CNRS Nantes University US2B US2B
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***  SUGAR BINDING PROTEIN 09-MAY-18 6GHV  ***

elNémo ID: 2404072221082869318

Job options:

ID        	=	 2404072221082869318
JOBID     	=	 SUGAR BINDING PROTEIN 09-MAY-18 6GHV
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    SUGAR BINDING PROTEIN                   09-MAY-18   6GHV              
TITLE     STRUCTURE OF A DC-SIGN CRD IN COMPLEX WITH HIGH AFFINITY GLYCOMIMETIC.
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD209 ANTIGEN;                                             
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER L,DENDRITIC CELL-      
COMPND   5 SPECIFIC ICAM-3-GRABBING NON-INTEGRIN 1,DC-SIGN1;                    
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: CD209, CLEC4L;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    DC-SIGN, INHIBITOR, SUGAR BINDING PROTEIN                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.THEPAUT,S.ACHILLI,L.MEDVE,A.BERNARDI,F.FIESCHI                      
REVDAT   3   17-JAN-24 6GHV    1       LINK                                     
REVDAT   2   27-NOV-19 6GHV    1       JRNL                                     
REVDAT   1   11-SEP-19 6GHV    0                                                
JRNL        AUTH   L.MEDVE,S.ACHILLI,J.GUZMAN-CALDENTEY,M.THEPAUT,L.SENALDI,    
JRNL        AUTH 2 A.LE ROY,S.SATTIN,C.EBEL,C.VIVES,S.MARTIN-SANTAMARIA,        
JRNL        AUTH 3 A.BERNARDI,F.FIESCHI                                         
JRNL        TITL   ENHANCING POTENCY AND SELECTIVITY OF A DC-SIGN GLYCOMIMETIC  
JRNL        TITL 2 LIGAND BY FRAGMENT-BASED DESIGN: STRUCTURAL BASIS.           
JRNL        REF    CHEMISTRY                     V.  25 14659 2019              
JRNL        REFN                   ISSN 0947-6539                               
JRNL        PMID   31469191                                                     
JRNL        DOI    10.1002/CHEM.201903391                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0218                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 62185                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3261                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4508                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 235                          
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6444                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 344                                     
REMARK   3   SOLVENT ATOMS            : 660                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.77                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.48000                                              
REMARK   3    B22 (A**2) : -2.31000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.55000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.856         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7139 ; 0.017 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  5793 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9737 ; 1.625 ; 1.932       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13637 ; 1.113 ; 3.019       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   829 ; 6.758 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   386 ;36.877 ;25.466       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1072 ;13.447 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;21.049 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   938 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7977 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1579 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3214 ; 2.538 ; 3.251       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3213 ; 2.534 ; 3.249       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4017 ; 3.727 ; 4.847       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4018 ; 3.727 ; 4.849       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3925 ; 2.901 ; 3.477       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3926 ; 2.901 ; 3.476       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5701 ; 4.379 ; 5.104       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  8791 ; 6.114 ;37.375       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  8707 ; 6.059 ;37.159       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6GHV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009734.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-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               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 20180126                       
REMARK 200  DATA SCALING SOFTWARE          : XSCALE 20180126                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65455                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.087                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.4700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.81                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.010                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 11.6.02                                        
REMARK 200 STARTING MODEL: 1K9I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200MM MG(NO3)2, 100MM      
REMARK 280  MES PH6. PROTEIN SAMPLE: 150MM NACL, 4MM CACL2, 25MM TRIS PH8, 2%   
REMARK 280  DMSO, 3.25 MM LIGAND AND 5.54MG/ML PROTEIN., VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       28.75350            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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     GLU A   250                                                      
REMARK 465     ARG A   251                                                      
REMARK 465     LEU A   252                                                      
REMARK 465     SER A   385                                                      
REMARK 465     ARG A   386                                                      
REMARK 465     ASP A   387                                                      
REMARK 465     GLU A   388                                                      
REMARK 465     GLU A   389                                                      
REMARK 465     GLN A   390                                                      
REMARK 465     PHE A   391                                                      
REMARK 465     LEU A   392                                                      
REMARK 465     SER A   393                                                      
REMARK 465     PRO A   394                                                      
REMARK 465     ALA A   395                                                      
REMARK 465     PRO A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     THR A   398                                                      
REMARK 465     PRO A   399                                                      
REMARK 465     ASN A   400                                                      
REMARK 465     PRO A   401                                                      
REMARK 465     PRO A   402                                                      
REMARK 465     PRO A   403                                                      
REMARK 465     ALA A   404                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     ARG B   251                                                      
REMARK 465     LEU B   252                                                      
REMARK 465     SER B   385                                                      
REMARK 465     ARG B   386                                                      
REMARK 465     ASP B   387                                                      
REMARK 465     GLU B   388                                                      
REMARK 465     GLU B   389                                                      
REMARK 465     GLN B   390                                                      
REMARK 465     PHE B   391                                                      
REMARK 465     LEU B   392                                                      
REMARK 465     SER B   393                                                      
REMARK 465     PRO B   394                                                      
REMARK 465     ALA B   395                                                      
REMARK 465     PRO B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     THR B   398                                                      
REMARK 465     PRO B   399                                                      
REMARK 465     ASN B   400                                                      
REMARK 465     PRO B   401                                                      
REMARK 465     PRO B   402                                                      
REMARK 465     PRO B   403                                                      
REMARK 465     ALA B   404                                                      
REMARK 465     GLU C   250                                                      
REMARK 465     ARG C   251                                                      
REMARK 465     SER C   385                                                      
REMARK 465     ARG C   386                                                      
REMARK 465     ASP C   387                                                      
REMARK 465     GLU C   388                                                      
REMARK 465     GLU C   389                                                      
REMARK 465     GLN C   390                                                      
REMARK 465     PHE C   391                                                      
REMARK 465     LEU C   392                                                      
REMARK 465     SER C   393                                                      
REMARK 465     PRO C   394                                                      
REMARK 465     ALA C   395                                                      
REMARK 465     PRO C   396                                                      
REMARK 465     ALA C   397                                                      
REMARK 465     THR C   398                                                      
REMARK 465     PRO C   399                                                      
REMARK 465     ASN C   400                                                      
REMARK 465     PRO C   401                                                      
REMARK 465     PRO C   402                                                      
REMARK 465     PRO C   403                                                      
REMARK 465     ALA C   404                                                      
REMARK 465     GLU D   250                                                      
REMARK 465     ARG D   251                                                      
REMARK 465     SER D   385                                                      
REMARK 465     ARG D   386                                                      
REMARK 465     ASP D   387                                                      
REMARK 465     GLU D   388                                                      
REMARK 465     GLU D   389                                                      
REMARK 465     GLN D   390                                                      
REMARK 465     PHE D   391                                                      
REMARK 465     LEU D   392                                                      
REMARK 465     SER D   393                                                      
REMARK 465     PRO D   394                                                      
REMARK 465     ALA D   395                                                      
REMARK 465     PRO D   396                                                      
REMARK 465     ALA D   397                                                      
REMARK 465     THR D   398                                                      
REMARK 465     PRO D   399                                                      
REMARK 465     ASN D   400                                                      
REMARK 465     PRO D   401                                                      
REMARK 465     PRO D   402                                                      
REMARK 465     PRO D   403                                                      
REMARK 465     ALA D   404                                                      
REMARK 465     GLU E   250                                                      
REMARK 465     ARG E   251                                                      
REMARK 465     SER E   385                                                      
REMARK 465     ARG E   386                                                      
REMARK 465     ASP E   387                                                      
REMARK 465     GLU E   388                                                      
REMARK 465     GLU E   389                                                      
REMARK 465     GLN E   390                                                      
REMARK 465     PHE E   391                                                      
REMARK 465     LEU E   392                                                      
REMARK 465     SER E   393                                                      
REMARK 465     PRO E   394                                                      
REMARK 465     ALA E   395                                                      
REMARK 465     PRO E   396                                                      
REMARK 465     ALA E   397                                                      
REMARK 465     THR E   398                                                      
REMARK 465     PRO E   399                                                      
REMARK 465     ASN E   400                                                      
REMARK 465     PRO E   401                                                      
REMARK 465     PRO E   402                                                      
REMARK 465     PRO E   403                                                      
REMARK 465     ALA E   404                                                      
REMARK 465     GLU F   250                                                      
REMARK 465     ARG F   251                                                      
REMARK 465     LEU F   252                                                      
REMARK 465     SER F   385                                                      
REMARK 465     ARG F   386                                                      
REMARK 465     ASP F   387                                                      
REMARK 465     GLU F   388                                                      
REMARK 465     GLU F   389                                                      
REMARK 465     GLN F   390                                                      
REMARK 465     PHE F   391                                                      
REMARK 465     LEU F   392                                                      
REMARK 465     SER F   393                                                      
REMARK 465     PRO F   394                                                      
REMARK 465     ALA F   395                                                      
REMARK 465     PRO F   396                                                      
REMARK 465     ALA F   397                                                      
REMARK 465     THR F   398                                                      
REMARK 465     PRO F   399                                                      
REMARK 465     ASN F   400                                                      
REMARK 465     PRO F   401                                                      
REMARK 465     PRO F   402                                                      
REMARK 465     PRO F   403                                                      
REMARK 465     ALA F   404                                                      
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    GLU A 259       -9.19     88.08                                   
REMARK 500    GLU A 353       95.07     63.86                                   
REMARK 500    GLU B 259      -10.31     87.58                                   
REMARK 500    GLN B 264       52.45     38.98                                   
REMARK 500    GLU B 353       97.74     76.19                                   
REMARK 500    GLU C 259      -14.16     82.94                                   
REMARK 500    GLU C 353       92.18     70.67                                   
REMARK 500    GLU D 259      -12.06     89.61                                   
REMARK 500    ASN D 311       47.70     34.04                                   
REMARK 500    GLU D 353       95.22     75.04                                   
REMARK 500    GLU E 259       -9.01     84.19                                   
REMARK 500    GLN E 264       53.29     32.95                                   
REMARK 500    GLU E 353      101.18     63.51                                   
REMARK 500    GLU F 259      -15.11     90.44                                   
REMARK 500    GLU F 353      105.04     79.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1195        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH B1225        DISTANCE =  7.06 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 320   OD1                                                    
REMARK 620 2 ASP A 320   OD2  51.3                                              
REMARK 620 3 GLU A 324   OE1  90.9  82.8                                        
REMARK 620 4 GLU A 324   OE2 116.4  71.6  53.0                                  
REMARK 620 5 ASN A 350   OD1 158.3 147.8  84.3  77.1                            
REMARK 620 6 GLU A 354   O    95.6 122.9 150.9 142.6  79.2                      
REMARK 620 7 ASP A 355   OD1  72.6 119.0  75.4 126.5  85.8  79.6                
REMARK 620 8 HOH A1129   O   111.2  79.1 131.1  78.2  87.4  72.2 151.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 347   OE1                                                    
REMARK 620 2 ASN A 349   OD1  71.4                                              
REMARK 620 3 GLU A 354   OE1 139.3  68.6                                        
REMARK 620 4 ASN A 365   OD1  70.6 141.1 150.1                                  
REMARK 620 5 ASP A 366   O   138.2 136.7  73.5  79.8                            
REMARK 620 6 ASP A 366   OD1  76.4  84.8  92.8  94.1  77.0                      
REMARK 620 7 EZ8 A1001   O4   72.9  75.8 103.6  85.5 134.3 147.6                
REMARK 620 8 EZ8 A1001   O3  129.5 118.7  78.0  80.8  71.0 148.0  63.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 355   OD2                                                    
REMARK 620 2 HOH A1102   O    84.1                                              
REMARK 620 3 HOH A1118   O    76.9  85.0                                        
REMARK 620 4 HOH A1139   O    89.1 166.2  81.7                                  
REMARK 620 5 HOH D 607   O    95.1  96.7 171.6  95.9                            
REMARK 620 6 HOH D 695   O   167.8  88.1  93.2  96.4  95.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 320   OD1                                                    
REMARK 620 2 ASP B 320   OD2  53.7                                              
REMARK 620 3 GLU B 324   OE1  99.5  79.7                                        
REMARK 620 4 GLU B 324   OE2 121.2  70.7  49.0                                  
REMARK 620 5 ASN B 350   OD1 159.5 142.2  76.6  71.5                            
REMARK 620 6 GLU B 354   O    93.8 134.5 142.6 143.0  78.8                      
REMARK 620 7 ASP B 355   OD1  75.9 116.7  73.0 120.3  83.8  76.7                
REMARK 620 8 HOH B1133   O   106.1  80.6 128.4  79.5  91.5  79.7 156.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 347   OE1                                                    
REMARK 620 2 ASN B 349   OD1  68.1                                              
REMARK 620 3 GLU B 354   OE1 141.7  75.6                                        
REMARK 620 4 ASN B 365   OD1  72.5 140.1 144.2                                  
REMARK 620 5 ASP B 366   O   130.5 140.5  73.8  72.9                            
REMARK 620 6 ASP B 366   OD1  71.3  82.9  93.1  90.3  74.6                      
REMARK 620 7 EZ8 B1001   O4   74.1  76.6 109.3  87.3 137.4 144.3                
REMARK 620 8 EZ8 B1001   O3  133.2 123.9  77.8  80.2  72.4 147.1  67.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 355   OD2                                                    
REMARK 620 2 HOH B1108   O    92.4                                              
REMARK 620 3 HOH B1126   O    86.9  83.0                                        
REMARK 620 4 HOH B1148   O    90.6  93.7 175.8                                  
REMARK 620 5 HOH B1155   O    85.0 174.6  92.1  91.1                            
REMARK 620 6 HOH B1212   O   165.6  99.4  86.4  96.7  82.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 320   OD1                                                    
REMARK 620 2 ASP C 320   OD2  51.7                                              
REMARK 620 3 GLU C 324   OE1  93.0  80.5                                        
REMARK 620 4 GLU C 324   OE2 116.4  71.1  48.2                                  
REMARK 620 5 ASN C 350   OD1 156.9 149.8  86.1  79.8                            
REMARK 620 6 GLU C 354   O    91.0 123.2 151.3 148.7  79.2                      
REMARK 620 7 ASP C 355   OD1  72.3 118.9  80.1 126.5  84.8  74.2                
REMARK 620 8 HOH C1121   O   108.5  81.7 133.4  85.3  88.3  71.1 145.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 347   OE1                                                    
REMARK 620 2 ASN C 349   OD1  72.6                                              
REMARK 620 3 GLU C 354   OE1 140.4  68.8                                        
REMARK 620 4 ASN C 365   OD1  68.3 140.6 150.6                                  
REMARK 620 5 ASP C 366   O   136.5 129.4  68.7  84.5                            
REMARK 620 6 ASP C 366   OD1  73.8  81.6  92.0  92.0  73.8                      
REMARK 620 7 EZ8 C1001   O4   71.4  78.6 108.4  84.6 141.1 143.7                
REMARK 620 8 EZ8 C1001   O3  131.9 120.8  77.6  83.8  74.1 148.0  67.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 355   OD2                                                    
REMARK 620 2 HOH C1112   O   104.4                                              
REMARK 620 3 HOH C1126   O    87.9  90.1                                        
REMARK 620 4 HOH C1128   O    91.1  95.3 174.6                                  
REMARK 620 5 HOH C1130   O    83.1 169.8  97.1  77.5                            
REMARK 620 6 HOH C1221   O   164.0  90.9  96.9  82.8  81.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 320   OD1                                                    
REMARK 620 2 ASP D 320   OD2  51.6                                              
REMARK 620 3 GLU D 324   OE1  94.9  78.7                                        
REMARK 620 4 GLU D 324   OE2 119.4  70.7  52.9                                  
REMARK 620 5 ASN D 350   OD1 156.3 149.0  83.5  78.3                            
REMARK 620 6 GLU D 354   O    91.5 129.1 146.3 145.3  77.8                      
REMARK 620 7 ASP D 355   OD1  71.8 112.9  72.8 124.4  85.3  78.0                
REMARK 620 8 HOH D 623   O   106.2  84.8 135.9  83.1  90.7  72.5 150.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 347   OE1                                                    
REMARK 620 2 ASN D 349   OD1  74.3                                              
REMARK 620 3 GLU D 354   OE1 150.7  76.4                                        
REMARK 620 4 ASN D 365   OD1  65.8 140.1 143.5                                  
REMARK 620 5 ASP D 366   O   131.6 140.2  73.0  74.1                            
REMARK 620 6 ASP D 366   OD1  74.7  84.2 100.8  86.8  77.2                      
REMARK 620 7 EZ8 D 502   O4   66.0  78.5 109.6  84.0 136.0 140.0                
REMARK 620 8 EZ8 D 502   O3  123.6 126.6  76.4  77.6  69.4 145.8  68.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 355   OD2                                                    
REMARK 620 2 HOH D 610   O    84.7                                              
REMARK 620 3 HOH D 617   O    88.7  94.1                                        
REMARK 620 4 HOH D 622   O    73.5  83.6 162.2                                  
REMARK 620 5 HOH D 649   O    83.7 168.3  86.6  92.2                            
REMARK 620 6 HOH D 697   O   161.8  92.0 109.3  88.4  98.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 320   OD1                                                    
REMARK 620 2 ASP E 320   OD2  50.4                                              
REMARK 620 3 GLU E 324   OE1  92.9  82.9                                        
REMARK 620 4 GLU E 324   OE2 111.5  66.5  52.2                                  
REMARK 620 5 ASN E 350   OD1 164.0 143.2  82.8  78.0                            
REMARK 620 6 GLU E 354   O    94.8 121.5 153.0 144.5  82.6                      
REMARK 620 7 ASP E 355   OD1  71.9 116.6  75.4 127.4  92.1  82.5                
REMARK 620 8 HOH E 638   O   106.8  72.5 124.3  72.0  88.2  77.9 160.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 347   OE1                                                    
REMARK 620 2 ASN E 349   OD1  70.9                                              
REMARK 620 3 GLU E 354   OE1 137.9  67.9                                        
REMARK 620 4 ASN E 365   OD1  74.7 145.5 145.6                                  
REMARK 620 5 ASP E 366   O   138.5 132.8  71.3  75.2                            
REMARK 620 6 ASP E 366   OD1  77.3  81.8  88.9  89.5  74.6                      
REMARK 620 7 EZ8 E 503   O4   71.2  83.1 111.1  87.2 134.4 148.0                
REMARK 620 8 EZ8 E 503   O3  132.6 119.7  77.3  85.2  71.5 146.0  65.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 355   OD1                                                    
REMARK 620 2 ASP E 355   OD2  47.8                                              
REMARK 620 3 HOH E 608   O    71.0  98.0                                        
REMARK 620 4 HOH E 613   O   113.8  72.1 153.9                                  
REMARK 620 5 HOH E 622   O   106.2  76.2  75.3  78.8                            
REMARK 620 6 HOH E 629   O    62.3  95.4  98.5 106.4 168.5                      
REMARK 620 7 HOH E 707   O   152.3 158.2  88.7  92.9  85.7 104.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E 614   O                                                      
REMARK 620 2 HOH E 616   O    77.5                                              
REMARK 620 3 ASP F 355   OD2  88.1  83.1                                        
REMARK 620 4 HOH F 604   O   158.7  82.6  82.2                                  
REMARK 620 5 HOH F 605   O    96.1 172.9  93.6 103.3                            
REMARK 620 6 HOH F 693   O    96.5  80.5 161.5  87.4 103.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 320   OD1                                                    
REMARK 620 2 ASP F 320   OD2  49.9                                              
REMARK 620 3 GLU F 324   OE1  94.3  76.5                                        
REMARK 620 4 GLU F 324   OE2 114.4  66.8  51.3                                  
REMARK 620 5 ASN F 350   OD1 161.4 141.0  78.1  74.2                            
REMARK 620 6 GLU F 354   O    98.5 133.4 147.6 142.1  80.4                      
REMARK 620 7 ASP F 355   OD1  76.5 115.7  74.9 124.9  85.1  79.3                
REMARK 620 8 HOH F 618   O   109.0  84.4 128.4  77.1  88.7  74.7 154.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 347   OE1                                                    
REMARK 620 2 ASN F 349   OD1  74.6                                              
REMARK 620 3 GLU F 354   OE1 148.1  75.6                                        
REMARK 620 4 ASN F 365   OD1  69.6 144.2 138.8                                  
REMARK 620 5 ASP F 366   O   129.5 136.9  69.4  70.4                            
REMARK 620 6 ASP F 366   OD1  74.6  81.3  89.8  88.0  74.5                      
REMARK 620 7 EZ8 F 502   O4   75.6  79.1 109.6  93.1 135.9 147.7                
REMARK 620 8 EZ8 F 502   O3  134.0 123.5  73.5  84.2  69.2 143.3  68.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 E 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 F 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 506                  
DBREF  6GHV A  250   404  UNP    Q9NNX6   CD209_HUMAN    250    404             
DBREF  6GHV B  250   404  UNP    Q9NNX6   CD209_HUMAN    250    404             
DBREF  6GHV C  250   404  UNP    Q9NNX6   CD209_HUMAN    250    404             
DBREF  6GHV D  250   404  UNP    Q9NNX6   CD209_HUMAN    250    404             
DBREF  6GHV E  250   404  UNP    Q9NNX6   CD209_HUMAN    250    404             
DBREF  6GHV F  250   404  UNP    Q9NNX6   CD209_HUMAN    250    404             
SEQRES   1 A  155  GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE          
SEQRES   2 A  155  PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG          
SEQRES   3 A  155  ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY          
SEQRES   4 A  155  ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN          
SEQRES   5 A  155  PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR          
SEQRES   6 A  155  TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP          
SEQRES   7 A  155  GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS          
SEQRES   8 A  155  GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU          
SEQRES   9 A  155  GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP          
SEQRES  10 A  155  ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS          
SEQRES  11 A  155  SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU          
SEQRES  12 A  155  SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA              
SEQRES   1 B  155  GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE          
SEQRES   2 B  155  PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG          
SEQRES   3 B  155  ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY          
SEQRES   4 B  155  ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN          
SEQRES   5 B  155  PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR          
SEQRES   6 B  155  TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP          
SEQRES   7 B  155  GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS          
SEQRES   8 B  155  GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU          
SEQRES   9 B  155  GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP          
SEQRES  10 B  155  ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS          
SEQRES  11 B  155  SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU          
SEQRES  12 B  155  SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA              
SEQRES   1 C  155  GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE          
SEQRES   2 C  155  PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG          
SEQRES   3 C  155  ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY          
SEQRES   4 C  155  ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN          
SEQRES   5 C  155  PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR          
SEQRES   6 C  155  TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP          
SEQRES   7 C  155  GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS          
SEQRES   8 C  155  GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU          
SEQRES   9 C  155  GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP          
SEQRES  10 C  155  ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS          
SEQRES  11 C  155  SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU          
SEQRES  12 C  155  SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA              
SEQRES   1 D  155  GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE          
SEQRES   2 D  155  PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG          
SEQRES   3 D  155  ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY          
SEQRES   4 D  155  ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN          
SEQRES   5 D  155  PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR          
SEQRES   6 D  155  TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP          
SEQRES   7 D  155  GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS          
SEQRES   8 D  155  GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU          
SEQRES   9 D  155  GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP          
SEQRES  10 D  155  ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS          
SEQRES  11 D  155  SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU          
SEQRES  12 D  155  SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA              
SEQRES   1 E  155  GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE          
SEQRES   2 E  155  PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG          
SEQRES   3 E  155  ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY          
SEQRES   4 E  155  ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN          
SEQRES   5 E  155  PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR          
SEQRES   6 E  155  TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP          
SEQRES   7 E  155  GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS          
SEQRES   8 E  155  GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU          
SEQRES   9 E  155  GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP          
SEQRES  10 E  155  ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS          
SEQRES  11 E  155  SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU          
SEQRES  12 E  155  SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA              
SEQRES   1 F  155  GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE          
SEQRES   2 F  155  PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG          
SEQRES   3 F  155  ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY          
SEQRES   4 F  155  ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN          
SEQRES   5 F  155  PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR          
SEQRES   6 F  155  TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP          
SEQRES   7 F  155  GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS          
SEQRES   8 F  155  GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU          
SEQRES   9 F  155  GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP          
SEQRES  10 F  155  ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS          
SEQRES  11 F  155  SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU          
SEQRES  12 F  155  SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA              
HET    EZ8  A1001      52                                                       
HET     CA  A1002       1                                                       
HET     CA  A1003       1                                                       
HET     CA  A1004       1                                                       
HET     CL  A1005       1                                                       
HET     CL  A1006       1                                                       
HET     CL  A1007       1                                                       
HET    EZ8  B1001      52                                                       
HET     CA  B1002       1                                                       
HET     CA  B1003       1                                                       
HET     CA  B1004       1                                                       
HET     CL  B1005       1                                                       
HET     CL  B1006       1                                                       
HET    EZ8  C1001      52                                                       
HET     CA  C1002       1                                                       
HET     CA  C1003       1                                                       
HET     CA  C1004       1                                                       
HET     CL  C1005       1                                                       
HET     CL  C1006       1                                                       
HET     CL  D 501       1                                                       
HET    EZ8  D 502      52                                                       
HET     CA  D 503       1                                                       
HET     CA  D 504       1                                                       
HET     CA  D 505       1                                                       
HET     CL  D 506       1                                                       
HET     CL  E 501       1                                                       
HET     CL  E 502       1                                                       
HET    EZ8  E 503      52                                                       
HET     CA  E 504       1                                                       
HET     CA  E 505       1                                                       
HET     CA  E 506       1                                                       
HET     CL  E 507       1                                                       
HET     CL  F 501       1                                                       
HET    EZ8  F 502      52                                                       
HET     CA  F 503       1                                                       
HET     CA  F 504       1                                                       
HET     CA  F 505       1                                                       
HET     CL  F 506       1                                                       
HETNAM     EZ8 [1-[(2~{S},3~{S},4~{R},5~{S},6~{R})-2-[(1~{S},2~{S},             
HETNAM   2 EZ8  4~{S},5~{S})-2-(2-CHLOROETHYLOXY)-4,5-BIS[[4-                   
HETNAM   3 EZ8  (HYDROXYMETHYL)PHENYL]METHYLCARBAMOYL]CYCLOHEXYL]OXY-           
HETNAM   4 EZ8  6-(HYDROXYMETHYL)-4,5-BIS(OXIDANYL)OXAN-3-YL]-1,2,3-            
HETNAM   5 EZ8  TRIAZOL-4-YL]METHYLAZANIUM                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   7  EZ8    6(C35 H48 CL N6 O10 1+)                                      
FORMUL   8   CA    18(CA 2+)                                                    
FORMUL  11   CL    14(CL 1-)                                                    
FORMUL  45  HOH   *660(H2 O)                                                    
HELIX    1   1 ASN B  276  VAL B  287  1                                  12
HELIX    2   2 SER B  296  ASN B  311  1                                  16
HELIX    3   3 LEU B  336  TRP B  343  1                                   8
HELIX    4   4 ASN C  276  VAL C  287  1                                  12
HELIX    5   5 SER C  296  ASN C  311  1                                  16
HELIX    6   6 LEU C  336  TRP C  343  1                                   8
SHEET    1   1 1 THR B 261  PHE B 263  0
SHEET    2   2 1 ASN B 266  MET B 270  0
SHEET    3   3 1 GLN B 290  LEU B 291  0
SHEET    4   4 1 THR B 314  SER B 319  0
SHEET    5   5 1 GLN B 328  TRP B 329  0
SHEET    6   6 1 CYS B 356  SER B 360  0
SHEET    7   7 1 GLY B 363  ASP B 367  0
SHEET    8   8 1 PHE B 374  SER B 380  0
SHEET    9   9 1 THR C 261  PHE C 263  0
SHEET   10  10 1 ASN C 266  MET C 270  0
SHEET   11  11 1 GLN C 290  LEU C 291  0
SHEET   12  12 1 THR C 314  GLN C 323  0
SHEET   13  13 1 THR C 326  TRP C 329  0
SHEET   14  14 1 CYS C 356  SER C 360  0
SHEET   15  15 1 GLY C 363  ASP C 367  0
SHEET   16  16 1 PHE C 374  SER C 380  0
SSBOND   1 CYS A  253    CYS A  384                          1555   1555  2.06  
SSBOND   2 CYS A  256    CYS A  267                          1555   1555  2.07  
SSBOND   3 CYS A  284    CYS A  377                          1555   1555  2.06  
SSBOND   4 CYS A  356    CYS A  369                          1555   1555  2.10  
SSBOND   5 CYS B  253    CYS B  384                          1555   1555  2.05  
SSBOND   6 CYS B  256    CYS B  267                          1555   1555  2.06  
SSBOND   7 CYS B  284    CYS B  377                          1555   1555  2.08  
SSBOND   8 CYS B  356    CYS B  369                          1555   1555  2.05  
SSBOND   9 CYS C  253    CYS C  384                          1555   1555  2.04  
SSBOND  10 CYS C  256    CYS C  267                          1555   1555  2.07  
SSBOND  11 CYS C  284    CYS C  377                          1555   1555  2.09  
SSBOND  12 CYS C  356    CYS C  369                          1555   1555  2.00  
SSBOND  13 CYS D  253    CYS D  384                          1555   1555  2.03  
SSBOND  14 CYS D  256    CYS D  267                          1555   1555  2.06  
SSBOND  15 CYS D  284    CYS D  377                          1555   1555  2.06  
SSBOND  16 CYS D  356    CYS D  369                          1555   1555  2.06  
SSBOND  17 CYS E  253    CYS E  384                          1555   1555  2.05  
SSBOND  18 CYS E  256    CYS E  267                          1555   1555  2.07  
SSBOND  19 CYS E  284    CYS E  377                          1555   1555  2.09  
SSBOND  20 CYS E  356    CYS E  369                          1555   1555  2.04  
SSBOND  21 CYS F  253    CYS F  384                          1555   1555  2.05  
SSBOND  22 CYS F  256    CYS F  267                          1555   1555  2.06  
SSBOND  23 CYS F  284    CYS F  377                          1555   1555  2.08  
SSBOND  24 CYS F  356    CYS F  369                          1555   1555  2.04  
LINK         OD1 ASP A 320                CA    CA A1003     1555   1555  2.53  
LINK         OD2 ASP A 320                CA    CA A1003     1555   1555  2.52  
LINK         OE1 GLU A 324                CA    CA A1003     1555   1555  2.38  
LINK         OE2 GLU A 324                CA    CA A1003     1555   1555  2.55  
LINK         OE1 GLU A 347                CA    CA A1002     1555   1555  2.40  
LINK         OD1 ASN A 349                CA    CA A1002     1555   1555  2.48  
LINK         OD1 ASN A 350                CA    CA A1003     1555   1555  2.54  
LINK         OE1 GLU A 354                CA    CA A1002     1555   1555  2.41  
LINK         O   GLU A 354                CA    CA A1003     1555   1555  2.54  
LINK         OD1 ASP A 355                CA    CA A1003     1555   1555  2.20  
LINK         OD2 ASP A 355                CA    CA A1004     1555   1555  2.21  
LINK         OD1 ASN A 365                CA    CA A1002     1555   1555  2.40  
LINK         O   ASP A 366                CA    CA A1002     1555   1555  2.43  
LINK         OD1 ASP A 366                CA    CA A1002     1555   1555  2.21  
LINK         O4  EZ8 A1001                CA    CA A1002     1555   1555  2.65  
LINK         O3  EZ8 A1001                CA    CA A1002     1555   1555  2.57  
LINK        CA    CA A1003                 O   HOH A1129     1555   1555  2.08  
LINK        CA    CA A1004                 O   HOH A1102     1555   1555  2.25  
LINK        CA    CA A1004                 O   HOH A1118     1555   1555  2.21  
LINK        CA    CA A1004                 O   HOH A1139     1555   1555  1.92  
LINK        CA    CA A1004                 O   HOH D 607     1555   2555  2.05  
LINK        CA    CA A1004                 O   HOH D 695     1555   2555  2.12  
LINK         OD1 ASP B 320                CA    CA B1003     1555   1555  2.50  
LINK         OD2 ASP B 320                CA    CA B1003     1555   1555  2.44  
LINK         OE1 GLU B 324                CA    CA B1003     1555   1555  2.56  
LINK         OE2 GLU B 324                CA    CA B1003     1555   1555  2.75  
LINK         OE1 GLU B 347                CA    CA B1002     1555   1555  2.51  
LINK         OD1 ASN B 349                CA    CA B1002     1555   1555  2.39  
LINK         OD1 ASN B 350                CA    CA B1003     1555   1555  2.59  
LINK         OE1 GLU B 354                CA    CA B1002     1555   1555  2.22  
LINK         O   GLU B 354                CA    CA B1003     1555   1555  2.30  
LINK         OD1 ASP B 355                CA    CA B1003     1555   1555  2.30  
LINK         OD2 ASP B 355                CA    CA B1004     1555   1555  2.09  
LINK         OD1 ASN B 365                CA    CA B1002     1555   1555  2.51  
LINK         O   ASP B 366                CA    CA B1002     1555   1555  2.53  
LINK         OD1 ASP B 366                CA    CA B1002     1555   1555  2.31  
LINK         O4  EZ8 B1001                CA    CA B1002     1555   1555  2.51  
LINK         O3  EZ8 B1001                CA    CA B1002     1555   1555  2.56  
LINK        CA    CA B1003                 O   HOH B1133     1555   1555  2.43  
LINK        CA    CA B1004                 O   HOH B1108     1555   1555  2.24  
LINK        CA    CA B1004                 O   HOH B1126     1555   1555  2.33  
LINK        CA    CA B1004                 O   HOH B1148     1555   1555  2.09  
LINK        CA    CA B1004                 O   HOH B1155     1555   1555  2.24  
LINK        CA    CA B1004                 O   HOH B1212     1555   1555  2.12  
LINK         OD1 ASP C 320                CA    CA C1003     1555   1555  2.54  
LINK         OD2 ASP C 320                CA    CA C1003     1555   1555  2.54  
LINK         OE1 GLU C 324                CA    CA C1003     1555   1555  2.52  
LINK         OE2 GLU C 324                CA    CA C1003     1555   1555  2.85  
LINK         OE1 GLU C 347                CA    CA C1002     1555   1555  2.54  
LINK         OD1 ASN C 349                CA    CA C1002     1555   1555  2.65  
LINK         OD1 ASN C 350                CA    CA C1003     1555   1555  2.49  
LINK         OE1 GLU C 354                CA    CA C1002     1555   1555  2.30  
LINK         O   GLU C 354                CA    CA C1003     1555   1555  2.46  
LINK         OD1 ASP C 355                CA    CA C1003     1555   1555  2.40  
LINK         OD2 ASP C 355                CA    CA C1004     1555   1555  2.05  
LINK         OD1 ASN C 365                CA    CA C1002     1555   1555  2.35  
LINK         O   ASP C 366                CA    CA C1002     1555   1555  2.37  
LINK         OD1 ASP C 366                CA    CA C1002     1555   1555  2.45  
LINK         O4  EZ8 C1001                CA    CA C1002     1555   1555  2.53  
LINK         O3  EZ8 C1001                CA    CA C1002     1555   1555  2.48  
LINK        CA    CA C1003                 O   HOH C1121     1555   1555  2.18  
LINK        CA    CA C1004                 O   HOH C1112     1555   1555  2.01  
LINK        CA    CA C1004                 O   HOH C1126     1555   1555  2.00  
LINK        CA    CA C1004                 O   HOH C1128     1555   1555  2.28  
LINK        CA    CA C1004                 O   HOH C1130     1555   1555  2.04  
LINK        CA    CA C1004                 O   HOH C1221     1555   1555  2.14  
LINK         OD1 ASP D 320                CA    CA D 504     1555   1555  2.62  
LINK         OD2 ASP D 320                CA    CA D 504     1555   1555  2.38  
LINK         OE1 GLU D 324                CA    CA D 504     1555   1555  2.40  
LINK         OE2 GLU D 324                CA    CA D 504     1555   1555  2.47  
LINK         OE1 GLU D 347                CA    CA D 503     1555   1555  2.46  
LINK         OD1 ASN D 349                CA    CA D 503     1555   1555  2.49  
LINK         OD1 ASN D 350                CA    CA D 504     1555   1555  2.42  
LINK         OE1 GLU D 354                CA    CA D 503     1555   1555  2.21  
LINK         O   GLU D 354                CA    CA D 504     1555   1555  2.39  
LINK         OD1 ASP D 355                CA    CA D 504     1555   1555  2.19  
LINK         OD2 ASP D 355                CA    CA D 505     1555   1555  2.38  
LINK         OD1 ASN D 365                CA    CA D 503     1555   1555  2.65  
LINK         O   ASP D 366                CA    CA D 503     1555   1555  2.49  
LINK         OD1 ASP D 366                CA    CA D 503     1555   1555  2.41  
LINK         O4  EZ8 D 502                CA    CA D 503     1555   1555  2.51  
LINK         O3  EZ8 D 502                CA    CA D 503     1555   1555  2.49  
LINK        CA    CA D 504                 O   HOH D 623     1555   1555  2.16  
LINK        CA    CA D 505                 O   HOH D 610     1555   1555  2.27  
LINK        CA    CA D 505                 O   HOH D 617     1555   1555  2.16  
LINK        CA    CA D 505                 O   HOH D 622     1555   1555  2.11  
LINK        CA    CA D 505                 O   HOH D 649     1555   1555  2.01  
LINK        CA    CA D 505                 O   HOH D 697     1555   1555  2.26  
LINK         OD1 ASP E 320                CA    CA E 505     1555   1555  2.54  
LINK         OD2 ASP E 320                CA    CA E 505     1555   1555  2.64  
LINK         OE1 GLU E 324                CA    CA E 505     1555   1555  2.48  
LINK         OE2 GLU E 324                CA    CA E 505     1555   1555  2.61  
LINK         OE1 GLU E 347                CA    CA E 504     1555   1555  2.40  
LINK         OD1 ASN E 349                CA    CA E 504     1555   1555  2.51  
LINK         OD1 ASN E 350                CA    CA E 505     1555   1555  2.52  
LINK         OE1 GLU E 354                CA    CA E 504     1555   1555  2.43  
LINK         O   GLU E 354                CA    CA E 505     1555   1555  2.45  
LINK         OD1 ASP E 355                CA    CA E 505     1555   1555  2.24  
LINK         OD1 ASP E 355                CA    CA E 506     1555   1555  2.99  
LINK         OD2 ASP E 355                CA    CA E 506     1555   1555  2.28  
LINK         OD1 ASN E 365                CA    CA E 504     1555   1555  2.35  
LINK         O   ASP E 366                CA    CA E 504     1555   1555  2.47  
LINK         OD1 ASP E 366                CA    CA E 504     1555   1555  2.41  
LINK         O4  EZ8 E 503                CA    CA E 504     1555   1555  2.59  
LINK         O3  EZ8 E 503                CA    CA E 504     1555   1555  2.56  
LINK        CA    CA E 505                 O   HOH E 638     1555   1555  2.03  
LINK        CA    CA E 506                 O   HOH E 608     1555   1555  2.04  
LINK        CA    CA E 506                 O   HOH E 613     1555   1555  2.09  
LINK        CA    CA E 506                 O   HOH E 622     1555   1555  2.31  
LINK        CA    CA E 506                 O   HOH E 629     1555   1555  2.03  
LINK        CA    CA E 506                 O   HOH E 707     1555   1555  2.16  
LINK         O   HOH E 614                CA    CA F 505     2657   1555  2.13  
LINK         O   HOH E 616                CA    CA F 505     2657   1555  2.09  
LINK         OD1 ASP F 320                CA    CA F 504     1555   1555  2.42  
LINK         OD2 ASP F 320                CA    CA F 504     1555   1555  2.64  
LINK         OE1 GLU F 324                CA    CA F 504     1555   1555  2.51  
LINK         OE2 GLU F 324                CA    CA F 504     1555   1555  2.65  
LINK         OE1 GLU F 347                CA    CA F 503     1555   1555  2.32  
LINK         OD1 ASN F 349                CA    CA F 503     1555   1555  2.43  
LINK         OD1 ASN F 350                CA    CA F 504     1555   1555  2.37  
LINK         OE1 GLU F 354                CA    CA F 503     1555   1555  2.33  
LINK         O   GLU F 354                CA    CA F 504     1555   1555  2.35  
LINK         OD1 ASP F 355                CA    CA F 504     1555   1555  2.38  
LINK         OD2 ASP F 355                CA    CA F 505     1555   1555  2.20  
LINK         OD1 ASN F 365                CA    CA F 503     1555   1555  2.36  
LINK         O   ASP F 366                CA    CA F 503     1555   1555  2.45  
LINK         OD1 ASP F 366                CA    CA F 503     1555   1555  2.36  
LINK         O4  EZ8 F 502                CA    CA F 503     1555   1555  2.51  
LINK         O3  EZ8 F 502                CA    CA F 503     1555   1555  2.45  
LINK        CA    CA F 504                 O   HOH F 618     1555   1555  2.33  
LINK        CA    CA F 505                 O   HOH F 604     1555   1555  2.06  
LINK        CA    CA F 505                 O   HOH F 605     1555   1555  2.02  
LINK        CA    CA F 505                 O   HOH F 693     1555   1555  2.29  
CISPEP   1 GLU A  347    PRO A  348          0         2.28                     
CISPEP   2 GLU B  347    PRO B  348          0       -11.02                     
CISPEP   3 GLU C  347    PRO C  348          0         4.23                     
CISPEP   4 GLU D  347    PRO D  348          0        -3.43                     
CISPEP   5 GLU E  347    PRO E  348          0        -6.96                     
CISPEP   6 GLU F  347    PRO F  348          0        -6.57                     
SITE     1 AC1 21 PHE A 313  GLU A 347  ASN A 349  GLY A 352                    
SITE     2 AC1 21 GLU A 354  GLU A 358  SER A 360  ASN A 365                    
SITE     3 AC1 21 ASP A 366  ASP A 367  LYS A 368   CA A1002                    
SITE     4 AC1 21 HOH A1108  HOH A1113  ASN D 272  ARG D 309                    
SITE     5 AC1 21 SER D 310  ASN D 311  ARG D 312  THR D 314                    
SITE     6 AC1 21  CL D 501                                                     
SITE     1 AC2  6 GLU A 347  ASN A 349  GLU A 354  ASN A 365                    
SITE     2 AC2  6 ASP A 366  EZ8 A1001                                          
SITE     1 AC3  6 ASP A 320  GLU A 324  ASN A 350  GLU A 354                    
SITE     2 AC3  6 ASP A 355  HOH A1129                                          
SITE     1 AC4  4 ASP A 355  HOH A1102  HOH A1118  HOH A1139                    
SITE     1 AC5  2 ASN A 272  SER A 273                                          
SITE     1 AC6  1 ARG A 309                                                     
SITE     1 AC7  2 GLN A 264  EZ8 B1001                                          
SITE     1 AC8 29 GLN A 264  GLY A 265   CL A1007  PHE B 313                    
SITE     2 AC8 29 GLU B 347  ASN B 349  VAL B 351  GLY B 352                    
SITE     3 AC8 29 GLU B 354  GLU B 358  SER B 360  ASN B 365                    
SITE     4 AC8 29 ASP B 366  ASP B 367  LYS B 368   CA B1002                    
SITE     5 AC8 29 HOH B1105  HOH B1111  HOH B1116  HOH B1151                    
SITE     6 AC8 29 ASN C 272  GLN C 306  ARG C 309  SER C 310                    
SITE     7 AC8 29 ASN C 311  ARG C 312  THR C 314  PHE C 374                    
SITE     8 AC8 29 HOH C1139                                                     
SITE     1 AC9  6 GLU B 347  ASN B 349  GLU B 354  ASN B 365                    
SITE     2 AC9  6 ASP B 366  EZ8 B1001                                          
SITE     1 AD1  6 ASP B 320  GLU B 324  ASN B 350  GLU B 354                    
SITE     2 AD1  6 ASP B 355  HOH B1133                                          
SITE     1 AD2  6 ASP B 355  HOH B1108  HOH B1126  HOH B1148                    
SITE     2 AD2  6 HOH B1155  HOH B1212                                          
SITE     1 AD3  1 SER B 273                                                     
SITE     1 AD4  2 GLN B 264  EZ8 F 502                                          
SITE     1 AD5 28 ASN B 272  GLN B 306  ARG B 309  SER B 310                    
SITE     2 AD5 28 ASN B 311  ARG B 312  THR B 314  PHE B 374                    
SITE     3 AD5 28 PHE C 313  GLU C 347  ASN C 349  VAL C 351                    
SITE     4 AD5 28 GLY C 352  GLU C 354  GLU C 358  SER C 360                    
SITE     5 AD5 28 ASN C 365  ASP C 366  ASP C 367  LYS C 368                    
SITE     6 AD5 28  CA C1002  HOH C1105  HOH C1111  HOH C1124                    
SITE     7 AD5 28 GLN E 264  GLY E 265  GLU E 298   CL E 502                    
SITE     1 AD6  6 GLU C 347  ASN C 349  GLU C 354  ASN C 365                    
SITE     2 AD6  6 ASP C 366  EZ8 C1001                                          
SITE     1 AD7  6 ASP C 320  GLU C 324  ASN C 350  GLU C 354                    
SITE     2 AD7  6 ASP C 355  HOH C1121                                          
SITE     1 AD8  6 ASP C 355  HOH C1112  HOH C1126  HOH C1128                    
SITE     2 AD8  6 HOH C1130  HOH C1221                                          
SITE     1 AD9  2 ASN C 272  SER C 273                                          
SITE     1 AE1  2 GLN C 264  EZ8 D 502                                          
SITE     1 AE2  1 EZ8 A1001                                                     
SITE     1 AE3 27 SER A 271  ASN A 272  ARG A 309  SER A 310                    
SITE     2 AE3 27 ASN A 311  ARG A 312  THR A 314  PHE A 374                    
SITE     3 AE3 27 PHE C 263  GLN C 264  GLY C 265  GLU C 298                    
SITE     4 AE3 27  CL C1006  PHE D 313  GLU D 347  ASN D 349                    
SITE     5 AE3 27 VAL D 351  GLU D 354  GLU D 358  SER D 360                    
SITE     6 AE3 27 ASN D 365  ASP D 366  ASP D 367  LYS D 368                    
SITE     7 AE3 27  CA D 503  HOH D 601  HOH D 628                               
SITE     1 AE4  6 GLU D 347  ASN D 349  GLU D 354  ASN D 365                    
SITE     2 AE4  6 ASP D 366  EZ8 D 502                                          
SITE     1 AE5  6 ASP D 320  GLU D 324  ASN D 350  GLU D 354                    
SITE     2 AE5  6 ASP D 355  HOH D 623                                          
SITE     1 AE6  6 ASP D 355  HOH D 610  HOH D 617  HOH D 622                    
SITE     2 AE6  6 HOH D 649  HOH D 697                                          
SITE     1 AE7  2 ASN D 272  SER D 273                                          
SITE     1 AE8  2 ARG B 309  ARG E 309                                          
SITE     1 AE9  2 EZ8 C1001  GLN E 264                                          
SITE     1 AF1 25 PHE E 313  GLU E 347  ASN E 349  VAL E 351                    
SITE     2 AF1 25 GLY E 352  GLU E 354  GLU E 358  SER E 360                    
SITE     3 AF1 25 ASN E 365  ASP E 366  ASP E 367  LYS E 368                    
SITE     4 AF1 25  CA E 504  HOH E 615  HOH E 620  HOH E 648                    
SITE     5 AF1 25 HOH E 650  ASN F 272  ARG F 309  SER F 310                    
SITE     6 AF1 25 ASN F 311  ARG F 312  THR F 314  PHE F 374                    
SITE     7 AF1 25  CL F 501                                                     
SITE     1 AF2  6 GLU E 347  ASN E 349  GLU E 354  ASN E 365                    
SITE     2 AF2  6 ASP E 366  EZ8 E 503                                          
SITE     1 AF3  6 ASP E 320  GLU E 324  ASN E 350  GLU E 354                    
SITE     2 AF3  6 ASP E 355  HOH E 638                                          
SITE     1 AF4  7 GLU E 324  ASP E 355  HOH E 608  HOH E 613                    
SITE     2 AF4  7 HOH E 622  HOH E 629  HOH E 707                               
SITE     1 AF5  2 ASN E 272  SER E 273                                          
SITE     1 AF6  1 EZ8 E 503                                                     
SITE     1 AF7 26 GLN B 264  GLY B 265   CL B1006  ASN E 272                    
SITE     2 AF7 26 ARG E 309  SER E 310  ASN E 311  ARG E 312                    
SITE     3 AF7 26 THR E 314  PHE E 374  PHE F 313  GLU F 347                    
SITE     4 AF7 26 ASN F 349  VAL F 351  GLY F 352  GLU F 354                    
SITE     5 AF7 26 GLU F 358  SER F 360  ASN F 365  ASP F 366                    
SITE     6 AF7 26 ASP F 367  LYS F 368   CA F 503  HOH F 602                    
SITE     7 AF7 26 HOH F 615  HOH F 622                                          
SITE     1 AF8  6 GLU F 347  ASN F 349  GLU F 354  ASN F 365                    
SITE     2 AF8  6 ASP F 366  EZ8 F 502                                          
SITE     1 AF9  6 ASP F 320  GLU F 324  ASN F 350  GLU F 354                    
SITE     2 AF9  6 ASP F 355  HOH F 618                                          
SITE     1 AG1  4 ASP F 355  HOH F 604  HOH F 605  HOH F 693                    
SITE     1 AG2  3 SER F 271  ASN F 272  SER F 273                               
CRYST1  105.612   57.507  107.247  90.00 118.67  90.00 P 1 21 1     12          
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      0.009469  0.000000  0.005177        0.00000                         
SCALE2      0.000000  0.017389  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010627        0.00000                         
ATOM      1  N   CYS B 253     -11.582   7.688  90.114  1.00 81.16           N
ATOM      2  CA  CYS B 253     -11.575   8.480  88.848  1.00 75.60           C
ATOM      3  C   CYS B 253     -10.837   7.737  87.741  1.00 70.65           C
ATOM      4  O   CYS B 253      -9.655   7.409  87.886  1.00 70.83           O
ATOM      5  CB  CYS B 253     -10.909   9.847  89.060  1.00 79.60           C
ATOM      6  SG  CYS B 253     -10.644  10.830  87.546  1.00 86.94           S
ATOM      7  N   HIS B 254     -11.530   7.492  86.630  1.00 62.49           N
ATOM      8  CA  HIS B 254     -10.897   6.938  85.423  1.00 49.05           C
ATOM      9  C   HIS B 254     -10.770   8.019  84.375  1.00 42.23           C
ATOM     10  O   HIS B 254     -11.740   8.689  84.090  1.00 40.45           O
ATOM     11  CB  HIS B 254     -11.735   5.797  84.878  1.00 47.07           C
ATOM     12  CG  HIS B 254     -11.937   4.708  85.868  1.00 46.05           C
ATOM     13  ND1 HIS B 254     -10.921   3.847  86.238  1.00 47.82           N
ATOM     14  CD2 HIS B 254     -13.008   4.381  86.623  1.00 45.16           C
ATOM     15  CE1 HIS B 254     -11.373   3.016  87.159  1.00 47.66           C
ATOM     16  NE2 HIS B 254     -12.634   3.324  87.415  1.00 49.23           N
ATOM     17  N   PRO B 255      -9.571   8.198  83.808  1.00 37.14           N
ATOM     18  CA  PRO B 255      -9.445   9.194  82.743  1.00 38.68           C
ATOM     19  C   PRO B 255     -10.379   8.962  81.538  1.00 35.93           C
ATOM     20  O   PRO B 255     -10.836   9.914  80.941  1.00 41.36           O
ATOM     21  CB  PRO B 255      -7.968   9.093  82.332  1.00 40.35           C
ATOM     22  CG  PRO B 255      -7.257   8.448  83.506  1.00 40.82           C
ATOM     23  CD  PRO B 255      -8.282   7.554  84.142  1.00 38.62           C
ATOM     24  N   CYS B 256     -10.672   7.713  81.205  1.00 34.81           N
ATOM     25  CA  CYS B 256     -11.433   7.380  80.017  1.00 34.69           C
ATOM     26  C   CYS B 256     -12.497   6.391  80.354  1.00 35.24           C
ATOM     27  O   CYS B 256     -12.339   5.652  81.310  1.00 34.95           O
ATOM     28  CB  CYS B 256     -10.495   6.732  78.977  1.00 34.23           C
ATOM     29  SG  CYS B 256      -9.316   7.950  78.399  1.00 39.50           S
ATOM     30  N   PRO B 257     -13.565   6.328  79.531  1.00 33.35           N
ATOM     31  CA  PRO B 257     -14.508   5.245  79.717  1.00 34.28           C
ATOM     32  C   PRO B 257     -13.882   3.865  79.518  1.00 35.65           C
ATOM     33  O   PRO B 257     -12.907   3.718  78.767  1.00 31.66           O
ATOM     34  CB  PRO B 257     -15.588   5.502  78.626  1.00 33.22           C
ATOM     35  CG  PRO B 257     -15.495   6.974  78.352  1.00 35.80           C
ATOM     36  CD  PRO B 257     -13.999   7.254  78.471  1.00 34.17           C
ATOM     37  N   TRP B 258     -14.494   2.867  80.159  1.00 33.85           N
ATOM     38  CA  TRP B 258     -14.044   1.493  80.092  1.00 36.29           C
ATOM     39  C   TRP B 258     -13.920   1.022  78.647  1.00 36.04           C
ATOM     40  O   TRP B 258     -14.847   1.154  77.842  1.00 36.20           O
ATOM     41  CB  TRP B 258     -15.012   0.593  80.876  1.00 37.88           C
ATOM     42  CG  TRP B 258     -14.435  -0.718  81.410  1.00 39.22           C
ATOM     43  CD1 TRP B 258     -13.490  -1.527  80.827  1.00 39.74           C
ATOM     44  CD2 TRP B 258     -14.839  -1.382  82.609  1.00 40.58           C
ATOM     45  NE1 TRP B 258     -13.264  -2.628  81.607  1.00 38.27           N
ATOM     46  CE2 TRP B 258     -14.078  -2.566  82.708  1.00 40.53           C
ATOM     47  CE3 TRP B 258     -15.754  -1.066  83.636  1.00 43.12           C
ATOM     48  CZ2 TRP B 258     -14.216  -3.454  83.778  1.00 40.46           C
ATOM     49  CZ3 TRP B 258     -15.885  -1.937  84.706  1.00 41.50           C
ATOM     50  CH2 TRP B 258     -15.129  -3.129  84.762  1.00 43.49           C
ATOM     51  N   GLU B 259     -12.760   0.459  78.331  1.00 38.08           N
ATOM     52  CA  GLU B 259     -12.472  -0.079  77.007  1.00 38.04           C
ATOM     53  C   GLU B 259     -11.911   0.947  76.034  1.00 35.68           C
ATOM     54  O   GLU B 259     -11.432   0.565  74.975  1.00 35.50           O
ATOM     55  CB  GLU B 259     -13.687  -0.767  76.369  1.00 40.72           C
ATOM     56  CG  GLU B 259     -14.282  -1.867  77.222  1.00 43.95           C
ATOM     57  CD  GLU B 259     -14.839  -3.009  76.400  1.00 47.42           C
ATOM     58  OE1 GLU B 259     -15.727  -3.710  76.900  1.00 51.79           O
ATOM     59  OE2 GLU B 259     -14.392  -3.219  75.259  1.00 52.86           O
ATOM     60  N   TRP B 260     -11.933   2.227  76.385  1.00 32.95           N
ATOM     61  CA  TRP B 260     -11.235   3.224  75.581  1.00 33.34           C
ATOM     62  C   TRP B 260      -9.766   3.323  76.032  1.00 33.27           C
ATOM     63  O   TRP B 260      -9.443   3.103  77.211  1.00 34.28           O
ATOM     64  CB  TRP B 260     -11.873   4.582  75.765  1.00 31.28           C
ATOM     65  CG  TRP B 260     -13.285   4.720  75.289  1.00 31.32           C
ATOM     66  CD1 TRP B 260     -14.332   3.910  75.574  1.00 31.57           C
ATOM     67  CD2 TRP B 260     -13.808   5.768  74.439  1.00 29.90           C
ATOM     68  NE1 TRP B 260     -15.475   4.390  74.984  1.00 31.60           N
ATOM     69  CE2 TRP B 260     -15.176   5.516  74.268  1.00 28.74           C
ATOM     70  CE3 TRP B 260     -13.237   6.877  73.796  1.00 28.16           C
ATOM     71  CZ2 TRP B 260     -15.995   6.339  73.512  1.00 27.63           C
ATOM     72  CZ3 TRP B 260     -14.048   7.697  73.064  1.00 28.49           C
ATOM     73  CH2 TRP B 260     -15.413   7.411  72.902  1.00 27.05           C
ATOM     74  N   THR B 261      -8.903   3.690  75.095  1.00 33.17           N
ATOM     75  CA  THR B 261      -7.488   3.863  75.324  1.00 32.72           C
ATOM     76  C   THR B 261      -7.206   5.326  75.600  1.00 34.87           C
ATOM     77  O   THR B 261      -7.570   6.215  74.837  1.00 34.04           O
ATOM     78  CB  THR B 261      -6.649   3.517  74.078  1.00 33.19           C
ATOM     79  OG1 THR B 261      -6.924   2.204  73.664  1.00 32.80           O
ATOM     80  CG2 THR B 261      -5.134   3.635  74.339  1.00 33.06           C
ATOM     81  N   PHE B 262      -6.435   5.540  76.644  1.00 35.14           N
ATOM     82  CA  PHE B 262      -5.907   6.836  76.974  1.00 34.15           C
ATOM     83  C   PHE B 262      -4.606   7.075  76.242  1.00 30.41           C
ATOM     84  O   PHE B 262      -3.721   6.262  76.291  1.00 28.76           O
ATOM     85  CB  PHE B 262      -5.679   6.891  78.474  1.00 32.74           C
ATOM     86  CG  PHE B 262      -5.004   8.129  78.939  1.00 33.67           C
ATOM     87  CD1 PHE B 262      -3.609   8.196  78.984  1.00 35.84           C
ATOM     88  CD2 PHE B 262      -5.746   9.192  79.405  1.00 32.89           C
ATOM     89  CE1 PHE B 262      -2.978   9.342  79.440  1.00 37.05           C
ATOM     90  CE2 PHE B 262      -5.124  10.335  79.858  1.00 34.91           C
ATOM     91  CZ  PHE B 262      -3.744  10.407  79.890  1.00 34.44           C
ATOM     92  N   PHE B 263      -4.484   8.207  75.581  1.00 28.52           N
ATOM     93  CA  PHE B 263      -3.192   8.596  75.034  1.00 30.96           C
ATOM     94  C   PHE B 263      -3.115  10.090  75.133  1.00 29.92           C
ATOM     95  O   PHE B 263      -4.001  10.794  74.629  1.00 30.90           O
ATOM     96  CB  PHE B 263      -3.061   8.166  73.570  1.00 32.68           C
ATOM     97  CG  PHE B 263      -1.789   8.606  72.921  1.00 33.19           C
ATOM     98  CD1 PHE B 263      -0.655   7.828  73.021  1.00 33.28           C
ATOM     99  CD2 PHE B 263      -1.728   9.800  72.197  1.00 36.04           C
ATOM    100  CE1 PHE B 263       0.534   8.225  72.425  1.00 35.37           C
ATOM    101  CE2 PHE B 263      -0.548  10.191  71.561  1.00 35.96           C
ATOM    102  CZ  PHE B 263       0.588   9.409  71.696  1.00 34.17           C
ATOM    103  N   GLN B 264      -2.084  10.547  75.833  1.00 29.64           N
ATOM    104  CA  GLN B 264      -1.777  11.968  76.024  1.00 28.84           C
ATOM    105  C   GLN B 264      -2.932  12.877  76.232  1.00 27.26           C
ATOM    106  O   GLN B 264      -3.040  13.861  75.560  1.00 28.30           O
ATOM    107  CB  GLN B 264      -0.910  12.502  74.879  1.00 31.45           C
ATOM    108  CG  GLN B 264       0.366  11.696  74.660  1.00 31.63           C
ATOM    109  CD  GLN B 264       1.316  12.358  73.687  1.00 33.47           C
ATOM    110  OE1 GLN B 264       0.900  13.201  72.894  1.00 35.76           O
ATOM    111  NE2 GLN B 264       2.605  11.970  73.731  1.00 28.32           N
ATOM    112  N   GLY B 265      -3.788  12.549  77.184  1.00 29.12           N
ATOM    113  CA  GLY B 265      -4.806  13.463  77.645  1.00 29.07           C
ATOM    114  C   GLY B 265      -6.139  13.239  76.956  1.00 33.22           C
ATOM    115  O   GLY B 265      -7.100  13.973  77.232  1.00 32.51           O
ATOM    116  N   ASN B 266      -6.200  12.268  76.029  1.00 31.71           N
ATOM    117  CA  ASN B 266      -7.443  12.036  75.266  1.00 32.43           C
ATOM    118  C   ASN B 266      -7.820  10.572  75.314  1.00 31.78           C
ATOM    119  O   ASN B 266      -6.975   9.733  75.662  1.00 30.97           O
ATOM    120  CB  ASN B 266      -7.299  12.522  73.816  1.00 32.90           C
ATOM    121  CG  ASN B 266      -7.226  14.045  73.721  1.00 31.58           C
ATOM    122  OD1 ASN B 266      -8.165  14.713  74.035  1.00 33.70           O
ATOM    123  ND2 ASN B 266      -6.126  14.565  73.263  1.00 31.25           N
ATOM    124  N   CYS B 267      -9.084  10.289  75.012  1.00 26.30           N
ATOM    125  CA  CYS B 267      -9.590   8.952  75.009  1.00 28.30           C
ATOM    126  C   CYS B 267      -9.927   8.548  73.567  1.00 29.56           C
ATOM    127  O   CYS B 267     -10.584   9.292  72.821  1.00 29.88           O
ATOM    128  CB  CYS B 267     -10.819   8.826  75.883  1.00 30.60           C
ATOM    129  SG  CYS B 267     -10.571   9.364  77.592  1.00 34.79           S
ATOM    130  N   TYR B 268      -9.507   7.353  73.202  1.00 27.67           N
ATOM    131  CA  TYR B 268      -9.749   6.825  71.861  1.00 28.56           C
ATOM    132  C   TYR B 268     -10.487   5.518  71.889  1.00 28.29           C
ATOM    133  O   TYR B 268     -10.206   4.619  72.695  1.00 27.90           O
ATOM    134  CB  TYR B 268      -8.478   6.687  71.101  1.00 25.98           C
ATOM    135  CG  TYR B 268      -7.707   7.983  71.020  1.00 26.71           C
ATOM    136  CD1 TYR B 268      -6.954   8.433  72.101  1.00 27.73           C
ATOM    137  CD2 TYR B 268      -7.692   8.716  69.859  1.00 26.81           C
ATOM    138  CE1 TYR B 268      -6.202   9.602  72.023  1.00 28.20           C
ATOM    139  CE2 TYR B 268      -6.987   9.875  69.763  1.00 27.45           C
ATOM    140  CZ  TYR B 268      -6.215  10.314  70.828  1.00 29.39           C
ATOM    141  OH  TYR B 268      -5.515  11.477  70.676  1.00 27.54           O
ATOM    142  N   PHE B 269     -11.496   5.470  71.026  1.00 30.70           N
ATOM    143  CA  PHE B 269     -12.295   4.282  70.810  1.00 31.43           C
ATOM    144  C   PHE B 269     -11.913   3.693  69.456  1.00 27.91           C
ATOM    145  O   PHE B 269     -12.070   4.372  68.434  1.00 26.55           O
ATOM    146  CB  PHE B 269     -13.789   4.633  70.791  1.00 34.67           C
ATOM    147  CG  PHE B 269     -14.651   3.412  70.632  1.00 40.37           C
ATOM    148  CD1 PHE B 269     -14.695   2.467  71.653  1.00 46.01           C
ATOM    149  CD2 PHE B 269     -15.347   3.165  69.458  1.00 42.56           C
ATOM    150  CE1 PHE B 269     -15.458   1.311  71.518  1.00 49.89           C
ATOM    151  CE2 PHE B 269     -16.126   2.014  69.321  1.00 45.94           C
ATOM    152  CZ  PHE B 269     -16.177   1.084  70.348  1.00 43.58           C
ATOM    153  N   MET B 270     -11.403   2.466  69.449  1.00 27.22           N
ATOM    154  CA  MET B 270     -11.058   1.754  68.213  1.00 30.94           C
ATOM    155  C   MET B 270     -12.221   0.823  67.932  1.00 31.92           C
ATOM    156  O   MET B 270     -12.455  -0.102  68.716  1.00 30.78           O
ATOM    157  CB  MET B 270      -9.784   0.927  68.335  1.00 34.30           C
ATOM    158  CG  MET B 270      -8.694   1.448  69.276  1.00 41.76           C
ATOM    159  SD  MET B 270      -8.088   3.099  68.935  1.00 46.67           S
ATOM    160  CE  MET B 270      -6.535   3.089  69.829  1.00 48.15           C
ATOM    161  N   SER B 271     -12.971   1.083  66.854  1.00 29.28           N
ATOM    162  CA  SER B 271     -14.121   0.221  66.494  1.00 28.15           C
ATOM    163  C   SER B 271     -13.641  -1.205  66.197  1.00 28.95           C
ATOM    164  O   SER B 271     -12.530  -1.390  65.778  1.00 29.59           O
ATOM    165  CB  SER B 271     -14.854   0.772  65.275  1.00 25.08           C
ATOM    166  OG  SER B 271     -14.176   0.436  64.021  1.00 24.81           O
ATOM    167  N   ASN B 272     -14.485  -2.189  66.415  1.00 31.15           N
ATOM    168  CA AASN B 272     -14.208  -3.566  65.934  0.30 32.33           C
ATOM    169  CA BASN B 272     -14.218  -3.541  65.967  0.70 36.69           C
ATOM    170  C   ASN B 272     -15.209  -3.986  64.858  1.00 33.99           C
ATOM    171  O   ASN B 272     -15.350  -5.171  64.567  1.00 35.78           O
ATOM    172  CB AASN B 272     -14.201  -4.619  67.065  0.30 31.58           C
ATOM    173  CB BASN B 272     -14.202  -4.438  67.214  0.70 39.46           C
ATOM    174  CG AASN B 272     -13.542  -5.940  66.633  0.30 30.69           C
ATOM    175  CG BASN B 272     -13.002  -4.120  68.110  0.70 45.64           C
ATOM    176  OD1AASN B 272     -12.856  -6.007  65.611  0.30 28.33           O
ATOM    177  OD1BASN B 272     -13.158  -3.550  69.198  0.70 46.33           O
ATOM    178  ND2AASN B 272     -13.760  -6.995  67.411  0.30 30.83           N
ATOM    179  ND2BASN B 272     -11.775  -4.417  67.608  0.70 39.98           N
ATOM    180  N   SER B 273     -15.900  -3.006  64.282  1.00 29.89           N
ATOM    181  CA  SER B 273     -16.723  -3.192  63.108  1.00 30.19           C
ATOM    182  C   SER B 273     -16.473  -2.031  62.158  1.00 26.62           C
ATOM    183  O   SER B 273     -15.755  -1.091  62.517  1.00 27.96           O
ATOM    184  CB  SER B 273     -18.198  -3.247  63.458  1.00 29.25           C
ATOM    185  OG  SER B 273     -18.603  -2.000  63.919  1.00 32.98           O
ATOM    186  N   GLN B 274     -17.104  -2.102  60.994  1.00 22.32           N
ATOM    187  CA  GLN B 274     -16.851  -1.205  59.874  1.00 24.05           C
ATOM    188  C   GLN B 274     -18.109  -0.428  59.454  1.00 22.89           C
ATOM    189  O   GLN B 274     -19.196  -0.983  59.434  1.00 21.08           O
ATOM    190  CB  GLN B 274     -16.403  -2.013  58.666  1.00 22.36           C
ATOM    191  CG  GLN B 274     -15.119  -2.767  58.820  1.00 24.26           C
ATOM    192  CD  GLN B 274     -15.126  -4.038  58.004  1.00 25.06           C
ATOM    193  OE1 GLN B 274     -15.857  -4.968  58.341  1.00 24.91           O
ATOM    194  NE2 GLN B 274     -14.338  -4.068  56.890  1.00 24.91           N
ATOM    195  N   ARG B 275     -17.925   0.842  59.090  1.00 22.82           N
ATOM    196  CA  ARG B 275     -18.979   1.669  58.602  1.00 21.37           C
ATOM    197  C   ARG B 275     -18.430   2.670  57.597  1.00 20.28           C
ATOM    198  O   ARG B 275     -17.233   2.906  57.487  1.00 16.48           O
ATOM    199  CB  ARG B 275     -19.584   2.439  59.760  1.00 24.89           C
ATOM    200  CG  ARG B 275     -20.438   1.616  60.725  1.00 27.18           C
ATOM    201  CD  ARG B 275     -20.835   2.600  61.794  1.00 30.19           C
ATOM    202  NE  ARG B 275     -21.663   2.071  62.849  1.00 34.30           N
ATOM    203  CZ  ARG B 275     -22.625   2.771  63.467  1.00 38.21           C
ATOM    204  NH1 ARG B 275     -22.990   4.018  63.069  1.00 39.04           N
ATOM    205  NH2 ARG B 275     -23.281   2.185  64.445  1.00 42.27           N
ATOM    206  N   ASN B 276     -19.335   3.306  56.887  1.00 19.80           N
ATOM    207  CA  ASN B 276     -18.919   4.310  55.921  1.00 21.10           C
ATOM    208  C   ASN B 276     -18.547   5.558  56.704  1.00 19.03           C
ATOM    209  O   ASN B 276     -18.815   5.618  57.914  1.00 17.92           O
ATOM    210  CB  ASN B 276     -19.955   4.499  54.813  1.00 22.16           C
ATOM    211  CG  ASN B 276     -21.229   5.128  55.270  1.00 24.01           C
ATOM    212  OD1 ASN B 276     -21.230   6.015  56.100  1.00 28.87           O
ATOM    213  ND2 ASN B 276     -22.336   4.703  54.677  1.00 24.09           N
ATOM    214  N   TRP B 277     -17.929   6.524  56.041  1.00 17.80           N
ATOM    215  CA  TRP B 277     -17.336   7.655  56.691  1.00 18.81           C
ATOM    216  C   TRP B 277     -18.387   8.423  57.535  1.00 21.47           C
ATOM    217  O   TRP B 277     -18.139   8.725  58.686  1.00 22.00           O
ATOM    218  CB  TRP B 277     -16.663   8.566  55.662  1.00 20.28           C
ATOM    219  CG  TRP B 277     -15.776   9.628  56.283  1.00 20.51           C
ATOM    220  CD1 TRP B 277     -14.519   9.455  56.778  1.00 19.30           C
ATOM    221  CD2 TRP B 277     -16.065  11.032  56.435  1.00 21.12           C
ATOM    222  NE1 TRP B 277     -14.025  10.643  57.247  1.00 18.41           N
ATOM    223  CE2 TRP B 277     -14.955  11.622  57.052  1.00 18.90           C
ATOM    224  CE3 TRP B 277     -17.152  11.830  56.117  1.00 23.22           C
ATOM    225  CZ2 TRP B 277     -14.908  12.965  57.374  1.00 20.98           C
ATOM    226  CZ3 TRP B 277     -17.099  13.192  56.413  1.00 23.19           C
ATOM    227  CH2 TRP B 277     -15.965  13.759  56.991  1.00 20.97           C
ATOM    228  N   HIS B 278     -19.555   8.696  56.937  1.00 21.98           N
ATOM    229  CA  HIS B 278     -20.612   9.444  57.542  1.00 21.44           C
ATOM    230  C   HIS B 278     -21.302   8.693  58.663  1.00 22.34           C
ATOM    231  O   HIS B 278     -21.680   9.307  59.625  1.00 22.52           O
ATOM    232  CB  HIS B 278     -21.668   9.830  56.467  1.00 22.98           C
ATOM    233  CG  HIS B 278     -21.270  11.005  55.645  1.00 22.72           C
ATOM    234  ND1 HIS B 278     -20.753  10.879  54.363  1.00 21.17           N
ATOM    235  CD2 HIS B 278     -21.283  12.326  55.935  1.00 22.96           C
ATOM    236  CE1 HIS B 278     -20.415  12.075  53.932  1.00 23.56           C
ATOM    237  NE2 HIS B 278     -20.750  12.972  54.852  1.00 24.61           N
ATOM    238  N   ASP B 279     -21.514   7.386  58.518  1.00 22.62           N
ATOM    239  CA  ASP B 279     -22.047   6.600  59.608  1.00 25.02           C
ATOM    240  C   ASP B 279     -20.997   6.481  60.741  1.00 25.69           C
ATOM    241  O   ASP B 279     -21.341   6.422  61.932  1.00 26.17           O
ATOM    242  CB  ASP B 279     -22.481   5.210  59.144  1.00 27.35           C
ATOM    243  CG  ASP B 279     -23.689   5.223  58.228  1.00 29.37           C
ATOM    244  OD1 ASP B 279     -24.294   6.289  58.031  1.00 30.90           O
ATOM    245  OD2 ASP B 279     -24.003   4.152  57.634  1.00 31.14           O
ATOM    246  N   SER B 280     -19.721   6.507  60.392  1.00 24.16           N
ATOM    247  CA  SER B 280     -18.674   6.578  61.432  1.00 25.94           C
ATOM    248  C   SER B 280     -18.720   7.856  62.315  1.00 26.97           C
ATOM    249  O   SER B 280     -18.559   7.799  63.546  1.00 26.18           O
ATOM    250  CB  SER B 280     -17.275   6.379  60.843  1.00 24.17           C
ATOM    251  OG  SER B 280     -17.149   5.058  60.285  1.00 22.54           O
ATOM    252  N   ILE B 281     -18.951   8.987  61.677  1.00 27.65           N
ATOM    253  CA  ILE B 281     -19.151  10.260  62.410  1.00 26.84           C
ATOM    254  C   ILE B 281     -20.303  10.128  63.424  1.00 27.77           C
ATOM    255  O   ILE B 281     -20.202  10.570  64.564  1.00 27.16           O
ATOM    256  CB  ILE B 281     -19.445  11.385  61.409  1.00 27.15           C
ATOM    257  CG1 ILE B 281     -18.162  11.855  60.715  1.00 31.40           C
ATOM    258  CG2 ILE B 281     -20.135  12.582  62.024  1.00 27.49           C
ATOM    259  CD1 ILE B 281     -18.422  12.395  59.336  1.00 33.08           C
ATOM    260  N   THR B 282     -21.407   9.576  62.965  1.00 26.76           N
ATOM    261  CA  THR B 282     -22.583   9.410  63.784  1.00 30.06           C
ATOM    262  C   THR B 282     -22.326   8.474  64.927  1.00 28.99           C
ATOM    263  O   THR B 282     -22.740   8.742  66.043  1.00 25.02           O
ATOM    264  CB  THR B 282     -23.721   8.820  62.926  1.00 28.51           C
ATOM    265  OG1 THR B 282     -23.951   9.736  61.880  1.00 27.53           O
ATOM    266  CG2 THR B 282     -24.996   8.609  63.709  1.00 29.70           C
ATOM    267  N   ALA B 283     -21.676   7.350  64.632  1.00 27.64           N
ATOM    268  CA  ALA B 283     -21.245   6.428  65.721  1.00 27.81           C
ATOM    269  C   ALA B 283     -20.433   7.141  66.807  1.00 28.37           C
ATOM    270  O   ALA B 283     -20.707   6.972  68.011  1.00 27.55           O
ATOM    271  CB  ALA B 283     -20.466   5.265  65.155  1.00 27.25           C
ATOM    272  N   CYS B 284     -19.504   8.009  66.404  1.00 27.61           N
ATOM    273  CA  CYS B 284     -18.722   8.766  67.404  1.00 28.18           C
ATOM    274  C   CYS B 284     -19.630   9.738  68.180  1.00 29.77           C
ATOM    275  O   CYS B 284     -19.491   9.830  69.417  1.00 27.18           O
ATOM    276  CB  CYS B 284     -17.534   9.498  66.768  1.00 27.41           C
ATOM    277  SG  CYS B 284     -16.336   8.307  66.063  1.00 28.11           S
ATOM    278  N   LYS B 285     -20.586  10.401  67.495  1.00 30.51           N
ATOM    279  CA  LYS B 285     -21.498  11.351  68.181  1.00 30.66           C
ATOM    280  C   LYS B 285     -22.291  10.596  69.238  1.00 29.69           C
ATOM    281  O   LYS B 285     -22.605  11.101  70.311  1.00 29.77           O
ATOM    282  CB  LYS B 285     -22.476  12.021  67.232  1.00 33.41           C
ATOM    283  CG  LYS B 285     -21.856  12.983  66.249  1.00 40.31           C
ATOM    284  CD  LYS B 285     -22.937  13.602  65.374  1.00 44.62           C
ATOM    285  CE  LYS B 285     -22.323  14.286  64.160  1.00 50.17           C
ATOM    286  NZ  LYS B 285     -21.386  15.412  64.440  1.00 51.02           N
ATOM    287  N   GLU B 286     -22.608   9.363  68.950  1.00 30.54           N
ATOM    288  CA  GLU B 286     -23.417   8.622  69.864  1.00 34.74           C
ATOM    289  C   GLU B 286     -22.722   8.359  71.180  1.00 35.86           C
ATOM    290  O   GLU B 286     -23.382   8.166  72.172  1.00 36.01           O
ATOM    291  CB  GLU B 286     -23.906   7.342  69.203  1.00 35.42           C
ATOM    292  CG  GLU B 286     -24.969   7.639  68.160  1.00 36.80           C
ATOM    293  CD  GLU B 286     -25.440   6.422  67.407  1.00 40.19           C
ATOM    294  OE1 GLU B 286     -26.588   6.446  66.881  1.00 44.62           O
ATOM    295  OE2 GLU B 286     -24.683   5.430  67.377  1.00 38.07           O
ATOM    296  N   VAL B 287     -21.388   8.409  71.201  1.00 36.67           N
ATOM    297  CA  VAL B 287     -20.630   8.217  72.443  1.00 30.83           C
ATOM    298  C   VAL B 287     -19.921   9.452  72.861  1.00 31.20           C
ATOM    299  O   VAL B 287     -18.886   9.377  73.501  1.00 37.01           O
ATOM    300  CB  VAL B 287     -19.648   7.043  72.352  1.00 30.18           C
ATOM    301  CG1 VAL B 287     -20.444   5.735  72.303  1.00 30.15           C
ATOM    302  CG2 VAL B 287     -18.736   7.139  71.110  1.00 30.07           C
ATOM    303  N   GLY B 288     -20.483  10.593  72.513  1.00 27.22           N
ATOM    304  CA  GLY B 288     -19.993  11.868  72.965  1.00 26.80           C
ATOM    305  C   GLY B 288     -18.643  12.226  72.388  1.00 29.99           C
ATOM    306  O   GLY B 288     -17.861  12.977  72.988  1.00 32.63           O
ATOM    307  N   ALA B 289     -18.364  11.745  71.193  1.00 29.06           N
ATOM    308  CA  ALA B 289     -17.012  11.850  70.693  1.00 27.89           C
ATOM    309  C   ALA B 289     -16.980  12.323  69.264  1.00 26.40           C
ATOM    310  O   ALA B 289     -17.996  12.595  68.666  1.00 28.72           O
ATOM    311  CB  ALA B 289     -16.310  10.496  70.845  1.00 29.14           C
ATOM    312  N   GLN B 290     -15.794  12.396  68.715  1.00 25.24           N
ATOM    313  CA AGLN B 290     -15.632  12.871  67.367  0.50 25.90           C
ATOM    314  CA BGLN B 290     -15.557  12.935  67.381  0.50 26.51           C
ATOM    315  C   GLN B 290     -14.771  11.906  66.561  1.00 25.77           C
ATOM    316  O   GLN B 290     -13.852  11.298  67.075  1.00 27.07           O
ATOM    317  CB AGLN B 290     -14.991  14.242  67.418  0.50 25.58           C
ATOM    318  CB BGLN B 290     -14.764  14.254  67.534  0.50 27.01           C
ATOM    319  CG AGLN B 290     -15.214  15.047  66.167  0.50 25.58           C
ATOM    320  CG BGLN B 290     -13.587  14.454  66.577  0.50 27.10           C
ATOM    321  CD AGLN B 290     -14.706  16.454  66.306  0.50 23.65           C
ATOM    322  CD BGLN B 290     -12.370  15.136  67.197  0.50 27.13           C
ATOM    323  OE1AGLN B 290     -15.449  17.393  66.069  0.50 22.05           O
ATOM    324  OE1BGLN B 290     -11.349  14.478  67.459  0.50 26.27           O
ATOM    325  NE2AGLN B 290     -13.438  16.602  66.693  0.50 21.54           N
ATOM    326  NE2BGLN B 290     -12.456  16.454  67.403  0.50 25.16           N
ATOM    327  N   LEU B 291     -15.106  11.729  65.289  1.00 27.90           N
ATOM    328  CA  LEU B 291     -14.267  10.926  64.411  1.00 25.51           C
ATOM    329  C   LEU B 291     -12.916  11.616  64.409  1.00 23.70           C
ATOM    330  O   LEU B 291     -12.834  12.840  64.267  1.00 24.86           O
ATOM    331  CB  LEU B 291     -14.862  10.818  63.003  1.00 27.96           C
ATOM    332  CG  LEU B 291     -14.126   9.946  61.975  1.00 27.27           C
ATOM    333  CD1 LEU B 291     -14.073   8.503  62.435  1.00 27.89           C
ATOM    334  CD2 LEU B 291     -14.791  10.092  60.591  1.00 29.77           C
ATOM    335  N   VAL B 292     -11.867  10.832  64.597  1.00 22.37           N
ATOM    336  CA  VAL B 292     -10.572  11.319  65.111  1.00 21.94           C
ATOM    337  C   VAL B 292      -9.964  12.433  64.278  1.00 24.71           C
ATOM    338  O   VAL B 292      -9.727  12.268  63.079  1.00 23.08           O
ATOM    339  CB  VAL B 292      -9.548  10.163  65.329  1.00 23.26           C
ATOM    340  CG1 VAL B 292      -9.194   9.431  64.018  1.00 23.81           C
ATOM    341  CG2 VAL B 292      -8.284  10.657  66.068  1.00 23.41           C
ATOM    342  N   VAL B 293      -9.698  13.549  64.958  1.00 26.26           N
ATOM    343  CA  VAL B 293      -8.974  14.709  64.430  1.00 25.07           C
ATOM    344  C   VAL B 293      -7.582  14.677  65.051  1.00 24.61           C
ATOM    345  O   VAL B 293      -7.446  14.707  66.232  1.00 25.86           O
ATOM    346  CB  VAL B 293      -9.647  16.039  64.838  1.00 25.54           C
ATOM    347  CG1 VAL B 293      -8.862  17.246  64.336  1.00 24.75           C
ATOM    348  CG2 VAL B 293     -11.092  16.102  64.350  1.00 27.87           C
ATOM    349  N   ILE B 294      -6.554  14.618  64.231  1.00 25.12           N
ATOM    350  CA  ILE B 294      -5.207  14.501  64.673  1.00 26.68           C
ATOM    351  C   ILE B 294      -4.610  15.921  64.816  1.00 31.40           C
ATOM    352  O   ILE B 294      -4.711  16.753  63.910  1.00 32.68           O
ATOM    353  CB  ILE B 294      -4.371  13.711  63.655  1.00 27.24           C
ATOM    354  CG1 ILE B 294      -5.046  12.343  63.327  1.00 26.30           C
ATOM    355  CG2 ILE B 294      -2.954  13.523  64.220  1.00 28.17           C
ATOM    356  CD1 ILE B 294      -4.306  11.554  62.251  1.00 27.42           C
ATOM    357  N   LYS B 295      -3.967  16.175  65.942  1.00 31.07           N
ATOM    358  CA  LYS B 295      -3.487  17.503  66.256  1.00 33.79           C
ATOM    359  C   LYS B 295      -1.966  17.573  66.388  1.00 33.75           C
ATOM    360  O   LYS B 295      -1.436  18.664  66.419  1.00 32.87           O
ATOM    361  CB  LYS B 295      -4.106  17.954  67.573  1.00 36.06           C
ATOM    362  CG  LYS B 295      -5.617  18.079  67.569  1.00 36.20           C
ATOM    363  CD  LYS B 295      -6.050  19.464  67.189  1.00 36.82           C
ATOM    364  CE  LYS B 295      -7.548  19.527  66.974  1.00 36.56           C
ATOM    365  NZ  LYS B 295      -7.890  20.251  65.722  1.00 33.96           N
ATOM    366  N   SER B 296      -1.290  16.426  66.479  1.00 32.79           N
ATOM    367  CA  SER B 296       0.166  16.359  66.647  1.00 34.10           C
ATOM    368  C   SER B 296       0.776  15.098  66.068  1.00 33.94           C
ATOM    369  O   SER B 296       0.080  14.136  65.728  1.00 35.20           O
ATOM    370  CB  SER B 296       0.540  16.381  68.124  1.00 34.38           C
ATOM    371  OG  SER B 296       0.393  15.082  68.662  1.00 33.96           O
ATOM    372  N   ALA B 297       2.096  15.092  66.031  1.00 31.74           N
ATOM    373  CA  ALA B 297       2.839  14.098  65.280  1.00 34.65           C
ATOM    374  C   ALA B 297       2.852  12.774  66.014  1.00 33.47           C
ATOM    375  O   ALA B 297       2.799  11.711  65.418  1.00 30.63           O
ATOM    376  CB  ALA B 297       4.260  14.577  65.061  1.00 35.11           C
ATOM    377  N   GLU B 298       2.980  12.885  67.327  1.00 34.19           N
ATOM    378  CA AGLU B 298       3.002  11.774  68.242  0.70 31.83           C
ATOM    379  CA BGLU B 298       3.043  11.717  68.181  0.30 31.80           C
ATOM    380  C   GLU B 298       1.645  11.097  68.256  1.00 29.52           C
ATOM    381  O   GLU B 298       1.518   9.876  68.347  1.00 30.80           O
ATOM    382  CB AGLU B 298       3.359  12.289  69.640  0.70 34.29           C
ATOM    383  CB BGLU B 298       3.678  12.036  69.555  0.30 33.10           C
ATOM    384  CG AGLU B 298       4.752  12.938  69.716  0.70 37.09           C
ATOM    385  CG BGLU B 298       5.177  11.669  69.630  0.30 34.09           C
ATOM    386  CD AGLU B 298       4.814  14.407  69.260  0.70 37.46           C
ATOM    387  CD BGLU B 298       6.039  12.680  70.374  0.30 34.54           C
ATOM    388  OE1AGLU B 298       5.950  14.906  69.049  0.70 42.86           O
ATOM    389  OE1BGLU B 298       5.492  13.686  70.858  0.30 38.76           O
ATOM    390  OE2AGLU B 298       3.768  15.071  69.114  0.70 33.45           O
ATOM    391  OE2BGLU B 298       7.271  12.483  70.478  0.30 34.36           O
ATOM    392  N   GLU B 299       0.614  11.907  68.185  1.00 27.44           N
ATOM    393  CA  GLU B 299      -0.742  11.371  68.002  1.00 28.27           C
ATOM    394  C   GLU B 299      -0.920  10.581  66.697  1.00 29.10           C
ATOM    395  O   GLU B 299      -1.404   9.446  66.695  1.00 28.12           O
ATOM    396  CB  GLU B 299      -1.766  12.459  68.101  1.00 28.30           C
ATOM    397  CG  GLU B 299      -3.158  11.911  68.246  1.00 31.17           C
ATOM    398  CD  GLU B 299      -4.174  13.032  68.321  1.00 31.81           C
ATOM    399  OE1 GLU B 299      -5.376  12.749  68.519  1.00 30.57           O
ATOM    400  OE2 GLU B 299      -3.751  14.191  68.193  1.00 32.05           O
ATOM    401  N   GLN B 300      -0.475  11.160  65.599  1.00 26.15           N
ATOM    402  CA  GLN B 300      -0.408  10.439  64.344  1.00 24.62           C
ATOM    403  C   GLN B 300       0.315   9.111  64.428  1.00 25.87           C
ATOM    404  O   GLN B 300      -0.225   8.111  63.989  1.00 25.74           O
ATOM    405  CB  GLN B 300       0.182  11.316  63.244  1.00 24.68           C
ATOM    406  CG  GLN B 300       0.886  10.576  62.121  1.00 25.37           C
ATOM    407  CD  GLN B 300      -0.016   9.748  61.205  1.00 26.79           C
ATOM    408  OE1 GLN B 300       0.492   8.996  60.367  1.00 26.30           O
ATOM    409  NE2 GLN B 300      -1.316   9.921  61.305  1.00 23.01           N
ATOM    410  N   ASN B 301       1.524   9.066  64.995  1.00 27.68           N
ATOM    411  CA  ASN B 301       2.279   7.801  65.080  1.00 24.99           C
ATOM    412  C   ASN B 301       1.514   6.801  65.908  1.00 22.91           C
ATOM    413  O   ASN B 301       1.470   5.633  65.565  1.00 24.64           O
ATOM    414  CB  ASN B 301       3.644   7.999  65.711  1.00 29.79           C
ATOM    415  CG  ASN B 301       4.492   9.022  64.984  1.00 30.31           C
ATOM    416  OD1 ASN B 301       4.337   9.239  63.800  1.00 34.68           O
ATOM    417  ND2 ASN B 301       5.416   9.647  65.711  1.00 35.17           N
ATOM    418  N   PHE B 302       0.866   7.249  66.974  1.00 22.50           N
ATOM    419  CA  PHE B 302       0.086   6.348  67.795  1.00 24.37           C
ATOM    420  C   PHE B 302      -1.064   5.745  66.981  1.00 27.32           C
ATOM    421  O   PHE B 302      -1.224   4.483  66.932  1.00 29.63           O
ATOM    422  CB  PHE B 302      -0.409   7.058  69.034  1.00 24.78           C
ATOM    423  CG  PHE B 302      -1.609   6.434  69.697  1.00 28.41           C
ATOM    424  CD1 PHE B 302      -1.492   5.268  70.435  1.00 30.35           C
ATOM    425  CD2 PHE B 302      -2.856   7.082  69.667  1.00 32.09           C
ATOM    426  CE1 PHE B 302      -2.592   4.713  71.089  1.00 29.91           C
ATOM    427  CE2 PHE B 302      -3.959   6.543  70.337  1.00 32.19           C
ATOM    428  CZ  PHE B 302      -3.821   5.340  71.027  1.00 30.91           C
ATOM    429  N   LEU B 303      -1.834   6.613  66.324  1.00 25.46           N
ATOM    430  CA  LEU B 303      -2.991   6.167  65.514  1.00 26.83           C
ATOM    431  C   LEU B 303      -2.609   5.350  64.251  1.00 26.02           C
ATOM    432  O   LEU B 303      -3.281   4.360  63.913  1.00 27.46           O
ATOM    433  CB  LEU B 303      -3.809   7.354  65.084  1.00 25.06           C
ATOM    434  CG  LEU B 303      -4.539   8.059  66.218  1.00 26.72           C
ATOM    435  CD1 LEU B 303      -4.920   9.415  65.694  1.00 27.13           C
ATOM    436  CD2 LEU B 303      -5.771   7.325  66.710  1.00 28.62           C
ATOM    437  N   GLN B 304      -1.554   5.762  63.565  1.00 23.94           N
ATOM    438  CA  GLN B 304      -1.128   5.050  62.350  1.00 27.41           C
ATOM    439  C   GLN B 304      -0.817   3.600  62.717  1.00 30.57           C
ATOM    440  O   GLN B 304      -1.231   2.628  62.026  1.00 30.97           O
ATOM    441  CB  GLN B 304       0.117   5.683  61.756  1.00 28.37           C
ATOM    442  CG  GLN B 304       0.495   5.148  60.385  1.00 28.93           C
ATOM    443  CD  GLN B 304      -0.564   5.449  59.357  1.00 31.39           C
ATOM    444  OE1 GLN B 304      -1.112   4.519  58.709  1.00 29.03           O
ATOM    445  NE2 GLN B 304      -0.858   6.755  59.179  1.00 25.90           N
ATOM    446  N   LEU B 305      -0.085   3.494  63.817  1.00 37.41           N
ATOM    447  CA  LEU B 305       0.331   2.239  64.405  1.00 37.96           C
ATOM    448  C   LEU B 305      -0.851   1.294  64.609  1.00 36.53           C
ATOM    449  O   LEU B 305      -0.742   0.123  64.305  1.00 35.09           O
ATOM    450  CB  LEU B 305       1.045   2.502  65.732  1.00 42.60           C
ATOM    451  CG  LEU B 305       1.497   1.179  66.366  1.00 47.80           C
ATOM    452  CD1 LEU B 305       2.883   0.837  65.860  1.00 48.65           C
ATOM    453  CD2 LEU B 305       1.387   1.179  67.884  1.00 49.13           C
ATOM    454  N   GLN B 306      -1.987   1.799  65.068  1.00 36.49           N
ATOM    455  CA  GLN B 306      -3.187   0.938  65.229  1.00 38.99           C
ATOM    456  C   GLN B 306      -3.529   0.224  63.935  1.00 34.47           C
ATOM    457  O   GLN B 306      -3.920  -0.926  63.964  1.00 38.04           O
ATOM    458  CB  GLN B 306      -4.442   1.693  65.717  1.00 35.84           C
ATOM    459  CG  GLN B 306      -4.272   2.477  67.009  1.00 38.39           C
ATOM    460  CD  GLN B 306      -3.481   1.741  68.079  1.00 38.79           C
ATOM    461  OE1 GLN B 306      -3.831   0.621  68.461  1.00 38.14           O
ATOM    462  NE2 GLN B 306      -2.389   2.371  68.567  1.00 38.33           N
ATOM    463  N   SER B 307      -3.353   0.895  62.816  1.00 35.10           N
ATOM    464  CA  SER B 307      -3.697   0.336  61.522  1.00 35.03           C
ATOM    465  C   SER B 307      -2.579  -0.431  60.826  1.00 34.50           C
ATOM    466  O   SER B 307      -2.859  -1.417  60.157  1.00 33.66           O
ATOM    467  CB  SER B 307      -4.222   1.434  60.592  1.00 35.41           C
ATOM    468  OG  SER B 307      -5.615   1.601  60.783  1.00 35.53           O
ATOM    469  N   SER B 308      -1.341   0.059  60.910  1.00 33.00           N
ATOM    470  CA  SER B 308      -0.214  -0.626  60.258  1.00 36.33           C
ATOM    471  C   SER B 308      -0.019  -2.014  60.859  1.00 36.89           C
ATOM    472  O   SER B 308       0.227  -2.963  60.142  1.00 39.62           O
ATOM    473  CB  SER B 308       1.084   0.148  60.373  1.00 34.08           C
ATOM    474  OG  SER B 308       1.372   0.411  61.728  1.00 33.71           O
ATOM    475  N   ARG B 309      -0.180  -2.099  62.172  1.00 35.16           N
ATOM    476  CA  ARG B 309       0.014  -3.319  62.933  1.00 37.83           C
ATOM    477  C   ARG B 309      -1.157  -4.276  62.700  1.00 34.13           C
ATOM    478  O   ARG B 309      -0.986  -5.467  62.642  1.00 31.54           O
ATOM    479  CB  ARG B 309       0.165  -2.939  64.408  1.00 40.90           C
ATOM    480  CG  ARG B 309       0.513  -4.054  65.360  1.00 47.32           C
ATOM    481  CD  ARG B 309       0.506  -3.556  66.810  1.00 51.87           C
ATOM    482  NE  ARG B 309      -0.694  -2.792  67.194  1.00 49.37           N
ATOM    483  CZ  ARG B 309      -0.801  -2.066  68.310  1.00 47.13           C
ATOM    484  NH1 ARG B 309       0.210  -1.996  69.162  1.00 49.97           N
ATOM    485  NH2 ARG B 309      -1.913  -1.390  68.568  1.00 46.36           N
ATOM    486  N   SER B 310      -2.361  -3.752  62.550  1.00 33.81           N
ATOM    487  CA  SER B 310      -3.520  -4.636  62.337  1.00 30.19           C
ATOM    488  C   SER B 310      -3.765  -5.042  60.883  1.00 30.54           C
ATOM    489  O   SER B 310      -4.603  -5.913  60.620  1.00 32.03           O
ATOM    490  CB  SER B 310      -4.749  -3.960  62.870  1.00 29.28           C
ATOM    491  OG  SER B 310      -4.965  -2.776  62.126  1.00 28.43           O
ATOM    492  N   ASN B 311      -3.062  -4.410  59.957  1.00 29.39           N
ATOM    493  CA  ASN B 311      -3.340  -4.519  58.534  1.00 32.54           C
ATOM    494  C   ASN B 311      -4.783  -4.106  58.142  1.00 32.20           C
ATOM    495  O   ASN B 311      -5.300  -4.557  57.147  1.00 31.20           O
ATOM    496  CB  ASN B 311      -3.050  -5.923  58.081  1.00 34.63           C
ATOM    497  CG  ASN B 311      -1.650  -6.338  58.442  1.00 37.66           C
ATOM    498  OD1 ASN B 311      -0.691  -5.710  57.973  1.00 38.77           O
ATOM    499  ND2 ASN B 311      -1.511  -7.383  59.279  1.00 34.91           N
ATOM    500  N   ARG B 312      -5.397  -3.243  58.938  1.00 29.67           N
ATOM    501  CA  ARG B 312      -6.747  -2.822  58.708  1.00 30.67           C
ATOM    502  C   ARG B 312      -6.820  -1.374  58.236  1.00 29.28           C
ATOM    503  O   ARG B 312      -5.897  -0.623  58.416  1.00 30.49           O
ATOM    504  CB  ARG B 312      -7.531  -3.068  59.975  1.00 34.66           C
ATOM    505  CG  ARG B 312      -7.511  -4.571  60.252  1.00 38.41           C
ATOM    506  CD  ARG B 312      -8.762  -5.087  60.904  1.00 39.29           C
ATOM    507  NE  ARG B 312      -8.645  -6.498  61.341  1.00 40.11           N
ATOM    508  CZ  ARG B 312      -9.049  -7.576  60.651  1.00 36.13           C
ATOM    509  NH1 ARG B 312      -8.912  -8.783  61.223  1.00 34.35           N
ATOM    510  NH2 ARG B 312      -9.560  -7.477  59.406  1.00 33.52           N
ATOM    511  N   PHE B 313      -7.896  -1.038  57.540  1.00 26.39           N
ATOM    512  CA  PHE B 313      -8.155   0.306  57.019  1.00 25.55           C
ATOM    513  C   PHE B 313      -9.132   1.000  57.905  1.00 25.98           C
ATOM    514  O   PHE B 313     -10.146   0.396  58.275  1.00 24.20           O
ATOM    515  CB  PHE B 313      -8.769   0.202  55.636  1.00 26.07           C
ATOM    516  CG  PHE B 313      -7.909  -0.552  54.663  1.00 26.67           C
ATOM    517  CD1 PHE B 313      -6.528  -0.492  54.756  1.00 26.35           C
ATOM    518  CD2 PHE B 313      -8.484  -1.292  53.641  1.00 26.92           C
ATOM    519  CE1 PHE B 313      -5.720  -1.139  53.822  1.00 29.95           C
ATOM    520  CE2 PHE B 313      -7.681  -1.959  52.720  1.00 28.61           C
ATOM    521  CZ  PHE B 313      -6.297  -1.876  52.815  1.00 27.71           C
ATOM    522  N   THR B 314      -8.839   2.271  58.229  1.00 26.31           N
ATOM    523  CA  THR B 314      -9.456   2.959  59.373  1.00 26.49           C
ATOM    524  C   THR B 314      -9.719   4.428  58.994  1.00 24.25           C
ATOM    525  O   THR B 314      -8.799   5.165  58.648  1.00 24.12           O
ATOM    526  CB  THR B 314      -8.564   2.836  60.656  1.00 25.79           C
ATOM    527  OG1 THR B 314      -8.250   1.453  60.905  1.00 28.48           O
ATOM    528  CG2 THR B 314      -9.226   3.418  61.902  1.00 24.68           C
ATOM    529  N   TRP B 315     -10.986   4.827  59.051  1.00 21.50           N
ATOM    530  CA  TRP B 315     -11.323   6.216  58.815  1.00 23.09           C
ATOM    531  C   TRP B 315     -10.711   7.137  59.851  1.00 23.48           C
ATOM    532  O   TRP B 315     -10.701   6.830  61.030  1.00 23.08           O
ATOM    533  CB  TRP B 315     -12.852   6.467  58.858  1.00 20.88           C
ATOM    534  CG  TRP B 315     -13.618   5.898  57.792  1.00 18.37           C
ATOM    535  CD1 TRP B 315     -14.700   5.065  57.915  1.00 19.52           C
ATOM    536  CD2 TRP B 315     -13.401   6.064  56.376  1.00 18.76           C
ATOM    537  NE1 TRP B 315     -15.148   4.685  56.659  1.00 19.71           N
ATOM    538  CE2 TRP B 315     -14.389   5.316  55.706  1.00 19.03           C
ATOM    539  CE3 TRP B 315     -12.480   6.788  55.611  1.00 20.08           C
ATOM    540  CZ2 TRP B 315     -14.460   5.251  54.299  1.00 19.57           C
ATOM    541  CZ3 TRP B 315     -12.549   6.716  54.232  1.00 19.29           C
ATOM    542  CH2 TRP B 315     -13.539   5.953  53.598  1.00 18.69           C
ATOM    543  N   MET B 316     -10.256   8.304  59.396  1.00 26.75           N
ATOM    544  CA  MET B 316     -10.068   9.460  60.293  1.00 25.60           C
ATOM    545  C   MET B 316     -11.066  10.590  59.930  1.00 26.09           C
ATOM    546  O   MET B 316     -11.709  10.533  58.919  1.00 25.26           O
ATOM    547  CB  MET B 316      -8.639   9.983  60.215  1.00 25.24           C
ATOM    548  CG  MET B 316      -8.319  10.718  58.904  1.00 27.11           C
ATOM    549  SD  MET B 316      -6.562  11.044  58.775  1.00 25.09           S
ATOM    550  CE  MET B 316      -5.990   9.416  58.286  1.00 25.34           C
ATOM    551  N   GLY B 317     -11.168  11.624  60.770  1.00 26.60           N
ATOM    552  CA  GLY B 317     -12.147  12.711  60.593  1.00 23.19           C
ATOM    553  C   GLY B 317     -11.642  13.789  59.669  1.00 23.22           C
ATOM    554  O   GLY B 317     -11.632  14.974  60.016  1.00 22.22           O
ATOM    555  N   LEU B 318     -11.245  13.392  58.471  1.00 22.44           N
ATOM    556  CA  LEU B 318     -10.640  14.314  57.511  1.00 23.53           C
ATOM    557  C   LEU B 318     -11.232  14.067  56.099  1.00 25.04           C
ATOM    558  O   LEU B 318     -11.362  12.903  55.665  1.00 23.53           O
ATOM    559  CB  LEU B 318      -9.143  14.094  57.543  1.00 22.37           C
ATOM    560  CG  LEU B 318      -8.346  14.886  56.559  1.00 24.03           C
ATOM    561  CD1 LEU B 318      -8.321  16.339  57.043  1.00 24.11           C
ATOM    562  CD2 LEU B 318      -6.943  14.316  56.453  1.00 23.79           C
ATOM    563  N   SER B 319     -11.635  15.139  55.412  1.00 25.54           N
ATOM    564  CA  SER B 319     -12.242  15.037  54.080  1.00 26.45           C
ATOM    565  C   SER B 319     -12.026  16.249  53.161  1.00 28.86           C
ATOM    566  O   SER B 319     -11.783  17.373  53.624  1.00 27.48           O
ATOM    567  CB  SER B 319     -13.726  14.760  54.173  1.00 25.87           C
ATOM    568  OG  SER B 319     -14.460  15.878  54.569  1.00 23.45           O
ATOM    569  N   ASP B 320     -12.112  16.002  51.859  1.00 25.87           N
ATOM    570  CA  ASP B 320     -12.199  17.084  50.887  1.00 27.16           C
ATOM    571  C   ASP B 320     -13.542  17.092  50.139  1.00 26.80           C
ATOM    572  O   ASP B 320     -13.631  17.598  49.009  1.00 24.69           O
ATOM    573  CB  ASP B 320     -11.001  17.127  49.935  1.00 25.19           C
ATOM    574  CG  ASP B 320     -11.007  16.031  48.915  1.00 26.07           C
ATOM    575  OD1 ASP B 320     -11.758  15.026  49.066  1.00 21.25           O
ATOM    576  OD2 ASP B 320     -10.271  16.210  47.894  1.00 28.13           O
ATOM    577  N   LEU B 321     -14.567  16.530  50.783  1.00 24.57           N
ATOM    578  CA  LEU B 321     -15.922  16.554  50.270  1.00 25.85           C
ATOM    579  C   LEU B 321     -16.402  17.971  49.909  1.00 28.54           C
ATOM    580  O   LEU B 321     -16.971  18.191  48.842  1.00 34.03           O
ATOM    581  CB  LEU B 321     -16.901  16.001  51.302  1.00 25.14           C
ATOM    582  CG  LEU B 321     -16.962  14.465  51.416  1.00 26.79           C
ATOM    583  CD1 LEU B 321     -17.528  14.049  52.767  1.00 25.99           C
ATOM    584  CD2 LEU B 321     -17.801  13.918  50.285  1.00 26.40           C
ATOM    585  N   ASN B 322     -16.198  18.901  50.826  1.00 28.50           N
ATOM    586  CA AASN B 322     -16.688  20.264  50.674  0.30 28.76           C
ATOM    587  CA BASN B 322     -16.680  20.254  50.653  0.70 32.16           C
ATOM    588  C   ASN B 322     -15.924  20.961  49.534  1.00 30.63           C
ATOM    589  O   ASN B 322     -16.544  21.486  48.643  1.00 31.26           O
ATOM    590  CB AASN B 322     -16.605  21.047  52.006  0.30 27.42           C
ATOM    591  CB BASN B 322     -16.588  21.029  51.962  0.70 34.59           C
ATOM    592  CG AASN B 322     -17.638  20.583  53.049  0.30 26.17           C
ATOM    593  CG BASN B 322     -17.226  22.392  51.868  0.70 39.47           C
ATOM    594  OD1AASN B 322     -18.176  19.480  52.978  0.30 25.40           O
ATOM    595  OD1BASN B 322     -16.670  23.373  52.378  0.70 40.22           O
ATOM    596  ND2AASN B 322     -17.898  21.432  54.034  0.30 25.60           N
ATOM    597  ND2BASN B 322     -18.391  22.476  51.191  0.70 38.50           N
ATOM    598  N   GLN B 323     -14.590  20.891  49.554  1.00 29.80           N
ATOM    599  CA  GLN B 323     -13.708  21.534  48.550  1.00 28.73           C
ATOM    600  C   GLN B 323     -12.645  20.591  48.032  1.00 24.44           C
ATOM    601  O   GLN B 323     -11.668  20.345  48.710  1.00 24.82           O
ATOM    602  CB  GLN B 323     -13.001  22.777  49.167  1.00 30.37           C
ATOM    603  CG  GLN B 323     -13.956  23.771  49.874  1.00 36.06           C
ATOM    604  CD  GLN B 323     -13.241  24.820  50.775  1.00 38.32           C
ATOM    605  OE1 GLN B 323     -12.272  24.491  51.449  1.00 37.03           O
ATOM    606  NE2 GLN B 323     -13.730  26.096  50.765  1.00 36.47           N
ATOM    607  N   GLU B 324     -12.800  20.086  46.810  1.00 27.63           N
ATOM    608  CA  GLU B 324     -11.873  19.098  46.256  1.00 26.82           C
ATOM    609  C   GLU B 324     -10.455  19.623  46.374  1.00 27.53           C
ATOM    610  O   GLU B 324     -10.169  20.750  45.979  1.00 28.67           O
ATOM    611  CB  GLU B 324     -12.208  18.763  44.798  1.00 27.33           C
ATOM    612  CG  GLU B 324     -11.186  17.810  44.156  1.00 27.81           C
ATOM    613  CD  GLU B 324     -11.123  16.435  44.841  1.00 29.64           C
ATOM    614  OE1 GLU B 324     -12.176  15.927  45.335  1.00 32.59           O
ATOM    615  OE2 GLU B 324     -10.011  15.853  44.910  1.00 29.49           O
ATOM    616  N   GLY B 325      -9.561  18.815  46.932  1.00 30.25           N
ATOM    617  CA  GLY B 325      -8.134  19.185  46.999  1.00 28.89           C
ATOM    618  C   GLY B 325      -7.734  19.939  48.261  1.00 29.25           C
ATOM    619  O   GLY B 325      -6.559  20.007  48.544  1.00 28.56           O
ATOM    620  N   THR B 326      -8.718  20.471  48.999  1.00 25.38           N
ATOM    621  CA  THR B 326      -8.492  21.183  50.228  1.00 29.71           C
ATOM    622  C   THR B 326      -9.119  20.375  51.370  1.00 27.01           C
ATOM    623  O   THR B 326     -10.328  20.283  51.475  1.00 23.71           O
ATOM    624  CB  THR B 326      -9.075  22.612  50.165  1.00 30.24           C
ATOM    625  OG1 THR B 326      -8.285  23.399  49.263  1.00 32.61           O
ATOM    626  CG2 THR B 326      -9.042  23.242  51.547  1.00 29.03           C
ATOM    627  N   TRP B 327      -8.252  19.736  52.155  1.00 26.27           N
ATOM    628  CA  TRP B 327      -8.661  18.772  53.185  1.00 25.43           C
ATOM    629  C   TRP B 327      -8.859  19.501  54.508  1.00 25.20           C
ATOM    630  O   TRP B 327      -8.059  20.354  54.886  1.00 25.88           O
ATOM    631  CB  TRP B 327      -7.622  17.659  53.342  1.00 23.86           C
ATOM    632  CG  TRP B 327      -7.532  16.841  52.126  1.00 24.98           C
ATOM    633  CD1 TRP B 327      -6.862  17.130  50.969  1.00 25.33           C
ATOM    634  CD2 TRP B 327      -8.210  15.592  51.906  1.00 24.49           C
ATOM    635  NE1 TRP B 327      -7.068  16.116  50.049  1.00 26.05           N
ATOM    636  CE2 TRP B 327      -7.897  15.169  50.603  1.00 24.61           C
ATOM    637  CE3 TRP B 327      -9.071  14.814  52.687  1.00 26.52           C
ATOM    638  CZ2 TRP B 327      -8.397  14.000  50.065  1.00 25.81           C
ATOM    639  CZ3 TRP B 327      -9.564  13.622  52.168  1.00 29.81           C
ATOM    640  CH2 TRP B 327      -9.217  13.229  50.849  1.00 26.99           C
ATOM    641  N   GLN B 328      -9.917  19.115  55.192  1.00 24.25           N
ATOM    642  CA  GLN B 328     -10.389  19.754  56.371  1.00 29.08           C
ATOM    643  C   GLN B 328     -10.799  18.705  57.387  1.00 25.97           C
ATOM    644  O   GLN B 328     -11.478  17.727  57.060  1.00 25.83           O
ATOM    645  CB  GLN B 328     -11.619  20.507  55.934  1.00 36.30           C
ATOM    646  CG  GLN B 328     -12.208  21.465  56.914  1.00 45.35           C
ATOM    647  CD  GLN B 328     -13.341  22.226  56.275  1.00 49.57           C
ATOM    648  OE1 GLN B 328     -14.325  22.547  56.943  1.00 57.93           O
ATOM    649  NE2 GLN B 328     -13.214  22.512  54.954  1.00 49.81           N
ATOM    650  N   TRP B 329     -10.439  18.940  58.630  1.00 26.20           N
ATOM    651  CA  TRP B 329     -10.834  18.064  59.724  1.00 26.34           C
ATOM    652  C   TRP B 329     -12.269  18.319  60.075  1.00 25.90           C
ATOM    653  O   TRP B 329     -12.767  19.396  59.871  1.00 27.99           O
ATOM    654  CB  TRP B 329      -9.940  18.246  60.948  1.00 25.42           C
ATOM    655  CG  TRP B 329      -8.543  17.925  60.705  1.00 24.68           C
ATOM    656  CD1 TRP B 329      -7.545  18.798  60.408  1.00 24.70           C
ATOM    657  CD2 TRP B 329      -7.949  16.612  60.700  1.00 26.08           C
ATOM    658  NE1 TRP B 329      -6.365  18.119  60.240  1.00 26.06           N
ATOM    659  CE2 TRP B 329      -6.590  16.774  60.403  1.00 25.19           C
ATOM    660  CE3 TRP B 329      -8.450  15.321  60.895  1.00 24.22           C
ATOM    661  CZ2 TRP B 329      -5.717  15.687  60.295  1.00 28.51           C
ATOM    662  CZ3 TRP B 329      -7.594  14.255  60.794  1.00 24.53           C
ATOM    663  CH2 TRP B 329      -6.241  14.427  60.522  1.00 24.23           C
ATOM    664  N   VAL B 330     -12.944  17.322  60.624  1.00 28.41           N
ATOM    665  CA  VAL B 330     -14.363  17.477  60.895  1.00 30.47           C
ATOM    666  C   VAL B 330     -14.677  18.504  62.002  1.00 30.09           C
ATOM    667  O   VAL B 330     -15.826  18.853  62.166  1.00 28.73           O
ATOM    668  CB  VAL B 330     -15.054  16.178  61.284  1.00 31.47           C
ATOM    669  CG1 VAL B 330     -15.005  15.208  60.128  1.00 33.13           C
ATOM    670  CG2 VAL B 330     -14.441  15.621  62.555  1.00 30.57           C
ATOM    671  N   ASP B 331     -13.678  18.960  62.748  1.00 29.10           N
ATOM    672  CA  ASP B 331     -13.867  20.091  63.657  1.00 30.07           C
ATOM    673  C   ASP B 331     -13.699  21.438  62.928  1.00 30.68           C
ATOM    674  O   ASP B 331     -13.845  22.474  63.531  1.00 33.39           O
ATOM    675  CB  ASP B 331     -12.904  20.020  64.844  1.00 28.54           C
ATOM    676  CG  ASP B 331     -11.469  20.237  64.438  1.00 31.65           C
ATOM    677  OD1 ASP B 331     -11.234  20.359  63.203  1.00 36.23           O
ATOM    678  OD2 ASP B 331     -10.549  20.238  65.312  1.00 29.69           O
ATOM    679  N   GLY B 332     -13.354  21.431  61.649  1.00 27.95           N
ATOM    680  CA  GLY B 332     -13.269  22.660  60.898  1.00 26.85           C
ATOM    681  C   GLY B 332     -11.848  23.066  60.642  1.00 28.46           C
ATOM    682  O   GLY B 332     -11.573  23.959  59.782  1.00 32.13           O
ATOM    683  N   SER B 333     -10.918  22.463  61.372  1.00 26.57           N
ATOM    684  CA  SER B 333      -9.528  22.921  61.277  1.00 28.23           C
ATOM    685  C   SER B 333      -8.973  22.485  59.889  1.00 27.85           C
ATOM    686  O   SER B 333      -9.498  21.599  59.268  1.00 29.36           O
ATOM    687  CB  SER B 333      -8.688  22.417  62.471  1.00 28.70           C
ATOM    688  OG  SER B 333      -8.748  20.982  62.653  1.00 31.22           O
ATOM    689  N   PRO B 334      -7.978  23.174  59.383  1.00 28.71           N
ATOM    690  CA  PRO B 334      -7.333  22.834  58.124  1.00 27.11           C
ATOM    691  C   PRO B 334      -6.306  21.720  58.278  1.00 29.32           C
ATOM    692  O   PRO B 334      -5.820  21.438  59.384  1.00 28.85           O
ATOM    693  CB  PRO B 334      -6.633  24.152  57.729  1.00 29.82           C
ATOM    694  CG  PRO B 334      -6.390  24.862  59.028  1.00 30.10           C
ATOM    695  CD  PRO B 334      -7.558  24.488  59.919  1.00 29.87           C
ATOM    696  N   LEU B 335      -5.994  21.051  57.175  1.00 30.05           N
ATOM    697  CA  LEU B 335      -4.854  20.192  57.143  1.00 29.79           C
ATOM    698  C   LEU B 335      -3.627  21.063  57.045  1.00 32.28           C
ATOM    699  O   LEU B 335      -3.409  21.725  56.029  1.00 36.20           O
ATOM    700  CB  LEU B 335      -4.891  19.234  55.943  1.00 30.58           C
ATOM    701  CG  LEU B 335      -3.832  18.130  55.901  1.00 28.44           C
ATOM    702  CD1 LEU B 335      -3.855  17.312  57.170  1.00 30.60           C
ATOM    703  CD2 LEU B 335      -4.079  17.227  54.716  1.00 30.96           C
ATOM    704  N   LEU B 336      -2.791  21.015  58.063  1.00 34.70           N
ATOM    705  CA  LEU B 336      -1.560  21.818  58.088  1.00 36.54           C
ATOM    706  C   LEU B 336      -0.472  21.227  57.206  1.00 39.53           C
ATOM    707  O   LEU B 336      -0.396  19.991  57.055  1.00 37.00           O
ATOM    708  CB  LEU B 336      -1.009  21.899  59.504  1.00 35.78           C
ATOM    709  CG  LEU B 336      -1.933  22.501  60.548  1.00 36.80           C
ATOM    710  CD1 LEU B 336      -1.287  22.263  61.901  1.00 37.60           C
ATOM    711  CD2 LEU B 336      -2.188  23.991  60.307  1.00 37.57           C
ATOM    712  N   PRO B 337       0.398  22.094  56.646  1.00 39.37           N
ATOM    713  CA  PRO B 337       1.389  21.614  55.696  1.00 38.70           C
ATOM    714  C   PRO B 337       2.320  20.612  56.282  1.00 36.19           C
ATOM    715  O   PRO B 337       2.745  19.694  55.586  1.00 36.15           O
ATOM    716  CB  PRO B 337       2.143  22.887  55.290  1.00 41.78           C
ATOM    717  CG  PRO B 337       1.121  23.970  55.415  1.00 42.66           C
ATOM    718  CD  PRO B 337       0.299  23.569  56.620  1.00 43.62           C
ATOM    719  N   SER B 338       2.593  20.726  57.567  1.00 38.73           N
ATOM    720  CA  SER B 338       3.489  19.764  58.222  1.00 40.69           C
ATOM    721  C   SER B 338       2.880  18.341  58.289  1.00 41.97           C
ATOM    722  O   SER B 338       3.603  17.408  58.557  1.00 44.32           O
ATOM    723  CB  SER B 338       3.874  20.236  59.619  1.00 39.18           C
ATOM    724  OG  SER B 338       2.742  20.301  60.464  1.00 45.18           O
ATOM    725  N   PHE B 339       1.568  18.190  58.067  1.00 39.26           N
ATOM    726  CA  PHE B 339       0.912  16.859  58.098  1.00 38.19           C
ATOM    727  C   PHE B 339       0.871  16.183  56.723  1.00 38.03           C
ATOM    728  O   PHE B 339       0.584  14.987  56.623  1.00 34.17           O
ATOM    729  CB  PHE B 339      -0.499  16.956  58.687  1.00 36.31           C
ATOM    730  CG  PHE B 339      -0.508  17.163  60.167  1.00 40.23           C
ATOM    731  CD1 PHE B 339       0.050  18.307  60.730  1.00 41.06           C
ATOM    732  CD2 PHE B 339      -1.054  16.216  61.010  1.00 43.59           C
ATOM    733  CE1 PHE B 339       0.054  18.503  62.097  1.00 42.02           C
ATOM    734  CE2 PHE B 339      -1.049  16.404  62.389  1.00 44.50           C
ATOM    735  CZ  PHE B 339      -0.494  17.549  62.931  1.00 42.30           C
ATOM    736  N   LYS B 340       1.168  16.929  55.660  1.00 34.86           N
ATOM    737  CA  LYS B 340       1.004  16.389  54.313  1.00 34.25           C
ATOM    738  C   LYS B 340       1.969  15.260  54.077  1.00 32.67           C
ATOM    739  O   LYS B 340       1.725  14.377  53.242  1.00 34.37           O
ATOM    740  CB  LYS B 340       1.188  17.481  53.242  1.00 37.96           C
ATOM    741  CG  LYS B 340       0.036  18.478  53.156  1.00 43.21           C
ATOM    742  CD  LYS B 340       0.300  19.558  52.107  1.00 50.48           C
ATOM    743  CE  LYS B 340      -0.910  20.495  51.908  1.00 60.03           C
ATOM    744  NZ  LYS B 340      -1.489  21.089  53.160  1.00 58.85           N
ATOM    745  N   GLN B 341       3.092  15.291  54.780  1.00 29.15           N
ATOM    746  CA  GLN B 341       4.047  14.214  54.724  1.00 31.50           C
ATOM    747  C   GLN B 341       3.444  12.816  55.040  1.00 32.22           C
ATOM    748  O   GLN B 341       3.999  11.806  54.623  1.00 29.98           O
ATOM    749  CB  GLN B 341       5.191  14.489  55.700  1.00 33.45           C
ATOM    750  CG  GLN B 341       4.773  14.452  57.171  1.00 36.03           C
ATOM    751  CD  GLN B 341       5.973  14.629  58.100  1.00 40.35           C
ATOM    752  OE1 GLN B 341       6.803  13.732  58.197  1.00 39.47           O
ATOM    753  NE2 GLN B 341       6.062  15.788  58.791  1.00 37.00           N
ATOM    754  N   TYR B 342       2.335  12.756  55.794  1.00 31.86           N
ATOM    755  CA  TYR B 342       1.724  11.452  56.130  1.00 32.24           C
ATOM    756  C   TYR B 342       0.922  10.746  55.014  1.00 31.03           C
ATOM    757  O   TYR B 342       0.697   9.532  55.094  1.00 34.05           O
ATOM    758  CB  TYR B 342       0.889  11.538  57.415  1.00 30.80           C
ATOM    759  CG  TYR B 342       1.667  12.061  58.580  1.00 29.88           C
ATOM    760  CD1 TYR B 342       2.848  11.457  58.985  1.00 32.01           C
ATOM    761  CD2 TYR B 342       1.258  13.207  59.232  1.00 28.90           C
ATOM    762  CE1 TYR B 342       3.589  11.981  60.032  1.00 32.26           C
ATOM    763  CE2 TYR B 342       1.961  13.727  60.260  1.00 30.46           C
ATOM    764  CZ  TYR B 342       3.135  13.122  60.676  1.00 32.40           C
ATOM    765  OH  TYR B 342       3.791  13.669  61.769  1.00 29.92           O
ATOM    766  N   TRP B 343       0.495  11.464  53.993  1.00 27.71           N
ATOM    767  CA  TRP B 343      -0.093  10.823  52.839  1.00 30.01           C
ATOM    768  C   TRP B 343       0.864   9.776  52.305  1.00 29.72           C
ATOM    769  O   TRP B 343       2.039  10.072  52.187  1.00 29.13           O
ATOM    770  CB  TRP B 343      -0.348  11.824  51.709  1.00 29.01           C
ATOM    771  CG  TRP B 343      -1.460  12.803  51.971  1.00 29.61           C
ATOM    772  CD1 TRP B 343      -1.349  14.161  52.094  1.00 28.78           C
ATOM    773  CD2 TRP B 343      -2.846  12.502  52.095  1.00 26.44           C
ATOM    774  NE1 TRP B 343      -2.583  14.713  52.304  1.00 27.33           N
ATOM    775  CE2 TRP B 343      -3.515  13.712  52.306  1.00 26.10           C
ATOM    776  CE3 TRP B 343      -3.588  11.308  52.066  1.00 27.33           C
ATOM    777  CZ2 TRP B 343      -4.893  13.784  52.471  1.00 26.54           C
ATOM    778  CZ3 TRP B 343      -4.949  11.381  52.246  1.00 26.36           C
ATOM    779  CH2 TRP B 343      -5.586  12.620  52.438  1.00 28.30           C
ATOM    780  N   ASN B 344       0.372   8.571  52.008  1.00 27.28           N
ATOM    781  CA  ASN B 344       1.172   7.586  51.297  1.00 30.60           C
ATOM    782  C   ASN B 344       1.626   8.198  49.952  1.00 32.24           C
ATOM    783  O   ASN B 344       1.026   9.169  49.432  1.00 31.87           O
ATOM    784  CB  ASN B 344       0.440   6.245  51.027  1.00 30.10           C
ATOM    785  CG  ASN B 344       0.039   5.508  52.290  1.00 29.93           C
ATOM    786  OD1 ASN B 344       0.748   5.544  53.305  1.00 31.39           O
ATOM    787  ND2 ASN B 344      -1.083   4.797  52.224  1.00 25.03           N
ATOM    788  N   ARG B 345       2.698   7.630  49.421  1.00 33.51           N
ATOM    789  CA  ARG B 345       3.258   8.068  48.149  1.00 37.97           C
ATOM    790  C   ARG B 345       2.185   7.997  47.057  1.00 33.77           C
ATOM    791  O   ARG B 345       1.489   6.989  46.889  1.00 34.63           O
ATOM    792  CB  ARG B 345       4.511   7.241  47.789  1.00 46.02           C
ATOM    793  CG  ARG B 345       5.016   7.423  46.347  1.00 56.96           C
ATOM    794  CD  ARG B 345       6.066   6.397  45.901  1.00 62.98           C
ATOM    795  NE  ARG B 345       7.425   6.889  46.157  1.00 73.94           N
ATOM    796  CZ  ARG B 345       8.056   6.841  47.335  1.00 77.58           C
ATOM    797  NH1 ARG B 345       7.476   6.306  48.413  1.00 80.99           N
ATOM    798  NH2 ARG B 345       9.293   7.325  47.440  1.00 76.48           N
ATOM    799  N   GLY B 346       2.052   9.101  46.335  1.00 30.07           N
ATOM    800  CA  GLY B 346       1.076   9.253  45.275  1.00 29.53           C
ATOM    801  C   GLY B 346      -0.292   9.706  45.765  1.00 30.25           C
ATOM    802  O   GLY B 346      -1.204   9.849  44.960  1.00 35.58           O
ATOM    803  N   GLU B 347      -0.460   9.933  47.067  1.00 28.34           N
ATOM    804  CA  GLU B 347      -1.771  10.324  47.573  1.00 27.71           C
ATOM    805  C   GLU B 347      -1.751  11.783  47.966  1.00 27.68           C
ATOM    806  O   GLU B 347      -0.683  12.345  48.145  1.00 28.34           O
ATOM    807  CB  GLU B 347      -2.174   9.431  48.747  1.00 25.42           C
ATOM    808  CG  GLU B 347      -2.144   7.933  48.368  1.00 25.73           C
ATOM    809  CD  GLU B 347      -3.145   7.497  47.271  1.00 26.30           C
ATOM    810  OE1 GLU B 347      -4.041   8.272  46.878  1.00 26.24           O
ATOM    811  OE2 GLU B 347      -3.072   6.318  46.810  1.00 24.30           O
ATOM    812  N   PRO B 348      -2.896  12.444  48.081  1.00 28.01           N
ATOM    813  CA  PRO B 348      -4.219  11.979  47.650  1.00 27.06           C
ATOM    814  C   PRO B 348      -4.347  12.090  46.142  1.00 29.33           C
ATOM    815  O   PRO B 348      -3.897  13.052  45.589  1.00 31.53           O
ATOM    816  CB  PRO B 348      -5.162  12.973  48.340  1.00 27.70           C
ATOM    817  CG  PRO B 348      -4.354  14.211  48.596  1.00 27.85           C
ATOM    818  CD  PRO B 348      -2.892  13.831  48.586  1.00 26.69           C
ATOM    819  N   ASN B 349      -4.942  11.106  45.490  1.00 27.71           N
ATOM    820  CA  ASN B 349      -5.015  11.085  44.043  1.00 26.25           C
ATOM    821  C   ASN B 349      -6.463  11.288  43.550  1.00 26.54           C
ATOM    822  O   ASN B 349      -6.676  11.470  42.393  1.00 22.31           O
ATOM    823  CB  ASN B 349      -4.378   9.820  43.469  1.00 25.25           C
ATOM    824  CG  ASN B 349      -4.997   8.545  44.016  1.00 26.92           C
ATOM    825  OD1 ASN B 349      -5.884   8.577  44.870  1.00 22.47           O
ATOM    826  ND2 ASN B 349      -4.509   7.405  43.537  1.00 25.90           N
ATOM    827  N   ASN B 350      -7.458  11.280  44.432  1.00 25.19           N
ATOM    828  CA  ASN B 350      -8.849  11.466  43.988  1.00 25.12           C
ATOM    829  C   ASN B 350      -9.314  10.465  42.926  1.00 25.59           C
ATOM    830  O   ASN B 350     -10.309  10.667  42.238  1.00 29.22           O
ATOM    831  CB  ASN B 350      -9.066  12.899  43.472  1.00 25.55           C
ATOM    832  CG  ASN B 350     -10.531  13.303  43.534  1.00 26.89           C
ATOM    833  OD1 ASN B 350     -11.219  12.998  44.514  1.00 28.45           O
ATOM    834  ND2 ASN B 350     -11.016  13.964  42.504  1.00 23.12           N
ATOM    835  N   VAL B 351      -8.641   9.333  42.830  1.00 26.99           N
ATOM    836  CA  VAL B 351      -8.948   8.411  41.772  1.00 25.29           C
ATOM    837  C   VAL B 351     -10.391   7.865  41.839  1.00 26.85           C
ATOM    838  O   VAL B 351     -10.765   7.190  42.757  1.00 26.38           O
ATOM    839  CB  VAL B 351      -7.876   7.322  41.667  1.00 25.53           C
ATOM    840  CG1 VAL B 351      -7.834   6.440  42.922  1.00 25.57           C
ATOM    841  CG2 VAL B 351      -8.102   6.554  40.369  1.00 28.70           C
ATOM    842  N   GLY B 352     -11.193   8.185  40.834  1.00 28.47           N
ATOM    843  CA  GLY B 352     -12.598   7.821  40.825  1.00 30.13           C
ATOM    844  C   GLY B 352     -13.450   8.647  41.805  1.00 33.03           C
ATOM    845  O   GLY B 352     -14.585   8.255  42.126  1.00 30.13           O
ATOM    846  N   GLU B 353     -12.898   9.777  42.274  1.00 30.46           N
ATOM    847  CA  GLU B 353     -13.540  10.604  43.328  1.00 33.41           C
ATOM    848  C   GLU B 353     -13.376   9.966  44.697  1.00 27.97           C
ATOM    849  O   GLU B 353     -14.080   9.064  45.061  1.00 32.28           O
ATOM    850  CB  GLU B 353     -15.022  10.976  43.019  1.00 31.38           C
ATOM    851  CG  GLU B 353     -15.112  12.106  42.009  1.00 36.41           C
ATOM    852  CD  GLU B 353     -16.536  12.620  41.742  1.00 39.17           C
ATOM    853  OE1 GLU B 353     -16.739  13.164  40.647  1.00 45.25           O
ATOM    854  OE2 GLU B 353     -17.442  12.502  42.605  1.00 39.59           O
ATOM    855  N   GLU B 354     -12.382  10.434  45.440  1.00 28.87           N
ATOM    856  CA  GLU B 354     -12.113   9.910  46.773  1.00 25.18           C
ATOM    857  C   GLU B 354     -12.072  11.101  47.628  1.00 27.07           C
ATOM    858  O   GLU B 354     -11.196  11.960  47.449  1.00 26.89           O
ATOM    859  CB  GLU B 354     -10.786   9.140  46.842  1.00 24.55           C
ATOM    860  CG  GLU B 354     -10.749   7.939  45.871  1.00 24.60           C
ATOM    861  CD  GLU B 354      -9.484   7.102  45.939  1.00 23.81           C
ATOM    862  OE1 GLU B 354      -8.361   7.696  45.899  1.00 18.90           O
ATOM    863  OE2 GLU B 354      -9.621   5.836  46.040  1.00 23.34           O
ATOM    864  N   ASP B 355     -12.990  11.180  48.590  1.00 27.56           N
ATOM    865  CA  ASP B 355     -13.058  12.417  49.416  1.00 28.40           C
ATOM    866  C   ASP B 355     -12.908  12.227  50.949  1.00 28.90           C
ATOM    867  O   ASP B 355     -12.947  13.221  51.686  1.00 28.10           O
ATOM    868  CB  ASP B 355     -14.343  13.213  49.056  1.00 27.90           C
ATOM    869  CG  ASP B 355     -14.378  13.696  47.603  1.00 28.71           C
ATOM    870  OD1 ASP B 355     -13.328  13.774  46.894  1.00 28.71           O
ATOM    871  OD2 ASP B 355     -15.513  13.992  47.114  1.00 32.32           O
ATOM    872  N   CYS B 356     -12.720  10.978  51.436  1.00 24.58           N
ATOM    873  CA  CYS B 356     -12.499  10.745  52.860  1.00 25.02           C
ATOM    874  C   CYS B 356     -11.160  10.086  53.143  1.00 23.12           C
ATOM    875  O   CYS B 356     -10.707   9.210  52.387  1.00 23.91           O
ATOM    876  CB  CYS B 356     -13.649   9.961  53.499  1.00 25.13           C
ATOM    877  SG  CYS B 356     -15.224  10.807  53.302  1.00 27.75           S
ATOM    878  N   ALA B 357     -10.500  10.536  54.205  1.00 20.26           N
ATOM    879  CA  ALA B 357      -9.142  10.023  54.537  1.00 21.13           C
ATOM    880  C   ALA B 357      -9.128   8.792  55.441  1.00 21.40           C
ATOM    881  O   ALA B 357      -9.829   8.719  56.467  1.00 23.07           O
ATOM    882  CB  ALA B 357      -8.288  11.113  55.159  1.00 20.32           C
ATOM    883  N   GLU B 358      -8.295   7.852  55.069  1.00 19.85           N
ATOM    884  CA  GLU B 358      -8.079   6.591  55.852  1.00 22.47           C
ATOM    885  C   GLU B 358      -6.596   6.392  56.259  1.00 22.31           C
ATOM    886  O   GLU B 358      -5.699   6.852  55.557  1.00 21.76           O
ATOM    887  CB  GLU B 358      -8.514   5.376  55.037  1.00 23.86           C
ATOM    888  CG  GLU B 358      -7.709   5.158  53.768  1.00 26.11           C
ATOM    889  CD  GLU B 358      -7.922   3.793  53.147  1.00 27.52           C
ATOM    890  OE1 GLU B 358      -7.566   3.635  51.955  1.00 29.38           O
ATOM    891  OE2 GLU B 358      -8.469   2.891  53.818  1.00 23.85           O
ATOM    892  N   PHE B 359      -6.364   5.748  57.397  1.00 24.37           N
ATOM    893  CA  PHE B 359      -5.065   5.099  57.731  1.00 24.61           C
ATOM    894  C   PHE B 359      -4.977   3.846  56.895  1.00 25.17           C
ATOM    895  O   PHE B 359      -5.868   3.020  56.966  1.00 23.53           O
ATOM    896  CB  PHE B 359      -4.971   4.688  59.193  1.00 25.77           C
ATOM    897  CG  PHE B 359      -5.151   5.819  60.140  1.00 25.94           C
ATOM    898  CD1 PHE B 359      -4.111   6.722  60.355  1.00 25.84           C
ATOM    899  CD2 PHE B 359      -6.351   6.000  60.801  1.00 25.71           C
ATOM    900  CE1 PHE B 359      -4.268   7.791  61.215  1.00 28.55           C
ATOM    901  CE2 PHE B 359      -6.522   7.071  61.665  1.00 29.73           C
ATOM    902  CZ  PHE B 359      -5.469   7.965  61.894  1.00 28.94           C
ATOM    903  N   SER B 360      -3.936   3.739  56.077  1.00 24.83           N
ATOM    904  CA  SER B 360      -3.738   2.613  55.190  1.00 28.51           C
ATOM    905  C   SER B 360      -2.247   2.261  55.097  1.00 28.84           C
ATOM    906  O   SER B 360      -1.488   2.969  54.477  1.00 31.95           O
ATOM    907  CB  SER B 360      -4.267   2.944  53.827  1.00 30.31           C
ATOM    908  OG  SER B 360      -4.087   1.855  52.959  1.00 36.19           O
ATOM    909  N   GLY B 361      -1.844   1.156  55.702  1.00 30.55           N
ATOM    910  CA  GLY B 361      -0.423   0.797  55.778  1.00 30.93           C
ATOM    911  C   GLY B 361       0.324   1.729  56.699  1.00 30.62           C
ATOM    912  O   GLY B 361      -0.038   1.913  57.882  1.00 28.13           O
ATOM    913  N   ASN B 362       1.329   2.393  56.159  1.00 31.44           N
ATOM    914  CA  ASN B 362       2.170   3.252  56.993  1.00 33.10           C
ATOM    915  C   ASN B 362       1.776   4.712  57.030  1.00 33.32           C
ATOM    916  O   ASN B 362       2.316   5.460  57.820  1.00 33.54           O
ATOM    917  CB  ASN B 362       3.620   3.068  56.558  1.00 36.83           C
ATOM    918  CG  ASN B 362       4.066   1.629  56.756  1.00 40.39           C
ATOM    919  OD1 ASN B 362       4.591   1.005  55.852  1.00 43.01           O
ATOM    920  ND2 ASN B 362       3.743   1.064  57.924  1.00 41.29           N
ATOM    921  N   GLY B 363       0.815   5.095  56.193  1.00 32.09           N
ATOM    922  CA  GLY B 363       0.347   6.462  56.088  1.00 30.58           C
ATOM    923  C   GLY B 363      -1.127   6.538  55.687  1.00 27.29           C
ATOM    924  O   GLY B 363      -1.907   5.609  55.877  1.00 25.88           O
ATOM    925  N   TRP B 364      -1.483   7.670  55.123  1.00 28.79           N
ATOM    926  CA  TRP B 364      -2.867   7.994  54.775  1.00 26.68           C
ATOM    927  C   TRP B 364      -3.207   7.783  53.329  1.00 25.02           C
ATOM    928  O   TRP B 364      -2.374   7.979  52.454  1.00 23.95           O
ATOM    929  CB  TRP B 364      -3.093   9.449  55.026  1.00 28.99           C
ATOM    930  CG  TRP B 364      -2.811   9.923  56.372  1.00 30.19           C
ATOM    931  CD1 TRP B 364      -2.473   9.195  57.460  1.00 29.17           C
ATOM    932  CD2 TRP B 364      -2.950  11.271  56.804  1.00 31.19           C
ATOM    933  NE1 TRP B 364      -2.371  10.012  58.545  1.00 31.12           N
ATOM    934  CE2 TRP B 364      -2.654  11.296  58.169  1.00 30.46           C
ATOM    935  CE3 TRP B 364      -3.282  12.466  56.154  1.00 32.65           C
ATOM    936  CZ2 TRP B 364      -2.639  12.471  58.906  1.00 32.19           C
ATOM    937  CZ3 TRP B 364      -3.297  13.638  56.893  1.00 34.23           C
ATOM    938  CH2 TRP B 364      -2.965  13.630  58.258  1.00 31.97           C
ATOM    939  N   ASN B 365      -4.472   7.479  53.063  1.00 24.53           N
ATOM    940  CA  ASN B 365      -4.960   7.474  51.686  1.00 25.34           C
ATOM    941  C   ASN B 365      -6.277   8.167  51.616  1.00 22.88           C
ATOM    942  O   ASN B 365      -7.071   8.092  52.553  1.00 20.42           O
ATOM    943  CB  ASN B 365      -5.166   5.998  51.280  1.00 26.71           C
ATOM    944  CG  ASN B 365      -5.673   5.813  49.877  1.00 26.66           C
ATOM    945  OD1 ASN B 365      -5.257   6.512  48.937  1.00 27.39           O
ATOM    946  ND2 ASN B 365      -6.585   4.845  49.712  1.00 25.75           N
ATOM    947  N   ASP B 366      -6.587   8.736  50.462  1.00 20.95           N
ATOM    948  CA  ASP B 366      -7.973   9.160  50.231  1.00 20.45           C
ATOM    949  C   ASP B 366      -8.693   7.986  49.593  1.00 21.99           C
ATOM    950  O   ASP B 366      -8.123   7.350  48.728  1.00 16.92           O
ATOM    951  CB  ASP B 366      -8.051  10.427  49.407  1.00 19.77           C
ATOM    952  CG  ASP B 366      -7.324  10.326  48.006  1.00 21.82           C
ATOM    953  OD1 ASP B 366      -6.389   9.527  47.785  1.00 20.58           O
ATOM    954  OD2 ASP B 366      -7.744  11.085  47.130  1.00 23.37           O
ATOM    955  N   ASP B 367      -9.905   7.668  50.075  1.00 21.04           N
ATOM    956  CA  ASP B 367     -10.677   6.581  49.527  1.00 22.94           C
ATOM    957  C   ASP B 367     -12.131   7.020  49.404  1.00 23.14           C
ATOM    958  O   ASP B 367     -12.485   8.120  49.835  1.00 17.60           O
ATOM    959  CB  ASP B 367     -10.537   5.313  50.383  1.00 25.34           C
ATOM    960  CG  ASP B 367     -10.850   4.019  49.586  1.00 27.21           C
ATOM    961  OD1 ASP B 367     -11.297   4.125  48.429  1.00 26.44           O
ATOM    962  OD2 ASP B 367     -10.656   2.907  50.131  1.00 28.09           O
ATOM    963  N   LYS B 368     -12.965   6.158  48.823  1.00 22.09           N
ATOM    964  CA  LYS B 368     -14.387   6.486  48.634  1.00 24.24           C
ATOM    965  C   LYS B 368     -15.149   6.494  49.958  1.00 23.42           C
ATOM    966  O   LYS B 368     -15.190   5.500  50.675  1.00 20.85           O
ATOM    967  CB  LYS B 368     -15.084   5.560  47.639  1.00 25.90           C
ATOM    968  CG  LYS B 368     -14.431   5.436  46.236  1.00 30.79           C
ATOM    969  CD  LYS B 368     -15.074   4.208  45.633  1.00 38.91           C
ATOM    970  CE  LYS B 368     -14.782   3.955  44.174  1.00 47.06           C
ATOM    971  NZ  LYS B 368     -13.370   3.525  44.029  1.00 50.74           N
ATOM    972  N   CYS B 369     -15.790   7.632  50.227  1.00 24.43           N
ATOM    973  CA  CYS B 369     -16.533   7.869  51.462  1.00 22.21           C
ATOM    974  C   CYS B 369     -17.611   6.807  51.788  1.00 22.75           C
ATOM    975  O   CYS B 369     -17.945   6.575  52.934  1.00 21.30           O
ATOM    976  CB  CYS B 369     -17.120   9.267  51.390  1.00 25.54           C
ATOM    977  SG  CYS B 369     -15.841  10.590  51.357  1.00 28.56           S
ATOM    978  N   ASN B 370     -18.129   6.135  50.779  1.00 21.23           N
ATOM    979  CA  ASN B 370     -19.243   5.253  50.949  1.00 24.52           C
ATOM    980  C   ASN B 370     -18.784   3.811  51.247  1.00 23.43           C
ATOM    981  O   ASN B 370     -19.591   2.954  51.487  1.00 24.84           O
ATOM    982  CB  ASN B 370     -20.175   5.347  49.729  1.00 27.62           C
ATOM    983  CG  ASN B 370     -19.409   5.199  48.409  1.00 33.88           C
ATOM    984  OD1 ASN B 370     -18.750   6.144  47.927  1.00 46.73           O
ATOM    985  ND2 ASN B 370     -19.408   4.016  47.887  1.00 34.05           N
ATOM    986  N   LEU B 371     -17.480   3.564  51.280  1.00 24.67           N
ATOM    987  CA  LEU B 371     -16.960   2.261  51.713  1.00 25.40           C
ATOM    988  C   LEU B 371     -16.979   2.089  53.228  1.00 21.58           C
ATOM    989  O   LEU B 371     -16.983   3.045  54.010  1.00 21.68           O
ATOM    990  CB  LEU B 371     -15.560   1.968  51.102  1.00 26.64           C
ATOM    991  CG  LEU B 371     -15.533   1.980  49.555  1.00 27.15           C
ATOM    992  CD1 LEU B 371     -14.104   1.805  49.039  1.00 27.97           C
ATOM    993  CD2 LEU B 371     -16.476   0.958  48.871  1.00 29.94           C
ATOM    994  N   ALA B 372     -17.053   0.846  53.633  1.00 22.34           N
ATOM    995  CA  ALA B 372     -17.048   0.481  55.040  1.00 24.74           C
ATOM    996  C   ALA B 372     -15.590   0.258  55.525  1.00 22.99           C
ATOM    997  O   ALA B 372     -14.804  -0.417  54.875  1.00 24.81           O
ATOM    998  CB  ALA B 372     -17.882  -0.778  55.229  1.00 26.76           C
ATOM    999  N   LYS B 373     -15.229   0.912  56.623  1.00 23.86           N
ATOM   1000  CA  LYS B 373     -13.921   0.769  57.215  1.00 22.59           C
ATOM   1001  C   LYS B 373     -14.096   0.813  58.705  1.00 23.18           C
ATOM   1002  O   LYS B 373     -15.118   1.229  59.190  1.00 24.81           O
ATOM   1003  CB  LYS B 373     -13.043   1.917  56.773  1.00 24.01           C
ATOM   1004  CG  LYS B 373     -12.689   1.890  55.309  1.00 23.51           C
ATOM   1005  CD  LYS B 373     -11.848   3.049  54.880  1.00 24.20           C
ATOM   1006  CE  LYS B 373     -11.794   3.159  53.347  1.00 24.82           C
ATOM   1007  NZ  LYS B 373     -10.880   2.122  52.859  1.00 25.22           N
ATOM   1008  N   PHE B 374     -13.051   0.458  59.432  1.00 24.59           N
ATOM   1009  CA  PHE B 374     -12.995   0.635  60.875  1.00 23.56           C
ATOM   1010  C   PHE B 374     -12.918   2.119  61.134  1.00 21.88           C
ATOM   1011  O   PHE B 374     -12.583   2.866  60.264  1.00 20.44           O
ATOM   1012  CB  PHE B 374     -11.790  -0.112  61.451  1.00 23.80           C
ATOM   1013  CG  PHE B 374     -11.947  -1.591  61.360  1.00 23.70           C
ATOM   1014  CD1 PHE B 374     -11.552  -2.251  60.227  1.00 25.94           C
ATOM   1015  CD2 PHE B 374     -12.606  -2.265  62.334  1.00 22.47           C
ATOM   1016  CE1 PHE B 374     -11.757  -3.608  60.083  1.00 27.68           C
ATOM   1017  CE2 PHE B 374     -12.831  -3.599  62.225  1.00 25.12           C
ATOM   1018  CZ  PHE B 374     -12.416  -4.279  61.087  1.00 26.11           C
ATOM   1019  N   TRP B 375     -13.285   2.553  62.321  1.00 21.11           N
ATOM   1020  CA  TRP B 375     -13.155   3.964  62.605  1.00 23.72           C
ATOM   1021  C   TRP B 375     -12.539   4.146  64.000  1.00 23.14           C
ATOM   1022  O   TRP B 375     -12.546   3.213  64.839  1.00 20.32           O
ATOM   1023  CB  TRP B 375     -14.511   4.686  62.453  1.00 22.15           C
ATOM   1024  CG  TRP B 375     -15.525   4.328  63.524  1.00 22.23           C
ATOM   1025  CD1 TRP B 375     -15.731   4.975  64.708  1.00 24.33           C
ATOM   1026  CD2 TRP B 375     -16.438   3.236  63.509  1.00 22.68           C
ATOM   1027  NE1 TRP B 375     -16.720   4.335  65.458  1.00 23.71           N
ATOM   1028  CE2 TRP B 375     -17.171   3.269  64.733  1.00 24.02           C
ATOM   1029  CE3 TRP B 375     -16.702   2.232  62.603  1.00 22.69           C
ATOM   1030  CZ2 TRP B 375     -18.144   2.339  65.049  1.00 23.36           C
ATOM   1031  CZ3 TRP B 375     -17.690   1.313  62.906  1.00 25.64           C
ATOM   1032  CH2 TRP B 375     -18.386   1.358  64.132  1.00 25.35           C
ATOM   1033  N   ILE B 376     -12.025   5.348  64.236  1.00 23.54           N
ATOM   1034  CA  ILE B 376     -11.605   5.750  65.589  1.00 23.84           C
ATOM   1035  C   ILE B 376     -12.230   7.030  66.056  1.00 22.98           C
ATOM   1036  O   ILE B 376     -12.134   8.031  65.363  1.00 22.87           O
ATOM   1037  CB  ILE B 376     -10.060   5.908  65.643  1.00 26.35           C
ATOM   1038  CG1 ILE B 376      -9.366   4.569  65.311  1.00 26.33           C
ATOM   1039  CG2 ILE B 376      -9.595   6.370  67.024  1.00 28.08           C
ATOM   1040  CD1 ILE B 376      -7.880   4.725  65.090  1.00 27.94           C
ATOM   1041  N   CYS B 377     -12.776   7.019  67.274  1.00 24.65           N
ATOM   1042  CA  CYS B 377     -13.362   8.193  67.920  1.00 25.50           C
ATOM   1043  C   CYS B 377     -12.399   8.754  69.002  1.00 27.78           C
ATOM   1044  O   CYS B 377     -11.662   7.997  69.647  1.00 28.17           O
ATOM   1045  CB  CYS B 377     -14.656   7.829  68.613  1.00 27.20           C
ATOM   1046  SG  CYS B 377     -15.946   7.034  67.659  1.00 30.65           S
ATOM   1047  N   LYS B 378     -12.437  10.071  69.184  1.00 26.18           N
ATOM   1048  CA  LYS B 378     -11.613  10.776  70.154  1.00 27.80           C
ATOM   1049  C   LYS B 378     -12.464  11.711  70.978  1.00 26.30           C
ATOM   1050  O   LYS B 378     -13.334  12.375  70.453  1.00 25.29           O
ATOM   1051  CB  LYS B 378     -10.552  11.621  69.471  1.00 28.77           C
ATOM   1052  CG  LYS B 378      -9.683  12.474  70.375  1.00 30.04           C
ATOM   1053  CD  LYS B 378      -8.731  13.241  69.482  1.00 33.34           C
ATOM   1054  CE  LYS B 378      -7.841  14.194  70.246  1.00 30.72           C
ATOM   1055  NZ  LYS B 378      -6.806  14.754  69.341  1.00 31.82           N
ATOM   1056  N   LYS B 379     -12.208  11.709  72.274  1.00 26.99           N
ATOM   1057  CA  LYS B 379     -12.716  12.727  73.184  1.00 29.35           C
ATOM   1058  C   LYS B 379     -11.785  12.989  74.337  1.00 31.04           C
ATOM   1059  O   LYS B 379     -10.858  12.214  74.594  1.00 29.58           O
ATOM   1060  CB  LYS B 379     -14.086  12.348  73.705  1.00 28.82           C
ATOM   1061  CG  LYS B 379     -14.148  11.239  74.721  1.00 29.52           C
ATOM   1062  CD  LYS B 379     -15.615  10.999  74.960  1.00 32.34           C
ATOM   1063  CE  LYS B 379     -15.816   9.925  75.971  1.00 36.87           C
ATOM   1064  NZ  LYS B 379     -17.192   9.400  75.825  1.00 41.90           N
ATOM   1065  N   SER B 380     -12.072  14.077  75.057  1.00 34.05           N
ATOM   1066  CA  SER B 380     -11.275  14.494  76.220  1.00 35.94           C
ATOM   1067  C   SER B 380     -11.253  13.482  77.330  1.00 34.87           C
ATOM   1068  O   SER B 380     -12.263  12.845  77.613  1.00 32.56           O
ATOM   1069  CB  SER B 380     -11.799  15.812  76.799  1.00 38.11           C
ATOM   1070  OG  SER B 380     -11.107  16.857  76.173  1.00 43.52           O
ATOM   1071  N   ALA B 381     -10.083  13.334  77.951  1.00 35.91           N
ATOM   1072  CA  ALA B 381      -9.972  12.563  79.197  1.00 40.06           C
ATOM   1073  C   ALA B 381     -10.526  13.388  80.331  1.00 39.06           C
ATOM   1074  O   ALA B 381     -10.366  14.602  80.326  1.00 38.28           O
ATOM   1075  CB  ALA B 381      -8.525  12.225  79.495  1.00 38.66           C
ATOM   1076  N   ALA B 382     -11.149  12.725  81.300  1.00 42.44           N
ATOM   1077  CA  ALA B 382     -11.501  13.342  82.591  1.00 50.31           C
ATOM   1078  C   ALA B 382     -10.259  13.695  83.420  1.00 60.22           C
ATOM   1079  O   ALA B 382      -9.204  13.025  83.317  1.00 61.38           O
ATOM   1080  CB  ALA B 382     -12.396  12.416  83.398  1.00 48.19           C
ATOM   1081  N   SER B 383     -10.407  14.745  84.237  1.00 73.89           N
ATOM   1082  CA  SER B 383      -9.406  15.147  85.247  1.00 81.94           C
ATOM   1083  C   SER B 383      -9.464  14.205  86.454  1.00 86.58           C
ATOM   1084  O   SER B 383     -10.551  13.946  87.003  1.00 84.07           O
ATOM   1085  CB  SER B 383      -9.661  16.582  85.741  1.00 82.33           C
ATOM   1086  OG  SER B 383      -9.567  17.530  84.690  1.00 79.90           O
ATOM   1087  N   CYS B 384      -8.294  13.707  86.849  1.00 86.14           N
ATOM   1088  CA  CYS B 384      -8.154  12.859  88.032  1.00 97.70           C
ATOM   1089  C   CYS B 384      -7.267  13.538  89.089  1.00103.19           C
ATOM   1090  O   CYS B 384      -6.068  13.264  89.193  1.00108.84           O
ATOM   1091  CB  CYS B 384      -7.592  11.482  87.642  1.00 96.02           C
ATOM   1092  SG  CYS B 384      -8.770  10.284  86.935  1.00 92.28           S
TER    1093      CYS B 384
ATOM   1094  N   LEU C 252     -29.118 -11.127  20.479  1.00 68.74           N
ATOM   1095  CA  LEU C 252     -27.729 -11.680  20.521  1.00 66.36           C
ATOM   1096  C   LEU C 252     -27.462 -12.380  21.863  1.00 65.89           C
ATOM   1097  O   LEU C 252     -27.884 -11.898  22.920  1.00 71.43           O
ATOM   1098  CB  LEU C 252     -26.692 -10.569  20.301  1.00 65.39           C
ATOM   1099  CG  LEU C 252     -25.307 -11.072  19.849  1.00 69.06           C
ATOM   1100  CD1 LEU C 252     -25.360 -11.516  18.385  1.00 67.88           C
ATOM   1101  CD2 LEU C 252     -24.210 -10.025  20.061  1.00 66.96           C
ATOM   1102  N   CYS C 253     -26.770 -13.517  21.806  1.00 60.18           N
ATOM   1103  CA  CYS C 253     -26.334 -14.261  22.994  1.00 52.49           C
ATOM   1104  C   CYS C 253     -24.956 -13.736  23.457  1.00 47.74           C
ATOM   1105  O   CYS C 253     -24.056 -13.542  22.634  1.00 44.62           O
ATOM   1106  CB  CYS C 253     -26.246 -15.733  22.618  1.00 49.88           C
ATOM   1107  SG  CYS C 253     -25.583 -16.872  23.859  1.00 44.89           S
ATOM   1108  N   HIS C 254     -24.786 -13.520  24.756  1.00 39.39           N
ATOM   1109  CA  HIS C 254     -23.457 -13.162  25.293  1.00 36.10           C
ATOM   1110  C   HIS C 254     -23.005 -14.242  26.237  1.00 35.49           C
ATOM   1111  O   HIS C 254     -23.838 -14.835  26.951  1.00 33.08           O
ATOM   1112  CB  HIS C 254     -23.466 -11.801  26.008  1.00 37.55           C
ATOM   1113  CG  HIS C 254     -24.049 -10.683  25.191  1.00 39.73           C
ATOM   1114  ND1 HIS C 254     -23.280  -9.850  24.404  1.00 41.14           N
ATOM   1115  CD2 HIS C 254     -25.331 -10.264  25.037  1.00 40.27           C
ATOM   1116  CE1 HIS C 254     -24.062  -8.970  23.800  1.00 39.56           C
ATOM   1117  NE2 HIS C 254     -25.309  -9.195  24.172  1.00 37.91           N
ATOM   1118  N   PRO C 255     -21.673 -14.518  26.257  1.00 30.93           N
ATOM   1119  CA  PRO C 255     -21.168 -15.519  27.181  1.00 28.15           C
ATOM   1120  C   PRO C 255     -21.536 -15.223  28.612  1.00 26.91           C
ATOM   1121  O   PRO C 255     -21.913 -16.124  29.353  1.00 23.00           O
ATOM   1122  CB  PRO C 255     -19.660 -15.425  26.994  1.00 31.22           C
ATOM   1123  CG  PRO C 255     -19.501 -14.973  25.574  1.00 31.48           C
ATOM   1124  CD  PRO C 255     -20.588 -13.956  25.432  1.00 30.92           C
ATOM   1125  N   CYS C 256     -21.425 -13.965  28.999  1.00 26.32           N
ATOM   1126  CA  CYS C 256     -21.693 -13.581  30.383  1.00 27.51           C
ATOM   1127  C   CYS C 256     -22.772 -12.498  30.480  1.00 29.78           C
ATOM   1128  O   CYS C 256     -23.051 -11.794  29.504  1.00 28.78           O
ATOM   1129  CB  CYS C 256     -20.421 -13.018  31.010  1.00 28.02           C
ATOM   1130  SG  CYS C 256     -19.110 -14.204  31.112  1.00 31.38           S
ATOM   1131  N   PRO C 257     -23.337 -12.311  31.681  1.00 33.01           N
ATOM   1132  CA  PRO C 257     -24.219 -11.189  31.844  1.00 31.49           C
ATOM   1133  C   PRO C 257     -23.450  -9.888  31.789  1.00 30.36           C
ATOM   1134  O   PRO C 257     -22.202  -9.845  31.939  1.00 29.30           O
ATOM   1135  CB  PRO C 257     -24.819 -11.409  33.247  1.00 34.15           C
ATOM   1136  CG  PRO C 257     -24.663 -12.879  33.493  1.00 36.60           C
ATOM   1137  CD  PRO C 257     -23.305 -13.145  32.897  1.00 36.41           C
ATOM   1138  N   TRP C 258     -24.209  -8.829  31.572  1.00 32.59           N
ATOM   1139  CA  TRP C 258     -23.658  -7.503  31.341  1.00 34.87           C
ATOM   1140  C   TRP C 258     -22.903  -7.092  32.601  1.00 35.94           C
ATOM   1141  O   TRP C 258     -23.415  -7.237  33.740  1.00 36.41           O
ATOM   1142  CB  TRP C 258     -24.804  -6.547  31.010  1.00 35.95           C
ATOM   1143  CG  TRP C 258     -24.440  -5.252  30.285  1.00 39.09           C
ATOM   1144  CD1 TRP C 258     -23.273  -4.554  30.375  1.00 39.58           C
ATOM   1145  CD2 TRP C 258     -25.298  -4.477  29.436  1.00 39.11           C
ATOM   1146  NE1 TRP C 258     -23.332  -3.424  29.605  1.00 39.96           N
ATOM   1147  CE2 TRP C 258     -24.567  -3.340  29.030  1.00 38.78           C
ATOM   1148  CE3 TRP C 258     -26.614  -4.633  28.987  1.00 40.88           C
ATOM   1149  CZ2 TRP C 258     -25.101  -2.358  28.194  1.00 41.13           C
ATOM   1150  CZ3 TRP C 258     -27.146  -3.665  28.155  1.00 43.22           C
ATOM   1151  CH2 TRP C 258     -26.381  -2.537  27.757  1.00 44.02           C
ATOM   1152  N   GLU C 259     -21.680  -6.619  32.391  1.00 35.39           N
ATOM   1153  CA  GLU C 259     -20.747  -6.209  33.459  1.00 39.35           C
ATOM   1154  C   GLU C 259     -19.937  -7.320  34.116  1.00 38.70           C
ATOM   1155  O   GLU C 259     -18.952  -7.018  34.793  1.00 45.38           O
ATOM   1156  CB  GLU C 259     -21.421  -5.356  34.549  1.00 42.94           C
ATOM   1157  CG  GLU C 259     -22.247  -4.232  33.947  1.00 47.40           C
ATOM   1158  CD  GLU C 259     -22.541  -3.104  34.900  1.00 49.70           C
ATOM   1159  OE1 GLU C 259     -22.036  -3.150  36.031  1.00 54.78           O
ATOM   1160  OE2 GLU C 259     -23.275  -2.173  34.504  1.00 50.31           O
ATOM   1161  N   TRP C 260     -20.306  -8.586  33.912  1.00 33.22           N
ATOM   1162  CA  TRP C 260     -19.502  -9.682  34.407  1.00 30.39           C
ATOM   1163  C   TRP C 260     -18.304  -9.763  33.490  1.00 30.21           C
ATOM   1164  O   TRP C 260     -18.396  -9.372  32.334  1.00 27.77           O
ATOM   1165  CB  TRP C 260     -20.259 -10.998  34.399  1.00 28.77           C
ATOM   1166  CG  TRP C 260     -21.359 -11.042  35.399  1.00 28.87           C
ATOM   1167  CD1 TRP C 260     -22.317 -10.107  35.574  1.00 31.75           C
ATOM   1168  CD2 TRP C 260     -21.624 -12.071  36.370  1.00 28.11           C
ATOM   1169  NE1 TRP C 260     -23.167 -10.484  36.584  1.00 31.95           N
ATOM   1170  CE2 TRP C 260     -22.748 -11.677  37.097  1.00 29.49           C
ATOM   1171  CE3 TRP C 260     -20.995 -13.262  36.715  1.00 29.35           C
ATOM   1172  CZ2 TRP C 260     -23.278 -12.433  38.111  1.00 30.58           C
ATOM   1173  CZ3 TRP C 260     -21.514 -14.007  37.741  1.00 29.34           C
ATOM   1174  CH2 TRP C 260     -22.649 -13.588  38.427  1.00 29.17           C
ATOM   1175  N   THR C 261     -17.187 -10.268  34.019  1.00 29.02           N
ATOM   1176  CA  THR C 261     -15.978 -10.500  33.235  1.00 29.20           C
ATOM   1177  C   THR C 261     -15.877 -11.941  32.797  1.00 28.70           C
ATOM   1178  O   THR C 261     -16.023 -12.855  33.607  1.00 30.78           O
ATOM   1179  CB  THR C 261     -14.770 -10.225  34.114  1.00 27.61           C
ATOM   1180  OG1 THR C 261     -14.845  -8.900  34.566  1.00 30.55           O
ATOM   1181  CG2 THR C 261     -13.475 -10.420  33.367  1.00 29.81           C
ATOM   1182  N   PHE C 262     -15.593 -12.151  31.522  1.00 30.86           N
ATOM   1183  CA  PHE C 262     -15.430 -13.489  30.976  1.00 27.19           C
ATOM   1184  C   PHE C 262     -14.016 -13.892  31.270  1.00 26.84           C
ATOM   1185  O   PHE C 262     -13.123 -13.124  30.953  1.00 29.48           O
ATOM   1186  CB  PHE C 262     -15.597 -13.493  29.450  1.00 29.33           C
ATOM   1187  CG  PHE C 262     -15.366 -14.858  28.831  1.00 27.68           C
ATOM   1188  CD1 PHE C 262     -16.394 -15.771  28.762  1.00 28.12           C
ATOM   1189  CD2 PHE C 262     -14.116 -15.231  28.360  1.00 28.00           C
ATOM   1190  CE1 PHE C 262     -16.196 -17.034  28.202  1.00 29.67           C
ATOM   1191  CE2 PHE C 262     -13.896 -16.504  27.843  1.00 28.03           C
ATOM   1192  CZ  PHE C 262     -14.940 -17.404  27.760  1.00 29.89           C
ATOM   1193  N   PHE C 263     -13.784 -15.068  31.834  1.00 23.91           N
ATOM   1194  CA  PHE C 263     -12.411 -15.582  31.953  1.00 26.83           C
ATOM   1195  C   PHE C 263     -12.420 -17.125  31.857  1.00 28.90           C
ATOM   1196  O   PHE C 263     -13.034 -17.843  32.713  1.00 26.03           O
ATOM   1197  CB  PHE C 263     -11.729 -15.087  33.238  1.00 28.52           C
ATOM   1198  CG  PHE C 263     -10.336 -15.606  33.442  1.00 29.35           C
ATOM   1199  CD1 PHE C 263     -10.120 -16.793  34.106  1.00 31.01           C
ATOM   1200  CD2 PHE C 263      -9.257 -14.923  32.952  1.00 31.58           C
ATOM   1201  CE1 PHE C 263      -8.846 -17.287  34.292  1.00 32.46           C
ATOM   1202  CE2 PHE C 263      -7.980 -15.404  33.146  1.00 32.91           C
ATOM   1203  CZ  PHE C 263      -7.774 -16.585  33.815  1.00 31.55           C
ATOM   1204  N   GLN C 264     -11.746 -17.612  30.802  1.00 24.96           N
ATOM   1205  CA  GLN C 264     -11.581 -19.047  30.534  1.00 26.16           C
ATOM   1206  C   GLN C 264     -12.859 -19.850  30.719  1.00 25.19           C
ATOM   1207  O   GLN C 264     -12.875 -20.864  31.398  1.00 26.58           O
ATOM   1208  CB  GLN C 264     -10.466 -19.667  31.401  1.00 25.50           C
ATOM   1209  CG  GLN C 264      -9.187 -18.898  31.340  1.00 26.07           C
ATOM   1210  CD  GLN C 264      -7.969 -19.726  31.692  1.00 30.34           C
ATOM   1211  OE1 GLN C 264      -8.028 -20.659  32.504  1.00 28.97           O
ATOM   1212  NE2 GLN C 264      -6.832 -19.377  31.075  1.00 28.56           N
ATOM   1213  N   GLY C 265     -13.923 -19.372  30.102  1.00 27.65           N
ATOM   1214  CA  GLY C 265     -15.196 -20.082  30.059  1.00 29.66           C
ATOM   1215  C   GLY C 265     -16.116 -19.868  31.248  1.00 29.17           C
ATOM   1216  O   GLY C 265     -17.150 -20.550  31.374  1.00 27.88           O
ATOM   1217  N   ASN C 266     -15.728 -18.977  32.154  1.00 28.69           N
ATOM   1218  CA  ASN C 266     -16.584 -18.646  33.294  1.00 26.57           C
ATOM   1219  C   ASN C 266     -16.748 -17.127  33.328  1.00 28.80           C
ATOM   1220  O   ASN C 266     -16.017 -16.363  32.657  1.00 27.54           O
ATOM   1221  CB  ASN C 266     -16.001 -19.193  34.610  1.00 26.31           C
ATOM   1222  CG  ASN C 266     -15.937 -20.751  34.657  1.00 28.55           C
ATOM   1223  OD1 ASN C 266     -16.945 -21.412  34.839  1.00 28.93           O
ATOM   1224  ND2 ASN C 266     -14.728 -21.315  34.565  1.00 24.94           N
ATOM   1225  N   CYS C 267     -17.742 -16.718  34.092  1.00 27.65           N
ATOM   1226  CA  CYS C 267     -18.127 -15.354  34.248  1.00 29.47           C
ATOM   1227  C   CYS C 267     -17.934 -15.002  35.693  1.00 29.99           C
ATOM   1228  O   CYS C 267     -18.440 -15.734  36.576  1.00 26.67           O
ATOM   1229  CB  CYS C 267     -19.622 -15.211  33.899  1.00 31.00           C
ATOM   1230  SG  CYS C 267     -19.969 -15.730  32.213  1.00 30.36           S
ATOM   1231  N   TYR C 268     -17.274 -13.866  35.920  1.00 27.72           N
ATOM   1232  CA  TYR C 268     -17.003 -13.365  37.243  1.00 27.75           C
ATOM   1233  C   TYR C 268     -17.654 -11.997  37.481  1.00 27.16           C
ATOM   1234  O   TYR C 268     -17.553 -11.056  36.650  1.00 27.39           O
ATOM   1235  CB  TYR C 268     -15.485 -13.311  37.502  1.00 28.40           C
ATOM   1236  CG  TYR C 268     -14.803 -14.654  37.334  1.00 28.61           C
ATOM   1237  CD1 TYR C 268     -14.495 -15.142  36.070  1.00 27.27           C
ATOM   1238  CD2 TYR C 268     -14.478 -15.447  38.430  1.00 28.12           C
ATOM   1239  CE1 TYR C 268     -13.877 -16.376  35.899  1.00 29.66           C
ATOM   1240  CE2 TYR C 268     -13.869 -16.681  38.264  1.00 28.29           C
ATOM   1241  CZ  TYR C 268     -13.551 -17.126  36.985  1.00 27.89           C
ATOM   1242  OH  TYR C 268     -12.971 -18.353  36.794  1.00 29.71           O
ATOM   1243  N   PHE C 269     -18.362 -11.916  38.605  1.00 26.07           N
ATOM   1244  CA  PHE C 269     -18.873 -10.675  39.133  1.00 26.73           C
ATOM   1245  C   PHE C 269     -17.933 -10.163  40.223  1.00 26.26           C
ATOM   1246  O   PHE C 269     -17.733 -10.834  41.222  1.00 26.50           O
ATOM   1247  CB  PHE C 269     -20.240 -10.885  39.730  1.00 28.84           C
ATOM   1248  CG  PHE C 269     -20.858  -9.618  40.256  1.00 31.35           C
ATOM   1249  CD1 PHE C 269     -21.165  -8.578  39.384  1.00 34.90           C
ATOM   1250  CD2 PHE C 269     -21.086  -9.445  41.618  1.00 33.18           C
ATOM   1251  CE1 PHE C 269     -21.724  -7.377  39.855  1.00 36.70           C
ATOM   1252  CE2 PHE C 269     -21.637  -8.252  42.105  1.00 34.31           C
ATOM   1253  CZ  PHE C 269     -21.964  -7.221  41.220  1.00 35.64           C
ATOM   1254  N   MET C 270     -17.354  -8.992  40.010  1.00 28.08           N
ATOM   1255  CA  MET C 270     -16.534  -8.334  41.012  1.00 27.74           C
ATOM   1256  C   MET C 270     -17.440  -7.320  41.691  1.00 25.64           C
ATOM   1257  O   MET C 270     -17.881  -6.405  41.044  1.00 24.80           O
ATOM   1258  CB  MET C 270     -15.344  -7.598  40.370  1.00 31.89           C
ATOM   1259  CG  MET C 270     -14.688  -8.277  39.169  1.00 39.62           C
ATOM   1260  SD  MET C 270     -14.141  -9.929  39.503  1.00 46.97           S
ATOM   1261  CE  MET C 270     -12.841 -10.162  38.298  1.00 48.86           C
ATOM   1262  N   SER C 271     -17.743  -7.482  42.972  1.00 24.65           N
ATOM   1263  CA  SER C 271     -18.640  -6.523  43.662  1.00 26.55           C
ATOM   1264  C   SER C 271     -17.985  -5.139  43.772  1.00 26.66           C
ATOM   1265  O   SER C 271     -16.767  -5.046  43.837  1.00 25.32           O
ATOM   1266  CB  SER C 271     -18.960  -7.027  45.082  1.00 22.62           C
ATOM   1267  OG  SER C 271     -17.849  -6.777  45.935  1.00 24.31           O
ATOM   1268  N   ASN C 272     -18.764  -4.079  43.886  1.00 29.43           N
ATOM   1269  CA AASN C 272     -18.207  -2.770  44.178  0.50 29.80           C
ATOM   1270  CA BASN C 272     -18.159  -2.763  44.235  0.50 30.39           C
ATOM   1271  C   ASN C 272     -18.696  -2.308  45.563  1.00 30.10           C
ATOM   1272  O   ASN C 272     -18.531  -1.152  45.917  1.00 29.82           O
ATOM   1273  CB AASN C 272     -18.536  -1.768  43.046  0.50 31.63           C
ATOM   1274  CB BASN C 272     -18.351  -1.657  43.169  0.50 33.18           C
ATOM   1275  CG AASN C 272     -17.700  -1.996  41.762  0.50 31.66           C
ATOM   1276  CG BASN C 272     -17.274  -0.529  43.238  0.50 34.59           C
ATOM   1277  OD1AASN C 272     -16.493  -2.313  41.805  0.50 30.89           O
ATOM   1278  OD1BASN C 272     -16.752  -0.155  44.313  0.50 36.43           O
ATOM   1279  ND2AASN C 272     -18.346  -1.799  40.608  0.50 30.93           N
ATOM   1280  ND2BASN C 272     -16.975   0.047  42.074  0.50 34.10           N
ATOM   1281  N   SER C 273     -19.276  -3.229  46.336  1.00 28.07           N
ATOM   1282  CA  SER C 273     -19.546  -2.957  47.754  1.00 27.93           C
ATOM   1283  C   SER C 273     -19.106  -4.162  48.624  1.00 27.46           C
ATOM   1284  O   SER C 273     -18.477  -5.131  48.116  1.00 25.90           O
ATOM   1285  CB  SER C 273     -21.032  -2.632  47.951  1.00 31.25           C
ATOM   1286  OG  SER C 273     -21.808  -3.786  47.659  1.00 33.61           O
ATOM   1287  N   GLN C 274     -19.387  -4.103  49.920  1.00 23.65           N
ATOM   1288  CA  GLN C 274     -18.796  -5.056  50.849  1.00 26.64           C
ATOM   1289  C   GLN C 274     -19.841  -5.789  51.694  1.00 26.39           C
ATOM   1290  O   GLN C 274     -20.825  -5.218  52.093  1.00 25.46           O
ATOM   1291  CB  GLN C 274     -17.776  -4.365  51.767  1.00 26.10           C
ATOM   1292  CG  GLN C 274     -16.703  -3.532  51.041  1.00 27.47           C
ATOM   1293  CD  GLN C 274     -16.321  -2.274  51.837  1.00 28.83           C
ATOM   1294  OE1 GLN C 274     -17.106  -1.315  51.912  1.00 28.11           O
ATOM   1295  NE2 GLN C 274     -15.132  -2.284  52.448  1.00 26.38           N
ATOM   1296  N   ARG C 275     -19.588  -7.056  51.951  1.00 24.80           N
ATOM   1297  CA  ARG C 275     -20.497  -7.911  52.706  1.00 26.00           C
ATOM   1298  C   ARG C 275     -19.677  -8.894  53.499  1.00 25.07           C
ATOM   1299  O   ARG C 275     -18.547  -9.235  53.126  1.00 22.00           O
ATOM   1300  CB  ARG C 275     -21.420  -8.687  51.767  1.00 28.84           C
ATOM   1301  CG  ARG C 275     -22.585  -7.915  51.233  1.00 28.98           C
ATOM   1302  CD  ARG C 275     -23.371  -8.768  50.289  1.00 34.31           C
ATOM   1303  NE  ARG C 275     -24.540  -8.053  49.796  1.00 40.38           N
ATOM   1304  CZ  ARG C 275     -25.787  -8.534  49.769  1.00 44.79           C
ATOM   1305  NH1 ARG C 275     -26.080  -9.795  50.153  1.00 43.60           N
ATOM   1306  NH2 ARG C 275     -26.753  -7.746  49.323  1.00 43.84           N
ATOM   1307  N   ASN C 276     -20.243  -9.370  54.593  1.00 26.13           N
ATOM   1308  CA  ASN C 276     -19.614 -10.439  55.302  1.00 25.05           C
ATOM   1309  C   ASN C 276     -19.651 -11.680  54.419  1.00 23.10           C
ATOM   1310  O   ASN C 276     -20.314 -11.726  53.385  1.00 26.16           O
ATOM   1311  CB  ASN C 276     -20.204 -10.638  56.730  1.00 24.33           C
ATOM   1312  CG  ASN C 276     -21.638 -11.182  56.735  1.00 26.28           C
ATOM   1313  OD1 ASN C 276     -22.030 -11.927  55.856  1.00 22.82           O
ATOM   1314  ND2 ASN C 276     -22.410 -10.821  57.758  1.00 23.04           N
ATOM   1315  N   TRP C 277     -18.937 -12.696  54.839  1.00 23.05           N
ATOM   1316  CA  TRP C 277     -18.762 -13.895  54.025  1.00 22.29           C
ATOM   1317  C   TRP C 277     -20.096 -14.587  53.694  1.00 22.51           C
ATOM   1318  O   TRP C 277     -20.327 -14.988  52.565  1.00 21.11           O
ATOM   1319  CB  TRP C 277     -17.786 -14.824  54.717  1.00 20.37           C
ATOM   1320  CG  TRP C 277     -17.254 -15.933  53.878  1.00 20.38           C
ATOM   1321  CD1 TRP C 277     -16.241 -15.877  52.995  1.00 18.82           C
ATOM   1322  CD2 TRP C 277     -17.684 -17.293  53.913  1.00 20.90           C
ATOM   1323  NE1 TRP C 277     -16.016 -17.117  52.444  1.00 17.83           N
ATOM   1324  CE2 TRP C 277     -16.889 -18.004  53.007  1.00 20.12           C
ATOM   1325  CE3 TRP C 277     -18.674 -17.976  54.628  1.00 23.18           C
ATOM   1326  CZ2 TRP C 277     -17.055 -19.349  52.778  1.00 20.85           C
ATOM   1327  CZ3 TRP C 277     -18.836 -19.325  54.399  1.00 23.75           C
ATOM   1328  CH2 TRP C 277     -18.029 -19.991  53.473  1.00 23.79           C
ATOM   1329  N   HIS C 278     -21.002 -14.651  54.660  1.00 22.48           N
ATOM   1330  CA  HIS C 278     -22.168 -15.445  54.545  1.00 24.58           C
ATOM   1331  C   HIS C 278     -23.139 -14.733  53.652  1.00 24.28           C
ATOM   1332  O   HIS C 278     -23.762 -15.343  52.764  1.00 27.61           O
ATOM   1333  CB  HIS C 278     -22.767 -15.784  55.958  1.00 27.51           C
ATOM   1334  CG  HIS C 278     -22.160 -17.003  56.578  1.00 33.72           C
ATOM   1335  ND1 HIS C 278     -21.226 -16.947  57.602  1.00 37.73           N
ATOM   1336  CD2 HIS C 278     -22.341 -18.324  56.304  1.00 38.26           C
ATOM   1337  CE1 HIS C 278     -20.863 -18.176  57.922  1.00 37.39           C
ATOM   1338  NE2 HIS C 278     -21.538 -19.030  57.164  1.00 36.89           N
ATOM   1339  N   ASP C 279     -23.228 -13.425  53.813  1.00 23.02           N
ATOM   1340  CA  ASP C 279     -24.003 -12.629  52.911  1.00 22.25           C
ATOM   1341  C   ASP C 279     -23.419 -12.577  51.483  1.00 24.13           C
ATOM   1342  O   ASP C 279     -24.177 -12.344  50.515  1.00 22.02           O
ATOM   1343  CB  ASP C 279     -24.102 -11.233  53.448  1.00 25.50           C
ATOM   1344  CG  ASP C 279     -24.943 -11.170  54.725  1.00 28.82           C
ATOM   1345  OD1 ASP C 279     -25.581 -12.191  55.069  1.00 30.43           O
ATOM   1346  OD2 ASP C 279     -24.956 -10.103  55.366  1.00 30.47           O
ATOM   1347  N   SER C 280     -22.097 -12.719  51.345  1.00 21.89           N
ATOM   1348  CA  SER C 280     -21.502 -12.774  50.001  1.00 21.85           C
ATOM   1349  C   SER C 280     -21.957 -14.077  49.327  1.00 22.44           C
ATOM   1350  O   SER C 280     -22.295 -14.092  48.175  1.00 25.02           O
ATOM   1351  CB  SER C 280     -19.993 -12.715  50.067  1.00 21.18           C
ATOM   1352  OG  SER C 280     -19.534 -11.489  50.613  1.00 20.81           O
ATOM   1353  N   ILE C 281     -21.991 -15.164  50.071  1.00 23.74           N
ATOM   1354  CA  ILE C 281     -22.445 -16.397  49.536  1.00 23.24           C
ATOM   1355  C   ILE C 281     -23.895 -16.241  49.007  1.00 26.92           C
ATOM   1356  O   ILE C 281     -24.235 -16.699  47.893  1.00 24.07           O
ATOM   1357  CB  ILE C 281     -22.351 -17.493  50.610  1.00 25.14           C
ATOM   1358  CG1 ILE C 281     -20.895 -17.880  50.686  1.00 28.26           C
ATOM   1359  CG2 ILE C 281     -23.248 -18.694  50.297  1.00 23.84           C
ATOM   1360  CD1 ILE C 281     -20.610 -18.989  51.613  1.00 33.07           C
ATOM   1361  N   THR C 282     -24.734 -15.591  49.801  1.00 23.92           N
ATOM   1362  CA  THR C 282     -26.109 -15.412  49.437  1.00 24.34           C
ATOM   1363  C   THR C 282     -26.219 -14.582  48.181  1.00 24.95           C
ATOM   1364  O   THR C 282     -27.013 -14.878  47.298  1.00 26.89           O
ATOM   1365  CB  THR C 282     -26.859 -14.670  50.547  1.00 26.06           C
ATOM   1366  OG1 THR C 282     -26.824 -15.458  51.744  1.00 25.80           O
ATOM   1367  CG2 THR C 282     -28.296 -14.424  50.122  1.00 28.17           C
ATOM   1368  N   ALA C 283     -25.466 -13.500  48.142  1.00 23.88           N
ATOM   1369  CA  ALA C 283     -25.519 -12.580  47.072  1.00 25.25           C
ATOM   1370  C   ALA C 283     -25.185 -13.317  45.761  1.00 25.16           C
ATOM   1371  O   ALA C 283     -25.874 -13.181  44.774  1.00 26.34           O
ATOM   1372  CB  ALA C 283     -24.549 -11.424  47.324  1.00 26.33           C
ATOM   1373  N   CYS C 284     -24.167 -14.140  45.790  1.00 24.46           N
ATOM   1374  CA  CYS C 284     -23.796 -14.945  44.613  1.00 25.87           C
ATOM   1375  C   CYS C 284     -24.931 -15.944  44.226  1.00 27.85           C
ATOM   1376  O   CYS C 284     -25.267 -16.029  43.046  1.00 24.37           O
ATOM   1377  CB  CYS C 284     -22.468 -15.669  44.847  1.00 24.79           C
ATOM   1378  SG  CYS C 284     -21.074 -14.532  44.912  1.00 24.03           S
ATOM   1379  N   LYS C 285     -25.536 -16.640  45.203  1.00 28.25           N
ATOM   1380  CA  LYS C 285     -26.614 -17.590  44.906  1.00 31.31           C
ATOM   1381  C   LYS C 285     -27.768 -16.930  44.152  1.00 29.57           C
ATOM   1382  O   LYS C 285     -28.268 -17.465  43.167  1.00 28.67           O
ATOM   1383  CB  LYS C 285     -27.145 -18.229  46.176  1.00 34.43           C
ATOM   1384  CG  LYS C 285     -26.268 -19.372  46.616  1.00 38.20           C
ATOM   1385  CD  LYS C 285     -26.676 -19.907  47.976  1.00 41.61           C
ATOM   1386  CE  LYS C 285     -25.765 -21.089  48.266  1.00 46.90           C
ATOM   1387  NZ  LYS C 285     -25.918 -21.605  49.647  1.00 52.01           N
ATOM   1388  N   GLU C 286     -28.124 -15.733  44.587  1.00 28.74           N
ATOM   1389  CA  GLU C 286     -29.258 -15.027  44.070  1.00 30.05           C
ATOM   1390  C   GLU C 286     -29.063 -14.568  42.623  1.00 30.43           C
ATOM   1391  O   GLU C 286     -30.048 -14.278  41.942  1.00 29.60           O
ATOM   1392  CB  GLU C 286     -29.633 -13.870  44.982  1.00 30.90           C
ATOM   1393  CG  GLU C 286     -30.276 -14.398  46.261  1.00 37.92           C
ATOM   1394  CD  GLU C 286     -30.690 -13.305  47.222  1.00 46.37           C
ATOM   1395  OE1 GLU C 286     -30.462 -12.096  46.923  1.00 53.77           O
ATOM   1396  OE2 GLU C 286     -31.229 -13.678  48.288  1.00 53.75           O
ATOM   1397  N   VAL C 287     -27.825 -14.546  42.135  1.00 29.20           N
ATOM   1398  CA  VAL C 287     -27.610 -14.284  40.689  1.00 28.29           C
ATOM   1399  C   VAL C 287     -27.181 -15.538  39.948  1.00 30.40           C
ATOM   1400  O   VAL C 287     -26.611 -15.466  38.840  1.00 32.40           O
ATOM   1401  CB  VAL C 287     -26.624 -13.122  40.441  1.00 27.45           C
ATOM   1402  CG1 VAL C 287     -27.199 -11.816  40.939  1.00 28.48           C
ATOM   1403  CG2 VAL C 287     -25.287 -13.383  41.093  1.00 27.90           C
ATOM   1404  N   GLY C 288     -27.481 -16.687  40.552  1.00 29.44           N
ATOM   1405  CA  GLY C 288     -27.163 -17.976  39.980  1.00 27.20           C
ATOM   1406  C   GLY C 288     -25.693 -18.335  39.909  1.00 28.14           C
ATOM   1407  O   GLY C 288     -25.281 -19.081  39.040  1.00 28.00           O
ATOM   1408  N   ALA C 289     -24.901 -17.831  40.850  1.00 29.37           N
ATOM   1409  CA  ALA C 289     -23.463 -18.050  40.848  1.00 26.60           C
ATOM   1410  C   ALA C 289     -23.064 -18.538  42.199  1.00 27.59           C
ATOM   1411  O   ALA C 289     -23.921 -18.741  43.071  1.00 26.77           O
ATOM   1412  CB  ALA C 289     -22.736 -16.751  40.519  1.00 28.07           C
ATOM   1413  N   GLN C 290     -21.744 -18.666  42.382  1.00 27.93           N
ATOM   1414  CA  GLN C 290     -21.171 -19.137  43.606  1.00 28.20           C
ATOM   1415  C   GLN C 290     -19.959 -18.293  44.033  1.00 26.90           C
ATOM   1416  O   GLN C 290     -19.144 -17.904  43.190  1.00 22.81           O
ATOM   1417  CB  GLN C 290     -20.720 -20.544  43.352  1.00 29.64           C
ATOM   1418  CG  GLN C 290     -20.249 -21.285  44.572  1.00 32.18           C
ATOM   1419  CD  GLN C 290     -19.959 -22.732  44.226  1.00 36.13           C
ATOM   1420  OE1 GLN C 290     -19.125 -23.030  43.328  1.00 38.61           O
ATOM   1421  NE2 GLN C 290     -20.663 -23.636  44.892  1.00 30.74           N
ATOM   1422  N   LEU C 291     -19.854 -18.029  45.334  1.00 22.86           N
ATOM   1423  CA  LEU C 291     -18.697 -17.305  45.899  1.00 22.46           C
ATOM   1424  C   LEU C 291     -17.446 -18.070  45.468  1.00 20.88           C
ATOM   1425  O   LEU C 291     -17.352 -19.296  45.599  1.00 18.96           O
ATOM   1426  CB  LEU C 291     -18.810 -17.147  47.409  1.00 22.35           C
ATOM   1427  CG  LEU C 291     -17.685 -16.300  48.012  1.00 23.67           C
ATOM   1428  CD1 LEU C 291     -17.846 -14.853  47.612  1.00 22.78           C
ATOM   1429  CD2 LEU C 291     -17.695 -16.456  49.520  1.00 22.74           C
ATOM   1430  N   VAL C 292     -16.565 -17.355  44.800  1.00 20.75           N
ATOM   1431  CA  VAL C 292     -15.615 -17.967  43.911  1.00 21.57           C
ATOM   1432  C   VAL C 292     -14.777 -19.145  44.469  1.00 24.39           C
ATOM   1433  O   VAL C 292     -14.096 -19.047  45.506  1.00 23.59           O
ATOM   1434  CB  VAL C 292     -14.757 -16.910  43.200  1.00 22.22           C
ATOM   1435  CG1 VAL C 292     -13.944 -16.096  44.172  1.00 22.41           C
ATOM   1436  CG2 VAL C 292     -13.886 -17.577  42.115  1.00 22.08           C
ATOM   1437  N   VAL C 293     -14.848 -20.245  43.724  1.00 24.27           N
ATOM   1438  CA  VAL C 293     -14.068 -21.427  43.975  1.00 26.70           C
ATOM   1439  C   VAL C 293     -12.967 -21.529  42.933  1.00 26.08           C
ATOM   1440  O   VAL C 293     -13.247 -21.525  41.755  1.00 26.01           O
ATOM   1441  CB  VAL C 293     -14.956 -22.675  43.917  1.00 26.74           C
ATOM   1442  CG1 VAL C 293     -14.129 -23.946  44.102  1.00 28.20           C
ATOM   1443  CG2 VAL C 293     -16.040 -22.603  44.996  1.00 28.37           C
ATOM   1444  N   ILE C 294     -11.723 -21.645  43.376  1.00 25.81           N
ATOM   1445  CA  ILE C 294     -10.564 -21.596  42.478  1.00 26.46           C
ATOM   1446  C   ILE C 294     -10.133 -23.040  42.115  1.00 28.25           C
ATOM   1447  O   ILE C 294     -10.037 -23.914  42.986  1.00 28.14           O
ATOM   1448  CB  ILE C 294      -9.389 -20.828  43.126  1.00 27.60           C
ATOM   1449  CG1 ILE C 294      -9.903 -19.471  43.672  1.00 28.48           C
ATOM   1450  CG2 ILE C 294      -8.274 -20.583  42.115  1.00 27.19           C
ATOM   1451  CD1 ILE C 294      -8.834 -18.621  44.313  1.00 27.76           C
ATOM   1452  N   LYS C 295      -9.916 -23.270  40.812  1.00 29.51           N
ATOM   1453  CA  LYS C 295      -9.578 -24.596  40.264  1.00 29.56           C
ATOM   1454  C   LYS C 295      -8.202 -24.676  39.601  1.00 33.28           C
ATOM   1455  O   LYS C 295      -7.692 -25.777  39.410  1.00 37.13           O
ATOM   1456  CB  LYS C 295     -10.591 -24.997  39.226  1.00 29.52           C
ATOM   1457  CG  LYS C 295     -12.015 -25.122  39.707  1.00 31.36           C
ATOM   1458  CD  LYS C 295     -12.238 -26.295  40.633  1.00 30.82           C
ATOM   1459  CE  LYS C 295     -13.737 -26.437  40.932  1.00 30.28           C
ATOM   1460  NZ  LYS C 295     -13.965 -27.013  42.264  1.00 30.80           N
ATOM   1461  N   SER C 296      -7.630 -23.534  39.207  1.00 29.81           N
ATOM   1462  CA  SER C 296      -6.297 -23.519  38.647  1.00 31.60           C
ATOM   1463  C   SER C 296      -5.463 -22.312  39.043  1.00 30.30           C
ATOM   1464  O   SER C 296      -5.934 -21.270  39.583  1.00 26.38           O
ATOM   1465  CB  SER C 296      -6.368 -23.587  37.112  1.00 31.91           C
ATOM   1466  OG  SER C 296      -6.962 -22.417  36.582  1.00 29.87           O
ATOM   1467  N   ALA C 297      -4.186 -22.496  38.787  1.00 32.19           N
ATOM   1468  CA  ALA C 297      -3.182 -21.510  39.077  1.00 33.54           C
ATOM   1469  C   ALA C 297      -3.460 -20.196  38.319  1.00 34.95           C
ATOM   1470  O   ALA C 297      -3.427 -19.101  38.932  1.00 36.91           O
ATOM   1471  CB  ALA C 297      -1.812 -22.067  38.720  1.00 35.37           C
ATOM   1472  N   GLU C 298      -3.760 -20.315  37.016  1.00 33.67           N
ATOM   1473  CA AGLU C 298      -4.056 -19.172  36.155  0.70 35.01           C
ATOM   1474  CA BGLU C 298      -4.035 -19.134  36.186  0.30 33.10           C
ATOM   1475  C   GLU C 298      -5.284 -18.402  36.669  1.00 32.37           C
ATOM   1476  O   GLU C 298      -5.360 -17.209  36.548  1.00 27.39           O
ATOM   1477  CB AGLU C 298      -4.371 -19.623  34.720  0.70 35.45           C
ATOM   1478  CB BGLU C 298      -4.231 -19.479  34.703  0.30 32.67           C
ATOM   1479  CG AGLU C 298      -3.270 -20.340  33.945  0.70 40.32           C
ATOM   1480  CG BGLU C 298      -2.974 -19.832  33.928  0.30 34.11           C
ATOM   1481  CD AGLU C 298      -2.988 -21.781  34.406  0.70 40.49           C
ATOM   1482  CD BGLU C 298      -2.107 -18.646  33.564  0.30 34.17           C
ATOM   1483  OE1AGLU C 298      -3.901 -22.494  34.870  0.70 36.51           O
ATOM   1484  OE1BGLU C 298      -2.314 -17.537  34.105  0.30 35.42           O
ATOM   1485  OE2AGLU C 298      -1.810 -22.194  34.312  0.70 42.47           O
ATOM   1486  OE2BGLU C 298      -1.195 -18.844  32.729  0.30 35.92           O
ATOM   1487  N   GLU C 299      -6.278 -19.138  37.156  1.00 31.11           N
ATOM   1488  CA  GLU C 299      -7.469 -18.524  37.713  1.00 31.36           C
ATOM   1489  C   GLU C 299      -7.087 -17.807  39.005  1.00 31.66           C
ATOM   1490  O   GLU C 299      -7.528 -16.706  39.223  1.00 30.97           O
ATOM   1491  CB  GLU C 299      -8.537 -19.559  38.011  1.00 31.77           C
ATOM   1492  CG  GLU C 299      -9.961 -19.030  38.177  1.00 32.14           C
ATOM   1493  CD  GLU C 299     -10.920 -20.061  38.766  1.00 32.16           C
ATOM   1494  OE1 GLU C 299     -12.068 -19.685  39.093  1.00 33.45           O
ATOM   1495  OE2 GLU C 299     -10.557 -21.252  38.909  1.00 31.79           O
ATOM   1496  N   GLN C 300      -6.283 -18.459  39.855  1.00 30.37           N
ATOM   1497  CA  GLN C 300      -5.713 -17.837  41.056  1.00 26.59           C
ATOM   1498  C   GLN C 300      -5.007 -16.559  40.708  1.00 25.93           C
ATOM   1499  O   GLN C 300      -5.191 -15.568  41.401  1.00 22.16           O
ATOM   1500  CB  GLN C 300      -4.762 -18.790  41.794  1.00 24.95           C
ATOM   1501  CG  GLN C 300      -3.707 -18.160  42.700  1.00 24.83           C
ATOM   1502  CD  GLN C 300      -4.271 -17.249  43.802  1.00 27.61           C
ATOM   1503  OE1 GLN C 300      -5.455 -17.330  44.176  1.00 28.43           O
ATOM   1504  NE2 GLN C 300      -3.434 -16.322  44.273  1.00 25.01           N
ATOM   1505  N   ASN C 301      -4.210 -16.578  39.638  1.00 23.71           N
ATOM   1506  CA  ASN C 301      -3.475 -15.374  39.219  1.00 25.47           C
ATOM   1507  C   ASN C 301      -4.401 -14.247  38.749  1.00 23.96           C
ATOM   1508  O   ASN C 301      -4.149 -13.106  38.994  1.00 25.97           O
ATOM   1509  CB  ASN C 301      -2.423 -15.684  38.112  1.00 27.88           C
ATOM   1510  CG  ASN C 301      -1.278 -16.575  38.605  1.00 32.46           C
ATOM   1511  OD1 ASN C 301      -1.088 -16.815  39.809  1.00 34.45           O
ATOM   1512  ND2 ASN C 301      -0.516 -17.094  37.651  1.00 36.91           N
ATOM   1513  N   PHE C 302      -5.441 -14.567  38.015  1.00 25.16           N
ATOM   1514  CA  PHE C 302      -6.358 -13.574  37.564  1.00 25.50           C
ATOM   1515  C   PHE C 302      -7.107 -12.939  38.757  1.00 25.93           C
ATOM   1516  O   PHE C 302      -7.290 -11.704  38.833  1.00 25.49           O
ATOM   1517  CB  PHE C 302      -7.314 -14.272  36.607  1.00 27.92           C
ATOM   1518  CG  PHE C 302      -8.569 -13.528  36.344  1.00 28.49           C
ATOM   1519  CD1 PHE C 302      -8.554 -12.367  35.593  1.00 31.47           C
ATOM   1520  CD2 PHE C 302      -9.764 -14.012  36.813  1.00 30.84           C
ATOM   1521  CE1 PHE C 302      -9.715 -11.693  35.319  1.00 29.80           C
ATOM   1522  CE2 PHE C 302     -10.940 -13.341  36.538  1.00 32.07           C
ATOM   1523  CZ  PHE C 302     -10.902 -12.175  35.819  1.00 32.58           C
ATOM   1524  N   LEU C 303      -7.548 -13.787  39.672  1.00 22.13           N
ATOM   1525  CA  LEU C 303      -8.294 -13.339  40.837  1.00 23.53           C
ATOM   1526  C   LEU C 303      -7.477 -12.520  41.847  1.00 25.63           C
ATOM   1527  O   LEU C 303      -7.919 -11.444  42.296  1.00 24.52           O
ATOM   1528  CB  LEU C 303      -8.918 -14.549  41.522  1.00 23.34           C
ATOM   1529  CG  LEU C 303      -9.907 -15.353  40.696  1.00 22.21           C
ATOM   1530  CD1 LEU C 303     -10.220 -16.612  41.456  1.00 24.78           C
ATOM   1531  CD2 LEU C 303     -11.171 -14.551  40.397  1.00 23.66           C
ATOM   1532  N   GLN C 304      -6.278 -13.014  42.176  1.00 24.95           N
ATOM   1533  CA  GLN C 304      -5.383 -12.333  43.087  1.00 24.37           C
ATOM   1534  C   GLN C 304      -5.073 -10.923  42.608  1.00 27.55           C
ATOM   1535  O   GLN C 304      -4.992  -9.966  43.421  1.00 27.66           O
ATOM   1536  CB  GLN C 304      -4.080 -13.140  43.260  1.00 25.04           C
ATOM   1537  CG  GLN C 304      -3.160 -12.707  44.403  1.00 22.44           C
ATOM   1538  CD  GLN C 304      -3.795 -12.950  45.732  1.00 23.68           C
ATOM   1539  OE1 GLN C 304      -4.136 -14.121  46.060  1.00 23.33           O
ATOM   1540  NE2 GLN C 304      -3.980 -11.867  46.526  1.00 21.12           N
ATOM   1541  N   LEU C 305      -4.896 -10.793  41.297  1.00 27.17           N
ATOM   1542  CA  LEU C 305      -4.578  -9.533  40.695  1.00 28.17           C
ATOM   1543  C   LEU C 305      -5.665  -8.488  40.952  1.00 27.71           C
ATOM   1544  O   LEU C 305      -5.355  -7.338  41.100  1.00 31.43           O
ATOM   1545  CB  LEU C 305      -4.364  -9.696  39.174  1.00 29.89           C
ATOM   1546  CG  LEU C 305      -4.012  -8.382  38.480  1.00 33.98           C
ATOM   1547  CD1 LEU C 305      -2.561  -7.981  38.757  1.00 33.34           C
ATOM   1548  CD2 LEU C 305      -4.294  -8.434  36.981  1.00 36.97           C
ATOM   1549  N   GLN C 306      -6.933  -8.883  40.993  1.00 27.26           N
ATOM   1550  CA  GLN C 306      -8.006  -7.907  41.172  1.00 29.74           C
ATOM   1551  C   GLN C 306      -7.825  -7.251  42.523  1.00 29.66           C
ATOM   1552  O   GLN C 306      -8.025  -6.048  42.650  1.00 35.50           O
ATOM   1553  CB  GLN C 306      -9.416  -8.523  41.076  1.00 28.84           C
ATOM   1554  CG  GLN C 306      -9.628  -9.480  39.925  1.00 30.00           C
ATOM   1555  CD  GLN C 306      -9.328  -8.855  38.584  1.00 32.36           C
ATOM   1556  OE1 GLN C 306      -9.880  -7.823  38.256  1.00 35.66           O
ATOM   1557  NE2 GLN C 306      -8.462  -9.479  37.806  1.00 33.29           N
ATOM   1558  N   SER C 307      -7.386  -8.016  43.515  1.00 27.26           N
ATOM   1559  CA  SER C 307      -7.156  -7.448  44.833  1.00 28.02           C
ATOM   1560  C   SER C 307      -5.776  -6.807  45.021  1.00 28.51           C
ATOM   1561  O   SER C 307      -5.661  -5.799  45.733  1.00 28.71           O
ATOM   1562  CB  SER C 307      -7.397  -8.524  45.919  1.00 29.58           C
ATOM   1563  OG  SER C 307      -8.767  -8.922  45.871  1.00 29.91           O
ATOM   1564  N   SER C 308      -4.730  -7.383  44.444  1.00 27.07           N
ATOM   1565  CA  SER C 308      -3.387  -6.879  44.726  1.00 32.94           C
ATOM   1566  C   SER C 308      -3.237  -5.484  44.100  1.00 32.71           C
ATOM   1567  O   SER C 308      -2.652  -4.584  44.695  1.00 37.89           O
ATOM   1568  CB  SER C 308      -2.290  -7.793  44.184  1.00 31.34           C
ATOM   1569  OG  SER C 308      -2.408  -7.904  42.784  1.00 35.40           O
ATOM   1570  N   ARG C 309      -3.787  -5.346  42.915  1.00 31.21           N
ATOM   1571  CA  ARG C 309      -3.747  -4.110  42.157  1.00 37.26           C
ATOM   1572  C   ARG C 309      -4.688  -3.041  42.718  1.00 36.32           C
ATOM   1573  O   ARG C 309      -4.359  -1.878  42.712  1.00 33.15           O
ATOM   1574  CB  ARG C 309      -4.153  -4.426  40.746  1.00 39.48           C
ATOM   1575  CG  ARG C 309      -4.123  -3.280  39.784  1.00 44.71           C
ATOM   1576  CD  ARG C 309      -4.467  -3.817  38.402  1.00 49.17           C
ATOM   1577  NE  ARG C 309      -5.820  -4.375  38.345  1.00 51.20           N
ATOM   1578  CZ  ARG C 309      -6.305  -5.096  37.339  1.00 54.57           C
ATOM   1579  NH1 ARG C 309      -5.552  -5.368  36.266  1.00 55.05           N
ATOM   1580  NH2 ARG C 309      -7.559  -5.547  37.403  1.00 55.87           N
ATOM   1581  N   SER C 310      -5.869  -3.447  43.172  1.00 34.57           N
ATOM   1582  CA  SER C 310      -6.806  -2.515  43.759  1.00 33.77           C
ATOM   1583  C   SER C 310      -6.498  -2.164  45.221  1.00 34.75           C
ATOM   1584  O   SER C 310      -7.070  -1.215  45.755  1.00 33.43           O
ATOM   1585  CB  SER C 310      -8.221  -3.080  43.647  1.00 32.87           C
ATOM   1586  OG  SER C 310      -8.376  -4.172  44.521  1.00 30.14           O
ATOM   1587  N   ASN C 311      -5.605  -2.925  45.861  1.00 34.63           N
ATOM   1588  CA  ASN C 311      -5.348  -2.810  47.306  1.00 35.96           C
ATOM   1589  C   ASN C 311      -6.580  -3.101  48.200  1.00 34.32           C
ATOM   1590  O   ASN C 311      -6.613  -2.665  49.369  1.00 36.80           O
ATOM   1591  CB  ASN C 311      -4.784  -1.416  47.645  1.00 36.07           C
ATOM   1592  CG  ASN C 311      -3.605  -1.063  46.787  1.00 41.05           C
ATOM   1593  OD1 ASN C 311      -2.558  -1.709  46.890  1.00 43.89           O
ATOM   1594  ND2 ASN C 311      -3.770  -0.057  45.890  1.00 36.58           N
ATOM   1595  N   ARG C 312      -7.563  -3.812  47.651  1.00 29.38           N
ATOM   1596  CA  ARG C 312      -8.820  -4.142  48.306  1.00 29.77           C
ATOM   1597  C   ARG C 312      -8.819  -5.593  48.833  1.00 28.78           C
ATOM   1598  O   ARG C 312      -8.152  -6.425  48.262  1.00 30.09           O
ATOM   1599  CB  ARG C 312      -9.940  -4.076  47.265  1.00 31.82           C
ATOM   1600  CG  ARG C 312     -10.050  -2.759  46.540  1.00 36.46           C
ATOM   1601  CD  ARG C 312     -10.932  -1.766  47.233  1.00 36.51           C
ATOM   1602  NE  ARG C 312     -10.964  -0.424  46.599  1.00 36.17           N
ATOM   1603  CZ  ARG C 312     -11.099   0.710  47.294  1.00 35.94           C
ATOM   1604  NH1 ARG C 312     -11.155   1.894  46.655  1.00 34.67           N
ATOM   1605  NH2 ARG C 312     -11.170   0.660  48.649  1.00 32.29           N
ATOM   1606  N   PHE C 313      -9.631  -5.884  49.848  1.00 24.24           N
ATOM   1607  CA  PHE C 313      -9.714  -7.184  50.467  1.00 23.49           C
ATOM   1608  C   PHE C 313     -10.987  -7.833  49.980  1.00 24.76           C
ATOM   1609  O   PHE C 313     -12.073  -7.224  50.014  1.00 20.00           O
ATOM   1610  CB  PHE C 313      -9.772  -7.053  51.981  1.00 27.42           C
ATOM   1611  CG  PHE C 313      -8.566  -6.390  52.594  1.00 27.78           C
ATOM   1612  CD1 PHE C 313      -7.278  -6.724  52.201  1.00 28.13           C
ATOM   1613  CD2 PHE C 313      -8.725  -5.465  53.625  1.00 26.26           C
ATOM   1614  CE1 PHE C 313      -6.165  -6.092  52.797  1.00 28.30           C
ATOM   1615  CE2 PHE C 313      -7.631  -4.904  54.255  1.00 27.28           C
ATOM   1616  CZ  PHE C 313      -6.353  -5.197  53.833  1.00 26.89           C
ATOM   1617  N   THR C 314     -10.849  -9.068  49.497  1.00 23.92           N
ATOM   1618  CA  THR C 314     -11.911  -9.714  48.783  1.00 23.59           C
ATOM   1619  C   THR C 314     -12.131 -11.182  49.220  1.00 23.36           C
ATOM   1620  O   THR C 314     -11.200 -11.997  49.280  1.00 20.54           O
ATOM   1621  CB  THR C 314     -11.583  -9.660  47.257  1.00 24.88           C
ATOM   1622  OG1 THR C 314     -11.315  -8.290  46.853  1.00 25.34           O
ATOM   1623  CG2 THR C 314     -12.724 -10.163  46.487  1.00 22.35           C
ATOM   1624  N   TRP C 315     -13.377 -11.564  49.442  1.00 23.92           N
ATOM   1625  CA  TRP C 315     -13.624 -12.935  49.897  1.00 24.85           C
ATOM   1626  C   TRP C 315     -13.577 -13.914  48.730  1.00 24.57           C
ATOM   1627  O   TRP C 315     -13.930 -13.557  47.613  1.00 22.34           O
ATOM   1628  CB  TRP C 315     -15.003 -13.124  50.503  1.00 25.76           C
ATOM   1629  CG  TRP C 315     -15.345 -12.436  51.799  1.00 24.55           C
ATOM   1630  CD1 TRP C 315     -16.395 -11.578  52.009  1.00 26.08           C
ATOM   1631  CD2 TRP C 315     -14.729 -12.617  53.062  1.00 25.28           C
ATOM   1632  NE1 TRP C 315     -16.473 -11.221  53.319  1.00 23.58           N
ATOM   1633  CE2 TRP C 315     -15.440 -11.833  53.986  1.00 24.25           C
ATOM   1634  CE3 TRP C 315     -13.648 -13.371  53.506  1.00 24.07           C
ATOM   1635  CZ2 TRP C 315     -15.103 -11.789  55.298  1.00 24.40           C
ATOM   1636  CZ3 TRP C 315     -13.307 -13.312  54.792  1.00 28.34           C
ATOM   1637  CH2 TRP C 315     -14.024 -12.537  55.701  1.00 25.87           C
ATOM   1638  N   MET C 316     -13.222 -15.162  49.045  1.00 22.33           N
ATOM   1639  CA  MET C 316     -13.363 -16.262  48.119  1.00 23.43           C
ATOM   1640  C   MET C 316     -14.220 -17.293  48.849  1.00 21.92           C
ATOM   1641  O   MET C 316     -14.435 -17.139  50.073  1.00 20.78           O
ATOM   1642  CB  MET C 316     -12.001 -16.776  47.715  1.00 23.80           C
ATOM   1643  CG  MET C 316     -11.246 -17.426  48.827  1.00 26.58           C
ATOM   1644  SD  MET C 316      -9.617 -18.025  48.373  1.00 26.92           S
ATOM   1645  CE  MET C 316      -8.662 -16.510  48.478  1.00 27.93           C
ATOM   1646  N   GLY C 317     -14.731 -18.291  48.115  1.00 21.35           N
ATOM   1647  CA  GLY C 317     -15.592 -19.351  48.685  1.00 22.95           C
ATOM   1648  C   GLY C 317     -14.788 -20.496  49.339  1.00 23.17           C
ATOM   1649  O   GLY C 317     -14.860 -21.665  48.882  1.00 27.26           O
ATOM   1650  N   LEU C 318     -13.969 -20.141  50.333  1.00 23.74           N
ATOM   1651  CA  LEU C 318     -13.063 -21.057  51.052  1.00 24.37           C
ATOM   1652  C   LEU C 318     -13.146 -20.744  52.535  1.00 24.82           C
ATOM   1653  O   LEU C 318     -12.984 -19.604  52.907  1.00 27.13           O
ATOM   1654  CB  LEU C 318     -11.661 -20.843  50.584  1.00 25.39           C
ATOM   1655  CG  LEU C 318     -10.571 -21.736  51.167  1.00 25.68           C
ATOM   1656  CD1 LEU C 318     -10.720 -23.187  50.778  1.00 26.29           C
ATOM   1657  CD2 LEU C 318      -9.217 -21.232  50.734  1.00 26.55           C
ATOM   1658  N   SER C 319     -13.451 -21.754  53.352  1.00 23.61           N
ATOM   1659  CA  SER C 319     -13.536 -21.634  54.772  1.00 26.21           C
ATOM   1660  C   SER C 319     -13.031 -22.891  55.526  1.00 28.54           C
ATOM   1661  O   SER C 319     -12.872 -23.987  54.940  1.00 29.57           O
ATOM   1662  CB  SER C 319     -14.967 -21.355  55.170  1.00 26.63           C
ATOM   1663  OG  SER C 319     -15.675 -22.570  55.212  1.00 28.31           O
ATOM   1664  N   ASP C 320     -12.756 -22.723  56.823  1.00 28.11           N
ATOM   1665  CA  ASP C 320     -12.512 -23.864  57.747  1.00 27.60           C
ATOM   1666  C   ASP C 320     -13.456 -23.796  58.922  1.00 30.71           C
ATOM   1667  O   ASP C 320     -13.110 -24.209  60.039  1.00 28.79           O
ATOM   1668  CB  ASP C 320     -11.063 -23.956  58.222  1.00 27.68           C
ATOM   1669  CG  ASP C 320     -10.653 -22.864  59.288  1.00 29.41           C
ATOM   1670  OD1 ASP C 320     -11.376 -21.844  59.514  1.00 29.73           O
ATOM   1671  OD2 ASP C 320      -9.541 -23.023  59.885  1.00 27.72           O
ATOM   1672  N   LEU C 321     -14.640 -23.257  58.658  1.00 28.09           N
ATOM   1673  CA  LEU C 321     -15.726 -23.229  59.620  1.00 29.60           C
ATOM   1674  C   LEU C 321     -16.134 -24.593  60.140  1.00 32.58           C
ATOM   1675  O   LEU C 321     -16.485 -24.711  61.316  1.00 34.65           O
ATOM   1676  CB  LEU C 321     -16.992 -22.625  58.982  1.00 29.76           C
ATOM   1677  CG  LEU C 321     -16.967 -21.093  58.822  1.00 31.85           C
ATOM   1678  CD1 LEU C 321     -17.996 -20.610  57.798  1.00 31.56           C
ATOM   1679  CD2 LEU C 321     -17.165 -20.466  60.188  1.00 32.45           C
ATOM   1680  N   ASN C 322     -16.155 -25.601  59.267  1.00 33.20           N
ATOM   1681  CA AASN C 322     -16.649 -26.910  59.661  0.70 37.44           C
ATOM   1682  CA BASN C 322     -16.647 -26.929  59.641  0.30 34.98           C
ATOM   1683  C   ASN C 322     -15.636 -27.661  60.498  1.00 37.55           C
ATOM   1684  O   ASN C 322     -15.993 -28.265  61.501  1.00 37.91           O
ATOM   1685  CB AASN C 322     -17.019 -27.721  58.442  0.70 41.34           C
ATOM   1686  CB BASN C 322     -16.952 -27.796  58.423  0.30 35.28           C
ATOM   1687  CG AASN C 322     -18.262 -27.207  57.775  0.70 41.78           C
ATOM   1688  CG BASN C 322     -17.313 -29.225  58.814  0.30 34.37           C
ATOM   1689  OD1AASN C 322     -19.087 -26.530  58.404  0.70 45.68           O
ATOM   1690  OD1BASN C 322     -18.111 -29.434  59.725  0.30 33.66           O
ATOM   1691  ND2AASN C 322     -18.406 -27.512  56.495  0.70 42.59           N
ATOM   1692  ND2BASN C 322     -16.708 -30.208  58.144  0.30 32.12           N
ATOM   1693  N   GLN C 323     -14.379 -27.601  60.088  1.00 34.32           N
ATOM   1694  CA  GLN C 323     -13.329 -28.313  60.785  1.00 34.45           C
ATOM   1695  C   GLN C 323     -12.094 -27.412  60.846  1.00 32.09           C
ATOM   1696  O   GLN C 323     -11.347 -27.235  59.836  1.00 32.08           O
ATOM   1697  CB  GLN C 323     -13.037 -29.621  60.059  1.00 31.93           C
ATOM   1698  CG  GLN C 323     -11.846 -30.392  60.601  1.00 34.69           C
ATOM   1699  CD  GLN C 323     -12.168 -31.144  61.882  1.00 40.35           C
ATOM   1700  OE1 GLN C 323     -13.337 -31.362  62.217  1.00 46.47           O
ATOM   1701  NE2 GLN C 323     -11.126 -31.562  62.600  1.00 42.33           N
ATOM   1702  N   GLU C 324     -11.895 -26.841  62.020  1.00 30.19           N
ATOM   1703  CA  GLU C 324     -10.814 -25.912  62.255  1.00 31.42           C
ATOM   1704  C   GLU C 324      -9.534 -26.458  61.696  1.00 30.28           C
ATOM   1705  O   GLU C 324      -9.182 -27.578  61.991  1.00 31.06           O
ATOM   1706  CB  GLU C 324     -10.658 -25.558  63.748  1.00 31.52           C
ATOM   1707  CG  GLU C 324      -9.465 -24.629  64.052  1.00 30.70           C
ATOM   1708  CD  GLU C 324      -9.477 -23.340  63.214  1.00 30.84           C
ATOM   1709  OE1 GLU C 324     -10.576 -22.758  62.974  1.00 29.82           O
ATOM   1710  OE2 GLU C 324      -8.378 -22.916  62.803  1.00 29.47           O
ATOM   1711  N   GLY C 325      -8.894 -25.694  60.806  1.00 30.15           N
ATOM   1712  CA  GLY C 325      -7.605 -26.090  60.197  1.00 29.79           C
ATOM   1713  C   GLY C 325      -7.728 -26.858  58.899  1.00 32.45           C
ATOM   1714  O   GLY C 325      -6.712 -27.061  58.178  1.00 32.02           O
ATOM   1715  N   THR C 326      -8.966 -27.276  58.568  1.00 31.50           N
ATOM   1716  CA  THR C 326      -9.219 -27.896  57.283  1.00 28.06           C
ATOM   1717  C   THR C 326     -10.045 -26.990  56.346  1.00 29.69           C
ATOM   1718  O   THR C 326     -11.250 -26.792  56.571  1.00 26.60           O
ATOM   1719  CB  THR C 326      -9.844 -29.294  57.440  1.00 29.84           C
ATOM   1720  OG1 THR C 326      -8.867 -30.146  58.044  1.00 32.83           O
ATOM   1721  CG2 THR C 326     -10.200 -29.881  56.080  1.00 27.69           C
ATOM   1722  N   TRP C 327      -9.386 -26.504  55.270  1.00 27.46           N
ATOM   1723  CA  TRP C 327     -10.009 -25.571  54.338  1.00 29.87           C
ATOM   1724  C   TRP C 327     -10.763 -26.261  53.220  1.00 28.64           C
ATOM   1725  O   TRP C 327     -10.262 -27.148  52.517  1.00 30.61           O
ATOM   1726  CB  TRP C 327      -8.993 -24.568  53.813  1.00 29.99           C
ATOM   1727  CG  TRP C 327      -8.522 -23.741  54.926  1.00 31.85           C
ATOM   1728  CD1 TRP C 327      -7.531 -24.056  55.825  1.00 32.21           C
ATOM   1729  CD2 TRP C 327      -9.062 -22.485  55.345  1.00 30.53           C
ATOM   1730  NE1 TRP C 327      -7.413 -23.061  56.759  1.00 29.73           N
ATOM   1731  CE2 TRP C 327      -8.329 -22.083  56.490  1.00 30.08           C
ATOM   1732  CE3 TRP C 327     -10.087 -21.649  54.859  1.00 28.52           C
ATOM   1733  CZ2 TRP C 327      -8.578 -20.882  57.157  1.00 28.98           C
ATOM   1734  CZ3 TRP C 327     -10.323 -20.438  55.517  1.00 30.47           C
ATOM   1735  CH2 TRP C 327      -9.573 -20.076  56.666  1.00 31.34           C
ATOM   1736  N   GLN C 328     -11.985 -25.806  53.055  1.00 29.24           N
ATOM   1737  CA  GLN C 328     -12.936 -26.392  52.146  1.00 29.88           C
ATOM   1738  C   GLN C 328     -13.577 -25.330  51.292  1.00 26.63           C
ATOM   1739  O   GLN C 328     -14.053 -24.323  51.791  1.00 26.36           O
ATOM   1740  CB  GLN C 328     -14.028 -27.089  52.949  1.00 36.09           C
ATOM   1741  CG  GLN C 328     -14.887 -28.005  52.099  1.00 43.50           C
ATOM   1742  CD  GLN C 328     -15.733 -28.977  52.928  1.00 50.91           C
ATOM   1743  OE1 GLN C 328     -16.043 -30.078  52.467  1.00 57.48           O
ATOM   1744  NE2 GLN C 328     -16.107 -28.576  54.148  1.00 56.30           N
ATOM   1745  N   TRP C 329     -13.626 -25.583  49.988  1.00 26.72           N
ATOM   1746  CA  TRP C 329     -14.296 -24.715  49.067  1.00 24.07           C
ATOM   1747  C   TRP C 329     -15.771 -24.938  49.257  1.00 24.23           C
ATOM   1748  O   TRP C 329     -16.177 -26.009  49.701  1.00 24.39           O
ATOM   1749  CB  TRP C 329     -13.889 -25.010  47.628  1.00 25.15           C
ATOM   1750  CG  TRP C 329     -12.462 -24.770  47.311  1.00 23.63           C
ATOM   1751  CD1 TRP C 329     -11.514 -25.691  47.210  1.00 24.31           C
ATOM   1752  CD2 TRP C 329     -11.817 -23.494  47.084  1.00 24.81           C
ATOM   1753  NE1 TRP C 329     -10.297 -25.108  46.910  1.00 25.80           N
ATOM   1754  CE2 TRP C 329     -10.465 -23.754  46.824  1.00 23.28           C
ATOM   1755  CE3 TRP C 329     -12.256 -22.162  47.107  1.00 25.19           C
ATOM   1756  CZ2 TRP C 329      -9.542 -22.747  46.579  1.00 23.64           C
ATOM   1757  CZ3 TRP C 329     -11.327 -21.150  46.861  1.00 23.77           C
ATOM   1758  CH2 TRP C 329      -9.995 -21.448  46.600  1.00 23.95           C
ATOM   1759  N   VAL C 330     -16.574 -23.935  48.920  1.00 25.07           N
ATOM   1760  CA  VAL C 330     -18.039 -23.982  49.115  1.00 26.78           C
ATOM   1761  C   VAL C 330     -18.734 -24.978  48.217  1.00 28.03           C
ATOM   1762  O   VAL C 330     -19.860 -25.331  48.488  1.00 27.67           O
ATOM   1763  CB  VAL C 330     -18.742 -22.590  48.937  1.00 28.02           C
ATOM   1764  CG1 VAL C 330     -18.348 -21.669  50.062  1.00 28.29           C
ATOM   1765  CG2 VAL C 330     -18.375 -21.896  47.647  1.00 28.64           C
ATOM   1766  N   ASP C 331     -18.087 -25.391  47.121  1.00 29.12           N
ATOM   1767  CA  ASP C 331     -18.645 -26.428  46.280  1.00 29.82           C
ATOM   1768  C   ASP C 331     -18.334 -27.800  46.853  1.00 32.29           C
ATOM   1769  O   ASP C 331     -18.602 -28.790  46.190  1.00 34.16           O
ATOM   1770  CB  ASP C 331     -18.108 -26.369  44.837  1.00 28.81           C
ATOM   1771  CG  ASP C 331     -16.671 -26.743  44.753  1.00 29.06           C
ATOM   1772  OD1 ASP C 331     -16.068 -26.898  45.818  1.00 30.05           O
ATOM   1773  OD2 ASP C 331     -16.108 -26.851  43.649  1.00 34.76           O
ATOM   1774  N   GLY C 332     -17.711 -27.867  48.020  1.00 30.41           N
ATOM   1775  CA  GLY C 332     -17.430 -29.157  48.675  1.00 35.00           C
ATOM   1776  C   GLY C 332     -16.004 -29.693  48.444  1.00 35.09           C
ATOM   1777  O   GLY C 332     -15.544 -30.584  49.156  1.00 37.93           O
ATOM   1778  N   SER C 333     -15.301 -29.135  47.465  1.00 31.43           N
ATOM   1779  CA  SER C 333     -14.024 -29.662  47.055  1.00 31.48           C
ATOM   1780  C   SER C 333     -13.013 -29.237  48.104  1.00 32.91           C
ATOM   1781  O   SER C 333     -13.227 -28.246  48.821  1.00 33.00           O
ATOM   1782  CB  SER C 333     -13.629 -29.165  45.641  1.00 32.27           C
ATOM   1783  OG  SER C 333     -13.560 -27.743  45.582  1.00 36.38           O
ATOM   1784  N   PRO C 334     -11.919 -29.992  48.209  1.00 33.63           N
ATOM   1785  CA  PRO C 334     -10.908 -29.784  49.224  1.00 32.01           C
ATOM   1786  C   PRO C 334      -9.885 -28.781  48.763  1.00 33.49           C
ATOM   1787  O   PRO C 334      -9.677 -28.640  47.568  1.00 33.32           O
ATOM   1788  CB  PRO C 334     -10.252 -31.175  49.332  1.00 34.12           C
ATOM   1789  CG  PRO C 334     -10.376 -31.762  47.953  1.00 33.29           C
ATOM   1790  CD  PRO C 334     -11.676 -31.232  47.423  1.00 34.73           C
ATOM   1791  N   LEU C 335      -9.222 -28.107  49.695  1.00 34.10           N
ATOM   1792  CA  LEU C 335      -8.097 -27.303  49.313  1.00 33.04           C
ATOM   1793  C   LEU C 335      -6.917 -28.225  49.058  1.00 36.36           C
ATOM   1794  O   LEU C 335      -6.380 -28.822  49.993  1.00 38.42           O
ATOM   1795  CB  LEU C 335      -7.741 -26.309  50.398  1.00 34.14           C
ATOM   1796  CG  LEU C 335      -6.539 -25.406  50.035  1.00 33.91           C
ATOM   1797  CD1 LEU C 335      -6.811 -24.475  48.849  1.00 31.59           C
ATOM   1798  CD2 LEU C 335      -6.191 -24.605  51.272  1.00 33.61           C
ATOM   1799  N   LEU C 336      -6.476 -28.290  47.808  1.00 35.66           N
ATOM   1800  CA  LEU C 336      -5.397 -29.185  47.405  1.00 33.63           C
ATOM   1801  C   LEU C 336      -4.049 -28.688  47.922  1.00 35.03           C
ATOM   1802  O   LEU C 336      -3.841 -27.470  48.055  1.00 36.26           O
ATOM   1803  CB  LEU C 336      -5.355 -29.340  45.882  1.00 33.24           C
ATOM   1804  CG  LEU C 336      -6.598 -29.996  45.250  1.00 37.38           C
ATOM   1805  CD1 LEU C 336      -6.496 -29.945  43.723  1.00 38.30           C
ATOM   1806  CD2 LEU C 336      -6.805 -31.430  45.699  1.00 36.97           C
ATOM   1807  N   PRO C 337      -3.115 -29.620  48.200  1.00 35.94           N
ATOM   1808  CA  PRO C 337      -1.790 -29.227  48.713  1.00 37.73           C
ATOM   1809  C   PRO C 337      -1.037 -28.222  47.845  1.00 34.22           C
ATOM   1810  O   PRO C 337      -0.326 -27.381  48.383  1.00 33.04           O
ATOM   1811  CB  PRO C 337      -1.024 -30.563  48.771  1.00 40.37           C
ATOM   1812  CG  PRO C 337      -2.110 -31.603  48.968  1.00 39.13           C
ATOM   1813  CD  PRO C 337      -3.248 -31.092  48.120  1.00 39.53           C
ATOM   1814  N   SER C 338      -1.209 -28.302  46.528  1.00 34.87           N
ATOM   1815  CA  SER C 338      -0.563 -27.381  45.570  1.00 36.72           C
ATOM   1816  C   SER C 338      -1.050 -25.927  45.623  1.00 36.27           C
ATOM   1817  O   SER C 338      -0.473 -25.070  44.938  1.00 35.37           O
ATOM   1818  CB  SER C 338      -0.824 -27.882  44.154  1.00 38.58           C
ATOM   1819  OG  SER C 338      -2.225 -28.065  43.999  1.00 41.56           O
ATOM   1820  N   PHE C 339      -2.141 -25.685  46.368  1.00 34.54           N
ATOM   1821  CA  PHE C 339      -2.728 -24.340  46.583  1.00 34.79           C
ATOM   1822  C   PHE C 339      -2.291 -23.743  47.899  1.00 35.74           C
ATOM   1823  O   PHE C 339      -2.580 -22.587  48.160  1.00 34.68           O
ATOM   1824  CB  PHE C 339      -4.272 -24.381  46.522  1.00 34.41           C
ATOM   1825  CG  PHE C 339      -4.794 -24.548  45.129  1.00 38.40           C
ATOM   1826  CD1 PHE C 339      -4.604 -25.731  44.448  1.00 40.18           C
ATOM   1827  CD2 PHE C 339      -5.400 -23.491  44.458  1.00 43.31           C
ATOM   1828  CE1 PHE C 339      -5.018 -25.883  43.131  1.00 41.33           C
ATOM   1829  CE2 PHE C 339      -5.824 -23.637  43.136  1.00 45.82           C
ATOM   1830  CZ  PHE C 339      -5.628 -24.838  42.469  1.00 40.69           C
ATOM   1831  N   LYS C 340      -1.575 -24.506  48.727  1.00 33.98           N
ATOM   1832  CA  LYS C 340      -1.211 -24.006  50.041  1.00 35.97           C
ATOM   1833  C   LYS C 340      -0.156 -22.905  50.005  1.00 32.50           C
ATOM   1834  O   LYS C 340      -0.111 -22.040  50.874  1.00 31.99           O
ATOM   1835  CB  LYS C 340      -0.879 -25.158  50.943  1.00 39.77           C
ATOM   1836  CG  LYS C 340      -2.180 -25.808  51.322  1.00 44.24           C
ATOM   1837  CD  LYS C 340      -2.061 -27.115  52.077  1.00 47.59           C
ATOM   1838  CE  LYS C 340      -3.373 -27.372  52.807  1.00 51.09           C
ATOM   1839  NZ  LYS C 340      -3.910 -28.726  52.520  1.00 56.90           N
ATOM   1840  N   GLN C 341       0.592 -22.885  48.919  1.00 28.65           N
ATOM   1841  CA  GLN C 341       1.531 -21.842  48.597  1.00 30.11           C
ATOM   1842  C   GLN C 341       0.924 -20.451  48.434  1.00 29.89           C
ATOM   1843  O   GLN C 341       1.639 -19.464  48.489  1.00 28.88           O
ATOM   1844  CB  GLN C 341       2.242 -22.189  47.285  1.00 31.98           C
ATOM   1845  CG  GLN C 341       1.350 -22.219  46.062  1.00 32.34           C
ATOM   1846  CD  GLN C 341       2.112 -22.590  44.801  1.00 37.37           C
ATOM   1847  OE1 GLN C 341       2.883 -21.800  44.280  1.00 36.65           O
ATOM   1848  NE2 GLN C 341       1.862 -23.787  44.280  1.00 37.17           N
ATOM   1849  N   TYR C 342      -0.381 -20.352  48.205  1.00 27.10           N
ATOM   1850  CA  TYR C 342      -0.944 -19.045  47.932  1.00 29.03           C
ATOM   1851  C   TYR C 342      -1.239 -18.257  49.214  1.00 27.26           C
ATOM   1852  O   TYR C 342      -1.503 -17.059  49.145  1.00 29.50           O
ATOM   1853  CB  TYR C 342      -2.220 -19.155  47.011  1.00 27.93           C
ATOM   1854  CG  TYR C 342      -1.908 -19.697  45.635  1.00 26.40           C
ATOM   1855  CD1 TYR C 342      -0.948 -19.116  44.860  1.00 26.60           C
ATOM   1856  CD2 TYR C 342      -2.551 -20.838  45.142  1.00 28.76           C
ATOM   1857  CE1 TYR C 342      -0.628 -19.621  43.618  1.00 28.13           C
ATOM   1858  CE2 TYR C 342      -2.235 -21.353  43.889  1.00 27.47           C
ATOM   1859  CZ  TYR C 342      -1.278 -20.721  43.136  1.00 26.97           C
ATOM   1860  OH  TYR C 342      -0.965 -21.172  41.893  1.00 29.91           O
ATOM   1861  N   TRP C 343      -1.238 -18.923  50.358  1.00 29.89           N
ATOM   1862  CA  TRP C 343      -1.420 -18.246  51.646  1.00 30.48           C
ATOM   1863  C   TRP C 343      -0.262 -17.309  51.826  1.00 32.32           C
ATOM   1864  O   TRP C 343       0.849 -17.733  51.545  1.00 27.49           O
ATOM   1865  CB  TRP C 343      -1.343 -19.225  52.810  1.00 28.72           C
ATOM   1866  CG  TRP C 343      -2.504 -20.173  52.966  1.00 31.52           C
ATOM   1867  CD1 TRP C 343      -2.476 -21.546  52.844  1.00 29.60           C
ATOM   1868  CD2 TRP C 343      -3.842 -19.836  53.344  1.00 29.88           C
ATOM   1869  NE1 TRP C 343      -3.717 -22.073  53.133  1.00 28.33           N
ATOM   1870  CE2 TRP C 343      -4.568 -21.053  53.450  1.00 29.46           C
ATOM   1871  CE3 TRP C 343      -4.494 -18.627  53.649  1.00 27.35           C
ATOM   1872  CZ2 TRP C 343      -5.932 -21.091  53.793  1.00 30.72           C
ATOM   1873  CZ3 TRP C 343      -5.854 -18.672  53.996  1.00 29.85           C
ATOM   1874  CH2 TRP C 343      -6.567 -19.901  54.032  1.00 27.62           C
ATOM   1875  N   ASN C 344      -0.519 -16.082  52.296  1.00 29.31           N
ATOM   1876  CA  ASN C 344       0.540 -15.155  52.744  1.00 32.16           C
ATOM   1877  C   ASN C 344       1.412 -15.794  53.816  1.00 30.54           C
ATOM   1878  O   ASN C 344       0.932 -16.644  54.603  1.00 30.57           O
ATOM   1879  CB  ASN C 344      -0.066 -13.865  53.360  1.00 32.86           C
ATOM   1880  CG  ASN C 344      -0.866 -13.039  52.346  1.00 31.35           C
ATOM   1881  OD1 ASN C 344      -0.560 -13.074  51.169  1.00 27.58           O
ATOM   1882  ND2 ASN C 344      -1.929 -12.340  52.804  1.00 27.72           N
ATOM   1883  N   ARG C 345       2.654 -15.328  53.918  1.00 33.66           N
ATOM   1884  CA  ARG C 345       3.578 -15.810  54.975  1.00 35.83           C
ATOM   1885  C   ARG C 345       2.857 -15.787  56.313  1.00 31.43           C
ATOM   1886  O   ARG C 345       2.215 -14.817  56.620  1.00 28.78           O
ATOM   1887  CB  ARG C 345       4.840 -14.953  55.078  1.00 43.76           C
ATOM   1888  CG  ARG C 345       5.967 -15.648  55.873  1.00 55.08           C
ATOM   1889  CD  ARG C 345       6.743 -14.776  56.888  1.00 62.02           C
ATOM   1890  NE  ARG C 345       5.905 -14.245  57.999  1.00 73.42           N
ATOM   1891  CZ  ARG C 345       5.515 -14.904  59.107  1.00 67.94           C
ATOM   1892  NH1 ARG C 345       5.863 -16.174  59.347  1.00 68.08           N
ATOM   1893  NH2 ARG C 345       4.750 -14.280  59.993  1.00 65.10           N
ATOM   1894  N   GLY C 346       2.897 -16.879  57.065  1.00 27.71           N
ATOM   1895  CA  GLY C 346       2.319 -16.918  58.385  1.00 27.21           C
ATOM   1896  C   GLY C 346       0.852 -17.256  58.417  1.00 28.20           C
ATOM   1897  O   GLY C 346       0.300 -17.436  59.497  1.00 29.94           O
ATOM   1898  N   GLU C 347       0.218 -17.357  57.246  1.00 30.07           N
ATOM   1899  CA  GLU C 347      -1.191 -17.708  57.176  1.00 30.63           C
ATOM   1900  C   GLU C 347      -1.380 -19.167  56.690  1.00 32.46           C
ATOM   1901  O   GLU C 347      -0.577 -19.640  55.891  1.00 32.56           O
ATOM   1902  CB  GLU C 347      -1.901 -16.715  56.254  1.00 31.03           C
ATOM   1903  CG  GLU C 347      -1.577 -15.216  56.515  1.00 31.97           C
ATOM   1904  CD  GLU C 347      -2.092 -14.705  57.860  1.00 33.19           C
ATOM   1905  OE1 GLU C 347      -2.847 -15.474  58.527  1.00 33.41           O
ATOM   1906  OE2 GLU C 347      -1.772 -13.520  58.237  1.00 31.34           O
ATOM   1907  N   PRO C 348      -2.460 -19.842  57.084  1.00 29.71           N
ATOM   1908  CA  PRO C 348      -3.532 -19.240  57.888  1.00 32.11           C
ATOM   1909  C   PRO C 348      -3.216 -19.405  59.363  1.00 32.42           C
ATOM   1910  O   PRO C 348      -2.594 -20.401  59.720  1.00 35.93           O
ATOM   1911  CB  PRO C 348      -4.769 -20.049  57.498  1.00 30.71           C
ATOM   1912  CG  PRO C 348      -4.226 -21.421  57.127  1.00 30.87           C
ATOM   1913  CD  PRO C 348      -2.789 -21.227  56.677  1.00 30.76           C
ATOM   1914  N   ASN C 349      -3.628 -18.469  60.220  1.00 28.85           N
ATOM   1915  CA  ASN C 349      -3.156 -18.531  61.611  1.00 30.65           C
ATOM   1916  C   ASN C 349      -4.295 -18.561  62.618  1.00 32.72           C
ATOM   1917  O   ASN C 349      -4.058 -18.717  63.815  1.00 33.07           O
ATOM   1918  CB  ASN C 349      -2.191 -17.373  61.934  1.00 28.51           C
ATOM   1919  CG  ASN C 349      -2.827 -15.999  61.699  1.00 27.80           C
ATOM   1920  OD1 ASN C 349      -4.005 -15.915  61.343  1.00 25.42           O
ATOM   1921  ND2 ASN C 349      -2.038 -14.926  61.840  1.00 26.69           N
ATOM   1922  N   ASN C 350      -5.513 -18.357  62.159  1.00 26.80           N
ATOM   1923  CA  ASN C 350      -6.660 -18.427  63.035  1.00 27.69           C
ATOM   1924  C   ASN C 350      -6.600 -17.454  64.191  1.00 28.45           C
ATOM   1925  O   ASN C 350      -7.180 -17.707  65.236  1.00 27.19           O
ATOM   1926  CB  ASN C 350      -6.853 -19.828  63.605  1.00 26.57           C
ATOM   1927  CG  ASN C 350      -8.264 -20.076  64.020  1.00 26.44           C
ATOM   1928  OD1 ASN C 350      -9.230 -19.638  63.354  1.00 28.48           O
ATOM   1929  ND2 ASN C 350      -8.426 -20.811  65.081  1.00 28.69           N
ATOM   1930  N   VAL C 351      -5.918 -16.337  63.990  1.00 28.11           N
ATOM   1931  CA  VAL C 351      -5.714 -15.435  65.083  1.00 32.27           C
ATOM   1932  C   VAL C 351      -7.008 -14.681  65.430  1.00 30.54           C
ATOM   1933  O   VAL C 351      -7.569 -13.969  64.598  1.00 30.20           O
ATOM   1934  CB  VAL C 351      -4.512 -14.516  64.833  1.00 32.26           C
ATOM   1935  CG1 VAL C 351      -4.783 -13.542  63.705  1.00 33.73           C
ATOM   1936  CG2 VAL C 351      -4.168 -13.793  66.129  1.00 34.15           C
ATOM   1937  N   GLY C 352      -7.498 -14.911  66.646  1.00 32.30           N
ATOM   1938  CA  GLY C 352      -8.789 -14.386  67.075  1.00 33.54           C
ATOM   1939  C   GLY C 352      -9.997 -15.123  66.483  1.00 36.13           C
ATOM   1940  O   GLY C 352     -11.109 -14.566  66.430  1.00 36.75           O
ATOM   1941  N   GLU C 353      -9.780 -16.355  66.015  1.00 34.12           N
ATOM   1942  CA  GLU C 353     -10.806 -17.146  65.276  1.00 34.87           C
ATOM   1943  C   GLU C 353     -11.084 -16.603  63.889  1.00 28.92           C
ATOM   1944  O   GLU C 353     -11.917 -15.727  63.691  1.00 26.00           O
ATOM   1945  CB  GLU C 353     -12.112 -17.271  66.052  1.00 39.26           C
ATOM   1946  CG  GLU C 353     -11.894 -17.762  67.472  1.00 47.91           C
ATOM   1947  CD  GLU C 353     -11.867 -19.276  67.598  1.00 59.42           C
ATOM   1948  OE1 GLU C 353     -12.695 -19.773  68.392  1.00 70.48           O
ATOM   1949  OE2 GLU C 353     -11.042 -19.966  66.926  1.00 66.69           O
ATOM   1950  N   GLU C 354     -10.365 -17.125  62.915  1.00 28.46           N
ATOM   1951  CA  GLU C 354     -10.498 -16.649  61.566  1.00 26.36           C
ATOM   1952  C   GLU C 354     -10.849 -17.813  60.690  1.00 26.15           C
ATOM   1953  O   GLU C 354     -10.015 -18.682  60.449  1.00 23.02           O
ATOM   1954  CB  GLU C 354      -9.185 -16.028  61.108  1.00 27.89           C
ATOM   1955  CG  GLU C 354      -8.826 -14.725  61.817  1.00 27.29           C
ATOM   1956  CD  GLU C 354      -7.577 -14.048  61.276  1.00 26.88           C
ATOM   1957  OE1 GLU C 354      -6.551 -14.753  61.077  1.00 24.84           O
ATOM   1958  OE2 GLU C 354      -7.606 -12.785  61.078  1.00 25.06           O
ATOM   1959  N   ASP C 355     -12.061 -17.830  60.152  1.00 27.71           N
ATOM   1960  CA  ASP C 355     -12.496 -19.032  59.406  1.00 26.77           C
ATOM   1961  C   ASP C 355     -12.822 -18.875  57.915  1.00 27.09           C
ATOM   1962  O   ASP C 355     -13.169 -19.848  57.280  1.00 27.47           O
ATOM   1963  CB  ASP C 355     -13.661 -19.699  60.118  1.00 26.00           C
ATOM   1964  CG  ASP C 355     -13.301 -20.172  61.513  1.00 26.34           C
ATOM   1965  OD1 ASP C 355     -12.095 -20.226  61.831  1.00 28.36           O
ATOM   1966  OD2 ASP C 355     -14.225 -20.489  62.291  1.00 28.30           O
ATOM   1967  N   CYS C 356     -12.659 -17.673  57.375  1.00 25.93           N
ATOM   1968  CA  CYS C 356     -12.958 -17.366  56.014  1.00 26.39           C
ATOM   1969  C   CYS C 356     -11.757 -16.761  55.270  1.00 26.71           C
ATOM   1970  O   CYS C 356     -11.085 -15.852  55.788  1.00 30.78           O
ATOM   1971  CB  CYS C 356     -14.138 -16.394  55.997  1.00 26.95           C
ATOM   1972  SG  CYS C 356     -15.647 -17.170  56.576  1.00 28.59           S
ATOM   1973  N   ALA C 357     -11.527 -17.220  54.040  1.00 25.21           N
ATOM   1974  CA  ALA C 357     -10.332 -16.857  53.297  1.00 23.22           C
ATOM   1975  C   ALA C 357     -10.588 -15.643  52.440  1.00 23.32           C
ATOM   1976  O   ALA C 357     -11.646 -15.517  51.815  1.00 25.17           O
ATOM   1977  CB  ALA C 357      -9.853 -18.023  52.439  1.00 22.14           C
ATOM   1978  N   GLU C 358      -9.636 -14.725  52.445  1.00 24.84           N
ATOM   1979  CA  GLU C 358      -9.693 -13.544  51.574  1.00 24.66           C
ATOM   1980  C   GLU C 358      -8.468 -13.451  50.711  1.00 23.74           C
ATOM   1981  O   GLU C 358      -7.428 -14.037  51.044  1.00 27.37           O
ATOM   1982  CB  GLU C 358      -9.821 -12.269  52.383  1.00 24.90           C
ATOM   1983  CG  GLU C 358      -8.637 -12.062  53.338  1.00 29.88           C
ATOM   1984  CD  GLU C 358      -8.587 -10.721  54.040  1.00 29.65           C
ATOM   1985  OE1 GLU C 358      -7.736 -10.574  54.935  1.00 30.62           O
ATOM   1986  OE2 GLU C 358      -9.327  -9.804  53.638  1.00 34.18           O
ATOM   1987  N   PHE C 359      -8.577 -12.702  49.614  1.00 20.75           N
ATOM   1988  CA  PHE C 359      -7.402 -12.256  48.903  1.00 22.94           C
ATOM   1989  C   PHE C 359      -6.934 -11.007  49.607  1.00 23.78           C
ATOM   1990  O   PHE C 359      -7.697 -10.070  49.760  1.00 26.83           O
ATOM   1991  CB  PHE C 359      -7.668 -11.932  47.421  1.00 22.12           C
ATOM   1992  CG  PHE C 359      -8.351 -13.024  46.649  1.00 21.90           C
ATOM   1993  CD1 PHE C 359      -7.620 -14.015  46.006  1.00 21.98           C
ATOM   1994  CD2 PHE C 359      -9.737 -13.010  46.472  1.00 22.47           C
ATOM   1995  CE1 PHE C 359      -8.245 -14.988  45.264  1.00 22.02           C
ATOM   1996  CE2 PHE C 359     -10.364 -13.999  45.756  1.00 22.78           C
ATOM   1997  CZ  PHE C 359      -9.613 -14.989  45.127  1.00 22.30           C
ATOM   1998  N   SER C 360      -5.678 -11.002  50.035  1.00 25.74           N
ATOM   1999  CA  SER C 360      -5.130  -9.923  50.820  1.00 28.24           C
ATOM   2000  C   SER C 360      -3.707  -9.616  50.390  1.00 29.49           C
ATOM   2001  O   SER C 360      -2.769 -10.333  50.717  1.00 31.90           O
ATOM   2002  CB  SER C 360      -5.215 -10.282  52.317  1.00 30.95           C
ATOM   2003  OG  SER C 360      -4.713  -9.251  53.110  1.00 30.83           O
ATOM   2004  N   GLY C 361      -3.570  -8.552  49.602  1.00 31.74           N
ATOM   2005  CA  GLY C 361      -2.315  -8.228  48.929  1.00 30.59           C
ATOM   2006  C   GLY C 361      -1.957  -9.253  47.861  1.00 29.71           C
ATOM   2007  O   GLY C 361      -2.669  -9.404  46.866  1.00 33.40           O
ATOM   2008  N   ASN C 362      -0.838  -9.951  48.054  1.00 29.71           N
ATOM   2009  CA  ASN C 362      -0.301 -10.853  47.022  1.00 30.66           C
ATOM   2010  C   ASN C 362      -0.727 -12.292  47.163  1.00 25.83           C
ATOM   2011  O   ASN C 362      -0.454 -13.086  46.305  1.00 25.58           O
ATOM   2012  CB  ASN C 362       1.235 -10.767  46.975  1.00 33.78           C
ATOM   2013  CG  ASN C 362       1.722  -9.380  46.548  1.00 39.81           C
ATOM   2014  OD1 ASN C 362       2.779  -8.935  46.998  1.00 46.64           O
ATOM   2015  ND2 ASN C 362       0.931  -8.673  45.716  1.00 36.61           N
ATOM   2016  N   GLY C 363      -1.410 -12.623  48.230  1.00 25.60           N
ATOM   2017  CA  GLY C 363      -1.844 -13.990  48.470  1.00 27.58           C
ATOM   2018  C   GLY C 363      -3.069 -14.024  49.365  1.00 28.97           C
ATOM   2019  O   GLY C 363      -3.819 -13.027  49.398  1.00 27.45           O
ATOM   2020  N   TRP C 364      -3.291 -15.156  50.058  1.00 27.53           N
ATOM   2021  CA  TRP C 364      -4.488 -15.319  50.869  1.00 26.98           C
ATOM   2022  C   TRP C 364      -4.263 -15.139  52.334  1.00 27.07           C
ATOM   2023  O   TRP C 364      -3.177 -15.373  52.847  1.00 29.10           O
ATOM   2024  CB  TRP C 364      -5.139 -16.676  50.711  1.00 26.80           C
ATOM   2025  CG  TRP C 364      -5.286 -17.189  49.318  1.00 28.17           C
ATOM   2026  CD1 TRP C 364      -5.230 -16.484  48.157  1.00 27.16           C
ATOM   2027  CD2 TRP C 364      -5.603 -18.520  48.965  1.00 28.90           C
ATOM   2028  NE1 TRP C 364      -5.446 -17.299  47.104  1.00 25.83           N
ATOM   2029  CE2 TRP C 364      -5.691 -18.563  47.563  1.00 27.93           C
ATOM   2030  CE3 TRP C 364      -5.771 -19.709  49.702  1.00 30.54           C
ATOM   2031  CZ2 TRP C 364      -5.954 -19.746  46.862  1.00 28.53           C
ATOM   2032  CZ3 TRP C 364      -6.047 -20.889  49.010  1.00 32.19           C
ATOM   2033  CH2 TRP C 364      -6.145 -20.892  47.596  1.00 29.39           C
ATOM   2034  N   ASN C 365      -5.339 -14.775  53.020  1.00 26.37           N
ATOM   2035  CA  ASN C 365      -5.319 -14.658  54.465  1.00 25.13           C
ATOM   2036  C   ASN C 365      -6.611 -15.213  54.989  1.00 25.63           C
ATOM   2037  O   ASN C 365      -7.654 -15.042  54.339  1.00 27.82           O
ATOM   2038  CB  ASN C 365      -5.143 -13.182  54.903  1.00 24.62           C
ATOM   2039  CG  ASN C 365      -5.198 -13.008  56.425  1.00 23.65           C
ATOM   2040  OD1 ASN C 365      -4.524 -13.757  57.190  1.00 21.08           O
ATOM   2041  ND2 ASN C 365      -6.046 -12.054  56.893  1.00 20.67           N
ATOM   2042  N   ASP C 366      -6.570 -15.875  56.145  1.00 25.10           N
ATOM   2043  CA  ASP C 366      -7.803 -16.109  56.906  1.00 24.66           C
ATOM   2044  C   ASP C 366      -8.141 -14.939  57.796  1.00 23.91           C
ATOM   2045  O   ASP C 366      -7.290 -14.467  58.567  1.00 23.24           O
ATOM   2046  CB  ASP C 366      -7.768 -17.376  57.766  1.00 25.29           C
ATOM   2047  CG  ASP C 366      -6.598 -17.423  58.735  1.00 25.52           C
ATOM   2048  OD1 ASP C 366      -5.547 -16.774  58.512  1.00 24.51           O
ATOM   2049  OD2 ASP C 366      -6.734 -18.188  59.692  1.00 30.51           O
ATOM   2050  N   ASP C 367      -9.412 -14.541  57.750  1.00 23.29           N
ATOM   2051  CA  ASP C 367      -9.914 -13.407  58.507  1.00 23.31           C
ATOM   2052  C   ASP C 367     -11.270 -13.747  59.073  1.00 24.66           C
ATOM   2053  O   ASP C 367     -11.777 -14.841  58.858  1.00 25.53           O
ATOM   2054  CB  ASP C 367      -9.994 -12.137  57.645  1.00 22.40           C
ATOM   2055  CG  ASP C 367      -9.870 -10.835  58.468  1.00 26.18           C
ATOM   2056  OD1 ASP C 367      -9.873 -10.891  59.732  1.00 24.18           O
ATOM   2057  OD2 ASP C 367      -9.777  -9.726  57.852  1.00 28.53           O
ATOM   2058  N   LYS C 368     -11.814 -12.825  59.862  1.00 24.79           N
ATOM   2059  CA  LYS C 368     -13.032 -13.067  60.585  1.00 27.98           C
ATOM   2060  C   LYS C 368     -14.195 -12.962  59.609  1.00 27.78           C
ATOM   2061  O   LYS C 368     -14.318 -11.984  58.831  1.00 27.53           O
ATOM   2062  CB  LYS C 368     -13.177 -12.109  61.785  1.00 31.10           C
ATOM   2063  CG  LYS C 368     -11.936 -12.010  62.652  1.00 35.95           C
ATOM   2064  CD  LYS C 368     -12.305 -11.644  64.085  1.00 43.96           C
ATOM   2065  CE  LYS C 368     -11.095 -11.180  64.897  1.00 51.46           C
ATOM   2066  NZ  LYS C 368     -10.814  -9.731  64.675  1.00 53.89           N
ATOM   2067  N   CYS C 369     -15.044 -13.988  59.651  1.00 26.87           N
ATOM   2068  CA  CYS C 369     -16.142 -14.164  58.716  1.00 25.73           C
ATOM   2069  C   CYS C 369     -17.193 -13.090  58.815  1.00 28.43           C
ATOM   2070  O   CYS C 369     -17.893 -12.842  57.850  1.00 29.33           O
ATOM   2071  CB  CYS C 369     -16.815 -15.519  58.927  1.00 29.66           C
ATOM   2072  SG  CYS C 369     -15.770 -16.952  58.559  1.00 31.71           S
ATOM   2073  N   ASN C 370     -17.327 -12.469  59.980  1.00 28.22           N
ATOM   2074  CA  ASN C 370     -18.368 -11.466  60.190  1.00 30.23           C
ATOM   2075  C   ASN C 370     -17.939 -10.082  59.677  1.00 28.52           C
ATOM   2076  O   ASN C 370     -18.712  -9.159  59.743  1.00 26.60           O
ATOM   2077  CB  ASN C 370     -18.814 -11.412  61.668  1.00 31.39           C
ATOM   2078  CG  ASN C 370     -17.673 -11.029  62.619  1.00 37.00           C
ATOM   2079  OD1 ASN C 370     -16.491 -11.325  62.376  1.00 41.54           O
ATOM   2080  ND2 ASN C 370     -18.023 -10.375  63.713  1.00 44.06           N
ATOM   2081  N   LEU C 371     -16.722  -9.957  59.169  1.00 26.98           N
ATOM   2082  CA  LEU C 371     -16.301  -8.723  58.576  1.00 26.50           C
ATOM   2083  C   LEU C 371     -16.732  -8.536  57.127  1.00 26.17           C
ATOM   2084  O   LEU C 371     -16.958  -9.493  56.414  1.00 28.68           O
ATOM   2085  CB  LEU C 371     -14.811  -8.593  58.675  1.00 27.00           C
ATOM   2086  CG  LEU C 371     -14.209  -8.502  60.063  1.00 29.44           C
ATOM   2087  CD1 LEU C 371     -12.679  -8.458  59.966  1.00 29.70           C
ATOM   2088  CD2 LEU C 371     -14.779  -7.371  60.927  1.00 28.84           C
ATOM   2089  N   ALA C 372     -16.829  -7.273  56.701  1.00 25.89           N
ATOM   2090  CA  ALA C 372     -17.321  -6.902  55.393  1.00 25.42           C
ATOM   2091  C   ALA C 372     -16.135  -6.691  54.433  1.00 26.03           C
ATOM   2092  O   ALA C 372     -15.197  -5.959  54.720  1.00 29.13           O
ATOM   2093  CB  ALA C 372     -18.176  -5.647  55.484  1.00 25.11           C
ATOM   2094  N   LYS C 373     -16.188  -7.359  53.297  1.00 25.36           N
ATOM   2095  CA  LYS C 373     -15.153  -7.262  52.291  1.00 23.34           C
ATOM   2096  C   LYS C 373     -15.822  -7.279  50.960  1.00 23.06           C
ATOM   2097  O   LYS C 373     -17.011  -7.592  50.823  1.00 25.76           O
ATOM   2098  CB  LYS C 373     -14.158  -8.424  52.399  1.00 24.74           C
ATOM   2099  CG  LYS C 373     -13.574  -8.640  53.793  1.00 25.78           C
ATOM   2100  CD  LYS C 373     -12.627  -9.813  53.780  1.00 27.18           C
ATOM   2101  CE  LYS C 373     -11.928 -10.032  55.097  1.00 28.48           C
ATOM   2102  NZ  LYS C 373     -11.020  -8.932  55.526  1.00 29.34           N
ATOM   2103  N   PHE C 374     -15.055  -6.962  49.936  1.00 20.54           N
ATOM   2104  CA  PHE C 374     -15.517  -7.183  48.606  1.00 20.62           C
ATOM   2105  C   PHE C 374     -15.749  -8.687  48.343  1.00 19.71           C
ATOM   2106  O   PHE C 374     -15.225  -9.477  49.044  1.00 21.44           O
ATOM   2107  CB  PHE C 374     -14.527  -6.531  47.611  1.00 20.07           C
ATOM   2108  CG  PHE C 374     -14.566  -5.031  47.694  1.00 21.01           C
ATOM   2109  CD1 PHE C 374     -13.752  -4.348  48.596  1.00 22.55           C
ATOM   2110  CD2 PHE C 374     -15.493  -4.323  46.984  1.00 20.48           C
ATOM   2111  CE1 PHE C 374     -13.831  -2.959  48.715  1.00 22.70           C
ATOM   2112  CE2 PHE C 374     -15.587  -2.965  47.106  1.00 22.68           C
ATOM   2113  CZ  PHE C 374     -14.766  -2.289  47.983  1.00 21.85           C
ATOM   2114  N   TRP C 375     -16.501  -9.048  47.301  1.00 22.72           N
ATOM   2115  CA  TRP C 375     -16.676 -10.445  46.919  1.00 22.96           C
ATOM   2116  C   TRP C 375     -16.629 -10.671  45.401  1.00 22.00           C
ATOM   2117  O   TRP C 375     -16.759  -9.755  44.599  1.00 23.34           O
ATOM   2118  CB  TRP C 375     -17.902 -11.073  47.558  1.00 22.87           C
ATOM   2119  CG  TRP C 375     -19.202 -10.638  46.938  1.00 24.94           C
ATOM   2120  CD1 TRP C 375     -19.888 -11.273  45.953  1.00 25.94           C
ATOM   2121  CD2 TRP C 375     -19.972  -9.495  47.277  1.00 25.46           C
ATOM   2122  NE1 TRP C 375     -21.013 -10.580  45.615  1.00 25.03           N
ATOM   2123  CE2 TRP C 375     -21.111  -9.497  46.429  1.00 24.63           C
ATOM   2124  CE3 TRP C 375     -19.797  -8.442  48.189  1.00 26.17           C
ATOM   2125  CZ2 TRP C 375     -22.071  -8.521  46.467  1.00 25.34           C
ATOM   2126  CZ3 TRP C 375     -20.759  -7.461  48.233  1.00 27.71           C
ATOM   2127  CH2 TRP C 375     -21.902  -7.521  47.400  1.00 28.69           C
ATOM   2128  N   ILE C 376     -16.326 -11.901  45.035  1.00 21.50           N
ATOM   2129  CA  ILE C 376     -16.338 -12.299  43.687  1.00 25.01           C
ATOM   2130  C   ILE C 376     -17.178 -13.557  43.548  1.00 24.55           C
ATOM   2131  O   ILE C 376     -17.013 -14.489  44.307  1.00 26.89           O
ATOM   2132  CB  ILE C 376     -14.945 -12.503  43.111  1.00 27.65           C
ATOM   2133  CG1 ILE C 376     -14.207 -11.168  43.073  1.00 28.05           C
ATOM   2134  CG2 ILE C 376     -15.057 -13.007  41.650  1.00 29.21           C
ATOM   2135  CD1 ILE C 376     -12.750 -11.318  42.668  1.00 30.63           C
ATOM   2136  N   CYS C 377     -18.084 -13.519  42.578  1.00 22.66           N
ATOM   2137  CA  CYS C 377     -18.949 -14.605  42.188  1.00 23.92           C
ATOM   2138  C   CYS C 377     -18.426 -15.164  40.851  1.00 23.72           C
ATOM   2139  O   CYS C 377     -17.845 -14.450  40.040  1.00 22.26           O
ATOM   2140  CB  CYS C 377     -20.382 -14.133  41.921  1.00 24.88           C
ATOM   2141  SG  CYS C 377     -21.258 -13.288  43.246  1.00 29.64           S
ATOM   2142  N   LYS C 378     -18.697 -16.435  40.643  1.00 23.68           N
ATOM   2143  CA  LYS C 378     -18.316 -17.160  39.430  1.00 24.79           C
ATOM   2144  C   LYS C 378     -19.473 -18.062  39.025  1.00 26.50           C
ATOM   2145  O   LYS C 378     -20.182 -18.647  39.888  1.00 22.48           O
ATOM   2146  CB  LYS C 378     -17.137 -18.043  39.752  1.00 24.44           C
ATOM   2147  CG  LYS C 378     -16.758 -19.074  38.708  1.00 25.70           C
ATOM   2148  CD  LYS C 378     -15.529 -19.818  39.186  1.00 25.93           C
ATOM   2149  CE  LYS C 378     -15.114 -20.936  38.242  1.00 27.37           C
ATOM   2150  NZ  LYS C 378     -13.976 -21.728  38.779  1.00 27.06           N
ATOM   2151  N   LYS C 379     -19.684 -18.134  37.722  1.00 26.61           N
ATOM   2152  CA  LYS C 379     -20.586 -19.109  37.141  1.00 29.10           C
ATOM   2153  C   LYS C 379     -20.155 -19.396  35.714  1.00 29.88           C
ATOM   2154  O   LYS C 379     -19.354 -18.651  35.135  1.00 26.70           O
ATOM   2155  CB  LYS C 379     -22.016 -18.602  37.168  1.00 31.41           C
ATOM   2156  CG  LYS C 379     -22.314 -17.484  36.212  1.00 32.85           C
ATOM   2157  CD  LYS C 379     -23.627 -16.833  36.557  1.00 35.14           C
ATOM   2158  CE  LYS C 379     -24.394 -16.367  35.344  1.00 41.35           C
ATOM   2159  NZ  LYS C 379     -25.695 -15.791  35.816  1.00 44.50           N
ATOM   2160  N   SER C 380     -20.726 -20.446  35.131  1.00 31.32           N
ATOM   2161  CA  SER C 380     -20.370 -20.850  33.774  1.00 33.29           C
ATOM   2162  C   SER C 380     -20.807 -19.869  32.710  1.00 30.71           C
ATOM   2163  O   SER C 380     -21.869 -19.286  32.778  1.00 28.43           O
ATOM   2164  CB  SER C 380     -20.977 -22.225  33.475  1.00 37.71           C
ATOM   2165  OG  SER C 380     -20.307 -23.176  34.279  1.00 37.50           O
ATOM   2166  N   ALA C 381     -19.969 -19.690  31.705  1.00 30.99           N
ATOM   2167  CA  ALA C 381     -20.381 -18.925  30.532  1.00 29.22           C
ATOM   2168  C   ALA C 381     -21.471 -19.669  29.750  1.00 28.40           C
ATOM   2169  O   ALA C 381     -21.598 -20.895  29.834  1.00 23.49           O
ATOM   2170  CB  ALA C 381     -19.193 -18.674  29.650  1.00 30.86           C
ATOM   2171  N   ALA C 382     -22.308 -18.909  29.065  1.00 29.48           N
ATOM   2172  CA  ALA C 382     -23.225 -19.469  28.114  1.00 31.42           C
ATOM   2173  C   ALA C 382     -22.397 -19.742  26.875  1.00 36.68           C
ATOM   2174  O   ALA C 382     -21.486 -18.983  26.575  1.00 37.45           O
ATOM   2175  CB  ALA C 382     -24.285 -18.465  27.781  1.00 30.09           C
ATOM   2176  N   SER C 383     -22.673 -20.827  26.171  1.00 40.08           N
ATOM   2177  CA  SER C 383     -22.075 -21.017  24.848  1.00 44.28           C
ATOM   2178  C   SER C 383     -22.958 -20.350  23.805  1.00 42.12           C
ATOM   2179  O   SER C 383     -24.082 -20.781  23.587  1.00 40.50           O
ATOM   2180  CB  SER C 383     -21.968 -22.511  24.516  1.00 50.38           C
ATOM   2181  OG  SER C 383     -21.594 -23.273  25.653  1.00 57.90           O
ATOM   2182  N   CYS C 384     -22.446 -19.349  23.104  1.00 45.94           N
ATOM   2183  CA  CYS C 384     -23.263 -18.678  22.097  1.00 53.95           C
ATOM   2184  C   CYS C 384     -23.067 -19.214  20.652  1.00 58.19           C
ATOM   2185  O   CYS C 384     -21.946 -19.295  20.149  1.00 70.81           O
ATOM   2186  CB  CYS C 384     -23.054 -17.171  22.212  1.00 53.80           C
ATOM   2187  SG  CYS C 384     -23.567 -16.579  23.849  1.00 49.63           S
TER    2188      CYS C 384
HETATM 2189  C4  EZ8 B1001      -5.415   4.393  45.810  1.00 23.60           C
HETATM 2190  C5  EZ8 B1001      -4.892   3.500  44.640  1.00 25.09           C
HETATM 2191  C6  EZ8 B1001      -3.382   3.444  44.631  1.00 25.15           C
HETATM 2192  N2  EZ8 B1001      -7.063   2.242  47.280  1.00 23.66           N
HETATM 2193  C3  EZ8 B1001      -6.907   4.307  45.849  1.00 22.25           C
HETATM 2194  CAP EZ8 B1001     -13.393  -2.641  43.667  1.00 39.77           C
HETATM 2195  CAL EZ8 B1001     -13.079  -3.833  44.364  1.00 42.46           C
HETATM 2196  CBM EZ8 B1001     -11.975  -4.622  44.003  1.00 42.86           C
HETATM 2197  CAV EZ8 B1001     -11.628  -5.747  44.724  1.00 47.81           C
HETATM 2198  OAE EZ8 B1001     -12.070  -6.975  44.133  1.00 54.00           O
HETATM 2199  CAM EZ8 B1001     -11.173  -4.180  42.948  1.00 43.86           C
HETATM 2200  CAQ EZ8 B1001     -11.471  -2.996  42.242  1.00 40.36           C
HETATM 2201  CBO EZ8 B1001     -12.577  -2.207  42.592  1.00 37.59           C
HETATM 2202  CAZ EZ8 B1001     -12.877  -1.037  41.896  1.00 35.09           C
HETATM 2203  NBF EZ8 B1001     -11.639  -0.184  41.740  1.00 34.40           N
HETATM 2204  CBK EZ8 B1001     -11.122   0.605  42.696  1.00 31.15           C
HETATM 2205  OAC EZ8 B1001     -11.546   0.620  43.856  1.00 32.27           O
HETATM 2206  CBW EZ8 B1001      -9.832   1.406  42.412  1.00 27.56           C
HETATM 2207  CBB EZ8 B1001      -8.717   0.487  42.648  1.00 25.63           C
HETATM 2208  CBV EZ8 B1001      -9.738   2.168  41.084  1.00 27.86           C
HETATM 2209  CBJ EZ8 B1001     -10.982   3.063  40.874  1.00 30.76           C
HETATM 2210  OAB EZ8 B1001     -11.466   3.757  41.793  1.00 29.76           O
HETATM 2211  NBE EZ8 B1001     -11.554   3.007  39.679  1.00 29.85           N
HETATM 2212  CAY EZ8 B1001     -12.793   3.808  39.388  1.00 31.04           C
HETATM 2213  CBN EZ8 B1001     -12.510   4.933  38.575  1.00 31.05           C
HETATM 2214  CAN EZ8 B1001     -11.237   5.461  38.510  1.00 34.03           C
HETATM 2215  CAJ EZ8 B1001     -10.991   6.562  37.693  1.00 36.54           C
HETATM 2216  CBL EZ8 B1001     -12.002   7.124  36.937  1.00 38.24           C
HETATM 2217  CAU EZ8 B1001     -11.738   8.191  36.139  1.00 42.39           C
HETATM 2218  OAD EZ8 B1001     -12.139   9.333  36.901  1.00 54.04           O
HETATM 2219  CAK EZ8 B1001     -13.286   6.596  37.003  1.00 35.19           C
HETATM 2220  CAO EZ8 B1001     -13.533   5.518  37.832  1.00 32.34           C
HETATM 2221  CBA EZ8 B1001      -8.548   3.084  41.160  1.00 28.69           C
HETATM 2222  CBT EZ8 B1001      -7.298   2.196  41.391  1.00 26.72           C
HETATM 2223  OBG EZ8 B1001      -7.129   1.328  40.265  1.00 29.02           O
HETATM 2224  CAX EZ8 B1001      -5.810   0.854  40.207  1.00 37.23           C
HETATM 2225  CAT EZ8 B1001      -5.783  -0.206  39.098  1.00 40.49           C
HETATM 2226 CL1  EZ8 B1001      -7.170  -1.384  39.333  1.00 53.02          Cl
HETATM 2227  CBU EZ8 B1001      -7.456   1.372  42.686  1.00 26.53           C
HETATM 2228  O1  EZ8 B1001      -7.472   2.323  43.745  1.00 24.33           O
HETATM 2229  C1  EZ8 B1001      -6.759   2.007  44.877  1.00 24.50           C
HETATM 2230  O5  EZ8 B1001      -5.327   2.170  44.847  1.00 24.14           O
HETATM 2231  O6  EZ8 B1001      -3.084   2.639  43.481  1.00 29.70           O
HETATM 2232  O4  EZ8 B1001      -5.049   5.742  45.562  1.00 22.66           O
HETATM 2233  O3  EZ8 B1001      -7.392   5.041  46.943  1.00 22.03           O
HETATM 2234  C2  EZ8 B1001      -7.377   2.849  46.001  1.00 23.78           C
HETATM 2235  CAR EZ8 B1001      -7.964   1.767  48.172  1.00 25.75           C
HETATM 2236  NBD EZ8 B1001      -5.862   2.048  47.804  1.00 25.64           N
HETATM 2237  NBC EZ8 B1001      -5.970   1.495  48.994  1.00 27.10           N
HETATM 2238  CBP EZ8 B1001      -7.275   1.294  49.194  1.00 26.34           C
HETATM 2239  CAS EZ8 B1001      -7.865   0.661  50.398  1.00 28.84           C
HETATM 2240  NAA EZ8 B1001      -7.062   1.078  51.526  1.00 30.31           N
HETATM 2241 CA   CA  B1002      -6.395   7.402  46.882  1.00 22.15          Ca
HETATM 2242 CA   CA  B1003     -11.063  14.169  46.818  1.00 25.55          Ca
HETATM 2243 CA   CA  B1004     -16.143  15.378  45.683  1.00 54.27          Ca
HETATM 2244 CL   CL  B1005     -17.990  -1.103  67.093  1.00 66.53          Cl
HETATM 2245 CL   CL  B1006       0.183   8.635  77.233  1.00 63.88          Cl
HETATM 2246  C4  EZ8 C1001      -3.556 -11.621  60.094  1.00 23.84           C
HETATM 2247  C5  EZ8 C1001      -2.659 -10.777  61.001  1.00 26.26           C
HETATM 2248  C6  EZ8 C1001      -1.247 -11.121  60.648  1.00 28.48           C
HETATM 2249  N2  EZ8 C1001      -5.455  -9.410  59.222  1.00 24.47           N
HETATM 2250  C3  EZ8 C1001      -4.919 -11.473  60.547  1.00 23.91           C
HETATM 2251  CAP EZ8 C1001      -7.303  -3.775  65.435  1.00 46.41           C
HETATM 2252  CAL EZ8 C1001      -7.142  -2.584  64.691  1.00 45.35           C
HETATM 2253  CBM EZ8 C1001      -8.181  -2.082  63.906  1.00 47.00           C
HETATM 2254  CAV EZ8 C1001      -7.990  -0.925  63.148  1.00 50.46           C
HETATM 2255  OAE EZ8 C1001      -8.353   0.281  63.861  1.00 48.10           O
HETATM 2256  CAM EZ8 C1001      -9.392  -2.810  63.867  1.00 43.80           C
HETATM 2257  CAQ EZ8 C1001      -9.564  -3.999  64.599  1.00 44.89           C
HETATM 2258  CBO EZ8 C1001      -8.500  -4.510  65.398  1.00 43.65           C
HETATM 2259  CAZ EZ8 C1001      -8.653  -5.687  66.168  1.00 41.22           C
HETATM 2260  NBF EZ8 C1001      -7.565  -6.671  65.883  1.00 36.32           N
HETATM 2261  CBK EZ8 C1001      -7.539  -7.442  64.780  1.00 33.61           C
HETATM 2262  OAC EZ8 C1001      -8.374  -7.345  63.888  1.00 36.15           O
HETATM 2263  CBW EZ8 C1001      -6.333  -8.402  64.582  1.00 30.77           C
HETATM 2264  CBB EZ8 C1001      -5.285  -7.613  63.970  1.00 28.76           C
HETATM 2265  CBV EZ8 C1001      -5.875  -9.082  65.861  1.00 31.38           C
HETATM 2266  CBJ EZ8 C1001      -7.028  -9.899  66.472  1.00 33.02           C
HETATM 2267  OAB EZ8 C1001      -7.731 -10.586  65.747  1.00 37.23           O
HETATM 2268  NBE EZ8 C1001      -7.165  -9.823  67.801  1.00 32.68           N
HETATM 2269  CAY EZ8 C1001      -8.227 -10.486  68.623  1.00 32.47           C
HETATM 2270  CBN EZ8 C1001      -7.751 -11.643  69.316  1.00 29.97           C
HETATM 2271  CAN EZ8 C1001      -8.479 -12.224  70.369  1.00 31.10           C
HETATM 2272  CAJ EZ8 C1001      -8.002 -13.377  71.002  1.00 28.33           C
HETATM 2273  CBL EZ8 C1001      -6.807 -13.943  70.591  1.00 28.90           C
HETATM 2274  CAU EZ8 C1001      -6.267 -15.029  71.176  1.00 32.48           C
HETATM 2275  OAD EZ8 C1001      -7.276 -16.005  71.243  1.00 39.73           O
HETATM 2276  CAK EZ8 C1001      -6.091 -13.363  69.567  1.00 29.46           C
HETATM 2277  CAO EZ8 C1001      -6.555 -12.222  68.946  1.00 28.06           C
HETATM 2278  CBA EZ8 C1001      -4.831 -10.028  65.584  1.00 31.43           C
HETATM 2279  CBT EZ8 C1001      -3.669  -9.323  64.866  1.00 29.34           C
HETATM 2280  OBG EZ8 C1001      -2.974  -8.496  65.754  1.00 32.73           O
HETATM 2281  CAX EZ8 C1001      -1.621  -8.390  65.375  1.00 37.63           C
HETATM 2282  CAT EZ8 C1001      -1.070  -7.215  66.218  1.00 43.43           C
HETATM 2283 CL1  EZ8 C1001      -2.374  -5.979  66.637  1.00 53.34          Cl
HETATM 2284  CBU EZ8 C1001      -4.129  -8.547  63.660  1.00 29.95           C
HETATM 2285  O1  EZ8 C1001      -4.428  -9.517  62.669  1.00 25.08           O
HETATM 2286  C1  EZ8 C1001      -4.232  -9.143  61.315  1.00 24.82           C
HETATM 2287  O5  EZ8 C1001      -2.975  -9.368  60.800  1.00 25.11           O
HETATM 2288  O6  EZ8 C1001      -0.406 -10.106  61.172  1.00 31.40           O
HETATM 2289  O4  EZ8 C1001      -3.191 -12.987  60.093  1.00 24.38           O
HETATM 2290  O3  EZ8 C1001      -5.835 -12.193  59.689  1.00 23.89           O
HETATM 2291  C2  EZ8 C1001      -5.278  -9.972  60.518  1.00 23.87           C
HETATM 2292  CAR EZ8 C1001      -6.592  -8.921  58.753  1.00 25.12           C
HETATM 2293  NBD EZ8 C1001      -4.512  -9.239  58.288  1.00 24.43           N
HETATM 2294  NBC EZ8 C1001      -4.963  -8.694  57.349  1.00 24.41           N
HETATM 2295  CBP EZ8 C1001      -6.255  -8.463  57.550  1.00 26.90           C
HETATM 2296  CAS EZ8 C1001      -7.197  -7.776  56.578  1.00 27.46           C
HETATM 2297  NAA EZ8 C1001      -6.713  -7.953  55.218  1.00 30.03           N
HETATM 2298 CA   CA  C1002      -5.057 -14.525  59.344  1.00 25.73          Ca
HETATM 2299 CA   CA  C1003      -9.862 -20.970  61.350  1.00 27.95          Ca
HETATM 2300 CA   CA  C1004     -14.113 -21.919  63.758  1.00 51.36          Ca
HETATM 2301 CL   CL  C1005     -22.111  -4.897  44.537  1.00 60.06          Cl
HETATM 2302 CL   CL  C1006     -10.000 -15.788  28.746  1.00 58.86          Cl
HETATM 2303  O   HOH B1101       5.763  13.347  73.136  1.00 35.41           O
HETATM 2304  O   HOH B1102     -20.460   8.528  53.644  1.00 44.81           O
HETATM 2305  O   HOH B1103     -17.305  -5.480  76.171  1.00 54.35           O
HETATM 2306  O   HOH B1104     -10.155  -2.560  67.966  1.00 38.38           O
HETATM 2307  O   HOH B1105     -11.062   4.192  44.699  1.00 30.95           O
HETATM 2308  O   HOH B1106       3.243   5.741  53.564  1.00 37.21           O
HETATM 2309  O   HOH B1107     -16.942  -7.080  63.971  1.00 43.76           O
HETATM 2310  O   HOH B1108     -17.533  16.379  47.128  1.00 28.63           O
HETATM 2311  O   HOH B1109      -5.527  22.488  61.698  1.00 35.77           O
HETATM 2312  O   HOH B1110     -11.172  19.198  67.603  1.00 32.75           O
HETATM 2313  O   HOH B1111      -3.585   2.370  50.456  1.00 41.29           O
HETATM 2314  O   HOH B1112      -2.095  20.640  64.849  1.00 36.40           O
HETATM 2315  O   HOH B1113     -12.924  20.244  51.807  1.00 29.37           O
HETATM 2316  O   HOH B1114      -6.390  22.373  54.849  1.00 43.70           O
HETATM 2317  O   HOH B1115      -8.511  22.840  46.709  1.00 34.12           O
HETATM 2318  O   HOH B1116     -10.394   9.952  38.766  1.00 41.90           O
HETATM 2319  O   HOH B1117     -24.290   6.883  55.468  1.00 49.48           O
HETATM 2320  O   HOH B1118     -20.659  18.601  52.922  1.00 56.54           O
HETATM 2321  O   HOH B1119       4.416  17.668  55.813  1.00 36.69           O
HETATM 2322  O   HOH B1120      -5.601   3.684  62.850  1.00 35.98           O
HETATM 2323  O   HOH B1121       3.376   4.691  63.993  1.00 36.94           O
HETATM 2324  O   HOH B1122      -4.020  12.616  72.698  1.00 29.16           O
HETATM 2325  O   HOH B1123      -5.022  17.844  48.411  1.00 43.96           O
HETATM 2326  O   HOH B1124       3.786   5.467  50.581  1.00 33.58           O
HETATM 2327  O   HOH B1125     -13.252   6.107  43.294  1.00 54.71           O
HETATM 2328  O   HOH B1126     -14.583  16.848  46.604  1.00 28.21           O
HETATM 2329  O   HOH B1127      -3.442  -0.733  57.295  1.00 32.69           O
HETATM 2330  O   HOH B1128      -5.835  24.436  49.758  1.00 48.03           O
HETATM 2331  O   HOH B1129       1.769   2.234  53.492  1.00 47.41           O
HETATM 2332  O   HOH B1130     -22.101   2.889  52.514  1.00 38.09           O
HETATM 2333  O   HOH B1131     -17.935  -4.781  60.081  1.00 20.90           O
HETATM 2334  O   HOH B1132     -15.790   6.110  40.963  1.00 49.35           O
HETATM 2335  O   HOH B1133      -8.706  13.628  47.004  1.00 18.48           O
HETATM 2336  O   HOH B1134     -15.715  20.023  66.737  1.00 53.54           O
HETATM 2337  O   HOH B1135       0.550  14.548  49.227  1.00 31.99           O
HETATM 2338  O   HOH B1136     -10.511   0.504  79.924  1.00 34.45           O
HETATM 2339  O   HOH B1137     -10.006  24.564  57.577  1.00 37.80           O
HETATM 2340  O   HOH B1138      -3.509  -2.464  66.561  1.00 34.45           O
HETATM 2341  O   HOH B1139       3.493   8.246  61.339  1.00 37.80           O
HETATM 2342  O   HOH B1140      -1.419  14.025  71.588  1.00 40.79           O
HETATM 2343  O   HOH B1141     -22.687  11.866  59.139  1.00 38.39           O
HETATM 2344  O   HOH B1142     -21.939   2.315  57.160  1.00 24.25           O
HETATM 2345  O   HOH B1143       2.136  15.218  71.392  1.00 42.90           O
HETATM 2346  O   HOH B1144      -9.446   5.279  81.871  1.00 37.69           O
HETATM 2347  O   HOH B1145      -5.608  16.633  71.072  1.00 42.46           O
HETATM 2348  O   HOH B1146      -9.351  15.153  40.531  1.00 41.74           O
HETATM 2349  O   HOH B1147     -12.640  27.563  52.947  1.00 64.98           O
HETATM 2350  O   HOH B1148     -17.598  14.043  44.999  1.00 29.91           O
HETATM 2351  O   HOH B1149     -14.152  16.755  57.348  1.00 34.46           O
HETATM 2352  O   HOH B1150       5.652  11.719  62.746  1.00 52.75           O
HETATM 2353  O   HOH B1151     -14.602  10.049  38.215  1.00 46.85           O
HETATM 2354  O   HOH B1152     -17.174   3.498  81.014  1.00 44.41           O
HETATM 2355  O   HOH B1153     -14.588  18.537  53.190  1.00 27.60           O
HETATM 2356  O   HOH B1154     -12.522  -2.088  55.470  1.00 49.92           O
HETATM 2357  O   HOH B1155     -14.597  14.432  44.370  1.00 23.33           O
HETATM 2358  O   HOH B1156     -10.361   3.166  80.049  1.00 33.93           O
HETATM 2359  O   HOH B1157       3.032   7.864  69.840  1.00 42.72           O
HETATM 2360  O   HOH B1158      -6.277  19.211  63.480  1.00 40.94           O
HETATM 2361  O   HOH B1159     -18.082  14.550  75.470  1.00 45.95           O
HETATM 2362  O   HOH B1160      -3.331  19.311  60.406  1.00 27.17           O
HETATM 2363  O   HOH B1161      -0.702   5.873  45.112  1.00 37.56           O
HETATM 2364  O   HOH B1162       4.060   3.944  59.653  1.00 48.54           O
HETATM 2365  O   HOH B1163     -25.292  12.232  62.708  1.00 47.40           O
HETATM 2366  O   HOH B1164      -7.359  15.777  47.130  1.00 36.42           O
HETATM 2367  O   HOH B1165      -2.324   4.604  49.096  1.00 30.82           O
HETATM 2368  O   HOH B1166     -21.677   0.282  66.045  1.00 57.65           O
HETATM 2369  O   HOH B1167       2.920   2.922  62.014  1.00 38.29           O
HETATM 2370  O   HOH B1168     -24.043  16.556  63.781  1.00 57.18           O
HETATM 2371  O   HOH B1169     -12.439  -0.410  52.667  1.00 38.92           O
HETATM 2372  O   HOH B1170     -15.568   9.878  47.833  1.00 21.39           O
HETATM 2373  O   HOH B1171     -17.277  11.575  47.294  1.00 34.04           O
HETATM 2374  O   HOH B1172       3.643  17.648  66.300  1.00 44.21           O
HETATM 2375  O   HOH B1173     -17.911  12.581  64.625  1.00 38.62           O
HETATM 2376  O   HOH B1174     -20.365   0.706  49.621  1.00 31.83           O
HETATM 2377  O   HOH B1175      -5.270  20.121  51.798  1.00 37.46           O
HETATM 2378  O   HOH B1176     -18.663   6.815  76.502  1.00 41.21           O
HETATM 2379  O   HOH B1177       3.729  18.784  62.920  1.00 57.72           O
HETATM 2380  O   HOH B1178     -14.212  16.056  74.080  1.00 37.24           O
HETATM 2381  O   HOH B1179     -18.286   4.574  68.095  1.00 35.40           O
HETATM 2382  O   HOH B1180       5.576   8.756  68.653  1.00 55.83           O
HETATM 2383  O   HOH B1181     -15.221  20.752  45.028  1.00 45.87           O
HETATM 2384  O   HOH B1182     -17.638  21.134  63.169  1.00 48.62           O
HETATM 2385  O   HOH B1183     -20.439  12.221  41.939  1.00 49.27           O
HETATM 2386  O   HOH B1184       2.508  23.224  59.476  1.00 38.46           O
HETATM 2387  O   HOH B1185      -6.539   3.227  78.788  1.00 48.00           O
HETATM 2388  O   HOH B1186      -9.080  16.725  68.330  1.00 39.97           O
HETATM 2389  O   HOH B1187      -3.014  17.604  51.043  1.00 25.08           O
HETATM 2390  O   HOH B1188     -21.496  14.086  70.596  1.00 37.25           O
HETATM 2391  O   HOH B1189      -0.532  -2.612  57.052  1.00 49.83           O
HETATM 2392  O  AHOH B1190      -9.819  -5.070  57.307  0.50 27.30           O
HETATM 2393  O  BHOH B1190     -10.225  -3.283  56.746  0.50 37.98           O
HETATM 2394  O   HOH B1191     -13.666  15.720  42.051  1.00 28.92           O
HETATM 2395  O   HOH B1192       2.927  13.792  50.293  1.00 47.25           O
HETATM 2396  O   HOH B1193       3.649   8.182  55.018  1.00 44.44           O
HETATM 2397  O   HOH B1194      -3.624  24.928  55.414  1.00 39.08           O
HETATM 2398  O   HOH B1195       2.900  -3.738  68.349  1.00 48.26           O
HETATM 2399  O   HOH B1196     -17.517  16.826  55.419  1.00 48.24           O
HETATM 2400  O   HOH B1197       5.269  16.821  52.665  1.00 57.75           O
HETATM 2401  O   HOH B1198       3.557   4.874  68.217  1.00 43.55           O
HETATM 2402  O   HOH B1199      -1.211   6.532  42.606  1.00 43.38           O
HETATM 2403  O   HOH B1200     -11.750  16.095  70.964  1.00 54.88           O
HETATM 2404  O   HOH B1201     -17.446  14.938  64.251  1.00 51.79           O
HETATM 2405  O   HOH B1202       0.408  21.388  64.833  1.00 37.47           O
HETATM 2406  O   HOH B1203      -4.214  20.287  62.853  1.00 37.34           O
HETATM 2407  O   HOH B1204       2.205  -6.881  61.329  1.00 56.70           O
HETATM 2408  O   HOH B1205     -21.955   9.489  75.940  1.00 47.93           O
HETATM 2409  O  AHOH B1206     -14.640   0.576  39.374  0.50 23.05           O
HETATM 2410  O  BHOH B1206     -15.034   1.595  41.183  0.50 36.02           O
HETATM 2411  O   HOH B1207      -4.422   7.714  39.641  1.00 48.27           O
HETATM 2412  O   HOH B1208      -6.412  22.491  45.366  1.00 42.68           O
HETATM 2413  O   HOH B1209      -1.584   2.830  76.749  1.00 40.29           O
HETATM 2414  O   HOH B1210      -5.600  13.953  81.025  1.00 51.60           O
HETATM 2415  O   HOH B1211     -23.394   3.436  48.645  1.00 43.38           O
HETATM 2416  O   HOH B1212     -16.279  16.746  44.064  1.00 29.10           O
HETATM 2417  O   HOH B1213       3.803  -4.079  62.100  1.00 39.47           O
HETATM 2418  O   HOH B1214     -16.252  18.251  57.697  1.00 36.27           O
HETATM 2419  O   HOH B1215       7.680  15.805  62.768  1.00 49.70           O
HETATM 2420  O   HOH B1216      -3.434  22.493  66.317  1.00 39.87           O
HETATM 2421  O   HOH B1217     -10.116  24.941  44.929  1.00 40.19           O
HETATM 2422  O   HOH B1218     -17.953  22.058  60.174  1.00 54.80           O
HETATM 2423  O   HOH B1219     -14.558  24.164  45.847  1.00 43.12           O
HETATM 2424  O   HOH B1220     -21.200   6.785  76.180  1.00 46.60           O
HETATM 2425  O   HOH B1221      -1.720   3.465  79.084  1.00 52.06           O
HETATM 2426  O   HOH B1222      -0.877  26.747  57.407  1.00 54.32           O
HETATM 2427  O   HOH B1223     -21.823  18.270  56.109  1.00 45.72           O
HETATM 2428  O   HOH B1224     -13.950  -1.447  87.975  1.00 53.02           O
HETATM 2429  O   HOH B1225      -2.279  25.426  64.583  1.00 38.42           O
HETATM 2430  O   HOH C1101      -6.071 -23.422  63.013  1.00 38.74           O
HETATM 2431  O   HOH C1102     -19.401  -1.470  51.134  1.00 28.21           O
HETATM 2432  O   HOH C1103     -13.588 -27.224  57.235  1.00 25.45           O
HETATM 2433  O   HOH C1104     -24.598  -5.755  48.877  1.00 53.62           O
HETATM 2434  O   HOH C1105      -9.410 -16.537  70.090  1.00 45.76           O
HETATM 2435  O   HOH C1106     -26.712 -13.529  36.235  1.00 48.45           O
HETATM 2436  O   HOH C1107     -16.250 -23.490  52.698  1.00 33.61           O
HETATM 2437  O   HOH C1108     -11.721  -7.517  63.860  1.00 49.58           O
HETATM 2438  O   HOH C1109     -21.227  -8.899  59.509  1.00 34.03           O
HETATM 2439  O   HOH C1110      -8.152 -27.783  40.904  1.00 33.14           O
HETATM 2440  O   HOH C1111     -10.623   0.671  64.967  1.00 33.32           O
HETATM 2441  O   HOH C1112     -13.047 -23.407  62.925  1.00 31.79           O
HETATM 2442  O   HOH C1113      -1.883 -12.289  39.985  1.00 30.43           O
HETATM 2443  O   HOH C1114      -6.586 -22.361  33.870  1.00 43.53           O
HETATM 2444  O   HOH C1115     -22.978  -8.410  55.095  1.00 23.90           O
HETATM 2445  O   HOH C1116      -9.668 -10.868  44.345  1.00 31.56           O
HETATM 2446  O   HOH C1117     -12.338 -19.776  34.653  1.00 26.94           O
HETATM 2447  O   HOH C1118     -23.997 -21.394  38.903  1.00 41.57           O
HETATM 2448  O   HOH C1119     -10.746 -22.570  66.512  1.00 46.96           O
HETATM 2449  O   HOH C1120     -16.039 -13.905  62.828  1.00 37.61           O
HETATM 2450  O   HOH C1121      -7.943 -20.430  60.465  1.00 24.95           O
HETATM 2451  O   HOH C1122     -25.230 -17.339  53.760  1.00 43.07           O
HETATM 2452  O   HOH C1123     -14.530   1.018  45.230  1.00 55.04           O
HETATM 2453  O   HOH C1124      -8.274 -11.125  63.067  1.00 28.39           O
HETATM 2454  O   HOH C1125     -20.465 -14.387  57.842  1.00 35.13           O
HETATM 2455  O   HOH C1126     -12.425 -21.049  64.373  1.00 31.90           O
HETATM 2456  O   HOH C1127     -27.618 -13.981  53.868  1.00 39.44           O
HETATM 2457  O   HOH C1128     -16.149 -22.756  63.159  1.00 34.62           O
HETATM 2458  O   HOH C1129     -27.133 -10.791  44.547  1.00 42.64           O
HETATM 2459  O   HOH C1130     -15.405 -20.675  64.728  1.00 37.80           O
HETATM 2460  O   HOH C1131       1.492 -25.480  47.679  1.00 42.57           O
HETATM 2461  O   HOH C1132     -25.399 -14.575  29.170  1.00 51.50           O
HETATM 2462  O   HOH C1133      -5.048  -6.457  48.648  1.00 36.61           O
HETATM 2463  O   HOH C1134       0.644  -9.826  50.355  1.00 46.15           O
HETATM 2464  O   HOH C1135       0.302 -12.521  43.732  1.00 42.34           O
HETATM 2465  O   HOH C1136      -8.184 -29.874  60.695  1.00 29.49           O
HETATM 2466  O   HOH C1137      -6.926 -27.439  54.424  1.00 39.54           O
HETATM 2467  O   HOH C1138     -12.030 -23.030  32.914  1.00 43.13           O
HETATM 2468  O   HOH C1139     -14.975  -7.169  43.917  1.00 31.87           O
HETATM 2469  O   HOH C1140     -17.811  -7.609  37.641  1.00 46.86           O
HETATM 2470  O   HOH C1141     -24.141 -20.012  34.236  1.00 40.11           O
HETATM 2471  O   HOH C1142     -22.992  -4.267  50.149  1.00 44.56           O
HETATM 2472  O   HOH C1143     -20.404  -9.508  29.818  1.00 28.59           O
HETATM 2473  O   HOH C1144     -18.480 -22.255  37.030  1.00 44.55           O
HETATM 2474  O   HOH C1145      -4.260 -15.258  34.857  1.00 43.79           O
HETATM 2475  O   HOH C1146       3.585 -13.489  52.010  1.00 38.01           O
HETATM 2476  O   HOH C1147     -11.767  -6.266  56.080  1.00 39.36           O
HETATM 2477  O   HOH C1148       0.263 -22.215  55.092  1.00 34.72           O
HETATM 2478  O   HOH C1149     -10.011 -21.084  34.488  1.00 39.15           O
HETATM 2479  O   HOH C1150     -10.195 -29.736  44.999  1.00 43.16           O
HETATM 2480  O   HOH C1151     -15.515 -23.542  40.339  1.00 31.92           O
HETATM 2481  O   HOH C1152      -9.844 -22.721  36.578  1.00 32.23           O
HETATM 2482  O   HOH C1153     -17.538 -20.953  42.186  1.00 42.19           O
HETATM 2483  O   HOH C1154      -0.663  -5.882  41.781  1.00 37.98           O
HETATM 2484  O   HOH C1155     -23.565 -16.545  31.658  1.00 41.92           O
HETATM 2485  O   HOH C1156     -11.219  -3.795  51.018  1.00 41.10           O
HETATM 2486  O   HOH C1157      -1.872 -11.930  55.846  1.00 42.38           O
HETATM 2487  O   HOH C1158     -22.166 -18.676  46.928  1.00 30.65           O
HETATM 2488  O   HOH C1159     -15.344  -9.813  29.854  1.00 37.10           O
HETATM 2489  O   HOH C1160      -8.411  -4.423  40.296  1.00 40.70           O
HETATM 2490  O  AHOH C1161     -13.796 -26.664  64.188  0.50 22.41           O
HETATM 2491  O  BHOH C1161     -15.911 -26.495  63.751  0.50 23.87           O
HETATM 2492  O   HOH C1162      -1.301 -10.372  41.732  1.00 40.84           O
HETATM 2493  O   HOH C1163     -11.534 -26.074  44.246  1.00 36.65           O
HETATM 2494  O   HOH C1164     -14.151 -16.285  61.474  1.00 22.60           O
HETATM 2495  O   HOH C1165     -17.889 -10.319  29.607  1.00 47.89           O
HETATM 2496  O   HOH C1166     -25.370 -21.282  43.314  1.00 49.89           O
HETATM 2497  O   HOH C1167     -12.881 -23.476  36.688  1.00 45.26           O
HETATM 2498  O   HOH C1168     -15.880 -18.060  62.467  1.00 42.05           O
HETATM 2499  O   HOH C1169     -13.031  -4.408  53.448  1.00 33.94           O
HETATM 2500  O   HOH C1170     -27.141  -9.146  31.720  1.00 29.22           O
HETATM 2501  O   HOH C1171     -26.201  -8.032  34.312  1.00 41.70           O
HETATM 2502  O   HOH C1172      -7.360 -29.344  52.730  1.00 36.66           O
HETATM 2503  O   HOH C1173      -7.738 -26.646  45.695  1.00 27.12           O
HETATM 2504  O   HOH C1174      -2.117  -4.732  47.625  1.00 37.58           O
HETATM 2505  O   HOH C1175       1.605 -28.617  50.293  1.00 50.84           O
HETATM 2506  O   HOH C1176     -11.046  -1.333  50.870  1.00 37.28           O
HETATM 2507  O   HOH C1177      -0.925 -15.673  42.578  1.00 38.66           O
HETATM 2508  O   HOH C1178     -20.353 -11.420  27.825  1.00 43.19           O
HETATM 2509  O   HOH C1179      -3.261 -25.195  37.834  1.00 38.29           O
HETATM 2510  O   HOH C1180      -4.129 -24.821  54.326  1.00 34.50           O
HETATM 2511  O   HOH C1181     -14.205 -29.820  56.466  1.00 46.13           O
HETATM 2512  O   HOH C1182     -23.400 -10.850  43.749  1.00 33.26           O
HETATM 2513  O   HOH C1183      -6.497 -22.894  59.892  1.00 32.63           O
HETATM 2514  O   HOH C1184     -22.807 -22.089  36.653  1.00 44.20           O
HETATM 2515  O   HOH C1185     -15.588 -25.556  56.255  1.00 32.66           O
HETATM 2516  O   HOH C1186      -1.068  -2.004  44.151  1.00 52.90           O
HETATM 2517  O   HOH C1187      -5.943 -16.894  68.428  1.00 40.33           O
HETATM 2518  O   HOH C1188     -21.344 -26.569  44.189  1.00 49.45           O
HETATM 2519  O   HOH C1189       2.184 -20.817  52.583  1.00 46.08           O
HETATM 2520  O   HOH C1190     -18.387  -6.893  61.864  1.00 37.09           O
HETATM 2521  O   HOH C1191     -30.920 -12.629  39.430  1.00 48.64           O
HETATM 2522  O   HOH C1192     -19.570 -21.712  39.728  1.00 46.75           O
HETATM 2523  O   HOH C1193     -23.136 -23.054  49.645  1.00 49.47           O
HETATM 2524  O   HOH C1194      -1.850 -27.802  40.890  1.00 40.17           O
HETATM 2525  O   HOH C1195     -25.131 -12.261  58.396  1.00 50.02           O
HETATM 2526  O   HOH C1196     -21.985 -21.824  58.634  1.00 54.80           O
HETATM 2527  O   HOH C1197     -31.396 -18.096  43.145  1.00 41.73           O
HETATM 2528  O   HOH C1198      -2.975  -3.598  35.622  1.00 44.29           O
HETATM 2529  O  AHOH C1199      -5.839 -27.536  37.442  0.50 32.44           O
HETATM 2530  O  BHOH C1199      -7.486 -26.812  36.388  0.50 36.43           O
HETATM 2531  O   HOH C1200     -26.519  -8.214  53.210  1.00 53.79           O
HETATM 2532  O   HOH C1201      -2.232 -31.197  45.020  1.00 47.50           O
HETATM 2533  O   HOH C1202      -0.909 -25.118  41.645  1.00 50.61           O
HETATM 2534  O   HOH C1203     -27.589 -12.802  26.389  1.00 43.16           O
HETATM 2535  O   HOH C1204       1.240 -15.473  62.084  1.00 49.11           O
HETATM 2536  O   HOH C1205      -4.056 -21.194  30.717  1.00 37.22           O
HETATM 2537  O   HOH C1206       1.612  -5.837  44.080  1.00 49.81           O
HETATM 2538  O   HOH C1207      -5.681 -21.840  66.729  1.00 47.19           O
HETATM 2539  O   HOH C1208      -3.570  -5.199  50.175  1.00 50.77           O
HETATM 2540  O   HOH C1209       1.905 -10.673  58.687  1.00 48.79           O
HETATM 2541  O   HOH C1210       1.817 -16.018  48.608  1.00 46.59           O
HETATM 2542  O   HOH C1211      -9.279 -27.204  43.788  1.00 41.30           O
HETATM 2543  O   HOH C1212       1.211 -20.854  59.965  1.00 47.79           O
HETATM 2544  O   HOH C1213     -32.561 -12.071  20.776  1.00 39.27           O
HETATM 2545  O   HOH C1214     -23.769  -1.539  45.575  1.00 49.90           O
HETATM 2546  O   HOH C1215       3.758 -24.932  49.502  1.00 39.97           O
HETATM 2547  O   HOH C1216     -22.555 -21.584  47.531  1.00 43.61           O
HETATM 2548  O   HOH C1217      -7.247 -24.942  33.683  1.00 38.53           O
HETATM 2549  O   HOH C1218     -18.773 -25.142  52.439  1.00 50.99           O
HETATM 2550  O   HOH C1219      -0.301 -15.438  65.276  1.00 50.45           O
HETATM 2551  O   HOH C1220      -5.152 -29.710  60.903  1.00 45.01           O
HETATM 2552  O   HOH C1221     -14.449 -23.098  65.517  1.00 33.95           O
HETATM 2553  O   HOH C1222      -1.124 -24.385  55.548  1.00 48.01           O
HETATM 2554  O   HOH C1223     -30.259 -17.599  49.634  1.00 49.11           O
HETATM 2555  O   HOH C1224      -9.990 -25.487  35.762  1.00 43.23           O
HETATM 2556  O   HOH C1225     -19.092 -17.087  61.366  1.00 53.67           O
HETATM 2557  O   HOH C1226     -17.086 -20.474  26.973  1.00 39.93           O
HETATM 2558  O   HOH C1227     -10.169 -29.271  40.672  1.00 37.44           O
HETATM 2559  O   HOH C1228     -29.659 -16.028  55.272  1.00 60.71           O
HETATM 2560  O   HOH C1229     -15.533  -4.618  37.378  1.00 51.93           O
HETATM 2561  O   HOH C1230       1.772  -8.841  40.799  1.00 44.89           O
HETATM 2562  O   HOH C1231     -17.240   1.706  37.600  1.00 55.38           O
HETATM 2563  O   HOH C1232     -26.683  -4.632  24.425  1.00 44.76           O
HETATM 2564  O   HOH C1233     -10.532 -25.322  67.138  1.00 61.18           O
HETATM 2565  O   HOH C1234     -12.201 -10.414  26.962  1.00 49.22           O
HETATM 2566  O   HOH C1235      -7.330 -25.567  67.189  1.00 57.65           O
CONECT    6    5 1092
CONECT   29  129   28
CONECT  129  128   29
CONECT  277  276 1046
CONECT  575 2242
CONECT  576 2242
CONECT  614 2242
CONECT  615 2242
CONECT  810 2241
CONECT  825 2241
CONECT  833 2242
CONECT  858 2242
CONECT  862 2241
CONECT  870 2242
CONECT  871 2243
CONECT  877  876  977
CONECT  945 2241
CONECT  950 2241
CONECT  953 2241
CONECT  977  877  976
CONECT 1046  277 1045
CONECT 1092    6 1091
CONECT 1107 2187 1106
CONECT 1130 1129 1230
CONECT 1230 1130 1229
CONECT 1378 2141 1377
CONECT 1670 2299
CONECT 1671 2299
CONECT 1709 2299
CONECT 1710 2299
CONECT 1905 2298
CONECT 1920 2298
CONECT 1928 2299
CONECT 1953 2299
CONECT 1957 2298
CONECT 1965 2299
CONECT 1966 2300
CONECT 1972 1971 2072
CONECT 2040 2298
CONECT 2045 2298
CONECT 2048 2298
CONECT 2072 1972 2071
CONECT 2141 2140 1378
CONECT 2187 2186 1107
CONECT 2229 2228 2230 2234
CONECT 2234 2192 2193 2229
CONECT 2193 2189 2233 2234
CONECT 2189 2193 2232 2190
CONECT 2190 2189 2191 2230
CONECT 2191 2231 2190
CONECT 2215 2216 2214
CONECT 2219 2216 2220
CONECT 2195 2194 2196
CONECT 2199 2200 2196
CONECT 2214 2215 2213
CONECT 2220 2213 2219
CONECT 2194 2195 2201
CONECT 2200 2199 2201
CONECT 2235 2192 2238
CONECT 2239 2238 2240
CONECT 2225 2224 2226
CONECT 2217 2216 2218
CONECT 2197 2196 2198
CONECT 2224 2223 2225
CONECT 2212 2213 2211
CONECT 2202 2203 2201
CONECT 2221 2208 2222
CONECT 2207 2206 2227
CONECT 2209 2210 2208 2211
CONECT 2204 2206 2203 2205
CONECT 2216 2215 2219 2217
CONECT 2196 2199 2195 2197
CONECT 2213 2220 2214 2212
CONECT 2201 2194 2200 2202
CONECT 2238 2235 2237 2239
CONECT 2222 2221 2223 2227
CONECT 2227 2228 2222 2207
CONECT 2208 2206 2221 2209
CONECT 2206 2208 2204 2207
CONECT 2226 2225
CONECT 2192 2234 2235 2236
CONECT 2240 2239
CONECT 2237 2236 2238
CONECT 2236 2192 2237
CONECT 2211 2212 2209
CONECT 2203 2202 2204
CONECT 2228 2227 2229
CONECT 2233 2193
CONECT 2233 2241
CONECT 2232 2189
CONECT 2232 2241
CONECT 2230 2190 2229
CONECT 2231 2191
CONECT 2210 2209
CONECT 2205 2204
CONECT 2218 2217
CONECT 2198 2197
CONECT 2223 2224 2222
CONECT 2241  945  950 2233  953
CONECT 2241 2232  810  825  862
CONECT 2242  575  576  614  615
CONECT 2242 2335  833  858  870
CONECT 2243 2350 2416 2357 2310
CONECT 2243 2328  871
CONECT 2286 2287 2285 2291
CONECT 2291 2286 2250 2249
CONECT 2250 2290 2291 2246
CONECT 2246 2289 2250 2247
CONECT 2247 2287 2246 2248
CONECT 2248 2288 2247
CONECT 2272 2273 2271
CONECT 2276 2273 2277
CONECT 2252 2253 2251
CONECT 2256 2253 2257
CONECT 2271 2270 2272
CONECT 2277 2270 2276
CONECT 2251 2252 2258
CONECT 2257 2256 2258
CONECT 2292 2295 2249
CONECT 2296 2297 2295
CONECT 2282 2281 2283
CONECT 2274 2273 2275
CONECT 2254 2253 2255
CONECT 2281 2280 2282
CONECT 2269 2270 2268
CONECT 2259 2258 2260
CONECT 2278 2279 2265
CONECT 2264 2284 2263
CONECT 2266 2267 2268 2265
CONECT 2261 2262 2263 2260
CONECT 2273 2272 2276 2274
CONECT 2253 2252 2254 2256
CONECT 2270 2271 2277 2269
CONECT 2258 2257 2251 2259
CONECT 2295 2292 2294 2296
CONECT 2279 2284 2280 2278
CONECT 2284 2285 2279 2264
CONECT 2265 2278 2266 2263
CONECT 2263 2264 2265 2261
CONECT 2283 2282
CONECT 2249 2292 2293 2291
CONECT 2297 2296
CONECT 2294 2295 2293
CONECT 2293 2294 2249
CONECT 2268 2266 2269
CONECT 2260 2259 2261
CONECT 2285 2284 2286
CONECT 2290 2250
CONECT 2290 2298
CONECT 2289 2246
CONECT 2289 2298
CONECT 2287 2286 2247
CONECT 2288 2248
CONECT 2267 2266
CONECT 2262 2261
CONECT 2275 2274
CONECT 2255 2254
CONECT 2280 2281 2279
CONECT 2298 2040 2045 2048 2290
CONECT 2298 2289 1905 1920 1957
CONECT 2299 1670 1671 1709 1710
CONECT 2299 2450 1928 1953 1965
CONECT 2300 2457 2459 2552 2441
CONECT 2300 2455 1966
CONECT 2310 2243
CONECT 2328 2243
CONECT 2335 2242
CONECT 2350 2243
CONECT 2357 2243
CONECT 2416 2243
CONECT 2441 2300
CONECT 2450 2299
CONECT 2455 2300
CONECT 2457 2300
CONECT 2459 2300
CONECT 2552 2300
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.