C  
ANISOU  169  C   VAL A 347    26045  27735  10936  -2313  -4865   -550       C  
ATOM    170  O   VAL A 347     -44.303 -30.694-124.948  1.00169.64           O  
ANISOU  170  O   VAL A 347    25656  27872  10927  -2466  -5065   -366       O  
ATOM    171  CB  VAL A 347     -45.742 -27.868-123.958  1.00178.05           C  
ANISOU  171  CB  VAL A 347    26376  29161  12114  -2332  -4779   -672       C  
ATOM    172  CG1 VAL A 347     -45.527 -26.445-124.453  1.00184.87           C  
ANISOU  172  CG1 VAL A 347    27325  30166  12750  -2499  -4274   -852       C  
ATOM    173  CG2 VAL A 347     -47.027 -27.995-123.166  1.00174.92           C  
ANISOU  173  CG2 VAL A 347    25890  28715  11855  -2082  -4915   -829       C  
ATOM    174  N   THR A 348     -43.385 -28.703-125.368  1.00170.13           N  
ANISOU  174  N   THR A 348    26451  27516  10677  -2304  -4517   -743       N  
ATOM    175  CA  THR A 348     -42.042 -29.257-125.513  1.00185.18           C  
ANISOU  175  CA  THR A 348    28417  29502  12440  -2435  -4362   -782       C  
ATOM    176  C   THR A 348     -41.231 -29.139-124.222  1.00168.36           C  
ANISOU  176  C   THR A 348    25838  27867  10266  -2736  -4035   -864       C  
ATOM    177  O   THR A 348     -40.501 -30.071-123.868  1.00167.72           O  
ANISOU  177  O   THR A 348    25524  28003  10197  -2835  -4129   -822       O  
ATOM    178  CB  THR A 348     -41.315 -28.597-126.693  1.00181.67           C  
ANISOU  178  CB  THR A 348    28609  28677  11739  -2358  -4112   -972       C  
ATOM    179  OG1 THR A 348     -40.045 -29.231-126.890  1.00169.64           O  
ANISOU  179  OG1 THR A 348    27065  27295  10097  -2459  -3978  -1063       O  
ATOM    180  CG2 THR A 348     -41.101 -27.111-126.466  1.00200.91           C  
ANISOU  180  CG2 THR A 348    31267  31081  13991  -2487  -3663  -1182       C  
ATOM    181  N   TYR A 349     -41.348 -28.024-123.503  1.00168.68           N  
ANISOU  181  N   TYR A 349    25774  28068  10249  -2855  -3699   -998       N  
ATOM    182  CA  TYR A 349     -40.734 -27.886-122.186  1.00176.32           C  
ANISOU  182  CA  TYR A 349    26306  29504  11185  -3129  -3431  -1066       C  
ATOM    183  C   TYR A 349     -41.375 -26.697-121.477  1.00171.03           C  
ANISOU  183  C   TYR A 349    25538  28947  10498  -3163  -3201  -1173       C  
ATOM    184  O   TYR A 349     -42.260 -26.029-122.018  1.00169.99           O  
ANISOU  184  O   TYR A 349    25667  28531  10389  -2952  -3282  -1215       O  
ATOM    185  CB  TYR A 349     -39.207 -27.747-122.274  1.00187.01           C  
ANISOU  185  CB  TYR A 349    27749  30944  12361  -3287  -3098  -1279       C  
ATOM    186  CG  TYR A 349     -38.696 -26.541-123.033  1.00184.57           C  
ANISOU  186  CG  TYR A 349    27931  30364  11832  -3322  -2708  -1513       C  
ATOM    187  CD1 TYR A 349     -38.444 -26.612-124.395  1.00175.10           C  
ANISOU  187  CD1 TYR A 349    27240  28779  10509  -3200  -2730  -1556       C  
ATOM    188  CD2 TYR A 349     -38.433 -25.343-122.380  1.00189.74           C  
ANISOU  188  CD2 TYR A 349    28589  31135  12368  -3510  -2323  -1690       C  
ATOM    189  CE1 TYR A 349     -37.969 -25.519-125.094  1.00171.68           C  
ANISOU  189  CE1 TYR A 349    27334  28080   9818  -3308  -2366  -1751       C  
ATOM    190  CE2 TYR A 349     -37.954 -24.243-123.070  1.00173.48           C  
ANISOU  190  CE2 TYR A 349    27055  28790  10071  -3607  -1988  -1886       C  
ATOM    191  CZ  TYR A 349     -37.725 -24.338-124.428  1.00172.08           C  
ANISOU  191  CZ  TYR A 349    27405  28228   9750  -3529  -2003  -1908       C  
ATOM    192  OH  TYR A 349     -37.250 -23.251-125.127  1.00178.21           O  
ANISOU  192  OH  TYR A 349    28780  28699  10233  -3697  -1664  -2085       O  
ATOM    193  N   TYR A 350     -40.926 -26.445-120.250  1.00189.24           N  
ANISOU  193  N   TYR A 350    27480  31663  12760  -3398  -2952  -1244       N  
ATOM    194  CA  TYR A 350     -41.504 -25.410-119.407  1.00180.90           C  
ANISOU  194  CA  TYR A 350    26266  30786  11681  -3427  -2748  -1363       C  
ATOM    195  C   TYR A 350     -40.415 -24.472-118.904  1.00169.56           C  
ANISOU  195  C   TYR A 350    24909  29461  10057  -3628  -2313  -1596       C  
ATOM    196  O   TYR A 350     -39.236 -24.829-118.836  1.00168.86           O  
ANISOU  196  O   TYR A 350    24782  29481   9896  -3806  -2178  -1652       O  
ATOM    197  CB  TYR A 350     -42.257 -26.013-118.212  1.00169.75           C  
ANISOU  197  CB  TYR A 350    24284  29825  10388  -3548  -2886  -1210       C  
ATOM    198  CG  TYR A 350     -43.393 -26.930-118.600  1.00170.29           C  
ANISOU  198  CG  TYR A 350    24218  29838  10646  -3429  -3307   -985       C  
ATOM    199  CD1 TYR A 350     -44.678 -26.436-118.786  1.00172.33           C  
ANISOU  199  CD1 TYR A 350    24416  30043  11018  -3223  -3422  -1043       C  
ATOM    200  CD2 TYR A 350     -43.182 -28.291-118.780  1.00169.53           C  
ANISOU  200  CD2 TYR A 350    24054  29739  10620  -3515  -3623   -743       C  
ATOM    201  CE1 TYR A 350     -45.720 -27.272-119.141  1.00175.65           C  
ANISOU  201  CE1 TYR A 350    24669  30441  11630  -3145  -3810   -864       C  
ATOM    202  CE2 TYR A 350     -44.217 -29.134-119.134  1.00177.78           C  
ANISOU  202  CE2 TYR A 350    24997  30716  11834  -3452  -4024   -530       C  
ATOM    203  CZ  TYR A 350     -45.483 -28.620-119.314  1.00172.76           C  
ANISOU  203  CZ  TYR A 350    24259  30060  11323  -3288  -4100   -590       C  
ATOM    204  OH  TYR A 350     -46.516 -29.456-119.667  1.00173.20           O  
ANISOU  204  OH  TYR A 350    24169  30075  11564  -3255  -4502   -404       O  
ATOM    205  N   GLY A 351     -40.834 -23.260-118.548  1.00170.80           N  
ANISOU  205  N   GLY A 351    25164  29592  10139  -3584  -2124  -1765       N  
ATOM    206  CA  GLY A 351     -39.943 -22.278-117.963  1.00171.24           C  
ANISOU  206  CA  GLY A 351    25295  29748  10018  -3791  -1738  -1986       C  
ATOM    207  C   GLY A 351     -40.471 -21.754-116.643  1.00175.57           C  
ANISOU  207  C   GLY A 351    25472  30664  10572  -3824  -1642  -2061       C  
ATOM    208  O   GLY A 351     -41.645 -21.385-116.544  1.00173.23           O  
ANISOU  208  O   GLY A 351    25120  30355  10346  -3598  -1780  -2086       O  
ATOM    209  N   ILE A 352     -39.621 -21.719-115.620  1.00180.03           N  
ANISOU  209  N   ILE A 352    25768  31574  11061  -4085  -1419  -2131       N  
ATOM    210  CA  ILE A 352     -40.015 -21.307-114.278  1.00172.36           C  
ANISOU  210  CA  ILE A 352    24438  30993  10059  -4146  -1311  -2201       C  
ATOM    211  C   ILE A 352     -39.431 -19.928-114.008  1.00173.52           C  
ANISOU  211  C   ILE A 352    24865  31037  10029  -4220  -1001  -2478       C  
ATOM    212  O   ILE A 352     -38.206 -19.749-114.015  1.00173.18           O  
ANISOU  212  O   ILE A 352    24937  30974   9888  -4457   -792  -2580       O  
ATOM    213  CB  ILE A 352     -39.560 -22.318-113.216  1.00171.47           C  
ANISOU  213  CB  ILE A 352    23859  31328   9963  -4385  -1351  -2063       C  
ATOM    214  CG1 ILE A 352     -40.072 -23.718-113.561  1.00170.69           C  
ANISOU  214  CG1 ILE A 352    23586  31257  10011  -4351  -1705  -1772       C  
ATOM    215  CG2 ILE A 352     -40.059 -21.897-111.848  1.00203.00           C  
ANISOU  215  CG2 ILE A 352    27521  35728  13882  -4458  -1229  -2129       C  
ATOM    216  CD1 ILE A 352     -39.685 -24.777-112.550  1.00172.25           C  
ANISOU  216  CD1 ILE A 352    23437  31821  10190  -4589  -1831  -1612       C  
ATOM    217  N   GLN A 353     -40.308 -18.959-113.762  1.00175.32           N  
ANISOU  217  N   GLN A 353    25187  31211  10217  -4016   -992  -2627       N  
ATOM    218  CA  GLN A 353     -39.929 -17.573-113.530  1.00183.01           C  
ANISOU  218  CA  GLN A 353    26509  32017  11009  -4044   -771  -2893       C  
ATOM    219  C   GLN A 353     -40.321 -17.191-112.111  1.00197.58           C  
ANISOU  219  C   GLN A 353    27955  34303  12812  -4037   -679  -3014       C  
ATOM    220  O   GLN A 353     -41.440 -17.485-111.676  1.00204.70           O  
ANISOU  220  O   GLN A 353    28496  35474  13805  -3844   -820  -2982       O  
ATOM    221  CB  GLN A 353     -40.613 -16.656-114.547  1.00204.72           C  
ANISOU  221  CB  GLN A 353    29846  34232  13708  -3743   -910  -3017       C  
ATOM    222  CG  GLN A 353     -39.893 -15.352-114.810  1.00221.67           C  
ANISOU  222  CG  GLN A 353    32617  35990  15618  -3869   -718  -3234       C  
ATOM    223  CD  GLN A 353     -40.626 -14.479-115.811  1.00223.38           C  
ANISOU  223  CD  GLN A 353    33513  35612  15747  -3552   -939  -3347       C  
ATOM    224  OE1 GLN A 353     -40.242 -13.334-116.053  1.00239.00           O  
ANISOU  224  OE1 GLN A 353    36112  37197  17501  -3627   -857  -3523       O  
ATOM    225  NE2 GLN A 353     -41.689 -15.017-116.399  1.00186.89           N  
ANISOU  225  NE2 GLN A 353    28814  30898  11295  -3204  -1259  -3254       N  
ATOM    226  N   TYR A 354     -39.408 -16.541-111.390  1.00209.97           N  
ANISOU  226  N   TYR A 354    29576  35969  14233  -4264   -435  -3171       N  
ATOM    227  CA  TYR A 354     -39.674 -16.232-109.993  1.00181.83           C  
ANISOU  227  CA  TYR A 354    25649  32840  10598  -4276   -338  -3286       C  
ATOM    228  C   TYR A 354     -38.991 -14.939-109.570  1.00207.03           C  
ANISOU  228  C   TYR A 354    29170  35891  13602  -4373   -135  -3556       C  
ATOM    229  O   TYR A 354     -37.889 -14.623-110.027  1.00193.23           O  
ANISOU  229  O   TYR A 354    27751  33886  11782  -4624      4  -3606       O  
ATOM    230  CB  TYR A 354     -39.236 -17.379-109.073  1.00180.32           C  
ANISOU  230  CB  TYR A 354    24943  33129  10442  -4536   -320  -3101       C  
ATOM    231  CG  TYR A 354     -37.759 -17.709-109.094  1.00180.89           C  
ANISOU  231  CG  TYR A 354    25063  33176  10490  -4849   -214  -3090       C  
ATOM    232  CD1 TYR A 354     -37.206 -18.448-110.132  1.00177.42           C  
ANISOU  232  CD1 TYR A 354    24741  32519  10152  -4911   -301  -2963       C  
ATOM    233  CD2 TYR A 354     -36.924 -17.309-108.058  1.00180.46           C  
ANISOU  233  CD2 TYR A 354    24903  33346  10316  -5061    -46  -3243       C  
ATOM    234  CE1 TYR A 354     -35.860 -18.761-110.150  1.00176.77           C  
ANISOU  234  CE1 TYR A 354    24628  32477  10060  -5164   -209  -3026       C  
ATOM    235  CE2 TYR A 354     -35.576 -17.619-108.067  1.00187.73           C  
ANISOU  235  CE2 TYR A 354    25802  34285  11243  -5325     24  -3293       C  
ATOM    236  CZ  TYR A 354     -35.051 -18.345-109.115  1.00217.48           C  
ANISOU  236  CZ  TYR A 354    29641  37870  15120  -5370    -53  -3202       C  
ATOM    237  OH  TYR A 354     -33.711 -18.656-109.126  1.00236.30           O  
ANISOU  237  OH  TYR A 354    31935  40329  17521  -5601     13  -3323       O  
ATOM    238  N   ARG A 355     -39.673 -14.198-108.697  1.00227.32           N  
ANISOU  238  N   ARG A 355    31638  38650  16084  -4183   -119  -3752       N  
ATOM    239  CA  ARG A 355     -39.134 -13.020-108.035  1.00198.91           C  
ANISOU  239  CA  ARG A 355    28290  34989  12298  -4257     36  -4014       C  
ATOM    240  C   ARG A 355     -39.696 -12.964-106.623  1.00213.60           C  
ANISOU  240  C   ARG A 355    29689  37381  14090  -4163     88  -4124       C  
ATOM    241  O   ARG A 355     -40.727 -13.569-106.320  1.00210.06           O  
ANISOU  241  O   ARG A 355    28815  37279  13718  -3987      2  -4054       O  
ATOM    242  CB  ARG A 355     -39.489 -11.718-108.771  1.00193.47           C  
ANISOU  242  CB  ARG A 355    28264  33744  11500  -4007    -63  -4241       C  
ATOM    243  CG  ARG A 355     -40.874 -11.174-108.416  1.00193.14           C  
ANISOU  243  CG  ARG A 355    28126  33802  11457  -3516   -247  -4456       C  
ATOM    244  CD  ARG A 355     -41.161  -9.823-109.057  1.00217.57           C  
ANISOU  244  CD  ARG A 355    31959  36293  14414  -3230   -426  -4723       C  
ATOM    245  NE  ARG A 355     -42.567  -9.452-108.908  1.00237.35           N  
ANISOU  245  NE  ARG A 355    34323  38891  16967  -2671   -678  -4966       N  
ATOM    246  CZ  ARG A 355     -43.145  -8.427-109.525  1.00252.02           C  
ANISOU  246  CZ  ARG A 355    36778  40233  18747  -2268   -968  -5226       C  
ATOM    247  NH1 ARG A 355     -42.441  -7.658-110.344  1.00268.21           N  
ANISOU  247  NH1 ARG A 355    39682  41598  20627  -2420  -1027  -5230       N  
ATOM    248  NH2 ARG A 355     -44.432  -8.171-109.326  1.00246.92           N  
ANISOU  248  NH2 ARG A 355    35886  39758  18176  -1720  -1216  -5504       N  
ATOM    249  N   ALA A 356     -39.003 -12.231-105.757  1.00221.15           N  
ANISOU  249  N   ALA A 356    30732  38411  14883  -4314    239  -4308       N  
ATOM    250  CA  ALA A 356     -39.552 -11.905-104.450  1.00211.67           C  
ANISOU  250  CA  ALA A 356    29218  37652  13556  -4183    298  -4481       C  
ATOM    251  C   ALA A 356     -40.437 -10.672-104.574  1.00225.14           C  
ANISOU  251  C   ALA A 356    31233  39133  15176  -3752    190  -4805       C  
ATOM    252  O   ALA A 356     -40.119  -9.737-105.314  1.00236.29           O  
ANISOU  252  O   ALA A 356    33259  39989  16531  -3690    115  -4939       O  
ATOM    253  CB  ALA A 356     -38.434 -11.669-103.435  1.00194.89           C  
ANISOU  253  CB  ALA A 356    27066  35694  11288  -4500    462  -4555       C  
ATOM    254  N   ALA A 357     -41.562 -10.685-103.853  1.00232.65           N  
ANISOU  254  N   ALA A 357    31774  40523  16099  -3459    167  -4952       N  
ATOM    255  CA  ALA A 357     -42.577  -9.648-104.023  1.00228.52           C  
ANISOU  255  CA  ALA A 357    31453  39841  15532  -2944     -4  -5312       C  
ATOM    256  C   ALA A 357     -42.025  -8.269-103.683  1.00223.86           C  
ANISOU  256  C   ALA A 357    31408  38915  14733  -2873    -12  -5615       C  
ATOM    257  O   ALA A 357     -42.023  -7.361-104.522  1.00206.36           O  
ANISOU  257  O   ALA A 357    29839  36088  12481  -2674   -211  -5766       O  
ATOM    258  CB  ALA A 357     -43.800  -9.965-103.161  1.00228.13           C  
ANISOU  258  CB  ALA A 357    30743  40462  15475  -2694     33  -5469       C  
ATOM    259  N   GLY A 358     -41.549  -8.096-102.451  1.00211.34           N  
ANISOU  259  N   GLY A 358    29625  37690  12984  -3050    174  -5703       N  
ATOM    260  CA  GLY A 358     -41.021  -6.836-101.980  1.00213.74           C  
ANISOU  260  CA  GLY A 358    30405  37725  13081  -3008    159  -5993       C  
ATOM    261  C   GLY A 358     -39.684  -6.418-102.550  1.00217.68           C  
ANISOU  261  C   GLY A 358    31495  37670  13544  -3414    190  -5886       C  
ATOM    262  O   GLY A 358     -39.110  -5.437-102.070  1.00231.01           O  
ANISOU  262  O   GLY A 358    33565  39156  15053  -3484    193  -6098       O  
ATOM    263  N   THR A 359     -39.164  -7.122-103.556  1.00227.28           N  
ANISOU  263  N   THR A 359    32791  38652  14912  -3701    220  -5587       N  
ATOM    264  CA  THR A 359     -37.881  -6.761-104.154  1.00244.46           C  
ANISOU  264  CA  THR A 359    35474  40369  17043  -4139    301  -5518       C  
ATOM    265  C   THR A 359     -38.075  -5.957-105.432  1.00233.58           C  
ANISOU  265  C   THR A 359    34864  38275  15608  -4013    112  -5583       C  
ATOM    266  O   THR A 359     -39.005  -5.151-105.528  1.00227.46           O  
ANISOU  266  O   THR A 359    34408  37264  14751  -3547   -134  -5820       O  
ATOM    267  CB  THR A 359     -37.054  -8.011-104.448  1.00246.28           C  
ANISOU  267  CB  THR A 359    35333  40804  17437  -4557    464  -5199       C  
ATOM    268  OG1 THR A 359     -37.855  -8.956-105.169  1.00226.57           O  
ANISOU  268  OG1 THR A 359    32584  38383  15121  -4361    364  -4984       O  
ATOM    269  CG2 THR A 359     -36.562  -8.645-103.156  1.00249.19           C  
ANISOU  269  CG2 THR A 359    35131  41750  17800  -4763    605  -5158       C  
ATOM    270  N   GLU A 360     -37.208  -6.168-106.417  1.00231.79           N  
ANISOU  270  N   GLU A 360    34960  37704  15405  -4415    207  -5400       N  
ATOM    271  CA  GLU A 360     -37.264  -5.422-107.664  1.00243.68           C  
ANISOU  271  CA  GLU A 360    37300  38493  16796  -4398     50  -5430       C  
ATOM    272  C   GLU A 360     -38.133  -6.141-108.688  1.00243.12           C  
ANISOU  272  C   GLU A 360    37179  38312  16884  -4099   -119  -5257       C  
ATOM    273  O   GLU A 360     -38.288  -7.365-108.655  1.00236.53           O  
ANISOU  273  O   GLU A 360    35699  37911  16262  -4109    -37  -5039       O  
ATOM    274  CB  GLU A 360     -35.855  -5.210-108.223  1.00250.92           C  
ANISOU  274  CB  GLU A 360    38626  39110  17604  -5049    283  -5354       C  
ATOM    275  CG  GLU A 360     -34.875  -4.583-107.229  1.00253.92           C  
ANISOU  275  CG  GLU A 360    38998  39622  17857  -5416    453  -5524       C  
ATOM    276  CD  GLU A 360     -35.026  -3.076-107.102  1.00260.65           C  
ANISOU  276  CD  GLU A 360    40646  39950  18439  -5323    260  -5789       C  
ATOM    277  OE1 GLU A 360     -36.147  -2.560-107.301  1.00270.84           O  
ANISOU  277  OE1 GLU A 360    42273  40965  19669  -4778    -57  -5914       O  
ATOM    278  OE2 GLU A 360     -34.014  -2.405-106.807  1.00258.13           O  
ANISOU  278  OE2 GLU A 360    40623  39487  17967  -5790    396  -5897       O  
ATOM    279  N   GLY A 361     -38.700  -5.356-109.602  1.00238.83           N  
ANISOU  279  N   GLY A 361    37379  37143  16222  -3829   -399  -5363       N  
ATOM    280  CA  GLY A 361     -39.571  -5.848-110.644  1.00255.54           C  
ANISOU  280  CA  GLY A 361    39584  39046  18465  -3496   -633  -5249       C  
ATOM    281  C   GLY A 361     -39.053  -7.020-111.461  1.00264.32           C  
ANISOU  281  C   GLY A 361    40472  40236  19721  -3828   -456  -4913       C  
ATOM    282  O   GLY A 361     -39.738  -8.040-111.591  1.00271.88           O  
ANISOU  282  O   GLY A 361    40884  41508  20908  -3595   -534  -4763       O  
ATOM    283  N   PRO A 362     -37.852  -6.905-112.040  1.00260.46           N  
ANISOU  283  N   PRO A 362    40393  39477  19093  -4381   -220  -4812       N  
ATOM    284  CA  PRO A 362     -37.384  -7.940-112.976  1.00255.87           C  
ANISOU  284  CA  PRO A 362    39689  38912  18617  -4641    -83  -4547       C  
ATOM    285  C   PRO A 362     -37.285  -9.311-112.321  1.00265.86           C  
ANISOU  285  C   PRO A 362    39978  40880  20157  -4672     49  -4375       C  
ATOM    286  O   PRO A 362     -36.644  -9.482-111.281  1.00276.69           O  
ANISOU  286  O   PRO A 362    40877  42695  21557  -4901    247  -4417       O  
ATOM    287  CB  PRO A 362     -36.008  -7.425-113.417  1.00242.80           C  
ANISOU  287  CB  PRO A 362    38544  36978  16732  -5284    215  -4568       C  
ATOM    288  CG  PRO A 362     -35.607  -6.451-112.362  1.00251.07           C  
ANISOU  288  CG  PRO A 362    39671  38084  17640  -5429    291  -4793       C  
ATOM    289  CD  PRO A 362     -36.876  -5.808-111.927  1.00255.57           C  
ANISOU  289  CD  PRO A 362    40385  38521  18198  -4813    -71  -4959       C  
ATOM    290  N   PHE A 363     -37.937 -10.288-112.943  1.00263.82           N  
ANISOU  290  N   PHE A 363    39474  40681  20084  -4436   -105  -4181       N  
ATOM    291  CA  PHE A 363     -37.922 -11.661-112.468  1.00244.72           C  
ANISOU  291  CA  PHE A 363    36243  38837  17901  -4466    -53  -3984       C  
ATOM    292  C   PHE A 363     -36.603 -12.347-112.806  1.00211.39           C  
ANISOU  292  C   PHE A 363    31907  34720  13692  -4931    192  -3872       C  
ATOM    293  O   PHE A 363     -35.931 -12.004-113.783  1.00213.82           O  
ANISOU  293  O   PHE A 363    32743  34638  13860  -5187    311  -3891       O  
ATOM    294  CB  PHE A 363     -39.061 -12.457-113.102  1.00249.55           C  
ANISOU  294  CB  PHE A 363    36687  39428  18701  -4083   -335  -3822       C  
ATOM    295  CG  PHE A 363     -40.399 -12.259-112.453  1.00243.17           C  
ANISOU  295  CG  PHE A 363    35579  38835  17980  -3628   -553  -3940       C  
ATOM    296  CD1 PHE A 363     -40.939 -13.248-111.649  1.00217.91           C  
ANISOU  296  CD1 PHE A 363    31612  36228  14957  -3567   -569  -3822       C  
ATOM    297  CD2 PHE A 363     -41.134 -11.106-112.674  1.00247.71           C  
ANISOU  297  CD2 PHE A 363    36650  39026  18444  -3267   -761  -4192       C  
ATOM    298  CE1 PHE A 363     -42.178 -13.087-111.061  1.00199.24           C  
ANISOU  298  CE1 PHE A 363    28906  34138  12657  -3196   -720  -3968       C  
ATOM    299  CE2 PHE A 363     -42.376 -10.939-112.088  1.00228.73           C  
ANISOU  299  CE2 PHE A 363    33890  36885  16132  -2813   -961  -4373       C  
ATOM    300  CZ  PHE A 363     -42.897 -11.932-111.280  1.00202.52           C  
ANISOU  300  CZ  PHE A 363    29731  34227  12990  -2797   -908  -4269       C  
ATOM    301  N   GLN A 364     -36.243 -13.333-111.990  1.00187.74           N  
ANISOU  301  N   GLN A 364    28223  32262  10846  -5040    255  -3778       N  
ATOM    302  CA  GLN A 364     -35.223 -14.291-112.379  1.00198.52           C  
ANISOU  302  CA  GLN A 364    29360  33778  12290  -5331    370  -3679       C  
ATOM    303  C   GLN A 364     -35.871 -15.422-113.176  1.00203.01           C  
ANISOU  303  C   GLN A 364    29794  34315  13026  -5098    143  -3436       C  
ATOM    304  O   GLN A 364     -37.070 -15.691-113.054  1.00212.00           O  
ANISOU  304  O   GLN A 364    30784  35498  14267  -4761    -90  -3325       O  
ATOM    305  CB  GLN A 364     -34.496 -14.841-111.149  1.00206.62           C  
ANISOU  305  CB  GLN A 364    29787  35336  13384  -5524    456  -3713       C  
ATOM    306  CG  GLN A 364     -33.188 -15.561-111.458  1.00219.28           C  
ANISOU  306  CG  GLN A 364    31186  37088  15041  -5837    581  -3747       C  
ATOM    307  CD  GLN A 364     -32.481 -16.054-110.209  1.00236.11           C  
ANISOU  307  CD  GLN A 364    32778  39699  17235  -5978    587  -3819       C  
ATOM    308  OE1 GLN A 364     -32.972 -15.876-109.094  1.00213.90           O  
ANISOU  308  OE1 GLN A 364    29767  37107  14398  -5876    524  -3812       O  
ATOM    309  NE2 GLN A 364     -31.323 -16.680-110.390  1.00248.55           N  
ANISOU  309  NE2 GLN A 364    34118  41443  18877  -6197    647  -3919       N  
ATOM    310  N   GLU A 365     -35.071 -16.084-114.008  1.00185.24           N  
ANISOU  310  N   GLU A 365    27579  32002  10800  -5283    210  -3381       N  
ATOM    311  CA  GLU A 365     -35.597 -17.056-114.958  1.00185.05           C  
ANISOU  311  CA  GLU A 365    27563  31847  10901  -5071    -14  -3170       C  
ATOM    312  C   GLU A 365     -34.794 -18.348-114.917  1.00175.08           C  
ANISOU  312  C   GLU A 365    25849  30907   9768  -5197    -43  -3094       C  
ATOM    313  O   GLU A 365     -33.562 -18.324-114.836  1.00175.67           O  
ANISOU  313  O   GLU A 365    25831  31127   9787  -5494    180  -3268       O  
ATOM    314  CB  GLU A 365     -35.588 -16.482-116.382  1.00186.05           C  
ANISOU  314  CB  GLU A 365    28402  31416  10873  -5081     29  -3198       C  
ATOM    315  CG  GLU A 365     -36.252 -17.363-117.430  1.00185.88           C  
ANISOU  315  CG  GLU A 365    28478  31184  10962  -4814   -240  -2992       C  
ATOM    316  CD  GLU A 365     -37.730 -17.578-117.166  1.00207.22           C  
ANISOU  316  CD  GLU A 365    31011  33895  13829  -4399   -584  -2856       C  
ATOM    317  OE1 GLU A 365     -38.089 -18.629-116.594  1.00224.13           O  
ANISOU  317  OE1 GLU A 365    32583  36410  16167  -4310   -752  -2697       O  
ATOM    318  OE2 GLU A 365     -38.534 -16.694-117.526  1.00209.72           O  
ANISOU  318  OE2 GLU A 365    31772  33844  14068  -4171   -704  -2929       O  
ATOM    319  N   VAL A 366     -35.505 -19.471-114.971  1.00174.64           N  
ANISOU  319  N   VAL A 366    25511  30960   9883  -4964   -347  -2861       N  
ATOM    320  CA  VAL A 366     -34.917 -20.795-115.148  1.00173.33           C  
ANISOU  320  CA  VAL A 366    25034  30986   9836  -4994   -494  -2767       C  
ATOM    321  C   VAL A 366     -35.515 -21.387-116.415  1.00172.77           C  
ANISOU  321  C   VAL A 366    25228  30589   9829  -4770   -716  -2594       C  
ATOM    322  O   VAL A 366     -36.728 -21.618-116.485  1.00172.30           O  
ANISOU  322  O   VAL A 366    25166  30437   9865  -4527   -970  -2403       O  
ATOM    323  CB  VAL A 366     -35.172 -21.710-113.940  1.00174.44           C  
ANISOU  323  CB  VAL A 366    24643  31542  10094  -4966   -719  -2623       C  
ATOM    324  CG1 VAL A 366     -34.703 -23.125-114.242  1.00174.92           C  
ANISOU  324  CG1 VAL A 366    24493  31699  10268  -4931   -986  -2512       C  
ATOM    325  CG2 VAL A 366     -34.472 -21.165-112.706  1.00205.39           C  
ANISOU  325  CG2 VAL A 366    28336  35772  13933  -5183   -519  -2811       C  
ATOM    326  N   ASP A 367     -34.671 -21.628-117.412  1.00193.84           N  
ANISOU  326  N   ASP A 367    28106  33106  12438  -4858   -618  -2686       N  
ATOM    327  CA  ASP A 367     -35.126 -22.019-118.735  1.00177.78           C  
ANISOU  327  CA  ASP A 367    26438  30702  10407  -4663   -786  -2561       C  
ATOM    328  C   ASP A 367     -34.800 -23.481-119.013  1.00170.77           C  
ANISOU  328  C   ASP A 367    25264  29964   9658  -4557  -1056  -2459       C  
ATOM    329  O   ASP A 367     -33.811 -24.026-118.513  1.00174.41           O  
ANISOU  329  O   ASP A 367    25363  30753  10150  -4684  -1020  -2593       O  
ATOM    330  CB  ASP A 367     -34.489 -21.132-119.810  1.00173.92           C  
ANISOU  330  CB  ASP A 367    26528  29874   9679  -4848   -463  -2749       C  
ATOM    331  CG  ASP A 367     -35.309 -21.078-121.085  1.00197.94           C  
ANISOU  331  CG  ASP A 367    30137  32411  12662  -4616   -644  -2611       C  
ATOM    332  OD1 ASP A 367     -36.407 -21.671-121.113  1.00207.20           O  
ANISOU  332  OD1 ASP A 367    31206  33509  14013  -4294  -1024  -2391       O  
ATOM    333  OD2 ASP A 367     -34.856 -20.439-122.059  1.00212.23           O  
ANISOU  333  OD2 ASP A 367    32513  33894  14229  -4780   -413  -2729       O  
ATOM    334  N   GLY A 368     -35.652 -24.110-119.819  1.00170.14           N  
ANISOU  334  N   GLY A 368    25365  29618   9661  -4294  -1375  -2244       N  
ATOM    335  CA  GLY A 368     -35.408 -25.457-120.294  1.00169.45           C  
ANISOU  335  CA  GLY A 368    25138  29567   9680  -4157  -1679  -2148       C  
ATOM    336  C   GLY A 368     -35.707 -26.557-119.299  1.00168.30           C  
ANISOU  336  C   GLY A 368    24512  29723   9709  -4103  -2042  -1959       C  
ATOM    337  O   GLY A 368     -34.846 -27.394-119.020  1.00183.21           O  
ANISOU  337  O   GLY A 368    26143  31836  11632  -4132  -2163  -2040       O  
ATOM    338  N   VAL A 369     -36.922 -26.577-118.764  1.00181.45           N  
ANISOU  338  N   VAL A 369    26070  31400  11471  -4031  -2236  -1730       N  
ATOM    339  CA  VAL A 369     -37.364 -27.628-117.856  1.00177.39           C  
ANISOU  339  CA  VAL A 369    25178  31144  11077  -4051  -2585  -1503       C  
ATOM    340  C   VAL A 369     -38.155 -28.628-118.690  1.00176.22           C  
ANISOU  340  C   VAL A 369    25160  30743  11053  -3847  -3021  -1253       C  
ATOM    341  O   VAL A 369     -39.317 -28.390-119.034  1.00179.37           O  
ANISOU  341  O   VAL A 369    25660  30968  11524  -3729  -3126  -1118       O  
ATOM    342  CB  VAL A 369     -38.191 -27.068-116.696  1.00167.52           C  
ANISOU  342  CB  VAL A 369    23681  30141   9828  -4164  -2489  -1435       C  
ATOM    343  CG1 VAL A 369     -38.676 -28.193-115.799  1.00193.57           C  
ANISOU  343  CG1 VAL A 369    26653  33701  13195  -4265  -2831  -1178       C  
ATOM    344  CG2 VAL A 369     -37.373 -26.060-115.899  1.00167.92           C  
ANISOU  344  CG2 VAL A 369    23648  30405   9748  -4351  -2085  -1693       C  
ATOM    345  N   ALA A 370     -37.522 -29.756-119.018  1.00180.04           N  
ANISOU  345  N   ALA A 370    25636  31204  11568  -3782  -3311  -1220       N  
ATOM    346  CA  ALA A 370     -38.126 -30.748-119.898  1.00191.90           C  
ANISOU  346  CA  ALA A 370    27315  32425  13173  -3579  -3755  -1004       C  
ATOM    347  C   ALA A 370     -39.118 -31.660-119.190  1.00181.76           C  
ANISOU  347  C   ALA A 370    25810  31249  12002  -3661  -4170   -675       C  
ATOM    348  O   ALA A 370     -39.850 -32.389-119.867  1.00168.75           O  
ANISOU  348  O   ALA A 370    24301  29359  10457  -3528  -4550   -468       O  
ATOM    349  CB  ALA A 370     -37.036 -31.596-120.559  1.00193.18           C  
ANISOU  349  CB  ALA A 370    27581  32512  13305  -3443  -3930  -1141       C  
ATOM    350  N   THR A 371     -39.162 -31.645-117.863  1.00172.91           N  
ANISOU  350  N   THR A 371    24375  30480  10844  -3907  -4108   -623       N  
ATOM    351  CA  THR A 371     -40.100 -32.449-117.096  1.00170.29           C  
ANISOU  351  CA  THR A 371    23848  30298  10558  -4090  -4436   -313       C  
ATOM    352  C   THR A 371     -41.163 -31.548-116.476  1.00170.99           C  
ANISOU  352  C   THR A 371    23712  30602  10654  -4220  -4154   -293       C  
ATOM    353  O   THR A 371     -41.189 -30.333-116.693  1.00168.45           O  
ANISOU  353  O   THR A 371    23441  30251  10312  -4115  -3776   -512       O  
ATOM    354  CB  THR A 371     -39.369 -33.254-116.018  1.00173.05           C  
ANISOU  354  CB  THR A 371    24062  30882  10807  -4293  -4638   -261       C  
ATOM    355  OG1 THR A 371     -38.657 -32.360-115.153  1.00168.74           O  
ANISOU  355  OG1 THR A 371    23347  30617  10148  -4413  -4224   -499       O  
ATOM    356  CG2 THR A 371     -38.389 -34.227-116.652  1.00168.94           C  
ANISOU  356  CG2 THR A 371    23743  30150  10297  -4092  -5007   -328       C  
ATOM    357  N   THR A 372     -42.055 -32.161-115.701  1.00180.91           N  
ANISOU  357  N   THR A 372    24736  32080  11920  -4462  -4356    -47       N  
ATOM    358  CA  THR A 372     -43.071 -31.433-114.956  1.00182.00           C  
ANISOU  358  CA  THR A 372    24570  32535  12049  -4610  -4095    -65       C  
ATOM    359  C   THR A 372     -42.730 -31.309-113.477  1.00172.37           C  
ANISOU  359  C   THR A 372    23111  31739  10642  -4927  -3888    -80       C  
ATOM    360  O   THR A 372     -43.562 -30.837-112.698  1.00173.98           O  
ANISOU  360  O   THR A 372    23025  32280  10797  -5093  -3676    -94       O  
ATOM    361  CB  THR A 372     -44.439 -32.099-115.124  1.00174.54           C  
ANISOU  361  CB  THR A 372    23470  31617  11228  -4710  -4394    176       C  
ATOM    362  OG1 THR A 372     -44.361 -33.467-114.705  1.00180.49           O  
ANISOU  362  OG1 THR A 372    24251  32404  11923  -4998  -4795    479       O  
ATOM    363  CG2 THR A 372     -44.886 -32.041-116.579  1.00172.72           C  
ANISOU  363  CG2 THR A 372    23480  30958  11187  -4355  -4590    150       C  
ATOM    364  N   ARG A 373     -41.530 -31.724-113.075  1.00174.25           N  
ANISOU  364  N   ARG A 373    23461  31978  10768  -4994  -3961   -108       N  
ATOM    365  CA  ARG A 373     -41.048 -31.548-111.714  1.00191.33           C  
ANISOU  365  CA  ARG A 373    25468  34489  12739  -5253  -3788   -158       C  
ATOM    366  C   ARG A 373     -39.687 -30.869-111.748  1.00185.30           C  
ANISOU  366  C   ARG A 373    24796  33675  11935  -5103  -3549   -471       C  
ATOM    367  O   ARG A 373     -38.910 -31.053-112.689  1.00184.60           O  
ANISOU  367  O   ARG A 373    24900  33310  11928  -4880  -3650   -586       O  
ATOM    368  CB  ARG A 373     -40.944 -32.886-110.961  1.00197.81           C  
ANISOU  368  CB  ARG A 373    26342  35386  13432  -5548  -4219    125       C  
ATOM    369  CG  ARG A 373     -39.898 -33.842-111.517  1.00198.57           C  
ANISOU  369  CG  ARG A 373    26717  35170  13562  -5376  -4652    132       C  
ATOM    370  CD  ARG A 373     -38.893 -34.257-110.449  1.00195.80           C  
ANISOU  370  CD  ARG A 373    26407  34875  13113  -5477  -4774     80       C  
ATOM    371  NE  ARG A 373     -38.067 -33.139-109.999  1.00201.74           N  
ANISOU  371  NE  ARG A 373    27023  35871  13760  -5440  -4355   -260       N  
ATOM    372  CZ  ARG A 373     -37.071 -33.250-109.126  1.00195.31           C  
ANISOU  372  CZ  ARG A 373    26205  35088  12916  -5453  -4394   -399       C  
ATOM    373  NH1 ARG A 373     -36.770 -34.432-108.604  1.00183.91           N  
ANISOU  373  NH1 ARG A 373    24929  33425  11523  -5474  -4853   -233       N  
ATOM    374  NH2 ARG A 373     -36.372 -32.179-108.774  1.00173.83           N  
ANISOU  374  NH2 ARG A 373    23348  32587  10114  -5437  -4007   -717       N  
ATOM    375  N   TYR A 374     -39.408 -30.079-110.714  1.00171.61           N  
ANISOU  375  N   TYR A 374    22907  32232  10064  -5244  -3221   -630       N  
ATOM    376  CA  TYR A 374     -38.133 -29.381-110.620  1.00190.32           C  
ANISOU  376  CA  TYR A 374    25321  34600  12392  -5166  -2978   -945       C  
ATOM    377  C   TYR A 374     -37.976 -28.813-109.218  1.00171.87           C  
ANISOU  377  C   TYR A 374    22810  32616   9877  -5384  -2742  -1037       C  
ATOM    378  O   TYR A 374     -38.965 -28.520-108.540  1.00181.99           O  
ANISOU  378  O   TYR A 374    23938  34136  11076  -5527  -2605   -939       O  
ATOM    379  CB  TYR A 374     -38.026 -28.259-111.660  1.00180.78           C  
ANISOU  379  CB  TYR A 374    24251  33166  11271  -4943  -2646  -1181       C  
ATOM    380  CG  TYR A 374     -36.603 -27.855-111.951  1.00170.74           C  
ANISOU  380  CG  TYR A 374    23068  31825   9980  -4895  -2474  -1485       C  
ATOM    381  CD1 TYR A 374     -35.815 -28.604-112.813  1.00168.71           C  
ANISOU  381  CD1 TYR A 374    22927  31378   9795  -4763  -2694  -1540       C  
ATOM    382  CD2 TYR A 374     -36.044 -26.731-111.360  1.00169.42           C  
ANISOU  382  CD2 TYR A 374    22849  31806   9718  -4993  -2092  -1747       C  
ATOM    383  CE1 TYR A 374     -34.513 -28.245-113.082  1.00192.73           C  
ANISOU  383  CE1 TYR A 374    25977  34433  12819  -4750  -2504  -1871       C  
ATOM    384  CE2 TYR A 374     -34.740 -26.362-111.623  1.00172.42           C  
ANISOU  384  CE2 TYR A 374    23267  32160  10083  -5010  -1917  -2048       C  
ATOM    385  CZ  TYR A 374     -33.980 -27.124-112.485  1.00195.26           C  
ANISOU  385  CZ  TYR A 374    26220  34916  13053  -4898  -2107  -2120       C  
ATOM    386  OH  TYR A 374     -32.681 -26.766-112.755  1.00206.09           O  
ANISOU  386  OH  TYR A 374    27560  36336  14410  -4942  -1901  -2471       O  
ATOM    387  N   SER A 375     -36.721 -28.656-108.798  1.00171.81           N  
ANISOU  387  N   SER A 375    22809  32662   9811  -5400  -2696  -1261       N  
ATOM    388  CA  SER A 375     -36.381 -28.131-107.480  1.00172.93           C  
ANISOU  388  CA  SER A 375    22827  33102   9778  -5584  -2510  -1382       C  
ATOM    389  C   SER A 375     -35.465 -26.926-107.648  1.00172.31           C  
ANISOU  389  C   SER A 375    22751  32998   9722  -5502  -2136  -1756       C  
ATOM    390  O   SER A 375     -34.338 -27.062-108.136  1.00171.95           O  
ANISOU  390  O   SER A 375    22742  32841   9751  -5421  -2191  -1961       O  
ATOM    391  CB  SER A 375     -35.706 -29.201-106.620  1.00180.15           C  
ANISOU  391  CB  SER A 375    23766  34088  10594  -5713  -2905  -1294       C  
ATOM    392  OG  SER A 375     -36.549 -30.326-106.444  1.00187.17           O  
ANISOU  392  OG  SER A 375    24723  34908  11488  -5830  -3251   -919       O  
ATOM    393  N   ILE A 376     -35.946 -25.757-107.238  1.00172.66           N  
ANISOU  393  N   ILE A 376    22753  33159   9690  -5536  -1767  -1867       N  
ATOM    394  CA  ILE A 376     -35.181 -24.519-107.330  1.00172.55           C  
ANISOU  394  CA  ILE A 376    22800  33097   9664  -5515  -1415  -2203       C  
ATOM    395  C   ILE A 376     -34.383 -24.348-106.044  1.00173.73           C  
ANISOU  395  C   ILE A 376    22827  33509   9675  -5682  -1382  -2358       C  
ATOM    396  O   ILE A 376     -34.961 -24.242-104.958  1.00174.88           O  
ANISOU  396  O   ILE A 376    22882  33901   9662  -5793  -1349  -2272       O  
ATOM    397  CB  ILE A 376     -36.101 -23.312-107.563  1.00172.76           C  
ANISOU  397  CB  ILE A 376    22919  33055   9668  -5420  -1107  -2272       C  
ATOM    398  CG1 ILE A 376     -36.997 -23.542-108.779  1.00171.98           C  
ANISOU  398  CG1 ILE A 376    22952  32687   9704  -5228  -1212  -2115       C  
ATOM    399  CG2 ILE A 376     -35.282 -22.041-107.722  1.00173.05           C  
ANISOU  399  CG2 ILE A 376    23119  32969   9662  -5441   -784  -2599       C  
ATOM    400  CD1 ILE A 376     -38.041 -22.469-108.961  1.00172.78           C  
ANISOU  400  CD1 ILE A 376    23140  32718   9789  -5073  -1019  -2198       C  
ATOM    401  N   GLY A 377     -33.056 -24.311-106.164  1.00173.85           N  
ANISOU  401  N   GLY A 377    22825  33492   9738  -5703  -1387  -2615       N  
ATOM    402  CA  GLY A 377     -32.184 -24.139-105.025  1.00175.20           C  
ANISOU  402  CA  GLY A 377    22881  33881   9806  -5834  -1400  -2811       C  
ATOM    403  C   GLY A 377     -31.579 -22.741-104.959  1.00175.73           C  
ANISOU  403  C   GLY A 377    22977  33944   9849  -5910  -1004  -3146       C  
ATOM    404  O   GLY A 377     -31.822 -21.879-105.799  1.00184.90           O  
ANISOU  404  O   GLY A 377    24298  34908  11046  -5876   -722  -3220       O  
ATOM    405  N   GLY A 378     -30.775 -22.531-103.920  1.00177.13           N  
ANISOU  405  N   GLY A 378    23036  34268   9998  -6005  -1018  -3334       N  
ATOM    406  CA  GLY A 378     -30.076 -21.272-103.765  1.00178.08           C  
ANISOU  406  CA  GLY A 378    23180  34385  10098  -6120   -692  -3663       C  
ATOM    407  C   GLY A 378     -30.899 -20.139-103.203  1.00178.52           C  
ANISOU  407  C   GLY A 378    23366  34421  10043  -6124   -419  -3638       C  
ATOM    408  O   GLY A 378     -30.504 -18.976-103.339  1.00179.30           O  
ANISOU  408  O   GLY A 378    23591  34416  10119  -6209   -142  -3880       O  
ATOM    409  N   LEU A 379     -32.028 -20.435-102.568  1.00178.52           N  
ANISOU  409  N   LEU A 379    23344  34526   9959  -6048   -494  -3377       N  
ATOM    410  CA  LEU A 379     -32.882 -19.390-102.031  1.00179.43           C  
ANISOU  410  CA  LEU A 379    23540  34679   9955  -5999   -253  -3407       C  
ATOM    411  C   LEU A 379     -32.423 -18.980-100.633  1.00181.23           C  
ANISOU  411  C   LEU A 379    23699  35063  10096  -6080   -223  -3541       C  
ATOM    412  O   LEU A 379     -31.668 -19.688 -99.962  1.00181.81           O  
ANISOU  412  O   LEU A 379    23661  35237  10182  -6166   -442  -3541       O  
ATOM    413  CB  LEU A 379     -34.338 -19.854-101.996  1.00179.30           C  
ANISOU  413  CB  LEU A 379    23467  34793   9867  -5900   -308  -3131       C  
ATOM    414  CG  LEU A 379     -34.935 -20.237-103.352  1.00177.75           C  
ANISOU  414  CG  LEU A 379    23354  34443   9738  -5797   -374  -2994       C  
ATOM    415  CD1 LEU A 379     -36.385 -20.668-103.204  1.00178.25           C  
ANISOU  415  CD1 LEU A 379    23297  34708   9719  -5737   -434  -2765       C  
ATOM    416  CD2 LEU A 379     -34.810 -19.082-104.332  1.00177.49           C  
ANISOU  416  CD2 LEU A 379    23590  34113   9737  -5704   -150  -3210       C  
ATOM    417  N   SER A 380     -32.893 -17.811-100.200  1.00182.42           N  
ANISOU  417  N   SER A 380    23953  35214  10143  -6022     12  -3679       N  
ATOM    418  CA  SER A 380     -32.550 -17.284 -98.884  1.00184.35           C  
ANISOU  418  CA  SER A 380    24175  35589  10282  -6073     57  -3823       C  
ATOM    419  C   SER A 380     -33.573 -17.737 -97.845  1.00185.63           C  
ANISOU  419  C   SER A 380    24217  36024  10289  -6037     19  -3623       C  
ATOM    420  O   SER A 380     -34.766 -17.833 -98.149  1.00185.58           O  
ANISOU  420  O   SER A 380    24163  36118  10232  -5938     88  -3486       O  
ATOM    421  CB  SER A 380     -32.491 -15.759 -98.910  1.00185.51           C  
ANISOU  421  CB  SER A 380    24535  35579  10372  -6024    302  -4101       C  
ATOM    422  OG  SER A 380     -31.472 -15.300 -99.781  1.00185.08           O  
ANISOU  422  OG  SER A 380    24620  35281  10422  -6157    372  -4294       O  
ATOM    423  N   PRO A 381     -33.133 -18.020 -96.621  1.00187.20           N  
ANISOU  423  N   PRO A 381    24371  36366  10392  -6136    -88  -3622       N  
ATOM    424  CA  PRO A 381     -34.068 -18.489 -95.594  1.00189.05           C  
ANISOU  424  CA  PRO A 381    24527  36868  10435  -6173    -94  -3426       C  
ATOM    425  C   PRO A 381     -34.992 -17.379 -95.120  1.00190.89           C  
ANISOU  425  C   PRO A 381    24757  37253  10519  -6036    197  -3583       C  
ATOM    426  O   PRO A 381     -34.617 -16.205 -95.065  1.00191.41           O  
ANISOU  426  O   PRO A 381    24949  37193  10584  -5930    334  -3864       O  
ATOM    427  CB  PRO A 381     -33.148 -18.961 -94.459  1.00190.56           C  
ANISOU  427  CB  PRO A 381    24769  37093  10544  -6308   -311  -3433       C  
ATOM    428  CG  PRO A 381     -31.784 -19.090 -95.078  1.00189.16           C  
ANISOU  428  CG  PRO A 381    24606  36707  10558  -6326   -494  -3600       C  
ATOM    429  CD  PRO A 381     -31.738 -18.055 -96.153  1.00187.74           C  
ANISOU  429  CD  PRO A 381    24457  36370  10505  -6242   -242  -3802       C  
ATOM    430  N   PHE A 382     -36.220 -17.775 -94.774  1.00192.34           N  
ANISOU  430  N   PHE A 382    24792  37728  10560  -6048    277  -3421       N  
ATOM    431  CA  PHE A 382     -37.226 -16.866 -94.219  1.00194.90           C  
ANISOU  431  CA  PHE A 382    25038  38307  10709  -5897    539  -3606       C  
ATOM    432  C   PHE A 382     -37.495 -15.694 -95.161  1.00194.19           C  
ANISOU  432  C   PHE A 382    25047  38039  10697  -5616    666  -3875       C  
ATOM    433  O   PHE A 382     -37.640 -14.546 -94.736  1.00196.07           O  
ANISOU  433  O   PHE A 382    25381  38286  10831  -5431    807  -4164       O  
ATOM    434  CB  PHE A 382     -36.813 -16.374 -92.828  1.00197.48           C  
ANISOU  434  CB  PHE A 382    25444  38731  10859  -5931    598  -3749       C  
ATOM    435  CG  PHE A 382     -37.936 -15.762 -92.039  1.00200.94           C  
ANISOU  435  CG  PHE A 382    25749  39534  11066  -5812    848  -3904       C  
ATOM    436  CD1 PHE A 382     -39.013 -16.532 -91.630  1.00203.10           C  
ANISOU  436  CD1 PHE A 382    25781  40212  11177  -5966    940  -3723       C  
ATOM    437  CD2 PHE A 382     -37.907 -14.421 -91.692  1.00202.54           C  
ANISOU  437  CD2 PHE A 382    26067  39693  11194  -5564    986  -4255       C  
ATOM    438  CE1 PHE A 382     -40.045 -15.972 -90.901  1.00206.91           C  
ANISOU  438  CE1 PHE A 382    26075  41106  11434  -5865   1200  -3922       C  
ATOM    439  CE2 PHE A 382     -38.935 -13.856 -90.964  1.00206.17           C  
ANISOU  439  CE2 PHE A 382    26383  40521  11432  -5407   1202  -4453       C  
ATOM    440  CZ  PHE A 382     -40.006 -14.633 -90.568  1.00208.43           C  
ANISOU  440  CZ  PHE A 382    26363  41265  11565  -5554   1326  -4302       C  
ATOM    441  N   SER A 383     -37.562 -15.984 -96.458  1.00191.77           N  
ANISOU  441  N   SER A 383    24774  37538  10550  -5576    585  -3786       N  
ATOM    442  CA  SER A 383     -37.828 -14.976 -97.472  1.00191.30           C  
ANISOU  442  CA  SER A 383    24904  37247  10534  -5332    654  -4011       C  
ATOM    443  C   SER A 383     -39.015 -15.414 -98.316  1.00191.02           C  
ANISOU  443  C   SER A 383    24718  37364  10499  -5215    628  -3913       C  
ATOM    444  O   SER A 383     -39.164 -16.599 -98.627  1.00189.68           O  
ANISOU  444  O   SER A 383    24390  37281  10399  -5382    504  -3618       O  
ATOM    445  CB  SER A 383     -36.603 -14.743 -98.364  1.00189.01           C  
ANISOU  445  CB  SER A 383    24889  36509  10416  -5413    582  -4050       C  
ATOM    446  OG  SER A 383     -35.493 -14.310 -97.597  1.00189.67           O  
ANISOU  446  OG  SER A 383    25070  36500  10495  -5540    596  -4187       O  
ATOM    447  N   GLU A 384     -39.859 -14.453 -98.680  1.00192.64           N  
ANISOU  447  N   GLU A 384    24992  37597  10607  -4915    703  -4189       N  
ATOM    448  CA  GLU A 384     -41.051 -14.732 -99.466  1.00193.02           C  
ANISOU  448  CA  GLU A 384    24871  37764  10702  -4729    649  -4163       C  
ATOM    449  C   GLU A 384     -40.758 -14.512-100.944  1.00190.75           C  
ANISOU  449  C   GLU A 384    24921  36889  10666  -4584    507  -4126       C  
ATOM    450  O   GLU A 384     -40.231 -13.464-101.331  1.00190.87           O  
ANISOU  450  O   GLU A 384    25340  36505  10679  -4462    516  -4338       O  
ATOM    451  CB  GLU A 384     -42.214 -13.847 -99.016  1.00205.00           C  
ANISOU  451  CB  GLU A 384    26228  39564  12099  -4381    755  -4511       C  
ATOM    452  CG  GLU A 384     -43.564 -14.268 -99.572  1.00198.15           C  
ANISOU  452  CG  GLU A 384    25024  38894  11372  -4183    697  -4496       C  
ATOM    453  CD  GLU A 384     -44.585 -14.525 -98.481  1.00215.27           C  
ANISOU  453  CD  GLU A 384    26677  41785  13332  -4232    882  -4608       C  
ATOM    454  OE1 GLU A 384     -44.323 -14.142 -97.320  1.00203.88           O  
ANISOU  454  OE1 GLU A 384    25207  40645  11612  -4324   1056  -4759       O  
ATOM    455  OE2 GLU A 384     -45.645 -15.112 -98.781  1.00203.40           O  
ANISOU  455  OE2 GLU A 384    24791  40563  11929  -4203    862  -4558       O  
ATOM    456  N   TYR A 385     -41.097 -15.503-101.763  1.00189.03           N  
ANISOU  456  N   TYR A 385    24580  36607  10635  -4629    370  -3853       N  
ATOM    457  CA  TYR A 385     -40.916 -15.440-103.204  1.00187.10           C  
ANISOU  457  CA  TYR A 385    24653  35833  10604  -4501    231  -3791       C  
ATOM    458  C   TYR A 385     -42.253 -15.636-103.906  1.00188.14           C  
ANISOU  458  C   TYR A 385    24626  35977  10880  -4213     99  -3780       C  
ATOM    459  O   TYR A 385     -43.241 -16.078-103.312  1.00190.05           O  
ANISOU  459  O   TYR A 385    24430  36691  11088  -4198    123  -3768       O  
ATOM    460  CB  TYR A 385     -39.912 -16.495-103.687  1.00187.76           C  
ANISOU  460  CB  TYR A 385    24781  35759  10799  -4798    137  -3494       C  
ATOM    461  CG  TYR A 385     -38.472 -16.208-103.328  1.00183.16           C  
ANISOU  461  CG  TYR A 385    24387  35064  10140  -5035    225  -3575       C  
ATOM    462  CD1 TYR A 385     -37.829 -16.924-102.326  1.00182.91           C  
ANISOU  462  CD1 TYR A 385    24137  35349  10013  -5305    212  -3472       C  
ATOM    463  CD2 TYR A 385     -37.752 -15.225-103.995  1.00183.07           C  
ANISOU  463  CD2 TYR A 385    24792  34625  10141  -5012    299  -3767       C  
ATOM    464  CE1 TYR A 385     -36.510 -16.667-101.997  1.00182.53           C  
ANISOU  464  CE1 TYR A 385    24205  35168   9980  -5477    256  -3579       C  
ATOM    465  CE2 TYR A 385     -36.435 -14.960-103.673  1.00182.79           C  
ANISOU  465  CE2 TYR A 385    24870  34531  10051  -5269    391  -3876       C  
ATOM    466  CZ  TYR A 385     -35.819 -15.683-102.674  1.00196.28           C  
ANISOU  466  CZ  TYR A 385    26283  36552  11743  -5474    362  -3795       C  
ATOM    467  OH  TYR A 385     -34.507 -15.420-102.353  1.00218.27           O  
ANISOU  467  OH  TYR A 385    29121  39226  14585  -5672    417  -3926       O  
ATOM    468  N   ALA A 386     -42.271 -15.298-105.191  1.00203.24           N  
ANISOU  468  N   ALA A 386    26909  37372  12941  -4006    -42  -3801       N  
ATOM    469  CA  ALA A 386     -43.414 -15.527-106.062  1.00188.04           C  
ANISOU  469  CA  ALA A 386    24905  35351  11190  -3714   -239  -3786       C  
ATOM    470  C   ALA A 386     -42.960 -16.343-107.262  1.00185.09           C  
ANISOU  470  C   ALA A 386    24748  34590  10988  -3823   -397  -3491       C  
ATOM    471  O   ALA A 386     -41.891 -16.088-107.824  1.00200.93           O  
ANISOU  471  O   ALA A 386    27174  36200  12971  -3947   -359  -3464       O  
ATOM    472  CB  ALA A 386     -44.038 -14.206-106.524  1.00190.73           C  
ANISOU  472  CB  ALA A 386    25581  35370  11518  -3253   -337  -4154       C  
ATOM    473  N   PHE A 387     -43.768 -17.328-107.649  1.00205.90           N  
ANISOU  473  N   PHE A 387    27086  37364  13782  -3797   -566  -3290       N  
ATOM    474  CA  PHE A 387     -43.427 -18.240-108.732  1.00193.97           C  
ANISOU  474  CA  PHE A 387    25741  35530  12427  -3883   -749  -3003       C  
ATOM    475  C   PHE A 387     -44.558 -18.282-109.748  1.00183.37           C  
ANISOU  475  C   PHE A 387    24435  33969  11267  -3543  -1001  -3027       C  
ATOM    476  O   PHE A 387     -45.735 -18.205-109.383  1.00185.99           O  
ANISOU  476  O   PHE A 387    24393  34625  11649  -3360  -1054  -3164       O  
ATOM    477  CB  PHE A 387     -43.156 -19.659-108.207  1.00189.46           C  
ANISOU  477  CB  PHE A 387    24815  35300  11871  -4244   -791  -2671       C  
ATOM    478  CG  PHE A 387     -42.018 -19.742-107.228  1.00179.99           C  
ANISOU  478  CG  PHE A 387    23591  34292  10504  -4555   -621  -2651       C  
ATOM    479  CD1 PHE A 387     -42.218 -19.461-105.886  1.00191.52           C  
ANISOU  479  CD1 PHE A 387    24777  36209  11783  -4670   -446  -2761       C  
ATOM    480  CD2 PHE A 387     -40.751 -20.114-107.647  1.00177.68           C  
ANISOU  480  CD2 PHE A 387    23534  33744  10232  -4718   -650  -2554       C  
ATOM    481  CE1 PHE A 387     -41.175 -19.540-104.983  1.00205.53           C  
ANISOU  481  CE1 PHE A 387    26559  38131  13401  -4935   -337  -2753       C  
ATOM    482  CE2 PHE A 387     -39.703 -20.193-106.748  1.00191.54           C  
ANISOU  482  CE2 PHE A 387    25238  35681  11857  -4970   -543  -2582       C  
ATOM    483  CZ  PHE A 387     -39.916 -19.906-105.414  1.00209.71           C  
ANISOU  483  CZ  PHE A 387    27310  38389  13981  -5075   -404  -2670       C  
ATOM    484  N   ARG A 388     -44.194 -18.407-111.022  1.00197.70           N  
ANISOU  484  N   ARG A 388    26689  35255  13172  -3460  -1158  -2921       N  
ATOM    485  CA  ARG A 388     -45.164 -18.568-112.095  1.00182.56           C  
ANISOU  485  CA  ARG A 388    24871  33062  11432  -3144  -1454  -2911       C  
ATOM    486  C   ARG A 388     -44.502 -19.319-113.240  1.00179.93           C  
ANISOU  486  C   ARG A 388    24882  32312  11172  -3243  -1592  -2649       C  
ATOM    487  O   ARG A 388     -43.284 -19.249-113.425  1.00178.17           O  
ANISOU  487  O   ARG A 388    24964  31893  10838  -3456  -1435  -2601       O  
ATOM    488  CB  ARG A 388     -45.717 -17.220-112.576  1.00185.22           C  
ANISOU  488  CB  ARG A 388    25609  33032  11732  -2711  -1552  -3263       C  
ATOM    489  CG  ARG A 388     -44.683 -16.286-113.183  1.00184.65           C  
ANISOU  489  CG  ARG A 388    26278  32395  11486  -2738  -1460  -3351       C  
ATOM    490  CD  ARG A 388     -45.287 -14.916-113.452  1.00188.03           C  
ANISOU  490  CD  ARG A 388    27145  32467  11830  -2317  -1607  -3714       C  
ATOM    491  NE  ARG A 388     -44.384 -14.052-114.206  1.00188.10           N  
ANISOU  491  NE  ARG A 388    27981  31848  11642  -2392  -1562  -3765       N  
ATOM    492  CZ  ARG A 388     -44.629 -12.776-114.484  1.00191.19           C  
ANISOU  492  CZ  ARG A 388    28963  31795  11883  -2106  -1704  -4055       C  
ATOM    493  NH1 ARG A 388     -45.752 -12.207-114.066  1.00194.40           N  
ANISOU  493  NH1 ARG A 388    29179  32339  12345  -1648  -1920  -4366       N  
ATOM    494  NH2 ARG A 388     -43.750 -12.067-115.179  1.00191.55           N  
ANISOU  494  NH2 ARG A 388    29805  31267  11708  -2287  -1641  -4059       N  
ATOM    495  N   VAL A 389     -45.316 -20.045-114.003  1.00208.80           N  
ANISOU  495  N   VAL A 389    28457  35862  15013  -3086  -1887  -2508       N  
ATOM    496  CA  VAL A 389     -44.835 -20.924-115.062  1.00201.98           C  
ANISOU  496  CA  VAL A 389    27860  34655  14226  -3153  -2061  -2252       C  
ATOM    497  C   VAL A 389     -45.557 -20.589-116.359  1.00179.03           C  
ANISOU  497  C   VAL A 389    25370  31238  11417  -2768  -2352  -2327       C  
ATOM    498  O   VAL A 389     -46.767 -20.341-116.363  1.00181.45           O  
ANISOU  498  O   VAL A 389    25474  31620  11848  -2477  -2550  -2474       O  
ATOM    499  CB  VAL A 389     -45.040 -22.412-114.700  1.00197.78           C  
ANISOU  499  CB  VAL A 389    26856  34475  13816  -3394  -2210  -1940       C  
ATOM    500  CG1 VAL A 389     -44.480 -23.314-115.792  1.00180.98           C  
ANISOU  500  CG1 VAL A 389    25031  31977  11755  -3418  -2419  -1709       C  
ATOM    501  CG2 VAL A 389     -44.401 -22.732-113.358  1.00196.25           C  
ANISOU  501  CG2 VAL A 389    26312  34760  13494  -3758  -1979  -1874       C  
ATOM    502  N   LEU A 390     -44.809 -20.578-117.460  1.00177.75           N  
ANISOU  502  N   LEU A 390    25785  30569  11183  -2765  -2384  -2257       N  
ATOM    503  CA  LEU A 390     -45.366 -20.454-118.797  1.00190.22           C  
ANISOU  503  CA  LEU A 390    27849  31606  12821  -2440  -2695  -2270       C  
ATOM    504  C   LEU A 390     -44.933 -21.651-119.634  1.00195.46           C  
ANISOU  504  C   LEU A 390    28610  32104  13552  -2550  -2846  -1986       C  
ATOM    505  O   LEU A 390     -43.909 -22.286-119.366  1.00176.31           O  
ANISOU  505  O   LEU A 390    26068  29855  11067  -2858  -2666  -1847       O  
ATOM    506  CB  LEU A 390     -44.933 -19.140-119.470  1.00181.23           C  
ANISOU  506  CB  LEU A 390    27490  29918  11453  -2315  -2606  -2489       C  
ATOM    507  CG  LEU A 390     -43.443 -18.889-119.721  1.00178.82           C  
ANISOU  507  CG  LEU A 390    27611  29429  10905  -2668  -2264  -2461       C  
ATOM    508  CD1 LEU A 390     -43.042 -19.306-121.131  1.00193.84           C  
ANISOU  508  CD1 LEU A 390    30065  30846  12738  -2663  -2376  -2330       C  
ATOM    509  CD2 LEU A 390     -43.097 -17.428-119.473  1.00180.89           C  
ANISOU  509  CD2 LEU A 390    28329  29473  10927  -2694  -2058  -2725       C  
ATOM    510  N   ALA A 391     -45.730 -21.957-120.652  1.00194.96           N  
ANISOU  510  N   ALA A 391    28763  31695  13617  -2260  -3216  -1932       N  
ATOM    511  CA  ALA A 391     -45.496 -23.102-121.517  1.00190.96           C  
ANISOU  511  CA  ALA A 391    28372  30998  13185  -2294  -3434  -1680       C  
ATOM    512  C   ALA A 391     -44.958 -22.651-122.869  1.00179.35           C  
ANISOU  512  C   ALA A 391    27720  28894  11530  -2170  -3453  -1727       C  
ATOM    513  O   ALA A 391     -45.245 -21.545-123.337  1.00181.18           O  
ANISOU  513  O   ALA A 391    28468  28735  11637  -1958  -3479  -1926       O  
ATOM    514  CB  ALA A 391     -46.778 -23.914-121.716  1.00191.60           C  
ANISOU  514  CB  ALA A 391    28105  31153  13541  -2099  -3866  -1562       C  
ATOM    515  N   VAL A 392     -44.176 -23.528-123.494  1.00176.20           N  
ANISOU  515  N   VAL A 392    27470  28391  11090  -2305  -3458  -1556       N  
ATOM    516  CA  VAL A 392     -43.594 -23.277-124.807  1.00193.20           C  
ANISOU  516  CA  VAL A 392    30375  30001  13030  -2249  -3438  -1586       C  
ATOM    517  C   VAL A 392     -43.684 -24.563-125.618  1.00187.50           C  
ANISOU  517  C   VAL A 392    29663  29151  12428  -2148  -3766  -1372       C  
ATOM    518  O   VAL A 392     -43.542 -25.663-125.074  1.00178.17           O  
ANISOU  518  O   VAL A 392    27956  28338  11404  -2276  -3856  -1207       O  
ATOM    519  CB  VAL A 392     -42.134 -22.780-124.696  1.00190.17           C  
ANISOU  519  CB  VAL A 392    30213  29675  12368  -2602  -2941  -1704       C  
ATOM    520  CG1 VAL A 392     -41.258 -23.825-124.036  1.00172.48           C  
ANISOU  520  CG1 VAL A 392    27412  27918  10205  -2861  -2807  -1607       C  
ATOM    521  CG2 VAL A 392     -41.581 -22.404-126.064  1.00200.32           C  
ANISOU  521  CG2 VAL A 392    32320  30420  13373  -2608  -2862  -1762       C  
ATOM    522  N   ASN A 393     -43.961 -24.428-126.910  1.00180.48           N  
ANISOU  522  N   ASN A 393    29419  27707  11448  -1909  -3992  -1375       N  
ATOM    523  CA  ASN A 393     -43.941 -25.566-127.823  1.00178.96           C  
ANISOU  523  CA  ASN A 393    29359  27320  11317  -1794  -4297  -1200       C  
ATOM    524  C   ASN A 393     -43.122 -25.164-129.048  1.00208.49           C  
ANISOU  524  C   ASN A 393    33908  30592  14715  -1816  -4119  -1288       C  
ATOM    525  O   ASN A 393     -42.343 -24.203-129.026  1.00215.56           O  
ANISOU  525  O   ASN A 393    35140  31432  15330  -2041  -3693  -1455       O  
ATOM    526  CB  ASN A 393     -45.364 -26.033-128.168  1.00178.43           C  
ANISOU  526  CB  ASN A 393    29191  27076  11528  -1452  -4861  -1092       C  
ATOM    527  CG  ASN A 393     -46.222 -24.934-128.775  1.00186.45           C  
ANISOU  527  CG  ASN A 393    30733  27618  12490  -1128  -5052  -1266       C  
ATOM    528  OD1 ASN A 393     -45.720 -23.911-129.240  1.00184.29           O  
ANISOU  528  OD1 ASN A 393    31112  26995  11913  -1148  -4822  -1419       O  
ATOM    529  ND2 ASN A 393     -47.534 -25.146-128.768  1.00186.84           N  
ANISOU  529  ND2 ASN A 393    30513  27649  12826   -836  -5505  -1262       N  
ATOM    530  N   SER A 394     -43.294 -25.907-130.144  1.00209.71           N  
ANISOU  530  N   SER A 394    34406  30406  14867  -1612  -4441  -1179       N  
ATOM    531  CA  SER A 394     -42.580 -25.590-131.376  1.00205.92           C  
ANISOU  531  CA  SER A 394    34729  29487  14024  -1642  -4274  -1262       C  
ATOM    532  C   SER A 394     -43.019 -24.261-131.978  1.00221.47           C  
ANISOU  532  C   SER A 394    37489  30910  15749  -1536  -4275  -1390       C  
ATOM    533  O   SER A 394     -42.242 -23.641-132.711  1.00232.03           O  
ANISOU  533  O   SER A 394    39521  31952  16688  -1731  -3960  -1496       O  
ATOM    534  CB  SER A 394     -42.772 -26.710-132.399  1.00187.82           C  
ANISOU  534  CB  SER A 394    32642  26939  11783  -1401  -4674  -1121       C  
ATOM    535  OG  SER A 394     -42.070 -26.424-133.596  1.00191.33           O  
ANISOU  535  OG  SER A 394    33872  26992  11833  -1449  -4479  -1216       O  
ATOM    536  N   ILE A 395     -44.239 -23.812-131.686  1.00228.05           N  
ANISOU  536  N   ILE A 395    38248  31607  16795  -1241  -4636  -1407       N  
ATOM    537  CA  ILE A 395     -44.719 -22.544-132.223  1.00222.80           C  
ANISOU  537  CA  ILE A 395    38372  30375  15905  -1067  -4745  -1561       C  
ATOM    538  C   ILE A 395     -44.093 -21.372-131.479  1.00197.95           C  
ANISOU  538  C   ILE A 395    35306  27366  12540  -1377  -4272  -1732       C  
ATOM    539  O   ILE A 395     -43.644 -20.398-132.092  1.00204.96           O  
ANISOU  539  O   ILE A 395    37048  27800  13026  -1518  -4089  -1840       O  
ATOM    540  CB  ILE A 395     -46.257 -22.492-132.167  1.00211.94           C  
ANISOU  540  CB  ILE A 395    36827  28840  14860   -583  -5347  -1594       C  
ATOM    541  CG1 ILE A 395     -46.859 -23.695-132.896  1.00195.21           C  
ANISOU  541  CG1 ILE A 395    34613  26588  12972   -318  -5833  -1419       C  
ATOM    542  CG2 ILE A 395     -46.775 -21.190-132.768  1.00189.62           C  
ANISOU  542  CG2 ILE A 395    34886  25363  11797   -321  -5567  -1794       C  
ATOM    543  CD1 ILE A 395     -46.454 -23.792-134.350  1.00189.75           C  
ANISOU  543  CD1 ILE A 395    34865  25284  11948   -250  -5929  -1371       C  
ATOM    544  N   GLY A 396     -44.054 -21.445-130.155  1.00187.32           N  
ANISOU  544  N   GLY A 396    33125  26623  11426  -1514  -4081  -1754       N  
ATOM    545  CA  GLY A 396     -43.468 -20.378-129.366  1.00216.13           C  
ANISOU  545  CA  GLY A 396    36799  30430  14892  -1799  -3657  -1919       C  
ATOM    546  C   GLY A 396     -43.873 -20.512-127.909  1.00190.86           C  
ANISOU  546  C   GLY A 396    32660  27850  12010  -1795  -3622  -1943       C  
ATOM    547  O   GLY A 396     -44.320 -21.569-127.470  1.00184.28           O  
ANISOU  547  O   GLY A 396    31122  27402  11494  -1710  -3813  -1801       O  
ATOM    548  N   ARG A 397     -43.702 -19.414-127.180  1.00183.39           N  
ANISOU  548  N   ARG A 397    31771  26972  10938  -1913  -3380  -2125       N  
ATOM    549  CA  ARG A 397     -44.036 -19.368-125.767  1.00193.14           C  
ANISOU  549  CA  ARG A 397    32197  28784  12403  -1927  -3296  -2187       C  
ATOM    550  C   ARG A 397     -45.506 -19.001-125.578  1.00197.97           C  
ANISOU  550  C   ARG A 397    32666  29321  13233  -1451  -3739  -2320       C  
ATOM    551  O   ARG A 397     -46.206 -18.612-126.516  1.00206.69           O  
ANISOU  551  O   ARG A 397    34367  29872  14295  -1095  -4124  -2399       O  
ATOM    552  CB  ARG A 397     -43.150 -18.365-125.024  1.00182.86           C  
ANISOU  552  CB  ARG A 397    30998  27616  10866  -2264  -2841  -2349       C  
ATOM    553  CG  ARG A 397     -41.731 -18.217-125.561  1.00204.09           C  
ANISOU  553  CG  ARG A 397    34150  30164  13231  -2713  -2418  -2340       C  
ATOM    554  CD  ARG A 397     -41.631 -17.128-126.629  1.00233.62           C  
ANISOU  554  CD  ARG A 397    38996  33180  16591  -2725  -2439  -2446       C  
ATOM    555  NE  ARG A 397     -42.419 -15.942-126.298  1.00239.97           N  
ANISOU  555  NE  ARG A 397    40139  33696  17343  -2462  -2660  -2634       N  
ATOM    556  CZ  ARG A 397     -43.572 -15.624-126.880  1.00238.59           C  
ANISOU  556  CZ  ARG A 397    40383  33053  17218  -1968  -3174  -2697       C  
ATOM    557  NH1 ARG A 397     -44.074 -16.402-127.829  1.00223.84           N  
ANISOU  557  NH1 ARG A 397    38654  30943  15451  -1716  -3506  -2560       N  
ATOM    558  NH2 ARG A 397     -44.222 -14.527-126.515  1.00230.88           N  
ANISOU  558  NH2 ARG A 397    39689  31844  16192  -1696  -3393  -2927       N  
ATOM    559  N   GLY A 398     -45.970 -19.128-124.339  1.00189.05           N  
ANISOU  559  N   GLY A 398    30728  28775  12326  -1445  -3687  -2376       N  
ATOM    560  CA  GLY A 398     -47.320 -18.760-123.988  1.00186.18           C  
ANISOU  560  CA  GLY A 398    30070  28494  12174  -1025  -4034  -2576       C  
ATOM    561  C   GLY A 398     -47.354 -17.829-122.794  1.00199.84           C  
ANISOU  561  C   GLY A 398    31515  30564  13850  -1052  -3799  -2821       C  
ATOM    562  O   GLY A 398     -46.320 -17.511-122.197  1.00202.17           O  
ANISOU  562  O   GLY A 398    31828  31031  13957  -1421  -3374  -2805       O  
ATOM    563  N   PRO A 399     -48.550 -17.368-122.423  1.00200.66           N  
ANISOU  563  N   PRO A 399    31334  30787  14122   -640  -4087  -3089       N  
ATOM    564  CA  PRO A 399     -48.661 -16.502-121.253  1.00191.78           C  
ANISOU  564  CA  PRO A 399    29901  30023  12944   -614  -3887  -3360       C  
ATOM    565  C   PRO A 399     -48.321 -17.267-119.987  1.00194.84           C  
ANISOU  565  C   PRO A 399    29407  31194  13428  -1017  -3508  -3205       C  
ATOM    566  O   PRO A 399     -48.442 -18.503-119.941  1.00190.04           O  
ANISOU  566  O   PRO A 399    28295  30904  13007  -1199  -3534  -2941       O  
ATOM    567  CB  PRO A 399     -50.139 -16.070-121.270  1.00200.06           C  
ANISOU  567  CB  PRO A 399    30739  31078  14198    -26  -4344  -3710       C  
ATOM    568  CG  PRO A 399     -50.834 -17.158-122.015  1.00218.90           C  
ANISOU  568  CG  PRO A 399    32881  33439  16851    101  -4684  -3536       C  
ATOM    569  CD  PRO A 399     -49.856 -17.623-123.055  1.00203.11           C  
ANISOU  569  CD  PRO A 399    31555  30935  14683   -161  -4623  -3198       C  
ATOM    570  N   PRO A 400     -47.871 -16.581-118.942  1.00209.61           N  
ANISOU  570  N   PRO A 400    31129  33358  15154  -1177  -3182  -3353       N  
ATOM    571  CA  PRO A 400     -47.541 -17.268-117.691  1.00187.45           C  
ANISOU  571  CA  PRO A 400    27553  31272  12399  -1557  -2846  -3215       C  
ATOM    572  C   PRO A 400     -48.790 -17.651-116.910  1.00189.48           C  
ANISOU  572  C   PRO A 400    26990  32126  12878  -1392  -2964  -3339       C  
ATOM    573  O   PRO A 400     -49.877 -17.102-117.099  1.00192.95           O  
ANISOU  573  O   PRO A 400    27379  32507  13425   -939  -3251  -3648       O  
ATOM    574  CB  PRO A 400     -46.711 -16.232-116.918  1.00187.77           C  
ANISOU  574  CB  PRO A 400    27810  31345  12188  -1724  -2508  -3388       C  
ATOM    575  CG  PRO A 400     -46.359 -15.166-117.922  1.00189.34           C  
ANISOU  575  CG  PRO A 400    28977  30786  12178  -1560  -2626  -3526       C  
ATOM    576  CD  PRO A 400     -47.480 -15.164-118.908  1.00208.17           C  
ANISOU  576  CD  PRO A 400    31595  32793  14707  -1075  -3109  -3621       C  
ATOM    577  N   SER A 401     -48.610 -18.619-116.016  1.00191.48           N  
ANISOU  577  N   SER A 401    26601  32971  13183  -1784  -2746  -3114       N  
ATOM    578  CA  SER A 401     -49.679 -19.047-115.131  1.00193.65           C  
ANISOU  578  CA  SER A 401    26066  33908  13605  -1783  -2757  -3205       C  
ATOM    579  C   SER A 401     -49.882 -18.020-114.020  1.00192.56           C  
ANISOU  579  C   SER A 401    25693  34142  13330  -1675  -2525  -3568       C  
ATOM    580  O   SER A 401     -49.155 -17.028-113.908  1.00192.35           O  
ANISOU  580  O   SER A 401    26143  33836  13103  -1623  -2380  -3715       O  
ATOM    581  CB  SER A 401     -49.369 -20.419-114.543  1.00197.79           C  
ANISOU  581  CB  SER A 401    26111  34878  14162  -2291  -2623  -2818       C  
ATOM    582  OG  SER A 401     -48.227 -20.369-113.705  1.00185.60           O  
ANISOU  582  OG  SER A 401    24609  33504  12407  -2651  -2276  -2712       O  
ATOM    583  N   GLU A 402     -50.886 -18.261-113.182  1.00196.03           N  
ANISOU  583  N   GLU A 402    25387  35234  13861  -1664  -2485  -3728       N  
ATOM    584  CA  GLU A 402     -51.075 -17.430-112.004  1.00201.48           C  
ANISOU  584  CA  GLU A 402    25770  36385  14399  -1599  -2229  -4070       C  
ATOM    585  C   GLU A 402     -49.934 -17.659-111.019  1.00195.34           C  
ANISOU  585  C   GLU A 402    24975  35853  13392  -2103  -1834  -3833       C  
ATOM    586  O   GLU A 402     -49.361 -18.749-110.937  1.00192.42           O  
ANISOU  586  O   GLU A 402    24513  35575  13023  -2543  -1759  -3426       O  
ATOM    587  CB  GLU A 402     -52.420 -17.728-111.342  1.00215.45           C  
ANISOU  587  CB  GLU A 402    26685  38878  16298  -1526  -2233  -4313       C  
ATOM    588  CG  GLU A 402     -52.528 -19.118-110.739  1.00217.73           C  
ANISOU  588  CG  GLU A 402    26390  39729  16610  -2110  -2066  -3935       C  
ATOM    589  CD  GLU A 402     -53.855 -19.351-110.044  1.00214.22           C  
ANISOU  589  CD  GLU A 402    25086  40060  16249  -2124  -2004  -4207       C  
ATOM    590  OE1 GLU A 402     -54.875 -18.794-110.503  1.00210.32           O  
ANISOU  590  OE1 GLU A 402    24400  39572  15941  -1615  -2253  -4633       O  
ATOM    591  OE2 GLU A 402     -53.877 -20.087-109.035  1.00214.89           O  
ANISOU  591  OE2 GLU A 402    24696  40756  16198  -2654  -1714  -4016       O  
ATOM    592  N   ALA A 403     -49.599 -16.611-110.273  1.00196.58           N  
ANISOU  592  N   ALA A 403    25253  36089  13351  -2008  -1628  -4113       N  
ATOM    593  CA  ALA A 403     -48.478 -16.676-109.348  1.00194.34           C  
ANISOU  593  CA  ALA A 403    25007  35987  12847  -2434  -1291  -3946       C  
ATOM    594  C   ALA A 403     -48.881 -17.369-108.052  1.00195.76           C  
ANISOU  594  C   ALA A 403    24471  36962  12946  -2772  -1052  -3884       C  
ATOM    595  O   ALA A 403     -50.022 -17.266-107.592  1.00199.64           O  
ANISOU  595  O   ALA A 403    24436  37942  13475  -2608  -1040  -4149       O  
ATOM    596  CB  ALA A 403     -47.942 -15.276-109.049  1.00195.39           C  
ANISOU  596  CB  ALA A 403    25589  35866  12783  -2227  -1185  -4265       C  
ATOM    597  N   VAL A 404     -47.925 -18.089-107.466  1.00193.04           N  
ANISOU  597  N   VAL A 404    24121  36752  12473  -3257   -872  -3552       N  
ATOM    598  CA  VAL A 404     -48.125 -18.803-106.212  1.00201.36           C  
ANISOU  598  CA  VAL A 404    24647  38483  13376  -3665   -656  -3430       C  
ATOM    599  C   VAL A 404     -47.113 -18.291-105.195  1.00193.64           C  
ANISOU  599  C   VAL A 404    23834  37604  12136  -3852   -394  -3483       C  
ATOM    600  O   VAL A 404     -46.030 -17.817-105.553  1.00191.08           O  
ANISOU  600  O   VAL A 404    24003  36813  11785  -3825   -397  -3468       O  
ATOM    601  CB  VAL A 404     -48.002 -20.334-106.396  1.00192.43           C  
ANISOU  601  CB  VAL A 404    23381  37416  12318  -4094   -782  -2956       C  
ATOM    602  CG1 VAL A 404     -48.556 -21.074-105.185  1.00195.19           C  
ANISOU  602  CG1 VAL A 404    23195  38475  12493  -4523   -605  -2850       C  
ATOM    603  CG2 VAL A 404     -48.715 -20.779-107.663  1.00192.24           C  
ANISOU  603  CG2 VAL A 404    23373  37092  12579  -3879  -1101  -2876       C  
ATOM    604  N   ARG A 405     -47.475 -18.388-103.919  1.00198.41           N  
ANISOU  604  N   ARG A 405    24019  38836  12532  -4067   -161  -3562       N  
ATOM    605  CA  ARG A 405     -46.661 -17.886-102.822  1.00199.36           C  
ANISOU  605  CA  ARG A 405    24251  39114  12382  -4225     75  -3650       C  
ATOM    606  C   ARG A 405     -45.861 -19.009-102.173  1.00194.53           C  
ANISOU  606  C   ARG A 405    23631  38653  11627  -4764    108  -3250       C  
ATOM    607  O   ARG A 405     -46.259 -20.177-102.198  1.00194.69           O  
ANISOU  607  O   ARG A 405    23427  38870  11679  -5064     12  -2946       O  
ATOM    608  CB  ARG A 405     -47.538 -17.203-101.772  1.00201.06           C  
ANISOU  608  CB  ARG A 405    24065  39923  12404  -4090    307  -4035       C  
ATOM    609  CG  ARG A 405     -48.052 -15.846-102.202  1.00218.10           C  
ANISOU  609  CG  ARG A 405    26353  41873  14642  -3488    237  -4523       C  
ATOM    610  CD  ARG A 405     -46.901 -14.870-102.326  1.00225.51           C  
ANISOU  610  CD  ARG A 405    27911  42268  15505  -3359    224  -4617       C  
ATOM    611  NE  ARG A 405     -47.319 -13.569-102.832  1.00232.11           N  
ANISOU  611  NE  ARG A 405    29028  42772  16391  -2795     79  -5053       N  
ATOM    612  CZ  ARG A 405     -46.561 -12.481-102.776  1.00228.17           C  
ANISOU  612  CZ  ARG A 405    29052  41870  15771  -2648     75  -5244       C  
ATOM    613  NH1 ARG A 405     -45.358 -12.550-102.224  1.00234.87           N  
ANISOU  613  NH1 ARG A 405    30115  42653  16471  -3025    235  -5059       N  
ATOM    614  NH2 ARG A 405     -47.006 -11.329-103.259  1.00213.00           N  
ANISOU  614  NH2 ARG A 405    27458  39600  13872  -2130   -122  -5636       N  
ATOM    615  N   ALA A 406     -44.725 -18.638-101.583  1.00197.97           N  
ANISOU  615  N   ALA A 406    14518  47967  12733  -7745    331  -2433       N  
ATOM    616  CA  ALA A 406     -43.857 -19.597-100.915  1.00206.73           C  
ANISOU  616  CA  ALA A 406    15696  48853  13998  -7789    486  -2709       C  
ATOM    617  C   ALA A 406     -42.927 -18.856 -99.965  1.00192.13           C  
ANISOU  617  C   ALA A 406    13899  46737  12364  -7443    476  -2578       C  
ATOM    618  O   ALA A 406     -42.471 -17.751-100.269  1.00191.58           O  
ANISOU  618  O   ALA A 406    13846  46646  12299  -7265    377  -2339       O  
ATOM    619  CB  ALA A 406     -43.040 -20.415-101.923  1.00226.27           C  
ANISOU  619  CB  ALA A 406    18235  51340  16395  -8098    563  -2950       C  
ATOM    620  N   ARG A 407     -42.655 -19.473 -98.818  1.00196.47           N  
ANISOU  620  N   ARG A 407    14475  47084  13091  -7358    576  -2738       N  
ATOM    621  CA  ARG A 407     -41.713 -18.948 -97.839  1.00195.42           C  
ANISOU  621  CA  ARG A 407    14434  46639  13180  -7039    560  -2655       C  
ATOM    622  C   ARG A 407     -40.720 -20.044 -97.483  1.00185.15           C  
ANISOU  622  C   ARG A 407    13264  45056  12029  -7121    643  -2955       C  
ATOM    623  O   ARG A 407     -41.120 -21.162 -97.140  1.00185.34           O  
ANISOU  623  O   ARG A 407    13323  45017  12079  -7273    714  -3199       O  
ATOM    624  CB  ARG A 407     -42.436 -18.439 -96.585  1.00207.56           C  
ANISOU  624  CB  ARG A 407    15984  48054  14825  -6743    515  -2501       C  
ATOM    625  CG  ARG A 407     -43.427 -19.425 -95.989  1.00225.60           C  
ANISOU  625  CG  ARG A 407    18275  50334  17110  -6848    568  -2688       C  
ATOM    626  CD  ARG A 407     -44.176 -18.828 -94.810  1.00226.23           C  
ANISOU  626  CD  ARG A 407    18359  50325  17273  -6561    517  -2519       C  
ATOM    627  NE  ARG A 407     -45.136 -19.774 -94.251  1.00218.64           N  
ANISOU  627  NE  ARG A 407    17401  49370  16304  -6669    568  -2701       N  
ATOM    628  CZ  ARG A 407     -46.358 -19.971 -94.737  1.00221.62           C  
ANISOU  628  CZ  ARG A 407    17658  50056  16493  -6853    563  -2697       C  
ATOM    629  NH1 ARG A 407     -46.771 -19.286 -95.795  1.00236.19           N  
ANISOU  629  NH1 ARG A 407    19373  52224  18144  -6945    501  -2513       N  
ATOM    630  NH2 ARG A 407     -47.167 -20.853 -94.166  1.00208.00           N  
ANISOU  630  NH2 ARG A 407    15945  48314  14773  -6948    614  -2875       N  
ATOM    631  N   THR A 408     -39.432 -19.726 -97.574  1.00183.35           N  
ANISOU  631  N   THR A 408    13102  44669  11894  -7026    633  -2938       N  
ATOM    632  CA  THR A 408     -38.399 -20.716 -97.321  1.00182.30           C  
ANISOU  632  CA  THR A 408    13083  44297  11884  -7110    704  -3214       C  
ATOM    633  C   THR A 408     -38.309 -21.043 -95.831  1.00205.43           C  
ANISOU  633  C   THR A 408    16114  46906  15033  -6880    709  -3276       C  
ATOM    634  O   THR A 408     -38.833 -20.326 -94.973  1.00177.88           O  
ANISOU  634  O   THR A 408    12620  43345  11620  -6616    653  -3078       O  
ATOM    635  CB  THR A 408     -37.046 -20.224 -97.832  1.00181.55           C  
ANISOU  635  CB  THR A 408    13024  44144  11811  -7065    686  -3164       C  
ATOM    636  OG1 THR A 408     -36.802 -18.900 -97.340  1.00179.48           O  
ANISOU  636  OG1 THR A 408    12760  43802  11634  -6731    597  -2859       O  
ATOM    637  CG2 THR A 408     -37.027 -20.207 -99.353  1.00191.87           C  
ANISOU  637  CG2 THR A 408    14317  45685  12901  -7331    688  -3177       C  
ATOM    638  N   GLY A 409     -37.628 -22.149 -95.534  1.00209.30           N  
ANISOU  638  N   GLY A 409    16699  47211  15614  -6993    781  -3560       N  
ATOM    639  CA  GLY A 409     -37.509 -22.637 -94.178  1.00206.90           C  
ANISOU  639  CA  GLY A 409    16492  46619  15500  -6824    792  -3659       C  
ATOM    640  C   GLY A 409     -36.546 -21.826 -93.335  1.00183.86           C  
ANISOU  640  C   GLY A 409    13648  43462  12749  -6485    726  -3491       C  
ATOM    641  O   GLY A 409     -35.922 -20.864 -93.783  1.00178.37           O  
ANISOU  641  O   GLY A 409    12932  42806  12035  -6373    675  -3298       O  
ATOM    642  N   GLU A 410     -36.422 -22.243 -92.078  1.00183.35           N  
ANISOU  642  N   GLU A 410    13672  43146  12847  -6330    729  -3571       N  
ATOM    643  CA  GLU A 410     -35.640 -21.522 -91.085  1.00173.94           C  
ANISOU  643  CA  GLU A 410    12556  41716  11819  -6000    667  -3414       C  
ATOM    644  C   GLU A 410     -34.237 -22.103 -90.949  1.00167.09           C  
ANISOU  644  C   GLU A 410    11782  40682  11021  -6018    714  -3589       C  
ATOM    645  O   GLU A 410     -33.994 -23.277 -91.236  1.00168.23           O  
ANISOU  645  O   GLU A 410    12046  40738  11136  -6217    835  -3855       O  
ATOM    646  CB  GLU A 410     -36.329 -21.554 -89.718  1.00175.40           C  
ANISOU  646  CB  GLU A 410    12782  41731  12130  -5803    638  -3377       C  
ATOM    647  CG  GLU A 410     -37.685 -20.870 -89.663  1.00203.79           C  
ANISOU  647  CG  GLU A 410    16286  45472  15673  -5735    602  -3178       C  
ATOM    648  CD  GLU A 410     -38.829 -21.795 -90.026  1.00235.04           C  
ANISOU  648  CD  GLU A 410    20183  49603  19519  -6001    664  -3358       C  
ATOM    649  OE1 GLU A 410     -38.616 -22.733 -90.824  1.00245.96           O  
ANISOU  649  OE1 GLU A 410    21561  51078  20813  -6292    731  -3593       O  
ATOM    650  OE2 GLU A 410     -39.944 -21.587 -89.505  1.00237.95           O  
ANISOU  650  OE2 GLU A 410    20512  50017  19880  -5925    657  -3268       O  
ATOM    651  N   GLN A 411     -33.315 -21.253 -90.503  1.00164.94           N  
ANISOU  651  N   GLN A 411    11556  40266  10846  -5761    656  -3412       N  
ATOM    652  CA  GLN A 411     -31.972 -21.635 -90.092  1.00164.19           C  
ANISOU  652  CA  GLN A 411    11670  39862  10853  -5645    731  -3501       C  
ATOM    653  C   GLN A 411     -31.658 -20.941 -88.772  1.00160.47           C  
ANISOU  653  C   GLN A 411    11221  39210  10540  -5323    650  -3329       C  
ATOM    654  O   GLN A 411     -32.468 -20.178 -88.238  1.00159.71           O  
ANISOU  654  O   GLN A 411    11035  39173  10473  -5181    552  -3144       O  
ATOM    655  CB  GLN A 411     -30.928 -21.266 -91.155  1.00164.19           C  
ANISOU  655  CB  GLN A 411    11727  39874  10783  -5687    760  -3458       C  
ATOM    656  CG  GLN A 411     -31.010 -22.072 -92.437  1.00170.98           C  
ANISOU  656  CG  GLN A 411    12628  40845  11490  -6002    867  -3655       C  
ATOM    657  CD  GLN A 411     -29.942 -21.682 -93.442  1.00180.13           C  
ANISOU  657  CD  GLN A 411    13860  42002  12580  -6031    896  -3611       C  
ATOM    658  OE1 GLN A 411     -29.219 -20.703 -93.252  1.00166.23           O  
ANISOU  658  OE1 GLN A 411    12086  40197  10876  -5825    821  -3412       O  
ATOM    659  NE2 GLN A 411     -29.835 -22.451 -94.519  1.00183.37           N  
ANISOU  659  NE2 GLN A 411    14352  42457  12865  -6294   1010  -3799       N  
ATOM    660  N   ALA A 412     -30.472 -21.212 -88.238  1.00163.67           N  
ANISOU  660  N   ALA A 412    11840  39280  11065  -5164    744  -3365       N  
ATOM    661  CA  ALA A 412     -30.014 -20.470 -87.079  1.00170.78           C  
ANISOU  661  CA  ALA A 412    12774  40008  12106  -4863    672  -3187       C  
ATOM    662  C   ALA A 412     -29.686 -19.035 -87.488  1.00168.58           C  
ANISOU  662  C   ALA A 412    12352  39911  11790  -4756    526  -2927       C  
ATOM    663  O   ALA A 412     -29.302 -18.782 -88.634  1.00172.79           O  
ANISOU  663  O   ALA A 412    12847  40582  12223  -4880    535  -2909       O  
ATOM    664  CB  ALA A 412     -28.788 -21.134 -86.460  1.00159.80           C  
ANISOU  664  CB  ALA A 412    11628  38222  10868  -4729    837  -3276       C  
ATOM    665  N   PRO A 413     -29.860 -18.073 -86.583  1.00155.22           N  
ANISOU  665  N   PRO A 413    10637  38153  10188  -4510    426  -2709       N  
ATOM    666  CA  PRO A 413     -29.521 -16.687 -86.918  1.00153.37           C  
ANISOU  666  CA  PRO A 413    10381  37933   9959  -4356    360  -2434       C  
ATOM    667  C   PRO A 413     -28.052 -16.548 -87.284  1.00152.89           C  
ANISOU  667  C   PRO A 413    10351  37836   9905  -4342    372  -2445       C  
ATOM    668  O   PRO A 413     -27.192 -17.286 -86.798  1.00152.02           O  
ANISOU  668  O   PRO A 413    10400  37493   9870  -4299    463  -2579       O  
ATOM    669  CB  PRO A 413     -29.858 -15.917 -85.636  1.00157.96           C  
ANISOU  669  CB  PRO A 413    11021  38327  10670  -4076    300  -2242       C  
ATOM    670  CG  PRO A 413     -30.889 -16.756 -84.959  1.00156.56           C  
ANISOU  670  CG  PRO A 413    10853  38126  10505  -4125    321  -2381       C  
ATOM    671  CD  PRO A 413     -30.519 -18.179 -85.270  1.00163.26           C  
ANISOU  671  CD  PRO A 413    11708  39016  11308  -4354    406  -2689       C  
ATOM    672  N   SER A 414     -27.773 -15.592 -88.168  1.00162.01           N  
ANISOU  672  N   SER A 414    11455  39102  10999  -4340    340  -2275       N  
ATOM    673  CA  SER A 414     -26.424 -15.344 -88.649  1.00153.38           C  
ANISOU  673  CA  SER A 414    10378  38004   9896  -4338    347  -2267       C  
ATOM    674  C   SER A 414     -25.891 -13.979 -88.241  1.00151.74           C  
ANISOU  674  C   SER A 414    10202  37682   9772  -4088    282  -1991       C  
ATOM    675  O   SER A 414     -24.737 -13.663 -88.554  1.00151.42           O  
ANISOU  675  O   SER A 414    10177  37625   9731  -4063    282  -1961       O  
ATOM    676  CB  SER A 414     -26.374 -15.480 -90.176  1.00155.88           C  
ANISOU  676  CB  SER A 414    10654  38517  10055  -4577    391  -2329       C  
ATOM    677  OG  SER A 414     -26.948 -16.706 -90.597  1.00157.60           O  
ANISOU  677  OG  SER A 414    10916  38769  10197  -4801    480  -2571       O  
ATOM    678  N   SER A 415     -26.690 -13.164 -87.563  1.00150.80           N  
ANISOU  678  N   SER A 415    10089  37488   9720  -3911    235  -1796       N  
ATOM    679  CA  SER A 415     -26.281 -11.851 -87.095  1.00149.28           C  
ANISOU  679  CA  SER A 415     9929  37178   9613  -3680    188  -1539       C  
ATOM    680  C   SER A 415     -26.778 -11.660 -85.671  1.00154.51           C  
ANISOU  680  C   SER A 415    10661  37639  10408  -3474    164  -1465       C  
ATOM    681  O   SER A 415     -27.781 -12.267 -85.274  1.00147.66           O  
ANISOU  681  O   SER A 415     9784  36779   9540  -3514    175  -1554       O  
ATOM    682  CB  SER A 415     -26.827 -10.732 -87.998  1.00150.57           C  
ANISOU  682  CB  SER A 415    10005  37520   9687  -3693    173  -1326       C  
ATOM    683  OG  SER A 415     -28.241 -10.762 -88.051  1.00151.61           O  
ANISOU  683  OG  SER A 415    10078  37769   9760  -3738    183  -1296       O  
ATOM    684  N   PRO A 416     -26.096 -10.841 -84.877  1.00145.52           N  
ANISOU  684  N   PRO A 416     9591  36320   9378  -3263    133  -1309       N  
ATOM    685  CA  PRO A 416     -26.526 -10.621 -83.497  1.00143.74           C  
ANISOU  685  CA  PRO A 416     9437  35903   9274  -3072    111  -1237       C  
ATOM    686  C   PRO A 416     -27.632  -9.584 -83.433  1.00147.17           C  
ANISOU  686  C   PRO A 416     9825  36390   9702  -2981    131  -1025       C  
ATOM    687  O   PRO A 416     -27.895  -8.887 -84.424  1.00148.29           O  
ANISOU  687  O   PRO A 416     9900  36713   9732  -3039    140   -904       O  
ATOM    688  CB  PRO A 416     -25.249 -10.114 -82.816  1.00141.92           C  
ANISOU  688  CB  PRO A 416     9296  35489   9137  -2908     87  -1154       C  
ATOM    689  CG  PRO A 416     -24.544  -9.381 -83.901  1.00142.79           C  
ANISOU  689  CG  PRO A 416     9354  35713   9187  -2957     90  -1052       C  
ATOM    690  CD  PRO A 416     -24.825 -10.153 -85.170  1.00144.98           C  
ANISOU  690  CD  PRO A 416     9546  36215   9325  -3201    120  -1211       C  
ATOM    691  N   PRO A 417     -28.317  -9.465 -82.294  1.00142.80           N  
ANISOU  691  N   PRO A 417     9324  35710   9225  -2843    145   -975       N  
ATOM    692  CA  PRO A 417     -29.245  -8.345 -82.110  1.00142.87           C  
ANISOU  692  CA  PRO A 417     9345  35775   9164  -2725    155   -757       C  
ATOM    693  C   PRO A 417     -28.535  -7.011 -82.288  1.00142.34           C  
ANISOU  693  C   PRO A 417     9289  35686   9107  -2606    124   -538       C  
ATOM    694  O   PRO A 417     -27.327  -6.889 -82.073  1.00141.24           O  
ANISOU  694  O   PRO A 417     9201  35411   9053  -2552    121   -537       O  
ATOM    695  CB  PRO A 417     -29.745  -8.530 -80.673  1.00145.65           C  
ANISOU  695  CB  PRO A 417     9798  35951   9590  -2583    164   -770       C  
ATOM    696  CG  PRO A 417     -29.617  -9.995 -80.429  1.00156.13           C  
ANISOU  696  CG  PRO A 417    11123  37215  10983  -2698    196  -1025       C  
ATOM    697  CD  PRO A 417     -28.394 -10.435 -81.187  1.00141.65           C  
ANISOU  697  CD  PRO A 417     9242  35404   9173  -2813     89  -1140       C  
ATOM    698  N   ARG A 418     -29.300  -6.005 -82.696  1.00143.24           N  
ANISOU  698  N   ARG A 418     9342  35947   9135  -2571     95   -348       N  
ATOM    699  CA  ARG A 418     -28.755  -4.703 -83.048  1.00143.15           C  
ANISOU  699  CA  ARG A 418     9315  35957   9117  -2486     64   -135       C  
ATOM    700  C   ARG A 418     -29.070  -3.666 -81.976  1.00141.80           C  
ANISOU  700  C   ARG A 418     9197  35663   9016  -2278     40     52       C  
ATOM    701  O   ARG A 418     -30.088  -3.751 -81.283  1.00141.61           O  
ANISOU  701  O   ARG A 418     9178  35632   8996  -2219     36     61       O  
ATOM    702  CB  ARG A 418     -29.307  -4.223 -84.393  1.00186.50           C  
ANISOU  702  CB  ARG A 418    14677  41727  14456  -2604     44    -37       C  
ATOM    703  CG  ARG A 418     -28.919  -5.085 -85.581  1.00165.48           C  
ANISOU  703  CG  ARG A 418    11954  39212  11710  -2824     63   -202       C  
ATOM    704  CD  ARG A 418     -29.340  -4.416 -86.877  1.00153.24           C  
ANISOU  704  CD  ARG A 418    10280  37936  10006  -2926     38    -69       C  
ATOM    705  NE  ARG A 418     -28.840  -3.047 -86.953  1.00177.98           N  
ANISOU  705  NE  ARG A 418    13413  41055  13156  -2798      6    164       N  
ATOM    706  CZ  ARG A 418     -29.103  -2.207 -87.949  1.00198.84           C  
ANISOU  706  CZ  ARG A 418    15954  43916  15682  -2844    -23    330       C  
ATOM    707  NH1 ARG A 418     -29.865  -2.593 -88.963  1.00205.84           N  
ANISOU  707  NH1 ARG A 418    16730  45060  16420  -3018    -26    292       N  
ATOM    708  NH2 ARG A 418     -28.603  -0.979 -87.929  1.00199.58           N  
ANISOU  708  NH2 ARG A 418    16052  43977  15802  -2723    -49    535       N  
ATOM    709  N   ARG A 419     -28.179  -2.681 -81.865  1.00140.95           N  
ANISOU  709  N   ARG A 419     9124  35470   8962  -2175     24    198       N  
ATOM    710  CA  ARG A 419     -28.337  -1.525 -80.981  1.00169.89           C  
ANISOU  710  CA  ARG A 419    12827  39033  12689  -1990      0    395       C  
ATOM    711  C   ARG A 419     -28.704  -1.952 -79.560  1.00175.41           C  
ANISOU  711  C   ARG A 419    13617  39548  13483  -1883      9    328       C  
ATOM    712  O   ARG A 419     -29.726  -1.551 -78.998  1.00169.73           O  
ANISOU  712  O   ARG A 419    12881  38852  12758  -1799     -5    416       O  
ATOM    713  CB  ARG A 419     -29.366  -0.543 -81.549  1.00158.35           C  
ANISOU  713  CB  ARG A 419    11259  37777  11129  -1970    -30    593       C  
ATOM    714  CG  ARG A 419     -28.986   0.021 -82.910  1.00142.89           C  
ANISOU  714  CG  ARG A 419     9211  36008   9074  -2064    -44    689       C  
ATOM    715  CD  ARG A 419     -27.543   0.510 -82.924  1.00187.85           C  
ANISOU  715  CD  ARG A 419    14965  41573  14837  -2027    -43    727       C  
ATOM    716  NE  ARG A 419     -27.352   1.728 -82.140  1.00208.34           N  
ANISOU  716  NE  ARG A 419    17602  44052  17506  -1854    -61    920       N  
ATOM    717  CZ  ARG A 419     -27.241   2.943 -82.666  1.00219.81           C  
ANISOU  717  CZ  ARG A 419    19037  45538  18943  -1806   -117   1121       C  
ATOM    718  NH1 ARG A 419     -27.067   3.996 -81.880  1.00203.12           N  
ANISOU  718  NH1 ARG A 419    16998  43252  16926  -1646   -157   1277       N  
ATOM    719  NH2 ARG A 419     -27.299   3.105 -83.982  1.00229.59           N  
ANISOU  719  NH2 ARG A 419    20200  46958  20077  -1919   -147   1163       N  
ATOM    720  N   VAL A 420     -27.841  -2.786 -78.983  1.00137.04           N  
ANISOU  720  N   VAL A 420     8848  34514   8708  -1888     33    171       N  
ATOM    721  CA  VAL A 420     -28.031  -3.229 -77.608  1.00135.53           C  
ANISOU  721  CA  VAL A 420     8748  34140   8606  -1790     40    102       C  
ATOM    722  C   VAL A 420     -27.703  -2.082 -76.664  1.00134.43           C  
ANISOU  722  C   VAL A 420     8667  33861   8550  -1617     19    280       C  
ATOM    723  O   VAL A 420     -26.687  -1.393 -76.825  1.00133.73           O  
ANISOU  723  O   VAL A 420     8598  33720   8494  -1583     14    371       O  
ATOM    724  CB  VAL A 420     -27.165  -4.463 -77.315  1.00134.76           C  
ANISOU  724  CB  VAL A 420     8725  33916   8561  -1849     69   -108       C  
ATOM    725  CG1 VAL A 420     -27.378  -4.937 -75.884  1.00140.46           C  
ANISOU  725  CG1 VAL A 420     9542  34463   9361  -1752     67   -175       C  
ATOM    726  CG2 VAL A 420     -27.478  -5.575 -78.304  1.00136.27           C  
ANISOU  726  CG2 VAL A 420     8851  34256   8670  -2035     95   -288       C  
ATOM    727  N   GLN A 421     -28.570  -1.864 -75.678  1.00133.58           N  
ANISOU  727  N   GLN A 421     8580  33701   8474  -1516      9    327       N  
ATOM    728  CA  GLN A 421     -28.380  -0.805 -74.701  1.00138.65           C  
ANISOU  728  CA  GLN A 421     9271  34217   9194  -1358     -7    487       C  
ATOM    729  C   GLN A 421     -28.881  -1.273 -73.345  1.00152.03           C  
ANISOU  729  C   GLN A 421    11031  35777  10955  -1279     -5    417       C  
ATOM    730  O   GLN A 421     -29.742  -2.152 -73.251  1.00131.67           O  
ANISOU  730  O   GLN A 421     8434  33250   8344  -1333      2    294       O  
ATOM    731  CB  GLN A 421     -29.106   0.482 -75.108  1.00149.63           C  
ANISOU  731  CB  GLN A 421    10578  35748  10527  -1298    -30    706       C  
ATOM    732  CG  GLN A 421     -28.180   1.601 -75.542  1.00136.00           C  
ANISOU  732  CG  GLN A 421     8846  34018   8811  -1263    -40    864       C  
ATOM    733  CD  GLN A 421     -28.919   2.898 -75.799  1.00165.36           C  
ANISOU  733  CD  GLN A 421    12523  37772  12535  -1178   -109   1083       C  
ATOM    734  OE1 GLN A 421     -28.459   3.973 -75.413  1.00149.71           O  
ANISOU  734  OE1 GLN A 421    10587  35669  10628  -1075   -145   1230       O  
ATOM    735  NE2 GLN A 421     -30.071   2.805 -76.457  1.00151.39           N  
ANISOU  735  NE2 GLN A 421    10672  36157  10693  -1220   -138   1106       N  
ATOM    736  N   ALA A 422     -28.335  -0.672 -72.291  1.00155.65           N  
ANISOU  736  N   ALA A 422    11563  36072  11504  -1158    -10    497       N  
ATOM    737  CA  ALA A 422     -28.711  -1.043 -70.937  1.00128.69           C  
ANISOU  737  CA  ALA A 422     8212  32527   8159  -1079    -10    441       C  
ATOM    738  C   ALA A 422     -28.499   0.139 -70.003  1.00149.23           C  
ANISOU  738  C   ALA A 422    10850  35025  10827   -938    -22    610       C  
ATOM    739  O   ALA A 422     -27.665   1.011 -70.258  1.00127.59           O  
ANISOU  739  O   ALA A 422     8115  32262   8102   -911    -26    727       O  
ATOM    740  CB  ALA A 422     -27.916  -2.259 -70.447  1.00127.74           C  
ANISOU  740  CB  ALA A 422     8171  32275   8092  -1123      4    252       C  
ATOM    741  N   ARG A 423     -29.274   0.157 -68.919  1.00130.84           N  
ANISOU  741  N   ARG A 423     8547  32609   8558   -854    -38    615       N  
ATOM    742  CA  ARG A 423     -29.132   1.158 -67.872  1.00126.31           C  
ANISOU  742  CA  ARG A 423     8024  31867   8100   -722    -71    747       C  
ATOM    743  C   ARG A 423     -29.674   0.581 -66.574  1.00125.45           C  
ANISOU  743  C   ARG A 423     7959  31639   8066   -669    -71    661       C  
ATOM    744  O   ARG A 423     -30.431  -0.392 -66.576  1.00132.18           O  
ANISOU  744  O   ARG A 423     8789  32548   8887   -722    -59    530       O  
ATOM    745  CB  ARG A 423     -29.860   2.462 -68.221  1.00127.26           C  
ANISOU  745  CB  ARG A 423     8089  32025   8237   -648   -122    944       C  
ATOM    746  CG  ARG A 423     -31.375   2.358 -68.174  1.00140.86           C  
ANISOU  746  CG  ARG A 423     9748  33818   9956   -624   -146    954       C  
ATOM    747  CD  ARG A 423     -32.028   3.701 -68.458  1.00177.30           C  
ANISOU  747  CD  ARG A 423    14307  38466  14593   -532   -201   1166       C  
ATOM    748  NE  ARG A 423     -33.478   3.652 -68.289  1.00156.01           N  
ANISOU  748  NE  ARG A 423    11542  35825  11912   -492   -227   1188       N  
ATOM    749  CZ  ARG A 423     -34.336   3.379 -69.266  1.00149.05           C  
ANISOU  749  CZ  ARG A 423    10567  35117  10948   -559   -242   1185       C  
ATOM    750  NH1 ARG A 423     -33.894   3.131 -70.491  1.00144.07           N  
ANISOU  750  NH1 ARG A 423     9904  34626  10211   -673   -231   1159       N  
ATOM    751  NH2 ARG A 423     -35.638   3.356 -69.019  1.00191.28           N  
ANISOU  751  NH2 ARG A 423    15847  40505  16324   -517   -267   1209       N  
ATOM    752  N   MET A 424     -29.278   1.194 -65.462  1.00155.17           N  
ANISOU  752  N   MET A 424    11786  35242  11932   -570    -85    732       N  
ATOM    753  CA  MET A 424     -29.745   0.767 -64.148  1.00123.58           C  
ANISOU  753  CA  MET A 424     7822  31118   8014   -513    -84    667       C  
ATOM    754  C   MET A 424     -31.091   1.417 -63.855  1.00124.25           C  
ANISOU  754  C   MET A 424     7852  31215   8143   -433   -113    764       C  
ATOM    755  O   MET A 424     -31.215   2.645 -63.898  1.00124.60           O  
ANISOU  755  O   MET A 424     7877  31250   8214   -355   -145    934       O  
ATOM    756  CB  MET A 424     -28.729   1.131 -63.068  1.00122.28           C  
ANISOU  756  CB  MET A 424     7738  30790   7933   -451    -85    701       C  
ATOM    757  CG  MET A 424     -27.373   0.459 -63.225  1.00121.63           C  
ANISOU  757  CG  MET A 424     7705  30685   7825   -518    -59    611       C  
ATOM    758  SD  MET A 424     -27.436  -1.337 -63.065  1.00121.40           S  
ANISOU  758  SD  MET A 424     7692  30665   7771   -599    -30    379       S  
ATOM    759  CE  MET A 424     -28.267  -1.514 -61.489  1.00120.70           C  
ANISOU  759  CE  MET A 424     7627  30430   7803   -515    -33    352       C  
ATOM    760  N   LEU A 425     -32.102   0.597 -63.574  1.00133.50           N  
ANISOU  760  N   LEU A 425     8990  32407   9325   -453   -102    657       N  
ATOM    761  CA  LEU A 425     -33.403   1.140 -63.201  1.00142.76           C  
ANISOU  761  CA  LEU A 425    10102  33585  10556   -373   -123    741       C  
ATOM    762  C   LEU A 425     -33.465   1.425 -61.708  1.00124.22           C  
ANISOU  762  C   LEU A 425     7798  31068   8331   -272   -113    761       C  
ATOM    763  O   LEU A 425     -34.084   2.406 -61.280  1.00143.13           O  
ANISOU  763  O   LEU A 425    10159  33435  10789   -168   -130    897       O  
ATOM    764  CB  LEU A 425     -34.518   0.179 -63.610  1.00140.66           C  
ANISOU  764  CB  LEU A 425     9767  33425  10254   -448   -113    623       C  
ATOM    765  CG  LEU A 425     -34.769  -0.020 -65.103  1.00127.57           C  
ANISOU  765  CG  LEU A 425     8039  31966   8467   -550   -125    616       C  
ATOM    766  CD1 LEU A 425     -35.879  -1.037 -65.325  1.00128.49           C  
ANISOU  766  CD1 LEU A 425     8089  32178   8554   -633   -114    483       C  
ATOM    767  CD2 LEU A 425     -35.117   1.302 -65.763  1.00128.62           C  
ANISOU  767  CD2 LEU A 425     8110  32176   8585   -483   -169    827       C  
ATOM    768  N   SER A 426     -32.825   0.582 -60.908  1.00138.77           N  
ANISOU  768  N   SER A 426     9711  32804  10211   -299    -80    631       N  
ATOM    769  CA  SER A 426     -32.793   0.754 -59.464  1.00122.13           C  
ANISOU  769  CA  SER A 426     7647  30540   8216   -217    -58    637       C  
ATOM    770  C   SER A 426     -31.393   0.379 -58.991  1.00120.93           C  
ANISOU  770  C   SER A 426     7584  30296   8068   -244    -47    579       C  
ATOM    771  O   SER A 426     -30.434   0.339 -59.771  1.00133.36           O  
ANISOU  771  O   SER A 426     9182  31919   9569   -300    -61    579       O  
ATOM    772  CB  SER A 426     -33.900  -0.078 -58.798  1.00136.14           C  
ANISOU  772  CB  SER A 426     9391  32273  10063   -219    -14    524       C  
ATOM    773  OG  SER A 426     -33.633  -1.467 -58.913  1.00138.20           O  
ANISOU  773  OG  SER A 426     9680  32528  10303   -319     17    340       O  
ATOM    774  N   ALA A 427     -31.265   0.100 -57.694  1.00142.62           N  
ANISOU  774  N   ALA A 427    10376  32908  10905   -205    -13    533       N  
ATOM    775  CA  ALA A 427     -29.987  -0.328 -57.147  1.00119.02           C  
ANISOU  775  CA  ALA A 427     7463  29832   7929   -227     -2    480       C  
ATOM    776  C   ALA A 427     -29.637  -1.751 -57.553  1.00118.93           C  
ANISOU  776  C   ALA A 427     7467  29832   7890   -321     24    310       C  
ATOM    777  O   ALA A 427     -28.469  -2.140 -57.454  1.00118.33           O  
ANISOU  777  O   ALA A 427     7438  29713   7807   -349     26    274       O  
ATOM    778  CB  ALA A 427     -30.011  -0.209 -55.624  1.00166.58           C  
ANISOU  778  CB  ALA A 427    13526  35716  14053   -161     40    486       C  
ATOM    779  N   SER A 428     -30.618  -2.532 -58.016  1.00136.86           N  
ANISOU  779  N   SER A 428     9691  32161  10150   -372     45    208       N  
ATOM    780  CA  SER A 428     -30.379  -3.934 -58.333  1.00122.23           C  
ANISOU  780  CA  SER A 428     7848  30308   8286   -464     78     35       C  
ATOM    781  C   SER A 428     -31.113  -4.397 -59.585  1.00129.80           C  
ANISOU  781  C   SER A 428     8738  31425   9156   -553     66    -33       C  
ATOM    782  O   SER A 428     -31.103  -5.600 -59.876  1.00121.82           O  
ANISOU  782  O   SER A 428     7723  30421   8140   -640     98   -190       O  
ATOM    783  CB  SER A 428     -30.778  -4.822 -57.148  1.00132.82           C  
ANISOU  783  CB  SER A 428     9224  31499   9742   -451    153    -75       C  
ATOM    784  OG  SER A 428     -32.163  -4.699 -56.866  1.00119.71           O  
ANISOU  784  OG  SER A 428     7518  29843   8122   -426    177    -74       O  
ATOM    785  N   THR A 429     -31.748  -3.497 -60.331  1.00147.74           N  
ANISOU  785  N   THR A 429    10952  33822  11359   -538     26     80       N  
ATOM    786  CA  THR A 429     -32.497  -3.851 -61.530  1.00122.92           C  
ANISOU  786  CA  THR A 429     7734  30850   8118   -626     15     32       C  
ATOM    787  C   THR A 429     -31.974  -3.045 -62.709  1.00123.48           C  
ANISOU  787  C   THR A 429     7787  31057   8075   -645    -19    145       C  
ATOM    788  O   THR A 429     -31.871  -1.817 -62.630  1.00123.42           O  
ANISOU  788  O   THR A 429     7780  31033   8083   -561    -43    314       O  
ATOM    789  CB  THR A 429     -33.996  -3.596 -61.343  1.00126.50           C  
ANISOU  789  CB  THR A 429     8117  31338   8610   -593     16     66       C  
ATOM    790  OG1 THR A 429     -34.494  -4.417 -60.279  1.00147.08           O  
ANISOU  790  OG1 THR A 429    10740  33815  11328   -587     69    -51       O  
ATOM    791  CG2 THR A 429     -34.754  -3.916 -62.622  1.00167.51           C  
ANISOU  791  CG2 THR A 429    13226  36730  13691   -691      0     27       C  
ATOM    792  N   MET A 430     -31.644  -3.738 -63.797  1.00143.21           N  
ANISOU  792  N   MET A 430    10267  33683  10465   -759    -13     51       N  
ATOM    793  CA  MET A 430     -31.190  -3.103 -65.025  1.00124.83           C  
ANISOU  793  CA  MET A 430     7910  31495   8023   -797    -24    142       C  
ATOM    794  C   MET A 430     -32.187  -3.371 -66.144  1.00126.39           C  
ANISOU  794  C   MET A 430     8017  31889   8116   -888    -26    110       C  
ATOM    795  O   MET A 430     -32.797  -4.444 -66.204  1.00126.85           O  
ANISOU  795  O   MET A 430     8049  31995   8154   -971    -13    -46       O  
ATOM    796  CB  MET A 430     -29.797  -3.601 -65.437  1.00124.36           C  
ANISOU  796  CB  MET A 430     7899  31438   7913   -859     -8     69       C  
ATOM    797  CG  MET A 430     -29.731  -5.073 -65.822  1.00124.70           C  
ANISOU  797  CG  MET A 430     7935  31536   7909   -981      6   -141       C  
ATOM    798  SD  MET A 430     -28.116  -5.536 -66.480  1.00129.88           S  
ANISOU  798  SD  MET A 430     8628  32153   8568  -1047      9   -206       S  
ATOM    799  CE  MET A 430     -28.284  -7.316 -66.596  1.00124.85           C  
ANISOU  799  CE  MET A 430     7968  31556   7915  -1172     22   -463       C  
ATOM    800  N   LEU A 431     -32.354  -2.386 -67.020  1.00148.80           N  
ANISOU  800  N   LEU A 431    10800  34837  10898   -876    -43    260       N  
ATOM    801  CA  LEU A 431     -33.189  -2.520 -68.205  1.00128.96           C  
ANISOU  801  CA  LEU A 431     8191  32529   8277   -967    -47    256       C  
ATOM    802  C   LEU A 431     -32.300  -2.736 -69.420  1.00129.48           C  
ANISOU  802  C   LEU A 431     8245  32731   8223  -1077    -18    221       C  
ATOM    803  O   LEU A 431     -31.337  -1.993 -69.627  1.00142.85           O  
ANISOU  803  O   LEU A 431     9965  34386   9928  -1039    -15    325       O  
ATOM    804  CB  LEU A 431     -34.060  -1.281 -68.414  1.00131.36           C  
ANISOU  804  CB  LEU A 431     8427  32874   8610   -879    -93    457       C  
ATOM    805  CG  LEU A 431     -34.868  -1.271 -69.713  1.00143.32           C  
ANISOU  805  CG  LEU A 431     9831  34609  10013   -969   -109    486       C  
ATOM    806  CD1 LEU A 431     -35.940  -2.348 -69.689  1.00143.25           C  
ANISOU  806  CD1 LEU A 431     9772  34685   9972  -1055   -100    334       C  
ATOM    807  CD2 LEU A 431     -35.481   0.096 -69.967  1.00132.68           C  
ANISOU  807  CD2 LEU A 431     8423  33290   8701   -865   -166    715       C  
ATOM    808  N   VAL A 432     -32.625  -3.748 -70.217  1.00130.50           N  
ANISOU  808  N   VAL A 432     8329  32991   8264  -1217     -2     71       N  
ATOM    809  CA  VAL A 432     -31.888  -4.064 -71.433  1.00137.91           C  
ANISOU  809  CA  VAL A 432     9249  33996   9154  -1335      8     17       C  
ATOM    810  C   VAL A 432     -32.832  -3.912 -72.616  1.00149.98           C  
ANISOU  810  C   VAL A 432    10661  35764  10562  -1426      5     58       C  
ATOM    811  O   VAL A 432     -34.008  -4.284 -72.532  1.00133.98           O  
ANISOU  811  O   VAL A 432     8577  33845   8484  -1458      3     15       O  
ATOM    812  CB  VAL A 432     -31.293  -5.487 -71.384  1.00131.64           C  
ANISOU  812  CB  VAL A 432     8507  33128   8381  -1438     24   -213       C  
ATOM    813  CG1 VAL A 432     -30.279  -5.680 -72.503  1.00131.41           C  
ANISOU  813  CG1 VAL A 432     8473  33138   8317  -1537     35   -254       C  
ATOM    814  CG2 VAL A 432     -30.663  -5.749 -70.026  1.00129.12           C  
ANISOU  814  CG2 VAL A 432     8285  32602   8173  -1343     20   -256       C  
ATOM    815  N   GLN A 433     -32.320  -3.355 -73.712  1.00133.97           N  
ANISOU  815  N   GLN A 433     8589  33829   8486  -1471      4    145       N  
ATOM    816  CA  GLN A 433     -33.101  -3.164 -74.925  1.00135.94           C  
ANISOU  816  CA  GLN A 433     8718  34323   8612  -1565     -2    199       C  
ATOM    817  C   GLN A 433     -32.213  -3.415 -76.135  1.00143.05           C  
ANISOU  817  C   GLN A 433     9597  35288   9467  -1692     10    146       C  
ATOM    818  O   GLN A 433     -30.988  -3.286 -76.070  1.00138.36           O  
ANISOU  818  O   GLN A 433     9069  34562   8938  -1668     17    143       O  
ATOM    819  CB  GLN A 433     -33.707  -1.757 -74.997  1.00136.53           C  
ANISOU  819  CB  GLN A 433     8731  34468   8677  -1451    -42    446       C  
ATOM    820  CG  GLN A 433     -32.684  -0.636 -74.940  1.00137.78           C  
ANISOU  820  CG  GLN A 433     8934  34512   8903  -1351    -59    606       C  
ATOM    821  CD  GLN A 433     -33.275   0.708 -75.313  1.00145.00           C  
ANISOU  821  CD  GLN A 433     9796  35455   9843  -1260   -136    841       C  
ATOM    822  OE1 GLN A 433     -34.172   0.793 -76.153  1.00138.49           O  
ANISOU  822  OE1 GLN A 433     8877  34800   8943  -1316   -172    891       O  
ATOM    823  NE2 GLN A 433     -32.778   1.768 -74.686  1.00151.82           N  
ANISOU  823  NE2 GLN A 433    10719  36158  10808  -1122   -165    988       N  
ATOM    824  N   TRP A 434     -32.848  -3.771 -77.248  1.00138.55           N  
ANISOU  824  N   TRP A 434     8925  34935   8780  -1833     13    106       N  
ATOM    825  CA  TRP A 434     -32.123  -4.110 -78.466  1.00139.52           C  
ANISOU  825  CA  TRP A 434     9014  35150   8847  -1977     27     38       C  
ATOM    826  C   TRP A 434     -33.078  -4.022 -79.650  1.00156.63           C  
ANISOU  826  C   TRP A 434    11044  37601  10868  -2099     17     82       C  
ATOM    827  O   TRP A 434     -34.260  -3.700 -79.502  1.00142.61           O  
ANISOU  827  O   TRP A 434     9201  35946   9037  -2065     -1    169       O  
ATOM    828  CB  TRP A 434     -31.501  -5.505 -78.364  1.00139.04           C  
ANISOU  828  CB  TRP A 434     9019  34987   8823  -2084     63   -213       C  
ATOM    829  CG  TRP A 434     -32.510  -6.581 -78.099  1.00139.61           C  
ANISOU  829  CG  TRP A 434     9076  35112   8859  -2169     77   -380       C  
ATOM    830  CD1 TRP A 434     -33.205  -7.301 -79.027  1.00160.65           C  
ANISOU  830  CD1 TRP A 434    11652  37976  11413  -2347     93   -493       C  
ATOM    831  CD2 TRP A 434     -32.944  -7.052 -76.818  1.00144.32           C  
ANISOU  831  CD2 TRP A 434     9742  35568   9525  -2090     75   -455       C  
ATOM    832  NE1 TRP A 434     -34.042  -8.193 -78.403  1.00142.10           N  
ANISOU  832  NE1 TRP A 434     9316  35615   9060  -2384    104   -636       N  
ATOM    833  CE2 TRP A 434     -33.900  -8.061 -77.047  1.00139.61           C  
ANISOU  833  CE2 TRP A 434     9096  35094   8856  -2226     90   -616       C  
ATOM    834  CE3 TRP A 434     -32.614  -6.722 -75.500  1.00143.80           C  
ANISOU  834  CE3 TRP A 434     9771  35294   9573  -1925     61   -403       C  
ATOM    835  CZ2 TRP A 434     -34.529  -8.741 -76.007  1.00163.74           C  
ANISOU  835  CZ2 TRP A 434    12191  38068  11953  -2200     89   -726       C  
ATOM    836  CZ3 TRP A 434     -33.241  -7.398 -74.470  1.00135.87           C  
ANISOU  836  CZ3 TRP A 434     8803  34213   8608  -1898     60   -510       C  
ATOM    837  CH2 TRP A 434     -34.188  -8.396 -74.729  1.00159.85           C  
ANISOU  837  CH2 TRP A 434    11786  37374  11574  -2033     73   -670       C  
ATOM    838  N   GLU A 435     -32.547  -4.315 -80.830  1.00162.43           N  
ANISOU  838  N   GLU A 435    11730  38451  11535  -2246     28     24       N  
ATOM    839  CA  GLU A 435     -33.290  -4.404 -82.074  1.00159.77           C  
ANISOU  839  CA  GLU A 435    11263  38395  11048  -2401     22     35       C  
ATOM    840  C   GLU A 435     -33.087  -5.791 -82.671  1.00154.44           C  
ANISOU  840  C   GLU A 435    10580  37766  10334  -2604     60   -218       C  
ATOM    841  O   GLU A 435     -32.100  -6.469 -82.358  1.00144.97           O  
ANISOU  841  O   GLU A 435     9466  36393   9222  -2620     88   -366       O  
ATOM    842  CB  GLU A 435     -32.828  -3.326 -83.066  1.00153.00           C  
ANISOU  842  CB  GLU A 435    10337  37667  10130  -2402     -3    223       C  
ATOM    843  CG  GLU A 435     -33.150  -1.907 -82.625  1.00152.97           C  
ANISOU  843  CG  GLU A 435    10317  37658  10146  -2219    -38    485       C  
ATOM    844  CD  GLU A 435     -32.711  -0.864 -83.634  1.00172.02           C  
ANISOU  844  CD  GLU A 435    12691  40145  12525  -2220    -94    665       C  
ATOM    845  OE1 GLU A 435     -32.136  -1.245 -84.676  1.00168.70           O  
ANISOU  845  OE1 GLU A 435    12216  39862  12021  -2376    -66    589       O  
ATOM    846  OE2 GLU A 435     -32.941   0.339 -83.385  1.00174.08           O  
ANISOU  846  OE2 GLU A 435    12977  40321  12845  -2067   -170    879       O  
ATOM    847  N   PRO A 436     -34.007  -6.257 -83.514  1.00148.21           N  
ANISOU  847  N   PRO A 436     9684  37216   9412  -2767     63   -275       N  
ATOM    848  CA  PRO A 436     -33.866  -7.598 -84.070  1.00149.12           C  
ANISOU  848  CA  PRO A 436     9789  37382   9490  -2976    104   -526       C  
ATOM    849  C   PRO A 436     -32.618  -7.693 -84.927  1.00149.34           C  
ANISOU  849  C   PRO A 436     9817  37408   9519  -3069    116   -577       C  
ATOM    850  O   PRO A 436     -32.131  -6.678 -85.456  1.00151.95           O  
ANISOU  850  O   PRO A 436    10119  37791   9825  -3018     88   -402       O  
ATOM    851  CB  PRO A 436     -35.140  -7.771 -84.907  1.00151.58           C  
ANISOU  851  CB  PRO A 436     9966  37989   9636  -3127     96   -520       C  
ATOM    852  CG  PRO A 436     -36.103  -6.784 -84.359  1.00151.49           C  
ANISOU  852  CG  PRO A 436     9919  38031   9611  -2966     55   -306       C  
ATOM    853  CD  PRO A 436     -35.272  -5.621 -83.926  1.00149.89           C  
ANISOU  853  CD  PRO A 436     9778  37671   9504  -2770     30   -115       C  
ATOM    854  N   PRO A 437     -32.059  -8.890 -85.073  1.00149.37           N  
ANISOU  854  N   PRO A 437     9847  37354   9555  -3207    156   -815       N  
ATOM    855  CA  PRO A 437     -30.880  -9.044 -85.926  1.00149.76           C  
ANISOU  855  CA  PRO A 437     9881  37421   9599  -3310    160   -878       C  
ATOM    856  C   PRO A 437     -31.230  -8.822 -87.387  1.00152.23           C  
ANISOU  856  C   PRO A 437    10073  38028   9739  -3490    150   -835       C  
ATOM    857  O   PRO A 437     -32.370  -9.020 -87.816  1.00153.91           O  
ANISOU  857  O   PRO A 437    10205  38439   9836  -3597    151   -842       O  
ATOM    858  CB  PRO A 437     -30.444 -10.490 -85.671  1.00149.46           C  
ANISOU  858  CB  PRO A 437     9877  37282   9631  -3429    191  -1159       C  
ATOM    859  CG  PRO A 437     -31.697 -11.184 -85.258  1.00150.03           C  
ANISOU  859  CG  PRO A 437     9932  37399   9675  -3484    216  -1257       C  
ATOM    860  CD  PRO A 437     -32.488 -10.169 -84.481  1.00149.18           C  
ANISOU  860  CD  PRO A 437     9855  37256   9572  -3282    195  -1041       C  
ATOM    861  N   GLU A 438     -30.227  -8.396 -88.157  1.00160.79           N  
ANISOU  861  N   GLU A 438    11141  39150  10800  -3527    137   -788       N  
ATOM    862  CA  GLU A 438     -30.459  -8.150 -89.574  1.00154.92           C  
ANISOU  862  CA  GLU A 438    10284  38690   9888  -3703    126   -741       C  
ATOM    863  C   GLU A 438     -30.638  -9.449 -90.348  1.00156.70           C  
ANISOU  863  C   GLU A 438    10460  39058  10021  -3972    163   -994       C  
ATOM    864  O   GLU A 438     -31.314  -9.463 -91.383  1.00159.01           O  
ANISOU  864  O   GLU A 438    10648  39616  10152  -4145    161   -980       O  
ATOM    865  CB  GLU A 438     -29.310  -7.331 -90.164  1.00154.76           C  
ANISOU  865  CB  GLU A 438    10265  38671   9865  -3672    104   -624       C  
ATOM    866  CG  GLU A 438     -29.635  -6.699 -91.509  1.00157.09           C  
ANISOU  866  CG  GLU A 438    10440  39261   9987  -3803     80   -496       C  
ATOM    867  CD  GLU A 438     -28.524  -5.804 -92.023  1.00172.19           C  
ANISOU  867  CD  GLU A 438    12356  41169  11901  -3759     57   -365       C  
ATOM    868  OE1 GLU A 438     -27.479  -5.702 -91.347  1.00157.13           O  
ANISOU  868  OE1 GLU A 438    10543  39032  10127  -3634     61   -381       O  
ATOM    869  OE2 GLU A 438     -28.697  -5.202 -93.105  1.00175.62           O  
ANISOU  869  OE2 GLU A 438    12692  41837  12197  -3855     34   -243       O  
ATOM    870  N   GLU A 439     -30.063 -10.549 -89.860  1.00155.79           N  
ANISOU  870  N   GLU A 439    10413  38782   9997  -4019    195  -1225       N  
ATOM    871  CA  GLU A 439     -30.130 -11.849 -90.525  1.00157.41           C  
ANISOU  871  CA  GLU A 439    10584  39102  10122  -4283    235  -1490       C  
ATOM    872  C   GLU A 439     -30.701 -12.892 -89.568  1.00156.69           C  
ANISOU  872  C   GLU A 439    10539  38883  10112  -4286    261  -1672       C  
ATOM    873  O   GLU A 439     -29.971 -13.759 -89.068  1.00155.68           O  
ANISOU  873  O   GLU A 439    10485  38600  10067  -4302    277  -1861       O  
ATOM    874  CB  GLU A 439     -28.751 -12.273 -91.027  1.00157.37           C  
ANISOU  874  CB  GLU A 439    10611  39062  10120  -4377    249  -1626       C  
ATOM    875  CG  GLU A 439     -28.091 -11.255 -91.943  1.00158.02           C  
ANISOU  875  CG  GLU A 439    10651  39259  10129  -4375    223  -1455       C  
ATOM    876  CD  GLU A 439     -26.712 -11.687 -92.398  1.00157.99           C  
ANISOU  876  CD  GLU A 439    10681  39225  10121  -4467    243  -1595       C  
ATOM    877  OE1 GLU A 439     -26.292 -12.810 -92.049  1.00157.60           O  
ANISOU  877  OE1 GLU A 439    10686  39085  10112  -4542    284  -1831       O  
ATOM    878  OE2 GLU A 439     -26.046 -10.902 -93.104  1.00176.46           O  
ANISOU  878  OE2 GLU A 439    12994  41644  12409  -4466    224  -1470       O  
ATOM    879  N   PRO A 440     -32.009 -12.842 -89.295  1.00157.28           N  
ANISOU  879  N   PRO A 440    10573  39036  10148  -4275    266  -1619       N  
ATOM    880  CA  PRO A 440     -32.595 -13.833 -88.377  1.00156.67           C  
ANISOU  880  CA  PRO A 440    10537  38843  10147  -4286    291  -1793       C  
ATOM    881  C   PRO A 440     -32.634 -15.240 -88.946  1.00158.27           C  
ANISOU  881  C   PRO A 440    10717  39138  10280  -4566    336  -2090       C  
ATOM    882  O   PRO A 440     -32.482 -16.203 -88.183  1.00157.36           O  
ANISOU  882  O   PRO A 440    10670  38871  10249  -4580    354  -2286       O  
ATOM    883  CB  PRO A 440     -34.011 -13.290 -88.128  1.00157.26           C  
ANISOU  883  CB  PRO A 440    10564  39031  10156  -4218    287  -1640       C  
ATOM    884  CG  PRO A 440     -33.968 -11.856 -88.563  1.00157.40           C  
ANISOU  884  CG  PRO A 440    10544  39148  10113  -4093    240  -1355       C  
ATOM    885  CD  PRO A 440     -32.990 -11.819 -89.690  1.00158.38           C  
ANISOU  885  CD  PRO A 440    10635  39368  10176  -4229    238  -1386       C  
ATOM    886  N   ASN A 441     -32.843 -15.388 -90.257  1.00182.42           N  
ANISOU  886  N   ASN A 441    13688  42450  13174  -4799    358  -2134       N  
ATOM    887  CA  ASN A 441     -32.946 -16.694 -90.915  1.00162.60           C  
ANISOU  887  CA  ASN A 441    11154  40053  10572  -5099    417  -2420       C  
ATOM    888  C   ASN A 441     -34.087 -17.532 -90.345  1.00163.06           C  
ANISOU  888  C   ASN A 441    11205  40112  10637  -5172    446  -2557       C  
ATOM    889  O   ASN A 441     -34.025 -18.764 -90.341  1.00163.69           O  
ANISOU  889  O   ASN A 441    11315  40170  10710  -5360    502  -2829       O  
ATOM    890  CB  ASN A 441     -31.628 -17.471 -90.836  1.00161.79           C  
ANISOU  890  CB  ASN A 441    11136  39811  10528  -5156    451  -2628       C  
ATOM    891  CG  ASN A 441     -30.464 -16.712 -91.437  1.00171.02           C  
ANISOU  891  CG  ASN A 441    12308  40990  11681  -5103    429  -2511       C  
ATOM    892  OD1 ASN A 441     -29.403 -16.595 -90.825  1.00172.11           O  
ANISOU  892  OD1 ASN A 441    12526  40939  11928  -4950    419  -2505       O  
ATOM    893  ND2 ASN A 441     -30.657 -16.189 -92.643  1.00163.45           N  
ANISOU  893  ND2 ASN A 441    11260  40267  10579  -5234    421  -2415       N  
ATOM    894  N   GLY A 442     -35.135 -16.877 -89.866  1.00162.83           N  
ANISOU  894  N   GLY A 442    11141  40116  10611  -5033    421  -2375       N  
ATOM    895  CA  GLY A 442     -36.279 -17.582 -89.332  1.00163.35           C  
ANISOU  895  CA  GLY A 442    11194  40200  10674  -5096    451  -2486       C  
ATOM    896  C   GLY A 442     -37.047 -16.704 -88.364  1.00162.00           C  
ANISOU  896  C   GLY A 442    11037  39962  10554  -4837    422  -2265       C  
ATOM    897  O   GLY A 442     -36.770 -15.515 -88.217  1.00160.92           O  
ANISOU  897  O   GLY A 442    10914  39792  10436  -4629    376  -2021       O  
ATOM    898  N   LEU A 443     -38.028 -17.325 -87.712  1.00162.17           N  
ANISOU  898  N   LEU A 443    11062  39972  10585  -4865    451  -2363       N  
ATOM    899  CA  LEU A 443     -38.829 -16.655 -86.696  1.00164.84           C  
ANISOU  899  CA  LEU A 443    11435  40250  10947  -4637    428  -2194       C  
ATOM    900  C   LEU A 443     -38.119 -16.765 -85.353  1.00158.11           C  
ANISOU  900  C   LEU A 443    10708  39065  10301  -4428    430  -2224       C  
ATOM    901  O   LEU A 443     -37.818 -17.873 -84.895  1.00157.62           O  
ANISOU  901  O   LEU A 443    10662  38861  10366  -4522    431  -2459       O  
ATOM    902  CB  LEU A 443     -40.228 -17.261 -86.616  1.00162.59           C  
ANISOU  902  CB  LEU A 443    11098  40124  10553  -4769    454  -2288       C  
ATOM    903  CG  LEU A 443     -41.192 -16.544 -85.665  1.00184.83           C  
ANISOU  903  CG  LEU A 443    13925  42936  13365  -4559    403  -2114       C  
ATOM    904  CD1 LEU A 443     -41.469 -15.134 -86.161  1.00185.81           C  
ANISOU  904  CD1 LEU A 443    13960  43239  13402  -4438    327  -1811       C  
ATOM    905  CD2 LEU A 443     -42.488 -17.324 -85.499  1.00175.80           C  
ANISOU  905  CD2 LEU A 443    12730  41933  12133  -4705    427  -2250       C  
ATOM    906  N   VAL A 444     -37.856 -15.620 -84.724  1.00174.15           N  
ANISOU  906  N   VAL A 444    12803  40985  12382  -4163    384  -1991       N  
ATOM    907  CA  VAL A 444     -37.157 -15.614 -83.445  1.00183.95           C  
ANISOU  907  CA  VAL A 444    14178  41923  13793  -3957    385  -1995       C  
ATOM    908  C   VAL A 444     -38.092 -16.116 -82.353  1.00163.45           C  
ANISOU  908  C   VAL A 444    11672  39257  11176  -3905    379  -2080       C  
ATOM    909  O   VAL A 444     -39.211 -15.613 -82.186  1.00153.74           O  
ANISOU  909  O   VAL A 444    10369  38161   9883  -3861    343  -1961       O  
ATOM    910  CB  VAL A 444     -36.622 -14.209 -83.130  1.00162.76           C  
ANISOU  910  CB  VAL A 444    11539  39155  11150  -3709    325  -1725       C  
ATOM    911  CG1 VAL A 444     -35.387 -13.917 -83.968  1.00153.43           C  
ANISOU  911  CG1 VAL A 444    10324  37968  10004  -3748    318  -1695       C  
ATOM    912  CG2 VAL A 444     -37.693 -13.156 -83.385  1.00179.02           C  
ANISOU  912  CG2 VAL A 444    13507  41417  13094  -3645    269  -1499       C  
ATOM    913  N   ARG A 445     -37.639 -17.125 -81.610  1.00152.03           N  
ANISOU  913  N   ARG A 445    10339  37623   9803  -3937    262  -2310       N  
ATOM    914  CA  ARG A 445     -38.405 -17.683 -80.506  1.00172.17           C  
ANISOU  914  CA  ARG A 445    12898  40105  12414  -3907    284  -2405       C  
ATOM    915  C   ARG A 445     -38.013 -17.100 -79.155  1.00148.81           C  
ANISOU  915  C   ARG A 445    10016  36925   9601  -3643    260  -2279       C  
ATOM    916  O   ARG A 445     -38.690 -17.375 -78.159  1.00155.00           O  
ANISOU  916  O   ARG A 445    10807  37652  10435  -3588    272  -2320       O  
ATOM    917  CB  ARG A 445     -38.244 -19.209 -80.468  1.00169.25           C  
ANISOU  917  CB  ARG A 445    12493  39713  12103  -4128    337  -2721       C  
ATOM    918  CG  ARG A 445     -38.708 -19.921 -81.732  1.00193.12           C  
ANISOU  918  CG  ARG A 445    15419  42955  15003  -4425    370  -2877       C  
ATOM    919  CD  ARG A 445     -40.226 -19.997 -81.817  1.00204.63           C  
ANISOU  919  CD  ARG A 445    16847  44585  16317  -4503    375  -2876       C  
ATOM    920  NE  ARG A 445     -40.795 -20.819 -80.752  1.00220.59           N  
ANISOU  920  NE  ARG A 445    18885  46519  18411  -4518    421  -3036       N  
ATOM    921  CZ  ARG A 445     -42.068 -21.197 -80.699  1.00207.87           C  
ANISOU  921  CZ  ARG A 445    17229  45048  16705  -4625    451  -3102       C  
ATOM    922  NH1 ARG A 445     -42.911 -20.830 -81.655  1.00210.74           N  
ANISOU  922  NH1 ARG A 445    17521  45665  16885  -4722    479  -3011       N  
ATOM    923  NH2 ARG A 445     -42.500 -21.945 -79.693  1.00172.94           N  
ANISOU  923  NH2 ARG A 445    12818  40527  12363  -4639    488  -3254       N  
ATOM    924  N   GLY A 446     -36.951 -16.312 -79.096  1.00147.43           N  
ANISOU  924  N   GLY A 446     9894  36630   9493  -3490    226  -2132       N  
ATOM    925  CA  GLY A 446     -36.521 -15.716 -77.849  1.00145.10           C  
ANISOU  925  CA  GLY A 446     9675  36128   9328  -3249    205  -2007       C  
ATOM    926  C   GLY A 446     -35.093 -15.225 -77.950  1.00162.12           C  
ANISOU  926  C   GLY A 446    11883  38156  11561  -3151    179  -1925       C  
ATOM    927  O   GLY A 446     -34.456 -15.293 -79.001  1.00169.10           O  
ANISOU  927  O   GLY A 446    12729  39117  12404  -3264    173  -1956       O  
ATOM    928  N   TYR A 447     -34.601 -14.726 -76.818  1.00141.78           N  
ANISOU  928  N   TYR A 447     9381  35388   9102  -2946    165  -1821       N  
ATOM    929  CA  TYR A 447     -33.244 -14.213 -76.711  1.00140.43           C  
ANISOU  929  CA  TYR A 447     9265  35081   9011  -2831    145  -1731       C  
ATOM    930  C   TYR A 447     -32.579 -14.780 -75.465  1.00142.74           C  
ANISOU  930  C   TYR A 447     9620  35183   9432  -2740    169  -1819       C  
ATOM    931  O   TYR A 447     -33.241 -15.279 -74.552  1.00138.19           O  
ANISOU  931  O   TYR A 447     9055  34560   8893  -2721    188  -1896       O  
ATOM    932  CB  TYR A 447     -33.216 -12.678 -76.657  1.00139.78           C  
ANISOU  932  CB  TYR A 447     9222  34972   8918  -2647    117  -1449       C  
ATOM    933  CG  TYR A 447     -33.747 -12.000 -77.899  1.00141.55           C  
ANISOU  933  CG  TYR A 447     9376  35402   9005  -2718    147  -1328       C  
ATOM    934  CD1 TYR A 447     -35.109 -11.794 -78.073  1.00147.26           C  
ANISOU  934  CD1 TYR A 447    10005  36296   9653  -2753    165  -1274       C  
ATOM    935  CD2 TYR A 447     -32.885 -11.556 -78.893  1.00167.84           C  
ANISOU  935  CD2 TYR A 447    12692  38780  12300  -2755    169  -1262       C  
ATOM    936  CE1 TYR A 447     -35.599 -11.172 -79.205  1.00167.13           C  
ANISOU  936  CE1 TYR A 447    12401  39036  12062  -2826    174  -1153       C  
ATOM    937  CE2 TYR A 447     -33.366 -10.931 -80.029  1.00168.41           C  
ANISOU  937  CE2 TYR A 447    12626  39071  12293  -2833    199  -1143       C  
ATOM    938  CZ  TYR A 447     -34.723 -10.743 -80.180  1.00172.13           C  
ANISOU  938  CZ  TYR A 447    13006  39719  12677  -2867    184  -1088       C  
ATOM    939  OH  TYR A 447     -35.206 -10.122 -81.309  1.00149.08           O  
ANISOU  939  OH  TYR A 447     9961  37041   9642  -2946    169   -966       O  
ATOM    940  N   ARG A 448     -31.250 -14.696 -75.438  1.00137.69           N  
ANISOU  940  N   ARG A 448     9019  34446   8852  -2686    170  -1804       N  
ATOM    941  CA  ARG A 448     -30.458 -15.108 -74.286  1.00136.02           C  
ANISOU  941  CA  ARG A 448     8882  34030   8769  -2576    208  -1848       C  
ATOM    942  C   ARG A 448     -29.498 -13.983 -73.939  1.00134.61           C  
ANISOU  942  C   ARG A 448     8755  33758   8632  -2397    153  -1644       C  
ATOM    943  O   ARG A 448     -28.639 -13.624 -74.752  1.00137.10           O  
ANISOU  943  O   ARG A 448     9061  34107   8924  -2419    144  -1596       O  
ATOM    944  CB  ARG A 448     -29.694 -16.405 -74.564  1.00136.49           C  
ANISOU  944  CB  ARG A 448     9000  33924   8937  -2684    363  -2049       C  
ATOM    945  CG  ARG A 448     -30.585 -17.570 -74.953  1.00138.03           C  
ANISOU  945  CG  ARG A 448     9168  34177   9101  -2877    448  -2262       C  
ATOM    946  CD  ARG A 448     -29.836 -18.888 -74.891  1.00149.23           C  
ANISOU  946  CD  ARG A 448    10700  35346  10653  -2938    643  -2449       C  
ATOM    947  NE  ARG A 448     -30.591 -19.964 -75.527  1.00170.93           N  
ANISOU  947  NE  ARG A 448    13424  38180  13343  -3157    728  -2660       N  
ATOM    948  CZ  ARG A 448     -30.253 -21.248 -75.475  1.00182.77           C  
ANISOU  948  CZ  ARG A 448    15029  39474  14943  -3236    917  -2848       C  
ATOM    949  NH1 ARG A 448     -29.171 -21.626 -74.809  1.00185.07           N  
ANISOU  949  NH1 ARG A 448    15452  39469  15400  -3105   1038  -2843       N  
ATOM    950  NH2 ARG A 448     -31.001 -22.155 -76.088  1.00191.73           N  
ANISOU  950  NH2 ARG A 448    16139  40702  16007  -3449    989  -3038       N  
ATOM    951  N   VAL A 449     -29.646 -13.428 -72.741  1.00133.14           N  
ANISOU  951  N   VAL A 449     8630  33434   8525  -2224    135  -1526       N  
ATOM    952  CA  VAL A 449     -28.839 -12.305 -72.284  1.00131.81           C  
ANISOU  952  CA  VAL A 449     8526  33139   8419  -2051    103  -1323       C  
ATOM    953  C   VAL A 449     -27.760 -12.836 -71.351  1.00130.49           C  
ANISOU  953  C   VAL A 449     8437  32725   8416  -1967    172  -1370       C  
ATOM    954  O   VAL A 449     -28.062 -13.500 -70.352  1.00135.78           O  
ANISOU  954  O   VAL A 449     9163  33202   9226  -1923    252  -1440       O  
ATOM    955  CB  VAL A 449     -29.702 -11.245 -71.582  1.00134.96           C  
ANISOU  955  CB  VAL A 449     8955  33489   8836  -1911     77  -1141       C  
ATOM    956  CG1 VAL A 449     -28.852 -10.055 -71.179  1.00144.33           C  
ANISOU  956  CG1 VAL A 449    10205  34554  10081  -1753     54   -940       C  
ATOM    957  CG2 VAL A 449     -30.850 -10.812 -72.481  1.00132.72           C  
ANISOU  957  CG2 VAL A 449     8609  33373   8446  -1980     70  -1085       C  
ATOM    958  N   TYR A 450     -26.504 -12.545 -71.673  1.00130.14           N  
ANISOU  958  N   TYR A 450     8414  32644   8388  -1937    170  -1318       N  
ATOM    959  CA  TYR A 450     -25.367 -12.941 -70.855  1.00129.00           C  
ANISOU  959  CA  TYR A 450     8362  32237   8415  -1842    259  -1328       C  
ATOM    960  C   TYR A 450     -24.753 -11.700 -70.223  1.00136.83           C  
ANISOU  960  C   TYR A 450     9387  33184   9419  -1685    181  -1123       C  
ATOM    961  O   TYR A 450     -24.512 -10.702 -70.911  1.00148.87           O  
ANISOU  961  O   TYR A 450    10873  34872  10819  -1684     89  -1001       O  
ATOM    962  CB  TYR A 450     -24.327 -13.694 -71.687  1.00129.75           C  
ANISOU  962  CB  TYR A 450     8467  32303   8528  -1933    346  -1442       C  
ATOM    963  CG  TYR A 450     -24.829 -15.012 -72.234  1.00131.05           C  
ANISOU  963  CG  TYR A 450     8628  32473   8694  -2091    457  -1658       C  
ATOM    964  CD1 TYR A 450     -25.515 -15.070 -73.441  1.00135.12           C  
ANISOU  964  CD1 TYR A 450     9050  33234   9053  -2256    412  -1728       C  
ATOM    965  CD2 TYR A 450     -24.620 -16.198 -71.543  1.00140.73           C  
ANISOU  965  CD2 TYR A 450     9942  33458  10070  -2079    611  -1789       C  
ATOM    966  CE1 TYR A 450     -25.978 -16.272 -73.943  1.00141.13           C  
ANISOU  966  CE1 TYR A 450     9812  34001   9809  -2416    519  -1932       C  
ATOM    967  CE2 TYR A 450     -25.079 -17.404 -72.037  1.00132.13           C  
ANISOU  967  CE2 TYR A 450     8862  32361   8980  -2228    727  -1989       C  
ATOM    968  CZ  TYR A 450     -25.756 -17.436 -73.237  1.00136.71           C  
ANISOU  968  CZ  TYR A 450     9355  33186   9403  -2401    681  -2065       C  
ATOM    969  OH  TYR A 450     -26.215 -18.635 -73.733  1.00135.05           O  
ANISOU  969  OH  TYR A 450     9159  32970   9185  -2565    801  -2270       O  
ATOM    970  N   TYR A 451     -24.506 -11.764 -68.916  1.00126.44           N  
ANISOU  970  N   TYR A 451     8146  31648   8247  -1561    223  -1086       N  
ATOM    971  CA  TYR A 451     -24.022 -10.613 -68.169  1.00140.72           C  
ANISOU  971  CA  TYR A 451     9993  33401  10074  -1419    159   -899       C  
ATOM    972  C   TYR A 451     -23.135 -11.088 -67.028  1.00124.17           C  
ANISOU  972  C   TYR A 451     7975  31057   8148  -1324    237   -908       C  
ATOM    973  O   TYR A 451     -23.278 -12.211 -66.538  1.00124.19           O  
ANISOU  973  O   TYR A 451     8012  30917   8257  -1340    339  -1038       O  
ATOM    974  CB  TYR A 451     -25.184  -9.772 -67.627  1.00124.94           C  
ANISOU  974  CB  TYR A 451     7992  31453   8027  -1354     97   -791       C  
ATOM    975  CG  TYR A 451     -26.120 -10.536 -66.716  1.00124.72           C  
ANISOU  975  CG  TYR A 451     7982  31300   8105  -1343    157   -886       C  
ATOM    976  CD1 TYR A 451     -27.128 -11.338 -67.237  1.00125.80           C  
ANISOU  976  CD1 TYR A 451     8069  31528   8201  -1459    186  -1027       C  
ATOM    977  CD2 TYR A 451     -26.000 -10.452 -65.334  1.00148.31           C  
ANISOU  977  CD2 TYR A 451    11036  34088  11228  -1224    188   -837       C  
ATOM    978  CE1 TYR A 451     -27.985 -12.038 -66.410  1.00125.66           C  
ANISOU  978  CE1 TYR A 451     8071  31395   8280  -1455    250  -1115       C  
ATOM    979  CE2 TYR A 451     -26.854 -11.148 -64.498  1.00127.66           C  
ANISOU  979  CE2 TYR A 451     8440  31358   8706  -1216    250   -922       C  
ATOM    980  CZ  TYR A 451     -27.845 -11.938 -65.042  1.00142.07           C  
ANISOU  980  CZ  TYR A 451    10219  33266  10495  -1330    284  -1061       C  
ATOM    981  OH  TYR A 451     -28.697 -12.633 -64.216  1.00146.87           O  
ANISOU  981  OH  TYR A 451    10848  33758  11197  -1328    354  -1148       O  
ATOM    982  N   THR A 452     -22.220 -10.218 -66.604  1.00123.33           N  
ANISOU  982  N   THR A 452     7897  30905   8057  -1228    194   -763       N  
ATOM    983  CA  THR A 452     -21.283 -10.548 -65.540  1.00145.95           C  
ANISOU  983  CA  THR A 452    10826  33565  11064  -1137    254   -747       C  
ATOM    984  C   THR A 452     -20.831  -9.270 -64.853  1.00121.45           C  
ANISOU  984  C   THR A 452     7747  30446   7951  -1030    177   -561       C  
ATOM    985  O   THR A 452     -20.764  -8.213 -65.493  1.00124.63           O  
ANISOU  985  O   THR A 452     8126  30988   8238  -1037    100   -450       O  
ATOM    986  CB  THR A 452     -20.061 -11.310 -66.079  1.00158.94           C  
ANISOU  986  CB  THR A 452    12475  35160  12755  -1176    333   -824       C  
ATOM    987  OG1 THR A 452     -19.213 -11.693 -64.990  1.00149.06           O  
ANISOU  987  OG1 THR A 452    11279  33719  11638  -1081    397   -803       O  
ATOM    988  CG2 THR A 452     -19.272 -10.437 -67.041  1.00123.19           C  
ANISOU  988  CG2 THR A 452     7908  30775   8125  -1201    263   -731       C  
ATOM    989  N   PRO A 453     -20.539  -9.325 -63.550  1.00120.50           N  
ANISOU  989  N   PRO A 453     7681  30162   7944   -936    205   -520       N  
ATOM    990  CA  PRO A 453     -19.922  -8.170 -62.884  1.00132.22           C  
ANISOU  990  CA  PRO A 453     9191  31622   9424   -848    144   -351       C  
ATOM    991  C   PRO A 453     -18.424  -8.067 -63.111  1.00130.40           C  
ANISOU  991  C   PRO A 453     8960  31376   9209   -839    148   -305       C  
ATOM    992  O   PRO A 453     -17.845  -7.006 -62.837  1.00119.22           O  
ANISOU  992  O   PRO A 453     7559  29974   7765   -793     94   -163       O  
ATOM    993  CB  PRO A 453     -20.237  -8.418 -61.404  1.00131.38           C  
ANISOU  993  CB  PRO A 453     9133  31356   9429   -767    178   -346       C  
ATOM    994  CG  PRO A 453     -20.295  -9.902 -61.295  1.00140.42           C  
ANISOU  994  CG  PRO A 453    10290  32401  10664   -800    283   -507       C  
ATOM    995  CD  PRO A 453     -20.883 -10.394 -62.595  1.00136.23           C  
ANISOU  995  CD  PRO A 453     9712  31990  10059   -910    295   -622       C  
ATOM    996  N   ASP A 454     -17.784  -9.127 -63.601  1.00144.71           N  
ANISOU  996  N   ASP A 454    10759  33154  11071   -885    223   -419       N  
ATOM    997  CA  ASP A 454     -16.351  -9.143 -63.881  1.00126.16           C  
ANISOU  997  CA  ASP A 454     8400  30789   8748   -878    242   -384       C  
ATOM    998  C   ASP A 454     -16.150  -9.514 -65.343  1.00144.16           C  
ANISOU  998  C   ASP A 454    10634  33182  10960   -980    266   -472       C  
ATOM    999  O   ASP A 454     -16.409 -10.655 -65.739  1.00126.38           O  
ANISOU  999  O   ASP A 454     8379  30896   8745  -1038    355   -622       O  
ATOM   1000  CB  ASP A 454     -15.621 -10.128 -62.971  1.00131.55           C  
ANISOU 1000  CB  ASP A 454     9108  31300   9573   -819    334   -429       C  
ATOM   1001  CG  ASP A 454     -14.123 -10.154 -63.221  1.00151.94           C  
ANISOU 1001  CG  ASP A 454    11669  33868  12193   -804    358   -385       C  
ATOM   1002  OD1 ASP A 454     -13.605  -9.223 -63.876  1.00147.47           O  
ANISOU 1002  OD1 ASP A 454    11077  33410  11546   -828    290   -296       O  
ATOM   1003  OD2 ASP A 454     -13.461 -11.108 -62.763  1.00171.62           O  
ANISOU 1003  OD2 ASP A 454    14168  36241  14797   -766    451   -434       O  
ATOM   1004  N   SER A 455     -15.670  -8.555 -66.137  1.00129.13           N  
ANISOU 1004  N   SER A 455     8701  31408   8956  -1007    197   -379       N  
ATOM   1005  CA  SER A 455     -15.378  -8.820 -67.540  1.00139.47           C  
ANISOU 1005  CA  SER A 455     9963  32835  10193  -1109    217   -451       C  
ATOM   1006  C   SER A 455     -14.237  -9.813 -67.720  1.00166.18           C  
ANISOU 1006  C   SER A 455    13345  36118  13677  -1117    328   -536       C  
ATOM   1007  O   SER A 455     -14.124 -10.418 -68.792  1.00185.72           O  
ANISOU 1007  O   SER A 455    15793  38651  16122  -1209    387   -645       O  
ATOM   1008  CB  SER A 455     -15.052  -7.510 -68.259  1.00154.14           C  
ANISOU 1008  CB  SER A 455    11795  34848  11922  -1128    124   -315       C  
ATOM   1009  OG  SER A 455     -13.997  -6.823 -67.608  1.00139.78           O  
ANISOU 1009  OG  SER A 455    10001  32962  10148  -1053    106   -186       O  
ATOM   1010  N   ARG A 456     -13.392  -9.997 -66.701  1.00171.29           N  
ANISOU 1010  N   ARG A 456    14019  36621  14443  -1024    365   -486       N  
ATOM   1011  CA  ARG A 456     -12.291 -10.949 -66.804  1.00170.25           C  
ANISOU 1011  CA  ARG A 456    13881  36388  14417  -1015    482   -552       C  
ATOM   1012  C   ARG A 456     -12.767 -12.395 -66.776  1.00174.92           C  
ANISOU 1012  C   ARG A 456    14498  36875  15089  -1042    614   -723       C  
ATOM   1013  O   ARG A 456     -12.006 -13.290 -67.158  1.00173.98           O  
ANISOU 1013  O   ARG A 456    14375  36687  15044  -1056    736   -804       O  
ATOM   1014  CB  ARG A 456     -11.284 -10.713 -65.678  1.00135.28           C  
ANISOU 1014  CB  ARG A 456     9460  31853  10089   -907    475   -436       C  
ATOM   1015  CG  ARG A 456     -10.627  -9.344 -65.714  1.00164.78           C  
ANISOU 1015  CG  ARG A 456    13176  35676  13757   -890    366   -273       C  
ATOM   1016  CD  ARG A 456      -9.700  -9.133 -64.525  1.00182.62           C  
ANISOU 1016  CD  ARG A 456    15438  37835  16113   -796    353   -161       C  
ATOM   1017  NE  ARG A 456     -10.417  -9.186 -63.254  1.00183.27           N  
ANISOU 1017  NE  ARG A 456    15562  37833  16238   -731    331   -139       N  
ATOM   1018  CZ  ARG A 456     -10.398 -10.226 -62.425  1.00158.46           C  
ANISOU 1018  CZ  ARG A 456    12433  34563  13211   -676    411   -198       C  
ATOM   1019  NH1 ARG A 456     -11.085 -10.186 -61.291  1.00125.59           N  
ANISOU 1019  NH1 ARG A 456     8308  30335   9073   -624    387   -173       N  
ATOM   1020  NH2 ARG A 456      -9.688 -11.304 -62.729  1.00141.24           N  
ANISOU 1020  NH2 ARG A 456    10228  32317  11120   -671    526   -279       N  
ATOM   1021  N   ARG A 457     -13.996 -12.643 -66.331  1.00162.14           N  
ANISOU 1021  N   ARG A 457    12907  35236  13461  -1050    604   -777       N  
ATOM   1022  CA  ARG A 457     -14.538 -13.990 -66.345  1.00156.30           C  
ANISOU 1022  CA  ARG A 457    12198  34401  12789  -1090    734   -944       C  
ATOM   1023  C   ARG A 457     -14.707 -14.478 -67.783  1.00156.69           C  
ANISOU 1023  C   ARG A 457    12223  34546  12764  -1224    790  -1076       C  
ATOM   1024  O   ARG A 457     -14.998 -13.688 -68.685  1.00150.54           O  
ANISOU 1024  O   ARG A 457    11403  33943  11854  -1296    694  -1043       O  
ATOM   1025  CB  ARG A 457     -15.883 -14.032 -65.627  1.00155.11           C  
ANISOU 1025  CB  ARG A 457    12075  34228  12631  -1082    701   -969       C  
ATOM   1026  CG  ARG A 457     -15.858 -14.725 -64.276  1.00164.74           C  
ANISOU 1026  CG  ARG A 457    13347  35262  13984   -987    777   -977       C  
ATOM   1027  CD  ARG A 457     -17.198 -14.577 -63.576  1.00178.32           C  
ANISOU 1027  CD  ARG A 457    15092  36973  15688   -980    733   -985       C  
ATOM   1028  NE  ARG A 457     -17.286 -15.383 -62.362  1.00171.94           N  
ANISOU 1028  NE  ARG A 457    14339  35988  15001   -907    824  -1015       N  
ATOM   1029  CZ  ARG A 457     -18.316 -15.351 -61.522  1.00173.58           C  
ANISOU 1029  CZ  ARG A 457    14579  36152  15223   -883    808  -1018       C  
ATOM   1030  NH1 ARG A 457     -19.343 -14.548 -61.763  1.00185.86           N  
ANISOU 1030  NH1 ARG A 457    16109  37825  16684   -920    706   -990       N  
ATOM   1031  NH2 ARG A 457     -18.318 -16.119 -60.441  1.00161.01           N  
ANISOU 1031  NH2 ARG A 457    13039  34400  13737   -818    901  -1044       N  
ATOM   1032  N   PRO A 458     -14.523 -15.775 -68.022  1.00154.64           N  
ANISOU 1032  N   PRO A 458    11993  34179  12584  -1262    951  -1224       N  
ATOM   1033  CA  PRO A 458     -14.768 -16.307 -69.358  1.00166.27           C  
ANISOU 1033  CA  PRO A 458    13453  35739  13983  -1404   1016  -1365       C  
ATOM   1034  C   PRO A 458     -16.217 -16.121 -69.747  1.00155.49           C  
ANISOU 1034  C   PRO A 458    12070  34507  12503  -1503    939  -1423       C  
ATOM   1035  O   PRO A 458     -17.110 -16.057 -68.880  1.00149.59           O  
ANISOU 1035  O   PRO A 458    11340  33723  11776  -1461    896  -1406       O  
ATOM   1036  CB  PRO A 458     -14.402 -17.793 -69.220  1.00171.88           C  
ANISOU 1036  CB  PRO A 458    14217  36266  14825  -1406   1222  -1508       C  
ATOM   1037  CG  PRO A 458     -14.473 -18.075 -67.755  1.00164.42           C  
ANISOU 1037  CG  PRO A 458    13311  35160  14002  -1279   1243  -1457       C  
ATOM   1038  CD  PRO A 458     -14.051 -16.809 -67.087  1.00167.50           C  
ANISOU 1038  CD  PRO A 458    13668  35602  14372  -1177   1088  -1264       C  
ATOM   1039  N   PRO A 459     -16.506 -16.017 -71.049  1.00155.59           N  
ANISOU 1039  N   PRO A 459    12040  34687  12389  -1638    918  -1488       N  
ATOM   1040  CA  PRO A 459     -17.885 -15.711 -71.472  1.00145.14           C  
ANISOU 1040  CA  PRO A 459    10675  33531  10940  -1733    823  -1521       C  
ATOM   1041  C   PRO A 459     -18.909 -16.730 -71.009  1.00186.59           C  
ANISOU 1041  C   PRO A 459    15962  38691  16243  -1774    907  -1660       C  
ATOM   1042  O   PRO A 459     -20.039 -16.357 -70.669  1.00206.38           O  
ANISOU 1042  O   PRO A 459    18442  41273  18700  -1779    817  -1635       O  
ATOM   1043  CB  PRO A 459     -17.773 -15.677 -73.002  1.00133.14           C  
ANISOU 1043  CB  PRO A 459     9107  32190   9291  -1882    823  -1588       C  
ATOM   1044  CG  PRO A 459     -16.338 -15.367 -73.270  1.00162.44           C  
ANISOU 1044  CG  PRO A 459    12822  35861  13036  -1831    852  -1515       C  
ATOM   1045  CD  PRO A 459     -15.573 -16.062 -72.187  1.00168.59           C  
ANISOU 1045  CD  PRO A 459    13666  36396  13993  -1708    970  -1519       C  
ATOM   1046  N   ASN A 460     -18.547 -18.012 -70.985  1.00180.75           N  
ANISOU 1046  N   ASN A 460    15283  37789  15605  -1802   1086  -1804       N  
ATOM   1047  CA  ASN A 460     -19.493 -19.043 -70.581  1.00188.48           C  
ANISOU 1047  CA  ASN A 460    16305  38672  16635  -1852   1183  -1945       C  
ATOM   1048  C   ASN A 460     -19.732 -19.069 -69.078  1.00158.72           C  
ANISOU 1048  C   ASN A 460    12580  34742  12984  -1713   1182  -1876       C  
ATOM   1049  O   ASN A 460     -20.607 -19.812 -68.622  1.00169.97           O  
ANISOU 1049  O   ASN A 460    14039  36089  14451  -1745   1250  -1977       O  
ATOM   1050  CB  ASN A 460     -19.008 -20.410 -71.063  1.00210.91           C  
ANISOU 1050  CB  ASN A 460    19208  41382  19547  -1928   1394  -2120       C  
ATOM   1051  CG  ASN A 460     -18.898 -20.487 -72.573  1.00211.88           C  
ANISOU 1051  CG  ASN A 460    19297  41663  19546  -2090   1412  -2212       C  
ATOM   1052  OD1 ASN A 460     -18.929 -19.466 -73.263  1.00207.24           O  
ANISOU 1052  OD1 ASN A 460    18635  41278  18827  -2126   1266  -2124       O  
ATOM   1053  ND2 ASN A 460     -18.768 -21.700 -73.095  1.00201.41           N  
ANISOU 1053  ND2 ASN A 460    18028  40242  18256  -2190   1598  -2389       N  
ATOM   1054  N   ALA A 461     -18.984 -18.285 -68.306  1.00155.19           N  
ANISOU 1054  N   ALA A 461    12133  34246  12585  -1568   1109  -1711       N  
ATOM   1055  CA  ALA A 461     -19.212 -18.155 -66.875  1.00174.70           C  
ANISOU 1055  CA  ALA A 461    14641  36588  15149  -1440   1089  -1630       C  
ATOM   1056  C   ALA A 461     -20.220 -17.065 -66.537  1.00165.48           C  
ANISOU 1056  C   ALA A 461    13433  35546  13897  -1421    926  -1528       C  
ATOM   1057  O   ALA A 461     -20.556 -16.893 -65.360  1.00153.09           O  
ANISOU 1057  O   ALA A 461    11895  33879  12393  -1326    906  -1464       O  
ATOM   1058  CB  ALA A 461     -17.890 -17.875 -66.152  1.00175.46           C  
ANISOU 1058  CB  ALA A 461    14755  36575  15339  -1300   1097  -1503       C  
ATOM   1059  N   TRP A 462     -20.707 -16.330 -67.534  1.00145.62           N  
ANISOU 1059  N   TRP A 462    10849  33244  11238  -1507    815  -1506       N  
ATOM   1060  CA  TRP A 462     -21.689 -15.287 -67.291  1.00125.72           C  
ANISOU 1060  CA  TRP A 462     8284  30850   8633  -1485    671  -1403       C  
ATOM   1061  C   TRP A 462     -23.047 -15.904 -66.963  1.00134.89           C  
ANISOU 1061  C   TRP A 462     9450  31997   9805  -1539    707  -1509       C  
ATOM   1062  O   TRP A 462     -23.325 -17.066 -67.274  1.00146.58           O  
ANISOU 1062  O   TRP A 462    10952  33425  11317  -1634    826  -1677       O  
ATOM   1063  CB  TRP A 462     -21.823 -14.365 -68.507  1.00160.05           C  
ANISOU 1063  CB  TRP A 462    12551  35444  12816  -1562    551  -1344       C  
ATOM   1064  CG  TRP A 462     -20.564 -13.642 -68.918  1.00158.38           C  
ANISOU 1064  CG  TRP A 462    12329  35270  12579  -1521    508  -1233       C  
ATOM   1065  CD1 TRP A 462     -19.279 -13.968 -68.592  1.00131.46           C  
ANISOU 1065  CD1 TRP A 462     8965  31714   9272  -1456    586  -1220       C  
ATOM   1066  CD2 TRP A 462     -20.481 -12.468 -69.737  1.00170.20           C  
ANISOU 1066  CD2 TRP A 462    13763  36969  13935  -1543    382  -1115       C  
ATOM   1067  NE1 TRP A 462     -18.404 -13.073 -69.157  1.00140.45           N  
ANISOU 1067  NE1 TRP A 462    10071  32949  10346  -1443    515  -1108       N  
ATOM   1068  CE2 TRP A 462     -19.116 -12.144 -69.867  1.00162.44           C  
ANISOU 1068  CE2 TRP A 462    12795  35944  12982  -1497    392  -1043       C  
ATOM   1069  CE3 TRP A 462     -21.429 -11.661 -70.374  1.00126.84           C  
ANISOU 1069  CE3 TRP A 462     8204  31696   8295  -1596    266  -1056       C  
ATOM   1070  CZ2 TRP A 462     -18.677 -11.044 -70.601  1.00139.90           C  
ANISOU 1070  CZ2 TRP A 462     9894  33247  10015  -1507    293   -921       C  
ATOM   1071  CZ3 TRP A 462     -20.991 -10.571 -71.104  1.00127.03           C  
ANISOU 1071  CZ3 TRP A 462     8184  31879   8203  -1599    169   -928       C  
ATOM   1072  CH2 TRP A 462     -19.626 -10.273 -71.212  1.00126.74           C  
ANISOU 1072  CH2 TRP A 462     8168  31785   8201  -1557    184   -864       C  
ATOM   1073  N   HIS A 463     -23.901 -15.106 -66.328  1.00125.33           N  
ANISOU 1073  N   HIS A 463     8221  30831   8570  -1479    610  -1411       N  
ATOM   1074  CA  HIS A 463     -25.253 -15.545 -66.020  1.00139.97           C  
ANISOU 1074  CA  HIS A 463    10066  32691  10427  -1528    631  -1495       C  
ATOM   1075  C   HIS A 463     -26.145 -15.393 -67.245  1.00141.42           C  
ANISOU 1075  C   HIS A 463    10157  33119  10456  -1668    566  -1549       C  
ATOM   1076  O   HIS A 463     -26.065 -14.397 -67.969  1.00147.40           O  
ANISOU 1076  O   HIS A 463    10852  34062  11089  -1676    450  -1442       O  
ATOM   1077  CB  HIS A 463     -25.823 -14.746 -64.849  1.00153.43           C  
ANISOU 1077  CB  HIS A 463    11785  34341  12169  -1405    566  -1367       C  
ATOM   1078  CG  HIS A 463     -24.915 -14.688 -63.659  1.00158.39           C  
ANISOU 1078  CG  HIS A 463    12492  34769  12922  -1270    604  -1287       C  
ATOM   1079  ND1 HIS A 463     -24.445 -15.818 -63.025  1.00154.22           N  
ANISOU 1079  ND1 HIS A 463    12035  34043  12519  -1250    741  -1382       N  
ATOM   1080  CD2 HIS A 463     -24.394 -13.635 -62.987  1.00150.37           C  
ANISOU 1080  CD2 HIS A 463    11491  33729  11915  -1151    525  -1120       C  
ATOM   1081  CE1 HIS A 463     -23.672 -15.463 -62.015  1.00150.04           C  
ANISOU 1081  CE1 HIS A 463    11553  33390  12065  -1125    736  -1271       C  
ATOM   1082  NE2 HIS A 463     -23.625 -14.144 -61.969  1.00124.17           N  
ANISOU 1082  NE2 HIS A 463     8243  30216   8720  -1069    605  -1117       N  
ATOM   1083  N   LYS A 464     -26.994 -16.390 -67.475  1.00127.90           N  
ANISOU 1083  N   LYS A 464     8436  31414   8746  -1785    645  -1713       N  
ATOM   1084  CA  LYS A 464     -27.867 -16.432 -68.641  1.00129.35           C  
ANISOU 1084  CA  LYS A 464     8527  31840   8780  -1942    596  -1788       C  
ATOM   1085  C   LYS A 464     -29.302 -16.145 -68.223  1.00129.46           C  
ANISOU 1085  C   LYS A 464     8494  31937   8759  -1944    541  -1768       C  
ATOM   1086  O   LYS A 464     -29.832 -16.797 -67.318  1.00153.32           O  
ANISOU 1086  O   LYS A 464    11563  34801  11891  -1922    624  -1838       O  
ATOM   1087  CB  LYS A 464     -27.785 -17.792 -69.337  1.00146.84           C  
ANISOU 1087  CB  LYS A 464    10762  34024  11007  -2099    734  -2001       C  
ATOM   1088  CG  LYS A 464     -28.610 -17.890 -70.609  1.00178.37           C  
ANISOU 1088  CG  LYS A 464    14655  38286  14833  -2286    685  -2091       C  
ATOM   1089  CD  LYS A 464     -28.712 -19.328 -71.089  1.00186.86           C  
ANISOU 1089  CD  LYS A 464    15766  39298  15934  -2448    843  -2319       C  
ATOM   1090  CE  LYS A 464     -29.435 -20.192 -70.068  1.00180.78           C  
ANISOU 1090  CE  LYS A 464    15058  38344  15288  -2436    951  -2416       C  
ATOM   1091  NZ  LYS A 464     -29.567 -21.604 -70.520  1.00181.28           N  
ANISOU 1091  NZ  LYS A 464    15167  38335  15374  -2598   1119  -2641       N  
ATOM   1092  N   HIS A 465     -29.927 -15.176 -68.888  1.00130.00           N  
ANISOU 1092  N   HIS A 465     8470  32252   8670  -1967    409  -1668       N  
ATOM   1093  CA  HIS A 465     -31.323 -14.823 -68.656  1.00130.37           C  
ANISOU 1093  CA  HIS A 465     8463  32412   8661  -1971    355  -1635       C  
ATOM   1094  C   HIS A 465     -32.074 -14.915 -69.976  1.00168.68           C  
ANISOU 1094  C   HIS A 465    13209  37559  13323  -2142    303  -1702       C  
ATOM   1095  O   HIS A 465     -31.790 -14.156 -70.909  1.00155.72           O  
ANISOU 1095  O   HIS A 465    11518  36118  11529  -2165    213  -1610       O  
ATOM   1096  CB  HIS A 465     -31.445 -13.418 -68.061  1.00129.35           C  
ANISOU 1096  CB  HIS A 465     8341  32293   8515  -1806    259  -1413       C  
ATOM   1097  CG  HIS A 465     -32.855 -12.927 -67.959  1.00129.94           C  
ANISOU 1097  CG  HIS A 465     8357  32493   8520  -1799    214  -1354       C  
ATOM   1098  ND1 HIS A 465     -33.743 -13.398 -67.016  1.00131.62           N  
ANISOU 1098  ND1 HIS A 465     8581  32582   8847  -1777    271  -1413       N  
ATOM   1099  CD2 HIS A 465     -33.532 -12.007 -68.686  1.00139.79           C  
ANISOU 1099  CD2 HIS A 465     9542  33971   9600  -1806    138  -1234       C  
ATOM   1100  CE1 HIS A 465     -34.905 -12.788 -67.165  1.00130.48           C  
ANISOU 1100  CE1 HIS A 465     8370  32585   8620  -1771    221  -1334       C  
ATOM   1101  NE2 HIS A 465     -34.804 -11.940 -68.172  1.00165.97           N  
ANISOU 1101  NE2 HIS A 465    12823  37291  12946  -1784    147  -1220       N  
ATOM   1102  N   ASN A 466     -33.028 -15.839 -70.053  1.00159.78           N  
ANISOU 1102  N   ASN A 466    12049  36466  12195  -2268    364  -1860       N  
ATOM   1103  CA  ASN A 466     -33.798 -16.056 -71.271  1.00158.10           C  
ANISOU 1103  CA  ASN A 466    11732  36543  11796  -2454    322  -1944       C  
ATOM   1104  C   ASN A 466     -35.035 -15.167 -71.287  1.00153.64           C  
ANISOU 1104  C   ASN A 466    11100  36174  11102  -2417    232  -1814       C  
ATOM   1105  O   ASN A 466     -35.675 -14.952 -70.253  1.00134.91           O  
ANISOU 1105  O   ASN A 466     8751  33674   8834  -2307    249  -1756       O  
ATOM   1106  CB  ASN A 466     -34.211 -17.524 -71.392  1.00146.04           C  
ANISOU 1106  CB  ASN A 466    10207  34959  10322  -2625    447  -2186       C  
ATOM   1107  CG  ASN A 466     -33.020 -18.459 -71.463  1.00151.78           C  
ANISOU 1107  CG  ASN A 466    11026  35477  11165  -2659    578  -2312       C  
ATOM   1108  OD1 ASN A 466     -31.974 -18.108 -72.008  1.00176.58           O  
ANISOU 1108  OD1 ASN A 466    14179  38634  14279  -2638    553  -2258       O  
ATOM   1109  ND2 ASN A 466     -33.174 -19.657 -70.912  1.00136.08           N  
ANISOU 1109  ND2 ASN A 466     9112  33284   9307  -2708    731  -2477       N  
ATOM   1110  N   THR A 467     -35.363 -14.646 -72.469  1.00138.48           N  
ANISOU 1110  N   THR A 467     9110  34526   8981  -2503    169  -1756       N  
ATOM   1111  CA  THR A 467     -36.530 -13.798 -72.674  1.00137.89           C  
ANISOU 1111  CA  THR A 467     8986  34577   8829  -2462    147  -1604       C  
ATOM   1112  C   THR A 467     -37.306 -14.300 -73.887  1.00145.32           C  
ANISOU 1112  C   THR A 467     9837  35743   9634  -2668    165  -1703       C  
ATOM   1113  O   THR A 467     -36.893 -15.240 -74.573  1.00140.99           O  
ANISOU 1113  O   THR A 467     9274  35237   9059  -2840    189  -1885       O  
ATOM   1114  CB  THR A 467     -36.137 -12.328 -72.869  1.00150.28           C  
ANISOU 1114  CB  THR A 467    10576  36124  10399  -2304    115  -1341       C  
ATOM   1115  OG1 THR A 467     -35.454 -12.175 -74.120  1.00177.13           O  
ANISOU 1115  OG1 THR A 467    13962  39605  13737  -2392    116  -1323       O  
ATOM   1116  CG2 THR A 467     -35.228 -11.858 -71.745  1.00175.07           C  
ANISOU 1116  CG2 THR A 467    13809  39041  13668  -2122    100  -1254       C  
ATOM   1117  N   ASP A 468     -38.442 -13.660 -74.152  1.00141.99           N  
ANISOU 1117  N   ASP A 468     9343  35481   9125  -2655    156  -1579       N  
ATOM   1118  CA  ASP A 468     -39.252 -13.992 -75.314  1.00143.56           C  
ANISOU 1118  CA  ASP A 468     9443  35923   9181  -2843    174  -1638       C  
ATOM   1119  C   ASP A 468     -38.822 -13.111 -76.490  1.00166.62           C  
ANISOU 1119  C   ASP A 468    12326  38956  12026  -2847    167  -1475       C  
ATOM   1120  O   ASP A 468     -37.742 -12.513 -76.470  1.00143.20           O  
ANISOU 1120  O   ASP A 468     9424  35861   9126  -2739    154  -1374       O  
ATOM   1121  CB  ASP A 468     -40.742 -13.855 -74.975  1.00144.51           C  
ANISOU 1121  CB  ASP A 468     9477  36190   9240  -2840    170  -1599       C  
ATOM   1122  CG  ASP A 468     -41.135 -12.437 -74.599  1.00148.90           C  
ANISOU 1122  CG  ASP A 468    10004  36769   9802  -2637    130  -1324       C  
ATOM   1123  OD1 ASP A 468     -40.242 -11.574 -74.459  1.00160.63           O  
ANISOU 1123  OD1 ASP A 468    11550  38129  11355  -2492    111  -1172       O  
ATOM   1124  OD2 ASP A 468     -42.348 -12.185 -74.439  1.00145.00           O  
ANISOU 1124  OD2 ASP A 468     9423  36362   9307  -2621    108  -1256       O  
ATOM   1125  N   ALA A 469     -39.663 -13.009 -77.517  1.00169.91           N  
ANISOU 1125  N   ALA A 469    12626  39625  12305  -2975    176  -1443       N  
ATOM   1126  CA  ALA A 469     -39.317 -12.288 -78.736  1.00147.67           C  
ANISOU 1126  CA  ALA A 469     9746  36954   9409  -3014    172  -1306       C  
ATOM   1127  C   ALA A 469     -39.382 -10.773 -78.585  1.00147.14           C  
ANISOU 1127  C   ALA A 469     9648  36903   9354  -2816    127  -1015       C  
ATOM   1128  O   ALA A 469     -39.108 -10.064 -79.560  1.00161.06           O  
ANISOU 1128  O   ALA A 469    11351  38792  11053  -2836    115   -880       O  
ATOM   1129  CB  ALA A 469     -40.230 -12.730 -79.883  1.00173.17           C  
ANISOU 1129  CB  ALA A 469    12845  40473  12478  -3233    192  -1373       C  
ATOM   1130  N   GLY A 470     -39.737 -10.260 -77.408  1.00145.78           N  
ANISOU 1130  N   GLY A 470     9513  36614   9260  -2635    101   -917       N  
ATOM   1131  CA  GLY A 470     -39.739  -8.825 -77.202  1.00145.24           C  
ANISOU 1131  CA  GLY A 470     9426  36544   9212  -2447     63   -648       C  
ATOM   1132  C   GLY A 470     -38.353  -8.225 -77.348  1.00143.96           C  
ANISOU 1132  C   GLY A 470     9344  36227   9129  -2365     61   -565       C  
ATOM   1133  O   GLY A 470     -37.332  -8.909 -77.263  1.00148.48           O  
ANISOU 1133  O   GLY A 470    10006  36641   9767  -2408     86   -711       O  
ATOM   1134  N   LEU A 471     -38.323  -6.914 -77.576  1.00144.06           N  
ANISOU 1134  N   LEU A 471     9316  36295   9127  -2245     31   -322       N  
ATOM   1135  CA  LEU A 471     -37.081  -6.200 -77.837  1.00143.14           C  
ANISOU 1135  CA  LEU A 471     9253  36067   9068  -2176     27   -219       C  
ATOM   1136  C   LEU A 471     -36.517  -5.513 -76.600  1.00140.97           C  
ANISOU 1136  C   LEU A 471     9083  35551   8928  -1972     15   -119       C  
ATOM   1137  O   LEU A 471     -35.607  -4.687 -76.725  1.00140.26           O  
ANISOU 1137  O   LEU A 471     9027  35381   8883  -1893      7      6       O  
ATOM   1138  CB  LEU A 471     -37.287  -5.178 -78.956  1.00179.21           C  
ANISOU 1138  CB  LEU A 471    13708  40852  13531  -2190      2    -17       C  
ATOM   1139  CG  LEU A 471     -37.708  -5.756 -80.309  1.00161.42           C  
ANISOU 1139  CG  LEU A 471    11344  38856  11134  -2405     12    -98       C  
ATOM   1140  CD1 LEU A 471     -37.781  -4.662 -81.362  1.00148.54           C  
ANISOU 1140  CD1 LEU A 471     9627  37365   9446  -2397    -49    118       C  
ATOM   1141  CD2 LEU A 471     -36.759  -6.866 -80.741  1.00146.86           C  
ANISOU 1141  CD2 LEU A 471     9559  36929   9311  -2557     51   -327       C  
ATOM   1142  N   LEU A 472     -37.031  -5.830 -75.414  1.00139.98           N  
ANISOU 1142  N   LEU A 472     9004  35317   8866  -1895     15   -174       N  
ATOM   1143  CA  LEU A 472     -36.486  -5.280 -74.180  1.00137.97           C  
ANISOU 1143  CA  LEU A 472     8850  34833   8739  -1717      6    -99       C  
ATOM   1144  C   LEU A 472     -36.850  -6.205 -73.029  1.00139.00           C  
ANISOU 1144  C   LEU A 472     9040  34834   8941  -1705     14   -261       C  
ATOM   1145  O   LEU A 472     -37.797  -6.991 -73.117  1.00138.03           O  
ANISOU 1145  O   LEU A 472     8862  34806   8776  -1803     16   -381       O  
ATOM   1146  CB  LEU A 472     -36.991  -3.855 -73.914  1.00138.07           C  
ANISOU 1146  CB  LEU A 472     8834  34775   8850  -1552    -66    153       C  
ATOM   1147  CG  LEU A 472     -38.402  -3.645 -73.357  1.00140.61           C  
ANISOU 1147  CG  LEU A 472     9099  35087   9241  -1483   -119    212       C  
ATOM   1148  CD1 LEU A 472     -38.567  -2.205 -72.898  1.00138.42           C  
ANISOU 1148  CD1 LEU A 472     8821  34695   9077  -1296   -179    454       C  
ATOM   1149  CD2 LEU A 472     -39.471  -4.000 -74.380  1.00178.71           C  
ANISOU 1149  CD2 LEU A 472    13797  40152  13951  -1616   -139    190       C  
ATOM   1150  N   THR A 473     -36.080  -6.103 -71.948  1.00149.87           N  
ANISOU 1150  N   THR A 473    10523  35988  10432  -1590     15   -261       N  
ATOM   1151  CA  THR A 473     -36.291  -6.942 -70.776  1.00135.53           C  
ANISOU 1151  CA  THR A 473     8765  34014   8715  -1569     18   -405       C  
ATOM   1152  C   THR A 473     -35.621  -6.295 -69.572  1.00132.22           C  
ANISOU 1152  C   THR A 473     8438  33350   8448  -1399      4   -308       C  
ATOM   1153  O   THR A 473     -34.829  -5.359 -69.701  1.00154.10           O  
ANISOU 1153  O   THR A 473    11241  36081  11228  -1320     -3   -164       O  
ATOM   1154  CB  THR A 473     -35.745  -8.357 -70.989  1.00140.55           C  
ANISOU 1154  CB  THR A 473     9437  34638   9327  -1715     45   -649       C  
ATOM   1155  OG1 THR A 473     -36.198  -9.209 -69.930  1.00133.41           O  
ANISOU 1155  OG1 THR A 473     8558  33626   8507  -1712     53   -788       O  
ATOM   1156  CG2 THR A 473     -34.223  -8.342 -70.993  1.00149.71           C  
ANISOU 1156  CG2 THR A 473    10685  35640  10559  -1688     46   -656       C  
ATOM   1157  N   THR A 474     -35.946  -6.821 -68.394  1.00139.47           N  
ANISOU 1157  N   THR A 474     9394  34104   9494  -1352      8   -393       N  
ATOM   1158  CA  THR A 474     -35.374  -6.376 -67.134  1.00143.94           C  
ANISOU 1158  CA  THR A 474    10045  34437  10210  -1208      5   -327       C  
ATOM   1159  C   THR A 474     -34.718  -7.553 -66.424  1.00135.55           C  
ANISOU 1159  C   THR A 474     9051  33227   9223  -1247     38   -512       C  
ATOM   1160  O   THR A 474     -35.185  -8.692 -66.515  1.00129.16           O  
ANISOU 1160  O   THR A 474     8215  32448   8413  -1358     66   -689       O  
ATOM   1161  CB  THR A 474     -36.438  -5.758 -66.218  1.00129.56           C  
ANISOU 1161  CB  THR A 474     8193  32523   8509  -1091     -9   -225       C  
ATOM   1162  OG1 THR A 474     -37.521  -6.681 -66.050  1.00130.32           O  
ANISOU 1162  OG1 THR A 474     8235  32654   8627  -1167     12   -363       O  
ATOM   1163  CG2 THR A 474     -36.967  -4.462 -66.809  1.00130.52           C  
ANISOU 1163  CG2 THR A 474     8247  32747   8596  -1022    -52    -14       C  
ATOM   1164  N   VAL A 475     -33.626  -7.268 -65.719  1.00134.08           N  
ANISOU 1164  N   VAL A 475     8949  32876   9119  -1158     39   -467       N  
ATOM   1165  CA  VAL A 475     -32.916  -8.264 -64.925  1.00135.41           C  
ANISOU 1165  CA  VAL A 475     9181  32867   9400  -1168     78   -607       C  
ATOM   1166  C   VAL A 475     -32.769  -7.717 -63.514  1.00124.81           C  
ANISOU 1166  C   VAL A 475     7900  31316   8205  -1023     89   -515       C  
ATOM   1167  O   VAL A 475     -32.173  -6.651 -63.317  1.00135.64           O  
ANISOU 1167  O   VAL A 475     9306  32654   9577   -928     58   -360       O  
ATOM   1168  CB  VAL A 475     -31.541  -8.611 -65.519  1.00125.87           C  
ANISOU 1168  CB  VAL A 475     8010  31670   8146  -1221     75   -657       C  
ATOM   1169  CG1 VAL A 475     -30.833  -9.640 -64.649  1.00124.94           C  
ANISOU 1169  CG1 VAL A 475     7952  31341   8178  -1216    136   -785       C  
ATOM   1170  CG2 VAL A 475     -31.688  -9.120 -66.945  1.00127.31           C  
ANISOU 1170  CG2 VAL A 475     8128  32074   8171  -1375     65   -752       C  
ATOM   1171  N   GLY A 476     -33.316  -8.439 -62.536  1.00124.46           N  
ANISOU 1171  N   GLY A 476     7872  31132   8285  -1013    145   -612       N  
ATOM   1172  CA  GLY A 476     -33.223  -8.055 -61.147  1.00123.30           C  
ANISOU 1172  CA  GLY A 476     7785  30790   8274   -890    171   -545       C  
ATOM   1173  C   GLY A 476     -32.176  -8.855 -60.393  1.00122.27           C  
ANISOU 1173  C   GLY A 476     7739  30478   8240   -882    231   -632       C  
ATOM   1174  O   GLY A 476     -31.407  -9.634 -60.960  1.00122.39           O  
ANISOU 1174  O   GLY A 476     7768  30505   8231   -958    251   -731       O  
ATOM   1175  N   SER A 477     -32.150  -8.638 -59.077  1.00134.26           N  
ANISOU 1175  N   SER A 477     9315  31824   9873   -784    269   -587       N  
ATOM   1176  CA  SER A 477     -31.250  -9.344 -58.164  1.00120.40           C  
ANISOU 1176  CA  SER A 477     7648  29882   8216   -758    339   -648       C  
ATOM   1177  C   SER A 477     -29.781  -9.138 -58.527  1.00119.91           C  
ANISOU 1177  C   SER A 477     7618  29826   8118   -749    303   -600       C  
ATOM   1178  O   SER A 477     -28.937  -9.993 -58.249  1.00119.56           O  
ANISOU 1178  O   SER A 477     7625  29672   8130   -763    362   -679       O  
ATOM   1179  CB  SER A 477     -31.580 -10.838 -58.105  1.00120.80           C  
ANISOU 1179  CB  SER A 477     7717  29859   8325   -845    439   -838       C  
ATOM   1180  OG  SER A 477     -32.909 -11.050 -57.659  1.00153.86           O  
ANISOU 1180  OG  SER A 477    11878  34026  12555   -854    481   -884       O  
ATOM   1181  N   LEU A 478     -29.461  -8.006 -59.149  1.00129.81           N  
ANISOU 1181  N   LEU A 478     8841  31201   9281   -723    215   -465       N  
ATOM   1182  CA  LEU A 478     -28.073  -7.685 -59.436  1.00128.70           C  
ANISOU 1182  CA  LEU A 478     8729  31065   9108   -711    181   -405       C  
ATOM   1183  C   LEU A 478     -27.337  -7.334 -58.148  1.00133.92           C  
ANISOU 1183  C   LEU A 478     9457  31569   9856   -616    198   -328       C  
ATOM   1184  O   LEU A 478     -27.940  -7.031 -57.115  1.00163.89           O  
ANISOU 1184  O   LEU A 478    13276  35279  13717   -551    221   -290       O  
ATOM   1185  CB  LEU A 478     -27.972  -6.515 -60.414  1.00139.36           C  
ANISOU 1185  CB  LEU A 478    10040  32579  10334   -710    101   -273       C  
ATOM   1186  CG  LEU A 478     -28.587  -6.619 -61.809  1.00121.19           C  
ANISOU 1186  CG  LEU A 478     7669  30471   7906   -804     76   -311       C  
ATOM   1187  CD1 LEU A 478     -28.285  -5.345 -62.576  1.00121.48           C  
ANISOU 1187  CD1 LEU A 478     7693  30629   7835   -780     26   -149       C  
ATOM   1188  CD2 LEU A 478     -28.061  -7.833 -62.554  1.00122.84           C  
ANISOU 1188  CD2 LEU A 478     7866  30713   8094   -914    106   -472       C  
ATOM   1189  N   LEU A 479     -26.021  -7.373 -58.220  1.00127.81           N  
ANISOU 1189  N   LEU A 479     8711  30769   9081   -612    189   -305       N  
ATOM   1190  CA  LEU A 479     -25.274  -6.918 -57.054  1.00118.12           C  
ANISOU 1190  CA  LEU A 479     7538  29427   7915   -530    192   -216       C  
ATOM   1191  C   LEU A 479     -25.070  -5.409 -57.137  1.00126.31           C  
ANISOU 1191  C   LEU A 479     8565  30535   8891   -482    114    -45       C  
ATOM   1192  O   LEU A 479     -24.693  -4.899 -58.197  1.00137.04           O  
ANISOU 1192  O   LEU A 479     9897  32011  10161   -516     66      5       O  
ATOM   1193  CB  LEU A 479     -23.937  -7.629 -56.953  1.00143.68           C  
ANISOU 1193  CB  LEU A 479    10806  32596  11189   -539    224   -255       C  
ATOM   1194  CG  LEU A 479     -24.069  -9.125 -56.655  1.00171.82           C  
ANISOU 1194  CG  LEU A 479    14399  36049  14835   -568    327   -412       C  
ATOM   1195  CD1 LEU A 479     -23.734  -9.956 -57.877  1.00156.85           C  
ANISOU 1195  CD1 LEU A 479    12470  34216  12908   -656    350   -522       C  
ATOM   1196  CD2 LEU A 479     -23.191  -9.515 -55.483  1.00165.20           C  
ANISOU 1196  CD2 LEU A 479    13622  35068  14077   -507    380   -393       C  
ATOM   1197  N   PRO A 480     -25.339  -4.670 -56.067  1.00116.84           N  
ANISOU 1197  N   PRO A 480     7391  29268   7736   -409    113     44       N  
ATOM   1198  CA  PRO A 480     -25.277  -3.208 -56.136  1.00118.22           C  
ANISOU 1198  CA  PRO A 480     7555  29498   7866   -366     51    204       C  
ATOM   1199  C   PRO A 480     -23.850  -2.681 -56.107  1.00116.12           C  
ANISOU 1199  C   PRO A 480     7315  29223   7581   -362     14    289       C  
ATOM   1200  O   PRO A 480     -22.923  -3.323 -55.613  1.00115.71           O  
ANISOU 1200  O   PRO A 480     7290  29106   7568   -368     32    247       O  
ATOM   1201  CB  PRO A 480     -26.048  -2.765 -54.888  1.00116.18           C  
ANISOU 1201  CB  PRO A 480     7312  29153   7677   -295     80    247       C  
ATOM   1202  CG  PRO A 480     -26.875  -3.950 -54.497  1.00116.25           C  
ANISOU 1202  CG  PRO A 480     7333  29093   7745   -313    158    105       C  
ATOM   1203  CD  PRO A 480     -26.032  -5.132 -54.855  1.00116.19           C  
ANISOU 1203  CD  PRO A 480     7344  29061   7740   -371    183     -7       C  
ATOM   1204  N   GLY A 481     -23.691  -1.477 -56.650  1.00116.36           N  
ANISOU 1204  N   GLY A 481     7339  29310   7561   -352    -31    416       N  
ATOM   1205  CA  GLY A 481     -22.409  -0.806 -56.566  1.00116.07           C  
ANISOU 1205  CA  GLY A 481     7336  29238   7526   -352    -65    510       C  
ATOM   1206  C   GLY A 481     -21.384  -1.252 -57.583  1.00116.31           C  
ANISOU 1206  C   GLY A 481     7356  29325   7511   -414    -54    474       C  
ATOM   1207  O   GLY A 481     -20.203  -0.924 -57.443  1.00123.41           O  
ANISOU 1207  O   GLY A 481     8279  30181   8429   -420    -74    531       O  
ATOM   1208  N   ILE A 482     -21.797  -1.983 -58.613  1.00116.86           N  
ANISOU 1208  N   ILE A 482     7390  29492   7521   -466    -30    379       N  
ATOM   1209  CA  ILE A 482     -20.870  -2.523 -59.596  1.00130.25           C  
ANISOU 1209  CA  ILE A 482     9070  31252   9165   -530    -20    326       C  
ATOM   1210  C   ILE A 482     -21.415  -2.272 -60.996  1.00118.07           C  
ANISOU 1210  C   ILE A 482     7485  29854   7522   -584    -16    329       C  
ATOM   1211  O   ILE A 482     -22.630  -2.210 -61.209  1.00118.47           O  
ANISOU 1211  O   ILE A 482     7510  29956   7547   -582    -15    316       O  
ATOM   1212  CB  ILE A 482     -20.613  -4.030 -59.358  1.00117.11           C  
ANISOU 1212  CB  ILE A 482     7404  29543   7550   -554      6    171       C  
ATOM   1213  CG1 ILE A 482     -19.420  -4.518 -60.181  1.00117.44           C  
ANISOU 1213  CG1 ILE A 482     7429  29625   7567   -606     13    132       C  
ATOM   1214  CG2 ILE A 482     -21.851  -4.842 -59.679  1.00167.01           C  
ANISOU 1214  CG2 ILE A 482    13697  35896  13864   -588     30     49       C  
ATOM   1215  CD1 ILE A 482     -18.116  -3.847 -59.821  1.00117.08           C  
ANISOU 1215  CD1 ILE A 482     7404  29538   7544   -580     -5    243       C  
ATOM   1216  N   THR A 483     -20.502  -2.105 -61.952  1.00118.45           N  
ANISOU 1216  N   THR A 483     7518  29974   7513   -633    -12    351       N  
ATOM   1217  CA  THR A 483     -20.851  -1.868 -63.348  1.00124.63           C  
ANISOU 1217  CA  THR A 483     8254  30870   8229   -693     -9    358       C  
ATOM   1218  C   THR A 483     -20.776  -3.184 -64.113  1.00120.52           C  
ANISOU 1218  C   THR A 483     7710  30413   7669   -774     -5    192       C  
ATOM   1219  O   THR A 483     -19.722  -3.829 -64.148  1.00119.79           O  
ANISOU 1219  O   THR A 483     7624  30307   7585   -798     -5    131       O  
ATOM   1220  CB  THR A 483     -19.926  -0.827 -63.980  1.00119.60           C  
ANISOU 1220  CB  THR A 483     7604  30254   7583   -705    -11    484       C  
ATOM   1221  OG1 THR A 483     -18.560  -1.160 -63.700  1.00144.90           O  
ANISOU 1221  OG1 THR A 483    10834  33408  10812   -713    -12    465       O  
ATOM   1222  CG2 THR A 483     -20.236   0.562 -63.441  1.00119.36           C  
ANISOU 1222  CG2 THR A 483     7577  30188   7588   -638    -25    646       C  
ATOM   1223  N   TYR A 484     -21.887  -3.572 -64.728  1.00120.62           N  
ANISOU 1223  N   TYR A 484     7686  30510   7636   -820     -3    122       N  
ATOM   1224  CA  TYR A 484     -21.990  -4.856 -65.402  1.00135.66           C  
ANISOU 1224  CA  TYR A 484     9556  32489   9501   -911      0    -50       C  
ATOM   1225  C   TYR A 484     -21.615  -4.745 -66.874  1.00146.56           C  
ANISOU 1225  C   TYR A 484    10894  33977  10814   -999     -1    -54       C  
ATOM   1226  O   TYR A 484     -21.706  -3.676 -67.483  1.00125.39           O  
ANISOU 1226  O   TYR A 484     8200  31338   8106   -994      1     75       O  
ATOM   1227  CB  TYR A 484     -23.408  -5.415 -65.279  1.00142.01           C  
ANISOU 1227  CB  TYR A 484    10332  33342  10283   -934      4   -138       C  
ATOM   1228  CG  TYR A 484     -23.665  -6.193 -64.011  1.00120.88           C  
ANISOU 1228  CG  TYR A 484     7682  30542   7703   -889     21   -220       C  
ATOM   1229  CD1 TYR A 484     -23.491  -7.569 -63.976  1.00154.95           C  
ANISOU 1229  CD1 TYR A 484    11989  34789  12097   -944     71   -389       C  
ATOM   1230  CD2 TYR A 484     -24.089  -5.556 -62.853  1.00136.59           C  
ANISOU 1230  CD2 TYR A 484     9709  32426   9764   -792     19   -128       C  
ATOM   1231  CE1 TYR A 484     -23.724  -8.289 -62.823  1.00155.60           C  
ANISOU 1231  CE1 TYR A 484    12107  34701  12312   -900    128   -456       C  
ATOM   1232  CE2 TYR A 484     -24.327  -6.270 -61.694  1.00138.96           C  
ANISOU 1232  CE2 TYR A 484    10035  32572  10190   -753     56   -201       C  
ATOM   1233  CZ  TYR A 484     -24.142  -7.635 -61.686  1.00119.66           C  
ANISOU 1233  CZ  TYR A 484     7590  30061   7812   -806    115   -361       C  
ATOM   1234  OH  TYR A 484     -24.380  -8.349 -60.537  1.00119.12           O  
ANISOU 1234  OH  TYR A 484     7562  29833   7867   -766    179   -426       O  
ATOM   1235  N   SER A 485     -21.182  -5.869 -67.438  1.00153.29           N  
ANISOU 1235  N   SER A 485    11714  34889  11640  -1083      3   -205       N  
ATOM   1236  CA  SER A 485     -21.021  -6.034 -68.873  1.00123.91           C  
ANISOU 1236  CA  SER A 485     7940  31295   7845  -1191      2   -253       C  
ATOM   1237  C   SER A 485     -22.102  -6.973 -69.387  1.00146.76           C  
ANISOU 1237  C   SER A 485    10782  34292  10687  -1287     10   -403       C  
ATOM   1238  O   SER A 485     -22.607  -7.823 -68.647  1.00142.67           O  
ANISOU 1238  O   SER A 485    10266  33747  10196  -1283     23   -511       O  
ATOM   1239  CB  SER A 485     -19.639  -6.586 -69.229  1.00124.00           C  
ANISOU 1239  CB  SER A 485     7936  31324   7856  -1230      8   -318       C  
ATOM   1240  OG  SER A 485     -18.646  -5.592 -69.076  1.00132.78           O  
ANISOU 1240  OG  SER A 485     9082  32374   8994  -1168     -2   -170       O  
ATOM   1241  N   LEU A 486     -22.453  -6.822 -70.661  1.00134.98           N  
ANISOU 1241  N   LEU A 486     9240  32929   9117  -1382      6   -409       N  
ATOM   1242  CA  LEU A 486     -23.630  -7.513 -71.164  1.00127.06           C  
ANISOU 1242  CA  LEU A 486     8184  32037   8055  -1478     12   -526       C  
ATOM   1243  C   LEU A 486     -23.554  -7.655 -72.677  1.00129.24           C  
ANISOU 1243  C   LEU A 486     8396  32470   8242  -1614      9   -575       C  
ATOM   1244  O   LEU A 486     -23.016  -6.789 -73.371  1.00128.84           O  
ANISOU 1244  O   LEU A 486     8344  32448   8160  -1610     -2   -456       O  
ATOM   1245  CB  LEU A 486     -24.903  -6.760 -70.759  1.00127.00           C  
ANISOU 1245  CB  LEU A 486     8187  32030   8039  -1413     12   -416       C  
ATOM   1246  CG  LEU A 486     -26.275  -7.282 -71.179  1.00128.10           C  
ANISOU 1246  CG  LEU A 486     8268  32292   8111  -1498     19   -503       C  
ATOM   1247  CD1 LEU A 486     -27.278  -6.983 -70.085  1.00131.20           C  
ANISOU 1247  CD1 LEU A 486     8679  32629   8543  -1401     21   -447       C  
ATOM   1248  CD2 LEU A 486     -26.722  -6.647 -72.486  1.00167.93           C  
ANISOU 1248  CD2 LEU A 486    13254  37494  13057  -1567     29   -421       C  
ATOM   1249  N   ARG A 487     -24.107  -8.761 -73.174  1.00134.52           N  
ANISOU 1249  N   ARG A 487     9005  33244   8863  -1743     25   -754       N  
ATOM   1250  CA  ARG A 487     -24.351  -8.936 -74.599  1.00131.63           C  
ANISOU 1250  CA  ARG A 487     8563  33049   8401  -1891     22   -810       C  
ATOM   1251  C   ARG A 487     -25.480  -9.940 -74.781  1.00132.62           C  
ANISOU 1251  C   ARG A 487     8637  33274   8477  -2009     42   -974       C  
ATOM   1252  O   ARG A 487     -25.662 -10.846 -73.962  1.00147.82           O  
ANISOU 1252  O   ARG A 487    10576  35144  10444  -2008     68  -1104       O  
ATOM   1253  CB  ARG A 487     -23.095  -9.387 -75.353  1.00131.59           C  
ANISOU 1253  CB  ARG A 487     8524  33097   8379  -1976     38   -894       C  
ATOM   1254  CG  ARG A 487     -22.448 -10.661 -74.851  1.00131.23           C  
ANISOU 1254  CG  ARG A 487     8479  33021   8360  -2009     81  -1080       C  
ATOM   1255  CD  ARG A 487     -21.184 -10.932 -75.647  1.00135.39           C  
ANISOU 1255  CD  ARG A 487     8990  33577   8875  -2075    121  -1133       C  
ATOM   1256  NE  ARG A 487     -20.327 -11.947 -75.045  1.00142.70           N  
ANISOU 1256  NE  ARG A 487    10017  34243   9958  -2035    270  -1242       N  
ATOM   1257  CZ  ARG A 487     -19.050 -12.122 -75.370  1.00165.21           C  
ANISOU 1257  CZ  ARG A 487    12903  37010  12858  -2031    345  -1254       C  
ATOM   1258  NH1 ARG A 487     -18.484 -11.344 -76.283  1.00131.95           N  
ANISOU 1258  NH1 ARG A 487     8638  32946   8552  -2070    283  -1170       N  
ATOM   1259  NH2 ARG A 487     -18.335 -13.067 -74.780  1.00202.70           N  
ANISOU 1259  NH2 ARG A 487    17736  41529  17753  -1984    486  -1343       N  
ATOM   1260  N   VAL A 488     -26.239  -9.759 -75.859  1.00134.21           N  
ANISOU 1260  N   VAL A 488     8777  33630   8585  -2115     30   -965       N  
ATOM   1261  CA  VAL A 488     -27.451 -10.526 -76.117  1.00134.77           C  
ANISOU 1261  CA  VAL A 488     8796  33818   8594  -2234     46  -1094       C  
ATOM   1262  C   VAL A 488     -27.313 -11.252 -77.449  1.00136.52           C  
ANISOU 1262  C   VAL A 488     8925  34211   8733  -2440     63  -1241       C  
ATOM   1263  O   VAL A 488     -26.696 -10.748 -78.393  1.00137.17           O  
ANISOU 1263  O   VAL A 488     8969  34366   8784  -2482     48  -1174       O  
ATOM   1264  CB  VAL A 488     -28.703  -9.617 -76.119  1.00135.22           C  
ANISOU 1264  CB  VAL A 488     8863  33934   8582  -2174     46   -936       C  
ATOM   1265  CG1 VAL A 488     -29.979 -10.449 -76.065  1.00136.16           C  
ANISOU 1265  CG1 VAL A 488     8932  34150   8652  -2274     63  -1069       C  
ATOM   1266  CG2 VAL A 488     -28.650  -8.628 -74.966  1.00133.62           C  
ANISOU 1266  CG2 VAL A 488     8727  33578   8462  -1973     52   -757       C  
ATOM   1267  N   LEU A 489     -27.896 -12.447 -77.517  1.00137.34           N  
ANISOU 1267  N   LEU A 489     8991  34389   8802  -2579    102  -1447       N  
ATOM   1268  CA  LEU A 489     -28.000 -13.198 -78.759  1.00139.23           C  
ANISOU 1268  CA  LEU A 489     9144  34812   8946  -2801    131  -1605       C  
ATOM   1269  C   LEU A 489     -29.448 -13.617 -78.968  1.00140.52           C  
ANISOU 1269  C   LEU A 489     9255  35096   9042  -2912    135  -1678       C  
ATOM   1270  O   LEU A 489     -30.228 -13.729 -78.019  1.00139.84           O  
ANISOU 1270  O   LEU A 489     9205  34940   8988  -2836    133  -1677       O  
ATOM   1271  CB  LEU A 489     -27.075 -14.432 -78.770  1.00141.37           C  
ANISOU 1271  CB  LEU A 489     9416  35076   9222  -2906    195  -1832       C  
ATOM   1272  CG  LEU A 489     -27.260 -15.567 -77.756  1.00138.62           C  
ANISOU 1272  CG  LEU A 489     9154  34537   8979  -2892    296  -1994       C  
ATOM   1273  CD1 LEU A 489     -28.311 -16.578 -78.203  1.00140.24           C  
ANISOU 1273  CD1 LEU A 489     9316  34846   9122  -3088    353  -2187       C  
ATOM   1274  CD2 LEU A 489     -25.932 -16.261 -77.509  1.00138.03           C  
ANISOU 1274  CD2 LEU A 489     9216  34178   9049  -2843    453  -2071       C  
ATOM   1275  N   ALA A 490     -29.800 -13.845 -80.228  1.00162.26           N  
ANISOU 1275  N   ALA A 490    11916  38042  11693  -3099    145  -1740       N  
ATOM   1276  CA  ALA A 490     -31.129 -14.298 -80.606  1.00157.18           C  
ANISOU 1276  CA  ALA A 490    11205  37547  10969  -3238    151  -1819       C  
ATOM   1277  C   ALA A 490     -31.080 -15.760 -81.026  1.00147.99           C  
ANISOU 1277  C   ALA A 490    10009  36469   9753  -3468    225  -2106       C  
ATOM   1278  O   ALA A 490     -30.049 -16.256 -81.491  1.00145.48           O  
ANISOU 1278  O   ALA A 490     9692  36160   9424  -3556    266  -2222       O  
ATOM   1279  CB  ALA A 490     -31.697 -13.451 -81.748  1.00145.73           C  
ANISOU 1279  CB  ALA A 490     9627  36282   9461  -3299    134  -1663       C  
ATOM   1280  N   PHE A 491     -32.204 -16.451 -80.854  1.00146.16           N  
ANISOU 1280  N   PHE A 491     9750  36303   9482  -3572    246  -2227       N  
ATOM   1281  CA  PHE A 491     -32.322 -17.824 -81.319  1.00158.72           C  
ANISOU 1281  CA  PHE A 491    11302  37990  11013  -3819    323  -2508       C  
ATOM   1282  C   PHE A 491     -33.699 -18.048 -81.922  1.00174.49           C  
ANISOU 1282  C   PHE A 491    13218  40173  12908  -3982    323  -2549       C  
ATOM   1283  O   PHE A 491     -34.701 -17.526 -81.426  1.00165.30           O  
ANISOU 1283  O   PHE A 491    12051  39011  11744  -3879    276  -2425       O  
ATOM   1284  CB  PHE A 491     -32.060 -18.844 -80.192  1.00154.16           C  
ANISOU 1284  CB  PHE A 491    10790  37259  10523  -3798    381  -2691       C  
ATOM   1285  CG  PHE A 491     -33.055 -18.797 -79.060  1.00154.75           C  
ANISOU 1285  CG  PHE A 491    10892  37257  10648  -3686    361  -2653       C  
ATOM   1286  CD1 PHE A 491     -32.790 -18.058 -77.920  1.00164.83           C  
ANISOU 1286  CD1 PHE A 491    12240  38359  12028  -3434    318  -2484       C  
ATOM   1287  CD2 PHE A 491     -34.236 -19.525 -79.120  1.00163.91           C  
ANISOU 1287  CD2 PHE A 491    12007  38520  11751  -3842    392  -2795       C  
ATOM   1288  CE1 PHE A 491     -33.691 -18.024 -76.871  1.00142.67           C  
ANISOU 1288  CE1 PHE A 491     9457  35486   9263  -3338    308  -2455       C  
ATOM   1289  CE2 PHE A 491     -35.143 -19.491 -78.077  1.00146.12           C  
ANISOU 1289  CE2 PHE A 491     9777  36203   9540  -3743    379  -2765       C  
ATOM   1290  CZ  PHE A 491     -34.869 -18.741 -76.951  1.00144.01           C  
ANISOU 1290  CZ  PHE A 491     9578  35766   9373  -3490    338  -2596       C  
ATOM   1291  N   THR A 492     -33.731 -18.814 -83.005  1.00163.13           N  
ANISOU 1291  N   THR A 492    11712  38899  11369  -4241    377  -2725       N  
ATOM   1292  CA  THR A 492     -34.961 -19.290 -83.607  1.00164.16           C  
ANISOU 1292  CA  THR A 492    11759  39217  11396  -4444    397  -2817       C  
ATOM   1293  C   THR A 492     -35.227 -20.708 -83.109  1.00156.38           C  
ANISOU 1293  C   THR A 492    10806  38192  10421  -4598    480  -3107       C  
ATOM   1294  O   THR A 492     -34.598 -21.185 -82.159  1.00161.39           O  
ANISOU 1294  O   THR A 492    11516  38647  11156  -4511    513  -3199       O  
ATOM   1295  CB  THR A 492     -34.861 -19.226 -85.132  1.00171.37           C  
ANISOU 1295  CB  THR A 492    12576  40353  12185  -4652    419  -2827       C  
ATOM   1296  OG1 THR A 492     -33.772 -20.045 -85.576  1.00185.18           O  
ANISOU 1296  OG1 THR A 492    14360  42085  13917  -4799    486  -3033       O  
ATOM   1297  CG2 THR A 492     -34.629 -17.794 -85.592  1.00171.96           C  
ANISOU 1297  CG2 THR A 492    12603  40476  12258  -4498    364  -2532       C  
ATOM   1298  N   ALA A 493     -36.165 -21.402 -83.754  1.00156.33           N  
ANISOU 1298  N   ALA A 493    10731  38357  10312  -4840    521  -3254       N  
ATOM   1299  CA  ALA A 493     -36.411 -22.796 -83.407  1.00156.92           C  
ANISOU 1299  CA  ALA A 493    10828  38402  10392  -5026    616  -3550       C  
ATOM   1300  C   ALA A 493     -35.251 -23.706 -83.789  1.00161.36           C  
ANISOU 1300  C   ALA A 493    11529  38773  11007  -5122    777  -3737       C  
ATOM   1301  O   ALA A 493     -35.207 -24.852 -83.328  1.00157.27           O  
ANISOU 1301  O   ALA A 493    11171  37996  10589  -5168    956  -3927       O  
ATOM   1302  CB  ALA A 493     -37.697 -23.286 -84.075  1.00159.43           C  
ANISOU 1302  CB  ALA A 493    11064  38924  10589  -5265    641  -3651       C  
ATOM   1303  N   VAL A 494     -34.315 -23.225 -84.601  1.00160.73           N  
ANISOU 1303  N   VAL A 494    11447  38733  10889  -5120    762  -3662       N  
ATOM   1304  CA  VAL A 494     -33.192 -24.038 -85.059  1.00157.80           C  
ANISOU 1304  CA  VAL A 494    11267  38120  10571  -5181    951  -3811       C  
ATOM   1305  C   VAL A 494     -32.036 -24.001 -84.068  1.00155.41           C  
ANISOU 1305  C   VAL A 494    11147  37436  10464  -4908   1036  -3742       C  
ATOM   1306  O   VAL A 494     -31.503 -25.044 -83.679  1.00155.26           O  
ANISOU 1306  O   VAL A 494    11311  37107  10574  -4899   1237  -3895       O  
ATOM   1307  CB  VAL A 494     -32.744 -23.574 -86.460  1.00171.43           C  
ANISOU 1307  CB  VAL A 494    12910  40072  12152  -5324    906  -3771       C  
ATOM   1308  CG1 VAL A 494     -31.539 -24.375 -86.928  1.00159.84           C  
ANISOU 1308  CG1 VAL A 494    11653  38348  10732  -5373   1104  -3921       C  
ATOM   1309  CG2 VAL A 494     -33.889 -23.696 -87.452  1.00194.02           C  
ANISOU 1309  CG2 VAL A 494    15578  43308  14832  -5613    847  -3840       C  
ATOM   1310  N   GLY A 495     -31.622 -22.811 -83.651  1.00160.87           N  
ANISOU 1310  N   GLY A 495    11786  38148  11189  -4685    895  -3506       N  
ATOM   1311  CA  GLY A 495     -30.509 -22.703 -82.727  1.00151.44           C  
ANISOU 1311  CA  GLY A 495    10746  36619  10176  -4434    966  -3426       C  
ATOM   1312  C   GLY A 495     -30.209 -21.253 -82.422  1.00163.39           C  
ANISOU 1312  C   GLY A 495    12171  38224  11685  -4227    783  -3159       C  
ATOM   1313  O   GLY A 495     -30.914 -20.340 -82.862  1.00190.10           O  
ANISOU 1313  O   GLY A 495    15372  41919  14939  -4262    606  -3029       O  
ATOM   1314  N   ASP A 496     -29.138 -21.055 -81.657  1.00167.97           N  
ANISOU 1314  N   ASP A 496    12875  38529  12415  -4010    834  -3073       N  
ATOM   1315  CA  ASP A 496     -28.743 -19.719 -81.238  1.00169.32           C  
ANISOU 1315  CA  ASP A 496    12992  38739  12602  -3802    681  -2825       C  
ATOM   1316  C   ASP A 496     -27.956 -19.011 -82.333  1.00173.19           C  
ANISOU 1316  C   ASP A 496    13426  39381  12998  -3844    624  -2737       C  
ATOM   1317  O   ASP A 496     -27.279 -19.639 -83.152  1.00148.10           O  
ANISOU 1317  O   ASP A 496    10317  36156   9797  -3970    746  -2865       O  
ATOM   1318  CB  ASP A 496     -27.902 -19.777 -79.962  1.00146.27           C  
ANISOU 1318  CB  ASP A 496    10219  35475   9882  -3566    758  -2765       C  
ATOM   1319  CG  ASP A 496     -28.678 -20.304 -78.773  1.00160.63           C  
ANISOU 1319  CG  ASP A 496    12085  37138  11809  -3497    803  -2813       C  
ATOM   1320  OD1 ASP A 496     -29.795 -20.826 -78.970  1.00158.40           O  
ANISOU 1320  OD1 ASP A 496    11745  36984  11455  -3649    806  -2931       O  
ATOM   1321  OD2 ASP A 496     -28.169 -20.192 -77.639  1.00180.34           O  
ANISOU 1321  OD2 ASP A 496    14672  39388  14461  -3298    837  -2732       O  
ATOM   1322  N   GLY A 497     -28.054 -17.684 -82.339  1.00165.94           N  
ANISOU 1322  N   GLY A 497    12384  38640  12028  -3737    447  -2514       N  
ATOM   1323  CA  GLY A 497     -27.263 -16.862 -83.221  1.00146.54           C  
ANISOU 1323  CA  GLY A 497     9869  36302   9509  -3741    391  -2395       C  
ATOM   1324  C   GLY A 497     -26.046 -16.310 -82.508  1.00152.51           C  
ANISOU 1324  C   GLY A 497    10733  36827  10385  -3518    399  -2266       C  
ATOM   1325  O   GLY A 497     -25.796 -16.609 -81.336  1.00143.04           O  
ANISOU 1325  O   GLY A 497     9652  35373   9324  -3365    457  -2271       O  
ATOM   1326  N   PRO A 498     -25.259 -15.487 -83.205  1.00150.53           N  
ANISOU 1326  N   PRO A 498    10440  36665  10091  -3502    349  -2143       N  
ATOM   1327  CA  PRO A 498     -24.061 -14.932 -82.582  1.00143.03           C  
ANISOU 1327  CA  PRO A 498     9584  35514   9247  -3305    356  -2020       C  
ATOM   1328  C   PRO A 498     -24.428 -13.868 -81.564  1.00141.32           C  
ANISOU 1328  C   PRO A 498     9316  35306   9074  -3110    214  -1815       C  
ATOM   1329  O   PRO A 498     -25.475 -13.209 -81.683  1.00141.69           O  
ANISOU 1329  O   PRO A 498     9340  35390   9107  -3086    175  -1689       O  
ATOM   1330  CB  PRO A 498     -23.291 -14.331 -83.771  1.00148.65           C  
ANISOU 1330  CB  PRO A 498    10244  36362   9873  -3378    337  -1954       C  
ATOM   1331  CG  PRO A 498     -24.354 -13.996 -84.758  1.00145.73           C  
ANISOU 1331  CG  PRO A 498     9693  36312   9367  -3545    252  -1930       C  
ATOM   1332  CD  PRO A 498     -25.409 -15.059 -84.607  1.00146.57           C  
ANISOU 1332  CD  PRO A 498     9799  36443   9449  -3672    301  -2114       C  
ATOM   1333  N   PRO A 499     -23.604 -13.672 -80.540  1.00139.54           N  
ANISOU 1333  N   PRO A 499     9208  34837   8974  -2922    242  -1743       N  
ATOM   1334  CA  PRO A 499     -23.885 -12.626 -79.554  1.00137.96           C  
ANISOU 1334  CA  PRO A 499     9028  34554   8836  -2724    153  -1538       C  
ATOM   1335  C   PRO A 499     -23.422 -11.258 -80.029  1.00137.82           C  
ANISOU 1335  C   PRO A 499     9009  34534   8821  -2640    106  -1313       C  
ATOM   1336  O   PRO A 499     -22.474 -11.125 -80.806  1.00138.35           O  
ANISOU 1336  O   PRO A 499     9050  34668   8850  -2697    116  -1315       O  
ATOM   1337  CB  PRO A 499     -23.085 -13.081 -78.329  1.00156.53           C  
ANISOU 1337  CB  PRO A 499    11499  36649  11325  -2584    221  -1570       C  
ATOM   1338  CG  PRO A 499     -21.918 -13.800 -78.918  1.00136.95           C  
ANISOU 1338  CG  PRO A 499     9093  34051   8889  -2647    361  -1683       C  
ATOM   1339  CD  PRO A 499     -22.431 -14.483 -80.165  1.00138.99           C  
ANISOU 1339  CD  PRO A 499     9295  34481   9033  -2870    405  -1842       C  
ATOM   1340  N   SER A 500     -24.115 -10.231 -79.547  1.00137.16           N  
ANISOU 1340  N   SER A 500     8951  34380   8782  -2507     60  -1122       N  
ATOM   1341  CA  SER A 500     -23.750  -8.863 -79.868  1.00136.96           C  
ANISOU 1341  CA  SER A 500     8916  34342   8781  -2418     23   -900       C  
ATOM   1342  C   SER A 500     -22.409  -8.509 -79.232  1.00135.51           C  
ANISOU 1342  C   SER A 500     8811  34012   8666  -2295     19   -837       C  
ATOM   1343  O   SER A 500     -21.919  -9.225 -78.355  1.00134.50           O  
ANISOU 1343  O   SER A 500     8740  33780   8583  -2249     43   -936       O  
ATOM   1344  CB  SER A 500     -24.833  -7.903 -79.380  1.00143.27           C  
ANISOU 1344  CB  SER A 500     9695  35099   9641  -2305      4   -721       C  
ATOM   1345  OG  SER A 500     -25.018  -8.023 -77.980  1.00153.65           O  
ANISOU 1345  OG  SER A 500    11158  36242  10981  -2165    -25   -722       O  
ATOM   1346  N   PRO A 501     -21.779  -7.420 -79.675  1.00135.50           N  
ANISOU 1346  N   PRO A 501     8792  34015   8677  -2249      0   -672       N  
ATOM   1347  CA  PRO A 501     -20.600  -6.926 -78.959  1.00134.10           C  
ANISOU 1347  CA  PRO A 501     8692  33691   8568  -2121    -10   -586       C  
ATOM   1348  C   PRO A 501     -20.964  -6.551 -77.531  1.00141.69           C  
ANISOU 1348  C   PRO A 501     9750  34471   9613  -1955    -29   -498       C  
ATOM   1349  O   PRO A 501     -22.077  -6.103 -77.249  1.00133.51           O  
ANISOU 1349  O   PRO A 501     8728  33424   8574  -1909    -51   -421       O  
ATOM   1350  CB  PRO A 501     -20.174  -5.698 -79.772  1.00134.62           C  
ANISOU 1350  CB  PRO A 501     8700  33819   8633  -2117    -18   -409       C  
ATOM   1351  CG  PRO A 501     -20.722  -5.942 -81.133  1.00136.52           C  
ANISOU 1351  CG  PRO A 501     8834  34272   8766  -2285      6   -467       C  
ATOM   1352  CD  PRO A 501     -22.017  -6.673 -80.923  1.00136.94           C  
ANISOU 1352  CD  PRO A 501     8867  34361   8803  -2332     14   -569       C  
ATOM   1353  N   THR A 502     -20.012  -6.754 -76.622  1.00135.48           N  
ANISOU 1353  N   THR A 502     9032  33557   8887  -1869    -15   -511       N  
ATOM   1354  CA  THR A 502     -20.263  -6.455 -75.219  1.00129.75           C  
ANISOU 1354  CA  THR A 502     8395  32667   8239  -1722    -18   -437       C  
ATOM   1355  C   THR A 502     -20.506  -4.963 -75.031  1.00129.35           C  
ANISOU 1355  C   THR A 502     8405  32559   8182  -1618    -27   -214       C  
ATOM   1356  O   THR A 502     -19.822  -4.124 -75.622  1.00129.62           O  
ANISOU 1356  O   THR A 502     8445  32619   8185  -1617    -13   -100       O  
ATOM   1357  CB  THR A 502     -19.086  -6.905 -74.351  1.00128.66           C  
ANISOU 1357  CB  THR A 502     8297  32423   8167  -1657      1   -478       C  
ATOM   1358  OG1 THR A 502     -17.898  -6.216 -74.757  1.00151.39           O  
ANISOU 1358  OG1 THR A 502    11176  35303  11044  -1643     -8   -382       O  
ATOM   1359  CG2 THR A 502     -18.867  -8.405 -74.482  1.00129.14           C  
ANISOU 1359  CG2 THR A 502     8314  32553   8202  -1753     40   -699       C  
ATOM   1360  N   ILE A 503     -21.505  -4.638 -74.214  1.00128.78           N  
ANISOU 1360  N   ILE A 503     8369  32429   8133  -1537     14   -150       N  
ATOM   1361  CA  ILE A 503     -21.847  -3.262 -73.899  1.00128.42           C  
ANISOU 1361  CA  ILE A 503     8302  32358   8133  -1439     45     56       C  
ATOM   1362  C   ILE A 503     -21.733  -3.070 -72.392  1.00135.04           C  
ANISOU 1362  C   ILE A 503     9218  33029   9063  -1311     29     98       C  
ATOM   1363  O   ILE A 503     -21.633  -4.027 -71.623  1.00126.23           O  
ANISOU 1363  O   ILE A 503     8149  31834   7978  -1300     13    -27       O  
ATOM   1364  CB  ILE A 503     -23.252  -2.875 -74.401  1.00129.44           C  
ANISOU 1364  CB  ILE A 503     8350  32621   8211  -1464     46    114       C  
ATOM   1365  CG1 ILE A 503     -24.314  -3.785 -73.779  1.00129.33           C  
ANISOU 1365  CG1 ILE A 503     8355  32594   8192  -1469     45     -9       C  
ATOM   1366  CG2 ILE A 503     -23.315  -2.935 -75.919  1.00131.08           C  
ANISOU 1366  CG2 ILE A 503     8461  33013   8330  -1596     57     95       C  
ATOM   1367  CD1 ILE A 503     -25.106  -3.131 -72.666  1.00128.51           C  
ANISOU 1367  CD1 ILE A 503     8273  32416   8140  -1343     31     99       C  
ATOM   1368  N   GLN A 504     -21.747  -1.807 -71.978  1.00149.99           N  
ANISOU 1368  N   GLN A 504    11110  34882  10999  -1220     24    278       N  
ATOM   1369  CA  GLN A 504     -21.717  -1.435 -70.571  1.00135.72           C  
ANISOU 1369  CA  GLN A 504     9365  32930   9272  -1104     14    340       C  
ATOM   1370  C   GLN A 504     -23.007  -0.709 -70.222  1.00125.27           C  
ANISOU 1370  C   GLN A 504     8013  31639   7945  -1041      5    443       C  
ATOM   1371  O   GLN A 504     -23.429   0.197 -70.948  1.00126.11           O  
ANISOU 1371  O   GLN A 504     8057  31853   8006  -1044     -3    568       O  
ATOM   1372  CB  GLN A 504     -20.506  -0.554 -70.259  1.00124.47           C  
ANISOU 1372  CB  GLN A 504     7969  31428   7896  -1054      8    459       C  
ATOM   1373  CG  GLN A 504     -20.565   0.113 -68.899  1.00133.90           C  
ANISOU 1373  CG  GLN A 504     9213  32500   9164   -942     -2    555       C  
ATOM   1374  CD  GLN A 504     -19.370   1.002 -68.641  1.00122.88           C  
ANISOU 1374  CD  GLN A 504     7837  31045   7805   -911     -9    670       C  
ATOM   1375  OE1 GLN A 504     -19.494   2.224 -68.574  1.00122.94           O  
ANISOU 1375  OE1 GLN A 504     7828  31065   7818   -868    -21    824       O  
ATOM   1376  NE2 GLN A 504     -18.202   0.392 -68.493  1.00122.49           N  
ANISOU 1376  NE2 GLN A 504     7821  30943   7776   -935     -5    599       N  
ATOM   1377  N   VAL A 505     -23.625  -1.109 -69.116  1.00124.53           N  
ANISOU 1377  N   VAL A 505     7959  31465   7894   -982      3    395       N  
ATOM   1378  CA  VAL A 505     -24.902  -0.541 -68.696  1.00124.71           C  
ANISOU 1378  CA  VAL A 505     7954  31522   7908   -918     -6    478       C  
ATOM   1379  C   VAL A 505     -24.666   0.809 -68.031  1.00124.13           C  
ANISOU 1379  C   VAL A 505     7897  31387   7880   -814    -17    661       C  
ATOM   1380  O   VAL A 505     -23.682   1.002 -67.306  1.00123.16           O  
ANISOU 1380  O   VAL A 505     7832  31144   7820   -775    -17    681       O  
ATOM   1381  CB  VAL A 505     -25.641  -1.527 -67.768  1.00124.22           C  
ANISOU 1381  CB  VAL A 505     7923  31405   7870   -904     -3    348       C  
ATOM   1382  CG1 VAL A 505     -24.682  -2.560 -67.215  1.00123.37           C  
ANISOU 1382  CG1 VAL A 505     7879  31185   7810   -924      1    210       C  
ATOM   1383  CG2 VAL A 505     -26.355  -0.805 -66.639  1.00123.64           C  
ANISOU 1383  CG2 VAL A 505     7864  31275   7838   -791    -11    450       C  
ATOM   1384  N   LYS A 506     -25.564   1.757 -68.294  1.00124.85           N  
ANISOU 1384  N   LYS A 506     7932  31566   7939   -771    -30    797       N  
ATOM   1385  CA  LYS A 506     -25.453   3.108 -67.768  1.00124.56           C  
ANISOU 1385  CA  LYS A 506     7922  31418   7985   -672    -78    972       C  
ATOM   1386  C   LYS A 506     -25.961   3.171 -66.328  1.00128.78           C  
ANISOU 1386  C   LYS A 506     8512  31809   8611   -576    -96    974       C  
ATOM   1387  O   LYS A 506     -26.564   2.231 -65.807  1.00123.39           O  
ANISOU 1387  O   LYS A 506     7836  31118   7927   -582    -78    852       O  
ATOM   1388  CB  LYS A 506     -26.237   4.084 -68.640  1.00144.90           C  
ANISOU 1388  CB  LYS A 506    10431  34099  10527   -653   -117   1120       C  
ATOM   1389  CG  LYS A 506     -26.069   3.855 -70.127  1.00165.06           C  
ANISOU 1389  CG  LYS A 506    12911  36829  12976   -761    -98   1102       C  
ATOM   1390  CD  LYS A 506     -27.109   4.630 -70.915  1.00128.47           C  
ANISOU 1390  CD  LYS A 506     8202  32311   8300   -741   -143   1237       C  
ATOM   1391  CE  LYS A 506     -26.922   4.435 -72.407  1.00171.27           C  
ANISOU 1391  CE  LYS A 506    13546  37916  13613   -857   -129   1224       C  
ATOM   1392  NZ  LYS A 506     -26.891   2.992 -72.767  1.00162.80           N  
ANISOU 1392  NZ  LYS A 506    12448  36942  12465   -975    -68   1021       N  
ATOM   1393  N   THR A 507     -25.728   4.313 -65.689  1.00123.29           N  
ANISOU 1393  N   THR A 507     7851  31003   7989   -491   -135   1113       N  
ATOM   1394  CA  THR A 507     -26.082   4.528 -64.295  1.00142.51           C  
ANISOU 1394  CA  THR A 507    10335  33303  10509   -401   -153   1130       C  
ATOM   1395  C   THR A 507     -27.271   5.474 -64.185  1.00139.24           C  
ANISOU 1395  C   THR A 507     9881  32910  10113   -313   -191   1264       C  
ATOM   1396  O   THR A 507     -27.573   6.240 -65.104  1.00139.04           O  
ANISOU 1396  O   THR A 507     9804  32976  10049   -307   -217   1382       O  
ATOM   1397  CB  THR A 507     -24.894   5.097 -63.511  1.00138.39           C  
ANISOU 1397  CB  THR A 507     9887  32641  10053   -375   -170   1182       C  
ATOM   1398  OG1 THR A 507     -24.538   6.378 -64.046  1.00122.11           O  
ANISOU 1398  OG1 THR A 507     7820  30588   7988   -355   -209   1342       O  
ATOM   1399  CG2 THR A 507     -23.698   4.163 -63.613  1.00120.95           C  
ANISOU 1399  CG2 THR A 507     7707  30417   7832   -453   -134   1061       C  
ATOM   1400  N   GLN A 508     -27.949   5.406 -63.040  1.00125.95           N  
ANISOU 1400  N   GLN A 508     8215  31147   8491   -242   -196   1248       N  
ATOM   1401  CA  GLN A 508     -29.036   6.335 -62.764  1.00123.45           C  
ANISOU 1401  CA  GLN A 508     7856  30841   8207   -141   -229   1381       C  
ATOM   1402  C   GLN A 508     -28.491   7.753 -62.670  1.00123.56           C  
ANISOU 1402  C   GLN A 508     7898  30804   8247    -79   -270   1556       C  
ATOM   1403  O   GLN A 508     -27.479   8.000 -62.007  1.00170.41           O  
ANISOU 1403  O   GLN A 508    13908  36627  14214    -82   -277   1558       O  
ATOM   1404  CB  GLN A 508     -29.752   5.949 -61.472  1.00136.09           C  
ANISOU 1404  CB  GLN A 508     9467  32361   9878    -81   -216   1320       C  
ATOM   1405  CG  GLN A 508     -30.405   4.582 -61.506  1.00158.48           C  
ANISOU 1405  CG  GLN A 508    12277  35241  12695   -140   -180   1150       C  
ATOM   1406  CD  GLN A 508     -31.089   4.229 -60.200  1.00122.33           C  
ANISOU 1406  CD  GLN A 508     7707  30573   8201    -81   -160   1091       C  
ATOM   1407  OE1 GLN A 508     -32.121   4.801 -59.850  1.00157.26           O  
ANISOU 1407  OE1 GLN A 508    12075  35001  12675      2   -167   1173       O  
ATOM   1408  NE2 GLN A 508     -30.514   3.282 -59.471  1.00121.30           N  
ANISOU 1408  NE2 GLN A 508     7635  30360   8094   -122   -130    953       N  
ATOM   1409  N   GLN A 509     -29.172   8.685 -63.335  1.00124.77           N  
ANISOU 1409  N   GLN A 509     7987  31039   8379    -25   -302   1707       N  
ATOM   1410  CA  GLN A 509     -28.655  10.030 -63.555  1.00161.22           C  
ANISOU 1410  CA  GLN A 509    12624  35636  12998     21   -344   1882       C  
ATOM   1411  C   GLN A 509     -28.375  10.769 -62.251  1.00168.07           C  
ANISOU 1411  C   GLN A 509    13560  36370  13928    101   -365   1945       C  
ATOM   1412  O   GLN A 509     -27.214  11.006 -61.905  1.00196.26           O  
ANISOU 1412  O   GLN A 509    17217  39848  17505     65   -375   1939       O  
ATOM   1413  CB  GLN A 509     -29.632  10.830 -64.423  1.00197.54           C  
ANISOU 1413  CB  GLN A 509    17132  40356  17568     81   -374   2040       C  
ATOM   1414  CG  GLN A 509     -29.717  10.361 -65.876  1.00198.74           C  
ANISOU 1414  CG  GLN A 509    17221  40655  17636    -11   -368   2011       C  
ATOM   1415  CD  GLN A 509     -30.435   9.032 -66.033  1.00187.04           C  
ANISOU 1415  CD  GLN A 509    15698  39244  16126    -75   -333   1847       C  
ATOM   1416  OE1 GLN A 509     -31.351   8.714 -65.275  1.00191.38           O  
ANISOU 1416  OE1 GLN A 509    16227  39769  16721    -21   -327   1809       O  
ATOM   1417  NE2 GLN A 509     -30.014   8.245 -67.018  1.00171.88           N  
ANISOU 1417  NE2 GLN A 509    13762  37415  14128   -195   -309   1745       N  
ATOM   1418  N   GLY A 510     -29.421  11.140 -61.524  1.00162.28           N  
ANISOU 1418  N   GLY A 510    12788  35631  13239    206   -372   2006       N  
ATOM   1419  CA  GLY A 510     -29.248  11.892 -60.301  1.00168.93           C  
ANISOU 1419  CA  GLY A 510    13691  36368  14125    284   -393   2074       C  
ATOM   1420  C   GLY A 510     -29.144  11.065 -59.040  1.00155.18           C  
ANISOU 1420  C   GLY A 510    12001  34533  12427    270   -368   1930       C  
ATOM   1421  O   GLY A 510     -29.140  11.632 -57.943  1.00137.58           O  
ANISOU 1421  O   GLY A 510     9883  32136  10254    328   -342   1968       O  
ATOM   1422  N   VAL A 511     -29.060   9.749 -59.158  1.00164.95           N  
ANISOU 1422  N   VAL A 511    13232  35777  13664    188   -327   1758       N  
ATOM   1423  CA  VAL A 511     -28.950   8.895 -57.971  1.00150.15           C  
ANISOU 1423  CA  VAL A 511    11402  33817  11832    174   -301   1622       C  
ATOM   1424  C   VAL A 511     -27.541   9.011 -57.399  1.00150.78           C  
ANISOU 1424  C   VAL A 511    11610  33785  11896    125   -327   1603       C  
ATOM   1425  O   VAL A 511     -26.558   8.968 -58.161  1.00150.81           O  
ANISOU 1425  O   VAL A 511    11645  33787  11870     51   -331   1596       O  
ATOM   1426  CB  VAL A 511     -29.291   7.447 -58.327  1.00121.27           C  
ANISOU 1426  CB  VAL A 511     7706  30203   8168    103   -250   1450       C  
ATOM   1427  CG1 VAL A 511     -28.477   6.474 -57.495  1.00120.07           C  
ANISOU 1427  CG1 VAL A 511     7628  29959   8033     46   -228   1306       C  
ATOM   1428  CG2 VAL A 511     -30.780   7.195 -58.134  1.00121.91           C  
ANISOU 1428  CG2 VAL A 511     7696  30331   8292    161   -219   1436       C  
ATOM   1429  N   PRO A 512     -27.387   9.174 -56.090  1.00138.89           N  
ANISOU 1429  N   PRO A 512    10252  32072  10450    153   -291   1585       N  
ATOM   1430  CA  PRO A 512     -26.055   9.351 -55.507  1.00123.99           C  
ANISOU 1430  CA  PRO A 512     8514  30046   8550     99   -310   1576       C  
ATOM   1431  C   PRO A 512     -25.290   8.035 -55.434  1.00118.34           C  
ANISOU 1431  C   PRO A 512     7777  29372   7816     17   -318   1426       C  
ATOM   1432  O   PRO A 512     -25.828   6.947 -55.646  1.00118.23           O  
ANISOU 1432  O   PRO A 512     7662  29454   7808      2   -291   1314       O  
ATOM   1433  CB  PRO A 512     -26.349   9.895 -54.103  1.00119.02           C  
ANISOU 1433  CB  PRO A 512     8067  29155   7999    153   -243   1597       C  
ATOM   1434  CG  PRO A 512     -27.803  10.287 -54.114  1.00129.64           C  
ANISOU 1434  CG  PRO A 512     9355  30505   9400    250   -188   1653       C  
ATOM   1435  CD  PRO A 512     -28.452   9.372 -55.095  1.00134.13           C  
ANISOU 1435  CD  PRO A 512     9714  31311   9938    235   -210   1589       C  
ATOM   1436  N   ALA A 513     -24.008   8.160 -55.108  1.00117.83           N  
ANISOU 1436  N   ALA A 513     7811  29227   7734    -37   -351   1428       N  
ATOM   1437  CA  ALA A 513     -23.103   7.023 -55.062  1.00117.15           C  
ANISOU 1437  CA  ALA A 513     7720  29136   7656   -108   -344   1306       C  
ATOM   1438  C   ALA A 513     -23.168   6.321 -53.709  1.00116.48           C  
ANISOU 1438  C   ALA A 513     7738  28903   7615    -98   -308   1217       C  
ATOM   1439  O   ALA A 513     -23.639   6.873 -52.711  1.00116.47           O  
ANISOU 1439  O   ALA A 513     7867  28727   7660    -52   -272   1252       O  
ATOM   1440  CB  ALA A 513     -21.667   7.468 -55.344  1.00117.05           C  
ANISOU 1440  CB  ALA A 513     7767  29061   7644   -171   -372   1352       C  
ATOM   1441  N   GLN A 514     -22.691   5.081 -53.699  1.00116.00           N  
ANISOU 1441  N   GLN A 514     7636  28882   7558   -143   -297   1098       N  
ATOM   1442  CA  GLN A 514     -22.518   4.339 -52.461  1.00115.40           C  
ANISOU 1442  CA  GLN A 514     7673  28638   7535   -142   -255   1016       C  
ATOM   1443  C   GLN A 514     -21.655   5.151 -51.497  1.00115.20           C  
ANISOU 1443  C   GLN A 514     7818  28439   7514   -153   -292   1092       C  
ATOM   1444  O   GLN A 514     -20.578   5.622 -51.887  1.00115.26           O  
ANISOU 1444  O   GLN A 514     7824  28488   7484   -198   -357   1152       O  
ATOM   1445  CB  GLN A 514     -21.858   2.989 -52.755  1.00115.06           C  
ANISOU 1445  CB  GLN A 514     7554  28674   7490   -191   -245    901       C  
ATOM   1446  CG  GLN A 514     -21.939   1.962 -51.641  1.00114.58           C  
ANISOU 1446  CG  GLN A 514     7578  28471   7486   -181   -187    801       C  
ATOM   1447  CD  GLN A 514     -21.346   0.626 -52.056  1.00114.42           C  
ANISOU 1447  CD  GLN A 514     7472  28532   7470   -221   -163    693       C  
ATOM   1448  OE1 GLN A 514     -20.338   0.575 -52.761  1.00154.89           O  
ANISOU 1448  OE1 GLN A 514    12532  33756  12564   -261   -206    708       O  
ATOM   1449  NE2 GLN A 514     -21.977  -0.461 -51.631  1.00114.28           N  
ANISOU 1449  NE2 GLN A 514     7455  28470   7495   -209    -83    581       N  
ATOM   1450  N   PRO A 515     -22.096   5.358 -50.256  1.00115.06           N  
ANISOU 1450  N   PRO A 515     7950  28229   7537   -122   -250   1091       N  
ATOM   1451  CA  PRO A 515     -21.298   6.154 -49.316  1.00119.27           C  
ANISOU 1451  CA  PRO A 515     8656  28598   8063   -148   -285   1159       C  
ATOM   1452  C   PRO A 515     -19.930   5.535 -49.076  1.00114.64           C  
ANISOU 1452  C   PRO A 515     8084  28013   7461   -211   -341   1128       C  
ATOM   1453  O   PRO A 515     -19.761   4.313 -49.090  1.00116.74           O  
ANISOU 1453  O   PRO A 515     8286  28322   7746   -217   -323   1035       O  
ATOM   1454  CB  PRO A 515     -22.147   6.153 -48.040  1.00114.94           C  
ANISOU 1454  CB  PRO A 515     8254  27857   7559   -107   -211   1129       C  
ATOM   1455  CG  PRO A 515     -23.540   5.914 -48.519  1.00115.18           C  
ANISOU 1455  CG  PRO A 515     8178  27960   7623    -44   -142   1097       C  
ATOM   1456  CD  PRO A 515     -23.406   4.989 -49.694  1.00115.08           C  
ANISOU 1456  CD  PRO A 515     7974  28160   7591    -66   -165   1034       C  
ATOM   1457  N   ALA A 516     -18.945   6.400 -48.854  1.00114.81           N  
ANISOU 1457  N   ALA A 516     8188  27983   7450   -259   -406   1211       N  
ATOM   1458  CA  ALA A 516     -17.555   5.996 -48.723  1.00135.01           C  
ANISOU 1458  CA  ALA A 516    10742  30562   9994   -322   -473   1207       C  
ATOM   1459  C   ALA A 516     -17.069   6.183 -47.292  1.00130.17           C  
ANISOU 1459  C   ALA A 516    10313  29763   9382   -354   -494   1222       C  
ATOM   1460  O   ALA A 516     -17.526   7.076 -46.572  1.00132.30           O  
ANISOU 1460  O   ALA A 516    10731  29893   9644   -351   -473   1266       O  
ATOM   1461  CB  ALA A 516     -16.662   6.790 -49.681  1.00126.90           C  
ANISOU 1461  CB  ALA A 516     9645  29649   8922   -371   -540   1291       C  
ATOM   1462  N   ASP A 517     -16.127   5.323 -46.895  1.00133.11           N  
ANISOU 1462  N   ASP A 517    10675  30137   9762   -387   -533   1187       N  
ATOM   1463  CA  ASP A 517     -15.504   5.370 -45.570  1.00147.43           C  
ANISOU 1463  CA  ASP A 517    12648  31802  11566   -429   -572   1205       C  
ATOM   1464  C   ASP A 517     -16.552   5.285 -44.461  1.00114.40           C  
ANISOU 1464  C   ASP A 517     8618  27452   7399   -392   -500   1165       C  
ATOM   1465  O   ASP A 517     -16.507   6.023 -43.475  1.00114.68           O  
ANISOU 1465  O   ASP A 517     8828  27340   7405   -427   -510   1205       O  
ATOM   1466  CB  ASP A 517     -14.633   6.619 -45.413  1.00181.25           C  
ANISOU 1466  CB  ASP A 517    17014  36052  15800   -506   -649   1303       C  
ATOM   1467  CG  ASP A 517     -13.622   6.489 -44.286  1.00238.90           C  
ANISOU 1467  CG  ASP A 517    24427  43262  23080   -573   -719   1323       C  
ATOM   1468  OD1 ASP A 517     -13.649   5.466 -43.569  1.00254.69           O  
ANISOU 1468  OD1 ASP A 517    26453  45214  25105   -551   -706   1269       O  
ATOM   1469  OD2 ASP A 517     -12.797   7.410 -44.120  1.00255.27           O  
ANISOU 1469  OD2 ASP A 517    26564  45318  25111   -653   -789   1397       O  
ATOM   1470  N   PHE A 518     -17.502   4.370 -44.630  1.00131.70           N  
ANISOU 1470  N   PHE A 518    10743  29665   9633   -328   -419   1081       N  
ATOM   1471  CA  PHE A 518     -18.556   4.164 -43.645  1.00114.00           C  
ANISOU 1471  CA  PHE A 518     8628  27274   7414   -289   -337   1033       C  
ATOM   1472  C   PHE A 518     -17.982   3.459 -42.420  1.00125.72           C  
ANISOU 1472  C   PHE A 518    10233  28641   8892   -316   -356   1009       C  
ATOM   1473  O   PHE A 518     -17.440   2.354 -42.528  1.00113.78           O  
ANISOU 1473  O   PHE A 518     8639  27189   7403   -312   -371    966       O  
ATOM   1474  CB  PHE A 518     -19.687   3.347 -44.268  1.00113.76           C  
ANISOU 1474  CB  PHE A 518     8474  27321   7430   -224   -248    949       C  
ATOM   1475  CG  PHE A 518     -20.935   3.280 -43.432  1.00113.78           C  
ANISOU 1475  CG  PHE A 518     8583  27186   7462   -179   -151    905       C  
ATOM   1476  CD1 PHE A 518     -21.448   4.415 -42.828  1.00114.11           C  
ANISOU 1476  CD1 PHE A 518     8767  27098   7493   -174   -124    961       C  
ATOM   1477  CD2 PHE A 518     -21.615   2.082 -43.282  1.00114.24           C  
ANISOU 1477  CD2 PHE A 518     8599  27243   7564   -145    -74    804       C  
ATOM   1478  CE1 PHE A 518     -22.601   4.351 -42.070  1.00114.21           C  
ANISOU 1478  CE1 PHE A 518     8874  26982   7539   -131    -22    919       C  
ATOM   1479  CE2 PHE A 518     -22.770   2.013 -42.528  1.00113.62           C  
ANISOU 1479  CE2 PHE A 518     8613  27041   7517   -107     23    762       C  
ATOM   1480  CZ  PHE A 518     -23.263   3.149 -41.921  1.00113.95           C  
ANISOU 1480  CZ  PHE A 518     8792  26956   7549    -98     49    821       C  
ATOM   1481  N   GLN A 519     -18.091   4.100 -41.257  1.00124.68           N  
ANISOU 1481  N   GLN A 519    10300  28343   8731   -346   -353   1039       N  
ATOM   1482  CA  GLN A 519     -17.526   3.574 -40.024  1.00126.35           C  
ANISOU 1482  CA  GLN A 519    10647  28442   8920   -382   -383   1031       C  
ATOM   1483  C   GLN A 519     -18.539   3.683 -38.892  1.00114.47           C  
ANISOU 1483  C   GLN A 519     9326  26755   7411   -366   -293    996       C  
ATOM   1484  O   GLN A 519     -19.485   4.475 -38.944  1.00124.79           O  
ANISOU 1484  O   GLN A 519    10684  28004   8727   -340   -222   1000       O  
ATOM   1485  CB  GLN A 519     -16.231   4.306 -39.635  1.00122.18           C  
ANISOU 1485  CB  GLN A 519    10193  27900   8329   -474   -501   1116       C  
ATOM   1486  CG  GLN A 519     -15.100   4.192 -40.654  1.00153.77           C  
ANISOU 1486  CG  GLN A 519    14017  32074  12335   -498   -590   1155       C  
ATOM   1487  CD  GLN A 519     -14.429   2.827 -40.663  1.00178.39           C  
ANISOU 1487  CD  GLN A 519    17032  35260  15489   -477   -616   1122       C  
ATOM   1488  OE1 GLN A 519     -14.984   1.837 -40.185  1.00201.90           O  
ANISOU 1488  OE1 GLN A 519    20034  38180  18500   -427   -551   1057       O  
ATOM   1489  NE2 GLN A 519     -13.219   2.772 -41.208  1.00174.59           N  
ANISOU 1489  NE2 GLN A 519    16434  34895  15006   -513   -704   1170       N  
ATOM   1490  N   ALA A 520     -18.318   2.869 -37.861  1.00114.52           N  
ANISOU 1490  N   ALA A 520     9434  26671   7407   -379   -294    967       N  
ATOM   1491  CA  ALA A 520     -19.151   2.842 -36.666  1.00129.98           C  
ANISOU 1491  CA  ALA A 520    11583  28451   9354   -374   -209    931       C  
ATOM   1492  C   ALA A 520     -18.257   2.899 -35.437  1.00124.95           C  
ANISOU 1492  C   ALA A 520    11123  27710   8642   -453   -287    973       C  
ATOM   1493  O   ALA A 520     -17.276   2.153 -35.344  1.00125.54           O  
ANISOU 1493  O   ALA A 520    11144  27846   8710   -472   -371    991       O  
ATOM   1494  CB  ALA A 520     -20.027   1.585 -36.623  1.00114.35           C  
ANISOU 1494  CB  ALA A 520     9550  26463   7437   -302   -108    837       C  
ATOM   1495  N   GLU A 521     -18.598   3.779 -34.498  1.00115.67           N  
ANISOU 1495  N   GLU A 521    10156  26380   7412   -501   -256    989       N  
ATOM   1496  CA  GLU A 521     -17.826   3.979 -33.278  1.00133.75           C  
ANISOU 1496  CA  GLU A 521    12638  28568   9613   -596   -329   1029       C  
ATOM   1497  C   GLU A 521     -18.740   3.782 -32.078  1.00136.40           C  
ANISOU 1497  C   GLU A 521    13177  28721   9926   -592   -222    978       C  
ATOM   1498  O   GLU A 521     -19.765   4.462 -31.955  1.00131.45           O  
ANISOU 1498  O   GLU A 521    12636  27994   9314   -570   -109    951       O  
ATOM   1499  CB  GLU A 521     -17.193   5.372 -33.253  1.00159.68           C  
ANISOU 1499  CB  GLU A 521    16007  31835  12829   -690   -399   1101       C  
ATOM   1500  CG  GLU A 521     -16.286   5.633 -32.060  1.00193.15           C  
ANISOU 1500  CG  GLU A 521    20434  35993  16963   -810   -493   1145       C  
ATOM   1501  CD  GLU A 521     -14.903   5.027 -32.221  1.00202.00           C  
ANISOU 1501  CD  GLU A 521    21435  37250  18066   -849   -645   1199       C  
ATOM   1502  OE1 GLU A 521     -14.657   4.342 -33.237  1.00193.88           O  
ANISOU 1502  OE1 GLU A 521    20185  36366  17113   -778   -665   1194       O  
ATOM   1503  OE2 GLU A 521     -14.057   5.242 -31.329  1.00201.42           O  
ANISOU 1503  OE2 GLU A 521    21487  37139  17903   -954   -744   1247       O  
ATOM   1504  N   VAL A 522     -18.369   2.856 -31.198  1.00134.23           N  
ANISOU 1504  N   VAL A 522    12979  28402   9620   -610   -251    969       N  
ATOM   1505  CA  VAL A 522     -19.151   2.575 -29.998  1.00143.25           C  
ANISOU 1505  CA  VAL A 522    14325  29372  10732   -614   -153    922       C  
ATOM   1506  C   VAL A 522     -18.897   3.676 -28.976  1.00119.75           C  
ANISOU 1506  C   VAL A 522    11593  26263   7645   -728   -177    960       C  
ATOM   1507  O   VAL A 522     -17.759   3.890 -28.546  1.00118.50           O  
ANISOU 1507  O   VAL A 522    11491  26130   7402   -822   -312   1024       O  
ATOM   1508  CB  VAL A 522     -18.805   1.196 -29.421  1.00128.98           C  
ANISOU 1508  CB  VAL A 522    12520  27564   8922   -595   -178    909       C  
ATOM   1509  CG1 VAL A 522     -19.509   0.987 -28.088  1.00117.61           C  
ANISOU 1509  CG1 VAL A 522    11317  25940   7432   -617    -84    870       C  
ATOM   1510  CG2 VAL A 522     -19.180   0.100 -30.407  1.00128.22           C  
ANISOU 1510  CG2 VAL A 522    12202  27577   8937   -488   -124    855       C  
ATOM   1511  N   GLU A 523     -19.960   4.372 -28.582  1.00124.81           N  
ANISOU 1511  N   GLU A 523    12376  26761   8285   -722    -43    920       N  
ATOM   1512  CA  GLU A 523     -19.877   5.453 -27.609  1.00131.11           C  
ANISOU 1512  CA  GLU A 523    13425  27409   8982   -831    -32    940       C  
ATOM   1513  C   GLU A 523     -20.187   4.995 -26.191  1.00139.22           C  
ANISOU 1513  C   GLU A 523    14684  28279   9934   -876     24    905       C  
ATOM   1514  O   GLU A 523     -19.521   5.427 -25.246  1.00123.35           O  
ANISOU 1514  O   GLU A 523    12866  26198   7802   -999    -46    939       O  
ATOM   1515  CB  GLU A 523     -20.831   6.587 -28.001  1.00131.21           C  
ANISOU 1515  CB  GLU A 523    13470  27344   9040   -798     96    925       C  
ATOM   1516  CG  GLU A 523     -20.575   7.163 -29.389  1.00168.32           C  
ANISOU 1516  CG  GLU A 523    17960  32191  13803   -758     46    969       C  
ATOM   1517  CD  GLU A 523     -19.334   8.037 -29.448  1.00171.12           C  
ANISOU 1517  CD  GLU A 523    18353  32589  14075   -874    -90   1043       C  
ATOM   1518  OE1 GLU A 523     -19.448   9.254 -29.187  1.00168.13           O  
ANISOU 1518  OE1 GLU A 523    18125  32103  13655   -936    -46   1063       O  
ATOM   1519  OE2 GLU A 523     -18.243   7.508 -29.750  1.00171.33           O  
ANISOU 1519  OE2 GLU A 523    18261  32756  14082   -905   -235   1081       O  
ATOM   1520  N   SER A 524     -21.174   4.122 -26.024  1.00133.14           N  
ANISOU 1520  N   SER A 524    13902  27457   9229   -788    147    838       N  
ATOM   1521  CA  SER A 524     -21.563   3.642 -24.706  1.00123.36           C  
ANISOU 1521  CA  SER A 524    12883  26063   7924   -824    217    801       C  
ATOM   1522  C   SER A 524     -22.341   2.341 -24.891  1.00127.73           C  
ANISOU 1522  C   SER A 524    13327  26633   8573   -713    311    737       C  
ATOM   1523  O   SER A 524     -22.261   1.703 -25.947  1.00130.80           O  
ANISOU 1523  O   SER A 524    13475  27168   9054   -631    281    732       O  
ATOM   1524  CB  SER A 524     -22.368   4.719 -23.958  1.00127.13           C  
ANISOU 1524  CB  SER A 524    13596  26350   8356   -875    354    769       C  
ATOM   1525  OG  SER A 524     -23.622   4.946 -24.579  1.00120.22           O  
ANISOU 1525  OG  SER A 524    12633  25445   7601   -768    513    717       O  
ATOM   1526  N   ASP A 525     -23.084   1.944 -23.859  1.00119.71           N  
ANISOU 1526  N   ASP A 525    12493  25463   7529   -719    430    685       N  
ATOM   1527  CA  ASP A 525     -23.976   0.797 -23.945  1.00119.26           C  
ANISOU 1527  CA  ASP A 525    12358  25393   7561   -623    547    614       C  
ATOM   1528  C   ASP A 525     -25.250   1.098 -24.722  1.00120.51           C  
ANISOU 1528  C   ASP A 525    12396  25550   7842   -532    698    552       C  
ATOM   1529  O   ASP A 525     -25.980   0.163 -25.068  1.00121.03           O  
ANISOU 1529  O   ASP A 525    12343  25644   7998   -451    787    490       O  
ATOM   1530  CB  ASP A 525     -24.341   0.312 -22.539  1.00135.74           C  
ANISOU 1530  CB  ASP A 525    14693  27310   9571   -668    629    583       C  
ATOM   1531  CG  ASP A 525     -24.953   1.409 -21.683  1.00136.08           C  
ANISOU 1531  CG  ASP A 525    14982  27175   9547   -736    739    561       C  
ATOM   1532  OD1 ASP A 525     -24.462   2.555 -21.743  1.00121.15           O  
ANISOU 1532  OD1 ASP A 525    13149  25282   7599   -805    675    606       O  
ATOM   1533  OD2 ASP A 525     -25.928   1.125 -20.955  1.00157.55           O  
ANISOU 1533  OD2 ASP A 525    17839  29751  12274   -722    898    497       O  
ATOM   1534  N   THR A 526     -25.536   2.372 -25.001  1.00119.00           N  
ANISOU 1534  N   THR A 526    12230  25328   7656   -544    732    569       N  
ATOM   1535  CA  THR A 526     -26.769   2.761 -25.669  1.00118.79           C  
ANISOU 1535  CA  THR A 526    12097  25295   7743   -454    875    526       C  
ATOM   1536  C   THR A 526     -26.556   3.681 -26.863  1.00127.81           C  
ANISOU 1536  C   THR A 526    13070  26561   8932   -426    813    578       C  
ATOM   1537  O   THR A 526     -27.531   4.005 -27.549  1.00142.51           O  
ANISOU 1537  O   THR A 526    14812  28445  10892   -344    914    558       O  
ATOM   1538  CB  THR A 526     -27.723   3.453 -24.680  1.00137.70           C  
ANISOU 1538  CB  THR A 526    14723  27479  10119   -475   1043    490       C  
ATOM   1539  OG1 THR A 526     -27.117   4.656 -24.191  1.00131.70           O  
ANISOU 1539  OG1 THR A 526    14145  26634   9260   -571    997    543       O  
ATOM   1540  CG2 THR A 526     -28.046   2.537 -23.505  1.00119.98           C  
ANISOU 1540  CG2 THR A 526    12652  25107   7829   -502   1122    435       C  
ATOM   1541  N   ARG A 527     -25.325   4.115 -27.132  1.00135.51           N  
ANISOU 1541  N   ARG A 527    14028  27620   9841   -491    653    649       N  
ATOM   1542  CA  ARG A 527     -25.053   5.060 -28.206  1.00134.86           C  
ANISOU 1542  CA  ARG A 527    13809  27643   9790   -475    595    705       C  
ATOM   1543  C   ARG A 527     -23.975   4.524 -29.136  1.00121.48           C  
ANISOU 1543  C   ARG A 527    11908  26150   8100   -475    431    745       C  
ATOM   1544  O   ARG A 527     -22.962   3.982 -28.684  1.00121.45           O  
ANISOU 1544  O   ARG A 527    11945  26172   8026   -537    317    768       O  
ATOM   1545  CB  ARG A 527     -24.615   6.427 -27.664  1.00122.07           C  
ANISOU 1545  CB  ARG A 527    12388  25909   8083   -570    578    757       C  
ATOM   1546  CG  ARG A 527     -25.721   7.243 -27.024  1.00136.25           C  
ANISOU 1546  CG  ARG A 527    14362  27512   9895   -558    758    727       C  
ATOM   1547  CD  ARG A 527     -25.271   8.683 -26.849  1.00171.71           C  
ANISOU 1547  CD  ARG A 527    19002  31920  14322   -640    743    783       C  
ATOM   1548  NE  ARG A 527     -26.182   9.460 -26.015  1.00198.14           N  
ANISOU 1548  NE  ARG A 527    22569  35050  17666   -648    922    752       N  
ATOM   1549  CZ  ARG A 527     -26.009  10.745 -25.721  1.00192.96           C  
ANISOU 1549  CZ  ARG A 527    22082  34275  16960   -718    959    785       C  
ATOM   1550  NH1 ARG A 527     -24.959  11.399 -26.198  1.00170.04           N  
ANISOU 1550  NH1 ARG A 527    19150  31454  14004   -789    823    851       N  
ATOM   1551  NH2 ARG A 527     -26.886  11.376 -24.953  1.00179.85           N  
ANISOU 1551  NH2 ARG A 527    20621  32408  15304   -719   1140    751       N  
ATOM   1552  N   ILE A 528     -24.205   4.685 -30.438  1.00117.11           N  
ANISOU 1552  N   ILE A 528    11130  25740   7627   -404    423    757       N  
ATOM   1553  CA  ILE A 528     -23.211   4.416 -31.472  1.00116.60           C  
ANISOU 1553  CA  ILE A 528    10866  25868   7568   -405    282    798       C  
ATOM   1554  C   ILE A 528     -23.251   5.570 -32.462  1.00116.64           C  
ANISOU 1554  C   ILE A 528    10775  25943   7598   -389    267    854       C  
ATOM   1555  O   ILE A 528     -24.323   5.921 -32.965  1.00116.63           O  
ANISOU 1555  O   ILE A 528    10707  25940   7669   -313    372    839       O  
ATOM   1556  CB  ILE A 528     -23.464   3.081 -32.202  1.00115.90           C  
ANISOU 1556  CB  ILE A 528    10568  25912   7557   -329    293    742       C  
ATOM   1557  CG1 ILE A 528     -23.383   1.902 -31.232  1.00117.61           C  
ANISOU 1557  CG1 ILE A 528    10881  26052   7752   -341    312    695       C  
ATOM   1558  CG2 ILE A 528     -22.470   2.902 -33.344  1.00115.47           C  
ANISOU 1558  CG2 ILE A 528    10309  26053   7512   -330    164    783       C  
ATOM   1559  CD1 ILE A 528     -23.622   0.558 -31.889  1.00115.38           C  
ANISOU 1559  CD1 ILE A 528    10413  25879   7546   -273    338    633       C  
ATOM   1560  N   GLN A 529     -22.093   6.164 -32.740  1.00116.76           N  
ANISOU 1560  N   GLN A 529    10784  26025   7557   -459    138    923       N  
ATOM   1561  CA  GLN A 529     -21.996   7.252 -33.704  1.00131.22           C  
ANISOU 1561  CA  GLN A 529    12527  27926   9403   -452    115    985       C  
ATOM   1562  C   GLN A 529     -21.478   6.707 -35.028  1.00139.81           C  
ANISOU 1562  C   GLN A 529    13355  29234  10532   -414     26    999       C  
ATOM   1563  O   GLN A 529     -20.393   6.116 -35.082  1.00116.02           O  
ANISOU 1563  O   GLN A 529    10287  26309   7488   -459    -87   1012       O  
ATOM   1564  CB  GLN A 529     -21.087   8.374 -33.201  1.00140.74           C  
ANISOU 1564  CB  GLN A 529    13900  29056  10519   -565     44   1051       C  
ATOM   1565  CG  GLN A 529     -21.023   9.558 -34.159  1.00162.17           C  
ANISOU 1565  CG  GLN A 529    16544  31823  13252   -558     36   1118       C  
ATOM   1566  CD  GLN A 529     -20.168  10.697 -33.643  1.00165.30           C  
ANISOU 1566  CD  GLN A 529    17116  32131  13558   -680    -20   1175       C  
ATOM   1567  OE1 GLN A 529     -20.499  11.868 -33.832  1.00151.46           O  
ANISOU 1567  OE1 GLN A 529    15433  30303  11812   -682     43   1216       O  
ATOM   1568  NE2 GLN A 529     -19.057  10.361 -32.996  1.00178.74           N  
ANISOU 1568  NE2 GLN A 529    18890  33845  15179   -786   -136   1183       N  
ATOM   1569  N   LEU A 530     -22.256   6.903 -36.087  1.00123.05           N  
ANISOU 1569  N   LEU A 530    11073  27202   8479   -332     80    999       N  
ATOM   1570  CA  LEU A 530     -21.848   6.544 -37.435  1.00115.53           C  
ANISOU 1570  CA  LEU A 530     9881  26459   7556   -303      8   1014       C  
ATOM   1571  C   LEU A 530     -21.192   7.743 -38.108  1.00115.84           C  
ANISOU 1571  C   LEU A 530     9898  26553   7564   -342    -62   1105       C  
ATOM   1572  O   LEU A 530     -21.558   8.895 -37.859  1.00116.40           O  
ANISOU 1572  O   LEU A 530    10089  26513   7624   -349    -12   1150       O  
ATOM   1573  CB  LEU A 530     -23.045   6.071 -38.264  1.00115.25           C  
ANISOU 1573  CB  LEU A 530     9676  26511   7601   -204     96    966       C  
ATOM   1574  CG  LEU A 530     -23.806   4.805 -37.852  1.00114.94           C  
ANISOU 1574  CG  LEU A 530     9617  26447   7608   -160    178    868       C  
ATOM   1575  CD1 LEU A 530     -22.849   3.666 -37.531  1.00114.59           C  
ANISOU 1575  CD1 LEU A 530     9565  26436   7538   -200    107    832       C  
ATOM   1576  CD2 LEU A 530     -24.767   5.058 -36.693  1.00115.34           C  
ANISOU 1576  CD2 LEU A 530     9857  26298   7670   -145    300    838       C  
ATOM   1577  N   SER A 531     -20.211   7.462 -38.963  1.00121.44           N  
ANISOU 1577  N   SER A 531    10455  27426   8260   -368   -169   1130       N  
ATOM   1578  CA  SER A 531     -19.489   8.511 -39.665  1.00115.86           C  
ANISOU 1578  CA  SER A 531     9714  26786   7522   -412   -240   1215       C  
ATOM   1579  C   SER A 531     -19.117   8.038 -41.062  1.00126.28           C  
ANISOU 1579  C   SER A 531    10792  28323   8866   -383   -297   1221       C  
ATOM   1580  O   SER A 531     -18.944   6.842 -41.310  1.00120.73           O  
ANISOU 1580  O   SER A 531     9970  27713   8186   -362   -313   1162       O  
ATOM   1581  CB  SER A 531     -18.225   8.941 -38.910  1.00116.26           C  
ANISOU 1581  CB  SER A 531     9902  26774   7496   -529   -337   1259       C  
ATOM   1582  OG  SER A 531     -17.268   7.896 -38.877  1.00125.32           O  
ANISOU 1582  OG  SER A 531    10965  28016   8634   -558   -428   1238       O  
ATOM   1583  N   TRP A 532     -18.998   9.002 -41.969  1.00118.85           N  
ANISOU 1583  N   TRP A 532     9787  27454   7916   -385   -318   1293       N  
ATOM   1584  CA  TRP A 532     -18.627   8.759 -43.356  1.00115.51           C  
ANISOU 1584  CA  TRP A 532     9149  27237   7502   -369   -369   1309       C  
ATOM   1585  C   TRP A 532     -18.177  10.089 -43.946  1.00129.55           C  
ANISOU 1585  C   TRP A 532    10940  29036   9246   -407   -406   1409       C  
ATOM   1586  O   TRP A 532     -18.244  11.133 -43.292  1.00149.07           O  
ANISOU 1586  O   TRP A 532    13584  31360  11696   -439   -382   1458       O  
ATOM   1587  CB  TRP A 532     -19.794   8.168 -44.149  1.00121.82           C  
ANISOU 1587  CB  TRP A 532     9796  28136   8354   -276   -297   1260       C  
ATOM   1588  CG  TRP A 532     -20.973   9.077 -44.161  1.00127.86           C  
ANISOU 1588  CG  TRP A 532    10612  28824   9145   -214   -212   1300       C  
ATOM   1589  CD1 TRP A 532     -21.279  10.010 -45.107  1.00116.12           C  
ANISOU 1589  CD1 TRP A 532     9053  27410   7658   -183   -209   1381       C  
ATOM   1590  CD2 TRP A 532     -21.995   9.167 -43.163  1.00138.29           C  
ANISOU 1590  CD2 TRP A 532    12069  29975  10499   -172   -111   1269       C  
ATOM   1591  NE1 TRP A 532     -22.434  10.668 -44.765  1.00121.36           N  
ANISOU 1591  NE1 TRP A 532     9791  27961   8360   -116   -113   1407       N  
ATOM   1592  CE2 TRP A 532     -22.894  10.168 -43.576  1.00125.91           C  
ANISOU 1592  CE2 TRP A 532    10496  28386   8960   -109    -47   1335       C  
ATOM   1593  CE3 TRP A 532     -22.241   8.492 -41.963  1.00115.66           C  
ANISOU 1593  CE3 TRP A 532     9331  26973   7643   -179    -63   1195       C  
ATOM   1594  CZ2 TRP A 532     -24.020  10.513 -42.833  1.00134.46           C  
ANISOU 1594  CZ2 TRP A 532    11688  29314  10087    -52     67   1327       C  
ATOM   1595  CZ3 TRP A 532     -23.357   8.836 -41.226  1.00133.91           C  
ANISOU 1595  CZ3 TRP A 532    11759  29131   9990   -131     50   1182       C  
ATOM   1596  CH2 TRP A 532     -24.233   9.837 -41.664  1.00138.02           C  
ANISOU 1596  CH2 TRP A 532    12264  29632  10546    -66    117   1246       C  
ATOM   1597  N   LEU A 533     -17.728  10.047 -45.196  1.00124.35           N  
ANISOU 1597  N   LEU A 533    10106  28558   8582   -407   -456   1438       N  
ATOM   1598  CA  LEU A 533     -17.281  11.246 -45.888  1.00140.09           C  
ANISOU 1598  CA  LEU A 533    12096  30589  10543   -442   -490   1535       C  
ATOM   1599  C   LEU A 533     -18.425  11.823 -46.712  1.00149.28           C  
ANISOU 1599  C   LEU A 533    13192  31795  11733   -355   -422   1578       C  
ATOM   1600  O   LEU A 533     -19.061  11.107 -47.493  1.00152.54           O  
ANISOU 1600  O   LEU A 533    13444  32342  12171   -292   -402   1539       O  
ATOM   1601  CB  LEU A 533     -16.078  10.945 -46.782  1.00157.75           C  
ANISOU 1601  CB  LEU A 533    14187  32997  12752   -498   -581   1552       C  
ATOM   1602  CG  LEU A 533     -15.359  12.177 -47.338  1.00171.74           C  
ANISOU 1602  CG  LEU A 533    15978  34793  14483   -560   -625   1652       C  
ATOM   1603  CD1 LEU A 533     -13.870  12.108 -47.036  1.00171.12           C  
ANISOU 1603  CD1 LEU A 533    15914  34732  14370   -669   -719   1664       C  
ATOM   1604  CD2 LEU A 533     -15.601  12.322 -48.833  1.00117.11           C  
ANISOU 1604  CD2 LEU A 533     8883  28051   7561   -518   -623   1691       C  
ATOM   1605  N   LEU A 534     -18.686  13.110 -46.527  1.00148.55           N  
ANISOU 1605  N   LEU A 534    13223  31586  11633   -354   -386   1660       N  
ATOM   1606  CA  LEU A 534     -19.736  13.774 -47.287  1.00154.28           C  
ANISOU 1606  CA  LEU A 534    13888  32345  12387   -264   -323   1725       C  
ATOM   1607  C   LEU A 534     -19.280  13.961 -48.731  1.00162.47           C  
ANISOU 1607  C   LEU A 534    14754  33584  13393   -271   -385   1785       C  
ATOM   1608  O   LEU A 534     -18.176  14.468 -48.966  1.00183.72           O  
ANISOU 1608  O   LEU A 534    17468  36297  16039   -353   -448   1833       O  
ATOM   1609  CB  LEU A 534     -20.081  15.120 -46.651  1.00146.73           C  
ANISOU 1609  CB  LEU A 534    13125  31190  11437   -259   -255   1801       C  
ATOM   1610  CG  LEU A 534     -21.378  15.803 -47.089  1.00141.98           C  
ANISOU 1610  CG  LEU A 534    12494  30566  10886   -143   -163   1870       C  
ATOM   1611  CD1 LEU A 534     -22.581  14.932 -46.761  1.00134.88           C  
ANISOU 1611  CD1 LEU A 534    11539  29663  10047    -55    -94   1793       C  
ATOM   1612  CD2 LEU A 534     -21.512  17.170 -46.433  1.00162.42           C  
ANISOU 1612  CD2 LEU A 534    15292  32940  13481   -150    -88   1948       C  
ATOM   1613  N   PRO A 535     -20.082  13.565 -49.714  1.00141.92           N  
ANISOU 1613  N   PRO A 535    11979  31136  10808   -195   -369   1783       N  
ATOM   1614  CA  PRO A 535     -19.644  13.644 -51.111  1.00145.92           C  
ANISOU 1614  CA  PRO A 535    12323  31848  11273   -210   -428   1833       C  
ATOM   1615  C   PRO A 535     -19.561  15.085 -51.579  1.00171.70           C  
ANISOU 1615  C   PRO A 535    15643  35080  14516   -207   -424   1970       C  
ATOM   1616  O   PRO A 535     -20.454  15.895 -51.290  1.00162.79           O  
ANISOU 1616  O   PRO A 535    14596  33834  13422   -136   -353   2034       O  
ATOM   1617  CB  PRO A 535     -20.738  12.875 -51.866  1.00169.24           C  
ANISOU 1617  CB  PRO A 535    15102  34953  14247   -131   -401   1791       C  
ATOM   1618  CG  PRO A 535     -21.944  13.008 -50.999  1.00173.71           C  
ANISOU 1618  CG  PRO A 535    15755  35370  14876    -52   -313   1780       C  
ATOM   1619  CD  PRO A 535     -21.433  12.994 -49.587  1.00163.43           C  
ANISOU 1619  CD  PRO A 535    14648  33861  13586   -102   -297   1733       C  
ATOM   1620  N   PRO A 536     -18.503  15.443 -52.303  1.00176.90           N  
ANISOU 1620  N   PRO A 536    16260  35832  15121   -279   -489   2019       N  
ATOM   1621  CA  PRO A 536     -18.369  16.821 -52.787  1.00183.79           C  
ANISOU 1621  CA  PRO A 536    17190  36671  15969   -282   -480   2154       C  
ATOM   1622  C   PRO A 536     -19.233  17.082 -54.011  1.00201.45           C  
ANISOU 1622  C   PRO A 536    19282  39059  18199   -195   -468   2233       C  
ATOM   1623  O   PRO A 536     -19.282  16.278 -54.946  1.00203.51           O  
ANISOU 1623  O   PRO A 536    19366  39525  18432   -191   -508   2195       O  
ATOM   1624  CB  PRO A 536     -16.878  16.925 -53.131  1.00179.62           C  
ANISOU 1624  CB  PRO A 536    16651  36209  15386   -400   -557   2163       C  
ATOM   1625  CG  PRO A 536     -16.493  15.529 -53.496  1.00179.92           C  
ANISOU 1625  CG  PRO A 536    16533  36410  15416   -422   -606   2056       C  
ATOM   1626  CD  PRO A 536     -17.317  14.625 -52.614  1.00183.64           C  
ANISOU 1626  CD  PRO A 536    17027  36808  15940   -365   -564   1956       C  
ATOM   1627  N   GLN A 537     -19.920  18.224 -53.986  1.00195.89           N  
ANISOU 1627  N   GLN A 537    18660  38249  17519   -128   -408   2347       N  
ATOM   1628  CA  GLN A 537     -20.707  18.727 -55.113  1.00214.44           C  
ANISOU 1628  CA  GLN A 537    20892  40725  19860    -41   -398   2459       C  
ATOM   1629  C   GLN A 537     -21.673  17.665 -55.638  1.00194.71           C  
ANISOU 1629  C   GLN A 537    18206  38400  17373     26   -406   2396       C  
ATOM   1630  O   GLN A 537     -21.655  17.279 -56.809  1.00209.47           O  
ANISOU 1630  O   GLN A 537    19907  40491  19189     20   -460   2408       O  
ATOM   1631  CB  GLN A 537     -19.789  19.240 -56.224  1.00233.32           C  
ANISOU 1631  CB  GLN A 537    23225  43248  22176   -105   -459   2542       C  
ATOM   1632  CG  GLN A 537     -18.862  20.363 -55.783  1.00241.92           C  
ANISOU 1632  CG  GLN A 537    24494  44171  23252   -180   -447   2610       C  
ATOM   1633  CD  GLN A 537     -19.616  21.593 -55.314  1.00246.82           C  
ANISOU 1633  CD  GLN A 537    25263  44594  23923   -102   -354   2721       C  
ATOM   1634  OE1 GLN A 537     -20.709  21.888 -55.797  1.00249.05           O  
ANISOU 1634  OE1 GLN A 537    25477  44916  24236     17   -314   2804       O  
ATOM   1635  NE2 GLN A 537     -19.035  22.316 -54.363  1.00244.86           N  
ANISOU 1635  NE2 GLN A 537    25219  44131  23685   -169   -316   2725       N  
ATOM   1636  N   GLU A 538     -22.531  17.200 -54.735  1.00185.53           N  
ANISOU 1636  N   GLU A 538    17082  37133  16279     83   -348   2325       N  
ATOM   1637  CA  GLU A 538     -23.510  16.161 -55.033  1.00168.23           C  
ANISOU 1637  CA  GLU A 538    14731  35079  14108    139   -342   2251       C  
ATOM   1638  C   GLU A 538     -24.807  16.532 -54.332  1.00191.37           C  
ANISOU 1638  C   GLU A 538    17716  37870  17124    250   -250   2283       C  
ATOM   1639  O   GLU A 538     -24.817  16.725 -53.112  1.00232.85           O  
ANISOU 1639  O   GLU A 538    23140  42905  22426    249   -187   2246       O  
ATOM   1640  CB  GLU A 538     -23.003  14.790 -54.574  1.00157.03           C  
ANISOU 1640  CB  GLU A 538    13290  33691  12685     68   -368   2084       C  
ATOM   1641  CG  GLU A 538     -23.970  13.639 -54.769  1.00157.89           C  
ANISOU 1641  CG  GLU A 538    13253  33920  12817    109   -351   1987       C  
ATOM   1642  CD  GLU A 538     -23.379  12.318 -54.311  1.00162.56           C  
ANISOU 1642  CD  GLU A 538    13836  34523  13406     39   -366   1830       C  
ATOM   1643  OE1 GLU A 538     -22.380  11.869 -54.912  1.00118.88           O  
ANISOU 1643  OE1 GLU A 538     8242  29110   7819    -38   -426   1795       O  
ATOM   1644  OE2 GLU A 538     -23.902  11.736 -53.337  1.00189.35           O  
ANISOU 1644  OE2 GLU A 538    17290  37800  16856     63   -312   1745       O  
ATOM   1645  N   ARG A 539     -25.892  16.643 -55.099  1.00157.28           N  
ANISOU 1645  N   ARG A 539    13253  33683  12824    342   -239   2353       N  
ATOM   1646  CA  ARG A 539     -27.157  17.127 -54.558  1.00188.17           C  
ANISOU 1646  CA  ARG A 539    17196  37474  16826    460   -146   2410       C  
ATOM   1647  C   ARG A 539     -27.758  16.133 -53.572  1.00198.80           C  
ANISOU 1647  C   ARG A 539    18560  38742  18232    469    -90   2267       C  
ATOM   1648  O   ARG A 539     -28.791  15.514 -53.847  1.00204.65           O  
ANISOU 1648  O   ARG A 539    19154  39598  19006    526    -75   2236       O  
ATOM   1649  CB  ARG A 539     -28.143  17.428 -55.689  1.00206.87           C  
ANISOU 1649  CB  ARG A 539    19377  40030  19194    554   -163   2529       C  
ATOM   1650  CG  ARG A 539     -27.730  18.606 -56.558  1.00217.33           C  
ANISOU 1650  CG  ARG A 539    20709  41395  20473    569   -195   2699       C  
ATOM   1651  CD  ARG A 539     -27.393  19.820 -55.707  1.00220.35           C  
ANISOU 1651  CD  ARG A 539    21319  41501  20901    588   -116   2779       C  
ATOM   1652  NE  ARG A 539     -26.721  20.865 -56.476  1.00213.82           N  
ANISOU 1652  NE  ARG A 539    20525  40696  20019    572   -148   2921       N  
ATOM   1653  CZ  ARG A 539     -27.314  21.969 -56.923  1.00198.90           C  
ANISOU 1653  CZ  ARG A 539    18633  38778  18160    676   -106   3098       C  
ATOM   1654  NH1 ARG A 539     -28.598  22.181 -56.676  1.00190.63           N  
ANISOU 1654  NH1 ARG A 539    17542  37683  17204    810    -30   3158       N  
ATOM   1655  NH2 ARG A 539     -26.620  22.866 -57.612  1.00182.84           N  
ANISOU 1655  NH2 ARG A 539    16640  36761  16070    650   -133   3220       N  
ATOM   1656  N   ILE A 540     -27.115  15.983 -52.419  1.00196.71           N  
ANISOU 1656  N   ILE A 540    18477  38285  17979    408    -61   2182       N  
ATOM   1657  CA  ILE A 540     -27.613  15.106 -51.368  1.00171.37           C  
ANISOU 1657  CA  ILE A 540    15317  34973  14822    412      0   2052       C  
ATOM   1658  C   ILE A 540     -28.767  15.794 -50.653  1.00154.57           C  
ANISOU 1658  C   ILE A 540    13270  32672  12788    520    120   2108       C  
ATOM   1659  O   ILE A 540     -28.699  16.987 -50.333  1.00156.35           O  
ANISOU 1659  O   ILE A 540    13635  32736  13035    552    173   2212       O  
ATOM   1660  CB  ILE A 540     -26.477  14.737 -50.394  1.00157.45           C  
ANISOU 1660  CB  ILE A 540    13722  33073  13029    306    -18   1954       C  
ATOM   1661  CG1 ILE A 540     -27.002  13.879 -49.240  1.00180.17           C  
ANISOU 1661  CG1 ILE A 540    16672  35827  15957    313     51   1830       C  
ATOM   1662  CG2 ILE A 540     -25.776  15.985 -49.872  1.00129.71           C  
ANISOU 1662  CG2 ILE A 540    10410  29372   9502    275      0   2041       C  
ATOM   1663  CD1 ILE A 540     -27.355  12.467 -49.644  1.00188.07           C  
ANISOU 1663  CD1 ILE A 540    17500  37000  16957    305     25   1714       C  
ATOM   1664  N   ILE A 541     -29.841  15.046 -50.412  1.00132.93           N  
ANISOU 1664  N   ILE A 541    10440  29962  10107    576    173   2040       N  
ATOM   1665  CA  ILE A 541     -31.036  15.578 -49.778  1.00130.40           C  
ANISOU 1665  CA  ILE A 541    10166  29494   9885    686    296   2087       C  
ATOM   1666  C   ILE A 541     -31.251  14.985 -48.391  1.00140.30           C  
ANISOU 1666  C   ILE A 541    11569  30556  11184    664    384   1959       C  
ATOM   1667  O   ILE A 541     -31.631  15.701 -47.462  1.00126.95           O  
ANISOU 1667  O   ILE A 541    10044  28641   9552    709    495   1989       O  
ATOM   1668  CB  ILE A 541     -32.276  15.362 -50.673  1.00134.57           C  
ANISOU 1668  CB  ILE A 541    10456  30219  10457    781    298   2138       C  
ATOM   1669  CG1 ILE A 541     -32.073  16.047 -52.026  1.00187.64           C  
ANISOU 1669  CG1 ILE A 541    17046  37124  17125    805    212   2283       C  
ATOM   1670  CG2 ILE A 541     -33.529  15.890 -49.991  1.00142.34           C  
ANISOU 1670  CG2 ILE A 541    11476  31050  11558    902    434   2190       C  
ATOM   1671  CD1 ILE A 541     -33.342  16.200 -52.833  1.00207.78           C  
ANISOU 1671  CD1 ILE A 541    19387  39838  19724    916    219   2381       C  
ATOM   1672  N   MET A 542     -31.012  13.685 -48.228  1.00121.61           N  
ANISOU 1672  N   MET A 542     9152  28268   8788    595    344   1816       N  
ATOM   1673  CA  MET A 542     -31.091  13.052 -46.918  1.00121.01           C  
ANISOU 1673  CA  MET A 542     9224  28015   8740    563    418   1694       C  
ATOM   1674  C   MET A 542     -30.448  11.676 -46.993  1.00135.09           C  
ANISOU 1674  C   MET A 542    10947  29913  10470    472    343   1559       C  
ATOM   1675  O   MET A 542     -30.391  11.062 -48.063  1.00151.00           O  
ANISOU 1675  O   MET A 542    12769  32154  12451    456    267   1541       O  
ATOM   1676  CB  MET A 542     -32.542  12.936 -46.427  1.00121.64           C  
ANISOU 1676  CB  MET A 542     9273  28026   8920    659    543   1678       C  
ATOM   1677  CG  MET A 542     -33.387  11.899 -47.148  1.00121.63           C  
ANISOU 1677  CG  MET A 542     9031  28241   8942    683    525   1618       C  
ATOM   1678  SD  MET A 542     -35.110  11.968 -46.614  1.00160.11           S  
ANISOU 1678  SD  MET A 542    13856  33035  13945    802    677   1624       S  
ATOM   1679  CE  MET A 542     -35.777  10.487 -47.369  1.00139.77           C  
ANISOU 1679  CE  MET A 542    11020  30720  11366    775    634   1511       C  
ATOM   1680  N   TYR A 543     -29.962  11.206 -45.849  1.00119.22           N  
ANISOU 1680  N   TYR A 543     9108  27742   8449    412    370   1467       N  
ATOM   1681  CA  TYR A 543     -29.401   9.871 -45.723  1.00118.25           C  
ANISOU 1681  CA  TYR A 543     8951  27689   8291    338    320   1340       C  
ATOM   1682  C   TYR A 543     -30.428   8.924 -45.118  1.00118.15           C  
ANISOU 1682  C   TYR A 543     8917  27636   8339    369    414   1234       C  
ATOM   1683  O   TYR A 543     -31.301   9.334 -44.349  1.00118.67           O  
ANISOU 1683  O   TYR A 543     9075  27548   8467    426    523   1244       O  
ATOM   1684  CB  TYR A 543     -28.137   9.883 -44.859  1.00117.68           C  
ANISOU 1684  CB  TYR A 543     9071  27479   8162    248    278   1313       C  
ATOM   1685  CG  TYR A 543     -26.882  10.295 -45.594  1.00117.51           C  
ANISOU 1685  CG  TYR A 543     9022  27557   8071    185    161   1375       C  
ATOM   1686  CD1 TYR A 543     -26.164   9.375 -46.347  1.00130.89           C  
ANISOU 1686  CD1 TYR A 543    10578  29432   9724    134     73   1322       C  
ATOM   1687  CD2 TYR A 543     -26.409  11.599 -45.527  1.00118.04           C  
ANISOU 1687  CD2 TYR A 543     9205  27531   8114    174    149   1482       C  
ATOM   1688  CE1 TYR A 543     -25.014   9.743 -47.018  1.00144.87           C  
ANISOU 1688  CE1 TYR A 543    12317  31292  11433     76    -25   1377       C  
ATOM   1689  CE2 TYR A 543     -25.259  11.976 -46.195  1.00117.95           C  
ANISOU 1689  CE2 TYR A 543     9166  27610   8039    110     48   1537       C  
ATOM   1690  CZ  TYR A 543     -24.567  11.044 -46.940  1.00117.34           C  
ANISOU 1690  CZ  TYR A 543     8942  27717   7924     63    -40   1485       C  
ATOM   1691  OH  TYR A 543     -23.422  11.413 -47.605  1.00117.31           O  
ANISOU 1691  OH  TYR A 543     8908  27804   7862     -1   -133   1539       O  
ATOM   1692  N   GLU A 544     -30.316   7.648 -45.476  1.00117.55           N  
ANISOU 1692  N   GLU A 544     8722  27694   8248    328    380   1129       N  
ATOM   1693  CA  GLU A 544     -31.178   6.598 -44.946  1.00117.41           C  
ANISOU 1693  CA  GLU A 544     8682  27649   8281    340    466   1014       C  
ATOM   1694  C   GLU A 544     -30.305   5.527 -44.311  1.00136.95           C  
ANISOU 1694  C   GLU A 544    11246  30070  10720    263    443    908       C  
ATOM   1695  O   GLU A 544     -29.522   4.868 -45.005  1.00148.63           O  
ANISOU 1695  O   GLU A 544    12629  31690  12153    212    361    873       O  
ATOM   1696  CB  GLU A 544     -32.061   5.998 -46.042  1.00122.33           C  
ANISOU 1696  CB  GLU A 544     9058  28495   8927    366    464    984       C  
ATOM   1697  CG  GLU A 544     -33.066   6.973 -46.631  1.00136.21           C  
ANISOU 1697  CG  GLU A 544    10709  30316  10730    454    489   1096       C  
ATOM   1698  CD  GLU A 544     -34.045   6.302 -47.575  1.00149.55           C  
ANISOU 1698  CD  GLU A 544    12158  32225  12440    470    490   1059       C  
ATOM   1699  OE1 GLU A 544     -33.928   5.076 -47.783  1.00141.62           O  
ANISOU 1699  OE1 GLU A 544    11080  31317  11413    405    478    936       O  
ATOM   1700  OE2 GLU A 544     -34.933   7.000 -48.108  1.00159.50           O  
ANISOU 1700  OE2 GLU A 544    13302  33561  13739    544    504   1154       O  
ATOM   1701  N   LEU A 545     -30.439   5.358 -42.999  1.00141.10           N  
ANISOU 1701  N   LEU A 545    11956  30390  11266    258    519    862       N  
ATOM   1702  CA  LEU A 545     -29.671   4.382 -42.237  1.00115.75           C  
ANISOU 1702  CA  LEU A 545     8852  27105   8025    194    504    775       C  
ATOM   1703  C   LEU A 545     -30.595   3.247 -41.820  1.00115.70           C  
ANISOU 1703  C   LEU A 545     8815  27076   8070    208    604    660       C  
ATOM   1704  O   LEU A 545     -31.601   3.480 -41.140  1.00116.14           O  
ANISOU 1704  O   LEU A 545     8940  27011   8179    251    713    649       O  
ATOM   1705  CB  LEU A 545     -29.027   5.034 -41.013  1.00124.15           C  
ANISOU 1705  CB  LEU A 545    10165  27952   9053    162    507    812       C  
ATOM   1706  CG  LEU A 545     -28.254   4.126 -40.053  1.00120.96           C  
ANISOU 1706  CG  LEU A 545     9895  27451   8614    100    490    742       C  
ATOM   1707  CD1 LEU A 545     -27.050   3.506 -40.746  1.00127.95           C  
ANISOU 1707  CD1 LEU A 545    10678  28481   9454     50    372    735       C  
ATOM   1708  CD2 LEU A 545     -27.827   4.899 -38.814  1.00115.51           C  
ANISOU 1708  CD2 LEU A 545     9456  26548   7883     64    502    784       C  
ATOM   1709  N   VAL A 546     -30.259   2.028 -42.229  1.00115.24           N  
ANISOU 1709  N   VAL A 546     8658  27128   8001    169    577    572       N  
ATOM   1710  CA  VAL A 546     -31.019   0.834 -41.879  1.00119.02           C  
ANISOU 1710  CA  VAL A 546     9110  27589   8524    168    672    453       C  
ATOM   1711  C   VAL A 546     -30.159  -0.032 -40.972  1.00116.21           C  
ANISOU 1711  C   VAL A 546     8899  27115   8141    121    667    395       C  
ATOM   1712  O   VAL A 546     -29.034  -0.396 -41.335  1.00120.60           O  
ANISOU 1712  O   VAL A 546     9429  27739   8653     82    577    400       O  
ATOM   1713  CB  VAL A 546     -31.464   0.056 -43.129  1.00115.29           C  
ANISOU 1713  CB  VAL A 546     8399  27341   8064    159    664    391       C  
ATOM   1714  CG1 VAL A 546     -32.041  -1.295 -42.736  1.00115.22           C  
ANISOU 1714  CG1 VAL A 546     8379  27305   8095    139    760    257       C  
ATOM   1715  CG2 VAL A 546     -32.486   0.861 -43.915  1.00115.98           C  
ANISOU 1715  CG2 VAL A 546     8342  27544   8183    211    675    453       C  
ATOM   1716  N   TYR A 547     -30.686  -0.360 -39.794  1.00114.79           N  
ANISOU 1716  N   TYR A 547     8869  26759   7987    128    766    346       N  
ATOM   1717  CA  TYR A 547     -29.957  -1.153 -38.818  1.00114.45           C  
ANISOU 1717  CA  TYR A 547     8980  26590   7917     89    766    303       C  
ATOM   1718  C   TYR A 547     -30.895  -2.168 -38.181  1.00114.60           C  
ANISOU 1718  C   TYR A 547     9032  26525   7985     96    898    197       C  
ATOM   1719  O   TYR A 547     -32.115  -1.994 -38.162  1.00115.02           O  
ANISOU 1719  O   TYR A 547     9044  26566   8093    130    996    170       O  
ATOM   1720  CB  TYR A 547     -29.314  -0.271 -37.737  1.00119.05           C  
ANISOU 1720  CB  TYR A 547     9789  26996   8448     70    733    380       C  
ATOM   1721  CG  TYR A 547     -30.300   0.510 -36.895  1.00115.06           C  
ANISOU 1721  CG  TYR A 547     9419  26330   7969    100    841    395       C  
ATOM   1722  CD1 TYR A 547     -30.774   0.001 -35.693  1.00115.24           C  
ANISOU 1722  CD1 TYR A 547     9605  26179   8001     93    945    335       C  
ATOM   1723  CD2 TYR A 547     -30.750   1.760 -37.299  1.00115.48           C  
ANISOU 1723  CD2 TYR A 547     9441  26396   8038    138    847    473       C  
ATOM   1724  CE1 TYR A 547     -31.672   0.711 -34.920  1.00115.80           C  
ANISOU 1724  CE1 TYR A 547     9805  26097   8098    120   1057    345       C  
ATOM   1725  CE2 TYR A 547     -31.649   2.479 -36.533  1.00116.07           C  
ANISOU 1725  CE2 TYR A 547     9641  26314   8147    172    960    488       C  
ATOM   1726  CZ  TYR A 547     -32.105   1.949 -35.344  1.00116.23           C  
ANISOU 1726  CZ  TYR A 547     9822  26164   8176    161   1067    421       C  
ATOM   1727  OH  TYR A 547     -33.000   2.659 -34.575  1.00116.91           O  
ANISOU 1727  OH  TYR A 547    10035  26087   8297    194   1193    432       O  
ATOM   1728  N   TRP A 548     -30.303  -3.237 -37.653  1.00114.33           N  
ANISOU 1728  N   TRP A 548     9071  26434   7936     64    902    141       N  
ATOM   1729  CA  TRP A 548     -31.071  -4.284 -36.995  1.00114.49           C  
ANISOU 1729  CA  TRP A 548     9141  26362   7998     64   1029     40       C  
ATOM   1730  C   TRP A 548     -30.162  -5.042 -36.040  1.00122.85           C  
ANISOU 1730  C   TRP A 548    10363  27295   9019     35   1012     30       C  
ATOM   1731  O   TRP A 548     -28.934  -4.960 -36.123  1.00114.05           O  
ANISOU 1731  O   TRP A 548     9270  26208   7856     16    897     89       O  
ATOM   1732  CB  TRP A 548     -31.707  -5.241 -38.012  1.00114.54           C  
ANISOU 1732  CB  TRP A 548     8938  26528   8055     60   1079    -57       C  
ATOM   1733  CG  TRP A 548     -30.719  -6.029 -38.829  1.00126.47           C  
ANISOU 1733  CG  TRP A 548    10341  28169   9544     31   1003    -81       C  
ATOM   1734  CD1 TRP A 548     -30.300  -7.308 -38.599  1.00149.09           C  
ANISOU 1734  CD1 TRP A 548    13231  30999  12417      9   1040   -154       C  
ATOM   1735  CD2 TRP A 548     -30.039  -5.591 -40.013  1.00119.12           C  
ANISOU 1735  CD2 TRP A 548     9261  27416   8583     23    890    -30       C  
ATOM   1736  NE1 TRP A 548     -29.398  -7.692 -39.563  1.00139.75           N  
ANISOU 1736  NE1 TRP A 548    11923  29959  11217     -9    962   -154       N  
ATOM   1737  CE2 TRP A 548     -29.221  -6.656 -40.442  1.00113.82           C  
ANISOU 1737  CE2 TRP A 548     8531  26809   7905     -5    868    -81       C  
ATOM   1738  CE3 TRP A 548     -30.040  -4.403 -40.750  1.00114.07           C  
ANISOU 1738  CE3 TRP A 548     8537  26883   7922     39    812     57       C  
ATOM   1739  CZ2 TRP A 548     -28.413  -6.567 -41.575  1.00134.80           C  
ANISOU 1739  CZ2 TRP A 548    11048  29634  10534    -22    774    -54       C  
ATOM   1740  CZ3 TRP A 548     -29.237  -4.317 -41.874  1.00113.90           C  
ANISOU 1740  CZ3 TRP A 548     8379  27030   7867     19    712     87       C  
ATOM   1741  CH2 TRP A 548     -28.434  -5.393 -42.275  1.00113.69           C  
ANISOU 1741  CH2 TRP A 548     8296  27067   7833    -13    696     29       C  
ATOM   1742  N   ALA A 549     -30.788  -5.775 -35.124  1.00122.92           N  
ANISOU 1742  N   ALA A 549    10486  27167   9052     34   1130    -39       N  
ATOM   1743  CA  ALA A 549     -30.055  -6.661 -34.236  1.00114.51           C  
ANISOU 1743  CA  ALA A 549     9566  25987   7957     12   1129    -51       C  
ATOM   1744  C   ALA A 549     -29.773  -7.978 -34.944  1.00114.36           C  
ANISOU 1744  C   ALA A 549     9410  26070   7972      7   1142   -125       C  
ATOM   1745  O   ALA A 549     -30.636  -8.524 -35.636  1.00148.34           O  
ANISOU 1745  O   ALA A 549    13571  30459  12331      9   1226   -214       O  
ATOM   1746  CB  ALA A 549     -30.845  -6.910 -32.951  1.00114.92           C  
ANISOU 1746  CB  ALA A 549     9807  25842   8014     10   1258    -92       C  
ATOM   1747  N   ALA A 550     -28.550  -8.484 -34.770  1.00116.77           N  
ANISOU 1747  N   ALA A 550     9757  26365   8244     -2   1061    -87       N  
ATOM   1748  CA  ALA A 550     -28.152  -9.710 -35.453  1.00121.26           C  
ANISOU 1748  CA  ALA A 550    10204  27020   8849     -2   1078   -150       C  
ATOM   1749  C   ALA A 550     -29.058 -10.875 -35.073  1.00134.61           C  
ANISOU 1749  C   ALA A 550    11926  28629  10593     -4   1237   -264       C  
ATOM   1750  O   ALA A 550     -29.347 -11.745 -35.904  1.00133.18           O  
ANISOU 1750  O   ALA A 550    11601  28543  10458    -14   1300   -355       O  
ATOM   1751  CB  ALA A 550     -26.692 -10.037 -35.139  1.00114.15           C  
ANISOU 1751  CB  ALA A 550     9362  26097   7913     -1    975    -75       C  
ATOM   1752  N   GLU A 551     -29.525 -10.904 -33.824  1.00128.21           N  
ANISOU 1752  N   GLU A 551    11305  27637   9770     -3   1310   -264       N  
ATOM   1753  CA  GLU A 551     -30.389 -11.985 -33.368  1.00139.74           C  
ANISOU 1753  CA  GLU A 551    12813  29003  11278     -9   1469   -369       C  
ATOM   1754  C   GLU A 551     -31.820 -11.847 -33.873  1.00137.61           C  
ANISOU 1754  C   GLU A 551    12429  28793  11064    -19   1578   -459       C  
ATOM   1755  O   GLU A 551     -32.566 -12.831 -33.851  1.00154.65           O  
ANISOU 1755  O   GLU A 551    14565  30924  13273    -35   1711   -565       O  
ATOM   1756  CB  GLU A 551     -30.385 -12.054 -31.840  1.00171.53           C  
ANISOU 1756  CB  GLU A 551    17091  32817  15267     -9   1513   -335       C  
ATOM   1757  CG  GLU A 551     -30.837 -10.775 -31.159  1.00182.18           C  
ANISOU 1757  CG  GLU A 551    18561  34085  16575    -13   1501   -279       C  
ATOM   1758  CD  GLU A 551     -30.801 -10.880 -29.647  1.00173.43           C  
ANISOU 1758  CD  GLU A 551    17713  32768  15414    -25   1547   -251       C  
ATOM   1759  OE1 GLU A 551     -30.601 -12.000 -29.132  1.00167.81           O  
ANISOU 1759  OE1 GLU A 551    17079  31973  14707    -26   1602   -280       O  
ATOM   1760  OE2 GLU A 551     -30.968  -9.844 -28.971  1.00176.92           O  
ANISOU 1760  OE2 GLU A 551    18288  33126  15808    -37   1532   -198       O  
ATOM   1761  N   ASP A 552     -32.215 -10.662 -34.329  1.00116.75           N  
ANISOU 1761  N   ASP A 552     9710  26234   8416     -9   1527   -415       N  
ATOM   1762  CA  ASP A 552     -33.559 -10.409 -34.842  1.00142.34           C  
ANISOU 1762  CA  ASP A 552    12823  29549  11710    -10   1615   -478       C  
ATOM   1763  C   ASP A 552     -33.449  -9.929 -36.287  1.00142.04           C  
ANISOU 1763  C   ASP A 552    12557  29737  11674    -11   1522   -461       C  
ATOM   1764  O   ASP A 552     -33.745  -8.771 -36.597  1.00153.77           O  
ANISOU 1764  O   ASP A 552    13992  31280  13154     12   1471   -394       O  
ATOM   1765  CB  ASP A 552     -34.296  -9.388 -33.962  1.00155.49           C  
ANISOU 1765  CB  ASP A 552    14617  31089  13375     12   1663   -433       C  
ATOM   1766  CG  ASP A 552     -34.694  -9.959 -32.614  1.00173.87           C  
ANISOU 1766  CG  ASP A 552    17153  33205  15706      2   1788   -475       C  
ATOM   1767  OD1 ASP A 552     -34.513 -11.177 -32.407  1.00187.93           O  
ANISOU 1767  OD1 ASP A 552    18965  34943  17497    -18   1844   -541       O  
ATOM   1768  OD2 ASP A 552     -35.189  -9.190 -31.763  1.00181.96           O  
ANISOU 1768  OD2 ASP A 552    18314  34101  16721     15   1838   -441       O  
ATOM   1769  N   GLU A 553     -33.024 -10.835 -37.173  1.00150.63           N  
ANISOU 1769  N   GLU A 553    13515  30948  12770    -38   1507   -521       N  
ATOM   1770  CA  GLU A 553     -32.876 -10.492 -38.584  1.00140.09           C  
ANISOU 1770  CA  GLU A 553    11968  29834  11426    -49   1423   -512       C  
ATOM   1771  C   GLU A 553     -34.203 -10.074 -39.208  1.00125.57           C  
ANISOU 1771  C   GLU A 553     9977  28111   9623    -54   1473   -549       C  
ATOM   1772  O   GLU A 553     -34.217  -9.302 -40.173  1.00115.48           O  
ANISOU 1772  O   GLU A 553     8554  26996   8327    -48   1386   -497       O  
ATOM   1773  CB  GLU A 553     -32.280 -11.678 -39.344  1.00125.70           C  
ANISOU 1773  CB  GLU A 553    10050  28103   9608    -86   1431   -590       C  
ATOM   1774  CG  GLU A 553     -31.940 -11.402 -40.799  1.00180.00           C  
ANISOU 1774  CG  GLU A 553    16726  35207  16460   -107   1340   -582       C  
ATOM   1775  CD  GLU A 553     -31.490 -12.650 -41.530  1.00210.36           C  
ANISOU 1775  CD  GLU A 553    20483  39129  20314   -151   1381   -679       C  
ATOM   1776  OE1 GLU A 553     -31.462 -13.728 -40.899  1.00215.53           O  
ANISOU 1776  OE1 GLU A 553    21234  39656  21002   -159   1482   -750       O  
ATOM   1777  OE2 GLU A 553     -31.168 -12.554 -42.733  1.00214.90           O  
ANISOU 1777  OE2 GLU A 553    20902  39887  20863   -178   1319   -685       O  
ATOM   1778  N   ASP A 554     -35.324 -10.563 -38.669  1.00115.95           N  
ANISOU 1778  N   ASP A 554     8785  26814   8456    -65   1610   -631       N  
ATOM   1779  CA  ASP A 554     -36.629 -10.240 -39.238  1.00116.52           C  
ANISOU 1779  CA  ASP A 554     8697  27003   8571    -70   1662   -665       C  
ATOM   1780  C   ASP A 554     -37.057  -8.812 -38.918  1.00116.62           C  
ANISOU 1780  C   ASP A 554     8740  26981   8590    -10   1629   -554       C  
ATOM   1781  O   ASP A 554     -37.739  -8.177 -39.730  1.00172.79           O  
ANISOU 1781  O   ASP A 554    15684  34246  15721      4   1603   -526       O  
ATOM   1782  CB  ASP A 554     -37.679 -11.229 -38.731  1.00117.07           C  
ANISOU 1782  CB  ASP A 554     8784  26998   8700   -105   1826   -789       C  
ATOM   1783  CG  ASP A 554     -37.678 -11.353 -37.218  1.00188.54           C  
ANISOU 1783  CG  ASP A 554    18080  35795  17762    -81   1912   -781       C  
ATOM   1784  OD1 ASP A 554     -36.599 -11.185 -36.611  1.00170.35           O  
ANISOU 1784  OD1 ASP A 554    15937  33379  15410    -59   1845   -711       O  
ATOM   1785  OD2 ASP A 554     -38.751 -11.621 -36.636  1.00186.21           O  
ANISOU 1785  OD2 ASP A 554    17815  35417  17519    -89   2047   -844       O  
ATOM   1786  N   GLN A 555     -36.679  -8.295 -37.753  1.00126.83           N  
ANISOU 1786  N   GLN A 555    10248  28076   9866     25   1634   -488       N  
ATOM   1787  CA  GLN A 555     -37.079  -6.962 -37.317  1.00116.59           C  
ANISOU 1787  CA  GLN A 555     9013  26709   8578     79   1629   -390       C  
ATOM   1788  C   GLN A 555     -35.952  -5.977 -37.599  1.00116.11           C  
ANISOU 1788  C   GLN A 555     8987  26678   8453     99   1479   -270       C  
ATOM   1789  O   GLN A 555     -34.851  -6.116 -37.055  1.00150.04           O  
ANISOU 1789  O   GLN A 555    13430  30881  12696     84   1420   -241       O  
ATOM   1790  CB  GLN A 555     -37.441  -6.964 -35.831  1.00116.80           C  
ANISOU 1790  CB  GLN A 555     9268  26492   8618     90   1744   -402       C  
ATOM   1791  CG  GLN A 555     -38.935  -7.051 -35.566  1.00117.56           C  
ANISOU 1791  CG  GLN A 555     9314  26557   8796    103   1896   -463       C  
ATOM   1792  CD  GLN A 555     -39.260  -7.737 -34.255  1.00146.64           C  
ANISOU 1792  CD  GLN A 555    13197  30026  12492     84   2034   -531       C  
ATOM   1793  OE1 GLN A 555     -38.448  -8.492 -33.719  1.00148.74           O  
ANISOU 1793  OE1 GLN A 555    13602  30201  12713     53   2022   -556       O  
ATOM   1794  NE2 GLN A 555     -40.454  -7.480 -33.731  1.00119.16           N  
ANISOU 1794  NE2 GLN A 555     9731  26466   9078    106   2170   -556       N  
ATOM   1795  N   GLN A 556     -36.230  -4.985 -38.442  1.00116.33           N  
ANISOU 1795  N   GLN A 556     8876  26837   8486    131   1417   -196       N  
ATOM   1796  CA  GLN A 556     -35.242  -3.997 -38.849  1.00115.98           C  
ANISOU 1796  CA  GLN A 556     8843  26839   8385    146   1280    -81       C  
ATOM   1797  C   GLN A 556     -35.798  -2.594 -38.647  1.00116.44           C  
ANISOU 1797  C   GLN A 556     8934  26842   8465    205   1294     20       C  
ATOM   1798  O   GLN A 556     -37.011  -2.392 -38.541  1.00117.08           O  
ANISOU 1798  O   GLN A 556     8961  26911   8614    241   1394      5       O  
ATOM   1799  CB  GLN A 556     -34.825  -4.194 -40.314  1.00115.82           C  
ANISOU 1799  CB  GLN A 556     8608  27060   8339    123   1178    -80       C  
ATOM   1800  CG  GLN A 556     -34.298  -5.586 -40.624  1.00146.84           C  
ANISOU 1800  CG  GLN A 556    12493  31047  12253     66   1180   -185       C  
ATOM   1801  CD  GLN A 556     -33.954  -5.773 -42.088  1.00158.20           C  
ANISOU 1801  CD  GLN A 556    13723  32722  13662     36   1095   -193       C  
ATOM   1802  OE1 GLN A 556     -34.072  -4.846 -42.889  1.00128.86           O  
ANISOU 1802  OE1 GLN A 556     9895  29136   9930     57   1022   -113       O  
ATOM   1803  NE2 GLN A 556     -33.528  -6.978 -42.446  1.00164.05           N  
ANISOU 1803  NE2 GLN A 556    14419  33518  14395    -15   1110   -289       N  
ATOM   1804  N   HIS A 557     -34.892  -1.619 -38.601  1.00116.19           N  
ANISOU 1804  N   HIS A 557     8990  26775   8381    214   1196    124       N  
ATOM   1805  CA  HIS A 557     -35.246  -0.232 -38.343  1.00116.66           C  
ANISOU 1805  CA  HIS A 557     9116  26755   8456    267   1212    226       C  
ATOM   1806  C   HIS A 557     -34.652   0.664 -39.423  1.00116.61           C  
ANISOU 1806  C   HIS A 557     8995  26897   8414    280   1085    330       C  
ATOM   1807  O   HIS A 557     -33.699   0.294 -40.112  1.00116.09           O  
ANISOU 1807  O   HIS A 557     8859  26954   8295    239    976    329       O  
ATOM   1808  CB  HIS A 557     -34.761   0.217 -36.955  1.00116.61           C  
ANISOU 1808  CB  HIS A 557     9388  26505   8412    253   1244    253       C  
ATOM   1809  CG  HIS A 557     -35.088  -0.751 -35.859  1.00122.73           C  
ANISOU 1809  CG  HIS A 557    10301  27133   9200    227   1352    155       C  
ATOM   1810  ND1 HIS A 557     -34.175  -1.661 -35.371  1.00116.07           N  
ANISOU 1810  ND1 HIS A 557     9559  26241   8302    172   1310    110       N  
ATOM   1811  CD2 HIS A 557     -36.231  -0.957 -35.163  1.00117.14           C  
ANISOU 1811  CD2 HIS A 557     9641  26312   8554    250   1504     99       C  
ATOM   1812  CE1 HIS A 557     -34.741  -2.382 -34.418  1.00116.28           C  
ANISOU 1812  CE1 HIS A 557     9700  26130   8350    161   1430     32       C  
ATOM   1813  NE2 HIS A 557     -35.989  -1.974 -34.274  1.00116.90           N  
ANISOU 1813  NE2 HIS A 557     9751  26168   8499    204   1551     20       N  
ATOM   1814  N   LYS A 558     -35.229   1.858 -39.561  1.00117.24           N  
ANISOU 1814  N   LYS A 558     9060  26958   8526    341   1108    423       N  
ATOM   1815  CA  LYS A 558     -34.799   2.813 -40.575  1.00117.98           C  
ANISOU 1815  CA  LYS A 558     9051  27183   8593    363   1002    533       C  
ATOM   1816  C   LYS A 558     -35.044   4.226 -40.065  1.00117.97           C  
ANISOU 1816  C   LYS A 558     9179  27032   8614    418   1048    641       C  
ATOM   1817  O   LYS A 558     -36.151   4.539 -39.619  1.00118.69           O  
ANISOU 1817  O   LYS A 558     9283  27034   8779    478   1170    644       O  
ATOM   1818  CB  LYS A 558     -35.546   2.591 -41.895  1.00142.99           C  
ANISOU 1818  CB  LYS A 558    11946  30592  11793    389    979    534       C  
ATOM   1819  CG  LYS A 558     -35.003   3.396 -43.068  1.00124.12           C  
ANISOU 1819  CG  LYS A 558     9436  28365   9358    400    857    642       C  
ATOM   1820  CD  LYS A 558     -36.123   3.894 -43.972  1.00126.32           C  
ANISOU 1820  CD  LYS A 558     9510  28797   9689    468    872    706       C  
ATOM   1821  CE  LYS A 558     -37.047   2.766 -44.409  1.00134.74           C  
ANISOU 1821  CE  LYS A 558    10394  30009  10791    448    915    599       C  
ATOM   1822  NZ  LYS A 558     -36.359   1.761 -45.264  1.00118.50           N  
ANISOU 1822  NZ  LYS A 558     8226  28131   8666    365    828    520       N  
ATOM   1823  N   VAL A 559     -34.018   5.073 -40.139  1.00117.79           N  
ANISOU 1823  N   VAL A 559     9248  26978   8529    398    959    726       N  
ATOM   1824  CA  VAL A 559     -34.104   6.458 -39.693  1.00118.43           C  
ANISOU 1824  CA  VAL A 559     9468  26908   8621    438   1001    829       C  
ATOM   1825  C   VAL A 559     -33.524   7.358 -40.777  1.00118.56           C  
ANISOU 1825  C   VAL A 559     9388  27056   8605    450    892    943       C  
ATOM   1826  O   VAL A 559     -32.446   7.079 -41.314  1.00117.93           O  
ANISOU 1826  O   VAL A 559     9269  27084   8454    389    768    943       O  
ATOM   1827  CB  VAL A 559     -33.378   6.674 -38.348  1.00118.23           C  
ANISOU 1827  CB  VAL A 559     9728  26651   8543    378   1025    811       C  
ATOM   1828  CG1 VAL A 559     -31.958   6.121 -38.397  1.00117.85           C  
ANISOU 1828  CG1 VAL A 559     9719  26656   8403    288    890    787       C  
ATOM   1829  CG2 VAL A 559     -33.372   8.149 -37.968  1.00124.23           C  
ANISOU 1829  CG2 VAL A 559    10639  27257   9304    405   1069    913       C  
ATOM   1830  N   THR A 560     -34.245   8.429 -41.104  1.00119.47           N  
ANISOU 1830  N   THR A 560     9461  27159   8774    532    942   1045       N  
ATOM   1831  CA  THR A 560     -33.828   9.391 -42.115  1.00125.92           C  
ANISOU 1831  CA  THR A 560    10194  28085   9566    556    856   1168       C  
ATOM   1832  C   THR A 560     -33.529  10.731 -41.457  1.00120.37           C  
ANISOU 1832  C   THR A 560     9702  27173   8859    568    904   1259       C  
ATOM   1833  O   THR A 560     -34.198  11.123 -40.495  1.00136.00           O  
ANISOU 1833  O   THR A 560    11826  28956  10893    606   1037   1253       O  
ATOM   1834  CB  THR A 560     -34.905   9.566 -43.190  1.00120.59           C  
ANISOU 1834  CB  THR A 560     9274  27588   8955    646    867   1230       C  
ATOM   1835  OG1 THR A 560     -36.120  10.024 -42.583  1.00121.53           O  
ANISOU 1835  OG1 THR A 560     9427  27575   9174    736   1014   1255       O  
ATOM   1836  CG2 THR A 560     -35.168   8.246 -43.900  1.00120.13           C  
ANISOU 1836  CG2 THR A 560     9009  27746   8889    614    818   1133       C  
ATOM   1837  N   PHE A 561     -32.529  11.436 -41.982  1.00120.28           N  
ANISOU 1837  N   PHE A 561     9715  27203   8784    531    804   1340       N  
ATOM   1838  CA  PHE A 561     -32.085  12.684 -41.381  1.00125.82           C  
ANISOU 1838  CA  PHE A 561    10631  27708   9468    519    841   1418       C  
ATOM   1839  C   PHE A 561     -31.445  13.567 -42.443  1.00137.95           C  
ANISOU 1839  C   PHE A 561    12093  29355  10967    521    746   1538       C  
ATOM   1840  O   PHE A 561     -31.058  13.102 -43.519  1.00120.65           O  
ANISOU 1840  O   PHE A 561     9717  27386   8740    504    632   1545       O  
ATOM   1841  CB  PHE A 561     -31.106  12.431 -40.227  1.00136.26           C  
ANISOU 1841  CB  PHE A 561    12187  28871  10716    406    824   1343       C  
ATOM   1842  CG  PHE A 561     -30.025  11.439 -40.554  1.00119.17           C  
ANISOU 1842  CG  PHE A 561     9954  26852   8475    316    683   1281       C  
ATOM   1843  CD1 PHE A 561     -30.218  10.085 -40.328  1.00118.50           C  
ANISOU 1843  CD1 PHE A 561     9804  26824   8395    300    682   1167       C  
ATOM   1844  CD2 PHE A 561     -28.817  11.859 -41.084  1.00118.94           C  
ANISOU 1844  CD2 PHE A 561     9925  26894   8373    250    561   1337       C  
ATOM   1845  CE1 PHE A 561     -29.228   9.169 -40.628  1.00117.64           C  
ANISOU 1845  CE1 PHE A 561     9633  26837   8226    227    565   1114       C  
ATOM   1846  CE2 PHE A 561     -27.822  10.947 -41.384  1.00118.07           C  
ANISOU 1846  CE2 PHE A 561     9744  26914   8203    175    441   1283       C  
ATOM   1847  CZ  PHE A 561     -28.028   9.601 -41.156  1.00117.43           C  
ANISOU 1847  CZ  PHE A 561     9600  26885   8134    168    446   1173       C  
ATOM   1848  N   ASP A 562     -31.333  14.853 -42.116  1.00149.60           N  
ANISOU 1848  N   ASP A 562    13726  30665  12449    536    805   1630       N  
ATOM   1849  CA  ASP A 562     -30.797  15.842 -43.036  1.00133.18           C  
ANISOU 1849  CA  ASP A 562    11605  28657  10342    543    738   1756       C  
ATOM   1850  C   ASP A 562     -29.322  15.565 -43.331  1.00126.28           C  
ANISOU 1850  C   ASP A 562    10746  27874   9361    419    590   1733       C  
ATOM   1851  O   ASP A 562     -28.646  14.874 -42.565  1.00145.89           O  
ANISOU 1851  O   ASP A 562    13334  30304  11795    327    556   1634       O  
ATOM   1852  CB  ASP A 562     -30.980  17.242 -42.455  1.00140.33           C  
ANISOU 1852  CB  ASP A 562    12710  29328  11280    576    855   1846       C  
ATOM   1853  CG  ASP A 562     -32.437  17.661 -42.401  1.00176.41           C  
ANISOU 1853  CG  ASP A 562    17228  33830  15969    720   1002   1901       C  
ATOM   1854  OD1 ASP A 562     -33.231  17.156 -43.223  1.00180.37           O  
ANISOU 1854  OD1 ASP A 562    17491  34520  16521    803    981   1919       O  
ATOM   1855  OD2 ASP A 562     -32.790  18.493 -41.539  1.00181.17           O  
ANISOU 1855  OD2 ASP A 562    18026  34194  16616    748   1142   1927       O  
ATOM   1856  N   PRO A 563     -28.804  16.088 -44.447  1.00147.70           N  
ANISOU 1856  N   PRO A 563    13351  30730  12041    417    503   1827       N  
ATOM   1857  CA  PRO A 563     -27.426  15.767 -44.841  1.00120.94           C  
ANISOU 1857  CA  PRO A 563     9943  27450   8558    304    364   1806       C  
ATOM   1858  C   PRO A 563     -26.409  16.188 -43.791  1.00137.01           C  
ANISOU 1858  C   PRO A 563    12223  29298  10536    193    358   1782       C  
ATOM   1859  O   PRO A 563     -26.493  17.274 -43.213  1.00137.56           O  
ANISOU 1859  O   PRO A 563    12475  29175  10617    193    439   1839       O  
ATOM   1860  CB  PRO A 563     -27.238  16.552 -46.144  1.00131.56           C  
ANISOU 1860  CB  PRO A 563    11162  28938   9887    336    307   1934       C  
ATOM   1861  CG  PRO A 563     -28.612  16.724 -46.678  1.00122.26           C  
ANISOU 1861  CG  PRO A 563     9843  27821   8789    472    379   1994       C  
ATOM   1862  CD  PRO A 563     -29.488  16.893 -45.475  1.00147.70           C  
ANISOU 1862  CD  PRO A 563    13215  30819  12086    523    522   1960       C  
ATOM   1863  N   THR A 564     -25.440  15.311 -43.559  1.00147.87           N  
ANISOU 1863  N   THR A 564    13601  30734  11851     95    262   1699       N  
ATOM   1864  CA  THR A 564     -24.349  15.539 -42.618  1.00119.85           C  
ANISOU 1864  CA  THR A 564    10253  27049   8234    -27    225   1674       C  
ATOM   1865  C   THR A 564     -23.286  14.480 -42.887  1.00118.91           C  
ANISOU 1865  C   THR A 564    10033  27087   8060   -107     93   1612       C  
ATOM   1866  O   THR A 564     -23.458  13.605 -43.742  1.00118.37           O  
ANISOU 1866  O   THR A 564     9760  27208   8009    -67     50   1581       O  
ATOM   1867  CB  THR A 564     -24.832  15.489 -41.167  1.00147.99           C  
ANISOU 1867  CB  THR A 564    14030  30389  11813    -39    329   1608       C  
ATOM   1868  OG1 THR A 564     -23.711  15.611 -40.282  1.00140.95           O  
ANISOU 1868  OG1 THR A 564    13322  29394  10839   -172    273   1581       O  
ATOM   1869  CG2 THR A 564     -25.552  14.178 -40.894  1.00156.19           C  
ANISOU 1869  CG2 THR A 564    14979  31475  12890     10    358   1506       C  
ATOM   1870  N   SER A 565     -22.182  14.566 -42.150  1.00133.84           N  
ANISOU 1870  N   SER A 565    12069  28899   9886   -222     33   1594       N  
ATOM   1871  CA  SER A 565     -21.095  13.604 -42.261  1.00126.24           C  
ANISOU 1871  CA  SER A 565    11025  28062   8878   -297    -87   1544       C  
ATOM   1872  C   SER A 565     -21.018  12.659 -41.070  1.00141.53           C  
ANISOU 1872  C   SER A 565    13066  29907  10803   -333    -81   1450       C  
ATOM   1873  O   SER A 565     -20.159  11.770 -41.057  1.00136.19           O  
ANISOU 1873  O   SER A 565    12326  29322  10098   -384   -172   1410       O  
ATOM   1874  CB  SER A 565     -19.758  14.334 -42.429  1.00118.41           C  
ANISOU 1874  CB  SER A 565    10083  27087   7819   -408   -182   1607       C  
ATOM   1875  OG  SER A 565     -19.541  15.250 -41.370  1.00140.21           O  
ANISOU 1875  OG  SER A 565    13088  29644  10544   -482   -145   1627       O  
ATOM   1876  N   SER A 566     -21.887  12.823 -40.076  1.00122.55           N  
ANISOU 1876  N   SER A 566    10819  27322   8421   -305     28   1418       N  
ATOM   1877  CA  SER A 566     -21.869  11.975 -38.894  1.00117.74           C  
ANISOU 1877  CA  SER A 566    10329  26614   7794   -340     42   1334       C  
ATOM   1878  C   SER A 566     -23.251  11.986 -38.259  1.00147.03           C  
ANISOU 1878  C   SER A 566    14124  30180  11560   -261    192   1295       C  
ATOM   1879  O   SER A 566     -23.982  12.975 -38.350  1.00168.53           O  
ANISOU 1879  O   SER A 566    16900  32815  14319   -211    285   1345       O  
ATOM   1880  CB  SER A 566     -20.817  12.440 -37.882  1.00132.77           C  
ANISOU 1880  CB  SER A 566    12441  28395   9610   -472    -16   1347       C  
ATOM   1881  OG  SER A 566     -21.163  13.699 -37.332  1.00165.10           O  
ANISOU 1881  OG  SER A 566    16732  32308  13690   -496     71   1387       O  
ATOM   1882  N   TYR A 567     -23.594  10.876 -37.611  1.00139.65           N  
ANISOU 1882  N   TYR A 567    13203  29220  10638   -249    221   1208       N  
ATOM   1883  CA  TYR A 567     -24.879  10.745 -36.939  1.00117.84           C  
ANISOU 1883  CA  TYR A 567    10519  26324   7930   -181    367   1159       C  
ATOM   1884  C   TYR A 567     -24.717   9.798 -35.762  1.00125.99           C  
ANISOU 1884  C   TYR A 567    11682  27262   8927   -231    375   1076       C  
ATOM   1885  O   TYR A 567     -24.104   8.735 -35.898  1.00127.19           O  
ANISOU 1885  O   TYR A 567    11742  27524   9061   -254    289   1038       O  
ATOM   1886  CB  TYR A 567     -25.957  10.232 -37.899  1.00117.57           C  
ANISOU 1886  CB  TYR A 567    10261  26424   7986    -65    420   1140       C  
ATOM   1887  CG  TYR A 567     -27.339  10.162 -37.292  1.00117.96           C  
ANISOU 1887  CG  TYR A 567    10367  26347   8104     10    577   1097       C  
ATOM   1888  CD1 TYR A 567     -27.859   8.957 -36.838  1.00117.54           C  
ANISOU 1888  CD1 TYR A 567    10291  26291   8079     27    624   1000       C  
ATOM   1889  CD2 TYR A 567     -28.124  11.301 -37.174  1.00118.82           C  
ANISOU 1889  CD2 TYR A 567    10555  26335   8258     64    688   1156       C  
ATOM   1890  CE1 TYR A 567     -29.123   8.889 -36.284  1.00117.96           C  
ANISOU 1890  CE1 TYR A 567    10390  26231   8198     92    774    959       C  
ATOM   1891  CE2 TYR A 567     -29.388  11.243 -36.621  1.00119.28           C  
ANISOU 1891  CE2 TYR A 567    10655  26277   8388    137    840   1119       C  
ATOM   1892  CZ  TYR A 567     -29.883  10.035 -36.178  1.00118.83           C  
ANISOU 1892  CZ  TYR A 567    10568  26227   8354    147    881   1019       C  
ATOM   1893  OH  TYR A 567     -31.142   9.974 -35.627  1.00127.45           O  
ANISOU 1893  OH  TYR A 567    11698  27206   9522    215   1037    981       O  
ATOM   1894  N   THR A 568     -25.262  10.186 -34.613  1.00118.18           N  
ANISOU 1894  N   THR A 568    10911  26067   7927   -247    484   1053       N  
ATOM   1895  CA  THR A 568     -25.150   9.413 -33.382  1.00125.67           C  
ANISOU 1895  CA  THR A 568    12017  26902   8828   -301    501    983       C  
ATOM   1896  C   THR A 568     -26.486   8.734 -33.105  1.00124.42           C  
ANISOU 1896  C   THR A 568    11834  26691   8748   -213    643    911       C  
ATOM   1897  O   THR A 568     -27.480   9.405 -32.805  1.00118.70           O  
ANISOU 1897  O   THR A 568    11190  25839   8070   -164    782    913       O  
ATOM   1898  CB  THR A 568     -24.738  10.305 -32.213  1.00146.28           C  
ANISOU 1898  CB  THR A 568    14912  29317  11352   -405    523   1001       C  
ATOM   1899  OG1 THR A 568     -23.484  10.934 -32.503  1.00157.08           O  
ANISOU 1899  OG1 THR A 568    16292  30745  12647   -497    388   1067       O  
ATOM   1900  CG2 THR A 568     -24.602   9.485 -30.940  1.00119.03           C  
ANISOU 1900  CG2 THR A 568    11628  25759   7838   -466    532    936       C  
ATOM   1901  N   LEU A 569     -26.507   7.409 -33.211  1.00117.41           N  
ANISOU 1901  N   LEU A 569    10834  25898   7880   -192    617    847       N  
ATOM   1902  CA  LEU A 569     -27.676   6.634 -32.825  1.00117.38           C  
ANISOU 1902  CA  LEU A 569    10821  25838   7941   -129    748    768       C  
ATOM   1903  C   LEU A 569     -27.703   6.463 -31.314  1.00127.07           C  
ANISOU 1903  C   LEU A 569    12310  26863   9109   -191    813    725       C  
ATOM   1904  O   LEU A 569     -26.674   6.193 -30.689  1.00150.81           O  
ANISOU 1904  O   LEU A 569    15432  29844  12025   -279    716    732       O  
ATOM   1905  CB  LEU A 569     -27.663   5.266 -33.505  1.00117.59           C  
ANISOU 1905  CB  LEU A 569    10641  26032   8007    -95    704    712       C  
ATOM   1906  CG  LEU A 569     -28.693   5.025 -34.607  1.00116.46           C  
ANISOU 1906  CG  LEU A 569    10262  26025   7961      0    762    691       C  
ATOM   1907  CD1 LEU A 569     -28.662   3.568 -35.032  1.00115.83           C  
ANISOU 1907  CD1 LEU A 569    10029  26074   7907     10    738    614       C  
ATOM   1908  CD2 LEU A 569     -30.085   5.425 -34.140  1.00125.87           C  
ANISOU 1908  CD2 LEU A 569    11515  27088   9221     61    929    669       C  
ATOM   1909  N   GLU A 570     -28.885   6.623 -30.727  1.00143.28           N  
ANISOU 1909  N   GLU A 570    14454  28775  11211   -146    978    685       N  
ATOM   1910  CA  GLU A 570     -29.045   6.575 -29.283  1.00129.38           C  
ANISOU 1910  CA  GLU A 570    12958  26808   9392   -204   1064    643       C  
ATOM   1911  C   GLU A 570     -30.108   5.550 -28.913  1.00118.79           C  
ANISOU 1911  C   GLU A 570    11591  25426   8116   -148   1192    555       C  
ATOM   1912  O   GLU A 570     -30.823   5.021 -29.769  1.00126.37           O  
ANISOU 1912  O   GLU A 570    12333  26509   9173    -65   1226    528       O  
ATOM   1913  CB  GLU A 570     -29.411   7.957 -28.722  1.00167.88           C  
ANISOU 1913  CB  GLU A 570    18030  31503  14254   -223   1168    678       C  
ATOM   1914  CG  GLU A 570     -28.470   9.071 -29.164  1.00183.91           C  
ANISOU 1914  CG  GLU A 570    20081  33566  16230   -277   1061    764       C  
ATOM   1915  CD  GLU A 570     -28.928  10.442 -28.705  1.00180.43           C  
ANISOU 1915  CD  GLU A 570    19825  32940  15791   -286   1187    796       C  
ATOM   1916  OE1 GLU A 570     -28.478  10.896 -27.632  1.00176.89           O  
ANISOU 1916  OE1 GLU A 570    19637  32332  15242   -394   1203    787       O  
ATOM   1917  OE2 GLU A 570     -29.747  11.063 -29.416  1.00168.38           O  
ANISOU 1917  OE2 GLU A 570    18185  31428  14364   -186   1274    832       O  
ATOM   1918  N   ASP A 571     -30.192   5.271 -27.610  1.00146.91           N  
ANISOU 1918  N   ASP A 571    15385  28816  11617   -205   1262    511       N  
ATOM   1919  CA  ASP A 571     -31.227   4.409 -27.034  1.00141.54           C  
ANISOU 1919  CA  ASP A 571    14734  28055  10988   -167   1408    426       C  
ATOM   1920  C   ASP A 571     -31.147   2.982 -27.574  1.00122.32           C  
ANISOU 1920  C   ASP A 571    12112  25772   8593   -136   1354    378       C  
ATOM   1921  O   ASP A 571     -32.167   2.329 -27.804  1.00120.73           O  
ANISOU 1921  O   ASP A 571    11798  25593   8482    -72   1463    315       O  
ATOM   1922  CB  ASP A 571     -32.624   4.995 -27.261  1.00172.24           C  
ANISOU 1922  CB  ASP A 571    18567  31886  14991    -77   1582    412       C  
ATOM   1923  CG  ASP A 571     -32.744   6.423 -26.762  1.00191.98           C  
ANISOU 1923  CG  ASP A 571    21255  34224  17466    -98   1658    460       C  
ATOM   1924  OD1 ASP A 571     -32.488   7.354 -27.554  1.00192.12           O  
ANISOU 1924  OD1 ASP A 571    21186  34309  17503    -73   1603    533       O  
ATOM   1925  OD2 ASP A 571     -33.081   6.616 -25.575  1.00199.26           O  
ANISOU 1925  OD2 ASP A 571    22419  34945  18345   -142   1780    423       O  
ATOM   1926  N   LEU A 572     -29.930   2.489 -27.772  1.00122.02           N  
ANISOU 1926  N   LEU A 572    12039  25834   8488   -185   1191    407       N  
ATOM   1927  CA  LEU A 572     -29.726   1.113 -28.193  1.00125.52           C  
ANISOU 1927  CA  LEU A 572    12332  26399   8962   -163   1145    362       C  
ATOM   1928  C   LEU A 572     -29.659   0.189 -26.980  1.00138.96           C  
ANISOU 1928  C   LEU A 572    14218  27971  10608   -206   1190    316       C  
ATOM   1929  O   LEU A 572     -29.445   0.622 -25.847  1.00137.24           O  
ANISOU 1929  O   LEU A 572    14246  27597  10303   -272   1207    333       O  
ATOM   1930  CB  LEU A 572     -28.449   0.985 -29.026  1.00122.98           C  
ANISOU 1930  CB  LEU A 572    11872  26248   8607   -184    961    419       C  
ATOM   1931  CG  LEU A 572     -28.428   1.749 -30.351  1.00120.07           C  
ANISOU 1931  CG  LEU A 572    11302  26033   8288   -144    905    466       C  
ATOM   1932  CD1 LEU A 572     -27.121   1.506 -31.089  1.00116.04           C  
ANISOU 1932  CD1 LEU A 572    10667  25683   7742   -172    733    515       C  
ATOM   1933  CD2 LEU A 572     -29.618   1.362 -31.220  1.00119.38           C  
ANISOU 1933  CD2 LEU A 572    11009  26037   8312    -58   1005    411       C  
ATOM   1934  N   LYS A 573     -29.845  -1.102 -27.237  1.00123.71           N  
ANISOU 1934  N   LYS A 573    12172  26106   8727   -173   1211    258       N  
ATOM   1935  CA  LYS A 573     -29.830  -2.085 -26.163  1.00117.53           C  
ANISOU 1935  CA  LYS A 573    11548  25205   7901   -203   1261    217       C  
ATOM   1936  C   LYS A 573     -28.392  -2.481 -25.829  1.00117.47           C  
ANISOU 1936  C   LYS A 573    11605  25230   7800   -258   1098    280       C  
ATOM   1937  O   LYS A 573     -27.577  -2.681 -26.734  1.00150.78           O  
ANISOU 1937  O   LYS A 573    15650  29606  12034   -245    972    317       O  
ATOM   1938  CB  LYS A 573     -30.633  -3.323 -26.555  1.00117.25           C  
ANISOU 1938  CB  LYS A 573    11371  25216   7961   -147   1364    128       C  
ATOM   1939  CG  LYS A 573     -32.122  -3.067 -26.717  1.00124.86           C  
ANISOU 1939  CG  LYS A 573    12281  26142   9019    -99   1535     63       C  
ATOM   1940  CD  LYS A 573     -32.713  -2.469 -25.451  1.00149.59           C  
ANISOU 1940  CD  LYS A 573    15667  29061  12110   -128   1659     54       C  
ATOM   1941  CE  LYS A 573     -34.189  -2.160 -25.622  1.00142.81           C  
ANISOU 1941  CE  LYS A 573    14740  28165  11356    -72   1835     -2       C  
ATOM   1942  NZ  LYS A 573     -34.758  -1.537 -24.397  1.00119.50           N  
ANISOU 1942  NZ  LYS A 573    12041  24996   8368   -100   1971    -12       N  
ATOM   1943  N   PRO A 574     -28.053  -2.589 -24.547  1.00140.97           N  
ANISOU 1943  N   PRO A 574    14824  28063  10677   -322   1096    298       N  
ATOM   1944  CA  PRO A 574     -26.679  -2.941 -24.177  1.00138.21           C  
ANISOU 1944  CA  PRO A 574    14530  27748  10234   -376    932    372       C  
ATOM   1945  C   PRO A 574     -26.356  -4.391 -24.502  1.00117.88           C  
ANISOU 1945  C   PRO A 574    11827  25252   7708   -328    910    353       C  
ATOM   1946  O   PRO A 574     -27.224  -5.269 -24.478  1.00117.79           O  
ANISOU 1946  O   PRO A 574    11787  25202   7767   -282   1043    274       O  
ATOM   1947  CB  PRO A 574     -26.641  -2.691 -22.663  1.00133.46           C  
ANISOU 1947  CB  PRO A 574    14235  26963   9512   -457    963    387       C  
ATOM   1948  CG  PRO A 574     -27.829  -1.818 -22.375  1.00134.54           C  
ANISOU 1948  CG  PRO A 574    14474  26973   9672   -455   1126    334       C  
ATOM   1949  CD  PRO A 574     -28.865  -2.224 -23.374  1.00118.84           C  
ANISOU 1949  CD  PRO A 574    12262  25060   7831   -356   1238    263       C  
ATOM   1950  N   ASP A 575     -25.078  -4.631 -24.808  1.00117.76           N  
ANISOU 1950  N   ASP A 575    11735  25348   7661   -342    745    427       N  
ATOM   1951  CA  ASP A 575     -24.563  -5.969 -25.112  1.00128.34           C  
ANISOU 1951  CA  ASP A 575    12957  26761   9045   -297    712    427       C  
ATOM   1952  C   ASP A 575     -25.299  -6.593 -26.297  1.00144.76           C  
ANISOU 1952  C   ASP A 575    14806  28940  11255   -220    806    341       C  
ATOM   1953  O   ASP A 575     -25.667  -7.770 -26.275  1.00135.86           O  
ANISOU 1953  O   ASP A 575    13646  27791  10183   -180    894    282       O  
ATOM   1954  CB  ASP A 575     -24.633  -6.883 -23.885  1.00137.36           C  
ANISOU 1954  CB  ASP A 575    14291  27761  10138   -310    767    424       C  
ATOM   1955  CG  ASP A 575     -23.743  -8.106 -24.016  1.00151.44           C  
ANISOU 1955  CG  ASP A 575    15990  29608  11943   -273    696    464       C  
ATOM   1956  OD1 ASP A 575     -22.728  -8.029 -24.740  1.00122.61           O  
ANISOU 1956  OD1 ASP A 575    12186  26096   8303   -264    559    526       O  
ATOM   1957  OD2 ASP A 575     -24.065  -9.147 -23.405  1.00136.41           O  
ANISOU 1957  OD2 ASP A 575    14169  27610  10049   -250    785    435       O  
ATOM   1958  N   THR A 576     -25.512  -5.800 -27.344  1.00155.42           N  
ANISOU 1958  N   THR A 576    15999  30403  12650   -204    786    334       N  
ATOM   1959  CA  THR A 576     -26.246  -6.241 -28.522  1.00115.85           C  
ANISOU 1959  CA  THR A 576    10766  25505   7748   -145    865    255       C  
ATOM   1960  C   THR A 576     -25.426  -5.947 -29.769  1.00115.67           C  
ANISOU 1960  C   THR A 576    10534  25669   7745   -134    739    298       C  
ATOM   1961  O   THR A 576     -24.897  -4.841 -29.923  1.00122.69           O  
ANISOU 1961  O   THR A 576    11436  26595   8588   -166    640    369       O  
ATOM   1962  CB  THR A 576     -27.613  -5.553 -28.614  1.00115.87           C  
ANISOU 1962  CB  THR A 576    10772  25460   7792   -129    995    196       C  
ATOM   1963  OG1 THR A 576     -28.387  -5.869 -27.450  1.00131.58           O  
ANISOU 1963  OG1 THR A 576    12955  27271   9767   -141   1126    151       O  
ATOM   1964  CG2 THR A 576     -28.364  -6.019 -29.854  1.00161.04           C  
ANISOU 1964  CG2 THR A 576    16252  31317  13617    -78   1062    120       C  
ATOM   1965  N   LEU A 577     -25.322  -6.939 -30.651  1.00117.12           N  
ANISOU 1965  N   LEU A 577    10536  25966   7999    -95    753    251       N  
ATOM   1966  CA  LEU A 577     -24.616  -6.791 -31.917  1.00117.56           C  
ANISOU 1966  CA  LEU A 577    10383  26204   8079    -84    655    278       C  
ATOM   1967  C   LEU A 577     -25.564  -6.198 -32.953  1.00114.37           C  
ANISOU 1967  C   LEU A 577     9830  25901   7726    -64    708    231       C  
ATOM   1968  O   LEU A 577     -26.619  -6.775 -33.240  1.00114.31           O  
ANISOU 1968  O   LEU A 577     9754  25898   7779    -39    831    138       O  
ATOM   1969  CB  LEU A 577     -24.073  -8.138 -32.391  1.00114.61           C  
ANISOU 1969  CB  LEU A 577     9892  25900   7756    -55    659    246       C  
ATOM   1970  CG  LEU A 577     -23.327  -8.146 -33.728  1.00114.29           C  
ANISOU 1970  CG  LEU A 577     9633  26047   7744    -44    576    262       C  
ATOM   1971  CD1 LEU A 577     -22.087  -7.268 -33.658  1.00114.35           C  
ANISOU 1971  CD1 LEU A 577     9662  26099   7688    -77    412    381       C  
ATOM   1972  CD2 LEU A 577     -22.960  -9.566 -34.132  1.00114.37           C  
ANISOU 1972  CD2 LEU A 577     9545  26098   7814    -13    620    213       C  
ATOM   1973  N   TYR A 578     -25.188  -5.051 -33.510  1.00114.20           N  
ANISOU 1973  N   TYR A 578     9754  25960   7676    -79    615    298       N  
ATOM   1974  CA  TYR A 578     -25.992  -4.352 -34.502  1.00114.02           C  
ANISOU 1974  CA  TYR A 578     9590  26039   7692    -57    647    279       C  
ATOM   1975  C   TYR A 578     -25.296  -4.367 -35.856  1.00113.70           C  
ANISOU 1975  C   TYR A 578     9339  26196   7664    -53    555    299       C  
ATOM   1976  O   TYR A 578     -24.065  -4.363 -35.942  1.00113.64           O  
ANISOU 1976  O   TYR A 578     9324  26234   7621    -76    443    361       O  
ATOM   1977  CB  TYR A 578     -26.258  -2.905 -34.078  1.00114.25           C  
ANISOU 1977  CB  TYR A 578     9738  25990   7682    -72    634    344       C  
ATOM   1978  CG  TYR A 578     -27.293  -2.751 -32.988  1.00114.64           C  
ANISOU 1978  CG  TYR A 578     9963  25860   7735    -67    761    308       C  
ATOM   1979  CD1 TYR A 578     -28.644  -2.677 -33.296  1.00114.75           C  
ANISOU 1979  CD1 TYR A 578     9905  25877   7817    -25    886    249       C  
ATOM   1980  CD2 TYR A 578     -26.920  -2.668 -31.652  1.00148.29           C  
ANISOU 1980  CD2 TYR A 578    14459  29954  11929   -109    758    335       C  
ATOM   1981  CE1 TYR A 578     -29.596  -2.532 -32.306  1.00115.18           C  
ANISOU 1981  CE1 TYR A 578    10115  25766   7883    -19   1014    215       C  
ATOM   1982  CE2 TYR A 578     -27.867  -2.522 -30.654  1.00122.90           C  
ANISOU 1982  CE2 TYR A 578    11413  26571   8713   -110    885    298       C  
ATOM   1983  CZ  TYR A 578     -29.203  -2.455 -30.987  1.00115.51           C  
ANISOU 1983  CZ  TYR A 578    10399  25634   7855    -62   1018    236       C  
ATOM   1984  OH  TYR A 578     -30.151  -2.310 -30.001  1.00131.06           O  
ANISOU 1984  OH  TYR A 578    12532  27435   9832    -60   1156    198       O  
ATOM   1985  N   ARG A 579     -26.101  -4.379 -36.915  1.00123.06           N  
ANISOU 1985  N   ARG A 579    10353  27506   8898    -29    605    249       N  
ATOM   1986  CA  ARG A 579     -25.614  -4.331 -38.284  1.00113.36           C  
ANISOU 1986  CA  ARG A 579     8922  26474   7675    -30    533    261       C  
ATOM   1987  C   ARG A 579     -26.118  -3.064 -38.958  1.00113.42           C  
ANISOU 1987  C   ARG A 579     8862  26557   7677    -19    509    313       C  
ATOM   1988  O   ARG A 579     -27.204  -2.570 -38.643  1.00113.66           O  
ANISOU 1988  O   ARG A 579     8936  26520   7729      4    588    303       O  
ATOM   1989  CB  ARG A 579     -26.052  -5.571 -39.067  1.00113.31           C  
ANISOU 1989  CB  ARG A 579     8760  26571   7722    -21    608    153       C  
ATOM   1990  CG  ARG A 579     -25.269  -6.808 -38.677  1.00113.31           C  
ANISOU 1990  CG  ARG A 579     8796  26524   7732    -26    616    119       C  
ATOM   1991  CD  ARG A 579     -25.850  -8.087 -39.242  1.00119.13           C  
ANISOU 1991  CD  ARG A 579     9419  27319   8525    -23    724     -3       C  
ATOM   1992  NE  ARG A 579     -25.001  -9.228 -38.910  1.00122.28           N  
ANISOU 1992  NE  ARG A 579     9854  27668   8940    -19    734    -22       N  
ATOM   1993  CZ  ARG A 579     -25.382 -10.498 -38.991  1.00136.26           C  
ANISOU 1993  CZ  ARG A 579    11594  29421  10759    -17    847   -125       C  
ATOM   1994  NH1 ARG A 579     -26.610 -10.799 -39.389  1.00145.76           N  
ANISOU 1994  NH1 ARG A 579    12726  30660  11995    -29    954   -226       N  
ATOM   1995  NH2 ARG A 579     -24.537 -11.467 -38.666  1.00126.66           N  
ANISOU 1995  NH2 ARG A 579    10415  28148   9562     -3    856   -124       N  
ATOM   1996  N   PHE A 580     -25.321  -2.533 -39.883  1.00113.31           N  
ANISOU 1996  N   PHE A 580     8739  26678   7634    -34    405    374       N  
ATOM   1997  CA  PHE A 580     -25.600  -1.223 -40.454  1.00113.45           C  
ANISOU 1997  CA  PHE A 580     8716  26754   7637    -24    369    448       C  
ATOM   1998  C   PHE A 580     -25.372  -1.216 -41.957  1.00113.38           C  
ANISOU 1998  C   PHE A 580     8493  26961   7626    -27    315    454       C  
ATOM   1999  O   PHE A 580     -24.396  -1.786 -42.455  1.00113.19           O  
ANISOU 1999  O   PHE A 580     8394  27026   7588    -52    256    446       O  
ATOM   2000  CB  PHE A 580     -24.729  -0.140 -39.808  1.00113.55           C  
ANISOU 2000  CB  PHE A 580     8880  26670   7594    -55    284    552       C  
ATOM   2001  CG  PHE A 580     -24.882  -0.050 -38.320  1.00125.07           C  
ANISOU 2001  CG  PHE A 580    10566  27919   9036    -67    329    551       C  
ATOM   2002  CD1 PHE A 580     -25.885   0.721 -37.759  1.00114.72           C  
ANISOU 2002  CD1 PHE A 580     9362  26488   7737    -44    414    560       C  
ATOM   2003  CD2 PHE A 580     -24.021  -0.738 -37.481  1.00116.01           C  
ANISOU 2003  CD2 PHE A 580     9525  26694   7858   -101    291    547       C  
ATOM   2004  CE1 PHE A 580     -26.026   0.805 -36.388  1.00136.63           C  
ANISOU 2004  CE1 PHE A 580    12357  29068  10488    -64    464    554       C  
ATOM   2005  CE2 PHE A 580     -24.158  -0.659 -36.112  1.00113.97           C  
ANISOU 2005  CE2 PHE A 580     9483  26249   7570   -120    329    548       C  
ATOM   2006  CZ  PHE A 580     -25.161   0.114 -35.564  1.00114.28           C  
ANISOU 2006  CZ  PHE A 580     9637  26168   7615   -107    418    547       C  
ATOM   2007  N   GLN A 581     -26.285  -0.557 -42.666  1.00123.64           N  
ANISOU 2007  N   GLN A 581     9695  28343   8940      2    340    472       N  
ATOM   2008  CA  GLN A 581     -26.126  -0.218 -44.071  1.00114.61           C  
ANISOU 2008  CA  GLN A 581     8369  27401   7777     -3    279    505       C  
ATOM   2009  C   GLN A 581     -26.594   1.217 -44.262  1.00114.10           C  
ANISOU 2009  C   GLN A 581     8319  27330   7704     28    262    607       C  
ATOM   2010  O   GLN A 581     -27.536   1.666 -43.605  1.00114.39           O  
ANISOU 2010  O   GLN A 581     8437  27251   7774     67    336    616       O  
ATOM   2011  CB  GLN A 581     -26.917  -1.165 -44.983  1.00116.94           C  
ANISOU 2011  CB  GLN A 581     8484  27848   8099     -1    336    407       C  
ATOM   2012  CG  GLN A 581     -26.388  -2.589 -45.013  1.00145.40           C  
ANISOU 2012  CG  GLN A 581    12058  31475  11714    -34    360    306       C  
ATOM   2013  CD  GLN A 581     -27.284  -3.526 -45.799  1.00137.79           C  
ANISOU 2013  CD  GLN A 581    10939  30640  10775    -46    435    195       C  
ATOM   2014  OE1 GLN A 581     -28.426  -3.191 -46.114  1.00122.60           O  
ANISOU 2014  OE1 GLN A 581     8943  28773   8868    -27    474    189       O  
ATOM   2015  NE2 GLN A 581     -26.770  -4.707 -46.121  1.00124.13           N  
ANISOU 2015  NE2 GLN A 581     9156  28959   9049    -80    458    108       N  
ATOM   2016  N   LEU A 582     -25.924   1.938 -45.157  1.00114.18           N  
ANISOU 2016  N   LEU A 582     8252  27457   7672     12    173    687       N  
ATOM   2017  CA  LEU A 582     -26.234   3.339 -45.405  1.00115.38           C  
ANISOU 2017  CA  LEU A 582     8421  27602   7815     42    154    798       C  
ATOM   2018  C   LEU A 582     -26.414   3.577 -46.896  1.00133.32           C  
ANISOU 2018  C   LEU A 582    10492  30095  10067     50    110    833       C  
ATOM   2019  O   LEU A 582     -25.711   2.984 -47.719  1.00123.79           O  
ANISOU 2019  O   LEU A 582     9174  29034   8828      8     57    801       O  
ATOM   2020  CB  LEU A 582     -25.133   4.258 -44.860  1.00114.58           C  
ANISOU 2020  CB  LEU A 582     8471  27392   7671      7     85    886       C  
ATOM   2021  CG  LEU A 582     -25.461   5.753 -44.833  1.00115.13           C  
ANISOU 2021  CG  LEU A 582     8612  27394   7736     36     90    997       C  
ATOM   2022  CD1 LEU A 582     -26.619   6.034 -43.885  1.00115.46           C  
ANISOU 2022  CD1 LEU A 582     8770  27271   7830     89    202    985       C  
ATOM   2023  CD2 LEU A 582     -24.238   6.569 -44.452  1.00115.14           C  
ANISOU 2023  CD2 LEU A 582     8746  27317   7685    -23     13   1073       C  
ATOM   2024  N   ALA A 583     -27.361   4.448 -47.237  1.00124.73           N  
ANISOU 2024  N   ALA A 583     9361  29031   8999    104    138    901       N  
ATOM   2025  CA  ALA A 583     -27.608   4.828 -48.618  1.00126.40           C  
ANISOU 2025  CA  ALA A 583     9392  29450   9184    116     91    957       C  
ATOM   2026  C   ALA A 583     -27.863   6.326 -48.682  1.00128.49           C  
ANISOU 2026  C   ALA A 583     9708  29662   9452    167     83   1098       C  
ATOM   2027  O   ALA A 583     -28.149   6.972 -47.671  1.00120.13           O  
ANISOU 2027  O   ALA A 583     8807  28409   8429    201    138   1134       O  
ATOM   2028  CB  ALA A 583     -28.792   4.056 -49.215  1.00124.61           C  
ANISOU 2028  CB  ALA A 583     8998  29363   8986    137    142    884       C  
ATOM   2029  N   ALA A 584     -27.754   6.876 -49.888  1.00128.18           N  
ANISOU 2029  N   ALA A 584     9538  29792   9371    170     20   1179       N  
ATOM   2030  CA  ALA A 584     -27.920   8.304 -50.120  1.00135.34           C  
ANISOU 2030  CA  ALA A 584    10479  30666  10277    220      9   1326       C  
ATOM   2031  C   ALA A 584     -29.053   8.527 -51.109  1.00138.74           C  
ANISOU 2031  C   ALA A 584    10728  31265  10722    282     17   1380       C  
ATOM   2032  O   ALA A 584     -29.104   7.877 -52.159  1.00153.70           O  
ANISOU 2032  O   ALA A 584    12449  33375  12574    250    -30   1342       O  
ATOM   2033  CB  ALA A 584     -26.625   8.934 -50.641  1.00127.59           C  
ANISOU 2033  CB  ALA A 584     9526  29726   9228    165    -81   1401       C  
ATOM   2034  N   ARG A 585     -29.957   9.440 -50.773  1.00126.38           N  
ANISOU 2034  N   ARG A 585     9202  29603   9214    369     78   1471       N  
ATOM   2035  CA  ARG A 585     -31.092   9.772 -51.622  1.00135.96           C  
ANISOU 2035  CA  ARG A 585    10244  30965  10451    443     86   1546       C  
ATOM   2036  C   ARG A 585     -30.952  11.201 -52.126  1.00139.58           C  
ANISOU 2036  C   ARG A 585    10722  31417  10896    495     57   1722       C  
ATOM   2037  O   ARG A 585     -30.670  12.116 -51.345  1.00142.82           O  
ANISOU 2037  O   ARG A 585    11313  31619  11335    521    101   1786       O  
ATOM   2038  CB  ARG A 585     -32.415   9.604 -50.869  1.00120.77           C  
ANISOU 2038  CB  ARG A 585     8319  28944   8622    517    195   1515       C  
ATOM   2039  CG  ARG A 585     -33.617  10.166 -51.616  1.00125.35           C  
ANISOU 2039  CG  ARG A 585     8731  29654   9243    610    207   1625       C  
ATOM   2040  CD  ARG A 585     -34.908  10.016 -50.826  1.00125.88           C  
ANISOU 2040  CD  ARG A 585     8794  29618   9415    685    324   1595       C  
ATOM   2041  NE  ARG A 585     -35.345   8.627 -50.735  1.00143.41           N  
ANISOU 2041  NE  ARG A 585    10922  31925  11643    631    344   1437       N  
ATOM   2042  CZ  ARG A 585     -36.053   8.005 -51.673  1.00185.61           C  
ANISOU 2042  CZ  ARG A 585    16043  37507  16973    619    309   1410       C  
ATOM   2043  NH1 ARG A 585     -36.400   8.647 -52.780  1.00171.48           N  
ANISOU 2043  NH1 ARG A 585    14095  35905  15157    660    242   1538       N  
ATOM   2044  NH2 ARG A 585     -36.411   6.739 -51.505  1.00199.12           N  
ANISOU 2044  NH2 ARG A 585    17693  39272  18692    559    341   1256       N  
ATOM   2045  N   SER A 586     -31.134  11.383 -53.427  1.00146.39           N  
ANISOU 2045  N   SER A 586    11407  32506  11711    505    -12   1797       N  
ATOM   2046  CA  SER A 586     -31.226  12.694 -54.044  1.00148.07           C  
ANISOU 2046  CA  SER A 586    11606  32739  11915    570    -34   1977       C  
ATOM   2047  C   SER A 586     -32.663  12.920 -54.505  1.00146.45           C  
ANISOU 2047  C   SER A 586    11238  32641  11764    674     -4   2058       C  
ATOM   2048  O   SER A 586     -33.566  12.131 -54.202  1.00152.53           O  
ANISOU 2048  O   SER A 586    11928  33441  12585    691     43   1969       O  
ATOM   2049  CB  SER A 586     -30.228  12.812 -55.198  1.00154.67           C  
ANISOU 2049  CB  SER A 586    12373  33752  12643    499   -143   2021       C  
ATOM   2050  OG  SER A 586     -30.404  14.031 -55.902  1.00160.55           O  
ANISOU 2050  OG  SER A 586    13089  34538  13376    565   -164   2201       O  
ATOM   2051  N   ASP A 587     -32.881  14.008 -55.246  1.00126.31           N  
ANISOU 2051  N   ASP A 587     8635  30152   9205    744    -30   2233       N  
ATOM   2052  CA  ASP A 587     -34.205  14.258 -55.803  1.00140.39           C  
ANISOU 2052  CA  ASP A 587    10240  32066  11036    846    -17   2332       C  
ATOM   2053  C   ASP A 587     -34.610  13.205 -56.825  1.00143.13           C  
ANISOU 2053  C   ASP A 587    10354  32713  11316    788    -98   2261       C  
ATOM   2054  O   ASP A 587     -35.791  13.132 -57.182  1.00128.90           O  
ANISOU 2054  O   ASP A 587     8383  31038   9553    854    -90   2307       O  
ATOM   2055  CB  ASP A 587     -34.261  15.651 -56.436  1.00158.98           C  
ANISOU 2055  CB  ASP A 587    12590  34428  13388    934    -34   2548       C  
ATOM   2056  CG  ASP A 587     -33.252  15.824 -57.554  1.00199.87           C  
ANISOU 2056  CG  ASP A 587    17728  39774  18440    856   -149   2598       C  
ATOM   2057  OD1 ASP A 587     -32.179  15.189 -57.491  1.00207.40           O  
ANISOU 2057  OD1 ASP A 587    18747  40730  19324    737   -191   2475       O  
ATOM   2058  OD2 ASP A 587     -33.533  16.595 -58.496  1.00211.08           O  
ANISOU 2058  OD2 ASP A 587    19050  41321  19832    916   -194   2764       O  
ATOM   2059  N   MET A 588     -33.666  12.388 -57.290  1.00157.94           N  
ANISOU 2059  N   MET A 588    12214  34703  13092    664   -170   2148       N  
ATOM   2060  CA  MET A 588     -33.928  11.345 -58.270  1.00151.46           C  
ANISOU 2060  CA  MET A 588    11194  34159  12195    587   -238   2062       C  
ATOM   2061  C   MET A 588     -34.014   9.958 -57.646  1.00158.71           C  
ANISOU 2061  C   MET A 588    12117  35051  13135    513   -192   1853       C  
ATOM   2062  O   MET A 588     -34.107   8.967 -58.377  1.00161.62           O  
ANISOU 2062  O   MET A 588    12461  35503  13443    422   -206   1741       O  
ATOM   2063  CB  MET A 588     -32.849  11.368 -59.356  1.00131.70           C  
ANISOU 2063  CB  MET A 588     8710  31758   9570    493   -316   2076       C  
ATOM   2064  CG  MET A 588     -32.682  12.723 -60.027  1.00161.80           C  
ANISOU 2064  CG  MET A 588    12507  35619  13349    557   -368   2286       C  
ATOM   2065  SD  MET A 588     -33.986  13.099 -61.212  1.00208.90           S  
ANISOU 2065  SD  MET A 588    18330  41734  19308    622   -380   2423       S  
ATOM   2066  CE  MET A 588     -33.561  11.978 -62.543  1.00203.31           C  
ANISOU 2066  CE  MET A 588    17643  41117  18490    452   -386   2281       C  
ATOM   2067  N   GLY A 589     -33.982   9.859 -56.324  1.00159.59           N  
ANISOU 2067  N   GLY A 589    12393  34912  13333    537   -102   1785       N  
ATOM   2068  CA  GLY A 589     -34.155   8.595 -55.635  1.00159.46           C  
ANISOU 2068  CA  GLY A 589    12393  34847  13348    481    -46   1600       C  
ATOM   2069  C   GLY A 589     -32.936   8.210 -54.818  1.00151.37           C  
ANISOU 2069  C   GLY A 589    11559  33643  12311    415    -31   1502       C  
ATOM   2070  O   GLY A 589     -31.942   8.932 -54.743  1.00141.41           O  
ANISOU 2070  O   GLY A 589    10418  32293  11018    406    -65   1572       O  
ATOM   2071  N   VAL A 590     -33.035   7.033 -54.206  1.00161.75           N  
ANISOU 2071  N   VAL A 590    12894  34911  13651    365     21   1340       N  
ATOM   2072  CA  VAL A 590     -32.015   6.512 -53.303  1.00134.30           C  
ANISOU 2072  CA  VAL A 590     9591  31262  10175    309     42   1241       C  
ATOM   2073  C   VAL A 590     -30.990   5.716 -54.101  1.00124.72           C  
ANISOU 2073  C   VAL A 590     8317  30198   8873    207    -28   1162       C  
ATOM   2074  O   VAL A 590     -31.315   5.064 -55.099  1.00126.84           O  
ANISOU 2074  O   VAL A 590     8416  30685   9094    161    -57   1112       O  
ATOM   2075  CB  VAL A 590     -32.667   5.658 -52.195  1.00126.47           C  
ANISOU 2075  CB  VAL A 590     8663  30131   9260    316    144   1116       C  
ATOM   2076  CG1 VAL A 590     -33.456   4.505 -52.802  1.00137.79           C  
ANISOU 2076  CG1 VAL A 590     9916  31752  10688    273    159   1002       C  
ATOM   2077  CG2 VAL A 590     -31.625   5.142 -51.213  1.00142.50           C  
ANISOU 2077  CG2 VAL A 590    10876  31980  11288    265    161   1029       C  
ATOM   2078  N   GLY A 591     -29.732   5.777 -53.661  1.00126.47           N  
ANISOU 2078  N   GLY A 591     8677  30302   9072    168    -52   1153       N  
ATOM   2079  CA  GLY A 591     -28.663   5.011 -54.263  1.00125.15           C  
ANISOU 2079  CA  GLY A 591     8471  30244   8839     78   -103   1077       C  
ATOM   2080  C   GLY A 591     -28.536   3.626 -53.657  1.00117.51           C  
ANISOU 2080  C   GLY A 591     7531  29218   7898     31    -47    913       C  
ATOM   2081  O   GLY A 591     -29.407   3.143 -52.930  1.00129.29           O  
ANISOU 2081  O   GLY A 591     9047  30625   9453     59     29    846       O  
ATOM   2082  N   VAL A 592     -27.421   2.979 -53.974  1.00117.02           N  
ANISOU 2082  N   VAL A 592     7466  29202   7793    -38    -79    852       N  
ATOM   2083  CA  VAL A 592     -27.139   1.646 -53.456  1.00119.07           C  
ANISOU 2083  CA  VAL A 592     7757  29405   8080    -80    -24    705       C  
ATOM   2084  C   VAL A 592     -26.683   1.752 -52.007  1.00115.79           C  
ANISOU 2084  C   VAL A 592     7536  28740   7717    -54      3    709       C  
ATOM   2085  O   VAL A 592     -26.071   2.743 -51.591  1.00115.67           O  
ANISOU 2085  O   VAL A 592     7631  28622   7695    -36    -41    812       O  
ATOM   2086  CB  VAL A 592     -26.089   0.934 -54.334  1.00116.29           C  
ANISOU 2086  CB  VAL A 592     7328  29187   7670   -157    -58    646       C  
ATOM   2087  CG1 VAL A 592     -26.586   0.810 -55.763  1.00125.52           C  
ANISOU 2087  CG1 VAL A 592     8439  30477   8774   -195    -61    631       C  
ATOM   2088  CG2 VAL A 592     -24.767   1.681 -54.306  1.00116.00           C  
ANISOU 2088  CG2 VAL A 592     7368  29101   7604   -167   -130    739       C  
ATOM   2089  N   PHE A 593     -26.993   0.724 -51.222  1.00115.45           N  
ANISOU 2089  N   PHE A 593     7544  28600   7723    -58     78    596       N  
ATOM   2090  CA  PHE A 593     -26.571   0.694 -49.833  1.00131.27           C  
ANISOU 2090  CA  PHE A 593     9734  30376   9766    -41    104    593       C  
ATOM   2091  C   PHE A 593     -25.094   0.335 -49.729  1.00130.52           C  
ANISOU 2091  C   PHE A 593     9689  30256   9647    -85     52    587       C  
ATOM   2092  O   PHE A 593     -24.514  -0.296 -50.617  1.00123.17           O  
ANISOU 2092  O   PHE A 593     8647  29465   8686   -129     31    541       O  
ATOM   2093  CB  PHE A 593     -27.394  -0.314 -49.029  1.00122.43           C  
ANISOU 2093  CB  PHE A 593     8654  29160   8705    -30    206    479       C  
ATOM   2094  CG  PHE A 593     -28.749   0.188 -48.624  1.00120.23           C  
ANISOU 2094  CG  PHE A 593     8385  28825   8470     25    268    500       C  
ATOM   2095  CD1 PHE A 593     -28.903   0.964 -47.486  1.00123.22           C  
ANISOU 2095  CD1 PHE A 593     8934  29004   8881     70    295    563       C  
ATOM   2096  CD2 PHE A 593     -29.872  -0.128 -49.370  1.00127.66           C  
ANISOU 2096  CD2 PHE A 593     9166  29915   9423     28    305    456       C  
ATOM   2097  CE1 PHE A 593     -30.151   1.424 -47.108  1.00129.12           C  
ANISOU 2097  CE1 PHE A 593     9688  29692   9678    126    366    583       C  
ATOM   2098  CE2 PHE A 593     -31.122   0.328 -48.996  1.00135.18           C  
ANISOU 2098  CE2 PHE A 593    10113  30821  10427     84    365    482       C  
ATOM   2099  CZ  PHE A 593     -31.262   1.106 -47.864  1.00117.86           C  
ANISOU 2099  CZ  PHE A 593     8088  28419   8274    139    401    546       C  
ATOM   2100  N   THR A 594     -24.484   0.751 -48.621  1.00130.40           N  
ANISOU 2100  N   THR A 594     9842  30060   9642    -77     34    635       N  
ATOM   2101  CA  THR A 594     -23.169   0.254 -48.270  1.00115.32           C  
ANISOU 2101  CA  THR A 594     7988  28105   7723   -114     -7    624       C  
ATOM   2102  C   THR A 594     -23.256  -1.242 -47.981  1.00117.11           C  
ANISOU 2102  C   THR A 594     8199  28311   7988   -121     64    498       C  
ATOM   2103  O   THR A 594     -24.344  -1.780 -47.761  1.00121.79           O  
ANISOU 2103  O   THR A 594     8781  28879   8615   -101    148    422       O  
ATOM   2104  CB  THR A 594     -22.628   0.981 -47.038  1.00118.45           C  
ANISOU 2104  CB  THR A 594     8576  28311   8118   -111    -40    698       C  
ATOM   2105  OG1 THR A 594     -23.502   0.752 -45.925  1.00113.59           O  
ANISOU 2105  OG1 THR A 594     8081  27535   7541    -80     39    656       O  
ATOM   2106  CG2 THR A 594     -22.523   2.473 -47.293  1.00113.92           C  
ANISOU 2106  CG2 THR A 594     8034  27741   7510   -109    -97    820       C  
ATOM   2107  N   PRO A 595     -22.125  -1.940 -47.988  1.00113.41           N  
ANISOU 2107  N   PRO A 595     7723  27849   7518   -149     39    475       N  
ATOM   2108  CA  PRO A 595     -22.106  -3.292 -47.428  1.00116.64           C  
ANISOU 2108  CA  PRO A 595     8161  28184   7972   -146    113    373       C  
ATOM   2109  C   PRO A 595     -22.374  -3.248 -45.931  1.00119.63           C  
ANISOU 2109  C   PRO A 595     8724  28353   8376   -119    140    385       C  
ATOM   2110  O   PRO A 595     -22.267  -2.208 -45.279  1.00137.47           O  
ANISOU 2110  O   PRO A 595    11099  30518  10614   -113     91    474       O  
ATOM   2111  CB  PRO A 595     -20.690  -3.788 -47.729  1.00113.26           C  
ANISOU 2111  CB  PRO A 595     7692  27802   7541   -171     66    383       C  
ATOM   2112  CG  PRO A 595     -20.212  -2.937 -48.849  1.00115.92           C  
ANISOU 2112  CG  PRO A 595     7922  28293   7827   -198     -9    451       C  
ATOM   2113  CD  PRO A 595     -20.856  -1.602 -48.654  1.00113.45           C  
ANISOU 2113  CD  PRO A 595     7670  27947   7487   -182    -47    537       C  
ATOM   2114  N   THR A 596     -22.737  -4.404 -45.388  1.00115.81           N  
ANISOU 2114  N   THR A 596     8275  27793   7935   -109    227    291       N  
ATOM   2115  CA  THR A 596     -23.119  -4.471 -43.984  1.00113.01           C  
ANISOU 2115  CA  THR A 596     8096  27242   7599    -87    269    291       C  
ATOM   2116  C   THR A 596     -21.890  -4.373 -43.086  1.00113.57           C  
ANISOU 2116  C   THR A 596     8293  27205   7653    -95    194    364       C  
ATOM   2117  O   THR A 596     -20.913  -5.104 -43.269  1.00123.68           O  
ANISOU 2117  O   THR A 596     9527  28520   8944   -103    169    358       O  
ATOM   2118  CB  THR A 596     -23.875  -5.769 -43.704  1.00113.08           C  
ANISOU 2118  CB  THR A 596     8104  27203   7657    -77    391    169       C  
ATOM   2119  OG1 THR A 596     -24.988  -5.878 -44.600  1.00113.26           O  
ANISOU 2119  OG1 THR A 596     7993  27349   7692    -82    452     99       O  
ATOM   2120  CG2 THR A 596     -24.383  -5.790 -42.275  1.00113.07           C  
ANISOU 2120  CG2 THR A 596     8288  27001   7672    -56    443    168       C  
ATOM   2121  N   ILE A 597     -21.937  -3.459 -42.120  1.00112.95           N  
ANISOU 2121  N   ILE A 597     8372  26998   7547    -97    160    436       N  
ATOM   2122  CA  ILE A 597     -20.922  -3.367 -41.081  1.00113.03           C  
ANISOU 2122  CA  ILE A 597     8524  26892   7530   -116     91    502       C  
ATOM   2123  C   ILE A 597     -21.577  -3.709 -39.749  1.00113.11           C  
ANISOU 2123  C   ILE A 597     8711  26718   7548   -102    164    470       C  
ATOM   2124  O   ILE A 597     -22.802  -3.682 -39.603  1.00122.20           O  
ANISOU 2124  O   ILE A 597     9887  27823   8723    -80    260    415       O  
ATOM   2125  CB  ILE A 597     -20.247  -1.981 -41.024  1.00113.13           C  
ANISOU 2125  CB  ILE A 597     8591  26906   7487   -151    -17    615       C  
ATOM   2126  CG1 ILE A 597     -21.231  -0.922 -40.525  1.00113.23           C  
ANISOU 2126  CG1 ILE A 597     8721  26818   7483   -145     22    638       C  
ATOM   2127  CG2 ILE A 597     -19.688  -1.604 -42.388  1.00113.09           C  
ANISOU 2127  CG2 ILE A 597     8412  27085   7474   -166    -79    646       C  
ATOM   2128  CD1 ILE A 597     -20.591   0.425 -40.265  1.00113.45           C  
ANISOU 2128  CD1 ILE A 597     8844  26808   7455   -188    -67    743       C  
ATOM   2129  N   GLU A 598     -20.743  -4.032 -38.762  1.00117.66           N  
ANISOU 2129  N   GLU A 598     9409  27192   8103   -118    119    509       N  
ATOM   2130  CA  GLU A 598     -21.227  -4.534 -37.485  1.00121.63           C  
ANISOU 2130  CA  GLU A 598    10084  27524   8606   -109    187    479       C  
ATOM   2131  C   GLU A 598     -20.578  -3.795 -36.324  1.00113.76           C  
ANISOU 2131  C   GLU A 598     9278  26407   7540   -152    104    569       C  
ATOM   2132  O   GLU A 598     -19.454  -3.297 -36.426  1.00113.90           O  
ANISOU 2132  O   GLU A 598     9281  26477   7519   -188    -16    651       O  
ATOM   2133  CB  GLU A 598     -20.966  -6.040 -37.344  1.00113.54           C  
ANISOU 2133  CB  GLU A 598     9028  26485   7626    -82    238    422       C  
ATOM   2134  CG  GLU A 598     -21.765  -6.892 -38.313  1.00126.03           C  
ANISOU 2134  CG  GLU A 598    10455  28157   9272    -54    346    311       C  
ATOM   2135  CD  GLU A 598     -21.545  -8.377 -38.113  1.00113.56           C  
ANISOU 2135  CD  GLU A 598     8867  26540   7742    -29    417    250       C  
ATOM   2136  OE1 GLU A 598     -20.456  -8.762 -37.640  1.00113.82           O  
ANISOU 2136  OE1 GLU A 598     8941  26537   7767    -24    353    312       O  
ATOM   2137  OE2 GLU A 598     -22.467  -9.161 -38.427  1.00121.16           O  
ANISOU 2137  OE2 GLU A 598     9778  27507   8751    -16    538    143       O  
ATOM   2138  N   ALA A 599     -21.311  -3.739 -35.214  1.00128.54           N  
ANISOU 2138  N   ALA A 599    11329  28117   9392   -155    174    548       N  
ATOM   2139  CA  ALA A 599     -20.827  -3.162 -33.968  1.00114.45           C  
ANISOU 2139  CA  ALA A 599     9754  26200   7531   -206    115    617       C  
ATOM   2140  C   ALA A 599     -21.661  -3.721 -32.827  1.00114.62           C  
ANISOU 2140  C   ALA A 599     9946  26056   7550   -196    224    563       C  
ATOM   2141  O   ALA A 599     -22.870  -3.921 -32.976  1.00114.46           O  
ANISOU 2141  O   ALA A 599     9907  26003   7579   -159    352    484       O  
ATOM   2142  CB  ALA A 599     -20.899  -1.630 -33.983  1.00114.51           C  
ANISOU 2142  CB  ALA A 599     9828  26190   7489   -249     74    673       C  
ATOM   2143  N   ARG A 600     -21.010  -3.979 -31.697  1.00136.13           N  
ANISOU 2143  N   ARG A 600    12830  28679  10213   -231    173    610       N  
ATOM   2144  CA  ARG A 600     -21.673  -4.481 -30.501  1.00147.43           C  
ANISOU 2144  CA  ARG A 600    14449  29944  11625   -232    268    571       C  
ATOM   2145  C   ARG A 600     -21.650  -3.402 -29.427  1.00127.48           C  
ANISOU 2145  C   ARG A 600    12149  27288   9001   -304    240    621       C  
ATOM   2146  O   ARG A 600     -20.591  -2.838 -29.132  1.00116.32           O  
ANISOU 2146  O   ARG A 600    10789  25894   7512   -366    106    707       O  
ATOM   2147  CB  ARG A 600     -20.998  -5.756 -29.987  1.00115.75           C  
ANISOU 2147  CB  ARG A 600    10457  25909   7614   -215    245    586       C  
ATOM   2148  CG  ARG A 600     -21.870  -6.584 -29.052  1.00116.02           C  
ANISOU 2148  CG  ARG A 600    10635  25791   7656   -195    378    523       C  
ATOM   2149  CD  ARG A 600     -21.104  -7.760 -28.465  1.00116.49           C  
ANISOU 2149  CD  ARG A 600    10733  25819   7709   -178    344    560       C  
ATOM   2150  NE  ARG A 600     -21.963  -8.619 -27.654  1.00146.76           N  
ANISOU 2150  NE  ARG A 600    14698  29510  11555   -157    483    496       N  
ATOM   2151  CZ  ARG A 600     -22.458  -9.783 -28.061  1.00139.19           C  
ANISOU 2151  CZ  ARG A 600    13647  28554  10684    -99    598    417       C  
ATOM   2152  NH1 ARG A 600     -22.171 -10.241 -29.272  1.00129.27           N  
ANISOU 2152  NH1 ARG A 600    12172  27439   9507    -58    590    389       N  
ATOM   2153  NH2 ARG A 600     -23.234 -10.495 -27.256  1.00153.35           N  
ANISOU 2153  NH2 ARG A 600    15576  30208  12482    -89    727    363       N  
ATOM   2154  N   THR A 601     -22.816  -3.115 -28.854  1.00140.37           N  
ANISOU 2154  N   THR A 601    16530  29185   7620   3980   -502   -521       N  
ATOM   2155  CA  THR A 601     -22.895  -2.128 -27.789  1.00140.66           C  
ANISOU 2155  CA  THR A 601    16995  28923   7526   3860   -226   -351       C  
ATOM   2156  C   THR A 601     -22.172  -2.626 -26.543  1.00140.18           C  
ANISOU 2156  C   THR A 601    17235  28597   7431   3599   -356   -428       C  
ATOM   2157  O   THR A 601     -21.998  -3.829 -26.327  1.00139.88           O  
ANISOU 2157  O   THR A 601    17097  28600   7452   3542   -625   -559       O  
ATOM   2158  CB  THR A 601     -24.352  -1.809 -27.447  1.00141.64           C  
ANISOU 2158  CB  THR A 601    17148  29091   7577   3986     14   -161       C  
ATOM   2159  OG1 THR A 601     -25.047  -3.021 -27.125  1.00141.82           O  
ANISOU 2159  OG1 THR A 601    17016  29255   7615   3988   -158   -235       O  
ATOM   2160  CG2 THR A 601     -25.039  -1.125 -28.619  1.00142.44           C  
ANISOU 2160  CG2 THR A 601    16987  29437   7695   4273    180    -61       C  
ATOM   2161  N   ALA A 602     -21.746  -1.676 -25.715  1.00140.32           N  
ANISOU 2161  N   ALA A 602    17626  28343   7347   3448   -148   -350       N  
ATOM   2162  CA  ALA A 602     -21.071  -2.014 -24.475  1.00140.17           C  
ANISOU 2162  CA  ALA A 602    17902  28087   7269   3223   -244   -418       C  
ATOM   2163  C   ALA A 602     -22.063  -2.606 -23.476  1.00140.64           C  
ANISOU 2163  C   ALA A 602    18086  28084   7266   3213   -216   -314       C  
ATOM   2164  O   ALA A 602     -23.284  -2.528 -23.642  1.00141.13           O  
ANISOU 2164  O   ALA A 602    18054  28253   7316   3353    -65   -179       O  
ATOM   2165  CB  ALA A 602     -20.385  -0.783 -23.885  1.00140.47           C  
ANISOU 2165  CB  ALA A 602    18280  27886   7204   3063     -3   -392       C  
ATOM   2166  N   GLN A 603     -21.520  -3.211 -22.426  1.00162.81           N  
ANISOU 2166  N   GLN A 603    21107  30726  10028   3060   -360   -382       N  
ATOM   2167  CA  GLN A 603     -22.350  -3.803 -21.392  1.00141.23           C  
ANISOU 2167  CA  GLN A 603    18533  27910   7216   3048   -326   -284       C  
ATOM   2168  C   GLN A 603     -22.845  -2.738 -20.421  1.00141.79           C  
ANISOU 2168  C   GLN A 603    18952  27756   7167   2969      9   -104       C  
ATOM   2169  O   GLN A 603     -22.249  -1.669 -20.263  1.00141.82           O  
ANISOU 2169  O   GLN A 603    19139  27617   7127   2866    174   -101       O  
ATOM   2170  CB  GLN A 603     -21.580  -4.876 -20.622  1.00141.29           C  
ANISOU 2170  CB  GLN A 603    18653  27822   7210   2950   -594   -408       C  
ATOM   2171  CG  GLN A 603     -21.274  -6.130 -21.416  1.00140.96           C  
ANISOU 2171  CG  GLN A 603    18294  27966   7296   3027   -911   -570       C  
ATOM   2172  CD  GLN A 603     -20.521  -7.160 -20.597  1.00141.29           C  
ANISOU 2172  CD  GLN A 603    18484  27883   7317   2955  -1143   -666       C  
ATOM   2173  OE1 GLN A 603     -21.022  -7.654 -19.587  1.00153.52           O  
ANISOU 2173  OE1 GLN A 603    20244  29333   8755   2956  -1099   -579       O  
ATOM   2174  NE2 GLN A 603     -19.306  -7.481 -21.024  1.00140.80           N  
ANISOU 2174  NE2 GLN A 603    18321  27820   7357   2907  -1375   -835       N  
ATOM   2175  N   SER A 604     -23.961  -3.048 -19.767  1.00142.38           N  
ANISOU 2175  N   SER A 604    19115  27796   7186   3012    128     37       N  
ATOM   2176  CA  SER A 604     -24.462  -2.222 -18.679  1.00142.96           C  
ANISOU 2176  CA  SER A 604    19538  27623   7159   2922    427    209       C  
ATOM   2177  C   SER A 604     -24.709  -3.098 -17.461  1.00143.52           C  
ANISOU 2177  C   SER A 604    19817  27571   7142   2869    360    243       C  
ATOM   2178  O   SER A 604     -24.349  -4.281 -17.455  1.00145.21           O  
ANISOU 2178  O   SER A 604    19932  27873   7366   2896     88    126       O  
ATOM   2179  CB  SER A 604     -25.744  -1.495 -19.092  1.00143.34           C  
ANISOU 2179  CB  SER A 604    19513  27720   7232   3050    724    395       C  
ATOM   2180  OG  SER A 604     -26.175  -0.606 -18.077  1.00143.89           O  
ANISOU 2180  OG  SER A 604    19925  27518   7229   2948   1029    559       O  
ATOM   2181  N   THR A 605     -25.305  -2.534 -16.430  1.00144.12           N  
ANISOU 2181  N   THR A 605    20192  27434   7135   2801    618    405       N  
ATOM   2182  CA  THR A 605     -25.717  -3.349 -15.303  1.00144.84           C  
ANISOU 2182  CA  THR A 605    20482  27413   7136   2786    600    473       C  
ATOM   2183  C   THR A 605     -26.988  -4.116 -15.658  1.00145.22           C  
ANISOU 2183  C   THR A 605    20331  27634   7213   2939    638    552       C  
ATOM   2184  O   THR A 605     -27.744  -3.700 -16.540  1.00145.09           O  
ANISOU 2184  O   THR A 605    20081  27778   7270   3041    761    600       O  
ATOM   2185  CB  THR A 605     -25.966  -2.476 -14.079  1.00145.43           C  
ANISOU 2185  CB  THR A 605    20934  27202   7119   2659    875    619       C  
ATOM   2186  OG1 THR A 605     -27.017  -1.547 -14.362  1.00145.49           O  
ANISOU 2186  OG1 THR A 605    20927  27177   7178   2697   1185    785       O  
ATOM   2187  CG2 THR A 605     -24.704  -1.705 -13.710  1.00147.63           C  
ANISOU 2187  CG2 THR A 605    21392  27356   7347   2495    855    496       C  
ATOM   2188  N   PRO A 606     -27.235  -5.253 -15.006  1.00145.92           N  
ANISOU 2188  N   PRO A 606    20498  27713   7232   2971    547    555       N  
ATOM   2189  CA  PRO A 606     -28.499  -5.962 -15.235  1.00146.61           C  
ANISOU 2189  CA  PRO A 606    20417  27971   7318   3096    639    611       C  
ATOM   2190  C   PRO A 606     -29.691  -5.070 -14.922  1.00147.01           C  
ANISOU 2190  C   PRO A 606    20562  27924   7370   3103    993    816       C  
ATOM   2191  O   PRO A 606     -29.608  -4.143 -14.114  1.00147.00           O  
ANISOU 2191  O   PRO A 606    20864  27648   7340   2994   1177    944       O  
ATOM   2192  CB  PRO A 606     -28.418  -7.153 -14.275  1.00147.57           C  
ANISOU 2192  CB  PRO A 606    20744  27999   7328   3107    555    611       C  
ATOM   2193  CG  PRO A 606     -26.960  -7.382 -14.092  1.00147.17           C  
ANISOU 2193  CG  PRO A 606    20788  27865   7266   3043    281    476       C  
ATOM   2194  CD  PRO A 606     -26.323  -6.019 -14.141  1.00148.61           C  
ANISOU 2194  CD  PRO A 606    21053  27924   7487   2919    350    481       C  
ATOM   2195  N   SER A 607     -30.806  -5.350 -15.593  1.00147.49           N  
ANISOU 2195  N   SER A 607    20340  28232   7468   3229   1088    826       N  
ATOM   2196  CA  SER A 607     -32.024  -4.569 -15.438  1.00148.02           C  
ANISOU 2196  CA  SER A 607    20435  28248   7556   3265   1415   1007       C  
ATOM   2197  C   SER A 607     -33.167  -5.373 -14.838  1.00167.25           C  
ANISOU 2197  C   SER A 607    22900  30717   9928   3308   1576   1074       C  
ATOM   2198  O   SER A 607     -34.275  -4.843 -14.697  1.00162.35           O  
ANISOU 2198  O   SER A 607    22278  30074   9335   3343   1849   1213       O  
ATOM   2199  CB  SER A 607     -32.450  -3.983 -16.790  1.00147.81           C  
ANISOU 2199  CB  SER A 607    20028  28505   7630   3403   1444    968       C  
ATOM   2200  OG  SER A 607     -32.626  -5.003 -17.757  1.00157.56           O  
ANISOU 2200  OG  SER A 607    20852  30136   8880   3523   1245    772       O  
ATOM   2201  N   ALA A 608     -32.930  -6.630 -14.479  1.00162.57           N  
ANISOU 2201  N   ALA A 608    22331  30063   9375   3272   1422    968       N  
ATOM   2202  CA  ALA A 608     -33.942  -7.494 -13.896  1.00168.57           C  
ANISOU 2202  CA  ALA A 608    23105  30576  10368   3210   1567    983       C  
ATOM   2203  C   ALA A 608     -33.295  -8.396 -12.858  1.00177.15           C  
ANISOU 2203  C   ALA A 608    24512  31320  11477   3127   1471    988       C  
ATOM   2204  O   ALA A 608     -32.130  -8.785 -13.007  1.00192.62           O  
ANISOU 2204  O   ALA A 608    26494  33334  13359   3137   1201    877       O  
ATOM   2205  CB  ALA A 608     -34.638  -8.355 -14.963  1.00160.52           C  
ANISOU 2205  CB  ALA A 608    21591  29781   9620   3244   1495    760       C  
ATOM   2206  N   PRO A 609     -34.020  -8.737 -11.798  1.00174.28           N  
ANISOU 2206  N   PRO A 609    24403  30611  11205   3065   1696   1120       N  
ATOM   2207  CA  PRO A 609     -33.462  -9.605 -10.766  1.00153.93           C  
ANISOU 2207  CA  PRO A 609    22155  27701   8629   3031   1642   1152       C  
ATOM   2208  C   PRO A 609     -33.572 -11.063 -11.169  1.00158.45           C  
ANISOU 2208  C   PRO A 609    22508  28203   9492   3017   1542    959       C  
ATOM   2209  O   PRO A 609     -34.233 -11.391 -12.167  1.00185.25           O  
ANISOU 2209  O   PRO A 609    25486  31793  13107   3006   1544    790       O  
ATOM   2210  CB  PRO A 609     -34.341  -9.296  -9.548  1.00154.90           C  
ANISOU 2210  CB  PRO A 609    22621  27492   8741   2983   1972   1384       C  
ATOM   2211  CG  PRO A 609     -35.666  -8.979 -10.148  1.00155.21           C  
ANISOU 2211  CG  PRO A 609    22366  27653   8954   2968   2185   1375       C  
ATOM   2212  CD  PRO A 609     -35.376  -8.272 -11.451  1.00162.03           C  
ANISOU 2212  CD  PRO A 609    22873  28959   9731   3043   2029   1263       C  
ATOM   2213  N   PRO A 610     -32.922 -11.968 -10.438  1.00156.02           N  
ANISOU 2213  N   PRO A 610    22462  27634   9186   3030   1463    967       N  
ATOM   2214  CA  PRO A 610     -33.159 -13.396 -10.665  1.00157.61           C  
ANISOU 2214  CA  PRO A 610    22515  27677   9692   3008   1459    810       C  
ATOM   2215  C   PRO A 610     -34.617 -13.751 -10.410  1.00159.26           C  
ANISOU 2215  C   PRO A 610    22666  27664  10183   2919   1804    830       C  
ATOM   2216  O   PRO A 610     -35.316 -13.093  -9.636  1.00159.48           O  
ANISOU 2216  O   PRO A 610    22921  27534  10142   2892   2054   1027       O  
ATOM   2217  CB  PRO A 610     -32.227 -14.076  -9.656  1.00158.49           C  
ANISOU 2217  CB  PRO A 610    23036  27507   9677   3081   1383    900       C  
ATOM   2218  CG  PRO A 610     -31.139 -13.080  -9.433  1.00156.87           C  
ANISOU 2218  CG  PRO A 610    23006  27502   9095   3143   1181    974       C  
ATOM   2219  CD  PRO A 610     -31.801 -11.735  -9.511  1.00155.73           C  
ANISOU 2219  CD  PRO A 610    22827  27493   8852   3086   1346   1084       C  
ATOM   2220  N   GLN A 611     -35.074 -14.802 -11.082  1.00178.04           N  
ANISOU 2220  N   GLN A 611    24724  30037  12885   2864   1827    601       N  
ATOM   2221  CA  GLN A 611     -36.469 -15.213 -11.042  1.00171.53           C  
ANISOU 2221  CA  GLN A 611    23745  29063  12366   2756   2149    534       C  
ATOM   2222  C   GLN A 611     -36.643 -16.454 -10.177  1.00164.98           C  
ANISOU 2222  C   GLN A 611    23188  27740  11755   2710   2363    551       C  
ATOM   2223  O   GLN A 611     -35.681 -17.153  -9.848  1.00165.14           O  
ANISOU 2223  O   GLN A 611    23433  27591  11721   2783   2230    571       O  
ATOM   2224  CB  GLN A 611     -36.996 -15.499 -12.452  1.00186.46           C  
ANISOU 2224  CB  GLN A 611    25032  31325  14490   2710   2074    216       C  
ATOM   2225  CG  GLN A 611     -36.821 -14.360 -13.437  1.00172.10           C  
ANISOU 2225  CG  GLN A 611    22916  30013  12461   2796   1874    190       C  
ATOM   2226  CD  GLN A 611     -37.258 -14.743 -14.837  1.00176.62           C  
ANISOU 2226  CD  GLN A 611    22883  30984  13241   2787   1777   -139       C  
ATOM   2227  OE1 GLN A 611     -36.497 -15.347 -15.594  1.00187.36           O  
ANISOU 2227  OE1 GLN A 611    24029  32504  14655   2807   1519   -335       O  
ATOM   2228  NE2 GLN A 611     -38.491 -14.398 -15.187  1.00178.46           N  
ANISOU 2228  NE2 GLN A 611    22826  31402  13581   2766   1981   -212       N  
ATOM   2229  N   LYS A 612     -37.902 -16.713  -9.812  1.00177.79           N  
ANISOU 2229  N   LYS A 612    24792  29137  13621   2601   2720    543       N  
ATOM   2230  CA  LYS A 612     -38.296 -17.950  -9.136  1.00187.40           C  
ANISOU 2230  CA  LYS A 612    26206  29875  15121   2534   3006    516       C  
ATOM   2231  C   LYS A 612     -37.524 -18.146  -7.833  1.00183.02           C  
ANISOU 2231  C   LYS A 612    26255  28930  14354   2657   3040    808       C  
ATOM   2232  O   LYS A 612     -37.040 -19.240  -7.532  1.00181.20           O  
ANISOU 2232  O   LYS A 612    26205  28413  14230   2706   3077    784       O  
ATOM   2233  CB  LYS A 612     -38.120 -19.154 -10.067  1.00187.98           C  
ANISOU 2233  CB  LYS A 612    25925  30000  15499   2475   2930    181       C  
ATOM   2234  CG  LYS A 612     -39.012 -20.344  -9.752  1.00198.49           C  
ANISOU 2234  CG  LYS A 612    27258  30919  17240   2334   3327     37       C  
ATOM   2235  CD  LYS A 612     -38.773 -21.469 -10.749  1.00194.74           C  
ANISOU 2235  CD  LYS A 612    26407  30526  17059   2266   3245   -321       C  
ATOM   2236  CE  LYS A 612     -39.656 -22.672 -10.464  1.00191.79           C  
ANISOU 2236  CE  LYS A 612    26028  29722  17122   2102   3688   -500       C  
ATOM   2237  NZ  LYS A 612     -39.386 -23.788 -11.413  1.00180.37           N  
ANISOU 2237  NZ  LYS A 612    24227  28337  15970   2024   3631   -864       N  
ATOM   2238  N   VAL A 613     -37.405 -17.078  -7.052  1.00170.21           N  
ANISOU 2238  N   VAL A 613    24945  27309  12418   2723   3041   1081       N  
ATOM   2239  CA  VAL A 613     -36.647 -17.124  -5.806  1.00172.41           C  
ANISOU 2239  CA  VAL A 613    25774  27297  12437   2863   3049   1349       C  
ATOM   2240  C   VAL A 613     -37.465 -17.850  -4.746  1.00181.26           C  
ANISOU 2240  C   VAL A 613    27226  27894  13752   2838   3470   1482       C  
ATOM   2241  O   VAL A 613     -38.618 -17.492  -4.477  1.00186.27           O  
ANISOU 2241  O   VAL A 613    27839  28416  14520   2722   3759   1530       O  
ATOM   2242  CB  VAL A 613     -36.270 -15.708  -5.345  1.00171.07           C  
ANISOU 2242  CB  VAL A 613    25801  27323  11874   2921   2928   1558       C  
ATOM   2243  CG1 VAL A 613     -35.514 -15.762  -4.026  1.00169.26           C  
ANISOU 2243  CG1 VAL A 613    26114  26836  11359   3074   2938   1804       C  
ATOM   2244  CG2 VAL A 613     -35.441 -15.007  -6.411  1.00166.05           C  
ANISOU 2244  CG2 VAL A 613    24853  27178  11062   2945   2551   1419       C  
ATOM   2245  N   MET A 614     -36.866 -18.872  -4.136  1.00177.56           N  
ANISOU 2245  N   MET A 614    27073  27101  13292   2962   3522   1549       N  
ATOM   2246  CA  MET A 614     -37.511 -19.654  -3.092  1.00178.30           C  
ANISOU 2246  CA  MET A 614    27534  26656  13556   2976   3945   1695       C  
ATOM   2247  C   MET A 614     -36.581 -19.773  -1.893  1.00188.74           C  
ANISOU 2247  C   MET A 614    29410  27765  14538   3228   3910   1980       C  
ATOM   2248  O   MET A 614     -35.356 -19.726  -2.031  1.00176.19           O  
ANISOU 2248  O   MET A 614    27865  26403  12675   3387   3564   1980       O  
ATOM   2249  CB  MET A 614     -37.896 -21.055  -3.587  1.00178.98           C  
ANISOU 2249  CB  MET A 614    27441  26486  14077   2889   4160   1461       C  
ATOM   2250  CG  MET A 614     -38.809 -21.063  -4.800  1.00196.53           C  
ANISOU 2250  CG  MET A 614    29072  28955  16644   2647   4197   1123       C  
ATOM   2251  SD  MET A 614     -39.209 -22.734  -5.345  1.00219.25           S  
ANISOU 2251  SD  MET A 614    31737  31527  20042   2519   4478    802       S  
ATOM   2252  CE  MET A 614     -40.143 -22.393  -6.833  1.00197.89           C  
ANISOU 2252  CE  MET A 614    28269  29308  17612   2268   4404    387       C  
ATOM   2253  N   CYS A 615     -37.179 -19.931  -0.713  1.00201.19           N  
ANISOU 2253  N   CYS A 615    31399  28923  16122   3274   4275   2213       N  
ATOM   2254  CA  CYS A 615     -36.431 -20.085   0.528  1.00180.46           C  
ANISOU 2254  CA  CYS A 615    29318  26083  13167   3544   4296   2496       C  
ATOM   2255  C   CYS A 615     -37.066 -21.187   1.361  1.00184.09           C  
ANISOU 2255  C   CYS A 615    30125  25955  13864   3605   4774   2624       C  
ATOM   2256  O   CYS A 615     -38.287 -21.208   1.540  1.00185.12           O  
ANISOU 2256  O   CYS A 615    30230  25830  14277   3424   5141   2623       O  
ATOM   2257  CB  CYS A 615     -36.394 -18.776   1.326  1.00178.87           C  
ANISOU 2257  CB  CYS A 615    29340  26028  12594   3582   4231   2716       C  
ATOM   2258  SG  CYS A 615     -35.487 -17.430   0.530  1.00200.04           S  
ANISOU 2258  SG  CYS A 615    31714  29350  14943   3544   3720   2598       S  
ATOM   2259  N   VAL A 616     -36.237 -22.103   1.861  1.00198.65           N  
ANISOU 2259  N   VAL A 616    32296  27590  15591   3871   4787   2731       N  
ATOM   2260  CA  VAL A 616     -36.682 -23.202   2.711  1.00203.19           C  
ANISOU 2260  CA  VAL A 616    33271  27581  16352   3991   5264   2887       C  
ATOM   2261  C   VAL A 616     -35.726 -23.320   3.889  1.00191.41           C  
ANISOU 2261  C   VAL A 616    32318  25998  14413   4386   5214   3194       C  
ATOM   2262  O   VAL A 616     -34.504 -23.245   3.719  1.00190.45           O  
ANISOU 2262  O   VAL A 616    32192  26202  13968   4587   4820   3178       O  
ATOM   2263  CB  VAL A 616     -36.753 -24.538   1.939  1.00213.98           C  
ANISOU 2263  CB  VAL A 616    34448  28720  18133   3927   5429   2654       C  
ATOM   2264  CG1 VAL A 616     -37.207 -25.665   2.859  1.00196.35           C  
ANISOU 2264  CG1 VAL A 616    32671  25837  16096   4061   5983   2829       C  
ATOM   2265  CG2 VAL A 616     -37.684 -24.424   0.741  1.00221.08           C  
ANISOU 2265  CG2 VAL A 616    34768  29776  19455   3547   5460   2308       C  
ATOM   2266  N   SER A 617     -36.284 -23.502   5.085  1.00193.85           N  
ANISOU 2266  N   SER A 617    33082  25883  14689   4508   5617   3465       N  
ATOM   2267  CA  SER A 617     -35.501 -23.727   6.295  1.00195.91           C  
ANISOU 2267  CA  SER A 617    33883  26021  14531   4924   5642   3772       C  
ATOM   2268  C   SER A 617     -35.452 -25.229   6.558  1.00199.94           C  
ANISOU 2268  C   SER A 617    34687  26034  15248   5137   6015   3847       C  
ATOM   2269  O   SER A 617     -36.457 -25.831   6.949  1.00202.52           O  
ANISOU 2269  O   SER A 617    35195  25843  15911   5054   6538   3918       O  
ATOM   2270  CB  SER A 617     -36.102 -22.979   7.484  1.00196.25           C  
ANISOU 2270  CB  SER A 617    34270  25919  14378   4963   5860   4041       C  
ATOM   2271  OG  SER A 617     -37.391 -23.474   7.802  1.00198.43           O  
ANISOU 2271  OG  SER A 617    34667  25671  15057   4804   6403   4098       O  
ATOM   2272  N   MET A 618     -34.283 -25.831   6.335  1.00200.63           N  
ANISOU 2272  N   MET A 618    34822  26272  15138   5413   5768   3825       N  
ATOM   2273  CA  MET A 618     -34.115 -27.263   6.543  1.00204.59           C  
ANISOU 2273  CA  MET A 618    35614  26315  15804   5655   6116   3905       C  
ATOM   2274  C   MET A 618     -33.913 -27.623   8.008  1.00208.05           C  
ANISOU 2274  C   MET A 618    36702  26430  15918   6100   6414   4298       C  
ATOM   2275  O   MET A 618     -34.175 -28.768   8.393  1.00212.60           O  
ANISOU 2275  O   MET A 618    37606  26470  16701   6272   6892   4425       O  
ATOM   2276  CB  MET A 618     -32.931 -27.776   5.720  1.00204.07           C  
ANISOU 2276  CB  MET A 618    35348  26550  15642   5801   5735   3736       C  
ATOM   2277  CG  MET A 618     -33.018 -27.450   4.235  1.00203.88           C  
ANISOU 2277  CG  MET A 618    34680  26883  15904   5405   5412   3348       C  
ATOM   2278  SD  MET A 618     -33.823 -28.737   3.263  1.00220.73           S  
ANISOU 2278  SD  MET A 618    36547  28587  18733   5124   5820   3067       S  
ATOM   2279  CE  MET A 618     -32.547 -29.994   3.248  1.00220.40           C  
ANISOU 2279  CE  MET A 618    36758  28439  18547   5546   5769   3129       C  
ATOM   2280  N   GLY A 619     -33.456 -26.680   8.828  1.00213.73           N  
ANISOU 2280  N   GLY A 619    37615  27461  16133   6295   6166   4485       N  
ATOM   2281  CA  GLY A 619     -33.227 -26.943  10.234  1.00210.22           C  
ANISOU 2281  CA  GLY A 619    37768  26784  15323   6749   6412   4852       C  
ATOM   2282  C   GLY A 619     -33.540 -25.758  11.124  1.00208.88           C  
ANISOU 2282  C   GLY A 619    37741  26782  14843   6731   6356   5014       C  
ATOM   2283  O   GLY A 619     -34.260 -24.839  10.721  1.00205.88           O  
ANISOU 2283  O   GLY A 619    37048  26536  14643   6323   6280   4874       O  
ATOM   2284  N   SER A 620     -32.999 -25.768  12.342  1.00214.10           N  
ANISOU 2284  N   SER A 620    38875  27453  15022   7191   6398   5309       N  
ATOM   2285  CA  SER A 620     -33.273 -24.705  13.298  1.00222.02           C  
ANISOU 2285  CA  SER A 620    40054  28594  15708   7207   6378   5473       C  
ATOM   2286  C   SER A 620     -32.412 -23.470  13.073  1.00218.43           C  
ANISOU 2286  C   SER A 620    39310  28843  14840   7146   5780   5307       C  
ATOM   2287  O   SER A 620     -32.768 -22.389  13.555  1.00216.28           O  
ANISOU 2287  O   SER A 620    39041  28729  14408   7003   5730   5350       O  
ATOM   2288  CB  SER A 620     -33.067 -25.219  14.724  1.00224.37           C  
ANISOU 2288  CB  SER A 620    40973  28634  15642   7743   6685   5847       C  
ATOM   2289  OG  SER A 620     -31.738 -25.672  14.909  1.00223.55           O  
ANISOU 2289  OG  SER A 620    40990  28835  15114   8214   6400   5880       O  
ATOM   2290  N   THR A 621     -31.291 -23.602  12.360  1.00205.89           N  
ANISOU 2290  N   THR A 621    37477  27669  13082   7244   5350   5112       N  
ATOM   2291  CA  THR A 621     -30.378 -22.487  12.142  1.00202.93           C  
ANISOU 2291  CA  THR A 621    36835  27959  12310   7197   4803   4931       C  
ATOM   2292  C   THR A 621     -29.932 -22.358  10.689  1.00216.20           C  
ANISOU 2292  C   THR A 621    37983  29965  14197   6906   4422   4589       C  
ATOM   2293  O   THR A 621     -28.957 -21.648  10.418  1.00215.63           O  
ANISOU 2293  O   THR A 621    37696  30444  13790   6923   3962   4416       O  
ATOM   2294  CB  THR A 621     -29.139 -22.621  13.036  1.00205.32           C  
ANISOU 2294  CB  THR A 621    37172  28506  12335   7582   4487   4926       C  
ATOM   2295  OG1 THR A 621     -28.494 -23.875  12.779  1.00207.86           O  
ANISOU 2295  OG1 THR A 621    37687  28738  12552   7962   4545   4992       O  
ATOM   2296  CG2 THR A 621     -29.520 -22.545  14.509  1.00208.20           C  
ANISOU 2296  CG2 THR A 621    37832  28595  12681   7767   4727   5149       C  
ATOM   2297  N   THR A 622     -30.615 -23.011   9.749  1.00216.08           N  
ANISOU 2297  N   THR A 622    37739  29640  14720   6638   4607   4468       N  
ATOM   2298  CA  THR A 622     -30.192 -23.034   8.355  1.00197.22           C  
ANISOU 2298  CA  THR A 622    34858  27541  12537   6401   4269   4152       C  
ATOM   2299  C   THR A 622     -31.380 -22.758   7.444  1.00194.61           C  
ANISOU 2299  C   THR A 622    34155  27051  12738   5906   4423   3982       C  
ATOM   2300  O   THR A 622     -32.481 -23.269   7.670  1.00196.31           O  
ANISOU 2300  O   THR A 622    34502  26772  13316   5795   4883   4079       O  
ATOM   2301  CB  THR A 622     -29.558 -24.387   7.993  1.00203.25           C  
ANISOU 2301  CB  THR A 622    35686  28154  13386   6663   4293   4128       C  
ATOM   2302  OG1 THR A 622     -28.502 -24.686   8.916  1.00201.76           O  
ANISOU 2302  OG1 THR A 622    35870  28117  12674   7179   4183   4310       O  
ATOM   2303  CG2 THR A 622     -28.989 -24.357   6.579  1.00196.50           C  
ANISOU 2303  CG2 THR A 622    34318  27658  12684   6445   3893   3795       C  
ATOM   2304  N   VAL A 623     -31.148 -21.944   6.416  1.00191.02           N  
ANISOU 2304  N   VAL A 623    33232  27030  12318   5623   4048   3721       N  
ATOM   2305  CA  VAL A 623     -32.152 -21.618   5.411  1.00189.68           C  
ANISOU 2305  CA  VAL A 623    32643  26826  12599   5189   4125   3527       C  
ATOM   2306  C   VAL A 623     -31.519 -21.771   4.036  1.00194.89           C  
ANISOU 2306  C   VAL A 623    32839  27827  13384   5064   3759   3224       C  
ATOM   2307  O   VAL A 623     -30.424 -21.253   3.791  1.00194.89           O  
ANISOU 2307  O   VAL A 623    32723  28281  13047   5158   3334   3130       O  
ATOM   2308  CB  VAL A 623     -32.712 -20.194   5.596  1.00186.27           C  
ANISOU 2308  CB  VAL A 623    32114  26594  12064   4955   4083   3549       C  
ATOM   2309  CG1 VAL A 623     -33.455 -19.744   4.348  1.00183.63           C  
ANISOU 2309  CG1 VAL A 623    31269  26399  12102   4562   4034   3306       C  
ATOM   2310  CG2 VAL A 623     -33.630 -20.142   6.805  1.00191.30           C  
ANISOU 2310  CG2 VAL A 623    33157  26821  12706   5006   4514   3825       C  
ATOM   2311  N   ARG A 624     -32.203 -22.482   3.145  1.00196.90           N  
ANISOU 2311  N   ARG A 624    32818  27874  14121   4850   3932   3053       N  
ATOM   2312  CA  ARG A 624     -31.729 -22.711   1.787  1.00189.33           C  
ANISOU 2312  CA  ARG A 624    31397  27210  13330   4718   3624   2754       C  
ATOM   2313  C   ARG A 624     -32.489 -21.799   0.833  1.00184.16           C  
ANISOU 2313  C   ARG A 624    30270  26806  12897   4344   3537   2553       C  
ATOM   2314  O   ARG A 624     -33.723 -21.839   0.781  1.00182.91           O  
ANISOU 2314  O   ARG A 624    30030  26392  13077   4128   3873   2537       O  
ATOM   2315  CB  ARG A 624     -31.908 -24.177   1.394  1.00192.19           C  
ANISOU 2315  CB  ARG A 624    31751  27203  14071   4749   3874   2667       C  
ATOM   2316  CG  ARG A 624     -31.580 -24.482  -0.057  1.00186.42           C  
ANISOU 2316  CG  ARG A 624    30514  26744  13574   4580   3601   2336       C  
ATOM   2317  CD  ARG A 624     -31.468 -25.980  -0.275  1.00197.76           C  
ANISOU 2317  CD  ARG A 624    32025  27821  15294   4685   3828   2274       C  
ATOM   2318  NE  ARG A 624     -30.467 -26.567   0.610  1.00203.20           N  
ANISOU 2318  NE  ARG A 624    33178  28393  15634   5111   3811   2505       N  
ATOM   2319  CZ  ARG A 624     -30.212 -27.867   0.698  1.00217.22           C  
ANISOU 2319  CZ  ARG A 624    35159  29818  17555   5310   4043   2538       C  
ATOM   2320  NH1 ARG A 624     -30.888 -28.731  -0.048  1.00231.03           N  
ANISOU 2320  NH1 ARG A 624    36683  31280  19817   5085   4321   2332       N  
ATOM   2321  NH2 ARG A 624     -29.281 -28.304   1.535  1.00197.01           N  
ANISOU 2321  NH2 ARG A 624    33029  27208  14619   5744   4011   2769       N  
ATOM   2322  N   VAL A 625     -31.755 -20.977   0.086  1.00179.43           N  
ANISOU 2322  N   VAL A 625    29365  26713  12098   4284   3102   2397       N  
ATOM   2323  CA  VAL A 625     -32.335 -20.070  -0.897  1.00176.72           C  
ANISOU 2323  CA  VAL A 625    28570  26664  11912   3986   2991   2214       C  
ATOM   2324  C   VAL A 625     -32.033 -20.609  -2.289  1.00175.75           C  
ANISOU 2324  C   VAL A 625    27989  26756  12030   3886   2769   1916       C  
ATOM   2325  O   VAL A 625     -30.915 -21.060  -2.565  1.00175.74           O  
ANISOU 2325  O   VAL A 625    27979  26917  11879   4047   2490   1842       O  
ATOM   2326  CB  VAL A 625     -31.812 -18.627  -0.725  1.00174.05           C  
ANISOU 2326  CB  VAL A 625    28230  26723  11178   3979   2718   2264       C  
ATOM   2327  CG1 VAL A 625     -30.297 -18.570  -0.852  1.00173.31           C  
ANISOU 2327  CG1 VAL A 625    28148  26971  10730   4169   2305   2192       C  
ATOM   2328  CG2 VAL A 625     -32.473 -17.693  -1.730  1.00171.47           C  
ANISOU 2328  CG2 VAL A 625    27468  26672  11010   3708   2657   2108       C  
ATOM   2329  N   SER A 626     -33.041 -20.585  -3.157  1.00175.67           N  
ANISOU 2329  N   SER A 626    27591  26765  12389   3631   2898   1734       N  
ATOM   2330  CA  SER A 626     -32.913 -21.070  -4.522  1.00189.29           C  
ANISOU 2330  CA  SER A 626    28838  28713  14370   3515   2716   1426       C  
ATOM   2331  C   SER A 626     -33.386 -19.994  -5.488  1.00177.98           C  
ANISOU 2331  C   SER A 626    26958  27692  12974   3316   2563   1273       C  
ATOM   2332  O   SER A 626     -34.255 -19.183  -5.159  1.00181.88           O  
ANISOU 2332  O   SER A 626    27475  28167  13462   3213   2746   1376       O  
ATOM   2333  CB  SER A 626     -33.716 -22.360  -4.740  1.00190.39           C  
ANISOU 2333  CB  SER A 626    28895  28469  14976   3418   3069   1293       C  
ATOM   2334  OG  SER A 626     -33.272 -23.390  -3.874  1.00196.56           O  
ANISOU 2334  OG  SER A 626    30114  28843  15728   3631   3251   1451       O  
ATOM   2335  N   TRP A 627     -32.807 -19.996  -6.686  1.00170.17           N  
ANISOU 2335  N   TRP A 627    25567  27077  12011   3282   2237   1036       N  
ATOM   2336  CA  TRP A 627     -33.152 -19.006  -7.698  1.00179.45           C  
ANISOU 2336  CA  TRP A 627    26311  28678  13194   3143   2080    892       C  
ATOM   2337  C   TRP A 627     -32.691 -19.511  -9.056  1.00172.10           C  
ANISOU 2337  C   TRP A 627    24924  28047  12419   3108   1810    591       C  
ATOM   2338  O   TRP A 627     -31.951 -20.491  -9.161  1.00170.42           O  
ANISOU 2338  O   TRP A 627    24759  27737  12256   3197   1703    512       O  
ATOM   2339  CB  TRP A 627     -32.518 -17.646  -7.390  1.00187.21           C  
ANISOU 2339  CB  TRP A 627    27437  29933  13760   3208   1869   1048       C  
ATOM   2340  CG  TRP A 627     -31.021 -17.655  -7.497  1.00188.05           C  
ANISOU 2340  CG  TRP A 627    27618  30256  13577   3357   1498   1016       C  
ATOM   2341  CD1 TRP A 627     -30.277 -17.454  -8.624  1.00162.71           C  
ANISOU 2341  CD1 TRP A 627    24059  27443  10319   3350   1158    813       C  
ATOM   2342  CD2 TRP A 627     -30.086 -17.878  -6.435  1.00184.33           C  
ANISOU 2342  CD2 TRP A 627    27585  29641  12813   3549   1432   1181       C  
ATOM   2343  NE1 TRP A 627     -28.938 -17.541  -8.330  1.00162.44           N  
ANISOU 2343  NE1 TRP A 627    24215  27511   9992   3505    886    830       N  
ATOM   2344  CE2 TRP A 627     -28.794 -17.799  -6.992  1.00191.88           C  
ANISOU 2344  CE2 TRP A 627    28418  30931  13556   3638   1041   1049       C  
ATOM   2345  CE3 TRP A 627     -30.217 -18.137  -5.068  1.00179.81           C  
ANISOU 2345  CE3 TRP A 627    27490  28708  12121   3671   1667   1422       C  
ATOM   2346  CZ2 TRP A 627     -27.641 -17.969  -6.229  1.00190.14           C  
ANISOU 2346  CZ2 TRP A 627    28517  30724  13005   3844    872   1132       C  
ATOM   2347  CZ3 TRP A 627     -29.071 -18.305  -4.313  1.00188.94           C  
ANISOU 2347  CZ3 TRP A 627    28969  29882  12936   3896   1499   1519       C  
ATOM   2348  CH2 TRP A 627     -27.800 -18.221  -4.895  1.00168.50           C  
ANISOU 2348  CH2 TRP A 627    26230  27657  10135   3980   1101   1365       C  
ATOM   2349  N   VAL A 628     -33.137 -18.821 -10.100  1.00165.41           N  
ANISOU 2349  N   VAL A 628    23636  27576  11636   2998   1709    430       N  
ATOM   2350  CA  VAL A 628     -32.641 -19.046 -11.454  1.00172.63           C  
ANISOU 2350  CA  VAL A 628    24093  28865  12633   2982   1410    154       C  
ATOM   2351  C   VAL A 628     -32.113 -17.717 -11.981  1.00186.03           C  
ANISOU 2351  C   VAL A 628    25655  31004  14023   3022   1135    185       C  
ATOM   2352  O   VAL A 628     -32.549 -16.658 -11.509  1.00177.43           O  
ANISOU 2352  O   VAL A 628    24708  29939  12768   3009   1257    365       O  
ATOM   2353  CB  VAL A 628     -33.731 -19.627 -12.367  1.00165.53           C  
ANISOU 2353  CB  VAL A 628    22725  28030  12138   2827   1575   -124       C  
ATOM   2354  CG1 VAL A 628     -34.227 -20.962 -11.824  1.00168.60           C  
ANISOU 2354  CG1 VAL A 628    23267  27939  12853   2765   1898   -175       C  
ATOM   2355  CG2 VAL A 628     -34.880 -18.646 -12.524  1.00164.97           C  
ANISOU 2355  CG2 VAL A 628    22465  28133  12082   2742   1747    -97       C  
ATOM   2356  N   PRO A 629     -31.178 -17.711 -12.928  1.00160.11           N  
ANISOU 2356  N   PRO A 629    22119  28058  10657   3071    791     21       N  
ATOM   2357  CA  PRO A 629     -30.636 -16.443 -13.435  1.00157.65           C  
ANISOU 2357  CA  PRO A 629    21700  28141  10060   3110    567     48       C  
ATOM   2358  C   PRO A 629     -31.723 -15.599 -14.077  1.00160.88           C  
ANISOU 2358  C   PRO A 629    21799  28785  10544   3044    711     20       C  
ATOM   2359  O   PRO A 629     -32.780 -16.121 -14.467  1.00164.30           O  
ANISOU 2359  O   PRO A 629    21961  29192  11274   2965    893   -115       O  
ATOM   2360  CB  PRO A 629     -29.594 -16.894 -14.470  1.00158.68           C  
ANISOU 2360  CB  PRO A 629    21551  28557  10185   3160    209   -175       C  
ATOM   2361  CG  PRO A 629     -29.219 -18.271 -14.060  1.00158.60           C  
ANISOU 2361  CG  PRO A 629    21698  28238  10325   3193    213   -224       C  
ATOM   2362  CD  PRO A 629     -30.475 -18.874 -13.491  1.00160.81           C  
ANISOU 2362  CD  PRO A 629    22060  28149  10893   3103    604   -181       C  
ATOM   2363  N   PRO A 630     -31.509 -14.290 -14.194  1.00164.25           N  
ANISOU 2363  N   PRO A 630    22254  29449  10703   3083    656    134       N  
ATOM   2364  CA  PRO A 630     -32.490 -13.429 -14.869  1.00158.21           C  
ANISOU 2364  CA  PRO A 630    21197  28946   9971   3071    793    125       C  
ATOM   2365  C   PRO A 630     -32.699 -13.873 -16.305  1.00154.78           C  
ANISOU 2365  C   PRO A 630    20209  28869   9730   3083    644   -160       C  
ATOM   2366  O   PRO A 630     -31.845 -14.569 -16.875  1.00154.52           O  
ANISOU 2366  O   PRO A 630    20031  28936   9742   3102    382   -334       O  
ATOM   2367  CB  PRO A 630     -31.841 -12.037 -14.805  1.00152.90           C  
ANISOU 2367  CB  PRO A 630    20690  28457   8950   3134    722    282       C  
ATOM   2368  CG  PRO A 630     -30.895 -12.112 -13.657  1.00152.89           C  
ANISOU 2368  CG  PRO A 630    21154  28187   8751   3137    662    418       C  
ATOM   2369  CD  PRO A 630     -30.376 -13.518 -13.654  1.00153.94           C  
ANISOU 2369  CD  PRO A 630    21269  28177   9045   3145    503    274       C  
ATOM   2370  N   PRO A 631     -33.823 -13.505 -16.922  1.00156.36           N  
ANISOU 2370  N   PRO A 631    20079  29291  10039   3085    802   -225       N  
ATOM   2371  CA  PRO A 631     -34.044 -13.890 -18.321  1.00167.72           C  
ANISOU 2371  CA  PRO A 631    20957  31132  11637   3119    656   -517       C  
ATOM   2372  C   PRO A 631     -32.943 -13.334 -19.210  1.00153.51           C  
ANISOU 2372  C   PRO A 631    19023  29685   9617   3234    345   -560       C  
ATOM   2373  O   PRO A 631     -32.426 -12.239 -18.979  1.00152.06           O  
ANISOU 2373  O   PRO A 631    19074  29552   9149   3300    329   -362       O  
ATOM   2374  CB  PRO A 631     -35.412 -13.278 -18.650  1.00164.04           C  
ANISOU 2374  CB  PRO A 631    20229  30878  11220   3149    899   -519       C  
ATOM   2375  CG  PRO A 631     -35.613 -12.205 -17.631  1.00168.18           C  
ANISOU 2375  CG  PRO A 631    21185  31194  11520   3166   1108   -185       C  
ATOM   2376  CD  PRO A 631     -34.924 -12.684 -16.391  1.00162.98           C  
ANISOU 2376  CD  PRO A 631    21027  30063  10836   3078   1113    -40       C  
ATOM   2377  N   ALA A 632     -32.579 -14.116 -20.232  1.00153.64           N  
ANISOU 2377  N   ALA A 632    18659  29937   9779   3245    115   -835       N  
ATOM   2378  CA  ALA A 632     -31.388 -13.814 -21.020  1.00151.93           C  
ANISOU 2378  CA  ALA A 632    18341  30003   9384   3338   -203   -896       C  
ATOM   2379  C   ALA A 632     -31.443 -12.415 -21.619  1.00150.66           C  
ANISOU 2379  C   ALA A 632    18085  30190   8968   3478   -182   -780       C  
ATOM   2380  O   ALA A 632     -30.416 -11.735 -21.717  1.00149.11           O  
ANISOU 2380  O   ALA A 632    18048  30075   8533   3534   -329   -694       O  
ATOM   2381  CB  ALA A 632     -31.212 -14.860 -22.121  1.00152.49           C  
ANISOU 2381  CB  ALA A 632    17956  30308   9676   3333   -419  -1227       C  
ATOM   2382  N   ASP A 633     -32.634 -11.961 -22.010  1.00162.04           N  
ANISOU 2382  N   ASP A 633    19276  31839  10451   3544     24   -778       N  
ATOM   2383  CA  ASP A 633     -32.759 -10.681 -22.697  1.00167.75           C  
ANISOU 2383  CA  ASP A 633    19881  32920  10938   3724     73   -668       C  
ATOM   2384  C   ASP A 633     -32.619  -9.480 -21.769  1.00163.81           C  
ANISOU 2384  C   ASP A 633    19854  32199  10185   3732    275   -342       C  
ATOM   2385  O   ASP A 633     -32.581  -8.347 -22.260  1.00149.09           O  
ANISOU 2385  O   ASP A 633    17968  30575   8106   3882    350   -222       O  
ATOM   2386  CB  ASP A 633     -34.100 -10.617 -23.431  1.00180.24           C  
ANISOU 2386  CB  ASP A 633    21019  34838  12623   3831    228   -782       C  
ATOM   2387  CG  ASP A 633     -35.280 -10.930 -22.528  1.00211.35           C  
ANISOU 2387  CG  ASP A 633    25065  38501  16737   3713    516   -734       C  
ATOM   2388  OD1 ASP A 633     -35.104 -10.969 -21.291  1.00216.42           O  
ANISOU 2388  OD1 ASP A 633    26173  38684  17373   3579    631   -547       O  
ATOM   2389  OD2 ASP A 633     -36.390 -11.144 -23.060  1.00226.33           O  
ANISOU 2389  OD2 ASP A 633    26566  40658  18770   3761    631   -898       O  
ATOM   2390  N   SER A 634     -32.545  -9.691 -20.455  1.00149.96           N  
ANISOU 2390  N   SER A 634    18530  29999   8448   3586    385   -199       N  
ATOM   2391  CA  SER A 634     -32.440  -8.594 -19.501  1.00149.33           C  
ANISOU 2391  CA  SER A 634    18897  29702   8138   3574    588     86       C  
ATOM   2392  C   SER A 634     -31.129  -8.612 -18.725  1.00172.64           C  
ANISOU 2392  C   SER A 634    22241  32410  10942   3486    438    142       C  
ATOM   2393  O   SER A 634     -30.979  -7.848 -17.764  1.00150.93           O  
ANISOU 2393  O   SER A 634    19889  29442   8017   3443    601    347       O  
ATOM   2394  CB  SER A 634     -33.620  -8.623 -18.526  1.00157.12           C  
ANISOU 2394  CB  SER A 634    20065  30405   9227   3502    896    230       C  
ATOM   2395  OG  SER A 634     -33.570  -9.775 -17.704  1.00188.25           O  
ANISOU 2395  OG  SER A 634    24175  33992  13358   3359    869    175       O  
ATOM   2396  N   ARG A 635     -30.178  -9.463 -19.111  1.00176.47           N  
ANISOU 2396  N   ARG A 635    22617  32949  11486   3464    133    -48       N  
ATOM   2397  CA  ARG A 635     -28.910  -9.531 -18.395  1.00147.34           C  
ANISOU 2397  CA  ARG A 635    19268  29079   7636   3404    -28    -23       C  
ATOM   2398  C   ARG A 635     -27.988  -8.373 -18.752  1.00145.97           C  
ANISOU 2398  C   ARG A 635    19140  28845   7476   3368    -84     11       C  
ATOM   2399  O   ARG A 635     -27.216  -7.920 -17.899  1.00145.62           O  
ANISOU 2399  O   ARG A 635    19437  28504   7390   3261    -77     89       O  
ATOM   2400  CB  ARG A 635     -28.220 -10.866 -18.682  1.00147.61           C  
ANISOU 2400  CB  ARG A 635    19161  29102   7822   3382   -322   -237       C  
ATOM   2401  CG  ARG A 635     -29.038 -12.082 -18.273  1.00149.27           C  
ANISOU 2401  CG  ARG A 635    19338  29059   8320   3320   -226   -287       C  
ATOM   2402  CD  ARG A 635     -28.437 -13.367 -18.818  1.00149.67           C  
ANISOU 2402  CD  ARG A 635    19177  29145   8544   3314   -488   -522       C  
ATOM   2403  NE  ARG A 635     -29.274 -14.528 -18.530  1.00151.54           N  
ANISOU 2403  NE  ARG A 635    19357  29133   9089   3244   -344   -597       N  
ATOM   2404  CZ  ARG A 635     -29.113 -15.723 -19.090  1.00166.86           C  
ANISOU 2404  CZ  ARG A 635    21053  31086  11262   3222   -481   -825       C  
ATOM   2405  NH1 ARG A 635     -28.146 -15.918 -19.975  1.00151.36           N  
ANISOU 2405  NH1 ARG A 635    18873  29388   9248   3274   -794   -991       N  
ATOM   2406  NH2 ARG A 635     -29.923 -16.723 -18.769  1.00168.86           N  
ANISOU 2406  NH2 ARG A 635    21278  31074  11805   3140   -285   -896       N  
ATOM   2407  N   ASN A 636     -28.053  -7.888 -19.994  1.00145.39           N  
ANISOU 2407  N   ASN A 636    18722  29005   7514   3444   -120    -62       N  
ATOM   2408  CA  ASN A 636     -27.222  -6.779 -20.470  1.00144.31           C  
ANISOU 2408  CA  ASN A 636    18603  28772   7454   3410   -126    -40       C  
ATOM   2409  C   ASN A 636     -25.733  -7.078 -20.316  1.00143.57           C  
ANISOU 2409  C   ASN A 636    18623  28530   7396   3299   -385   -167       C  
ATOM   2410  O   ASN A 636     -24.917  -6.167 -20.154  1.00142.96           O  
ANISOU 2410  O   ASN A 636    18722  28272   7323   3208   -343   -139       O  
ATOM   2411  CB  ASN A 636     -27.581  -5.469 -19.762  1.00144.36           C  
ANISOU 2411  CB  ASN A 636    18922  28527   7401   3357    195    184       C  
ATOM   2412  CG  ASN A 636     -29.053  -5.129 -19.884  1.00153.64           C  
ANISOU 2412  CG  ASN A 636    19993  29825   8558   3475    464    322       C  
ATOM   2413  OD1 ASN A 636     -29.667  -5.350 -20.928  1.00145.51           O  
ANISOU 2413  OD1 ASN A 636    18578  29125   7582   3627    434    246       O  
ATOM   2414  ND2 ASN A 636     -29.629  -4.594 -18.813  1.00145.65           N  
ANISOU 2414  ND2 ASN A 636    19309  28558   7474   3408    727    514       N  
ATOM   2415  N   GLY A 637     -25.375  -8.348 -20.373  1.00143.80           N  
ANISOU 2415  N   GLY A 637    18546  28642   7448   3308   -638   -321       N  
ATOM   2416  CA  GLY A 637     -23.998  -8.763 -20.201  1.00143.32           C  
ANISOU 2416  CA  GLY A 637    18579  28445   7429   3223   -892   -444       C  
ATOM   2417  C   GLY A 637     -23.942 -10.133 -19.561  1.00144.24           C  
ANISOU 2417  C   GLY A 637    18788  28532   7482   3241  -1043   -506       C  
ATOM   2418  O   GLY A 637     -24.957 -10.713 -19.183  1.00145.27           O  
ANISOU 2418  O   GLY A 637    18944  28735   7518   3304   -924   -452       O  
ATOM   2419  N   VAL A 638     -22.721 -10.644 -19.454  1.00156.84           N  
ANISOU 2419  N   VAL A 638    20440  30026   9126   3195  -1286   -623       N  
ATOM   2420  CA  VAL A 638     -22.488 -11.931 -18.809  1.00153.87           C  
ANISOU 2420  CA  VAL A 638    20194  29591   8677   3240  -1429   -670       C  
ATOM   2421  C   VAL A 638     -22.563 -11.746 -17.300  1.00155.93           C  
ANISOU 2421  C   VAL A 638    20905  29594   8749   3216  -1269   -496       C  
ATOM   2422  O   VAL A 638     -21.871 -10.894 -16.731  1.00165.93           O  
ANISOU 2422  O   VAL A 638    22385  30675   9987   3118  -1233   -448       O  
ATOM   2423  CB  VAL A 638     -21.132 -12.517 -19.230  1.00154.16           C  
ANISOU 2423  CB  VAL A 638    20131  29603   8840   3219  -1735   -845       C  
ATOM   2424  CG1 VAL A 638     -20.832 -13.780 -18.436  1.00146.01           C  
ANISOU 2424  CG1 VAL A 638    19295  28478   7702   3296  -1854   -863       C  
ATOM   2425  CG2 VAL A 638     -21.117 -12.805 -20.723  1.00143.84           C  
ANISOU 2425  CG2 VAL A 638    18374  28544   7734   3250  -1886  -1016       C  
ATOM   2426  N   ILE A 639     -23.410 -12.541 -16.649  1.00172.56           N  
ANISOU 2426  N   ILE A 639    23153  31697  10715   3308  -1153   -413       N  
ATOM   2427  CA  ILE A 639     -23.510 -12.500 -15.194  1.00178.72           C  
ANISOU 2427  CA  ILE A 639    24370  32222  11313   3319   -992   -235       C  
ATOM   2428  C   ILE A 639     -22.209 -13.026 -14.602  1.00169.01           C  
ANISOU 2428  C   ILE A 639    23328  30841  10046   3336  -1214   -297       C  
ATOM   2429  O   ILE A 639     -21.789 -14.152 -14.891  1.00169.07           O  
ANISOU 2429  O   ILE A 639    23247  30922  10069   3435  -1409   -411       O  
ATOM   2430  CB  ILE A 639     -24.717 -13.307 -14.702  1.00175.46           C  
ANISOU 2430  CB  ILE A 639    24048  31687  10932   3381   -772   -129       C  
ATOM   2431  CG1 ILE A 639     -26.015 -12.718 -15.259  1.00154.35           C  
ANISOU 2431  CG1 ILE A 639    21150  29069   8428   3318   -532    -79       C  
ATOM   2432  CG2 ILE A 639     -24.753 -13.335 -13.183  1.00186.07           C  
ANISOU 2432  CG2 ILE A 639    25858  32711  12129   3405   -604     69       C  
ATOM   2433  CD1 ILE A 639     -26.255 -11.278 -14.859  1.00148.84           C  
ANISOU 2433  CD1 ILE A 639    20629  28406   7516   3286   -336     87       C  
ATOM   2434  N   THR A 640     -21.563 -12.209 -13.771  1.00168.97           N  
ANISOU 2434  N   THR A 640    23571  30644   9986   3243  -1176   -236       N  
ATOM   2435  CA  THR A 640     -20.250 -12.537 -13.233  1.00177.94           C  
ANISOU 2435  CA  THR A 640    24844  31677  11089   3248  -1384   -320       C  
ATOM   2436  C   THR A 640     -20.262 -12.941 -11.768  1.00173.13           C  
ANISOU 2436  C   THR A 640    24633  30879  10272   3347  -1290   -175       C  
ATOM   2437  O   THR A 640     -19.415 -13.739 -11.360  1.00174.72           O  
ANISOU 2437  O   THR A 640    24929  31040  10414   3452  -1465   -226       O  
ATOM   2438  CB  THR A 640     -19.290 -11.353 -13.410  1.00173.13           C  
ANISOU 2438  CB  THR A 640    24184  31039  10559   3070  -1436   -421       C  
ATOM   2439  OG1 THR A 640     -19.865 -10.176 -12.829  1.00156.94           O  
ANISOU 2439  OG1 THR A 640    22313  28886   8432   2966  -1168   -293       O  
ATOM   2440  CG2 THR A 640     -19.022 -11.105 -14.887  1.00169.51           C  
ANISOU 2440  CG2 THR A 640    23345  30752  10310   3013  -1558   -571       C  
ATOM   2441  N   GLN A 641     -21.190 -12.420 -10.968  1.00162.95           N  
ANISOU 2441  N   GLN A 641    23576  29465   8871   3333  -1011     13       N  
ATOM   2442  CA  GLN A 641     -21.246 -12.785  -9.560  1.00165.27           C  
ANISOU 2442  CA  GLN A 641    24258  29566   8973   3443   -899    167       C  
ATOM   2443  C   GLN A 641     -22.615 -12.436  -8.995  1.00154.09           C  
ANISOU 2443  C   GLN A 641    23032  28033   7481   3450   -557    387       C  
ATOM   2444  O   GLN A 641     -23.386 -11.683  -9.595  1.00166.88           O  
ANISOU 2444  O   GLN A 641    24492  29721   9194   3340   -410    412       O  
ATOM   2445  CB  GLN A 641     -20.144 -12.092  -8.750  1.00189.52           C  
ANISOU 2445  CB  GLN A 641    27476  32549  11984   3344   -981    107       C  
ATOM   2446  CG  GLN A 641     -20.235 -10.577  -8.738  1.00196.71           C  
ANISOU 2446  CG  GLN A 641    28372  33433  12936   3117   -834     96       C  
ATOM   2447  CD  GLN A 641     -19.298  -9.945  -7.727  1.00216.45           C  
ANISOU 2447  CD  GLN A 641    31058  35858  15324   3028   -859     33       C  
ATOM   2448  OE1 GLN A 641     -19.610  -9.867  -6.537  1.00184.84           O  
ANISOU 2448  OE1 GLN A 641    27340  31719  11170   3067   -709    168       O  
ATOM   2449  NE2 GLN A 641     -18.141  -9.491  -8.194  1.00229.38           N  
ANISOU 2449  NE2 GLN A 641    32527  37595  17032   2911  -1041   -183       N  
ATOM   2450  N   TYR A 642     -22.901 -13.004  -7.827  1.00162.92           N  
ANISOU 2450  N   TYR A 642    24503  28965   8436   3599   -416    557       N  
ATOM   2451  CA  TYR A 642     -24.111 -12.726  -7.072  1.00173.01           C  
ANISOU 2451  CA  TYR A 642    26026  30069   9641   3614    -71    787       C  
ATOM   2452  C   TYR A 642     -23.739 -12.196  -5.693  1.00168.74           C  
ANISOU 2452  C   TYR A 642    25815  29318   8982   3584      8    890       C  
ATOM   2453  O   TYR A 642     -22.613 -12.372  -5.220  1.00161.33           O  
ANISOU 2453  O   TYR A 642    24942  28383   7974   3620   -194    797       O  
ATOM   2454  CB  TYR A 642     -24.986 -13.982  -6.930  1.00177.54           C  
ANISOU 2454  CB  TYR A 642    26678  30390  10387   3731    101    897       C  
ATOM   2455  CG  TYR A 642     -25.624 -14.449  -8.220  1.00194.54           C  
ANISOU 2455  CG  TYR A 642    28425  32579  12911   3629     92    769       C  
ATOM   2456  CD1 TYR A 642     -26.096 -13.538  -9.154  1.00189.97           C  
ANISOU 2456  CD1 TYR A 642    27540  32218  12420   3484    112    699       C  
ATOM   2457  CD2 TYR A 642     -25.754 -15.803  -8.503  1.00198.20           C  
ANISOU 2457  CD2 TYR A 642    28810  32868  13629   3692     82    709       C  
ATOM   2458  CE1 TYR A 642     -26.683 -13.960 -10.332  1.00170.88           C  
ANISOU 2458  CE1 TYR A 642    24728  29884  10314   3417     96    563       C  
ATOM   2459  CE2 TYR A 642     -26.337 -16.235  -9.682  1.00187.54           C  
ANISOU 2459  CE2 TYR A 642    27061  31580  12616   3589     77    552       C  
ATOM   2460  CZ  TYR A 642     -26.799 -15.308 -10.592  1.00180.60           C  
ANISOU 2460  CZ  TYR A 642    25861  30960  11798   3457     70    475       C  
ATOM   2461  OH  TYR A 642     -27.381 -15.730 -11.766  1.00196.38           O  
ANISOU 2461  OH  TYR A 642    27439  33072  14104   3380     56    302       O  
ATOM   2462  N   SER A 643     -24.701 -11.536  -5.053  1.00164.56           N  
ANISOU 2462  N   SER A 643    25468  28624   8433   3515    307   1072       N  
ATOM   2463  CA  SER A 643     -24.529 -11.036  -3.698  1.00180.16           C  
ANISOU 2463  CA  SER A 643    27753  30405  10296   3484    417   1178       C  
ATOM   2464  C   SER A 643     -25.838 -11.191  -2.944  1.00177.96           C  
ANISOU 2464  C   SER A 643    27752  29883   9983   3560    773   1445       C  
ATOM   2465  O   SER A 643     -26.916 -10.959  -3.500  1.00162.66           O  
ANISOU 2465  O   SER A 643    25715  27947   8141   3506    975   1523       O  
ATOM   2466  CB  SER A 643     -24.086  -9.566  -3.680  1.00176.33           C  
ANISOU 2466  CB  SER A 643    27176  29967   9855   3219    404   1067       C  
ATOM   2467  OG  SER A 643     -25.116  -8.714  -4.151  1.00156.44           O  
ANISOU 2467  OG  SER A 643    24570  27423   7446   3081    637   1151       O  
ATOM   2468  N   VAL A 644     -25.738 -11.590  -1.679  1.00176.94           N  
ANISOU 2468  N   VAL A 644    27962  29547   9722   3693    859   1583       N  
ATOM   2469  CA  VAL A 644     -26.894 -11.791  -0.816  1.00165.61           C  
ANISOU 2469  CA  VAL A 644    26841  27821   8262   3775   1213   1849       C  
ATOM   2470  C   VAL A 644     -26.770 -10.859   0.378  1.00163.96           C  
ANISOU 2470  C   VAL A 644    26820  27482   7996   3654   1297   1913       C  
ATOM   2471  O   VAL A 644     -25.740 -10.850   1.062  1.00165.06           O  
ANISOU 2471  O   VAL A 644    27027  27675   8013   3697   1115   1827       O  
ATOM   2472  CB  VAL A 644     -27.014 -13.255  -0.356  1.00165.72           C  
ANISOU 2472  CB  VAL A 644    27130  27646   8190   4080   1301   1987       C  
ATOM   2473  CG1 VAL A 644     -28.198 -13.420   0.584  1.00167.20           C  
ANISOU 2473  CG1 VAL A 644    27610  27415   8505   4083   1690   2243       C  
ATOM   2474  CG2 VAL A 644     -27.148 -14.179  -1.556  1.00165.28           C  
ANISOU 2474  CG2 VAL A 644    26747  27572   8481   4040   1204   1849       C  
ATOM   2475  N   ALA A 645     -27.816 -10.074   0.621  1.00163.36           N  
ANISOU 2475  N   ALA A 645    26805  27259   8003   3507   1575   2050       N  
ATOM   2476  CA  ALA A 645     -27.904  -9.203   1.781  1.00165.02           C  
ANISOU 2476  CA  ALA A 645    27203  27328   8169   3389   1705   2129       C  
ATOM   2477  C   ALA A 645     -29.071  -9.646   2.651  1.00189.02           C  
ANISOU 2477  C   ALA A 645    30556  30033  11229   3498   2043   2409       C  
ATOM   2478  O   ALA A 645     -30.092 -10.128   2.149  1.00186.81           O  
ANISOU 2478  O   ALA A 645    30287  29641  11052   3549   2254   2528       O  
ATOM   2479  CB  ALA A 645     -28.082  -7.737   1.368  1.00178.74           C  
ANISOU 2479  CB  ALA A 645    28753  29156  10005   3094   1759   2042       C  
ATOM   2480  N   TYR A 646     -28.913  -9.487   3.963  1.00202.65           N  
ANISOU 2480  N   TYR A 646    32529  31610  12858   3535   2107   2500       N  
ATOM   2481  CA  TYR A 646     -29.932  -9.915   4.909  1.00168.81           C  
ANISOU 2481  CA  TYR A 646    28565  26976   8601   3645   2429   2767       C  
ATOM   2482  C   TYR A 646     -30.055  -8.899   6.035  1.00169.26           C  
ANISOU 2482  C   TYR A 646    28733  26946   8632   3501   2527   2818       C  
ATOM   2483  O   TYR A 646     -29.098  -8.195   6.370  1.00169.22           O  
ANISOU 2483  O   TYR A 646    28638  27145   8511   3406   2327   2647       O  
ATOM   2484  CB  TYR A 646     -29.623 -11.307   5.481  1.00171.39           C  
ANISOU 2484  CB  TYR A 646    29160  27149   8810   3977   2435   2877       C  
ATOM   2485  CG  TYR A 646     -28.347 -11.385   6.291  1.00178.61           C  
ANISOU 2485  CG  TYR A 646    30128  28209   9528   4108   2179   2776       C  
ATOM   2486  CD1 TYR A 646     -27.119 -11.591   5.674  1.00172.58           C  
ANISOU 2486  CD1 TYR A 646    29147  27752   8675   4151   1830   2544       C  
ATOM   2487  CD2 TYR A 646     -28.372 -11.265   7.675  1.00186.22           C  
ANISOU 2487  CD2 TYR A 646    31341  29018  10395   4196   2288   2902       C  
ATOM   2488  CE1 TYR A 646     -25.952 -11.668   6.412  1.00174.28           C  
ANISOU 2488  CE1 TYR A 646    29387  28124   8707   4275   1605   2434       C  
ATOM   2489  CE2 TYR A 646     -27.211 -11.339   8.421  1.00184.89           C  
ANISOU 2489  CE2 TYR A 646    31196  29029  10026   4338   2059   2793       C  
ATOM   2490  CZ  TYR A 646     -26.005 -11.541   7.784  1.00182.52           C  
ANISOU 2490  CZ  TYR A 646    30673  29041   9637   4376   1723   2557       C  
ATOM   2491  OH  TYR A 646     -24.850 -11.616   8.527  1.00182.21           O  
ANISOU 2491  OH  TYR A 646    30636  29200   9396   4520   1504   2434       O  
ATOM   2492  N   GLU A 647     -31.252  -8.837   6.616  1.00186.90           N  
ANISOU 2492  N   GLU A 647    31161  28878  10976   3480   2853   3040       N  
ATOM   2493  CA  GLU A 647     -31.548  -7.917   7.708  1.00204.20           C  
ANISOU 2493  CA  GLU A 647    33466  30957  13164   3350   2981   3112       C  
ATOM   2494  C   GLU A 647     -32.749  -8.451   8.473  1.00207.04           C  
ANISOU 2494  C   GLU A 647    34114  30922  13628   3451   3325   3387       C  
ATOM   2495  O   GLU A 647     -33.785  -8.748   7.869  1.00204.71           O  
ANISOU 2495  O   GLU A 647    33811  30468  13500   3420   3548   3493       O  
ATOM   2496  CB  GLU A 647     -31.832  -6.506   7.182  1.00195.51           C  
ANISOU 2496  CB  GLU A 647    32129  29984  12173   3035   3010   3012       C  
ATOM   2497  CG  GLU A 647     -32.120  -5.482   8.268  1.00194.84           C  
ANISOU 2497  CG  GLU A 647    32144  29802  12083   2883   3147   3066       C  
ATOM   2498  CD  GLU A 647     -32.645  -4.173   7.711  1.00188.65           C  
ANISOU 2498  CD  GLU A 647    31165  29071  11442   2597   3257   3019       C  
ATOM   2499  OE1 GLU A 647     -33.664  -4.197   6.987  1.00180.39           O  
ANISOU 2499  OE1 GLU A 647    30041  27920  10579   2555   3428   3121       O  
ATOM   2500  OE2 GLU A 647     -32.035  -3.120   7.989  1.00190.26           O  
ANISOU 2500  OE2 GLU A 647    31293  29429  11568   2423   3190   2873       O  
ATOM   2501  N   ALA A 648     -32.609  -8.573   9.790  1.00181.51           N  
ANISOU 2501  N   ALA A 648    31126  27544  10294   3572   3378   3490       N  
ATOM   2502  CA  ALA A 648     -33.669  -9.078  10.651  1.00183.25           C  
ANISOU 2502  CA  ALA A 648    31647  27365  10615   3677   3711   3752       C  
ATOM   2503  C   ALA A 648     -34.376  -7.912  11.330  1.00194.87           C  
ANISOU 2503  C   ALA A 648    33113  28743  12183   3452   3864   3809       C  
ATOM   2504  O   ALA A 648     -33.723  -7.008  11.862  1.00203.61           O  
ANISOU 2504  O   ALA A 648    34144  30047  13169   3350   3711   3688       O  
ATOM   2505  CB  ALA A 648     -33.112 -10.042  11.699  1.00211.14           C  
ANISOU 2505  CB  ALA A 648    35472  30774  13979   4002   3697   3852       C  
ATOM   2506  N   VAL A 649     -35.707  -7.937  11.310  1.00191.47           N  
ANISOU 2506  N   VAL A 649    32760  28019  11970   3372   4180   3981       N  
ATOM   2507  CA  VAL A 649     -36.479  -6.855  11.912  1.00206.23           C  
ANISOU 2507  CA  VAL A 649    34615  29783  13958   3164   4336   4045       C  
ATOM   2508  C   VAL A 649     -36.693  -7.109  13.398  1.00229.66           C  
ANISOU 2508  C   VAL A 649    37887  32492  16882   3306   4477   4210       C  
ATOM   2509  O   VAL A 649     -36.655  -6.180  14.213  1.00242.90           O  
ANISOU 2509  O   VAL A 649    39562  34210  18520   3195   4463   4193       O  
ATOM   2510  CB  VAL A 649     -37.813  -6.677  11.161  1.00203.61           C  
ANISOU 2510  CB  VAL A 649    34180  29299  13884   3005   4593   4128       C  
ATOM   2511  CG1 VAL A 649     -38.679  -5.628  11.843  1.00198.90           C  
ANISOU 2511  CG1 VAL A 649    33583  28564  13425   2816   4767   4212       C  
ATOM   2512  CG2 VAL A 649     -37.555  -6.306   9.710  1.00179.37           C  
ANISOU 2512  CG2 VAL A 649    30786  26532  10835   2884   4440   3956       C  
ATOM   2513  N   ASP A 650     -36.917  -8.365  13.776  1.00231.37           N  
ANISOU 2513  N   ASP A 650    38375  32435  17101   3560   4634   4369       N  
ATOM   2514  CA  ASP A 650     -37.190  -8.723  15.163  1.00223.44           C  
ANISOU 2514  CA  ASP A 650    37681  31147  16068   3732   4804   4548       C  
ATOM   2515  C   ASP A 650     -35.953  -9.186  15.920  1.00240.91           C  
ANISOU 2515  C   ASP A 650    40026  33513  17997   4012   4586   4505       C  
ATOM   2516  O   ASP A 650     -35.771  -8.816  17.085  1.00185.38           O  
ANISOU 2516  O   ASP A 650    33109  26475  10852   4078   4578   4541       O  
ATOM   2517  CB  ASP A 650     -38.265  -9.814  15.221  1.00207.14           C  
ANISOU 2517  CB  ASP A 650    35871  28635  14196   3850   5180   4765       C  
ATOM   2518  CG  ASP A 650     -37.962 -10.985  14.304  1.00214.41           C  
ANISOU 2518  CG  ASP A 650    36828  29542  15095   4012   5190   4750       C  
ATOM   2519  OD1 ASP A 650     -36.835 -11.055  13.763  1.00230.69           O  
ANISOU 2519  OD1 ASP A 650    38743  31937  16972   4085   4872   4587       O  
ATOM   2520  OD2 ASP A 650     -38.855 -11.838  14.122  1.00210.01           O  
ANISOU 2520  OD2 ASP A 650    36442  28640  14711   4056   5535   4889       O  
ATOM   2521  N   GLY A 651     -35.092  -9.977  15.288  1.00235.71           N  
ANISOU 2521  N   GLY A 651    39337  33012  17210   4188   4406   4420       N  
ATOM   2522  CA  GLY A 651     -33.888 -10.444  15.944  1.00244.14           C  
ANISOU 2522  CA  GLY A 651    40501  34259  18003   4475   4186   4366       C  
ATOM   2523  C   GLY A 651     -32.901  -9.323  16.211  1.00238.53           C  
ANISOU 2523  C   GLY A 651    39561  33973  17096   4336   3877   4131       C  
ATOM   2524  O   GLY A 651     -33.074  -8.176  15.798  1.00262.91           O  
ANISOU 2524  O   GLY A 651    42417  37215  20261   4012   3829   4003       O  
ATOM   2525  N   GLU A 652     -31.833  -9.676  16.918  1.00241.65           N  
ANISOU 2525  N   GLU A 652    40027  34562  17228   4596   3685   4066       N  
ATOM   2526  CA  GLU A 652     -30.810  -8.709  17.302  1.00216.58           C  
ANISOU 2526  CA  GLU A 652    36658  31801  13832   4488   3415   3820       C  
ATOM   2527  C   GLU A 652     -29.893  -8.363  16.131  1.00221.81           C  
ANISOU 2527  C   GLU A 652    37000  32831  14448   4319   3122   3541       C  
ATOM   2528  O   GLU A 652     -30.306  -8.400  14.972  1.00223.40           O  
ANISOU 2528  O   GLU A 652    37071  32979  14833   4162   3149   3531       O  
ATOM   2529  CB  GLU A 652     -29.987  -9.247  18.474  1.00219.09           C  
ANISOU 2529  CB  GLU A 652    37148  32226  13872   4849   3318   3834       C  
ATOM   2530  CG  GLU A 652     -29.071  -8.222  19.118  1.00218.05           C  
ANISOU 2530  CG  GLU A 652    36852  32498  13500   4739   3105   3586       C  
ATOM   2531  CD  GLU A 652     -28.324  -8.786  20.311  1.00231.22           C  
ANISOU 2531  CD  GLU A 652    38683  34288  14881   5129   3023   3606       C  
ATOM   2532  OE1 GLU A 652     -28.191 -10.024  20.397  1.00225.49           O  
ANISOU 2532  OE1 GLU A 652    38145  33414  14116   5505   3052   3761       O  
ATOM   2533  OE2 GLU A 652     -27.875  -7.993  21.166  1.00244.39           O  
ANISOU 2533  OE2 GLU A 652    40296  36204  16356   5073   2947   3464       O  
ATOM   2534  N   VAL A 658     -23.469  -9.084   4.837  1.00169.86           N  
ANISOU 2534  N   VAL A 658    28007  28391   8141   3600    950   1642       N  
ATOM   2535  CA  VAL A 658     -23.608  -9.186   3.390  1.00188.38           C  
ANISOU 2535  CA  VAL A 658    30114  30813  10648   3512    873   1564       C  
ATOM   2536  C   VAL A 658     -22.504 -10.063   2.817  1.00179.33           C  
ANISOU 2536  C   VAL A 658    28817  29859   9462   3671    559   1397       C  
ATOM   2537  O   VAL A 658     -21.323  -9.854   3.096  1.00173.08           O  
ANISOU 2537  O   VAL A 658    27937  29259   8567   3653    341   1192       O  
ATOM   2538  CB  VAL A 658     -23.592  -7.798   2.729  1.00185.76           C  
ANISOU 2538  CB  VAL A 658    29571  30590  10417   3173    897   1405       C  
ATOM   2539  CG1 VAL A 658     -23.873  -7.916   1.237  1.00163.08           C  
ANISOU 2539  CG1 VAL A 658    26452  27793   7718   3116    845   1355       C  
ATOM   2540  CG2 VAL A 658     -24.600  -6.884   3.401  1.00199.56           C  
ANISOU 2540  CG2 VAL A 658    31475  32153  12195   3020   1207   1564       C  
ATOM   2541  N   VAL A 659     -22.895 -11.048   2.015  1.00167.52           N  
ANISOU 2541  N   VAL A 659    27285  28317   8048   3823    548   1473       N  
ATOM   2542  CA  VAL A 659     -21.962 -11.963   1.369  1.00167.82           C  
ANISOU 2542  CA  VAL A 659    27174  28517   8072   3981    267   1331       C  
ATOM   2543  C   VAL A 659     -21.966 -11.650  -0.121  1.00180.18           C  
ANISOU 2543  C   VAL A 659    28407  30239   9813   3795    151   1172       C  
ATOM   2544  O   VAL A 659     -22.965 -11.884  -0.813  1.00172.03           O  
ANISOU 2544  O   VAL A 659    27338  29138   8888   3797    302   1278       O  
ATOM   2545  CB  VAL A 659     -22.327 -13.430   1.628  1.00169.78           C  
ANISOU 2545  CB  VAL A 659    27661  28594   8256   4333    354   1531       C  
ATOM   2546  CG1 VAL A 659     -21.403 -14.351   0.846  1.00169.94           C  
ANISOU 2546  CG1 VAL A 659    27509  28786   8276   4484     71   1378       C  
ATOM   2547  CG2 VAL A 659     -22.258 -13.739   3.115  1.00199.39           C  
ANISOU 2547  CG2 VAL A 659    31743  32184  11831   4551    473   1697       C  
ATOM   2548  N   ASP A 660     -20.853 -11.122  -0.615  1.00167.61           N  
ANISOU 2548  N   ASP A 660    26568  28864   8251   3645   -100    911       N  
ATOM   2549  CA  ASP A 660     -20.663 -10.837  -2.028  1.00166.73           C  
ANISOU 2549  CA  ASP A 660    26131  28907   8310   3489   -236    742       C  
ATOM   2550  C   ASP A 660     -19.653 -11.817  -2.618  1.00186.91           C  
ANISOU 2550  C   ASP A 660    28524  31611  10882   3636   -540    589       C  
ATOM   2551  O   ASP A 660     -19.164 -12.727  -1.942  1.00211.19           O  
ANISOU 2551  O   ASP A 660    31749  34664  13829   3873   -625    631       O  
ATOM   2552  CB  ASP A 660     -20.223  -9.384  -2.230  1.00185.04           C  
ANISOU 2552  CB  ASP A 660    28312  31313  10680   3190   -235    568       C  
ATOM   2553  CG  ASP A 660     -19.064  -8.991  -1.331  1.00207.36           C  
ANISOU 2553  CG  ASP A 660    31202  34221  13364   3150   -356    409       C  
ATOM   2554  OD1 ASP A 660     -18.430  -9.887  -0.735  1.00222.01           O  
ANISOU 2554  OD1 ASP A 660    33138  36113  15103   3364   -505    403       O  
ATOM   2555  OD2 ASP A 660     -18.792  -7.777  -1.213  1.00213.21           O  
ANISOU 2555  OD2 ASP A 660    31913  34997  14098   2918   -284    284       O  
ATOM   2556  N   GLY A 661     -19.344 -11.623  -3.897  1.00188.60           N  
ANISOU 2556  N   GLY A 661    28427  31973  11260   3507   -692    419       N  
ATOM   2557  CA  GLY A 661     -18.390 -12.483  -4.567  1.00184.17           C  
ANISOU 2557  CA  GLY A 661    27677  31550  10750   3614   -981    262       C  
ATOM   2558  C   GLY A 661     -18.863 -13.896  -4.817  1.00178.08           C  
ANISOU 2558  C   GLY A 661    26967  30736   9959   3882   -986    381       C  
ATOM   2559  O   GLY A 661     -18.040 -14.772  -5.093  1.00170.68           O  
ANISOU 2559  O   GLY A 661    25949  29880   9020   4027  -1206    283       O  
ATOM   2560  N   ILE A 662     -20.168 -14.148  -4.721  1.00180.01           N  
ANISOU 2560  N   ILE A 662    27363  30851  10183   3956   -725    586       N  
ATOM   2561  CA  ILE A 662     -20.709 -15.470  -5.020  1.00163.04           C  
ANISOU 2561  CA  ILE A 662    25290  28658   8001   4207   -673    684       C  
ATOM   2562  C   ILE A 662     -20.545 -15.736  -6.510  1.00180.64           C  
ANISOU 2562  C   ILE A 662    27136  31101  10397   4136   -869    492       C  
ATOM   2563  O   ILE A 662     -21.012 -14.956  -7.347  1.00191.86           O  
ANISOU 2563  O   ILE A 662    28307  32630  11961   3931   -838    423       O  
ATOM   2564  CB  ILE A 662     -22.180 -15.567  -4.595  1.00166.12           C  
ANISOU 2564  CB  ILE A 662    25924  28857   8337   4274   -301    930       C  
ATOM   2565  CG1 ILE A 662     -22.314 -15.328  -3.089  1.00183.80           C  
ANISOU 2565  CG1 ILE A 662    28545  30861  10431   4347   -108   1126       C  
ATOM   2566  CG2 ILE A 662     -22.765 -16.917  -4.990  1.00164.77           C  
ANISOU 2566  CG2 ILE A 662    25761  28501   8344   4417   -193    985       C  
ATOM   2567  CD1 ILE A 662     -23.745 -15.230  -2.611  1.00175.79           C  
ANISOU 2567  CD1 ILE A 662    27775  29615   9401   4364    284   1372       C  
ATOM   2568  N   SER A 663     -19.881 -16.841  -6.848  1.00178.56           N  
ANISOU 2568  N   SER A 663    26824  30902  10117   4321  -1062    408       N  
ATOM   2569  CA  SER A 663     -19.554 -17.123  -8.238  1.00208.06           C  
ANISOU 2569  CA  SER A 663    30178  34850  14026   4249  -1287    198       C  
ATOM   2570  C   SER A 663     -20.821 -17.293  -9.074  1.00181.75           C  
ANISOU 2570  C   SER A 663    26686  31577  10793   4212  -1117    218       C  
ATOM   2571  O   SER A 663     -21.900 -17.611  -8.567  1.00168.17           O  
ANISOU 2571  O   SER A 663    25122  29507   9268   4189   -802    391       O  
ATOM   2572  CB  SER A 663     -18.682 -18.374  -8.343  1.00230.21           C  
ANISOU 2572  CB  SER A 663    33000  37683  16785   4479  -1493    126       C  
ATOM   2573  OG  SER A 663     -19.421 -19.540  -8.030  1.00240.00           O  
ANISOU 2573  OG  SER A 663    34487  38752  17952   4727  -1287    280       O  
ATOM   2574  N   ARG A 664     -20.670 -17.080 -10.384  1.00178.38           N  
ANISOU 2574  N   ARG A 664    25854  31400  10522   4080  -1298     19       N  
ATOM   2575  CA  ARG A 664     -21.816 -17.065 -11.286  1.00190.78           C  
ANISOU 2575  CA  ARG A 664    27128  32906  12456   3910  -1139     -9       C  
ATOM   2576  C   ARG A 664     -22.427 -18.446 -11.488  1.00174.35           C  
ANISOU 2576  C   ARG A 664    24991  30532  10723   3942  -1012    -17       C  
ATOM   2577  O   ARG A 664     -23.556 -18.542 -11.980  1.00157.85           O  
ANISOU 2577  O   ARG A 664    22698  28327   8949   3805   -808    -31       O  
ATOM   2578  CB  ARG A 664     -21.405 -16.483 -12.638  1.00206.41           C  
ANISOU 2578  CB  ARG A 664    28691  35271  14463   3804  -1377   -224       C  
ATOM   2579  CG  ARG A 664     -20.490 -17.391 -13.444  1.00231.47           C  
ANISOU 2579  CG  ARG A 664    31648  38610  17690   3886  -1686   -427       C  
ATOM   2580  CD  ARG A 664     -19.761 -16.625 -14.535  1.00247.18           C  
ANISOU 2580  CD  ARG A 664    33274  40737  19905   3698  -1899   -604       C  
ATOM   2581  NE  ARG A 664     -18.802 -15.675 -13.979  1.00258.86           N  
ANISOU 2581  NE  ARG A 664    34885  42073  21396   3576  -1947   -589       N  
ATOM   2582  CZ  ARG A 664     -18.055 -14.851 -14.706  1.00261.03           C  
ANISOU 2582  CZ  ARG A 664    34936  42396  21849   3410  -2067   -719       C  
ATOM   2583  NH1 ARG A 664     -18.154 -14.853 -16.029  1.00255.48           N  
ANISOU 2583  NH1 ARG A 664    33869  41861  21341   3360  -2162   -848       N  
ATOM   2584  NH2 ARG A 664     -17.209 -14.021 -14.110  1.00262.33           N  
ANISOU 2584  NH2 ARG A 664    35241  42450  21983   3302  -2077   -729       N  
ATOM   2585  N   GLU A 665     -21.713 -19.511 -11.127  1.00198.13           N  
ANISOU 2585  N   GLU A 665    28170  33429  13682   4125  -1109    -20       N  
ATOM   2586  CA  GLU A 665     -22.221 -20.862 -11.319  1.00180.92           C  
ANISOU 2586  CA  GLU A 665    25957  30942  11842   4155   -953    -41       C  
ATOM   2587  C   GLU A 665     -23.150 -21.314 -10.201  1.00181.30           C  
ANISOU 2587  C   GLU A 665    26365  30523  11997   4197   -551    188       C  
ATOM   2588  O   GLU A 665     -23.779 -22.369 -10.332  1.00165.53           O  
ANISOU 2588  O   GLU A 665    24344  28217  10332   4180   -331    168       O  
ATOM   2589  CB  GLU A 665     -21.054 -21.843 -11.450  1.00177.78           C  
ANISOU 2589  CB  GLU A 665    25597  30602  11350   4354  -1200   -133       C  
ATOM   2590  CG  GLU A 665     -20.253 -21.677 -12.732  1.00211.39           C  
ANISOU 2590  CG  GLU A 665    29445  35271  15602   4295  -1572   -391       C  
ATOM   2591  CD  GLU A 665     -18.966 -22.475 -12.724  1.00231.12           C  
ANISOU 2591  CD  GLU A 665    32019  37872  17923   4514  -1843   -467       C  
ATOM   2592  OE1 GLU A 665     -18.540 -22.901 -11.630  1.00223.15           O  
ANISOU 2592  OE1 GLU A 665    31402  36694  16690   4742  -1781   -305       O  
ATOM   2593  OE2 GLU A 665     -18.380 -22.676 -13.809  1.00239.76           O  
ANISOU 2593  OE2 GLU A 665    32781  39228  19089   4477  -2114   -684       O  
ATOM   2594  N   HIS A 666     -23.256 -20.549  -9.117  1.00190.42           N  
ANISOU 2594  N   HIS A 666    27848  31614  12891   4245   -431    391       N  
ATOM   2595  CA  HIS A 666     -24.113 -20.926  -8.003  1.00188.75           C  
ANISOU 2595  CA  HIS A 666    28002  30961  12755   4298    -45    624       C  
ATOM   2596  C   HIS A 666     -25.575 -20.661  -8.341  1.00183.74           C  
ANISOU 2596  C   HIS A 666    27181  30162  12471   4056    255    624       C  
ATOM   2597  O   HIS A 666     -25.928 -19.575  -8.813  1.00172.03           O  
ANISOU 2597  O   HIS A 666    25477  28923  10964   3893    205    577       O  
ATOM   2598  CB  HIS A 666     -23.724 -20.159  -6.739  1.00194.29           C  
ANISOU 2598  CB  HIS A 666    29097  31683  13041   4434    -29    826       C  
ATOM   2599  CG  HIS A 666     -22.512 -20.700  -6.045  1.00187.35           C  
ANISOU 2599  CG  HIS A 666    28500  30860  11823   4739   -207    874       C  
ATOM   2600  ND1 HIS A 666     -21.231 -20.310  -6.369  1.00179.21           N  
ANISOU 2600  ND1 HIS A 666    27351  30257  10483   4819   -599    718       N  
ATOM   2601  CD2 HIS A 666     -22.389 -21.597  -5.038  1.00187.90           C  
ANISOU 2601  CD2 HIS A 666    28966  30629  11798   5007    -35   1059       C  
ATOM   2602  CE1 HIS A 666     -20.370 -20.945  -5.593  1.00181.43           C  
ANISOU 2602  CE1 HIS A 666    27924  30527  10484   5126   -679    793       C  
ATOM   2603  NE2 HIS A 666     -21.047 -21.733  -4.778  1.00189.86           N  
ANISOU 2603  NE2 HIS A 666    29317  31155  11667   5261   -339   1013       N  
ATOM   2604  N   SER A 667     -26.423 -21.660  -8.099  1.00184.33           N  
ANISOU 2604  N   SER A 667    27346  29824  12866   4040    587    670       N  
ATOM   2605  CA  SER A 667     -27.866 -21.489  -8.164  1.00177.30           C  
ANISOU 2605  CA  SER A 667    26343  28734  12288   3832    927    683       C  
ATOM   2606  C   SER A 667     -28.518 -21.509  -6.791  1.00178.29           C  
ANISOU 2606  C   SER A 667    26927  28451  12365   3898   1294    959       C  
ATOM   2607  O   SER A 667     -29.718 -21.230  -6.687  1.00170.51           O  
ANISOU 2607  O   SER A 667    25890  27302  11592   3731   1586    996       O  
ATOM   2608  CB  SER A 667     -28.496 -22.580  -9.045  1.00169.61           C  
ANISOU 2608  CB  SER A 667    25053  27612  11777   3706   1072    463       C  
ATOM   2609  OG  SER A 667     -28.278 -23.869  -8.499  1.00172.49           O  
ANISOU 2609  OG  SER A 667    25703  27584  12250   3855   1257    524       O  
ATOM   2610  N   SER A 668     -27.761 -21.829  -5.743  1.00171.82           N  
ANISOU 2610  N   SER A 668    26543  27482  11257   4152   1287   1149       N  
ATOM   2611  CA  SER A 668     -28.263 -21.822  -4.378  1.00174.99           C  
ANISOU 2611  CA  SER A 668    27410  27521  11556   4258   1616   1429       C  
ATOM   2612  C   SER A 668     -27.100 -21.557  -3.433  1.00185.38           C  
ANISOU 2612  C   SER A 668    29089  28970  12377   4544   1417   1587       C  
ATOM   2613  O   SER A 668     -25.935 -21.780  -3.772  1.00181.65           O  
ANISOU 2613  O   SER A 668    28551  28764  11704   4692   1086   1481       O  
ATOM   2614  CB  SER A 668     -28.957 -23.143  -4.021  1.00177.01           C  
ANISOU 2614  CB  SER A 668    27855  27250  12151   4300   2026   1491       C  
ATOM   2615  OG  SER A 668     -28.030 -24.214  -3.965  1.00178.85           O  
ANISOU 2615  OG  SER A 668    28241  27393  12321   4546   1942   1486       O  
ATOM   2616  N   TRP A 669     -27.433 -21.076  -2.237  1.00182.87           N  
ANISOU 2616  N   TRP A 669    29142  28484  11855   4625   1621   1826       N  
ATOM   2617  CA  TRP A 669     -26.439 -20.778  -1.216  1.00175.88           C  
ANISOU 2617  CA  TRP A 669    28606  27741  10478   4904   1468   1970       C  
ATOM   2618  C   TRP A 669     -27.083 -20.982   0.147  1.00185.47           C  
ANISOU 2618  C   TRP A 669    30294  28549  11629   5050   1854   2263       C  
ATOM   2619  O   TRP A 669     -28.250 -20.638   0.346  1.00191.53           O  
ANISOU 2619  O   TRP A 669    31078  29077  12617   4856   2155   2349       O  
ATOM   2620  CB  TRP A 669     -25.904 -19.348  -1.359  1.00173.13           C  
ANISOU 2620  CB  TRP A 669    28106  27858   9819   4795   1171   1879       C  
ATOM   2621  CG  TRP A 669     -24.586 -19.113  -0.687  1.00178.49           C  
ANISOU 2621  CG  TRP A 669    28989  28832   9997   5059    898   1889       C  
ATOM   2622  CD1 TRP A 669     -23.347 -19.316  -1.219  1.00173.28           C  
ANISOU 2622  CD1 TRP A 669    28169  28523   9147   5179    524   1703       C  
ATOM   2623  CD2 TRP A 669     -24.376 -18.618   0.641  1.00219.46           C  
ANISOU 2623  CD2 TRP A 669    34558  34028  14801   5238    974   2069       C  
ATOM   2624  NE1 TRP A 669     -22.378 -18.983  -0.304  1.00198.79           N  
ANISOU 2624  NE1 TRP A 669    31644  31995  11894   5422    363   1742       N  
ATOM   2625  CE2 TRP A 669     -22.984 -18.552   0.846  1.00226.72           C  
ANISOU 2625  CE2 TRP A 669    35505  35329  15308   5460    632   1959       C  
ATOM   2626  CE3 TRP A 669     -25.230 -18.227   1.676  1.00243.33           C  
ANISOU 2626  CE3 TRP A 669    37883  36782  17788   5230   1298   2298       C  
ATOM   2627  CZ2 TRP A 669     -22.426 -18.111   2.045  1.00248.33           C  
ANISOU 2627  CZ2 TRP A 669    38370  38047  17935   5506    583   2002       C  
ATOM   2628  CZ3 TRP A 669     -24.674 -17.790   2.864  1.00257.56           C  
ANISOU 2628  CZ3 TRP A 669    39980  38692  19188   5426   1264   2402       C  
ATOM   2629  CH2 TRP A 669     -23.287 -17.735   3.039  1.00257.85           C  
ANISOU 2629  CH2 TRP A 669    39856  38994  19122   5493    894   2221       C  
ATOM   2630  N   ASP A 670     -26.322 -21.550   1.079  1.00188.16           N  
ANISOU 2630  N   ASP A 670    31013  28824  11654   5412   1849   2418       N  
ATOM   2631  CA  ASP A 670     -26.843 -21.942   2.384  1.00183.85           C  
ANISOU 2631  CA  ASP A 670    30951  27869  11035   5621   2231   2714       C  
ATOM   2632  C   ASP A 670     -26.474 -20.887   3.421  1.00183.58           C  
ANISOU 2632  C   ASP A 670    31153  28072  10528   5738   2135   2839       C  
ATOM   2633  O   ASP A 670     -25.296 -20.719   3.755  1.00186.33           O  
ANISOU 2633  O   ASP A 670    31580  28774  10443   5984   1834   2802       O  
ATOM   2634  CB  ASP A 670     -26.309 -23.315   2.786  1.00205.86           C  
ANISOU 2634  CB  ASP A 670    34036  30406  13774   5994   2345   2829       C  
ATOM   2635  CG  ASP A 670     -26.878 -24.433   1.934  1.00211.16           C  
ANISOU 2635  CG  ASP A 670    34538  30729  14965   5862   2566   2725       C  
ATOM   2636  OD1 ASP A 670     -27.793 -24.162   1.129  1.00200.59           O  
ANISOU 2636  OD1 ASP A 670    32862  29333  14022   5486   2657   2572       O  
ATOM   2637  OD2 ASP A 670     -26.410 -25.583   2.068  1.00215.30           O  
ANISOU 2637  OD2 ASP A 670    35260  31048  15495   6141   2660   2787       O  
ATOM   2638  N   LEU A 671     -27.483 -20.182   3.928  1.00184.98           N  
ANISOU 2638  N   LEU A 671    31429  28069  10787   5558   2395   2967       N  
ATOM   2639  CA  LEU A 671     -27.303 -19.265   5.046  1.00188.59           C  
ANISOU 2639  CA  LEU A 671    32157  28668  10831   5666   2391   3109       C  
ATOM   2640  C   LEU A 671     -27.219 -20.070   6.337  1.00191.93           C  
ANISOU 2640  C   LEU A 671    33091  28793  11040   6068   2641   3386       C  
ATOM   2641  O   LEU A 671     -28.123 -20.854   6.644  1.00191.02           O  
ANISOU 2641  O   LEU A 671    33185  28174  11222   6092   3046   3560       O  
ATOM   2642  CB  LEU A 671     -28.458 -18.267   5.112  1.00183.44           C  
ANISOU 2642  CB  LEU A 671    31436  27903  10359   5340   2605   3159       C  
ATOM   2643  CG  LEU A 671     -28.642 -17.267   3.968  1.00216.71           C  
ANISOU 2643  CG  LEU A 671    35189  32421  14731   4974   2408   2930       C  
ATOM   2644  CD1 LEU A 671     -30.022 -16.637   4.046  1.00205.85           C  
ANISOU 2644  CD1 LEU A 671    33787  30810  13618   4703   2726   3026       C  
ATOM   2645  CD2 LEU A 671     -27.569 -16.194   4.016  1.00223.77           C  
ANISOU 2645  CD2 LEU A 671    36001  33821  15201   4987   2055   2797       C  
ATOM   2646  N   VAL A 672     -26.138 -19.883   7.092  1.00188.37           N  
ANISOU 2646  N   VAL A 672    32776  28631  10163   6347   2401   3393       N  
ATOM   2647  CA  VAL A 672     -25.911 -20.641   8.313  1.00192.25           C  
ANISOU 2647  CA  VAL A 672    33654  28873  10520   6734   2576   3617       C  
ATOM   2648  C   VAL A 672     -25.810 -19.681   9.491  1.00203.83           C  
ANISOU 2648  C   VAL A 672    35114  30412  11919   6667   2511   3632       C  
ATOM   2649  O   VAL A 672     -25.499 -18.497   9.341  1.00203.09           O  
ANISOU 2649  O   VAL A 672    34687  30642  11836   6360   2239   3417       O  
ATOM   2650  CB  VAL A 672     -24.649 -21.524   8.223  1.00201.67           C  
ANISOU 2650  CB  VAL A 672    34835  30253  11537   7084   2316   3540       C  
ATOM   2651  CG1 VAL A 672     -24.794 -22.546   7.106  1.00207.35           C  
ANISOU 2651  CG1 VAL A 672    35562  30848  12375   7141   2412   3523       C  
ATOM   2652  CG2 VAL A 672     -23.416 -20.663   8.007  1.00192.50           C  
ANISOU 2652  CG2 VAL A 672    33227  29625  10288   6931   1783   3216       C  
ATOM   2653  N   GLY A 673     -26.084 -20.214  10.680  1.00196.13           N  
ANISOU 2653  N   GLY A 673    34526  29119  10876   6964   2794   3890       N  
ATOM   2654  CA  GLY A 673     -25.951 -19.444  11.900  1.00203.24           C  
ANISOU 2654  CA  GLY A 673    35452  30092  11679   6967   2748   3912       C  
ATOM   2655  C   GLY A 673     -27.110 -18.532  12.224  1.00214.30           C  
ANISOU 2655  C   GLY A 673    36883  31296  13244   6645   2986   3998       C  
ATOM   2656  O   GLY A 673     -26.929 -17.563  12.967  1.00224.70           O  
ANISOU 2656  O   GLY A 673    38096  32788  14492   6521   2862   3925       O  
ATOM   2657  N   LEU A 674     -28.297 -18.810  11.695  1.00196.49           N  
ANISOU 2657  N   LEU A 674    34764  28690  11205   6503   3340   4141       N  
ATOM   2658  CA  LEU A 674     -29.454 -17.978  11.974  1.00195.09           C  
ANISOU 2658  CA  LEU A 674    34607  28315  11206   6201   3584   4227       C  
ATOM   2659  C   LEU A 674     -30.040 -18.319  13.343  1.00231.12           C  
ANISOU 2659  C   LEU A 674    39566  32476  15772   6418   3934   4505       C  
ATOM   2660  O   LEU A 674     -29.695 -19.324  13.970  1.00201.73           O  
ANISOU 2660  O   LEU A 674    36141  28568  11938   6816   4059   4663       O  
ATOM   2661  CB  LEU A 674     -30.507 -18.145  10.881  1.00193.10           C  
ANISOU 2661  CB  LEU A 674    34319  27866  11183   5965   3844   4252       C  
ATOM   2662  CG  LEU A 674     -30.045 -17.796   9.464  1.00207.83           C  
ANISOU 2662  CG  LEU A 674    35781  30126  13060   5755   3522   3980       C  
ATOM   2663  CD1 LEU A 674     -31.164 -18.018   8.461  1.00209.71           C  
ANISOU 2663  CD1 LEU A 674    35859  30131  13689   5479   3770   3952       C  
ATOM   2664  CD2 LEU A 674     -29.541 -16.362   9.400  1.00187.29           C  
ANISOU 2664  CD2 LEU A 674    32807  27932  10424   5465   3159   3753       C  
ATOM   2665  N   GLU A 675     -30.939 -17.458  13.808  1.00219.38           N  
ANISOU 2665  N   GLU A 675    38079  30855  14420   6162   4100   4566       N  
ATOM   2666  CA  GLU A 675     -31.593 -17.643  15.093  1.00219.35           C  
ANISOU 2666  CA  GLU A 675    38418  30474  14450   6319   4429   4814       C  
ATOM   2667  C   GLU A 675     -32.849 -18.492  14.934  1.00226.25           C  
ANISOU 2667  C   GLU A 675    39600  30789  15576   6321   4964   5049       C  
ATOM   2668  O   GLU A 675     -33.511 -18.469  13.892  1.00229.05           O  
ANISOU 2668  O   GLU A 675    39832  31082  16114   6060   5093   4997       O  
ATOM   2669  CB  GLU A 675     -31.948 -16.293  15.717  1.00210.77           C  
ANISOU 2669  CB  GLU A 675    37181  29510  13393   6037   4357   4758       C  
ATOM   2670  CG  GLU A 675     -30.758 -15.372  15.934  1.00201.46           C  
ANISOU 2670  CG  GLU A 675    35707  28859  11978   5985   3897   4506       C  
ATOM   2671  CD  GLU A 675     -31.165 -14.006  16.453  1.00203.77           C  
ANISOU 2671  CD  GLU A 675    35859  29251  12314   5671   3874   4443       C  
ATOM   2672  OE1 GLU A 675     -32.376 -13.702  16.445  1.00199.49           O  
ANISOU 2672  OE1 GLU A 675    35388  28408  12003   5461   4165   4572       O  
ATOM   2673  OE2 GLU A 675     -30.274 -13.236  16.870  1.00203.81           O  
ANISOU 2673  OE2 GLU A 675    35681  29634  12122   5631   3581   4254       O  
ATOM   2674  N   LYS A 676     -33.168 -19.247  15.982  1.00230.07           N  
ANISOU 2674  N   LYS A 676    40480  30867  16067   6620   5299   5298       N  
ATOM   2675  CA  LYS A 676     -34.331 -20.123  15.953  1.00216.86           C  
ANISOU 2675  CA  LYS A 676    39135  28608  14653   6628   5872   5521       C  
ATOM   2676  C   LYS A 676     -35.622 -19.316  15.908  1.00213.98           C  
ANISOU 2676  C   LYS A 676    38682  28065  14554   6223   6100   5537       C  
ATOM   2677  O   LYS A 676     -35.778 -18.326  16.628  1.00205.08           O  
ANISOU 2677  O   LYS A 676    37458  27054  13407   6098   5970   5520       O  
ATOM   2678  CB  LYS A 676     -34.343 -21.038  17.177  1.00213.87           C  
ANISOU 2678  CB  LYS A 676    39202  27828  14231   7051   6186   5782       C  
ATOM   2679  CG  LYS A 676     -33.280 -22.122  17.177  1.00218.35           C  
ANISOU 2679  CG  LYS A 676    39938  28440  14584   7503   6108   5824       C  
ATOM   2680  CD  LYS A 676     -33.611 -23.181  18.217  1.00216.90           C  
ANISOU 2680  CD  LYS A 676    40249  27718  14444   7901   6585   6123       C  
ATOM   2681  CE  LYS A 676     -32.644 -24.349  18.162  1.00219.98           C  
ANISOU 2681  CE  LYS A 676    40839  28097  14646   8374   6578   6192       C  
ATOM   2682  NZ  LYS A 676     -33.186 -25.539  18.874  1.00224.67           N  
ANISOU 2682  NZ  LYS A 676    41949  28043  15374   8711   7184   6497       N  
ATOM   2683  N   TRP A 677     -36.552 -19.756  15.057  1.00209.65           N  
ANISOU 2683  N   TRP A 677    38162  27241  14253   6019   6461   5560       N  
ATOM   2684  CA  TRP A 677     -37.881 -19.150  14.951  1.00218.87           C  
ANISOU 2684  CA  TRP A 677    39254  28206  15701   5652   6746   5578       C  
ATOM   2685  C   TRP A 677     -37.795 -17.645  14.701  1.00205.65           C  
ANISOU 2685  C   TRP A 677    37172  26986  13979   5346   6340   5391       C  
ATOM   2686  O   TRP A 677     -38.554 -16.855  15.266  1.00216.15           O  
ANISOU 2686  O   TRP A 677    38470  28220  15436   5154   6434   5436       O  
ATOM   2687  CB  TRP A 677     -38.719 -19.445  16.199  1.00220.98           C  
ANISOU 2687  CB  TRP A 677    39875  27961  16128   5749   7169   5816       C  
ATOM   2688  CG  TRP A 677     -39.307 -20.827  16.245  1.00222.00           C  
ANISOU 2688  CG  TRP A 677    40385  27512  16453   5898   7756   5995       C  
ATOM   2689  CD1 TRP A 677     -40.388 -21.279  15.544  1.00213.58           C  
ANISOU 2689  CD1 TRP A 677    39190  26106  15857   5584   8133   5904       C  
ATOM   2690  CD2 TRP A 677     -38.864 -21.928  17.052  1.00246.38           C  
ANISOU 2690  CD2 TRP A 677    43878  30271  19462   6331   7970   6192       C  
ATOM   2691  NE1 TRP A 677     -40.637 -22.594  15.855  1.00235.92           N  
ANISOU 2691  NE1 TRP A 677    42326  28392  18922   5766   8588   6020       N  
ATOM   2692  CE2 TRP A 677     -39.717 -23.016  16.778  1.00248.84           C  
ANISOU 2692  CE2 TRP A 677    44416  30017  20116   6278   8574   6278       C  
ATOM   2693  CE3 TRP A 677     -37.826 -22.100  17.973  1.00249.43           C  
ANISOU 2693  CE3 TRP A 677    44413  30797  19562   6752   7711   6271       C  
ATOM   2694  CZ2 TRP A 677     -39.566 -24.257  17.395  1.00245.29           C  
ANISOU 2694  CZ2 TRP A 677    44420  29102  19677   6657   8975   6495       C  
ATOM   2695  CZ3 TRP A 677     -37.677 -23.335  18.583  1.00244.77           C  
ANISOU 2695  CZ3 TRP A 677    44247  29783  18971   7157   8071   6483       C  
ATOM   2696  CH2 TRP A 677     -38.541 -24.396  18.289  1.00244.51           C  
ANISOU 2696  CH2 TRP A 677    44501  29153  19247   7115   8710   6611       C  
ATOM   2697  N   THR A 678     -36.862 -17.245  13.842  1.00200.24           N  
ANISOU 2697  N   THR A 678    36174  26786  13122   5298   5902   5175       N  
ATOM   2698  CA  THR A 678     -36.598 -15.840  13.565  1.00208.90           C  
ANISOU 2698  CA  THR A 678    36887  28319  14164   5027   5519   4982       C  
ATOM   2699  C   THR A 678     -36.777 -15.563  12.078  1.00190.25           C  
ANISOU 2699  C   THR A 678    34198  26206  11883   4779   5429   4799       C  
ATOM   2700  O   THR A 678     -36.327 -16.342  11.233  1.00190.33           O  
ANISOU 2700  O   THR A 678    34157  26296  11865   4878   5369   4714       O  
ATOM   2701  CB  THR A 678     -35.184 -15.450  14.012  1.00207.38           C  
ANISOU 2701  CB  THR A 678    36586  28527  13680   5191   5052   4855       C  
ATOM   2702  OG1 THR A 678     -35.056 -15.665  15.423  1.00196.33           O  
ANISOU 2702  OG1 THR A 678    35473  26937  12186   5442   5145   5017       O  
ATOM   2703  CG2 THR A 678     -34.904 -13.986  13.704  1.00203.15           C  
ANISOU 2703  CG2 THR A 678    35670  28406  13112   4879   4720   4643       C  
ATOM   2704  N   GLU A 679     -37.440 -14.453  11.765  1.00197.88           N  
ANISOU 2704  N   GLU A 679    34912  27295  12980   4459   5412   4726       N  
ATOM   2705  CA  GLU A 679     -37.712 -14.059  10.389  1.00205.37           C  
ANISOU 2705  CA  GLU A 679    35523  28500  14007   4232   5344   4557       C  
ATOM   2706  C   GLU A 679     -36.658 -13.071   9.907  1.00180.33           C  
ANISOU 2706  C   GLU A 679    32006  25834  10678   4135   4848   4333       C  
ATOM   2707  O   GLU A 679     -36.357 -12.090  10.594  1.00179.75           O  
ANISOU 2707  O   GLU A 679    31866  25882  10549   4042   4675   4304       O  
ATOM   2708  CB  GLU A 679     -39.106 -13.443  10.266  1.00199.06           C  
ANISOU 2708  CB  GLU A 679    34631  27540  13463   3958   5646   4606       C  
ATOM   2709  CG  GLU A 679     -40.080 -14.281   9.460  1.00188.44           C  
ANISOU 2709  CG  GLU A 679    33030  25938  12632   3780   5873   4488       C  
ATOM   2710  CD  GLU A 679     -41.480 -13.703   9.450  1.00198.55           C  
ANISOU 2710  CD  GLU A 679    34207  27068  14164   3530   6174   4525       C  
ATOM   2711  OE1 GLU A 679     -41.624 -12.485   9.213  1.00193.78           O  
ANISOU 2711  OE1 GLU A 679    33444  26750  13433   3394   6057   4505       O  
ATOM   2712  OE2 GLU A 679     -42.437 -14.470   9.689  1.00216.43           O  
ANISOU 2712  OE2 GLU A 679    36556  28923  16753   3474   6548   4570       O  
ATOM   2713  N   TYR A 680     -36.107 -13.331   8.724  1.00178.98           N  
ANISOU 2713  N   TYR A 680    31614  25948  10442   4146   4646   4164       N  
ATOM   2714  CA  TYR A 680     -35.125 -12.461   8.099  1.00176.62           C  
ANISOU 2714  CA  TYR A 680    30967  26112  10027   4035   4209   3931       C  
ATOM   2715  C   TYR A 680     -35.652 -11.960   6.763  1.00193.07           C  
ANISOU 2715  C   TYR A 680    32693  28405  12262   3811   4198   3792       C  
ATOM   2716  O   TYR A 680     -36.466 -12.621   6.109  1.00174.34           O  
ANISOU 2716  O   TYR A 680    30120  25841  10282   3701   4351   3737       O  
ATOM   2717  CB  TYR A 680     -33.790 -13.184   7.874  1.00180.49           C  
ANISOU 2717  CB  TYR A 680    31449  26815  10315   4265   3894   3812       C  
ATOM   2718  CG  TYR A 680     -33.036 -13.537   9.135  1.00179.85           C  
ANISOU 2718  CG  TYR A 680    31625  26644  10067   4503   3812   3895       C  
ATOM   2719  CD1 TYR A 680     -33.340 -14.687   9.851  1.00185.93           C  
ANISOU 2719  CD1 TYR A 680    32780  27036  10830   4776   4097   4112       C  
ATOM   2720  CD2 TYR A 680     -32.005 -12.730   9.598  1.00179.45           C  
ANISOU 2720  CD2 TYR A 680    31428  26895   9859   4463   3475   3744       C  
ATOM   2721  CE1 TYR A 680     -32.647 -15.017  11.001  1.00213.87           C  
ANISOU 2721  CE1 TYR A 680    36540  30519  14200   5037   4023   4193       C  
ATOM   2722  CE2 TYR A 680     -31.306 -13.051  10.746  1.00201.43           C  
ANISOU 2722  CE2 TYR A 680    34415  29652  12465   4703   3399   3799       C  
ATOM   2723  CZ  TYR A 680     -31.631 -14.195  11.444  1.00212.41           C  
ANISOU 2723  CZ  TYR A 680    36177  30686  13843   5007   3661   4030       C  
ATOM   2724  OH  TYR A 680     -30.937 -14.519  12.588  1.00187.76           O  
ANISOU 2724  OH  TYR A 680    33249  27560  10531   5288   3590   4092       O  
ATOM   2725  N   ARG A 681     -35.185 -10.782   6.363  1.00174.53           N  
ANISOU 2725  N   ARG A 681    30062  26387   9865   3633   3937   3638       N  
ATOM   2726  CA  ARG A 681     -35.417 -10.279   5.017  1.00172.76           C  
ANISOU 2726  CA  ARG A 681    29478  26442   9720   3480   3865   3490       C  
ATOM   2727  C   ARG A 681     -34.219 -10.641   4.149  1.00168.68           C  
ANISOU 2727  C   ARG A 681    28742  26251   9098   3561   3495   3274       C  
ATOM   2728  O   ARG A 681     -33.070 -10.449   4.560  1.00168.85           O  
ANISOU 2728  O   ARG A 681    28784  26420   8953   3609   3218   3183       O  
ATOM   2729  CB  ARG A 681     -35.637  -8.765   5.030  1.00189.08           C  
ANISOU 2729  CB  ARG A 681    31346  28629  11867   3218   3825   3443       C  
ATOM   2730  CG  ARG A 681     -36.849  -8.316   5.835  1.00168.22           C  
ANISOU 2730  CG  ARG A 681    28860  25682   9376   3110   4158   3633       C  
ATOM   2731  CD  ARG A 681     -37.038  -6.807   5.763  1.00166.45           C  
ANISOU 2731  CD  ARG A 681    28431  25585   9228   2863   4123   3579       C  
ATOM   2732  NE  ARG A 681     -37.174  -6.334   4.389  1.00202.47           N  
ANISOU 2732  NE  ARG A 681    32651  30425  13855   2770   4056   3449       N  
ATOM   2733  CZ  ARG A 681     -37.481  -5.085   4.055  1.00203.57           C  
ANISOU 2733  CZ  ARG A 681    32593  30669  14087   2577   4078   3410       C  
ATOM   2734  NH1 ARG A 681     -37.690  -4.174   4.997  1.00204.04           N  
ANISOU 2734  NH1 ARG A 681    32760  30582  14184   2439   4166   3482       N  
ATOM   2735  NH2 ARG A 681     -37.581  -4.746   2.777  1.00195.75           N  
ANISOU 2735  NH2 ARG A 681    31295  29933  13148   2539   4021   3300       N  
ATOM   2736  N   VAL A 682     -34.486 -11.177   2.961  1.00175.96           N  
ANISOU 2736  N   VAL A 682    29298  27227  10333   3473   3424   3115       N  
ATOM   2737  CA  VAL A 682     -33.447 -11.700   2.082  1.00172.91           C  
ANISOU 2737  CA  VAL A 682    28672  27099   9928   3539   3083   2902       C  
ATOM   2738  C   VAL A 682     -33.665 -11.157   0.677  1.00165.14           C  
ANISOU 2738  C   VAL A 682    27223  26405   9120   3361   2960   2714       C  
ATOM   2739  O   VAL A 682     -34.772 -11.249   0.136  1.00165.00           O  
ANISOU 2739  O   VAL A 682    26990  26287   9413   3234   3150   2700       O  
ATOM   2740  CB  VAL A 682     -33.435 -13.242   2.065  1.00169.49           C  
ANISOU 2740  CB  VAL A 682    28284  26404   9711   3666   3121   2887       C  
ATOM   2741  CG1 VAL A 682     -32.407 -13.755   1.069  1.00168.76           C  
ANISOU 2741  CG1 VAL A 682    27914  26590   9618   3720   2768   2658       C  
ATOM   2742  CG2 VAL A 682     -33.152 -13.790   3.457  1.00175.74           C  
ANISOU 2742  CG2 VAL A 682    29560  26921  10290   3899   3253   3095       C  
ATOM   2743  N   TRP A 683     -32.609 -10.601   0.089  1.00183.29           N  
ANISOU 2743  N   TRP A 683    29358  29075  11209   3366   2653   2559       N  
ATOM   2744  CA  TRP A 683     -32.616 -10.130  -1.288  1.00161.57           C  
ANISOU 2744  CA  TRP A 683    26175  26631   8584   3245   2506   2376       C  
ATOM   2745  C   TRP A 683     -31.517 -10.838  -2.070  1.00161.27           C  
ANISOU 2745  C   TRP A 683    25930  26813   8532   3326   2160   2166       C  
ATOM   2746  O   TRP A 683     -30.433 -11.097  -1.539  1.00190.31           O  
ANISOU 2746  O   TRP A 683    29800  30552  11955   3461   1972   2143       O  
ATOM   2747  CB  TRP A 683     -32.406  -8.612  -1.364  1.00159.88           C  
ANISOU 2747  CB  TRP A 683    25948  26663   8136   3155   2504   2384       C  
ATOM   2748  CG  TRP A 683     -33.344  -7.809  -0.514  1.00162.27           C  
ANISOU 2748  CG  TRP A 683    26462  26739   8452   3060   2818   2583       C  
ATOM   2749  CD1 TRP A 683     -34.517  -7.232  -0.906  1.00172.67           C  
ANISOU 2749  CD1 TRP A 683    27654  28043   9908   2972   3067   2666       C  
ATOM   2750  CD2 TRP A 683     -33.178  -7.480   0.871  1.00175.74           C  
ANISOU 2750  CD2 TRP A 683    28482  28189  10104   3012   2890   2694       C  
ATOM   2751  NE1 TRP A 683     -35.095  -6.570   0.150  1.00160.05           N  
ANISOU 2751  NE1 TRP A 683    26286  26168   8360   2861   3286   2826       N  
ATOM   2752  CE2 TRP A 683     -34.292  -6.707   1.252  1.00163.39           C  
ANISOU 2752  CE2 TRP A 683    26973  26444   8664   2880   3181   2843       C  
ATOM   2753  CE3 TRP A 683     -32.198  -7.767   1.825  1.00182.86           C  
ANISOU 2753  CE3 TRP A 683    29594  29025  10860   3081   2729   2671       C  
ATOM   2754  CZ2 TRP A 683     -34.454  -6.219   2.547  1.00185.85           C  
ANISOU 2754  CZ2 TRP A 683    30075  29042  11500   2802   3309   2966       C  
ATOM   2755  CZ3 TRP A 683     -32.360  -7.281   3.111  1.00163.50           C  
ANISOU 2755  CZ3 TRP A 683    27387  26355   8381   3019   2862   2790       C  
ATOM   2756  CH2 TRP A 683     -33.478  -6.515   3.459  1.00170.52           C  
ANISOU 2756  CH2 TRP A 683    28324  27063   9404   2875   3147   2935       C  
ATOM   2757  N   VAL A 684     -31.802 -11.151  -3.333  1.00163.86           N  
ANISOU 2757  N   VAL A 684    25853  27283   9122   3254   2074   2002       N  
ATOM   2758  CA  VAL A 684     -30.839 -11.769  -4.237  1.00161.83           C  
ANISOU 2758  CA  VAL A 684    25347  27256   8884   3310   1747   1787       C  
ATOM   2759  C   VAL A 684     -30.586 -10.810  -5.391  1.00178.88           C  
ANISOU 2759  C   VAL A 684    27161  29803  11003   3221   1588   1641       C  
ATOM   2760  O   VAL A 684     -31.515 -10.157  -5.881  1.00187.25           O  
ANISOU 2760  O   VAL A 684    28038  30917  12190   3124   1757   1670       O  
ATOM   2761  CB  VAL A 684     -31.335 -13.136  -4.754  1.00161.15           C  
ANISOU 2761  CB  VAL A 684    25077  26994   9160   3318   1788   1694       C  
ATOM   2762  CG1 VAL A 684     -30.218 -13.869  -5.487  1.00160.92           C  
ANISOU 2762  CG1 VAL A 684    24864  27163   9115   3402   1450   1494       C  
ATOM   2763  CG2 VAL A 684     -31.868 -13.977  -3.606  1.00167.69           C  
ANISOU 2763  CG2 VAL A 684    26266  27375  10074   3389   2062   1871       C  
ATOM   2764  N   ARG A 685     -29.331 -10.733  -5.831  1.00178.91           N  
ANISOU 2764  N   ARG A 685    27075  30082  10821   3272   1274   1486       N  
ATOM   2765  CA  ARG A 685     -28.905  -9.719  -6.785  1.00156.93           C  
ANISOU 2765  CA  ARG A 685    24034  27653   7940   3204   1140   1362       C  
ATOM   2766  C   ARG A 685     -27.922 -10.316  -7.781  1.00166.96           C  
ANISOU 2766  C   ARG A 685    25025  29178   9234   3253    796   1131       C  
ATOM   2767  O   ARG A 685     -27.107 -11.171  -7.424  1.00155.17           O  
ANISOU 2767  O   ARG A 685    23648  27644   7665   3356    612   1074       O  
ATOM   2768  CB  ARG A 685     -28.264  -8.532  -6.055  1.00154.45           C  
ANISOU 2768  CB  ARG A 685    23927  27286   7469   3095   1148   1391       C  
ATOM   2769  CG  ARG A 685     -27.930  -7.349  -6.935  1.00170.97           C  
ANISOU 2769  CG  ARG A 685    25768  29518   9676   2929   1089   1267       C  
ATOM   2770  CD  ARG A 685     -27.193  -6.294  -6.138  1.00159.74           C  
ANISOU 2770  CD  ARG A 685    24542  27949   8203   2763   1105   1242       C  
ATOM   2771  NE  ARG A 685     -27.969  -5.816  -4.999  1.00156.32           N  
ANISOU 2771  NE  ARG A 685    24402  27268   7725   2710   1391   1441       N  
ATOM   2772  CZ  ARG A 685     -28.845  -4.820  -5.060  1.00182.11           C  
ANISOU 2772  CZ  ARG A 685    27669  30449  11075   2604   1656   1554       C  
ATOM   2773  NH1 ARG A 685     -29.061  -4.193  -6.208  1.00151.73           N  
ANISOU 2773  NH1 ARG A 685    23553  26749   7348   2563   1681   1498       N  
ATOM   2774  NH2 ARG A 685     -29.503  -4.445  -3.973  1.00217.23           N  
ANISOU 2774  NH2 ARG A 685    32382  34660  15493   2550   1898   1727       N  
ATOM   2775  N   ALA A 686     -28.005  -9.858  -9.028  1.00173.24           N  
ANISOU 2775  N   ALA A 686    25458  30245  10122   3200    717   1006       N  
ATOM   2776  CA  ALA A 686     -27.126 -10.299 -10.101  1.00159.74           C  
ANISOU 2776  CA  ALA A 686    23447  28807   8441   3236    398    782       C  
ATOM   2777  C   ALA A 686     -26.167  -9.181 -10.492  1.00150.90           C  
ANISOU 2777  C   ALA A 686    22236  27750   7348   3101    259    673       C  
ATOM   2778  O   ALA A 686     -26.478  -7.995 -10.345  1.00149.97           O  
ANISOU 2778  O   ALA A 686    22178  27542   7263   2984    447    755       O  
ATOM   2779  CB  ALA A 686     -27.935 -10.743 -11.324  1.00171.85           C  
ANISOU 2779  CB  ALA A 686    24560  30445  10290   3213    403    677       C  
ATOM   2780  N   HIS A 687     -24.996  -9.567 -10.999  1.00150.14           N  
ANISOU 2780  N   HIS A 687    21995  27757   7292   3103    -50    480       N  
ATOM   2781  CA  HIS A 687     -23.951  -8.614 -11.345  1.00149.49           C  
ANISOU 2781  CA  HIS A 687    21835  27683   7282   2960   -173    349       C  
ATOM   2782  C   HIS A 687     -23.385  -8.905 -12.725  1.00149.70           C  
ANISOU 2782  C   HIS A 687    21484  27939   7456   2976   -420    153       C  
ATOM   2783  O   HIS A 687     -23.279 -10.059 -13.146  1.00148.29           O  
ANISOU 2783  O   HIS A 687    21161  27883   7300   3088   -604     67       O  
ATOM   2784  CB  HIS A 687     -22.789  -8.639 -10.344  1.00165.02           C  
ANISOU 2784  CB  HIS A 687    24048  29506   9144   2917   -304    291       C  
ATOM   2785  CG  HIS A 687     -23.207  -8.468  -8.919  1.00156.46           C  
ANISOU 2785  CG  HIS A 687    23335  28204   7909   2918    -98    465       C  
ATOM   2786  ND1 HIS A 687     -23.886  -9.443  -8.222  1.00169.27           N  
ANISOU 2786  ND1 HIS A 687    25150  29734   9432   3077     -9    618       N  
ATOM   2787  CD2 HIS A 687     -23.031  -7.440  -8.057  1.00162.01           C  
ANISOU 2787  CD2 HIS A 687    24255  28761   8540   2782     51    506       C  
ATOM   2788  CE1 HIS A 687     -24.118  -9.019  -6.993  1.00180.62           C  
ANISOU 2788  CE1 HIS A 687    26903  30967  10757   3045    177    759       C  
ATOM   2789  NE2 HIS A 687     -23.609  -7.807  -6.866  1.00179.71           N  
ANISOU 2789  NE2 HIS A 687    26796  30829  10656   2859    206    685       N  
ATOM   2790  N   THR A 688     -23.008  -7.835 -13.413  1.00146.79           N  
ANISOU 2790  N   THR A 688    20973  27617   7184   2868   -402     84       N  
ATOM   2791  CA  THR A 688     -22.153  -7.876 -14.587  1.00145.77           C  
ANISOU 2791  CA  THR A 688    20539  27651   7195   2855   -633   -109       C  
ATOM   2792  C   THR A 688     -20.811  -7.242 -14.230  1.00145.66           C  
ANISOU 2792  C   THR A 688    20647  27534   7162   2724   -725   -229       C  
ATOM   2793  O   THR A 688     -20.559  -6.878 -13.079  1.00164.72           O  
ANISOU 2793  O   THR A 688    23357  29782   9445   2654   -634   -182       O  
ATOM   2794  CB  THR A 688     -22.811  -7.156 -15.766  1.00155.68           C  
ANISOU 2794  CB  THR A 688    21519  29067   8566   2871   -508    -93       C  
ATOM   2795  OG1 THR A 688     -23.219  -5.843 -15.359  1.00144.70           O  
ANISOU 2795  OG1 THR A 688    20313  27542   7127   2786   -211     42       O  
ATOM   2796  CG2 THR A 688     -24.022  -7.931 -16.258  1.00157.10           C  
ANISOU 2796  CG2 THR A 688    21494  29427   8769   3007   -466    -42       C  
ATOM   2797  N   ASP A 689     -19.939  -7.109 -15.231  1.00155.02           N  
ANISOU 2797  N   ASP A 689    21590  28835   8475   2691   -898   -400       N  
ATOM   2798  CA  ASP A 689     -18.695  -6.379 -15.013  1.00150.75           C  
ANISOU 2798  CA  ASP A 689    21133  28229   7916   2556   -945   -537       C  
ATOM   2799  C   ASP A 689     -18.938  -4.898 -14.752  1.00144.67           C  
ANISOU 2799  C   ASP A 689    20520  27370   7079   2435   -640   -470       C  
ATOM   2800  O   ASP A 689     -18.106  -4.247 -14.112  1.00145.23           O  
ANISOU 2800  O   ASP A 689    20763  27356   7064   2307   -603   -563       O  
ATOM   2801  CB  ASP A 689     -17.761  -6.544 -16.214  1.00181.31           C  
ANISOU 2801  CB  ASP A 689    24703  32238  11948   2551  -1166   -726       C  
ATOM   2802  CG  ASP A 689     -17.095  -7.903 -16.253  1.00180.00           C  
ANISOU 2802  CG  ASP A 689    24442  32108  11840   2628  -1478   -835       C  
ATOM   2803  OD1 ASP A 689     -16.902  -8.503 -15.174  1.00178.01           O  
ANISOU 2803  OD1 ASP A 689    24411  31756  11469   2659  -1536   -806       O  
ATOM   2804  OD2 ASP A 689     -16.758  -8.366 -17.362  1.00177.28           O  
ANISOU 2804  OD2 ASP A 689    23809  31890  11660   2669  -1652   -945       O  
ATOM   2805  N   VAL A 690     -20.059  -4.356 -15.231  1.00161.42           N  
ANISOU 2805  N   VAL A 690    22581  29519   9232   2479   -408   -319       N  
ATOM   2806  CA  VAL A 690     -20.352  -2.941 -15.031  1.00144.27           C  
ANISOU 2806  CA  VAL A 690    20568  27243   7005   2379    -83   -235       C  
ATOM   2807  C   VAL A 690     -20.772  -2.681 -13.591  1.00147.14           C  
ANISOU 2807  C   VAL A 690    21279  27406   7221   2308    100   -113       C  
ATOM   2808  O   VAL A 690     -20.443  -1.639 -13.012  1.00157.37           O  
ANISOU 2808  O   VAL A 690    22781  28579   8432   2167    295   -134       O  
ATOM   2809  CB  VAL A 690     -21.428  -2.482 -16.033  1.00158.29           C  
ANISOU 2809  CB  VAL A 690    22155  29116   8870   2483    108   -100       C  
ATOM   2810  CG1 VAL A 690     -21.730  -0.998 -15.862  1.00143.89           C  
ANISOU 2810  CG1 VAL A 690    20514  27158   7000   2396    474      2       C  
ATOM   2811  CG2 VAL A 690     -20.982  -2.781 -17.454  1.00142.76           C  
ANISOU 2811  CG2 VAL A 690    19833  27367   7043   2569    -87   -228       C  
ATOM   2812  N   GLY A 691     -21.503  -3.616 -12.992  1.00187.48           N  
ANISOU 2812  N   GLY A 691    26461  32481  12291   2403     60      8       N  
ATOM   2813  CA  GLY A 691     -21.936  -3.476 -11.625  1.00146.84           C  
ANISOU 2813  CA  GLY A 691    21639  27145   7009   2356    227    137       C  
ATOM   2814  C   GLY A 691     -23.152  -4.320 -11.311  1.00147.23           C  
ANISOU 2814  C   GLY A 691    21724  27172   7046   2490    290    325       C  
ATOM   2815  O   GLY A 691     -23.569  -5.179 -12.094  1.00146.87           O  
ANISOU 2815  O   GLY A 691    21445  27281   7079   2620    169    321       O  
ATOM   2816  N   PRO A 692     -23.737  -4.096 -10.141  1.00170.64           N  
ANISOU 2816  N   PRO A 692    24980  29950   9907   2455    494    479       N  
ATOM   2817  CA  PRO A 692     -24.926  -4.854  -9.747  1.00155.22           C  
ANISOU 2817  CA  PRO A 692    23095  27949   7931   2577    603    666       C  
ATOM   2818  C   PRO A 692     -26.199  -4.314 -10.381  1.00153.20           C  
ANISOU 2818  C   PRO A 692    22710  27727   7771   2606    855    810       C  
ATOM   2819  O   PRO A 692     -26.364  -3.110 -10.589  1.00155.95           O  
ANISOU 2819  O   PRO A 692    23073  28017   8164   2513   1055    849       O  
ATOM   2820  CB  PRO A 692     -24.959  -4.674  -8.226  1.00149.96           C  
ANISOU 2820  CB  PRO A 692    22798  27054   7124   2517    738    771       C  
ATOM   2821  CG  PRO A 692     -24.286  -3.371  -8.002  1.00149.76           C  
ANISOU 2821  CG  PRO A 692    22865  26963   7075   2331    833    682       C  
ATOM   2822  CD  PRO A 692     -23.209  -3.277  -9.036  1.00148.91           C  
ANISOU 2822  CD  PRO A 692    22512  27031   7036   2305    610    460       C  
ATOM   2823  N   GLY A 693     -27.109  -5.237 -10.683  1.00154.62           N  
ANISOU 2823  N   GLY A 693    22763  28012   7975   2748    862    882       N  
ATOM   2824  CA  GLY A 693     -28.432  -4.885 -11.140  1.00151.16           C  
ANISOU 2824  CA  GLY A 693    22198  27628   7608   2801   1108   1018       C  
ATOM   2825  C   GLY A 693     -29.388  -4.779  -9.972  1.00149.33           C  
ANISOU 2825  C   GLY A 693    22263  27162   7315   2783   1386   1230       C  
ATOM   2826  O   GLY A 693     -28.977  -4.800  -8.808  1.00150.99           O  
ANISOU 2826  O   GLY A 693    22787  27157   7425   2718   1400   1276       O  
ATOM   2827  N   PRO A 694     -30.683  -4.665 -10.252  1.00149.56           N  
ANISOU 2827  N   PRO A 694    22185  27238   7402   2847   1615   1357       N  
ATOM   2828  CA  PRO A 694     -31.661  -4.591  -9.164  1.00150.53           C  
ANISOU 2828  CA  PRO A 694    22581  27124   7488   2829   1896   1563       C  
ATOM   2829  C   PRO A 694     -31.840  -5.942  -8.492  1.00151.74           C  
ANISOU 2829  C   PRO A 694    22877  27237   7540   2931   1864   1597       C  
ATOM   2830  O   PRO A 694     -31.602  -6.998  -9.085  1.00169.03           O  
ANISOU 2830  O   PRO A 694    24869  29604   9750   3024   1671   1463       O  
ATOM   2831  CB  PRO A 694     -32.944  -4.145  -9.871  1.00150.49           C  
ANISOU 2831  CB  PRO A 694    22348  27242   7590   2888   2124   1649       C  
ATOM   2832  CG  PRO A 694     -32.800  -4.696 -11.247  1.00150.03           C  
ANISOU 2832  CG  PRO A 694    21871  27558   7576   3006   1918   1473       C  
ATOM   2833  CD  PRO A 694     -31.330  -4.617 -11.575  1.00149.11           C  
ANISOU 2833  CD  PRO A 694    21736  27470   7449   2949   1627   1307       C  
ATOM   2834  N   GLU A 695     -32.255  -5.898  -7.233  1.00157.38           N  
ANISOU 2834  N   GLU A 695    23940  27658   8197   2897   2065   1770       N  
ATOM   2835  CA  GLU A 695     -32.492  -7.100  -6.451  1.00173.63           C  
ANISOU 2835  CA  GLU A 695    26193  29530  10249   2975   2095   1832       C  
ATOM   2836  C   GLU A 695     -33.969  -7.474  -6.481  1.00161.65           C  
ANISOU 2836  C   GLU A 695    24571  27837   9014   2945   2354   1915       C  
ATOM   2837  O   GLU A 695     -34.845  -6.636  -6.709  1.00154.69           O  
ANISOU 2837  O   GLU A 695    23606  27014   8155   2916   2569   2005       O  
ATOM   2838  CB  GLU A 695     -32.026  -6.904  -5.006  1.00154.99           C  
ANISOU 2838  CB  GLU A 695    24273  26911   7704   2956   2153   1957       C  
ATOM   2839  CG  GLU A 695     -32.762  -5.801  -4.268  1.00154.99           C  
ANISOU 2839  CG  GLU A 695    24452  26673   7764   2816   2434   2123       C  
ATOM   2840  CD  GLU A 695     -32.143  -5.491  -2.921  1.00173.10           C  
ANISOU 2840  CD  GLU A 695    27088  28720   9963   2733   2428   2173       C  
ATOM   2841  OE1 GLU A 695     -31.004  -5.941  -2.672  1.00160.00           O  
ANISOU 2841  OE1 GLU A 695    25490  27111   8192   2773   2180   2054       O  
ATOM   2842  OE2 GLU A 695     -32.793  -4.793  -2.114  1.00156.11           O  
ANISOU 2842  OE2 GLU A 695    25119  26346   7847   2630   2665   2319       O  
ATOM   2843  N   SER A 696     -34.237  -8.755  -6.246  1.00157.44           N  
ANISOU 2843  N   SER A 696    24040  27085   8694   2956   2351   1874       N  
ATOM   2844  CA  SER A 696     -35.605  -9.244  -6.257  1.00168.12           C  
ANISOU 2844  CA  SER A 696    25278  28259  10342   2906   2607   1903       C  
ATOM   2845  C   SER A 696     -36.368  -8.735  -5.039  1.00182.02           C  
ANISOU 2845  C   SER A 696    27400  29723  12036   2870   2927   2149       C  
ATOM   2846  O   SER A 696     -35.787  -8.272  -4.053  1.00163.79           O  
ANISOU 2846  O   SER A 696    25466  27297   9471   2895   2939   2291       O  
ATOM   2847  CB  SER A 696     -35.628 -10.772  -6.282  1.00166.88           C  
ANISOU 2847  CB  SER A 696    25058  27905  10443   2912   2563   1779       C  
ATOM   2848  OG  SER A 696     -35.010 -11.305  -5.123  1.00164.33           O  
ANISOU 2848  OG  SER A 696    25157  27287   9994   2976   2563   1898       O  
ATOM   2849  N   SER A 697     -37.691  -8.815  -5.124  1.00189.45           N  
ANISOU 2849  N   SER A 697    28210  30568  13206   2813   3187   2179       N  
ATOM   2850  CA  SER A 697     -38.514  -8.541  -3.959  1.00160.23           C  
ANISOU 2850  CA  SER A 697    24842  26543   9493   2774   3506   2402       C  
ATOM   2851  C   SER A 697     -38.171  -9.540  -2.857  1.00176.33           C  
ANISOU 2851  C   SER A 697    27248  28203  11548   2806   3544   2479       C  
ATOM   2852  O   SER A 697     -37.956 -10.726  -3.140  1.00162.90           O  
ANISOU 2852  O   SER A 697    25442  26417  10037   2825   3455   2340       O  
ATOM   2853  CB  SER A 697     -40.000  -8.626  -4.309  1.00161.11           C  
ANISOU 2853  CB  SER A 697    24704  26631   9880   2706   3771   2376       C  
ATOM   2854  OG  SER A 697     -40.368  -7.618  -5.235  1.00174.33           O  
ANISOU 2854  OG  SER A 697    26077  28668  11494   2726   3767   2344       O  
ATOM   2855  N   PRO A 698     -38.095  -9.103  -1.602  1.00177.50           N  
ANISOU 2855  N   PRO A 698    27831  28122  11489   2830   3687   2700       N  
ATOM   2856  CA  PRO A 698     -37.644 -10.008  -0.540  1.00163.99           C  
ANISOU 2856  CA  PRO A 698    26490  26089   9731   2917   3710   2790       C  
ATOM   2857  C   PRO A 698     -38.646 -11.122  -0.277  1.00166.14           C  
ANISOU 2857  C   PRO A 698    26780  26002  10344   2882   3980   2800       C  
ATOM   2858  O   PRO A 698     -39.861 -10.920  -0.331  1.00193.20           O  
ANISOU 2858  O   PRO A 698    30100  29337  13969   2776   4245   2830       O  
ATOM   2859  CB  PRO A 698     -37.498  -9.085   0.676  1.00189.10           C  
ANISOU 2859  CB  PRO A 698    30085  29163  12602   2945   3830   3016       C  
ATOM   2860  CG  PRO A 698     -38.405  -7.940   0.390  1.00177.26           C  
ANISOU 2860  CG  PRO A 698    28456  27771  11124   2834   4013   3080       C  
ATOM   2861  CD  PRO A 698     -38.376  -7.748  -1.097  1.00161.37           C  
ANISOU 2861  CD  PRO A 698    25966  26118   9229   2796   3839   2875       C  
ATOM   2862  N   VAL A 699     -38.114 -12.310  -0.003  1.00167.71           N  
ANISOU 2862  N   VAL A 699    27115  26000  10609   2976   3928   2765       N  
ATOM   2863  CA  VAL A 699     -38.903 -13.473   0.384  1.00175.47           C  
ANISOU 2863  CA  VAL A 699    28192  26575  11904   2957   4223   2780       C  
ATOM   2864  C   VAL A 699     -38.658 -13.733   1.863  1.00171.94           C  
ANISOU 2864  C   VAL A 699    28294  25769  11266   3102   4386   3036       C  
ATOM   2865  O   VAL A 699     -37.506 -13.736   2.316  1.00171.87           O  
ANISOU 2865  O   VAL A 699    28516  25839  10949   3271   4168   3096       O  
ATOM   2866  CB  VAL A 699     -38.547 -14.707  -0.463  1.00171.11           C  
ANISOU 2866  CB  VAL A 699    27382  26030  11601   2969   4099   2545       C  
ATOM   2867  CG1 VAL A 699     -39.231 -15.951   0.086  1.00175.28           C  
ANISOU 2867  CG1 VAL A 699    28086  26076  12436   2961   4451   2570       C  
ATOM   2868  CG2 VAL A 699     -38.937 -14.483  -1.916  1.00169.70           C  
ANISOU 2868  CG2 VAL A 699    26638  26214  11626   2830   3970   2281       C  
ATOM   2869  N   LEU A 700     -39.735 -13.944   2.612  1.00173.63           N  
ANISOU 2869  N   LEU A 700    28708  25613  11649   3049   4770   3177       N  
ATOM   2870  CA  LEU A 700     -39.662 -14.134   4.053  1.00181.53           C  
ANISOU 2870  CA  LEU A 700    30239  26262  12472   3196   4973   3443       C  
ATOM   2871  C   LEU A 700     -39.636 -15.620   4.385  1.00178.35           C  
ANISOU 2871  C   LEU A 700    30024  25467  12276   3308   5159   3450       C  
ATOM   2872  O   LEU A 700     -40.339 -16.421   3.761  1.00179.49           O  
ANISOU 2872  O   LEU A 700    29925  25455  12817   3179   5338   3285       O  
ATOM   2873  CB  LEU A 700     -40.843 -13.458   4.755  1.00175.69           C  
ANISOU 2873  CB  LEU A 700    29651  25322  11780   3086   5311   3617       C  
ATOM   2874  CG  LEU A 700     -40.757 -11.951   5.024  1.00173.53           C  
ANISOU 2874  CG  LEU A 700    29433  25307  11195   3051   5218   3729       C  
ATOM   2875  CD1 LEU A 700     -40.666 -11.136   3.739  1.00179.73           C  
ANISOU 2875  CD1 LEU A 700    29756  26541  11991   2928   4978   3536       C  
ATOM   2876  CD2 LEU A 700     -41.942 -11.493   5.861  1.00185.56           C  
ANISOU 2876  CD2 LEU A 700    31165  26555  12783   2968   5592   3924       C  
ATOM   2877  N   VAL A 701     -38.820 -15.981   5.371  1.00179.79           N  
ANISOU 2877  N   VAL A 701    30635  25500  12179   3559   5135   3632       N  
ATOM   2878  CA  VAL A 701     -38.647 -17.374   5.768  1.00194.88           C  
ANISOU 2878  CA  VAL A 701    32790  27032  14224   3730   5323   3681       C  
ATOM   2879  C   VAL A 701     -38.267 -17.408   7.242  1.00208.65           C  
ANISOU 2879  C   VAL A 701    35099  28553  15628   4005   5450   3985       C  
ATOM   2880  O   VAL A 701     -37.546 -16.534   7.732  1.00204.27           O  
ANISOU 2880  O   VAL A 701    34681  28275  14656   4118   5214   4075       O  
ATOM   2881  CB  VAL A 701     -37.594 -18.080   4.882  1.00182.57           C  
ANISOU 2881  CB  VAL A 701    31012  25688  12670   3822   5002   3479       C  
ATOM   2882  CG1 VAL A 701     -36.243 -17.383   4.987  1.00180.86           C  
ANISOU 2882  CG1 VAL A 701    30850  25892  11977   3994   4567   3495       C  
ATOM   2883  CG2 VAL A 701     -37.479 -19.557   5.240  1.00185.95           C  
ANISOU 2883  CG2 VAL A 701    31694  25692  13267   4001   5246   3530       C  
ATOM   2884  N   ARG A 702     -38.769 -18.415   7.953  1.00217.21           N  
ANISOU 2884  N   ARG A 702    36506  29137  16889   4115   5848   4131       N  
ATOM   2885  CA  ARG A 702     -38.513 -18.587   9.376  1.00205.75           C  
ANISOU 2885  CA  ARG A 702    35609  27431  15135   4414   6029   4438       C  
ATOM   2886  C   ARG A 702     -37.804 -19.913   9.614  1.00196.62           C  
ANISOU 2886  C   ARG A 702    34706  26042  13958   4723   6097   4495       C  
ATOM   2887  O   ARG A 702     -38.180 -20.940   9.039  1.00208.27           O  
ANISOU 2887  O   ARG A 702    36061  27242  15831   4643   6307   4373       O  
ATOM   2888  CB  ARG A 702     -39.816 -18.535  10.185  1.00205.37           C  
ANISOU 2888  CB  ARG A 702    35802  26947  15283   4312   6514   4621       C  
ATOM   2889  CG  ARG A 702     -39.637 -18.793  11.673  1.00219.95           C  
ANISOU 2889  CG  ARG A 702    38240  28495  16836   4641   6748   4952       C  
ATOM   2890  CD  ARG A 702     -40.966 -18.739  12.410  1.00211.93           C  
ANISOU 2890  CD  ARG A 702    37442  27039  16044   4517   7238   5119       C  
ATOM   2891  NE  ARG A 702     -41.584 -17.418  12.326  1.00216.68           N  
ANISOU 2891  NE  ARG A 702    37847  27873  16607   4257   7161   5096       N  
ATOM   2892  CZ  ARG A 702     -42.776 -17.117  12.832  1.00204.83           C  
ANISOU 2892  CZ  ARG A 702    36453  26087  15288   4098   7525   5207       C  
ATOM   2893  NH1 ARG A 702     -43.487 -18.044  13.459  1.00196.99           N  
ANISOU 2893  NH1 ARG A 702    35756  24554  14539   4155   8001   5340       N  
ATOM   2894  NH2 ARG A 702     -43.259 -15.888  12.709  1.00206.86           N  
ANISOU 2894  NH2 ARG A 702    36526  26588  15483   3886   7435   5187       N  
ATOM   2895  N   THR A 703     -36.777 -19.886  10.461  1.00194.26           N  
ANISOU 2895  N   THR A 703    34752  25870  13189   5083   5933   4670       N  
ATOM   2896  CA  THR A 703     -36.023 -21.091  10.765  1.00202.85           C  
ANISOU 2896  CA  THR A 703    36116  26773  14184   5445   5991   4759       C  
ATOM   2897  C   THR A 703     -36.858 -22.046  11.619  1.00220.27           C  
ANISOU 2897  C   THR A 703    38746  28334  16612   5574   6576   4993       C  
ATOM   2898  O   THR A 703     -37.940 -21.707  12.109  1.00240.76           O  
ANISOU 2898  O   THR A 703    41449  30654  19374   5405   6908   5101       O  
ATOM   2899  CB  THR A 703     -34.717 -20.744  11.477  1.00203.31           C  
ANISOU 2899  CB  THR A 703    36413  27200  13637   5823   5654   4871       C  
ATOM   2900  OG1 THR A 703     -34.994 -19.907  12.607  1.00211.24           O  
ANISOU 2900  OG1 THR A 703    37710  28210  14344   5896   5755   5083       O  
ATOM   2901  CG2 THR A 703     -33.770 -20.019  10.531  1.00197.33           C  
ANISOU 2901  CG2 THR A 703    35233  27045  12700   5707   5101   4602       C  
ATOM   2902  N   ASP A 704     -36.331 -23.257  11.792  1.00213.71           N  
ANISOU 2902  N   ASP A 704    38164  27255  15781   5887   6720   5073       N  
ATOM   2903  CA  ASP A 704     -37.018 -24.337  12.501  1.00211.73           C  
ANISOU 2903  CA  ASP A 704    38329  26350  15770   6038   7318   5283       C  
ATOM   2904  C   ASP A 704     -38.360 -24.652  11.847  1.00212.48           C  
ANISOU 2904  C   ASP A 704    38164  26072  16498   5597   7700   5103       C  
ATOM   2905  O   ASP A 704     -38.412 -25.186  10.739  1.00207.98           O  
ANISOU 2905  O   ASP A 704    37224  25512  16285   5384   7658   4825       O  
ATOM   2906  CB  ASP A 704     -37.223 -23.986  13.978  1.00210.31           C  
ANISOU 2906  CB  ASP A 704    38663  25995  15251   6310   7551   5634       C  
ATOM   2907  CG  ASP A 704     -37.727 -25.164  14.792  1.00228.20           C  
ANISOU 2907  CG  ASP A 704    41427  27590  17688   6561   8170   5889       C  
ATOM   2908  OD1 ASP A 704     -36.921 -25.764  15.533  1.00218.02           O  
ANISOU 2908  OD1 ASP A 704    40553  26242  16044   7062   8215   6120       O  
ATOM   2909  OD2 ASP A 704     -38.926 -25.497  14.682  1.00229.90           O  
ANISOU 2909  OD2 ASP A 704    41619  27343  18390   6270   8628   5852       O  
TER    2910      ASP A 704                                                      
HETATM 2911  S   SO4 A 801     -21.623 -13.829 -59.116  1.00182.56           S  
HETATM 2912  O1  SO4 A 801     -21.160 -13.111 -60.300  1.00198.84           O  
HETATM 2913  O2  SO4 A 801     -23.042 -14.141 -59.259  1.00188.10           O  
HETATM 2914  O3  SO4 A 801     -20.865 -15.069 -58.971  1.00168.58           O  
HETATM 2915  O4  SO4 A 801     -21.425 -12.996 -57.933  1.00142.54           O  
HETATM 2916  S   SO4 A 802     -15.939 -14.427 -77.182  1.00188.75           S  
HETATM 2917  O1  SO4 A 802     -14.813 -14.646 -78.085  1.00197.43           O  
HETATM 2918  O2  SO4 A 802     -17.096 -13.973 -77.948  1.00190.93           O  
HETATM 2919  O3  SO4 A 802     -16.267 -15.677 -76.502  1.00169.91           O  
HETATM 2920  O4  SO4 A 802     -15.580 -13.414 -76.193  1.00179.79           O  
HETATM 2921  O   HOH A 901     -25.952   5.420 -51.955  1.00103.41           O  
CONECT 2911 2912 2913 2914 2915                                                 
CONECT 2912 2911                                                                
CONECT 2913 2911                                                                
CONECT 2914 2911                                                                
CONECT 2915 2911                                                                
CONECT 2916 2917 2918 2919 2920                                                 
CONECT 2917 2916                                                                
CONECT 2918 2916                                                                
CONECT 2919 2916                                                                
CONECT 2920 2916                                                                
MASTER      355    0    2    2   40    0    2    6 2920    1   10   31          
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.