CNRS Nantes University US2B US2B
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***  TRANSCRIPTION 30-APR-04 1T4W  ***

elNémo ID: 23043011422516520

Job options:

ID        	=	 23043011422516520
JOBID     	=	 TRANSCRIPTION 30-APR-04 1T4W
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    TRANSCRIPTION                           30-APR-04   1T4W              
TITLE     STRUCTURAL DIFFERENCES IN THE DNA BINDING DOMAINS OF HUMAN            
TITLE    2 P53 AND ITS C. ELEGANS ORTHOLOG CEP-1: STRUCTURE OF C.               
TITLE    3 ELEGANS CEP-1                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C.ELEGANS P53 TUMOR SUPPRESSOR-LIKE                        
COMPND   3 TRANSCRIPTION FACTOR;                                                
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: DNA BINDING DOMAIN;                                        
COMPND   6 SYNONYM: CEP-1;                                                      
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    DNA-BINDING DOMAIN, TRANSCRIPTION                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.HUYEN,P.D.JEFFREY,W.B.DERRY,J.H.ROTHMAN,N.P.PAVLETICH,              
AUTHOR   2 E.S.STAVRIDI,T.D.HALAZONETIS                                         
REVDAT   2   24-FEB-09 1T4W    1       VERSN                                    
REVDAT   1   20-JUL-04 1T4W    0                                                
JRNL        AUTH   Y.HUYEN,P.D.JEFFREY,W.B.DERRY,J.H.ROTHMAN,                   
JRNL        AUTH 2 N.P.PAVLETICH,E.S.STAVRIDI,T.D.HALAZONETIS                   
JRNL        TITL   STRUCTURAL DIFFERENCES IN THE DNA BINDING DOMAINS            
JRNL        TITL 2 OF HUMAN P53 AND ITS C. ELEGANS ORTHOLOG CEP-1.              
JRNL        REF    STRUCTURE                     V.  12  1237 2004              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15242600                                                     
JRNL        DOI    10.1016/J.STR.2004.05.007                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1522442.610                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14247                          
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 SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1414                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2075                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1920                       
REMARK   3   BIN FREE R VALUE                    : 0.2820                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 241                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1652                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.39000                                             
REMARK   3    B22 (A**2) : -1.37000                                             
REMARK   3    B33 (A**2) : 3.75000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 63.39                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1T4W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022315.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 9.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16384                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, ISOPROPYL ALCOHOL,       
REMARK 280  DTT, BTP, PH 9.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  298.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.68000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.09000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.21500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.09000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.68000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.21500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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    ALA A 236      -59.02    -23.70                                   
REMARK 500    MET A 346     -160.01   -113.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 307   SG                                                     
REMARK 620 2 HIS A 310   ND1 103.3                                              
REMARK 620 3 CYS A 361   SG  111.5 119.9                                        
REMARK 620 4 CYS A 365   SG  108.1 104.5 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201                  
DBREF  1T4W A  223   418  UNP    Q20646   Q20646_CAEEL   223    418             
SEQRES   1 A  196  GLU LYS TRP MET GLU ILE ASP VAL LEU LYS GLN LYS VAL          
SEQRES   2 A  196  ALA LYS SER SER ASP MET ALA PHE ALA ILE SER SER GLU          
SEQRES   3 A  196  HIS GLU LYS TYR LEU TRP THR LYS MET GLY CYS LEU VAL          
SEQRES   4 A  196  PRO ILE GLN VAL LYS TRP LYS LEU ASP LYS ARG HIS PHE          
SEQRES   5 A  196  ASN SER ASN LEU SER LEU ARG ILE ARG PHE VAL LYS TYR          
SEQRES   6 A  196  ASP LYS LYS GLU ASN VAL GLU TYR ALA ILE ARG ASN PRO          
SEQRES   7 A  196  ARG SER ASP VAL MET LYS CYS ARG SER HIS THR GLU ARG          
SEQRES   8 A  196  GLU GLN HIS PHE PRO PHE ASP SER PHE PHE TYR ILE ARG          
SEQRES   9 A  196  ASN SER GLU HIS GLU PHE SER TYR SER ALA GLU LYS GLY          
SEQRES  10 A  196  SER THR PHE THR LEU ILE MET TYR PRO GLY ALA VAL GLN          
SEQRES  11 A  196  ALA ASN PHE ASP ILE ILE PHE MET CYS GLN GLU LYS CYS          
SEQRES  12 A  196  LEU ASP LEU ASP ASP ARG ARG LYS THR MET CYS LEU ALA          
SEQRES  13 A  196  VAL PHE LEU ASP ASP GLU ASN GLY ASN GLU ILE LEU HIS          
SEQRES  14 A  196  ALA TYR ILE LYS GLN VAL ARG ILE VAL ALA TYR PRO ARG          
SEQRES  15 A  196  ARG ASP TRP LYS ASN PHE CYS GLU ARG GLU ASP ALA LYS          
SEQRES  16 A  196  GLN                                                          
HET     ZN  A 201       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *155(H2 O)                                                    
HELIX    1   1 LEU A  231  ALA A  236  1                                   6    
HELIX    2   2 ASN A  292  ILE A  297  1                                   6    
HELIX    3   3 CYS A  307  ARG A  313  1                                   7    
HELIX    4   4 GLN A  362  LEU A  366  5                                   5    
HELIX    5   5 ASP A  367  ARG A  372  1                                   6    
HELIX    6   6 TYR A  402  LYS A  417  1                                  16    
SHEET    1   A 4 TRP A 225  VAL A 230  0                                        
SHEET    2   A 4 VAL A 261  LYS A 268 -1  O  GLN A 264   N  ASP A 229           
SHEET    3   A 4 GLN A 352  PHE A 359 -1  O  ALA A 353   N  VAL A 265           
SHEET    4   A 4 PHE A 323  ARG A 326 -1  N  ARG A 326   O  ASP A 356           
SHEET    1   B 7 MET A 241  ILE A 245  0                                        
SHEET    2   B 7 LYS A 251  THR A 255 -1  O  TYR A 252   N  ALA A 244           
SHEET    3   B 7 GLU A 388  ILE A 399  1  O  GLN A 396   N  LEU A 253           
SHEET    4   B 7 THR A 374  ASP A 382 -1  N  LEU A 381   O  ILE A 389           
SHEET    5   B 7 SER A 279  TYR A 287 -1  N  VAL A 285   O  CYS A 376           
SHEET    6   B 7 THR A 341  ILE A 345 -1  O  LEU A 344   N  LEU A 280           
SHEET    7   B 7 GLU A 331  SER A 335 -1  N  GLU A 331   O  ILE A 345           
LINK        ZN    ZN A 201                 SG  CYS A 307     1555   1555  2.39  
LINK        ZN    ZN A 201                 ND1 HIS A 310     1555   1555  1.95  
LINK        ZN    ZN A 201                 SG  CYS A 361     1555   1555  2.36  
LINK        ZN    ZN A 201                 SG  CYS A 365     1555   1555  2.40  
CISPEP   1 PHE A  317    PRO A  318          0        -0.48                     
SITE     1 AC1  4 CYS A 307  HIS A 310  CYS A 361  CYS A 365                    
CRYST1   39.360   68.430   88.180  90.00  90.00  90.00 P 21 21 21    4          
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      0.025407  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014613  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011340        0.00000                         
ATOM      1  N   GLU A 223      53.212  37.898   8.510  1.00 63.02           N  
ATOM      2  CA  GLU A 223      52.162  37.056   7.865  1.00 61.74           C  
ATOM      3  C   GLU A 223      50.919  37.876   7.518  1.00 64.18           C  
ATOM      4  O   GLU A 223      50.672  38.178   6.348  1.00 65.67           O  
ATOM      5  CB  GLU A 223      51.750  35.913   8.790  1.00 63.58           C  
ATOM      6  CG  GLU A 223      50.731  34.983   8.163  1.00 74.68           C  
ATOM      7  CD  GLU A 223      49.932  34.213   9.191  1.00 80.11           C  
ATOM      8  OE1 GLU A 223      50.549  33.590  10.083  1.00 91.71           O  
ATOM      9  OE2 GLU A 223      48.685  34.228   9.102  1.00 81.80           O  
ATOM     10  N   LYS A 224      50.128  38.212   8.535  1.00 47.92           N  
ATOM     11  CA  LYS A 224      48.921  39.002   8.328  1.00 40.15           C  
ATOM     12  C   LYS A 224      48.662  39.940   9.503  1.00 26.72           C  
ATOM     13  O   LYS A 224      48.928  39.601  10.656  1.00 32.30           O  
ATOM     14  CB  LYS A 224      47.707  38.088   8.136  1.00 42.97           C  
ATOM     15  CG  LYS A 224      47.351  37.248   9.379  1.00 52.98           C  
ATOM     16  CD  LYS A 224      46.003  36.533   9.238  1.00 39.02           C  
ATOM     17  CE  LYS A 224      45.692  35.675  10.478  1.00 50.99           C  
ATOM     18  NZ  LYS A 224      44.342  35.011  10.435  1.00 40.49           N  
ATOM     19  N   TRP A 225      48.156  41.130   9.213  1.00 23.72           N  
ATOM     20  CA  TRP A 225      47.835  42.072  10.286  1.00 21.65           C  
ATOM     21  C   TRP A 225      46.777  43.049   9.824  1.00 29.67           C  
ATOM     22  O   TRP A 225      46.486  43.151   8.620  1.00 24.26           O  
ATOM     23  CB  TRP A 225      49.078  42.852  10.737  1.00 25.03           C  
ATOM     24  CG  TRP A 225      49.797  43.528   9.605  1.00 29.55           C  
ATOM     25  CD1 TRP A 225      50.917  43.075   8.956  1.00 35.53           C  
ATOM     26  CD2 TRP A 225      49.438  44.760   8.968  1.00 33.94           C  
ATOM     27  NE1 TRP A 225      51.275  43.950   7.963  1.00 27.22           N  
ATOM     28  CE2 TRP A 225      50.386  44.992   7.944  1.00 34.87           C  
ATOM     29  CE3 TRP A 225      48.403  45.690   9.157  1.00 38.99           C  
ATOM     30  CZ2 TRP A 225      50.333  46.118   7.113  1.00 32.69           C  
ATOM     31  CZ3 TRP A 225      48.351  46.813   8.325  1.00 38.85           C  
ATOM     32  CH2 TRP A 225      49.311  47.013   7.317  1.00 31.84           C  
ATOM     33  N   MET A 226      46.186  43.752  10.785  1.00 24.45           N  
ATOM     34  CA  MET A 226      45.195  44.773  10.470  1.00 24.47           C  
ATOM     35  C   MET A 226      45.278  45.877  11.505  1.00 26.16           C  
ATOM     36  O   MET A 226      45.567  45.629  12.676  1.00 29.33           O  
ATOM     37  CB  MET A 226      43.771  44.205  10.411  1.00 30.61           C  
ATOM     38  CG  MET A 226      42.715  45.277  10.014  1.00 27.76           C  
ATOM     39  SD  MET A 226      41.092  44.615   9.493  1.00 33.25           S  
ATOM     40  CE  MET A 226      40.705  43.736  10.863  1.00 17.90           C  
ATOM     41  N   GLU A 227      45.063  47.107  11.060  1.00 25.21           N  
ATOM     42  CA  GLU A 227      45.115  48.254  11.950  1.00 24.93           C  
ATOM     43  C   GLU A 227      43.985  49.190  11.622  1.00 27.78           C  
ATOM     44  O   GLU A 227      43.578  49.283  10.462  1.00 19.57           O  
ATOM     45  CB  GLU A 227      46.412  49.048  11.762  1.00 25.13           C  
ATOM     46  CG  GLU A 227      47.694  48.334  12.158  1.00 35.32           C  
ATOM     47  CD  GLU A 227      47.811  48.146  13.652  1.00 44.18           C  
ATOM     48  OE1 GLU A 227      47.465  49.084  14.404  1.00 47.50           O  
ATOM     49  OE2 GLU A 227      48.260  47.064  14.076  1.00 50.43           O  
ATOM     50  N   ILE A 228      43.461  49.863  12.645  1.00 19.80           N  
ATOM     51  CA  ILE A 228      42.441  50.861  12.411  1.00 20.76           C  
ATOM     52  C   ILE A 228      43.033  52.165  12.972  1.00 21.56           C  
ATOM     53  O   ILE A 228      43.646  52.164  14.026  1.00 20.26           O  
ATOM     54  CB  ILE A 228      41.084  50.500  13.072  1.00 18.88           C  
ATOM     55  CG1 ILE A 228      40.110  51.657  12.854  1.00 23.36           C  
ATOM     56  CG2 ILE A 228      41.268  50.141  14.558  1.00 20.21           C  
ATOM     57  CD1 ILE A 228      38.656  51.358  13.179  1.00 15.00           C  
ATOM     58  N   ASP A 229      42.897  53.265  12.237  1.00 17.61           N  
ATOM     59  CA  ASP A 229      43.436  54.544  12.688  1.00 24.20           C  
ATOM     60  C   ASP A 229      42.585  55.678  12.151  1.00 20.67           C  
ATOM     61  O   ASP A 229      41.790  55.481  11.240  1.00 18.39           O  
ATOM     62  CB  ASP A 229      44.860  54.751  12.159  1.00 22.29           C  
ATOM     63  CG  ASP A 229      45.860  53.820  12.778  1.00 33.40           C  
ATOM     64  OD1 ASP A 229      46.294  54.085  13.923  1.00 33.90           O  
ATOM     65  OD2 ASP A 229      46.205  52.818  12.107  1.00 31.21           O  
ATOM     66  N   VAL A 230      42.741  56.874  12.702  1.00 23.46           N  
ATOM     67  CA  VAL A 230      41.999  57.994  12.130  1.00 29.36           C  
ATOM     68  C   VAL A 230      42.973  58.567  11.086  1.00 29.13           C  
ATOM     69  O   VAL A 230      44.160  58.278  11.132  1.00 34.90           O  
ATOM     70  CB  VAL A 230      41.671  59.089  13.174  1.00 30.90           C  
ATOM     71  CG1 VAL A 230      40.795  58.505  14.299  1.00 22.25           C  
ATOM     72  CG2 VAL A 230      42.970  59.683  13.718  1.00 43.55           C  
ATOM     73  N   LEU A 231      42.475  59.339  10.131  1.00 29.66           N  
ATOM     74  CA  LEU A 231      43.349  59.952   9.136  1.00 23.18           C  
ATOM     75  C   LEU A 231      44.026  61.124   9.850  1.00 30.39           C  
ATOM     76  O   LEU A 231      43.468  62.208   9.931  1.00 27.81           O  
ATOM     77  CB  LEU A 231      42.524  60.455   7.957  1.00 25.28           C  
ATOM     78  CG  LEU A 231      43.264  61.060   6.765  1.00 45.38           C  
ATOM     79  CD1 LEU A 231      44.332  60.082   6.260  1.00 51.23           C  
ATOM     80  CD2 LEU A 231      42.258  61.372   5.662  1.00 45.10           C  
ATOM     81  N   LYS A 232      45.228  60.883  10.363  1.00 25.42           N  
ATOM     82  CA  LYS A 232      45.982  61.862  11.127  1.00 45.45           C  
ATOM     83  C   LYS A 232      46.099  63.262  10.565  1.00 49.50           C  
ATOM     84  O   LYS A 232      45.960  64.239  11.300  1.00 45.64           O  
ATOM     85  CB  LYS A 232      47.372  61.304  11.437  1.00 47.54           C  
ATOM     86  CG  LYS A 232      47.332  60.141  12.424  1.00 58.61           C  
ATOM     87  CD  LYS A 232      46.453  60.486  13.635  1.00 66.47           C  
ATOM     88  CE  LYS A 232      46.930  61.771  14.341  1.00 75.40           C  
ATOM     89  NZ  LYS A 232      45.817  62.627  14.869  1.00 41.01           N  
ATOM     90  N   GLN A 233      46.350  63.370   9.270  1.00 43.57           N  
ATOM     91  CA  GLN A 233      46.479  64.676   8.649  1.00 54.86           C  
ATOM     92  C   GLN A 233      45.366  65.590   9.134  1.00 49.10           C  
ATOM     93  O   GLN A 233      45.618  66.640   9.716  1.00 58.88           O  
ATOM     94  CB  GLN A 233      46.404  64.567   7.119  1.00 62.97           C  
ATOM     95  CG  GLN A 233      47.516  63.757   6.459  1.00 70.36           C  
ATOM     96  CD  GLN A 233      47.306  62.252   6.549  1.00 77.20           C  
ATOM     97  OE1 GLN A 233      47.427  61.650   7.622  1.00 71.71           O  
ATOM     98  NE2 GLN A 233      46.988  61.635   5.413  1.00 77.09           N  
ATOM     99  N   LYS A 234      44.128  65.179   8.910  1.00 46.92           N  
ATOM    100  CA  LYS A 234      42.990  65.995   9.303  1.00 47.34           C  
ATOM    101  C   LYS A 234      42.746  66.080  10.804  1.00 38.63           C  
ATOM    102  O   LYS A 234      42.446  67.146  11.331  1.00 49.99           O  
ATOM    103  CB  LYS A 234      41.734  65.488   8.608  1.00 52.38           C  
ATOM    104  CG  LYS A 234      41.899  65.333   7.111  1.00 61.26           C  
ATOM    105  CD  LYS A 234      40.563  65.489   6.405  1.00 70.49           C  
ATOM    106  CE  LYS A 234      39.533  64.499   6.918  1.00 67.03           C  
ATOM    107  NZ  LYS A 234      38.176  64.825   6.399  1.00 70.24           N  
ATOM    108  N   VAL A 235      42.883  64.965  11.502  1.00 43.21           N  
ATOM    109  CA  VAL A 235      42.641  64.966  12.937  1.00 48.69           C  
ATOM    110  C   VAL A 235      43.645  65.802  13.740  1.00 42.51           C  
ATOM    111  O   VAL A 235      43.274  66.461  14.709  1.00 49.14           O  
ATOM    112  CB  VAL A 235      42.604  63.514  13.470  1.00 45.92           C  
ATOM    113  CG1 VAL A 235      42.511  63.495  15.003  1.00 47.10           C  
ATOM    114  CG2 VAL A 235      41.403  62.793  12.856  1.00 49.47           C  
ATOM    115  N   ALA A 236      44.901  65.781  13.308  1.00 46.04           N  
ATOM    116  CA  ALA A 236      46.010  66.493  13.945  1.00 33.80           C  
ATOM    117  C   ALA A 236      45.714  67.725  14.817  1.00 38.25           C  
ATOM    118  O   ALA A 236      46.065  67.740  15.997  1.00 40.26           O  
ATOM    119  CB  ALA A 236      47.053  66.854  12.884  1.00 40.00           C  
ATOM    120  N   LYS A 237      45.087  68.755  14.256  1.00 31.43           N  
ATOM    121  CA  LYS A 237      44.797  69.967  15.033  1.00 35.27           C  
ATOM    122  C   LYS A 237      43.328  70.352  15.085  1.00 43.06           C  
ATOM    123  O   LYS A 237      42.997  71.495  15.396  1.00 34.68           O  
ATOM    124  CB  LYS A 237      45.601  71.146  14.481  1.00 42.01           C  
ATOM    125  CG  LYS A 237      47.104  70.893  14.447  1.00 43.01           C  
ATOM    126  CD  LYS A 237      47.877  72.166  14.180  1.00 53.06           C  
ATOM    127  CE  LYS A 237      49.379  71.930  14.265  1.00 53.48           C  
ATOM    128  NZ  LYS A 237      50.136  73.210  14.142  1.00 53.11           N  
ATOM    129  N   SER A 238      42.447  69.399  14.796  1.00 32.93           N  
ATOM    130  CA  SER A 238      41.018  69.664  14.798  1.00 22.37           C  
ATOM    131  C   SER A 238      40.476  69.984  16.193  1.00 30.98           C  
ATOM    132  O   SER A 238      40.929  69.422  17.188  1.00 27.53           O  
ATOM    133  CB  SER A 238      40.260  68.448  14.248  1.00 21.93           C  
ATOM    134  OG  SER A 238      38.895  68.524  14.600  1.00 23.60           O  
ATOM    135  N   SER A 239      39.501  70.886  16.257  1.00 26.15           N  
ATOM    136  CA  SER A 239      38.875  71.239  17.527  1.00 35.31           C  
ATOM    137  C   SER A 239      37.845  70.187  17.890  1.00 30.79           C  
ATOM    138  O   SER A 239      37.556  69.980  19.061  1.00 35.37           O  
ATOM    139  CB  SER A 239      38.152  72.591  17.435  1.00 27.39           C  
ATOM    140  OG  SER A 239      39.066  73.657  17.257  1.00 54.58           O  
ATOM    141  N   ASP A 240      37.312  69.521  16.870  1.00 26.30           N  
ATOM    142  CA  ASP A 240      36.253  68.525  17.026  1.00 28.15           C  
ATOM    143  C   ASP A 240      36.617  67.097  17.357  1.00 26.97           C  
ATOM    144  O   ASP A 240      35.722  66.299  17.654  1.00 23.24           O  
ATOM    145  CB  ASP A 240      35.404  68.475  15.758  1.00 31.94           C  
ATOM    146  CG  ASP A 240      34.813  69.807  15.415  1.00 35.79           C  
ATOM    147  OD1 ASP A 240      34.826  70.694  16.296  1.00 34.67           O  
ATOM    148  OD2 ASP A 240      34.332  69.948  14.273  1.00 32.50           O  
ATOM    149  N   MET A 241      37.898  66.760  17.259  1.00 24.96           N  
ATOM    150  CA  MET A 241      38.344  65.392  17.536  1.00 22.21           C  
ATOM    151  C   MET A 241      39.838  65.357  17.739  1.00 18.88           C  
ATOM    152  O   MET A 241      40.550  66.251  17.296  1.00 23.94           O  
ATOM    153  CB  MET A 241      37.966  64.473  16.376  1.00 15.85           C  
ATOM    154  CG  MET A 241      38.430  65.014  15.022  1.00 25.54           C  
ATOM    155  SD  MET A 241      37.644  64.170  13.630  1.00 25.88           S  
ATOM    156  CE  MET A 241      35.952  64.837  13.764  1.00 21.30           C  
ATOM    157  N   ALA A 242      40.306  64.290  18.375  1.00 21.77           N  
ATOM    158  CA  ALA A 242      41.717  64.118  18.679  1.00 22.91           C  
ATOM    159  C   ALA A 242      41.973  62.630  18.892  1.00 29.26           C  
ATOM    160  O   ALA A 242      41.105  61.897  19.377  1.00 21.93           O  
ATOM    161  CB  ALA A 242      42.064  64.887  19.939  1.00 15.63           C  
ATOM    162  N   PHE A 243      43.178  62.201  18.548  1.00 27.10           N  
ATOM    163  CA  PHE A 243      43.570  60.802  18.649  1.00 28.96           C  
ATOM    164  C   PHE A 243      44.897  60.698  19.363  1.00 30.45           C  
ATOM    165  O   PHE A 243      45.737  61.585  19.247  1.00 32.62           O  
ATOM    166  CB  PHE A 243      43.677  60.213  17.234  1.00 30.72           C  
ATOM    167  CG  PHE A 243      44.134  58.782  17.195  1.00 47.67           C  
ATOM    168  CD1 PHE A 243      45.458  58.448  17.486  1.00 56.48           C  
ATOM    169  CD2 PHE A 243      43.236  57.762  16.896  1.00 53.62           C  
ATOM    170  CE1 PHE A 243      45.875  57.118  17.483  1.00 56.70           C  
ATOM    171  CE2 PHE A 243      43.644  56.430  16.889  1.00 46.19           C  
ATOM    172  CZ  PHE A 243      44.964  56.109  17.185  1.00 56.49           C  
ATOM    173  N   ALA A 244      45.088  59.625  20.119  1.00 23.51           N  
ATOM    174  CA  ALA A 244      46.357  59.436  20.802  1.00 23.63           C  
ATOM    175  C   ALA A 244      46.563  57.954  21.072  1.00 31.47           C  
ATOM    176  O   ALA A 244      45.640  57.138  20.932  1.00 22.33           O  
ATOM    177  CB  ALA A 244      46.401  60.226  22.125  1.00 23.29           C  
ATOM    178  N   ILE A 245      47.786  57.622  21.460  1.00 26.42           N  
ATOM    179  CA  ILE A 245      48.165  56.260  21.772  1.00 27.69           C  
ATOM    180  C   ILE A 245      48.573  56.315  23.214  1.00 32.29           C  
ATOM    181  O   ILE A 245      49.100  57.334  23.654  1.00 30.59           O  
ATOM    182  CB  ILE A 245      49.394  55.813  20.973  1.00 34.40           C  
ATOM    183  CG1 ILE A 245      49.140  55.958  19.472  1.00 41.33           C  
ATOM    184  CG2 ILE A 245      49.723  54.378  21.323  1.00 43.65           C  
ATOM    185  CD1 ILE A 245      48.107  55.017  18.914  1.00 42.30           C  
ATOM    186  N   SER A 246      48.331  55.236  23.953  1.00 21.12           N  
ATOM    187  CA  SER A 246      48.718  55.205  25.350  1.00 24.09           C  
ATOM    188  C   SER A 246      50.161  54.724  25.414  1.00 42.56           C  
ATOM    189  O   SER A 246      50.746  54.364  24.388  1.00 35.31           O  
ATOM    190  CB  SER A 246      47.827  54.248  26.139  1.00 31.23           C  
ATOM    191  OG  SER A 246      48.078  52.898  25.784  1.00 24.37           O  
ATOM    192  N   SER A 247      50.735  54.729  26.611  1.00 38.18           N  
ATOM    193  CA  SER A 247      52.102  54.267  26.788  1.00 54.29           C  
ATOM    194  C   SER A 247      52.134  52.792  26.405  1.00 50.95           C  
ATOM    195  O   SER A 247      53.177  52.268  26.033  1.00 52.33           O  
ATOM    196  CB  SER A 247      52.542  54.422  28.241  1.00 52.52           C  
ATOM    197  OG  SER A 247      51.952  53.417  29.045  1.00 60.13           O  
ATOM    198  N   GLU A 248      50.981  52.129  26.493  1.00 49.35           N  
ATOM    199  CA  GLU A 248      50.885  50.718  26.132  1.00 48.44           C  
ATOM    200  C   GLU A 248      50.555  50.555  24.649  1.00 41.09           C  
ATOM    201  O   GLU A 248      50.266  49.458  24.182  1.00 39.47           O  
ATOM    202  CB  GLU A 248      49.826  50.020  26.978  1.00 42.72           C  
ATOM    203  CG  GLU A 248      50.054  50.199  28.460  1.00 64.34           C  
ATOM    204  CD  GLU A 248      51.448  49.768  28.873  1.00 73.55           C  
ATOM    205  OE1 GLU A 248      51.732  48.551  28.834  1.00 79.18           O  
ATOM    206  OE2 GLU A 248      52.266  50.646  29.225  1.00 77.73           O  
ATOM    207  N   HIS A 249      50.581  51.661  23.918  1.00 36.21           N  
ATOM    208  CA  HIS A 249      50.318  51.642  22.478  1.00 45.78           C  
ATOM    209  C   HIS A 249      48.883  51.344  22.009  1.00 44.09           C  
ATOM    210  O   HIS A 249      48.663  51.012  20.852  1.00 35.37           O  
ATOM    211  CB  HIS A 249      51.295  50.682  21.794  1.00 58.09           C  
ATOM    212  CG  HIS A 249      52.725  51.111  21.900  1.00 65.77           C  
ATOM    213  ND1 HIS A 249      53.200  52.264  21.313  1.00 68.12           N  
ATOM    214  CD2 HIS A 249      53.774  50.564  22.559  1.00 67.44           C  
ATOM    215  CE1 HIS A 249      54.479  52.412  21.608  1.00 65.38           C  
ATOM    216  NE2 HIS A 249      54.851  51.395  22.364  1.00 71.43           N  
ATOM    217  N   GLU A 250      47.917  51.458  22.909  1.00 33.16           N  
ATOM    218  CA  GLU A 250      46.523  51.251  22.569  1.00 27.00           C  
ATOM    219  C   GLU A 250      46.002  52.582  22.042  1.00 22.74           C  
ATOM    220  O   GLU A 250      46.512  53.650  22.408  1.00 19.13           O  
ATOM    221  CB  GLU A 250      45.777  50.795  23.810  1.00 24.17           C  
ATOM    222  CG  GLU A 250      46.392  49.518  24.351  1.00 33.07           C  
ATOM    223  CD  GLU A 250      45.519  48.818  25.357  1.00 46.86           C  
ATOM    224  OE1 GLU A 250      45.285  49.381  26.455  1.00 34.90           O  
ATOM    225  OE2 GLU A 250      45.067  47.696  25.039  1.00 55.80           O  
ATOM    226  N   LYS A 251      44.986  52.528  21.192  1.00 22.21           N  
ATOM    227  CA  LYS A 251      44.467  53.733  20.567  1.00 18.47           C  
ATOM    228  C   LYS A 251      43.256  54.368  21.220  1.00 19.84           C  
ATOM    229  O   LYS A 251      42.299  53.683  21.573  1.00 20.87           O  
ATOM    230  CB  LYS A 251      44.190  53.428  19.108  1.00 23.48           C  
ATOM    231  CG  LYS A 251      45.405  52.758  18.468  1.00 30.53           C  
ATOM    232  CD  LYS A 251      45.204  52.496  17.017  1.00 25.09           C  
ATOM    233  CE  LYS A 251      46.482  51.908  16.419  1.00 25.70           C  
ATOM    234  NZ  LYS A 251      46.203  51.530  15.037  1.00 27.95           N  
ATOM    235  N   TYR A 252      43.304  55.691  21.348  1.00 19.62           N  
ATOM    236  CA  TYR A 252      42.224  56.457  21.976  1.00 26.44           C  
ATOM    237  C   TYR A 252      41.714  57.568  21.079  1.00 23.20           C  
ATOM    238  O   TYR A 252      42.485  58.318  20.480  1.00 21.92           O  
ATOM    239  CB  TYR A 252      42.703  57.082  23.293  1.00 20.23           C  
ATOM    240  CG  TYR A 252      43.061  56.077  24.366  1.00 18.01           C  
ATOM    241  CD1 TYR A 252      44.116  55.182  24.190  1.00 17.79           C  
ATOM    242  CD2 TYR A 252      42.326  56.011  25.553  1.00 14.42           C  
ATOM    243  CE1 TYR A 252      44.433  54.240  25.170  1.00 21.00           C  
ATOM    244  CE2 TYR A 252      42.633  55.078  26.538  1.00 20.21           C  
ATOM    245  CZ  TYR A 252      43.686  54.199  26.341  1.00 30.08           C  
ATOM    246  OH  TYR A 252      43.999  53.304  27.331  1.00 29.74           O  
ATOM    247  N   LEU A 253      40.399  57.672  20.989  1.00 21.04           N  
ATOM    248  CA  LEU A 253      39.775  58.719  20.192  1.00 18.04           C  
ATOM    249  C   LEU A 253      38.789  59.538  21.038  1.00 17.73           C  
ATOM    250  O   LEU A 253      38.032  58.981  21.835  1.00 16.98           O  
ATOM    251  CB  LEU A 253      39.001  58.114  19.005  1.00 16.18           C  
ATOM    252  CG  LEU A 253      38.047  59.079  18.277  1.00 23.61           C  
ATOM    253  CD1 LEU A 253      38.853  60.048  17.413  1.00 19.82           C  
ATOM    254  CD2 LEU A 253      37.068  58.280  17.400  1.00 20.59           C  
ATOM    255  N   TRP A 254      38.823  60.856  20.879  1.00 18.04           N  
ATOM    256  CA  TRP A 254      37.864  61.730  21.553  1.00 20.58           C  
ATOM    257  C   TRP A 254      37.302  62.526  20.396  1.00 21.58           C  
ATOM    258  O   TRP A 254      38.066  63.001  19.556  1.00 19.06           O  
ATOM    259  CB  TRP A 254      38.536  62.698  22.539  1.00 19.19           C  
ATOM    260  CG  TRP A 254      39.258  62.027  23.697  1.00 17.39           C  
ATOM    261  CD1 TRP A 254      38.779  61.806  24.960  1.00 18.72           C  
ATOM    262  CD2 TRP A 254      40.583  61.503  23.672  1.00 13.65           C  
ATOM    263  NE1 TRP A 254      39.735  61.183  25.731  1.00 11.74           N  
ATOM    264  CE2 TRP A 254      40.852  60.981  24.961  1.00 17.99           C  
ATOM    265  CE3 TRP A 254      41.572  61.418  22.680  1.00 17.56           C  
ATOM    266  CZ2 TRP A 254      42.072  60.383  25.286  1.00 15.58           C  
ATOM    267  CZ3 TRP A 254      42.786  60.823  23.003  1.00 19.02           C  
ATOM    268  CH2 TRP A 254      43.025  60.315  24.298  1.00 19.93           C  
ATOM    269  N   THR A 255      35.983  62.668  20.337  1.00 16.37           N  
ATOM    270  CA  THR A 255      35.352  63.442  19.253  1.00 15.26           C  
ATOM    271  C   THR A 255      34.021  63.994  19.742  1.00 23.20           C  
ATOM    272  O   THR A 255      33.451  63.477  20.703  1.00 20.86           O  
ATOM    273  CB  THR A 255      35.075  62.536  18.008  1.00 11.40           C  
ATOM    274  OG1 THR A 255      34.324  63.252  17.016  1.00 17.09           O  
ATOM    275  CG2 THR A 255      34.288  61.299  18.427  1.00 15.21           C  
ATOM    276  N   LYS A 256      33.535  65.051  19.095  1.00 21.40           N  
ATOM    277  CA  LYS A 256      32.229  65.608  19.450  1.00 26.50           C  
ATOM    278  C   LYS A 256      31.227  64.768  18.669  1.00 26.07           C  
ATOM    279  O   LYS A 256      31.602  64.132  17.682  1.00 17.61           O  
ATOM    280  CB  LYS A 256      32.088  67.052  18.956  1.00 16.32           C  
ATOM    281  CG  LYS A 256      33.043  68.064  19.543  1.00 23.53           C  
ATOM    282  CD  LYS A 256      32.670  69.387  18.950  1.00 30.86           C  
ATOM    283  CE  LYS A 256      33.627  70.477  19.339  1.00 40.07           C  
ATOM    284  NZ  LYS A 256      33.094  71.771  18.835  1.00 47.74           N  
ATOM    285  N   MET A 257      29.960  64.760  19.079  1.00 18.41           N  
ATOM    286  CA  MET A 257      28.980  63.996  18.311  1.00 26.93           C  
ATOM    287  C   MET A 257      28.616  64.829  17.074  1.00 25.99           C  
ATOM    288  O   MET A 257      28.895  66.023  17.031  1.00 22.96           O  
ATOM    289  CB  MET A 257      27.734  63.664  19.156  1.00 33.60           C  
ATOM    290  CG  MET A 257      26.826  64.811  19.524  1.00 35.90           C  
ATOM    291  SD  MET A 257      25.208  64.180  20.177  1.00 31.65           S  
ATOM    292  CE  MET A 257      24.271  64.056  18.664  1.00 44.53           C  
ATOM    293  N   GLY A 258      28.027  64.208  16.059  1.00 19.64           N  
ATOM    294  CA  GLY A 258      27.678  64.962  14.864  1.00 17.06           C  
ATOM    295  C   GLY A 258      28.866  65.408  14.018  1.00 23.84           C  
ATOM    296  O   GLY A 258      28.720  66.269  13.161  1.00 26.65           O  
ATOM    297  N   CYS A 259      30.049  64.850  14.246  1.00 24.61           N  
ATOM    298  CA  CYS A 259      31.214  65.244  13.445  1.00 23.53           C  
ATOM    299  C   CYS A 259      31.790  64.044  12.710  1.00 28.20           C  
ATOM    300  O   CYS A 259      31.855  62.940  13.264  1.00 21.73           O  
ATOM    301  CB  CYS A 259      32.309  65.881  14.327  1.00 27.38           C  
ATOM    302  SG  CYS A 259      31.788  67.466  15.079  1.00 31.60           S  
ATOM    303  N   LEU A 260      32.205  64.273  11.468  1.00 22.34           N  
ATOM    304  CA  LEU A 260      32.769  63.222  10.620  1.00 37.44           C  
ATOM    305  C   LEU A 260      34.186  62.885  11.026  1.00 25.36           C  
ATOM    306  O   LEU A 260      35.083  63.721  10.929  1.00 28.41           O  
ATOM    307  CB  LEU A 260      32.746  63.652   9.149  1.00 25.96           C  
ATOM    308  CG  LEU A 260      31.324  63.866   8.612  1.00 26.51           C  
ATOM    309  CD1 LEU A 260      31.375  64.572   7.260  1.00 34.20           C  
ATOM    310  CD2 LEU A 260      30.616  62.529   8.511  1.00 27.70           C  
ATOM    311  N   VAL A 261      34.383  61.668  11.518  1.00 28.36           N  
ATOM    312  CA  VAL A 261      35.714  61.240  11.917  1.00 15.48           C  
ATOM    313  C   VAL A 261      36.254  60.375  10.770  1.00 22.26           C  
ATOM    314  O   VAL A 261      35.677  59.348  10.430  1.00 18.86           O  
ATOM    315  CB  VAL A 261      35.700  60.398  13.206  1.00 24.75           C  
ATOM    316  CG1 VAL A 261      37.123  60.032  13.588  1.00 18.78           C  
ATOM    317  CG2 VAL A 261      35.013  61.156  14.336  1.00 16.00           C  
ATOM    318  N   PRO A 262      37.373  60.793  10.166  1.00 22.28           N  
ATOM    319  CA  PRO A 262      38.010  60.076   9.052  1.00 21.96           C  
ATOM    320  C   PRO A 262      38.797  58.847   9.520  1.00 21.79           C  
ATOM    321  O   PRO A 262      39.822  58.963  10.183  1.00 22.80           O  
ATOM    322  CB  PRO A 262      38.903  61.147   8.415  1.00 22.64           C  
ATOM    323  CG  PRO A 262      39.333  61.972   9.615  1.00 25.95           C  
ATOM    324  CD  PRO A 262      38.068  62.068  10.468  1.00 16.27           C  
ATOM    325  N   ILE A 263      38.289  57.672   9.180  1.00 19.92           N  
ATOM    326  CA  ILE A 263      38.918  56.410   9.568  1.00 24.15           C  
ATOM    327  C   ILE A 263      39.604  55.738   8.373  1.00 20.61           C  
ATOM    328  O   ILE A 263      39.143  55.830   7.223  1.00 21.12           O  
ATOM    329  CB  ILE A 263      37.876  55.376  10.100  1.00 18.65           C  
ATOM    330  CG1 ILE A 263      37.105  55.939  11.305  1.00 18.21           C  
ATOM    331  CG2 ILE A 263      38.584  54.022  10.431  1.00 13.39           C  
ATOM    332  CD1 ILE A 263      37.974  56.217  12.555  1.00 22.34           C  
ATOM    333  N   GLN A 264      40.716  55.080   8.650  1.00 17.10           N  
ATOM    334  CA  GLN A 264      41.402  54.319   7.610  1.00 23.77           C  
ATOM    335  C   GLN A 264      41.693  52.946   8.192  1.00 23.68           C  
ATOM    336  O   GLN A 264      42.363  52.847   9.215  1.00 19.71           O  
ATOM    337  CB  GLN A 264      42.730  54.964   7.224  1.00 18.91           C  
ATOM    338  CG  GLN A 264      42.586  56.357   6.641  1.00 32.34           C  
ATOM    339  CD  GLN A 264      43.804  56.755   5.835  1.00 38.45           C  
ATOM    340  OE1 GLN A 264      44.939  56.647   6.309  1.00 31.18           O  
ATOM    341  NE2 GLN A 264      43.576  57.212   4.606  1.00 31.72           N  
ATOM    342  N   VAL A 265      41.167  51.898   7.569  1.00 19.21           N  
ATOM    343  CA  VAL A 265      41.439  50.536   8.035  1.00 17.73           C  
ATOM    344  C   VAL A 265      42.419  49.910   7.027  1.00 25.53           C  
ATOM    345  O   VAL A 265      42.164  49.920   5.830  1.00 22.05           O  
ATOM    346  CB  VAL A 265      40.146  49.679   8.104  1.00 19.10           C  
ATOM    347  CG1 VAL A 265      40.494  48.226   8.536  1.00 19.10           C  
ATOM    348  CG2 VAL A 265      39.146  50.313   9.110  1.00 17.48           C  
ATOM    349  N   LYS A 266      43.539  49.381   7.510  1.00 18.35           N  
ATOM    350  CA  LYS A 266      44.525  48.792   6.613  1.00 21.13           C  
ATOM    351  C   LYS A 266      44.865  47.378   7.051  1.00 27.06           C  
ATOM    352  O   LYS A 266      44.764  47.041   8.237  1.00 20.24           O  
ATOM    353  CB  LYS A 266      45.808  49.647   6.600  1.00 19.11           C  
ATOM    354  CG  LYS A 266      45.638  51.046   5.988  1.00 25.57           C  
ATOM    355  CD  LYS A 266      46.907  51.868   6.193  1.00 25.81           C  
ATOM    356  CE  LYS A 266      46.857  53.218   5.460  1.00 27.16           C  
ATOM    357  NZ  LYS A 266      48.150  53.975   5.607  1.00 41.00           N  
ATOM    358  N   TRP A 267      45.255  46.541   6.098  1.00 19.97           N  
ATOM    359  CA  TRP A 267      45.636  45.180   6.439  1.00 22.24           C  
ATOM    360  C   TRP A 267      46.570  44.550   5.415  1.00 29.26           C  
ATOM    361  O   TRP A 267      46.702  45.034   4.295  1.00 24.79           O  
ATOM    362  CB  TRP A 267      44.393  44.282   6.609  1.00 16.72           C  
ATOM    363  CG  TRP A 267      43.485  44.194   5.400  1.00 25.63           C  
ATOM    364  CD1 TRP A 267      43.568  43.295   4.365  1.00 21.25           C  
ATOM    365  CD2 TRP A 267      42.400  45.076   5.074  1.00 19.54           C  
ATOM    366  NE1 TRP A 267      42.608  43.566   3.417  1.00 18.79           N  
ATOM    367  CE2 TRP A 267      41.879  44.655   3.823  1.00 21.14           C  
ATOM    368  CE3 TRP A 267      41.822  46.184   5.717  1.00 20.07           C  
ATOM    369  CZ2 TRP A 267      40.804  45.302   3.199  1.00 23.07           C  
ATOM    370  CZ3 TRP A 267      40.753  46.834   5.101  1.00 21.58           C  
ATOM    371  CH2 TRP A 267      40.252  46.388   3.847  1.00 21.43           C  
ATOM    372  N   LYS A 268      47.232  43.480   5.843  1.00 28.52           N  
ATOM    373  CA  LYS A 268      48.099  42.692   4.990  1.00 29.60           C  
ATOM    374  C   LYS A 268      47.615  41.247   5.159  1.00 34.72           C  
ATOM    375  O   LYS A 268      47.454  40.754   6.280  1.00 23.61           O  
ATOM    376  CB  LYS A 268      49.557  42.787   5.404  1.00 30.73           C  
ATOM    377  CG  LYS A 268      50.454  42.027   4.436  1.00 37.47           C  
ATOM    378  CD  LYS A 268      51.417  41.134   5.185  1.00 55.71           C  
ATOM    379  CE  LYS A 268      52.062  40.110   4.256  1.00 59.44           C  
ATOM    380  NZ  LYS A 268      52.996  39.221   5.006  1.00 74.38           N  
ATOM    381  N   LEU A 269      47.367  40.582   4.041  1.00 31.10           N  
ATOM    382  CA  LEU A 269      46.873  39.215   4.071  1.00 48.23           C  
ATOM    383  C   LEU A 269      47.921  38.166   3.784  1.00 52.26           C  
ATOM    384  O   LEU A 269      48.955  38.441   3.185  1.00 42.21           O  
ATOM    385  CB  LEU A 269      45.740  39.052   3.069  1.00 51.23           C  
ATOM    386  CG  LEU A 269      44.450  39.771   3.453  1.00 52.53           C  
ATOM    387  CD1 LEU A 269      43.438  39.642   2.328  1.00 49.27           C  
ATOM    388  CD2 LEU A 269      43.919  39.180   4.747  1.00 39.63           C  
ATOM    389  N   ASP A 270      47.638  36.949   4.224  1.00 62.54           N  
ATOM    390  CA  ASP A 270      48.541  35.845   3.994  1.00 65.16           C  
ATOM    391  C   ASP A 270      48.292  35.277   2.607  1.00 63.05           C  
ATOM    392  O   ASP A 270      47.567  35.854   1.789  1.00 53.86           O  
ATOM    393  CB  ASP A 270      48.350  34.763   5.061  1.00 78.46           C  
ATOM    394  CG  ASP A 270      46.889  34.480   5.351  1.00 87.73           C  
ATOM    395  OD1 ASP A 270      46.219  35.339   5.970  1.00 93.01           O  
ATOM    396  OD2 ASP A 270      46.407  33.401   4.953  1.00 97.70           O  
ATOM    397  N   LYS A 271      48.890  34.125   2.360  1.00 67.80           N  
ATOM    398  CA  LYS A 271      48.802  33.463   1.074  1.00 68.68           C  
ATOM    399  C   LYS A 271      47.403  32.988   0.686  1.00 61.19           C  
ATOM    400  O   LYS A 271      46.894  33.329  -0.385  1.00 43.46           O  
ATOM    401  CB  LYS A 271      49.789  32.290   1.061  1.00 74.51           C  
ATOM    402  CG  LYS A 271      51.236  32.695   1.387  1.00 85.60           C  
ATOM    403  CD  LYS A 271      51.368  33.303   2.793  1.00 88.06           C  
ATOM    404  CE  LYS A 271      52.683  34.053   2.985  1.00 90.72           C  
ATOM    405  NZ  LYS A 271      52.732  34.789   4.287  1.00 87.93           N  
ATOM    406  N   ARG A 272      46.772  32.215   1.560  1.00 63.00           N  
ATOM    407  CA  ARG A 272      45.454  31.681   1.250  1.00 66.82           C  
ATOM    408  C   ARG A 272      44.331  32.688   1.005  1.00 68.30           C  
ATOM    409  O   ARG A 272      43.289  32.326   0.455  1.00 63.26           O  
ATOM    410  CB  ARG A 272      45.027  30.695   2.335  1.00 70.59           C  
ATOM    411  CG  ARG A 272      44.996  31.261   3.732  1.00 75.27           C  
ATOM    412  CD  ARG A 272      44.305  30.284   4.658  1.00 74.41           C  
ATOM    413  NE  ARG A 272      43.020  29.887   4.094  1.00 80.78           N  
ATOM    414  CZ  ARG A 272      42.120  29.137   4.721  1.00 81.99           C  
ATOM    415  NH1 ARG A 272      42.360  28.692   5.949  1.00 79.98           N  
ATOM    416  NH2 ARG A 272      40.976  28.838   4.117  1.00 74.19           N  
ATOM    417  N   HIS A 273      44.529  33.945   1.387  1.00 59.68           N  
ATOM    418  CA  HIS A 273      43.477  34.937   1.190  1.00 55.59           C  
ATOM    419  C   HIS A 273      43.754  35.913   0.053  1.00 57.17           C  
ATOM    420  O   HIS A 273      42.866  36.664  -0.371  1.00 47.02           O  
ATOM    421  CB  HIS A 273      43.240  35.701   2.494  1.00 46.34           C  
ATOM    422  CG  HIS A 273      42.901  34.814   3.649  1.00 44.10           C  
ATOM    423  ND1 HIS A 273      41.735  34.080   3.706  1.00 41.42           N  
ATOM    424  CD2 HIS A 273      43.598  34.501   4.768  1.00 44.93           C  
ATOM    425  CE1 HIS A 273      41.729  33.352   4.808  1.00 48.63           C  
ATOM    426  NE2 HIS A 273      42.849  33.589   5.470  1.00 47.67           N  
ATOM    427  N   PHE A 274      44.976  35.877  -0.464  1.00 55.19           N  
ATOM    428  CA  PHE A 274      45.363  36.783  -1.533  1.00 54.93           C  
ATOM    429  C   PHE A 274      44.294  37.074  -2.587  1.00 50.57           C  
ATOM    430  O   PHE A 274      44.143  38.214  -3.015  1.00 47.59           O  
ATOM    431  CB  PHE A 274      46.621  36.282  -2.234  1.00 56.56           C  
ATOM    432  CG  PHE A 274      47.205  37.284  -3.182  1.00 62.75           C  
ATOM    433  CD1 PHE A 274      47.928  38.374  -2.698  1.00 58.97           C  
ATOM    434  CD2 PHE A 274      46.993  37.167  -4.558  1.00 58.84           C  
ATOM    435  CE1 PHE A 274      48.431  39.333  -3.570  1.00 60.94           C  
ATOM    436  CE2 PHE A 274      47.491  38.120  -5.441  1.00 53.96           C  
ATOM    437  CZ  PHE A 274      48.212  39.206  -4.946  1.00 64.02           C  
ATOM    438  N   ASN A 275      43.547  36.062  -3.014  1.00 54.34           N  
ATOM    439  CA  ASN A 275      42.524  36.297  -4.033  1.00 52.80           C  
ATOM    440  C   ASN A 275      41.098  36.208  -3.495  1.00 51.52           C  
ATOM    441  O   ASN A 275      40.136  36.110  -4.258  1.00 50.49           O  
ATOM    442  CB  ASN A 275      42.698  35.306  -5.188  1.00 66.64           C  
ATOM    443  CG  ASN A 275      44.053  35.433  -5.867  1.00 71.02           C  
ATOM    444  OD1 ASN A 275      44.383  36.477  -6.435  1.00 68.64           O  
ATOM    445  ND2 ASN A 275      44.850  34.366  -5.805  1.00 74.47           N  
ATOM    446  N   SER A 276      40.962  36.268  -2.177  1.00 44.86           N  
ATOM    447  CA  SER A 276      39.649  36.173  -1.558  1.00 37.97           C  
ATOM    448  C   SER A 276      38.787  37.418  -1.671  1.00 26.58           C  
ATOM    449  O   SER A 276      39.273  38.545  -1.690  1.00 30.71           O  
ATOM    450  CB  SER A 276      39.806  35.829  -0.084  1.00 34.62           C  
ATOM    451  OG  SER A 276      40.597  34.674   0.075  1.00 57.34           O  
ATOM    452  N   ASN A 277      37.487  37.204  -1.766  1.00 32.62           N  
ATOM    453  CA  ASN A 277      36.577  38.315  -1.793  1.00 36.99           C  
ATOM    454  C   ASN A 277      36.344  38.518  -0.299  1.00 39.73           C  
ATOM    455  O   ASN A 277      35.965  37.588   0.391  1.00 49.52           O  
ATOM    456  CB  ASN A 277      35.287  37.927  -2.479  1.00 41.80           C  
ATOM    457  CG  ASN A 277      34.614  39.103  -3.106  1.00 55.70           C  
ATOM    458  OD1 ASN A 277      34.396  40.122  -2.453  1.00 50.83           O  
ATOM    459  ND2 ASN A 277      34.290  38.985  -4.390  1.00 65.82           N  
ATOM    460  N   LEU A 278      36.576  39.718   0.204  1.00 32.41           N  
ATOM    461  CA  LEU A 278      36.412  39.961   1.632  1.00 36.36           C  
ATOM    462  C   LEU A 278      35.377  41.011   1.968  1.00 30.60           C  
ATOM    463  O   LEU A 278      34.933  41.763   1.103  1.00 24.85           O  
ATOM    464  CB  LEU A 278      37.752  40.376   2.239  1.00 26.74           C  
ATOM    465  CG  LEU A 278      38.923  39.395   2.065  1.00 31.32           C  
ATOM    466  CD1 LEU A 278      40.110  39.814   2.900  1.00 33.72           C  
ATOM    467  CD2 LEU A 278      38.479  38.017   2.494  1.00 43.70           C  
ATOM    468  N   SER A 279      34.974  41.027   3.234  1.00 26.56           N  
ATOM    469  CA  SER A 279      34.036  42.023   3.732  1.00 28.46           C  
ATOM    470  C   SER A 279      34.578  42.550   5.069  1.00 26.79           C  
ATOM    471  O   SER A 279      35.352  41.876   5.762  1.00 24.79           O  
ATOM    472  CB  SER A 279      32.629  41.434   3.903  1.00 18.43           C  
ATOM    473  OG  SER A 279      32.630  40.326   4.769  1.00 25.37           O  
ATOM    474  N   LEU A 280      34.212  43.776   5.410  1.00 23.01           N  
ATOM    475  CA  LEU A 280      34.670  44.363   6.658  1.00 20.06           C  
ATOM    476  C   LEU A 280      33.459  44.743   7.514  1.00 27.22           C  
ATOM    477  O   LEU A 280      32.584  45.481   7.069  1.00 24.13           O  
ATOM    478  CB  LEU A 280      35.507  45.612   6.395  1.00 19.45           C  
ATOM    479  CG  LEU A 280      36.166  46.204   7.658  1.00 16.14           C  
ATOM    480  CD1 LEU A 280      37.421  45.404   8.032  1.00 13.66           C  
ATOM    481  CD2 LEU A 280      36.540  47.641   7.393  1.00 27.73           C  
ATOM    482  N   ARG A 281      33.405  44.224   8.732  1.00 17.17           N  
ATOM    483  CA  ARG A 281      32.308  44.547   9.632  1.00 25.98           C  
ATOM    484  C   ARG A 281      32.787  45.616  10.610  1.00 19.37           C  
ATOM    485  O   ARG A 281      33.918  45.562  11.104  1.00 18.62           O  
ATOM    486  CB  ARG A 281      31.836  43.296  10.390  1.00 19.72           C  
ATOM    487  CG  ARG A 281      30.929  42.379   9.570  1.00 18.53           C  
ATOM    488  CD  ARG A 281      30.501  41.113  10.366  1.00 20.71           C  
ATOM    489  NE  ARG A 281      31.625  40.215  10.669  1.00 23.31           N  
ATOM    490  CZ  ARG A 281      32.128  40.010  11.886  1.00 20.32           C  
ATOM    491  NH1 ARG A 281      31.625  40.647  12.937  1.00 19.71           N  
ATOM    492  NH2 ARG A 281      33.107  39.130  12.069  1.00 18.85           N  
ATOM    493  N   ILE A 282      31.921  46.584  10.883  1.00 18.92           N  
ATOM    494  CA  ILE A 282      32.236  47.688  11.787  1.00 19.64           C  
ATOM    495  C   ILE A 282      31.193  47.716  12.913  1.00 18.60           C  
ATOM    496  O   ILE A 282      29.998  47.785  12.650  1.00 17.59           O  
ATOM    497  CB  ILE A 282      32.184  49.039  11.048  1.00 16.88           C  
ATOM    498  CG1 ILE A 282      33.138  49.014   9.849  1.00 23.18           C  
ATOM    499  CG2 ILE A 282      32.556  50.174  12.017  1.00 14.78           C  
ATOM    500  CD1 ILE A 282      32.804  50.053   8.792  1.00 35.11           C  
ATOM    501  N   ARG A 283      31.663  47.661  14.152  1.00 16.00           N  
ATOM    502  CA  ARG A 283      30.794  47.670  15.321  1.00 20.71           C  
ATOM    503  C   ARG A 283      31.223  48.737  16.317  1.00 22.86           C  
ATOM    504  O   ARG A 283      32.374  49.185  16.327  1.00 19.17           O  
ATOM    505  CB  ARG A 283      30.839  46.316  16.039  1.00 19.51           C  
ATOM    506  CG  ARG A 283      30.213  45.123  15.281  1.00 12.93           C  
ATOM    507  CD  ARG A 283      29.988  43.959  16.291  1.00 20.20           C  
ATOM    508  NE  ARG A 283      28.949  44.317  17.252  1.00 25.46           N  
ATOM    509  CZ  ARG A 283      28.729  43.703  18.407  1.00 26.71           C  
ATOM    510  NH1 ARG A 283      27.744  44.125  19.191  1.00 24.07           N  
ATOM    511  NH2 ARG A 283      29.497  42.683  18.791  1.00 18.37           N  
ATOM    512  N   PHE A 284      30.285  49.137  17.163  1.00 17.73           N  
ATOM    513  CA  PHE A 284      30.581  50.113  18.185  1.00 15.97           C  
ATOM    514  C   PHE A 284      29.925  49.552  19.444  1.00 21.02           C  
ATOM    515  O   PHE A 284      28.692  49.575  19.614  1.00 19.21           O  
ATOM    516  CB  PHE A 284      30.053  51.496  17.797  1.00 14.95           C  
ATOM    517  CG  PHE A 284      30.532  52.598  18.714  1.00 17.54           C  
ATOM    518  CD1 PHE A 284      31.905  52.820  18.893  1.00 21.60           C  
ATOM    519  CD2 PHE A 284      29.616  53.407  19.400  1.00 13.88           C  
ATOM    520  CE1 PHE A 284      32.372  53.827  19.737  1.00 14.56           C  
ATOM    521  CE2 PHE A 284      30.060  54.428  20.255  1.00 20.02           C  
ATOM    522  CZ  PHE A 284      31.444  54.644  20.427  1.00 19.28           C  
ATOM    523  N   VAL A 285      30.782  49.033  20.317  1.00 17.15           N  
ATOM    524  CA  VAL A 285      30.356  48.358  21.537  1.00 19.37           C  
ATOM    525  C   VAL A 285      30.905  48.944  22.835  1.00 20.46           C  
ATOM    526  O   VAL A 285      31.778  49.825  22.829  1.00 21.35           O  
ATOM    527  CB  VAL A 285      30.788  46.865  21.480  1.00 21.52           C  
ATOM    528  CG1 VAL A 285      30.406  46.277  20.124  1.00 18.29           C  
ATOM    529  CG2 VAL A 285      32.312  46.724  21.711  1.00 17.81           C  
ATOM    530  N   LYS A 286      30.385  48.442  23.951  1.00 21.97           N  
ATOM    531  CA  LYS A 286      30.840  48.880  25.267  1.00 21.88           C  
ATOM    532  C   LYS A 286      31.325  47.672  26.048  1.00 26.21           C  
ATOM    533  O   LYS A 286      30.874  46.554  25.817  1.00 29.83           O  
ATOM    534  CB  LYS A 286      29.716  49.591  26.038  1.00 22.99           C  
ATOM    535  CG  LYS A 286      28.548  48.719  26.445  1.00 34.20           C  
ATOM    536  CD  LYS A 286      27.421  49.589  26.993  1.00 47.13           C  
ATOM    537  CE  LYS A 286      26.199  48.775  27.383  1.00 34.77           C  
ATOM    538  NZ  LYS A 286      25.655  47.987  26.246  1.00 53.70           N  
ATOM    539  N   TYR A 287      32.249  47.901  26.970  1.00 24.67           N  
ATOM    540  CA  TYR A 287      32.789  46.820  27.763  1.00 29.71           C  
ATOM    541  C   TYR A 287      33.318  47.409  29.062  1.00 35.07           C  
ATOM    542  O   TYR A 287      33.392  48.628  29.218  1.00 30.77           O  
ATOM    543  CB  TYR A 287      33.915  46.122  26.986  1.00 23.60           C  
ATOM    544  CG  TYR A 287      35.196  46.925  26.815  1.00 28.29           C  
ATOM    545  CD1 TYR A 287      36.137  47.018  27.850  1.00 39.89           C  
ATOM    546  CD2 TYR A 287      35.460  47.608  25.628  1.00 30.52           C  
ATOM    547  CE1 TYR A 287      37.313  47.780  27.706  1.00 28.80           C  
ATOM    548  CE2 TYR A 287      36.625  48.372  25.469  1.00 27.17           C  
ATOM    549  CZ  TYR A 287      37.550  48.456  26.510  1.00 32.96           C  
ATOM    550  OH  TYR A 287      38.702  49.216  26.355  1.00 24.00           O  
ATOM    551  N   ASP A 288      33.672  46.550  30.005  1.00 47.11           N  
ATOM    552  CA  ASP A 288      34.217  47.031  31.267  1.00 57.56           C  
ATOM    553  C   ASP A 288      35.186  45.998  31.807  1.00 61.95           C  
ATOM    554  O   ASP A 288      35.644  45.121  31.071  1.00 64.91           O  
ATOM    555  CB  ASP A 288      33.091  47.304  32.267  1.00 54.31           C  
ATOM    556  CG  ASP A 288      32.439  46.035  32.783  1.00 71.23           C  
ATOM    557  OD1 ASP A 288      32.096  45.152  31.967  1.00 65.14           O  
ATOM    558  OD2 ASP A 288      32.262  45.924  34.017  1.00 77.38           O  
ATOM    559  N   LYS A 289      35.498  46.097  33.092  1.00 76.53           N  
ATOM    560  CA  LYS A 289      36.427  45.167  33.722  1.00 77.02           C  
ATOM    561  C   LYS A 289      35.849  43.758  33.797  1.00 79.48           C  
ATOM    562  O   LYS A 289      36.586  42.776  33.746  1.00 81.02           O  
ATOM    563  CB  LYS A 289      36.781  45.653  35.130  1.00 81.42           C  
ATOM    564  CG  LYS A 289      37.327  47.083  35.183  1.00 88.60           C  
ATOM    565  CD  LYS A 289      36.289  48.110  34.730  1.00 84.07           C  
ATOM    566  CE  LYS A 289      36.867  49.511  34.689  1.00 88.06           C  
ATOM    567  NZ  LYS A 289      35.890  50.479  34.112  1.00 92.21           N  
ATOM    568  N   LYS A 290      34.528  43.664  33.900  1.00 79.76           N  
ATOM    569  CA  LYS A 290      33.854  42.375  34.002  1.00 80.34           C  
ATOM    570  C   LYS A 290      33.712  41.612  32.680  1.00 85.30           C  
ATOM    571  O   LYS A 290      33.633  40.381  32.672  1.00 88.17           O  
ATOM    572  CB  LYS A 290      32.482  42.567  34.660  1.00 84.86           C  
ATOM    573  CG  LYS A 290      32.559  43.185  36.057  1.00 85.91           C  
ATOM    574  CD  LYS A 290      33.444  42.351  36.980  1.00 88.52           C  
ATOM    575  CE  LYS A 290      33.630  43.015  38.335  1.00 86.30           C  
ATOM    576  NZ  LYS A 290      34.461  42.179  39.246  1.00 83.57           N  
ATOM    577  N   GLU A 291      33.673  42.334  31.565  1.00 80.10           N  
ATOM    578  CA  GLU A 291      33.567  41.692  30.256  1.00 76.62           C  
ATOM    579  C   GLU A 291      34.595  42.340  29.342  1.00 69.96           C  
ATOM    580  O   GLU A 291      34.343  43.403  28.775  1.00 72.75           O  
ATOM    581  CB  GLU A 291      32.155  41.860  29.680  1.00 70.33           C  
ATOM    582  CG  GLU A 291      31.999  41.373  28.245  1.00 70.04           C  
ATOM    583  CD  GLU A 291      30.554  41.401  27.758  1.00 71.17           C  
ATOM    584  OE1 GLU A 291      30.323  41.845  26.609  1.00 27.91           O  
ATOM    585  OE2 GLU A 291      29.652  40.972  28.516  1.00 68.77           O  
ATOM    586  N   ASN A 292      35.751  41.690  29.214  1.00 58.98           N  
ATOM    587  CA  ASN A 292      36.856  42.190  28.405  1.00 38.87           C  
ATOM    588  C   ASN A 292      36.586  42.460  26.930  1.00 39.42           C  
ATOM    589  O   ASN A 292      35.613  41.978  26.338  1.00 27.86           O  
ATOM    590  CB  ASN A 292      38.069  41.278  28.561  1.00 57.42           C  
ATOM    591  CG  ASN A 292      38.663  41.364  29.947  1.00 70.65           C  
ATOM    592  OD1 ASN A 292      39.703  40.773  30.235  1.00 78.44           O  
ATOM    593  ND2 ASN A 292      37.998  42.111  30.822  1.00 69.72           N  
ATOM    594  N   VAL A 293      37.483  43.237  26.337  1.00 26.35           N  
ATOM    595  CA  VAL A 293      37.308  43.650  24.966  1.00 34.04           C  
ATOM    596  C   VAL A 293      37.128  42.528  23.948  1.00 17.94           C  
ATOM    597  O   VAL A 293      36.205  42.590  23.145  1.00 25.00           O  
ATOM    598  CB  VAL A 293      38.460  44.607  24.532  1.00 23.12           C  
ATOM    599  CG1 VAL A 293      39.777  43.853  24.473  1.00 30.72           C  
ATOM    600  CG2 VAL A 293      38.131  45.245  23.181  1.00 26.65           C  
ATOM    601  N   GLU A 294      37.983  41.501  23.988  1.00 22.81           N  
ATOM    602  CA  GLU A 294      37.886  40.428  23.002  1.00 21.18           C  
ATOM    603  C   GLU A 294      36.515  39.774  23.060  1.00 25.66           C  
ATOM    604  O   GLU A 294      35.933  39.433  22.024  1.00 18.64           O  
ATOM    605  CB  GLU A 294      39.027  39.402  23.181  1.00 14.28           C  
ATOM    606  CG  GLU A 294      40.416  39.939  22.799  1.00 21.70           C  
ATOM    607  CD  GLU A 294      40.607  40.123  21.282  1.00 32.88           C  
ATOM    608  OE1 GLU A 294      40.103  39.281  20.512  1.00 21.52           O  
ATOM    609  OE2 GLU A 294      41.279  41.091  20.859  1.00 22.01           O  
ATOM    610  N   TYR A 295      35.957  39.632  24.257  1.00 19.51           N  
ATOM    611  CA  TYR A 295      34.622  39.059  24.327  1.00 21.16           C  
ATOM    612  C   TYR A 295      33.577  40.069  23.828  1.00 19.50           C  
ATOM    613  O   TYR A 295      32.737  39.761  22.978  1.00 19.03           O  
ATOM    614  CB  TYR A 295      34.281  38.632  25.769  1.00 20.14           C  
ATOM    615  CG  TYR A 295      32.982  37.884  25.869  1.00 20.29           C  
ATOM    616  CD1 TYR A 295      31.783  38.551  26.124  1.00 25.63           C  
ATOM    617  CD2 TYR A 295      32.937  36.498  25.650  1.00 25.70           C  
ATOM    618  CE1 TYR A 295      30.561  37.854  26.157  1.00 21.54           C  
ATOM    619  CE2 TYR A 295      31.732  35.800  25.676  1.00 28.45           C  
ATOM    620  CZ  TYR A 295      30.550  36.484  25.928  1.00 29.09           C  
ATOM    621  OH  TYR A 295      29.362  35.795  25.924  1.00 26.69           O  
ATOM    622  N   ALA A 296      33.626  41.280  24.367  1.00 19.26           N  
ATOM    623  CA  ALA A 296      32.632  42.296  24.023  1.00 21.52           C  
ATOM    624  C   ALA A 296      32.471  42.582  22.534  1.00 21.51           C  
ATOM    625  O   ALA A 296      31.348  42.674  22.029  1.00 18.55           O  
ATOM    626  CB  ALA A 296      32.945  43.604  24.766  1.00 20.98           C  
ATOM    627  N   ILE A 297      33.583  42.698  21.817  1.00 15.18           N  
ATOM    628  CA  ILE A 297      33.478  43.028  20.402  1.00 15.91           C  
ATOM    629  C   ILE A 297      32.824  41.969  19.547  1.00 22.17           C  
ATOM    630  O   ILE A 297      32.400  42.259  18.430  1.00 20.31           O  
ATOM    631  CB  ILE A 297      34.853  43.399  19.818  1.00 18.98           C  
ATOM    632  CG1 ILE A 297      35.793  42.194  19.884  1.00 15.52           C  
ATOM    633  CG2 ILE A 297      35.406  44.642  20.567  1.00 18.88           C  
ATOM    634  CD1 ILE A 297      37.179  42.487  19.304  1.00 18.89           C  
ATOM    635  N   ARG A 298      32.732  40.743  20.064  1.00 18.46           N  
ATOM    636  CA  ARG A 298      32.097  39.678  19.304  1.00 21.33           C  
ATOM    637  C   ARG A 298      30.745  39.246  19.922  1.00 17.80           C  
ATOM    638  O   ARG A 298      30.093  38.331  19.442  1.00 24.44           O  
ATOM    639  CB  ARG A 298      33.060  38.489  19.181  1.00 20.23           C  
ATOM    640  CG  ARG A 298      34.341  38.792  18.368  1.00 15.27           C  
ATOM    641  CD  ARG A 298      35.284  37.576  18.308  1.00 18.11           C  
ATOM    642  NE  ARG A 298      36.549  37.938  17.659  1.00 20.28           N  
ATOM    643  CZ  ARG A 298      37.612  38.390  18.315  1.00 20.59           C  
ATOM    644  NH1 ARG A 298      37.568  38.514  19.636  1.00 20.83           N  
ATOM    645  NH2 ARG A 298      38.700  38.784  17.655  1.00 17.91           N  
ATOM    646  N   ASN A 299      30.341  39.926  20.985  1.00 19.89           N  
ATOM    647  CA  ASN A 299      29.071  39.654  21.677  1.00 19.35           C  
ATOM    648  C   ASN A 299      27.973  40.467  20.994  1.00 19.59           C  
ATOM    649  O   ASN A 299      28.005  41.694  21.014  1.00 21.97           O  
ATOM    650  CB  ASN A 299      29.217  40.072  23.143  1.00 24.23           C  
ATOM    651  CG  ASN A 299      27.905  40.016  23.913  1.00 27.02           C  
ATOM    652  OD1 ASN A 299      26.918  39.509  23.426  1.00 19.10           O  
ATOM    653  ND2 ASN A 299      27.909  40.547  25.127  1.00 24.29           N  
ATOM    654  N   PRO A 300      26.964  39.800  20.402  1.00 17.87           N  
ATOM    655  CA  PRO A 300      25.914  40.579  19.738  1.00 21.70           C  
ATOM    656  C   PRO A 300      25.081  41.481  20.640  1.00 28.52           C  
ATOM    657  O   PRO A 300      24.346  42.337  20.151  1.00 23.07           O  
ATOM    658  CB  PRO A 300      25.078  39.509  19.037  1.00 24.38           C  
ATOM    659  CG  PRO A 300      25.226  38.324  19.920  1.00 28.95           C  
ATOM    660  CD  PRO A 300      26.692  38.355  20.318  1.00 26.83           C  
ATOM    661  N   ARG A 301      25.218  41.317  21.951  1.00 16.22           N  
ATOM    662  CA  ARG A 301      24.438  42.128  22.883  1.00 28.05           C  
ATOM    663  C   ARG A 301      25.203  43.307  23.482  1.00 28.78           C  
ATOM    664  O   ARG A 301      24.691  43.988  24.364  1.00 24.83           O  
ATOM    665  CB  ARG A 301      23.925  41.241  24.032  1.00 29.49           C  
ATOM    666  CG  ARG A 301      22.870  40.196  23.623  1.00 37.31           C  
ATOM    667  CD  ARG A 301      22.729  39.121  24.705  1.00 53.95           C  
ATOM    668  NE  ARG A 301      24.021  38.508  25.035  1.00 70.66           N  
ATOM    669  CZ  ARG A 301      24.703  37.689  24.231  1.00 77.08           C  
ATOM    670  NH1 ARG A 301      24.220  37.362  23.035  1.00 76.83           N  
ATOM    671  NH2 ARG A 301      25.881  37.208  24.613  1.00 62.83           N  
ATOM    672  N   SER A 302      26.412  43.579  23.008  1.00 24.83           N  
ATOM    673  CA  SER A 302      27.187  44.659  23.624  1.00 25.20           C  
ATOM    674  C   SER A 302      27.130  46.037  22.971  1.00 13.90           C  
ATOM    675  O   SER A 302      27.930  46.908  23.306  1.00 21.58           O  
ATOM    676  CB  SER A 302      28.650  44.229  23.732  1.00 24.11           C  
ATOM    677  OG  SER A 302      29.202  44.142  22.430  1.00 22.83           O  
ATOM    678  N   ASP A 303      26.210  46.259  22.043  1.00 18.21           N  
ATOM    679  CA  ASP A 303      26.166  47.572  21.402  1.00 22.90           C  
ATOM    680  C   ASP A 303      26.044  48.745  22.352  1.00 31.52           C  
ATOM    681  O   ASP A 303      25.427  48.633  23.417  1.00 22.10           O  
ATOM    682  CB  ASP A 303      24.991  47.676  20.435  1.00 18.04           C  
ATOM    683  CG  ASP A 303      25.143  46.784  19.243  1.00 18.03           C  
ATOM    684  OD1 ASP A 303      26.269  46.298  19.008  1.00 22.41           O  
ATOM    685  OD2 ASP A 303      24.142  46.576  18.542  1.00 27.74           O  
ATOM    686  N   VAL A 304      26.630  49.878  21.960  1.00 21.29           N  
ATOM    687  CA  VAL A 304      26.465  51.101  22.736  1.00 27.37           C  
ATOM    688  C   VAL A 304      25.069  51.498  22.259  1.00 33.30           C  
ATOM    689  O   VAL A 304      24.813  51.503  21.047  1.00 21.95           O  
ATOM    690  CB  VAL A 304      27.447  52.198  22.325  1.00 28.84           C  
ATOM    691  CG1 VAL A 304      27.151  53.468  23.113  1.00 18.11           C  
ATOM    692  CG2 VAL A 304      28.861  51.733  22.572  1.00 20.80           C  
ATOM    693  N   MET A 305      24.171  51.804  23.193  1.00 23.79           N  
ATOM    694  CA  MET A 305      22.785  52.123  22.849  1.00 23.83           C  
ATOM    695  C   MET A 305      22.498  53.608  22.794  1.00 26.09           C  
ATOM    696  O   MET A 305      22.815  54.351  23.719  1.00 22.49           O  
ATOM    697  CB  MET A 305      21.835  51.478  23.860  1.00 29.10           C  
ATOM    698  CG  MET A 305      22.025  49.977  24.036  1.00 44.03           C  
ATOM    699  SD  MET A 305      21.876  49.066  22.477  1.00 33.74           S  
ATOM    700  CE  MET A 305      20.138  49.263  22.087  1.00 35.02           C  
ATOM    701  N   LYS A 306      21.868  54.017  21.706  1.00 16.95           N  
ATOM    702  CA  LYS A 306      21.512  55.414  21.470  1.00 22.70           C  
ATOM    703  C   LYS A 306      20.438  55.819  22.494  1.00 33.28           C  
ATOM    704  O   LYS A 306      19.583  55.006  22.821  1.00 21.52           O  
ATOM    705  CB  LYS A 306      20.965  55.505  20.053  1.00 27.44           C  
ATOM    706  CG  LYS A 306      21.003  56.863  19.423  1.00 27.01           C  
ATOM    707  CD  LYS A 306      20.542  56.730  17.991  1.00 29.48           C  
ATOM    708  CE  LYS A 306      20.664  58.011  17.238  1.00 28.99           C  
ATOM    709  NZ  LYS A 306      20.465  57.676  15.805  1.00 36.80           N  
ATOM    710  N   CYS A 307      20.470  57.046  23.012  1.00 26.58           N  
ATOM    711  CA  CYS A 307      19.440  57.435  23.975  1.00 27.49           C  
ATOM    712  C   CYS A 307      18.105  57.661  23.277  1.00 29.15           C  
ATOM    713  O   CYS A 307      18.027  57.784  22.042  1.00 19.41           O  
ATOM    714  CB  CYS A 307      19.832  58.692  24.764  1.00 21.44           C  
ATOM    715  SG  CYS A 307      19.725  60.241  23.847  1.00 24.39           S  
ATOM    716  N   ARG A 308      17.053  57.727  24.081  1.00 24.42           N  
ATOM    717  CA  ARG A 308      15.706  57.889  23.564  1.00 28.20           C  
ATOM    718  C   ARG A 308      15.555  59.141  22.737  1.00 31.58           C  
ATOM    719  O   ARG A 308      15.040  59.077  21.623  1.00 33.89           O  
ATOM    720  CB  ARG A 308      14.698  57.914  24.725  1.00 29.31           C  
ATOM    721  CG  ARG A 308      13.226  57.827  24.323  1.00 31.30           C  
ATOM    722  CD  ARG A 308      12.331  58.380  25.457  1.00 39.89           C  
ATOM    723  NE  ARG A 308      12.444  59.840  25.504  1.00 34.86           N  
ATOM    724  CZ  ARG A 308      12.016  60.650  24.535  1.00 36.75           C  
ATOM    725  NH1 ARG A 308      11.432  60.138  23.459  1.00 41.06           N  
ATOM    726  NH2 ARG A 308      12.216  61.966  24.608  1.00 27.48           N  
ATOM    727  N   SER A 309      16.021  60.283  23.251  1.00 25.98           N  
ATOM    728  CA  SER A 309      15.854  61.530  22.509  1.00 29.83           C  
ATOM    729  C   SER A 309      16.644  61.636  21.216  1.00 37.45           C  
ATOM    730  O   SER A 309      16.185  62.272  20.263  1.00 28.36           O  
ATOM    731  CB  SER A 309      16.167  62.745  23.387  1.00 33.46           C  
ATOM    732  OG  SER A 309      17.539  62.806  23.689  1.00 46.93           O  
ATOM    733  N   HIS A 310      17.837  61.049  21.160  1.00 31.09           N  
ATOM    734  CA  HIS A 310      18.576  61.140  19.904  1.00 36.98           C  
ATOM    735  C   HIS A 310      17.992  60.138  18.916  1.00 22.35           C  
ATOM    736  O   HIS A 310      18.027  60.358  17.707  1.00 43.54           O  
ATOM    737  CB  HIS A 310      20.074  60.910  20.125  1.00 28.26           C  
ATOM    738  CG  HIS A 310      20.796  62.130  20.596  1.00 26.35           C  
ATOM    739  ND1 HIS A 310      21.605  62.137  21.712  1.00 19.83           N  
ATOM    740  CD2 HIS A 310      20.798  63.400  20.122  1.00 27.26           C  
ATOM    741  CE1 HIS A 310      22.073  63.359  21.911  1.00 26.74           C  
ATOM    742  NE2 HIS A 310      21.598  64.143  20.959  1.00 31.17           N  
ATOM    743  N   THR A 311      17.433  59.052  19.434  1.00 33.48           N  
ATOM    744  CA  THR A 311      16.823  58.049  18.572  1.00 40.32           C  
ATOM    745  C   THR A 311      15.658  58.672  17.798  1.00 51.27           C  
ATOM    746  O   THR A 311      15.668  58.721  16.566  1.00 48.17           O  
ATOM    747  CB  THR A 311      16.270  56.861  19.375  1.00 37.19           C  
ATOM    748  OG1 THR A 311      17.346  56.059  19.869  1.00 41.52           O  
ATOM    749  CG2 THR A 311      15.373  55.999  18.494  1.00 48.79           C  
ATOM    750  N   GLU A 312      14.667  59.184  18.520  1.00 54.74           N  
ATOM    751  CA  GLU A 312      13.499  59.758  17.855  1.00 63.54           C  
ATOM    752  C   GLU A 312      13.791  61.037  17.069  1.00 57.11           C  
ATOM    753  O   GLU A 312      13.051  61.395  16.158  1.00 65.77           O  
ATOM    754  CB  GLU A 312      12.359  59.983  18.868  1.00 66.33           C  
ATOM    755  CG  GLU A 312      12.423  61.268  19.673  1.00 58.42           C  
ATOM    756  CD  GLU A 312      11.162  61.489  20.506  1.00 65.11           C  
ATOM    757  OE1 GLU A 312      10.995  62.606  21.040  1.00 57.94           O  
ATOM    758  OE2 GLU A 312      10.345  60.546  20.632  1.00 47.07           O  
ATOM    759  N   ARG A 313      14.874  61.717  17.410  1.00 52.52           N  
ATOM    760  CA  ARG A 313      15.262  62.937  16.713  1.00 52.55           C  
ATOM    761  C   ARG A 313      16.145  62.621  15.484  1.00 63.71           C  
ATOM    762  O   ARG A 313      16.516  63.520  14.724  1.00 62.49           O  
ATOM    763  CB  ARG A 313      16.008  63.851  17.694  1.00 64.05           C  
ATOM    764  CG  ARG A 313      16.932  64.883  17.069  1.00 63.49           C  
ATOM    765  CD  ARG A 313      17.692  65.643  18.144  1.00 71.66           C  
ATOM    766  NE  ARG A 313      18.668  66.570  17.574  1.00 81.97           N  
ATOM    767  CZ  ARG A 313      19.470  67.351  18.292  1.00 86.25           C  
ATOM    768  NH1 ARG A 313      20.328  68.161  17.684  1.00 86.79           N  
ATOM    769  NH2 ARG A 313      19.415  67.324  19.619  1.00 84.61           N  
ATOM    770  N   GLU A 314      16.451  61.338  15.281  1.00 60.38           N  
ATOM    771  CA  GLU A 314      17.311  60.903  14.173  1.00 58.15           C  
ATOM    772  C   GLU A 314      16.684  60.932  12.783  1.00 63.82           C  
ATOM    773  O   GLU A 314      15.577  60.422  12.584  1.00 63.98           O  
ATOM    774  CB  GLU A 314      17.822  59.481  14.424  1.00 55.28           C  
ATOM    775  CG  GLU A 314      18.871  59.023  13.412  1.00 41.06           C  
ATOM    776  CD  GLU A 314      20.101  59.916  13.432  1.00 50.33           C  
ATOM    777  OE1 GLU A 314      20.333  60.632  12.438  1.00 37.56           O  
ATOM    778  OE2 GLU A 314      20.832  59.917  14.448  1.00 35.92           O  
ATOM    779  N   GLN A 315      17.413  61.502  11.822  1.00 59.23           N  
ATOM    780  CA  GLN A 315      16.944  61.581  10.439  1.00 68.12           C  
ATOM    781  C   GLN A 315      17.785  60.752   9.466  1.00 67.33           C  
ATOM    782  O   GLN A 315      17.703  60.931   8.252  1.00 68.15           O  
ATOM    783  CB  GLN A 315      16.895  63.035   9.978  1.00 65.80           C  
ATOM    784  CG  GLN A 315      18.079  63.865  10.412  1.00 75.57           C  
ATOM    785  CD  GLN A 315      17.855  65.340  10.147  1.00 85.12           C  
ATOM    786  OE1 GLN A 315      18.686  66.185  10.496  1.00 83.76           O  
ATOM    787  NE2 GLN A 315      16.722  65.659   9.525  1.00 82.39           N  
ATOM    788  N   HIS A 316      18.596  59.850  10.011  1.00 63.69           N  
ATOM    789  CA  HIS A 316      19.434  58.961   9.211  1.00 60.16           C  
ATOM    790  C   HIS A 316      18.984  57.546   9.528  1.00 48.51           C  
ATOM    791  O   HIS A 316      18.883  57.169  10.694  1.00 51.04           O  
ATOM    792  CB  HIS A 316      20.912  59.106   9.578  1.00 59.28           C  
ATOM    793  CG  HIS A 316      21.503  60.425   9.201  1.00 76.67           C  
ATOM    794  ND1 HIS A 316      21.565  60.866   7.897  1.00 79.09           N  
ATOM    795  CD2 HIS A 316      22.055  61.404   9.957  1.00 79.99           C  
ATOM    796  CE1 HIS A 316      22.132  62.059   7.865  1.00 80.68           C  
ATOM    797  NE2 HIS A 316      22.438  62.409   9.102  1.00 83.44           N  
ATOM    798  N   PHE A 317      18.704  56.764   8.498  1.00 41.95           N  
ATOM    799  CA  PHE A 317      18.265  55.393   8.711  1.00 47.13           C  
ATOM    800  C   PHE A 317      19.478  54.467   8.835  1.00 41.22           C  
ATOM    801  O   PHE A 317      20.452  54.633   8.109  1.00 40.78           O  
ATOM    802  CB  PHE A 317      17.391  54.932   7.543  1.00 45.64           C  
ATOM    803  CG  PHE A 317      16.847  53.557   7.726  1.00 52.68           C  
ATOM    804  CD1 PHE A 317      15.755  53.339   8.554  1.00 57.56           C  
ATOM    805  CD2 PHE A 317      17.473  52.468   7.136  1.00 56.11           C  
ATOM    806  CE1 PHE A 317      15.291  52.046   8.797  1.00 69.57           C  
ATOM    807  CE2 PHE A 317      17.021  51.168   7.370  1.00 63.98           C  
ATOM    808  CZ  PHE A 317      15.928  50.956   8.204  1.00 66.21           C  
ATOM    809  N   PRO A 318      19.458  53.513   9.786  1.00 42.34           N  
ATOM    810  CA  PRO A 318      18.409  53.212  10.777  1.00 50.26           C  
ATOM    811  C   PRO A 318      18.464  54.254  11.899  1.00 43.69           C  
ATOM    812  O   PRO A 318      19.540  54.614  12.364  1.00 40.71           O  
ATOM    813  CB  PRO A 318      18.780  51.812  11.250  1.00 49.91           C  
ATOM    814  CG  PRO A 318      20.270  51.831  11.163  1.00 48.18           C  
ATOM    815  CD  PRO A 318      20.531  52.507   9.844  1.00 42.99           C  
ATOM    816  N   PHE A 319      17.305  54.733  12.327  1.00 38.17           N  
ATOM    817  CA  PHE A 319      17.240  55.782  13.336  1.00 43.31           C  
ATOM    818  C   PHE A 319      17.797  55.454  14.708  1.00 37.38           C  
ATOM    819  O   PHE A 319      18.239  56.353  15.433  1.00 34.10           O  
ATOM    820  CB  PHE A 319      15.801  56.270  13.468  1.00 52.80           C  
ATOM    821  CG  PHE A 319      15.184  56.666  12.157  1.00 66.18           C  
ATOM    822  CD1 PHE A 319      15.726  57.709  11.406  1.00 64.07           C  
ATOM    823  CD2 PHE A 319      14.083  55.977  11.654  1.00 65.27           C  
ATOM    824  CE1 PHE A 319      15.186  58.058  10.177  1.00 57.82           C  
ATOM    825  CE2 PHE A 319      13.533  56.320  10.424  1.00 64.53           C  
ATOM    826  CZ  PHE A 319      14.086  57.362   9.684  1.00 62.94           C  
ATOM    827  N   ASP A 320      17.798  54.181  15.070  1.00 29.93           N  
ATOM    828  CA  ASP A 320      18.298  53.819  16.389  1.00 42.34           C  
ATOM    829  C   ASP A 320      19.783  53.451  16.434  1.00 37.65           C  
ATOM    830  O   ASP A 320      20.280  53.062  17.494  1.00 35.86           O  
ATOM    831  CB  ASP A 320      17.456  52.678  16.965  1.00 36.77           C  
ATOM    832  CG  ASP A 320      17.474  51.460  16.087  1.00 41.79           C  
ATOM    833  OD1 ASP A 320      17.996  51.570  14.962  1.00 37.77           O  
ATOM    834  OD2 ASP A 320      16.972  50.399  16.508  1.00 48.11           O  
ATOM    835  N   SER A 321      20.503  53.560  15.309  1.00 28.64           N  
ATOM    836  CA  SER A 321      21.928  53.217  15.352  1.00 22.87           C  
ATOM    837  C   SER A 321      22.692  54.353  16.033  1.00 26.06           C  
ATOM    838  O   SER A 321      22.442  55.532  15.773  1.00 28.24           O  
ATOM    839  CB  SER A 321      22.491  53.004  13.951  1.00 29.00           C  
ATOM    840  OG  SER A 321      23.831  52.548  14.030  1.00 27.81           O  
ATOM    841  N   PHE A 322      23.613  53.997  16.915  1.00 22.71           N  
ATOM    842  CA  PHE A 322      24.402  54.994  17.622  1.00 21.55           C  
ATOM    843  C   PHE A 322      25.337  55.733  16.640  1.00 27.43           C  
ATOM    844  O   PHE A 322      25.622  56.934  16.795  1.00 20.64           O  
ATOM    845  CB  PHE A 322      25.222  54.302  18.721  1.00 20.38           C  
ATOM    846  CG  PHE A 322      25.734  55.243  19.791  1.00 20.50           C  
ATOM    847  CD1 PHE A 322      26.826  56.081  19.547  1.00 24.21           C  
ATOM    848  CD2 PHE A 322      25.090  55.325  21.026  1.00 26.48           C  
ATOM    849  CE1 PHE A 322      27.275  57.002  20.527  1.00 16.04           C  
ATOM    850  CE2 PHE A 322      25.522  56.241  22.009  1.00 18.13           C  
ATOM    851  CZ  PHE A 322      26.613  57.076  21.752  1.00 26.66           C  
ATOM    852  N   PHE A 323      25.780  55.017  15.611  1.00 20.92           N  
ATOM    853  CA  PHE A 323      26.723  55.575  14.645  1.00 25.94           C  
ATOM    854  C   PHE A 323      26.367  55.288  13.195  1.00 26.09           C  
ATOM    855  O   PHE A 323      25.602  54.377  12.905  1.00 25.42           O  
ATOM    856  CB  PHE A 323      28.129  55.024  14.922  1.00 18.29           C  
ATOM    857  CG  PHE A 323      28.280  53.554  14.613  1.00 18.63           C  
ATOM    858  CD1 PHE A 323      27.628  52.600  15.376  1.00 17.98           C  
ATOM    859  CD2 PHE A 323      29.062  53.129  13.536  1.00 17.36           C  
ATOM    860  CE1 PHE A 323      27.741  51.230  15.081  1.00 15.48           C  
ATOM    861  CE2 PHE A 323      29.192  51.771  13.229  1.00 18.53           C  
ATOM    862  CZ  PHE A 323      28.530  50.816  14.006  1.00 25.42           C  
ATOM    863  N   TYR A 324      26.955  56.060  12.288  1.00 24.47           N  
ATOM    864  CA  TYR A 324      26.728  55.889  10.855  1.00 24.94           C  
ATOM    865  C   TYR A 324      28.046  55.997  10.081  1.00 34.26           C  
ATOM    866  O   TYR A 324      29.053  56.506  10.590  1.00 23.39           O  
ATOM    867  CB  TYR A 324      25.738  56.940  10.335  1.00 24.19           C  
ATOM    868  CG  TYR A 324      24.421  56.944  11.084  1.00 34.18           C  
ATOM    869  CD1 TYR A 324      24.259  57.688  12.261  1.00 38.91           C  
ATOM    870  CD2 TYR A 324      23.354  56.146  10.654  1.00 32.01           C  
ATOM    871  CE1 TYR A 324      23.066  57.631  12.992  1.00 35.80           C  
ATOM    872  CE2 TYR A 324      22.173  56.080  11.373  1.00 44.40           C  
ATOM    873  CZ  TYR A 324      22.035  56.820  12.544  1.00 39.62           C  
ATOM    874  OH  TYR A 324      20.881  56.691  13.270  1.00 24.62           O  
ATOM    875  N   ILE A 325      28.020  55.513   8.846  1.00 28.05           N  
ATOM    876  CA  ILE A 325      29.180  55.512   7.972  1.00 23.66           C  
ATOM    877  C   ILE A 325      28.887  56.423   6.779  1.00 28.52           C  
ATOM    878  O   ILE A 325      27.868  56.268   6.101  1.00 30.83           O  
ATOM    879  CB  ILE A 325      29.459  54.057   7.485  1.00 24.64           C  
ATOM    880  CG1 ILE A 325      29.640  53.140   8.703  1.00 30.63           C  
ATOM    881  CG2 ILE A 325      30.683  54.014   6.562  1.00 29.13           C  
ATOM    882  CD1 ILE A 325      30.790  53.527   9.624  1.00 28.60           C  
ATOM    883  N   ARG A 326      29.778  57.376   6.525  1.00 29.99           N  
ATOM    884  CA  ARG A 326      29.600  58.313   5.420  1.00 30.02           C  
ATOM    885  C   ARG A 326      30.882  58.405   4.594  1.00 28.26           C  
ATOM    886  O   ARG A 326      31.983  58.071   5.069  1.00 24.19           O  
ATOM    887  CB  ARG A 326      29.237  59.707   5.957  1.00 35.46           C  
ATOM    888  CG  ARG A 326      27.979  59.751   6.838  1.00 51.10           C  
ATOM    889  CD  ARG A 326      26.705  59.483   6.038  1.00 49.07           C  
ATOM    890  NE  ARG A 326      26.441  60.530   5.048  1.00 57.39           N  
ATOM    891  CZ  ARG A 326      25.834  61.685   5.313  1.00 59.67           C  
ATOM    892  NH1 ARG A 326      25.418  61.958   6.542  1.00 68.38           N  
ATOM    893  NH2 ARG A 326      25.642  62.571   4.346  1.00 50.14           N  
ATOM    894  N   ASN A 327      30.730  58.884   3.366  1.00 27.90           N  
ATOM    895  CA  ASN A 327      31.848  59.032   2.443  1.00 19.60           C  
ATOM    896  C   ASN A 327      32.661  57.754   2.402  1.00 24.98           C  
ATOM    897  O   ASN A 327      33.887  57.785   2.427  1.00 24.74           O  
ATOM    898  CB  ASN A 327      32.734  60.210   2.865  1.00 30.45           C  
ATOM    899  CG  ASN A 327      31.970  61.515   2.872  1.00 45.33           C  
ATOM    900  OD1 ASN A 327      31.359  61.885   1.869  1.00 32.68           O  
ATOM    901  ND2 ASN A 327      31.982  62.213   4.002  1.00 32.29           N  
ATOM    902  N   SER A 328      31.965  56.626   2.326  1.00 22.22           N  
ATOM    903  CA  SER A 328      32.638  55.342   2.281  1.00 17.93           C  
ATOM    904  C   SER A 328      33.039  55.056   0.861  1.00 32.80           C  
ATOM    905  O   SER A 328      32.197  55.122  -0.062  1.00 22.03           O  
ATOM    906  CB  SER A 328      31.697  54.221   2.756  1.00 17.26           C  
ATOM    907  OG  SER A 328      32.349  52.964   2.667  1.00 25.81           O  
ATOM    908  N   GLU A 329      34.315  54.733   0.680  1.00 19.16           N  
ATOM    909  CA  GLU A 329      34.818  54.413  -0.645  1.00 35.16           C  
ATOM    910  C   GLU A 329      34.219  53.057  -1.046  1.00 32.16           C  
ATOM    911  O   GLU A 329      34.007  52.793  -2.219  1.00 26.88           O  
ATOM    912  CB  GLU A 329      36.352  54.335  -0.645  1.00 22.27           C  
ATOM    913  CG  GLU A 329      36.891  53.188   0.198  1.00 56.24           C  
ATOM    914  CD  GLU A 329      38.355  52.873  -0.083  1.00 60.18           C  
ATOM    915  OE1 GLU A 329      38.740  52.799  -1.272  1.00 71.51           O  
ATOM    916  OE2 GLU A 329      39.119  52.684   0.882  1.00 35.53           O  
ATOM    917  N   HIS A 330      33.932  52.212  -0.057  1.00 29.22           N  
ATOM    918  CA  HIS A 330      33.357  50.897  -0.307  1.00 31.28           C  
ATOM    919  C   HIS A 330      31.849  50.830  -0.163  1.00 29.96           C  
ATOM    920  O   HIS A 330      31.246  51.569   0.626  1.00 24.52           O  
ATOM    921  CB  HIS A 330      33.990  49.866   0.633  1.00 24.43           C  
ATOM    922  CG  HIS A 330      35.431  49.600   0.337  1.00 36.47           C  
ATOM    923  ND1 HIS A 330      35.852  49.073  -0.862  1.00 32.46           N  
ATOM    924  CD2 HIS A 330      36.547  49.771   1.086  1.00 29.47           C  
ATOM    925  CE1 HIS A 330      37.165  48.925  -0.839  1.00 37.91           C  
ATOM    926  NE2 HIS A 330      37.610  49.341   0.333  1.00 40.22           N  
ATOM    927  N   GLU A 331      31.237  49.938  -0.935  1.00 24.76           N  
ATOM    928  CA  GLU A 331      29.799  49.734  -0.849  1.00 20.94           C  
ATOM    929  C   GLU A 331      29.586  49.120   0.530  1.00 21.17           C  
ATOM    930  O   GLU A 331      30.448  48.382   1.006  1.00 23.35           O  
ATOM    931  CB  GLU A 331      29.346  48.730  -1.918  1.00 26.64           C  
ATOM    932  CG  GLU A 331      27.955  48.161  -1.687  1.00 35.83           C  
ATOM    933  CD  GLU A 331      27.600  47.057  -2.682  1.00 37.26           C  
ATOM    934  OE1 GLU A 331      28.434  46.718  -3.555  1.00 29.53           O  
ATOM    935  OE2 GLU A 331      26.483  46.525  -2.582  1.00 24.10           O  
ATOM    936  N   PHE A 332      28.455  49.406   1.175  1.00 26.18           N  
ATOM    937  CA  PHE A 332      28.199  48.822   2.498  1.00 30.36           C  
ATOM    938  C   PHE A 332      26.721  48.531   2.681  1.00 34.76           C  
ATOM    939  O   PHE A 332      25.888  49.037   1.932  1.00 30.12           O  
ATOM    940  CB  PHE A 332      28.675  49.771   3.619  1.00 19.85           C  
ATOM    941  CG  PHE A 332      27.925  51.080   3.667  1.00 21.72           C  
ATOM    942  CD1 PHE A 332      26.734  51.197   4.396  1.00 19.72           C  
ATOM    943  CD2 PHE A 332      28.403  52.192   2.972  1.00 27.68           C  
ATOM    944  CE1 PHE A 332      26.028  52.414   4.435  1.00 28.56           C  
ATOM    945  CE2 PHE A 332      27.713  53.407   3.000  1.00 28.29           C  
ATOM    946  CZ  PHE A 332      26.522  53.522   3.734  1.00 27.26           C  
ATOM    947  N   SER A 333      26.420  47.686   3.663  1.00 22.64           N  
ATOM    948  CA  SER A 333      25.058  47.321   4.029  1.00 25.79           C  
ATOM    949  C   SER A 333      25.027  47.368   5.557  1.00 30.85           C  
ATOM    950  O   SER A 333      26.069  47.436   6.204  1.00 27.71           O  
ATOM    951  CB  SER A 333      24.707  45.905   3.571  1.00 30.16           C  
ATOM    952  OG  SER A 333      25.510  44.944   4.248  1.00 29.86           O  
ATOM    953  N   TYR A 334      23.833  47.302   6.120  1.00 27.71           N  
ATOM    954  CA  TYR A 334      23.658  47.359   7.555  1.00 28.33           C  
ATOM    955  C   TYR A 334      22.711  46.280   8.053  1.00 29.19           C  
ATOM    956  O   TYR A 334      21.813  45.838   7.335  1.00 32.47           O  
ATOM    957  CB  TYR A 334      23.101  48.734   7.962  1.00 27.44           C  
ATOM    958  CG  TYR A 334      22.809  48.863   9.450  1.00 31.94           C  
ATOM    959  CD1 TYR A 334      21.555  48.543   9.964  1.00 30.21           C  
ATOM    960  CD2 TYR A 334      23.812  49.258  10.347  1.00 29.09           C  
ATOM    961  CE1 TYR A 334      21.292  48.609  11.334  1.00 27.19           C  
ATOM    962  CE2 TYR A 334      23.567  49.326  11.714  1.00 24.56           C  
ATOM    963  CZ  TYR A 334      22.299  48.998  12.199  1.00 31.31           C  
ATOM    964  OH  TYR A 334      22.040  49.054  13.544  1.00 31.96           O  
ATOM    965  N   SER A 335      22.949  45.846   9.288  1.00 26.60           N  
ATOM    966  CA  SER A 335      22.105  44.876   9.965  1.00 28.04           C  
ATOM    967  C   SER A 335      22.366  44.969  11.462  1.00 36.03           C  
ATOM    968  O   SER A 335      23.473  45.306  11.892  1.00 33.05           O  
ATOM    969  CB  SER A 335      22.400  43.452   9.519  1.00 33.53           C  
ATOM    970  OG  SER A 335      21.666  42.564  10.349  1.00 36.51           O  
ATOM    971  N   ALA A 336      21.353  44.653  12.258  1.00 29.94           N  
ATOM    972  CA  ALA A 336      21.499  44.688  13.702  1.00 28.09           C  
ATOM    973  C   ALA A 336      21.339  43.283  14.255  1.00 31.85           C  
ATOM    974  O   ALA A 336      21.537  43.050  15.452  1.00 27.98           O  
ATOM    975  CB  ALA A 336      20.471  45.611  14.309  1.00 30.70           C  
ATOM    976  N   GLU A 337      21.002  42.347  13.370  1.00 38.12           N  
ATOM    977  CA  GLU A 337      20.803  40.944  13.737  1.00 46.76           C  
ATOM    978  C   GLU A 337      21.766  40.481  14.827  1.00 44.19           C  
ATOM    979  O   GLU A 337      21.333  40.010  15.871  1.00 42.51           O  
ATOM    980  CB  GLU A 337      20.979  40.033  12.516  1.00 54.98           C  
ATOM    981  CG  GLU A 337      20.256  40.479  11.258  1.00 72.97           C  
ATOM    982  CD  GLU A 337      18.745  40.536  11.411  1.00 85.43           C  
ATOM    983  OE1 GLU A 337      18.252  41.346  12.231  1.00 88.77           O  
ATOM    984  OE2 GLU A 337      18.052  39.770  10.702  1.00 87.56           O  
ATOM    985  N   LYS A 338      23.070  40.607  14.582  1.00 35.39           N  
ATOM    986  CA  LYS A 338      24.058  40.184  15.568  1.00 33.82           C  
ATOM    987  C   LYS A 338      24.739  41.377  16.225  1.00 27.98           C  
ATOM    988  O   LYS A 338      25.909  41.306  16.609  1.00 36.17           O  
ATOM    989  CB  LYS A 338      25.114  39.303  14.909  1.00 41.76           C  
ATOM    990  CG  LYS A 338      24.559  38.208  14.027  1.00 54.88           C  
ATOM    991  CD  LYS A 338      25.635  37.171  13.733  1.00 65.15           C  
ATOM    992  CE  LYS A 338      25.307  36.326  12.508  1.00 70.94           C  
ATOM    993  NZ  LYS A 338      25.502  37.094  11.238  1.00 73.17           N  
ATOM    994  N   GLY A 339      23.985  42.461  16.371  1.00 28.48           N  
ATOM    995  CA  GLY A 339      24.509  43.687  16.937  1.00 26.38           C  
ATOM    996  C   GLY A 339      24.637  44.672  15.787  1.00 32.72           C  
ATOM    997  O   GLY A 339      24.885  44.272  14.640  1.00 27.86           O  
ATOM    998  N   SER A 340      24.457  45.955  16.085  1.00 25.38           N  
ATOM    999  CA  SER A 340      24.544  47.023  15.086  1.00 20.35           C  
ATOM   1000  C   SER A 340      25.881  46.914  14.313  1.00 28.86           C  
ATOM   1001  O   SER A 340      26.958  47.145  14.854  1.00 19.32           O  
ATOM   1002  CB  SER A 340      24.422  48.377  15.787  1.00 17.70           C  
ATOM   1003  OG  SER A 340      24.280  49.430  14.852  1.00 30.57           O  
ATOM   1004  N   THR A 341      25.801  46.567  13.039  1.00 23.19           N  
ATOM   1005  CA  THR A 341      26.993  46.361  12.235  1.00 23.14           C  
ATOM   1006  C   THR A 341      26.879  46.896  10.816  1.00 28.43           C  
ATOM   1007  O   THR A 341      25.883  46.648  10.139  1.00 25.47           O  
ATOM   1008  CB  THR A 341      27.301  44.840  12.104  1.00 25.89           C  
ATOM   1009  OG1 THR A 341      27.450  44.264  13.404  1.00 28.80           O  
ATOM   1010  CG2 THR A 341      28.576  44.603  11.271  1.00 24.20           C  
ATOM   1011  N   PHE A 342      27.900  47.622  10.368  1.00 23.49           N  
ATOM   1012  CA  PHE A 342      27.929  48.092   8.993  1.00 19.29           C  
ATOM   1013  C   PHE A 342      28.923  47.151   8.331  1.00 24.95           C  
ATOM   1014  O   PHE A 342      30.029  46.938   8.844  1.00 23.96           O  
ATOM   1015  CB  PHE A 342      28.420  49.538   8.882  1.00 19.23           C  
ATOM   1016  CG  PHE A 342      27.354  50.568   9.190  1.00 17.82           C  
ATOM   1017  CD1 PHE A 342      27.079  50.944  10.505  1.00 25.00           C  
ATOM   1018  CD2 PHE A 342      26.593  51.116   8.169  1.00 21.94           C  
ATOM   1019  CE1 PHE A 342      26.045  51.853  10.794  1.00 21.69           C  
ATOM   1020  CE2 PHE A 342      25.556  52.024   8.444  1.00 24.35           C  
ATOM   1021  CZ  PHE A 342      25.285  52.387   9.764  1.00 24.54           C  
ATOM   1022  N   THR A 343      28.512  46.547   7.225  1.00 18.53           N  
ATOM   1023  CA  THR A 343      29.380  45.641   6.487  1.00 18.53           C  
ATOM   1024  C   THR A 343      29.799  46.233   5.165  1.00 22.83           C  
ATOM   1025  O   THR A 343      28.965  46.516   4.285  1.00 24.60           O  
ATOM   1026  CB  THR A 343      28.701  44.285   6.217  1.00 24.53           C  
ATOM   1027  OG1 THR A 343      28.381  43.658   7.464  1.00 26.86           O  
ATOM   1028  CG2 THR A 343      29.641  43.358   5.431  1.00 19.56           C  
ATOM   1029  N   LEU A 344      31.100  46.410   5.009  1.00 21.27           N  
ATOM   1030  CA  LEU A 344      31.629  46.950   3.773  1.00 21.36           C  
ATOM   1031  C   LEU A 344      31.859  45.794   2.819  1.00 34.62           C  
ATOM   1032  O   LEU A 344      32.496  44.807   3.191  1.00 21.69           O  
ATOM   1033  CB  LEU A 344      32.973  47.643   4.010  1.00 20.65           C  
ATOM   1034  CG  LEU A 344      33.033  48.772   5.027  1.00 21.30           C  
ATOM   1035  CD1 LEU A 344      34.402  49.462   4.918  1.00 29.78           C  
ATOM   1036  CD2 LEU A 344      31.925  49.751   4.775  1.00 25.75           C  
ATOM   1037  N   ILE A 345      31.344  45.910   1.599  1.00 31.08           N  
ATOM   1038  CA  ILE A 345      31.547  44.861   0.603  1.00 31.15           C  
ATOM   1039  C   ILE A 345      32.729  45.285  -0.227  1.00 39.33           C  
ATOM   1040  O   ILE A 345      32.711  46.340  -0.862  1.00 36.60           O  
ATOM   1041  CB  ILE A 345      30.325  44.674  -0.326  1.00 35.46           C  
ATOM   1042  CG1 ILE A 345      29.167  44.037   0.445  1.00 39.87           C  
ATOM   1043  CG2 ILE A 345      30.694  43.776  -1.485  1.00 41.15           C  
ATOM   1044  CD1 ILE A 345      28.486  44.959   1.448  1.00 56.10           C  
ATOM   1045  N   MET A 346      33.771  44.469  -0.213  1.00 30.45           N  
ATOM   1046  CA  MET A 346      34.955  44.809  -0.965  1.00 36.50           C  
ATOM   1047  C   MET A 346      35.242  43.887  -2.128  1.00 44.97           C  
ATOM   1048  O   MET A 346      34.354  43.188  -2.604  1.00 55.22           O  
ATOM   1049  CB  MET A 346      36.117  44.884  -0.008  1.00 20.71           C  
ATOM   1050  CG  MET A 346      35.755  45.911   1.071  1.00 39.34           C  
ATOM   1051  SD  MET A 346      37.064  46.267   2.182  1.00 33.51           S  
ATOM   1052  CE  MET A 346      37.290  44.634   2.896  1.00 29.48           C  
ATOM   1053  N   TYR A 347      36.480  43.882  -2.592  1.00 36.46           N  
ATOM   1054  CA  TYR A 347      36.822  43.057  -3.736  1.00 43.38           C  
ATOM   1055  C   TYR A 347      38.175  42.427  -3.499  1.00 40.27           C  
ATOM   1056  O   TYR A 347      38.976  42.939  -2.706  1.00 36.45           O  
ATOM   1057  CB  TYR A 347      36.858  43.938  -4.983  1.00 40.44           C  
ATOM   1058  CG  TYR A 347      37.697  45.170  -4.755  1.00 56.74           C  
ATOM   1059  CD1 TYR A 347      39.087  45.131  -4.893  1.00 55.96           C  
ATOM   1060  CD2 TYR A 347      37.111  46.363  -4.334  1.00 60.81           C  
ATOM   1061  CE1 TYR A 347      39.873  46.252  -4.615  1.00 66.13           C  
ATOM   1062  CE2 TYR A 347      37.887  47.490  -4.051  1.00 58.49           C  
ATOM   1063  CZ  TYR A 347      39.262  47.427  -4.193  1.00 63.36           C  
ATOM   1064  OH  TYR A 347      40.021  48.536  -3.908  1.00 63.07           O  
ATOM   1065  N   PRO A 348      38.448  41.305  -4.182  1.00 36.89           N  
ATOM   1066  CA  PRO A 348      39.726  40.617  -4.026  1.00 36.82           C  
ATOM   1067  C   PRO A 348      40.814  41.629  -4.260  1.00 34.19           C  
ATOM   1068  O   PRO A 348      40.706  42.467  -5.154  1.00 32.36           O  
ATOM   1069  CB  PRO A 348      39.681  39.547  -5.119  1.00 41.80           C  
ATOM   1070  CG  PRO A 348      38.207  39.275  -5.261  1.00 32.56           C  
ATOM   1071  CD  PRO A 348      37.637  40.666  -5.235  1.00 43.85           C  
ATOM   1072  N   GLY A 349      41.845  41.565  -3.437  1.00 28.76           N  
ATOM   1073  CA  GLY A 349      42.950  42.488  -3.568  1.00 23.82           C  
ATOM   1074  C   GLY A 349      42.820  43.777  -2.766  1.00 35.15           C  
ATOM   1075  O   GLY A 349      43.797  44.511  -2.649  1.00 31.66           O  
ATOM   1076  N   ALA A 350      41.639  44.087  -2.229  1.00 27.06           N  
ATOM   1077  CA  ALA A 350      41.518  45.325  -1.458  1.00 27.58           C  
ATOM   1078  C   ALA A 350      42.365  45.173  -0.192  1.00 29.24           C  
ATOM   1079  O   ALA A 350      42.381  44.107   0.424  1.00 23.27           O  
ATOM   1080  CB  ALA A 350      40.051  45.594  -1.109  1.00 24.19           C  
ATOM   1081  N   VAL A 351      43.098  46.216   0.184  1.00 23.62           N  
ATOM   1082  CA  VAL A 351      43.941  46.148   1.381  1.00 26.44           C  
ATOM   1083  C   VAL A 351      43.724  47.364   2.289  1.00 26.87           C  
ATOM   1084  O   VAL A 351      44.461  47.580   3.250  1.00 23.34           O  
ATOM   1085  CB  VAL A 351      45.440  46.063   1.013  1.00 28.53           C  
ATOM   1086  CG1 VAL A 351      45.733  44.750   0.258  1.00 25.26           C  
ATOM   1087  CG2 VAL A 351      45.823  47.271   0.136  1.00 21.02           C  
ATOM   1088  N   GLN A 352      42.715  48.166   1.978  1.00 26.13           N  
ATOM   1089  CA  GLN A 352      42.439  49.337   2.803  1.00 28.00           C  
ATOM   1090  C   GLN A 352      40.989  49.723   2.679  1.00 21.94           C  
ATOM   1091  O   GLN A 352      40.331  49.424   1.688  1.00 21.16           O  
ATOM   1092  CB  GLN A 352      43.316  50.531   2.376  1.00 30.23           C  
ATOM   1093  CG  GLN A 352      43.237  51.756   3.316  1.00 35.04           C  
ATOM   1094  CD  GLN A 352      44.352  52.770   3.057  1.00 36.40           C  
ATOM   1095  OE1 GLN A 352      45.475  52.385   2.776  1.00 29.53           O  
ATOM   1096  NE2 GLN A 352      44.046  54.063   3.172  1.00 25.56           N  
ATOM   1097  N   ALA A 353      40.461  50.358   3.712  1.00 18.54           N  
ATOM   1098  CA  ALA A 353      39.096  50.819   3.624  1.00 17.60           C  
ATOM   1099  C   ALA A 353      39.086  52.181   4.277  1.00 21.62           C  
ATOM   1100  O   ALA A 353      39.544  52.334   5.412  1.00 22.49           O  
ATOM   1101  CB  ALA A 353      38.145  49.877   4.355  1.00 19.27           C  
ATOM   1102  N   ASN A 354      38.562  53.157   3.551  1.00 20.18           N  
ATOM   1103  CA  ASN A 354      38.439  54.522   4.036  1.00 21.01           C  
ATOM   1104  C   ASN A 354      36.977  54.907   4.152  1.00 17.28           C  
ATOM   1105  O   ASN A 354      36.142  54.515   3.324  1.00 18.05           O  
ATOM   1106  CB  ASN A 354      39.131  55.490   3.076  1.00 26.22           C  
ATOM   1107  CG  ASN A 354      40.608  55.210   2.950  1.00 29.17           C  
ATOM   1108  OD1 ASN A 354      41.279  54.935   3.939  1.00 31.70           O  
ATOM   1109  ND2 ASN A 354      41.128  55.288   1.732  1.00 45.41           N  
ATOM   1110  N   PHE A 355      36.660  55.660   5.195  1.00 24.01           N  
ATOM   1111  CA  PHE A 355      35.296  56.141   5.399  1.00 23.46           C  
ATOM   1112  C   PHE A 355      35.261  57.039   6.622  1.00 17.64           C  
ATOM   1113  O   PHE A 355      36.185  57.034   7.446  1.00 20.82           O  
ATOM   1114  CB  PHE A 355      34.318  54.963   5.606  1.00 18.54           C  
ATOM   1115  CG  PHE A 355      34.696  54.045   6.751  1.00 23.40           C  
ATOM   1116  CD1 PHE A 355      34.275  54.314   8.059  1.00 23.78           C  
ATOM   1117  CD2 PHE A 355      35.513  52.943   6.530  1.00 22.88           C  
ATOM   1118  CE1 PHE A 355      34.669  53.495   9.139  1.00 21.42           C  
ATOM   1119  CE2 PHE A 355      35.919  52.112   7.603  1.00 22.83           C  
ATOM   1120  CZ  PHE A 355      35.491  52.396   8.915  1.00 23.63           C  
ATOM   1121  N   ASP A 356      34.203  57.827   6.725  1.00 22.05           N  
ATOM   1122  CA  ASP A 356      34.038  58.640   7.907  1.00 20.02           C  
ATOM   1123  C   ASP A 356      33.032  57.945   8.777  1.00 19.46           C  
ATOM   1124  O   ASP A 356      32.113  57.301   8.273  1.00 20.28           O  
ATOM   1125  CB  ASP A 356      33.470  60.007   7.593  1.00 25.41           C  
ATOM   1126  CG  ASP A 356      34.436  60.865   6.843  1.00 34.08           C  
ATOM   1127  OD1 ASP A 356      35.634  60.827   7.189  1.00 26.31           O  
ATOM   1128  OD2 ASP A 356      33.987  61.571   5.923  1.00 23.27           O  
ATOM   1129  N   ILE A 357      33.223  58.037  10.081  1.00 16.89           N  
ATOM   1130  CA  ILE A 357      32.222  57.513  10.988  1.00 19.70           C  
ATOM   1131  C   ILE A 357      31.698  58.739  11.738  1.00 24.87           C  
ATOM   1132  O   ILE A 357      32.450  59.689  11.996  1.00 23.60           O  
ATOM   1133  CB  ILE A 357      32.803  56.494  11.978  1.00 19.78           C  
ATOM   1134  CG1 ILE A 357      31.694  56.001  12.907  1.00 19.84           C  
ATOM   1135  CG2 ILE A 357      33.947  57.115  12.746  1.00 20.31           C  
ATOM   1136  CD1 ILE A 357      32.038  54.713  13.660  1.00 23.41           C  
ATOM   1137  N   ILE A 358      30.406  58.751  12.056  1.00 19.93           N  
ATOM   1138  CA  ILE A 358      29.847  59.887  12.778  1.00 20.05           C  
ATOM   1139  C   ILE A 358      28.950  59.355  13.903  1.00 25.91           C  
ATOM   1140  O   ILE A 358      28.158  58.436  13.687  1.00 24.66           O  
ATOM   1141  CB  ILE A 358      29.083  60.838  11.794  1.00 23.64           C  
ATOM   1142  CG1 ILE A 358      28.523  62.035  12.561  1.00 23.88           C  
ATOM   1143  CG2 ILE A 358      27.926  60.092  11.097  1.00 22.40           C  
ATOM   1144  CD1 ILE A 358      27.799  63.024  11.667  1.00 27.01           C  
ATOM   1145  N   PHE A 359      29.123  59.894  15.110  1.00 17.86           N  
ATOM   1146  CA  PHE A 359      28.362  59.453  16.292  1.00 20.81           C  
ATOM   1147  C   PHE A 359      27.197  60.403  16.538  1.00 20.81           C  
ATOM   1148  O   PHE A 359      27.371  61.622  16.577  1.00 22.25           O  
ATOM   1149  CB  PHE A 359      29.298  59.386  17.501  1.00 15.76           C  
ATOM   1150  CG  PHE A 359      30.449  58.450  17.296  1.00 20.93           C  
ATOM   1151  CD1 PHE A 359      30.286  57.073  17.485  1.00 24.77           C  
ATOM   1152  CD2 PHE A 359      31.666  58.921  16.832  1.00 17.83           C  
ATOM   1153  CE1 PHE A 359      31.332  56.167  17.203  1.00 19.56           C  
ATOM   1154  CE2 PHE A 359      32.728  58.029  16.544  1.00 21.50           C  
ATOM   1155  CZ  PHE A 359      32.557  56.649  16.729  1.00 24.14           C  
ATOM   1156  N   MET A 360      26.002  59.836  16.682  1.00 27.65           N  
ATOM   1157  CA  MET A 360      24.812  60.645  16.853  1.00 27.46           C  
ATOM   1158  C   MET A 360      24.197  60.614  18.249  1.00 31.54           C  
ATOM   1159  O   MET A 360      23.000  60.821  18.422  1.00 29.84           O  
ATOM   1160  CB  MET A 360      23.781  60.271  15.785  1.00 29.97           C  
ATOM   1161  CG  MET A 360      24.252  60.602  14.357  1.00 27.85           C  
ATOM   1162  SD  MET A 360      24.765  62.344  14.150  1.00 36.96           S  
ATOM   1163  CE  MET A 360      23.166  63.145  14.218  1.00 43.50           C  
ATOM   1164  N   CYS A 361      25.030  60.351  19.245  1.00 21.19           N  
ATOM   1165  CA  CYS A 361      24.587  60.359  20.632  1.00 18.62           C  
ATOM   1166  C   CYS A 361      25.903  60.533  21.367  1.00 20.94           C  
ATOM   1167  O   CYS A 361      26.978  60.451  20.761  1.00 22.23           O  
ATOM   1168  CB  CYS A 361      23.861  59.050  20.978  1.00 20.36           C  
ATOM   1169  SG  CYS A 361      23.220  58.905  22.663  1.00 22.37           S  
ATOM   1170  N   GLN A 362      25.859  60.804  22.654  1.00 20.65           N  
ATOM   1171  CA  GLN A 362      27.121  61.008  23.331  1.00 22.19           C  
ATOM   1172  C   GLN A 362      27.155  60.512  24.761  1.00 28.20           C  
ATOM   1173  O   GLN A 362      26.133  60.125  25.334  1.00 26.37           O  
ATOM   1174  CB  GLN A 362      27.466  62.486  23.258  1.00 18.47           C  
ATOM   1175  CG  GLN A 362      26.524  63.371  24.023  1.00 31.67           C  
ATOM   1176  CD  GLN A 362      26.732  64.815  23.667  1.00 39.57           C  
ATOM   1177  OE1 GLN A 362      27.861  65.254  23.479  1.00 49.39           O  
ATOM   1178  NE2 GLN A 362      25.645  65.568  23.578  1.00 42.36           N  
ATOM   1179  N   GLU A 363      28.352  60.528  25.329  1.00 22.72           N  
ATOM   1180  CA  GLU A 363      28.575  60.075  26.689  1.00 23.93           C  
ATOM   1181  C   GLU A 363      27.601  60.739  27.665  1.00 33.85           C  
ATOM   1182  O   GLU A 363      27.016  60.081  28.521  1.00 26.86           O  
ATOM   1183  CB  GLU A 363      30.017  60.416  27.094  1.00 20.93           C  
ATOM   1184  CG  GLU A 363      30.563  59.610  28.252  1.00 42.05           C  
ATOM   1185  CD  GLU A 363      31.991  59.993  28.557  1.00 35.94           C  
ATOM   1186  OE1 GLU A 363      32.201  61.022  29.238  1.00 35.39           O  
ATOM   1187  OE2 GLU A 363      32.898  59.280  28.089  1.00 38.57           O  
ATOM   1188  N   LYS A 364      27.433  62.050  27.526  1.00 28.53           N  
ATOM   1189  CA  LYS A 364      26.566  62.805  28.414  1.00 35.92           C  
ATOM   1190  C   LYS A 364      25.154  62.215  28.511  1.00 39.69           C  
ATOM   1191  O   LYS A 364      24.512  62.309  29.553  1.00 41.05           O  
ATOM   1192  CB  LYS A 364      26.512  64.257  27.937  1.00 41.07           C  
ATOM   1193  CG  LYS A 364      25.920  65.225  28.925  1.00 57.70           C  
ATOM   1194  CD  LYS A 364      25.956  66.650  28.381  1.00 61.79           C  
ATOM   1195  CE  LYS A 364      25.406  67.642  29.403  1.00 69.15           C  
ATOM   1196  NZ  LYS A 364      25.392  69.046  28.895  1.00 60.71           N  
ATOM   1197  N   CYS A 365      24.686  61.591  27.431  1.00 38.02           N  
ATOM   1198  CA  CYS A 365      23.346  60.991  27.378  1.00 33.65           C  
ATOM   1199  C   CYS A 365      23.148  59.713  28.180  1.00 40.86           C  
ATOM   1200  O   CYS A 365      22.019  59.382  28.554  1.00 43.68           O  
ATOM   1201  CB  CYS A 365      22.976  60.661  25.932  1.00 28.79           C  
ATOM   1202  SG  CYS A 365      22.983  62.071  24.873  1.00 28.47           S  
ATOM   1203  N   LEU A 366      24.230  58.992  28.436  1.00 41.04           N  
ATOM   1204  CA  LEU A 366      24.137  57.703  29.114  1.00 56.54           C  
ATOM   1205  C   LEU A 366      23.921  57.672  30.623  1.00 56.82           C  
ATOM   1206  O   LEU A 366      24.175  58.649  31.325  1.00 50.14           O  
ATOM   1207  CB  LEU A 366      25.371  56.866  28.768  1.00 58.48           C  
ATOM   1208  CG  LEU A 366      25.791  56.821  27.292  1.00 66.82           C  
ATOM   1209  CD1 LEU A 366      26.697  55.623  27.114  1.00 68.07           C  
ATOM   1210  CD2 LEU A 366      24.589  56.699  26.351  1.00 61.92           C  
ATOM   1211  N   ASP A 367      23.445  56.524  31.104  1.00 64.19           N  
ATOM   1212  CA  ASP A 367      23.204  56.304  32.529  1.00 74.48           C  
ATOM   1213  C   ASP A 367      24.558  56.107  33.199  1.00 76.33           C  
ATOM   1214  O   ASP A 367      25.441  55.464  32.630  1.00 76.46           O  
ATOM   1215  CB  ASP A 367      22.363  55.048  32.737  1.00 77.83           C  
ATOM   1216  CG  ASP A 367      21.550  54.687  31.515  1.00 89.00           C  
ATOM   1217  OD1 ASP A 367      20.865  55.581  30.967  1.00 89.90           O  
ATOM   1218  OD2 ASP A 367      21.594  53.506  31.104  1.00 92.83           O  
ATOM   1219  N   LEU A 368      24.715  56.643  34.405  1.00 76.19           N  
ATOM   1220  CA  LEU A 368      25.980  56.535  35.131  1.00 79.62           C  
ATOM   1221  C   LEU A 368      26.708  55.206  34.932  1.00 81.37           C  
ATOM   1222  O   LEU A 368      27.905  55.192  34.637  1.00 81.33           O  
ATOM   1223  CB  LEU A 368      25.764  56.772  36.629  1.00 75.71           C  
ATOM   1224  CG  LEU A 368      27.029  56.753  37.500  1.00 80.01           C  
ATOM   1225  CD1 LEU A 368      28.067  57.715  36.928  1.00 76.61           C  
ATOM   1226  CD2 LEU A 368      26.679  57.132  38.940  1.00 72.96           C  
ATOM   1227  N   ASP A 369      25.996  54.093  35.083  1.00 78.70           N  
ATOM   1228  CA  ASP A 369      26.624  52.786  34.924  1.00 83.77           C  
ATOM   1229  C   ASP A 369      27.175  52.558  33.515  1.00 83.85           C  
ATOM   1230  O   ASP A 369      28.223  51.931  33.356  1.00 86.49           O  
ATOM   1231  CB  ASP A 369      25.652  51.662  35.313  1.00 87.92           C  
ATOM   1232  CG  ASP A 369      24.355  51.705  34.532  1.00 96.05           C  
ATOM   1233  OD1 ASP A 369      24.398  51.532  33.294  1.00 95.99           O  
ATOM   1234  OD2 ASP A 369      23.291  51.908  35.160  1.00 95.74           O  
ATOM   1235  N   ASP A 370      26.479  53.066  32.499  1.00 77.15           N  
ATOM   1236  CA  ASP A 370      26.937  52.923  31.116  1.00 72.15           C  
ATOM   1237  C   ASP A 370      28.067  53.909  30.838  1.00 71.05           C  
ATOM   1238  O   ASP A 370      28.979  53.629  30.056  1.00 59.86           O  
ATOM   1239  CB  ASP A 370      25.796  53.189  30.131  1.00 72.47           C  
ATOM   1240  CG  ASP A 370      24.974  51.949  29.832  1.00 81.69           C  
ATOM   1241  OD1 ASP A 370      24.009  52.065  29.046  1.00 82.15           O  
ATOM   1242  OD2 ASP A 370      25.291  50.862  30.370  1.00 77.01           O  
ATOM   1243  N   ARG A 371      27.995  55.067  31.488  1.00 71.79           N  
ATOM   1244  CA  ARG A 371      28.994  56.116  31.320  1.00 72.60           C  
ATOM   1245  C   ARG A 371      30.360  55.614  31.802  1.00 69.81           C  
ATOM   1246  O   ARG A 371      31.401  56.059  31.317  1.00 69.49           O  
ATOM   1247  CB  ARG A 371      28.578  57.361  32.116  1.00 74.11           C  
ATOM   1248  CG  ARG A 371      29.125  58.680  31.578  1.00 78.99           C  
ATOM   1249  CD  ARG A 371      28.994  59.808  32.604  1.00 82.82           C  
ATOM   1250  NE  ARG A 371      27.673  59.849  33.231  1.00 84.15           N  
ATOM   1251  CZ  ARG A 371      26.539  60.095  32.585  1.00 83.15           C  
ATOM   1252  NH1 ARG A 371      26.553  60.328  31.280  1.00 83.48           N  
ATOM   1253  NH2 ARG A 371      25.388  60.100  33.247  1.00 81.14           N  
ATOM   1254  N   ARG A 372      30.338  54.682  32.754  1.00 60.64           N  
ATOM   1255  CA  ARG A 372      31.553  54.106  33.321  1.00 56.56           C  
ATOM   1256  C   ARG A 372      32.144  53.000  32.450  1.00 53.59           C  
ATOM   1257  O   ARG A 372      33.310  52.633  32.591  1.00 44.47           O  
ATOM   1258  CB  ARG A 372      31.263  53.578  34.726  1.00 61.44           C  
ATOM   1259  CG  ARG A 372      30.948  54.693  35.712  1.00 77.11           C  
ATOM   1260  CD  ARG A 372      30.665  54.171  37.111  1.00 84.78           C  
ATOM   1261  NE  ARG A 372      30.534  55.261  38.079  1.00 89.55           N  
ATOM   1262  CZ  ARG A 372      31.527  56.076  38.430  1.00 90.46           C  
ATOM   1263  NH1 ARG A 372      32.734  55.929  37.897  1.00 91.83           N  
ATOM   1264  NH2 ARG A 372      31.313  57.038  39.318  1.00 90.01           N  
ATOM   1265  N   LYS A 373      31.336  52.453  31.554  1.00 45.04           N  
ATOM   1266  CA  LYS A 373      31.836  51.428  30.657  1.00 43.52           C  
ATOM   1267  C   LYS A 373      32.681  52.129  29.592  1.00 38.10           C  
ATOM   1268  O   LYS A 373      32.615  53.343  29.428  1.00 33.15           O  
ATOM   1269  CB  LYS A 373      30.668  50.672  30.026  1.00 34.20           C  
ATOM   1270  CG  LYS A 373      29.802  49.966  31.064  1.00 40.68           C  
ATOM   1271  CD  LYS A 373      28.668  49.185  30.436  1.00 52.07           C  
ATOM   1272  CE  LYS A 373      27.791  48.550  31.503  1.00 60.76           C  
ATOM   1273  NZ  LYS A 373      26.590  47.889  30.912  1.00 73.66           N  
ATOM   1274  N   THR A 374      33.497  51.368  28.886  1.00 30.45           N  
ATOM   1275  CA  THR A 374      34.340  51.931  27.850  1.00 29.11           C  
ATOM   1276  C   THR A 374      33.715  51.630  26.484  1.00 27.01           C  
ATOM   1277  O   THR A 374      33.302  50.495  26.224  1.00 21.28           O  
ATOM   1278  CB  THR A 374      35.732  51.309  27.933  1.00 30.60           C  
ATOM   1279  OG1 THR A 374      36.237  51.498  29.256  1.00 29.22           O  
ATOM   1280  CG2 THR A 374      36.691  51.950  26.928  1.00 25.14           C  
ATOM   1281  N   MET A 375      33.609  52.644  25.628  1.00 24.66           N  
ATOM   1282  CA  MET A 375      33.055  52.431  24.282  1.00 21.22           C  
ATOM   1283  C   MET A 375      34.235  52.062  23.394  1.00 32.19           C  
ATOM   1284  O   MET A 375      35.316  52.626  23.545  1.00 16.77           O  
ATOM   1285  CB  MET A 375      32.376  53.686  23.769  1.00 18.53           C  
ATOM   1286  CG  MET A 375      31.216  54.111  24.625  1.00 15.48           C  
ATOM   1287  SD  MET A 375      30.388  55.520  23.895  1.00 25.56           S  
ATOM   1288  CE  MET A 375      29.078  55.780  25.072  1.00 36.10           C  
ATOM   1289  N   CYS A 376      34.004  51.144  22.459  1.00 20.81           N  
ATOM   1290  CA  CYS A 376      35.047  50.605  21.590  1.00 18.01           C  
ATOM   1291  C   CYS A 376      34.630  50.468  20.115  1.00 20.64           C  
ATOM   1292  O   CYS A 376      33.559  49.920  19.819  1.00 17.29           O  
ATOM   1293  CB  CYS A 376      35.437  49.225  22.131  1.00 13.01           C  
ATOM   1294  SG  CYS A 376      36.695  48.363  21.170  1.00 21.06           S  
ATOM   1295  N   LEU A 377      35.449  50.988  19.201  1.00 14.24           N  
ATOM   1296  CA  LEU A 377      35.155  50.894  17.759  1.00 17.43           C  
ATOM   1297  C   LEU A 377      35.984  49.715  17.260  1.00 18.91           C  
ATOM   1298  O   LEU A 377      37.230  49.770  17.273  1.00 16.07           O  
ATOM   1299  CB  LEU A 377      35.593  52.170  17.014  1.00 13.96           C  
ATOM   1300  CG  LEU A 377      35.350  52.132  15.489  1.00 23.18           C  
ATOM   1301  CD1 LEU A 377      33.851  51.956  15.242  1.00 19.35           C  
ATOM   1302  CD2 LEU A 377      35.849  53.419  14.815  1.00 17.83           C  
ATOM   1303  N   ALA A 378      35.301  48.656  16.832  1.00 16.13           N  
ATOM   1304  CA  ALA A 378      35.969  47.435  16.367  1.00 17.25           C  
ATOM   1305  C   ALA A 378      35.616  47.071  14.932  1.00 18.59           C  
ATOM   1306  O   ALA A 378      34.467  47.249  14.508  1.00 13.24           O  
ATOM   1307  CB  ALA A 378      35.596  46.243  17.299  1.00 17.40           C  
ATOM   1308  N   VAL A 379      36.615  46.554  14.205  1.00 17.27           N  
ATOM   1309  CA  VAL A 379      36.446  46.120  12.823  1.00 19.42           C  
ATOM   1310  C   VAL A 379      36.950  44.684  12.658  1.00 20.58           C  
ATOM   1311  O   VAL A 379      37.911  44.264  13.303  1.00 18.76           O  
ATOM   1312  CB  VAL A 379      37.193  47.044  11.817  1.00 18.38           C  
ATOM   1313  CG1 VAL A 379      36.472  48.403  11.734  1.00 19.57           C  
ATOM   1314  CG2 VAL A 379      38.629  47.212  12.237  1.00 18.87           C  
ATOM   1315  N   PHE A 380      36.294  43.954  11.766  1.00 19.66           N  
ATOM   1316  CA  PHE A 380      36.595  42.547  11.511  1.00 18.45           C  
ATOM   1317  C   PHE A 380      36.681  42.327  10.019  1.00 24.88           C  
ATOM   1318  O   PHE A 380      35.836  42.830   9.254  1.00 18.52           O  
ATOM   1319  CB  PHE A 380      35.465  41.666  12.069  1.00 14.23           C  
ATOM   1320  CG  PHE A 380      35.225  41.856  13.541  1.00 12.64           C  
ATOM   1321  CD1 PHE A 380      35.940  41.116  14.480  1.00 19.66           C  
ATOM   1322  CD2 PHE A 380      34.343  42.832  13.992  1.00 14.63           C  
ATOM   1323  CE1 PHE A 380      35.786  41.358  15.870  1.00 16.26           C  
ATOM   1324  CE2 PHE A 380      34.176  43.082  15.365  1.00 20.05           C  
ATOM   1325  CZ  PHE A 380      34.902  42.347  16.307  1.00 15.67           C  
ATOM   1326  N   LEU A 381      37.713  41.603   9.601  1.00 16.35           N  
ATOM   1327  CA  LEU A 381      37.848  41.279   8.195  1.00 25.08           C  
ATOM   1328  C   LEU A 381      37.379  39.831   8.088  1.00 18.08           C  
ATOM   1329  O   LEU A 381      37.936  38.958   8.757  1.00 18.30           O  
ATOM   1330  CB  LEU A 381      39.308  41.403   7.741  1.00 22.16           C  
ATOM   1331  CG  LEU A 381      39.498  41.347   6.215  1.00 21.08           C  
ATOM   1332  CD1 LEU A 381      38.835  42.553   5.561  1.00 19.39           C  
ATOM   1333  CD2 LEU A 381      40.978  41.327   5.883  1.00 30.66           C  
ATOM   1334  N   ASP A 382      36.337  39.585   7.287  1.00 15.03           N  
ATOM   1335  CA  ASP A 382      35.808  38.227   7.109  1.00 14.84           C  
ATOM   1336  C   ASP A 382      36.112  37.665   5.726  1.00 30.68           C  
ATOM   1337  O   ASP A 382      36.146  38.413   4.740  1.00 22.53           O  
ATOM   1338  CB  ASP A 382      34.293  38.187   7.225  1.00 16.69           C  
ATOM   1339  CG  ASP A 382      33.774  38.444   8.634  1.00 24.61           C  
ATOM   1340  OD1 ASP A 382      34.522  38.354   9.633  1.00 18.82           O  
ATOM   1341  OD2 ASP A 382      32.577  38.743   8.716  1.00 22.30           O  
ATOM   1342  N   ASP A 383      36.291  36.345   5.646  1.00 28.82           N  
ATOM   1343  CA  ASP A 383      36.518  35.705   4.352  1.00 35.09           C  
ATOM   1344  C   ASP A 383      35.155  35.466   3.700  1.00 26.92           C  
ATOM   1345  O   ASP A 383      34.128  35.900   4.229  1.00 27.99           O  
ATOM   1346  CB  ASP A 383      37.283  34.385   4.509  1.00 30.46           C  
ATOM   1347  CG  ASP A 383      36.495  33.318   5.246  1.00 25.27           C  
ATOM   1348  OD1 ASP A 383      35.274  33.465   5.464  1.00 33.88           O  
ATOM   1349  OD2 ASP A 383      37.124  32.315   5.615  1.00 32.98           O  
ATOM   1350  N   GLU A 384      35.133  34.775   2.565  1.00 35.12           N  
ATOM   1351  CA  GLU A 384      33.879  34.506   1.845  1.00 43.45           C  
ATOM   1352  C   GLU A 384      32.885  33.657   2.628  1.00 38.86           C  
ATOM   1353  O   GLU A 384      31.674  33.788   2.458  1.00 44.36           O  
ATOM   1354  CB  GLU A 384      34.161  33.814   0.506  1.00 48.54           C  
ATOM   1355  CG  GLU A 384      35.262  34.447  -0.310  1.00 56.62           C  
ATOM   1356  CD  GLU A 384      36.611  34.329   0.365  1.00 71.94           C  
ATOM   1357  OE1 GLU A 384      37.070  33.190   0.601  1.00 72.82           O  
ATOM   1358  OE2 GLU A 384      37.212  35.379   0.670  1.00 81.42           O  
ATOM   1359  N   ASN A 385      33.388  32.778   3.483  1.00 37.85           N  
ATOM   1360  CA  ASN A 385      32.507  31.922   4.268  1.00 39.98           C  
ATOM   1361  C   ASN A 385      32.006  32.579   5.550  1.00 45.35           C  
ATOM   1362  O   ASN A 385      31.267  31.967   6.331  1.00 34.53           O  
ATOM   1363  CB  ASN A 385      33.226  30.614   4.573  1.00 49.77           C  
ATOM   1364  CG  ASN A 385      33.544  29.839   3.314  1.00 47.08           C  
ATOM   1365  OD1 ASN A 385      34.647  29.324   3.148  1.00 51.78           O  
ATOM   1366  ND2 ASN A 385      32.572  29.756   2.415  1.00 46.75           N  
ATOM   1367  N   GLY A 386      32.399  33.833   5.758  1.00 34.64           N  
ATOM   1368  CA  GLY A 386      31.955  34.550   6.941  1.00 32.97           C  
ATOM   1369  C   GLY A 386      32.818  34.337   8.175  1.00 22.86           C  
ATOM   1370  O   GLY A 386      32.408  34.681   9.281  1.00 27.02           O  
ATOM   1371  N   ASN A 387      33.994  33.748   8.000  1.00 19.79           N  
ATOM   1372  CA  ASN A 387      34.896  33.534   9.134  1.00 23.77           C  
ATOM   1373  C   ASN A 387      35.747  34.784   9.308  1.00 27.87           C  
ATOM   1374  O   ASN A 387      36.291  35.325   8.321  1.00 20.36           O  
ATOM   1375  CB  ASN A 387      35.848  32.362   8.878  1.00 29.07           C  
ATOM   1376  CG  ASN A 387      35.119  31.060   8.631  1.00 39.77           C  
ATOM   1377  OD1 ASN A 387      34.425  30.548   9.509  1.00 32.00           O  
ATOM   1378  ND2 ASN A 387      35.271  30.517   7.427  1.00 28.22           N  
ATOM   1379  N   GLU A 388      35.845  35.248  10.550  1.00 19.66           N  
ATOM   1380  CA  GLU A 388      36.683  36.400  10.871  1.00 18.95           C  
ATOM   1381  C   GLU A 388      38.126  35.934  10.675  1.00 27.12           C  
ATOM   1382  O   GLU A 388      38.502  34.873  11.186  1.00 22.20           O  
ATOM   1383  CB  GLU A 388      36.510  36.815  12.331  1.00 23.16           C  
ATOM   1384  CG  GLU A 388      37.577  37.798  12.805  1.00 18.71           C  
ATOM   1385  CD  GLU A 388      37.617  37.965  14.329  1.00 20.83           C  
ATOM   1386  OE1 GLU A 388      36.559  37.840  14.980  1.00 17.30           O  
ATOM   1387  OE2 GLU A 388      38.705  38.245  14.878  1.00 15.29           O  
ATOM   1388  N   ILE A 389      38.926  36.688   9.920  1.00 22.24           N  
ATOM   1389  CA  ILE A 389      40.325  36.293   9.753  1.00 19.34           C  
ATOM   1390  C   ILE A 389      41.280  37.307  10.405  1.00 17.11           C  
ATOM   1391  O   ILE A 389      42.430  36.975  10.719  1.00 20.58           O  
ATOM   1392  CB  ILE A 389      40.711  36.038   8.255  1.00 28.43           C  
ATOM   1393  CG1 ILE A 389      40.533  37.290   7.411  1.00 28.06           C  
ATOM   1394  CG2 ILE A 389      39.842  34.915   7.677  1.00 30.83           C  
ATOM   1395  CD1 ILE A 389      41.001  37.083   5.957  1.00 41.40           C  
ATOM   1396  N   LEU A 390      40.795  38.526  10.634  1.00 17.99           N  
ATOM   1397  CA  LEU A 390      41.588  39.571  11.304  1.00 23.08           C  
ATOM   1398  C   LEU A 390      40.633  40.525  11.984  1.00 20.64           C  
ATOM   1399  O   LEU A 390      39.467  40.610  11.603  1.00 19.58           O  
ATOM   1400  CB  LEU A 390      42.428  40.384  10.312  1.00 21.26           C  
ATOM   1401  CG  LEU A 390      43.722  39.812   9.715  1.00 25.67           C  
ATOM   1402  CD1 LEU A 390      44.141  40.659   8.514  1.00 21.06           C  
ATOM   1403  CD2 LEU A 390      44.817  39.799  10.761  1.00 25.94           C  
ATOM   1404  N   HIS A 391      41.134  41.251  12.975  1.00 14.22           N  
ATOM   1405  CA  HIS A 391      40.317  42.235  13.690  1.00 20.03           C  
ATOM   1406  C   HIS A 391      41.212  43.334  14.203  1.00 19.48           C  
ATOM   1407  O   HIS A 391      42.430  43.173  14.237  1.00 20.66           O  
ATOM   1408  CB  HIS A 391      39.531  41.604  14.866  1.00 16.63           C  
ATOM   1409  CG  HIS A 391      40.363  41.231  16.059  1.00 15.74           C  
ATOM   1410  ND1 HIS A 391      41.286  40.213  16.040  1.00 18.45           N  
ATOM   1411  CD2 HIS A 391      40.365  41.712  17.330  1.00 18.75           C  
ATOM   1412  CE1 HIS A 391      41.822  40.077  17.243  1.00 19.36           C  
ATOM   1413  NE2 HIS A 391      41.278  40.975  18.044  1.00 18.84           N  
ATOM   1414  N   ALA A 392      40.609  44.461  14.574  1.00 14.52           N  
ATOM   1415  CA  ALA A 392      41.358  45.596  15.113  1.00 20.72           C  
ATOM   1416  C   ALA A 392      40.347  46.500  15.785  1.00 19.04           C  
ATOM   1417  O   ALA A 392      39.158  46.435  15.488  1.00 19.43           O  
ATOM   1418  CB  ALA A 392      42.079  46.367  13.992  1.00 14.46           C  
ATOM   1419  N   TYR A 393      40.807  47.343  16.697  1.00 14.01           N  
ATOM   1420  CA  TYR A 393      39.889  48.250  17.347  1.00 19.07           C  
ATOM   1421  C   TYR A 393      40.586  49.458  17.927  1.00 18.95           C  
ATOM   1422  O   TYR A 393      41.815  49.477  18.067  1.00 20.92           O  
ATOM   1423  CB  TYR A 393      39.107  47.523  18.464  1.00 17.95           C  
ATOM   1424  CG  TYR A 393      39.986  46.823  19.491  1.00 20.66           C  
ATOM   1425  CD1 TYR A 393      40.623  47.550  20.497  1.00 23.50           C  
ATOM   1426  CD2 TYR A 393      40.219  45.450  19.420  1.00 21.80           C  
ATOM   1427  CE1 TYR A 393      41.469  46.944  21.396  1.00 19.38           C  
ATOM   1428  CE2 TYR A 393      41.077  44.815  20.325  1.00 21.01           C  
ATOM   1429  CZ  TYR A 393      41.696  45.582  21.309  1.00 28.42           C  
ATOM   1430  OH  TYR A 393      42.548  45.010  22.199  1.00 21.84           O  
ATOM   1431  N   ILE A 394      39.778  50.483  18.198  1.00 15.76           N  
ATOM   1432  CA  ILE A 394      40.224  51.679  18.885  1.00 16.14           C  
ATOM   1433  C   ILE A 394      39.749  51.343  20.306  1.00 18.39           C  
ATOM   1434  O   ILE A 394      38.549  51.259  20.587  1.00 18.94           O  
ATOM   1435  CB  ILE A 394      39.537  52.921  18.381  1.00 17.52           C  
ATOM   1436  CG1 ILE A 394      40.033  53.205  16.953  1.00 21.49           C  
ATOM   1437  CG2 ILE A 394      39.873  54.122  19.326  1.00 19.97           C  
ATOM   1438  CD1 ILE A 394      39.341  54.348  16.268  1.00 21.67           C  
ATOM   1439  N   LYS A 395      40.718  51.107  21.172  1.00 18.64           N  
ATOM   1440  CA  LYS A 395      40.478  50.688  22.546  1.00 17.94           C  
ATOM   1441  C   LYS A 395      39.489  51.537  23.318  1.00 20.77           C  
ATOM   1442  O   LYS A 395      38.640  51.020  24.047  1.00 21.79           O  
ATOM   1443  CB  LYS A 395      41.837  50.600  23.255  1.00 22.50           C  
ATOM   1444  CG  LYS A 395      41.826  49.926  24.616  1.00 22.33           C  
ATOM   1445  CD  LYS A 395      41.873  50.959  25.687  1.00 25.43           C  
ATOM   1446  CE  LYS A 395      42.040  50.344  27.086  1.00 29.44           C  
ATOM   1447  NZ  LYS A 395      42.113  51.447  28.097  1.00 24.76           N  
ATOM   1448  N   GLN A 396      39.591  52.848  23.186  1.00 18.63           N  
ATOM   1449  CA  GLN A 396      38.631  53.697  23.864  1.00 18.59           C  
ATOM   1450  C   GLN A 396      38.230  54.875  23.005  1.00 17.57           C  
ATOM   1451  O   GLN A 396      39.077  55.601  22.487  1.00 18.93           O  
ATOM   1452  CB  GLN A 396      39.165  54.230  25.213  1.00 17.43           C  
ATOM   1453  CG  GLN A 396      38.266  55.326  25.805  1.00 16.49           C  
ATOM   1454  CD  GLN A 396      38.862  55.955  27.048  1.00 29.09           C  
ATOM   1455  OE1 GLN A 396      38.979  55.286  28.057  1.00 22.82           O  
ATOM   1456  NE2 GLN A 396      39.263  57.240  26.973  1.00 18.40           N  
ATOM   1457  N   VAL A 397      36.921  55.046  22.875  1.00 19.71           N  
ATOM   1458  CA  VAL A 397      36.348  56.146  22.143  1.00 13.62           C  
ATOM   1459  C   VAL A 397      35.468  56.924  23.123  1.00 20.07           C  
ATOM   1460  O   VAL A 397      34.624  56.347  23.837  1.00 17.75           O  
ATOM   1461  CB  VAL A 397      35.475  55.646  20.970  1.00 17.29           C  
ATOM   1462  CG1 VAL A 397      34.717  56.814  20.359  1.00 19.84           C  
ATOM   1463  CG2 VAL A 397      36.344  54.973  19.915  1.00 15.44           C  
ATOM   1464  N   ARG A 398      35.673  58.231  23.192  1.00 16.98           N  
ATOM   1465  CA  ARG A 398      34.833  59.039  24.062  1.00 22.43           C  
ATOM   1466  C   ARG A 398      34.193  60.138  23.236  1.00 22.72           C  
ATOM   1467  O   ARG A 398      34.867  60.798  22.456  1.00 18.89           O  
ATOM   1468  CB  ARG A 398      35.645  59.638  25.222  1.00 19.53           C  
ATOM   1469  CG  ARG A 398      35.992  58.635  26.300  1.00 20.56           C  
ATOM   1470  CD  ARG A 398      36.567  59.343  27.534  1.00 29.71           C  
ATOM   1471  NE  ARG A 398      35.538  60.132  28.206  1.00 26.96           N  
ATOM   1472  CZ  ARG A 398      35.784  61.167  28.995  1.00 34.78           C  
ATOM   1473  NH1 ARG A 398      37.032  61.553  29.218  1.00 28.19           N  
ATOM   1474  NH2 ARG A 398      34.780  61.808  29.570  1.00 36.64           N  
ATOM   1475  N   ILE A 399      32.884  60.307  23.391  1.00 19.52           N  
ATOM   1476  CA  ILE A 399      32.147  61.323  22.660  1.00 22.11           C  
ATOM   1477  C   ILE A 399      31.811  62.373  23.718  1.00 24.09           C  
ATOM   1478  O   ILE A 399      30.920  62.189  24.551  1.00 22.00           O  
ATOM   1479  CB  ILE A 399      30.893  60.707  22.005  1.00 20.22           C  
ATOM   1480  CG1 ILE A 399      31.318  59.578  21.049  1.00 22.80           C  
ATOM   1481  CG2 ILE A 399      30.160  61.773  21.195  1.00 20.02           C  
ATOM   1482  CD1 ILE A 399      30.561  58.302  21.236  1.00 27.85           C  
ATOM   1483  N   VAL A 400      32.557  63.467  23.671  1.00 18.88           N  
ATOM   1484  CA  VAL A 400      32.480  64.532  24.661  1.00 17.88           C  
ATOM   1485  C   VAL A 400      32.316  65.910  24.042  1.00 24.91           C  
ATOM   1486  O   VAL A 400      32.354  66.056  22.833  1.00 21.66           O  
ATOM   1487  CB  VAL A 400      33.778  64.539  25.470  1.00 24.96           C  
ATOM   1488  CG1 VAL A 400      33.980  63.202  26.141  1.00 23.16           C  
ATOM   1489  CG2 VAL A 400      34.965  64.821  24.516  1.00 17.36           C  
ATOM   1490  N   ALA A 401      32.189  66.925  24.893  1.00 25.34           N  
ATOM   1491  CA  ALA A 401      32.011  68.310  24.450  1.00 23.74           C  
ATOM   1492  C   ALA A 401      33.312  68.996  23.993  1.00 21.45           C  
ATOM   1493  O   ALA A 401      33.332  69.756  23.019  1.00 24.80           O  
ATOM   1494  CB  ALA A 401      31.373  69.121  25.590  1.00 25.58           C  
ATOM   1495  N   TYR A 402      34.402  68.717  24.694  1.00 25.44           N  
ATOM   1496  CA  TYR A 402      35.689  69.330  24.380  1.00 23.74           C  
ATOM   1497  C   TYR A 402      36.772  68.256  24.226  1.00 23.95           C  
ATOM   1498  O   TYR A 402      37.592  68.034  25.126  1.00 19.62           O  
ATOM   1499  CB  TYR A 402      36.040  70.309  25.504  1.00 25.65           C  
ATOM   1500  CG  TYR A 402      35.047  71.441  25.584  1.00 27.06           C  
ATOM   1501  CD1 TYR A 402      35.017  72.435  24.602  1.00 28.65           C  
ATOM   1502  CD2 TYR A 402      34.106  71.497  26.613  1.00 21.06           C  
ATOM   1503  CE1 TYR A 402      34.055  73.478  24.641  1.00 30.16           C  
ATOM   1504  CE2 TYR A 402      33.137  72.523  26.668  1.00 27.90           C  
ATOM   1505  CZ  TYR A 402      33.122  73.501  25.683  1.00 32.01           C  
ATOM   1506  OH  TYR A 402      32.171  74.491  25.727  1.00 44.49           O  
ATOM   1507  N   PRO A 403      36.789  67.575  23.073  1.00 22.48           N  
ATOM   1508  CA  PRO A 403      37.798  66.529  22.878  1.00 18.51           C  
ATOM   1509  C   PRO A 403      39.236  66.953  23.184  1.00 23.74           C  
ATOM   1510  O   PRO A 403      40.007  66.137  23.688  1.00 22.81           O  
ATOM   1511  CB  PRO A 403      37.582  66.090  21.410  1.00 20.18           C  
ATOM   1512  CG  PRO A 403      36.796  67.230  20.781  1.00 29.39           C  
ATOM   1513  CD  PRO A 403      35.904  67.703  21.902  1.00 22.69           C  
ATOM   1514  N   ARG A 404      39.613  68.207  22.899  1.00 16.51           N  
ATOM   1515  CA  ARG A 404      40.998  68.623  23.181  1.00 27.78           C  
ATOM   1516  C   ARG A 404      41.331  68.689  24.675  1.00 25.07           C  
ATOM   1517  O   ARG A 404      42.472  68.473  25.054  1.00 22.50           O  
ATOM   1518  CB  ARG A 404      41.340  69.955  22.487  1.00 23.15           C  
ATOM   1519  CG  ARG A 404      41.496  69.801  20.966  1.00 26.98           C  
ATOM   1520  CD  ARG A 404      42.771  68.996  20.579  1.00 19.77           C  
ATOM   1521  NE  ARG A 404      42.730  68.496  19.191  1.00 26.60           N  
ATOM   1522  CZ  ARG A 404      43.636  67.674  18.664  1.00 23.19           C  
ATOM   1523  NH1 ARG A 404      44.661  67.263  19.388  1.00 15.61           N  
ATOM   1524  NH2 ARG A 404      43.504  67.241  17.422  1.00 21.69           N  
ATOM   1525  N   ARG A 405      40.344  68.983  25.519  1.00 21.48           N  
ATOM   1526  CA  ARG A 405      40.581  69.002  26.960  1.00 17.91           C  
ATOM   1527  C   ARG A 405      40.949  67.584  27.419  1.00 18.17           C  
ATOM   1528  O   ARG A 405      41.996  67.365  28.040  1.00 16.06           O  
ATOM   1529  CB  ARG A 405      39.330  69.453  27.722  1.00 17.93           C  
ATOM   1530  CG  ARG A 405      39.377  69.173  29.236  1.00 22.45           C  
ATOM   1531  CD  ARG A 405      38.041  69.478  29.898  1.00 24.24           C  
ATOM   1532  NE  ARG A 405      37.618  70.858  29.650  1.00 22.60           N  
ATOM   1533  CZ  ARG A 405      36.386  71.314  29.878  1.00 28.57           C  
ATOM   1534  NH1 ARG A 405      36.081  72.580  29.635  1.00 21.96           N  
ATOM   1535  NH2 ARG A 405      35.449  70.503  30.344  1.00 23.45           N  
ATOM   1536  N   ASP A 406      40.099  66.619  27.078  1.00 15.53           N  
ATOM   1537  CA  ASP A 406      40.318  65.240  27.490  1.00 19.25           C  
ATOM   1538  C   ASP A 406      41.585  64.630  26.881  1.00 21.94           C  
ATOM   1539  O   ASP A 406      42.332  63.916  27.557  1.00 21.24           O  
ATOM   1540  CB  ASP A 406      39.076  64.405  27.158  1.00 19.88           C  
ATOM   1541  CG  ASP A 406      37.849  64.846  27.967  1.00 26.33           C  
ATOM   1542  OD1 ASP A 406      37.985  64.952  29.190  1.00 33.70           O  
ATOM   1543  OD2 ASP A 406      36.766  65.080  27.394  1.00 28.64           O  
ATOM   1544  N   TRP A 407      41.817  64.912  25.607  1.00 17.73           N  
ATOM   1545  CA  TRP A 407      43.017  64.440  24.920  1.00 19.65           C  
ATOM   1546  C   TRP A 407      44.265  64.990  25.624  1.00 16.78           C  
ATOM   1547  O   TRP A 407      45.237  64.256  25.863  1.00 20.03           O  
ATOM   1548  CB  TRP A 407      43.029  64.939  23.474  1.00 16.10           C  
ATOM   1549  CG  TRP A 407      44.395  64.874  22.793  1.00 21.46           C  
ATOM   1550  CD1 TRP A 407      44.981  63.772  22.230  1.00 28.14           C  
ATOM   1551  CD2 TRP A 407      45.289  65.974  22.540  1.00 22.73           C  
ATOM   1552  NE1 TRP A 407      46.176  64.120  21.635  1.00 20.00           N  
ATOM   1553  CE2 TRP A 407      46.388  65.462  21.811  1.00 20.41           C  
ATOM   1554  CE3 TRP A 407      45.264  67.341  22.855  1.00 25.71           C  
ATOM   1555  CZ2 TRP A 407      47.457  66.270  21.390  1.00 24.43           C  
ATOM   1556  CZ3 TRP A 407      46.331  68.148  22.436  1.00 19.38           C  
ATOM   1557  CH2 TRP A 407      47.411  67.608  21.712  1.00 17.37           C  
ATOM   1558  N   LYS A 408      44.252  66.283  25.943  1.00 20.89           N  
ATOM   1559  CA  LYS A 408      45.418  66.887  26.584  1.00 17.76           C  
ATOM   1560  C   LYS A 408      45.672  66.301  27.966  1.00 24.79           C  
ATOM   1561  O   LYS A 408      46.834  66.028  28.340  1.00 19.90           O  
ATOM   1562  CB  LYS A 408      45.263  68.408  26.659  1.00 23.83           C  
ATOM   1563  CG  LYS A 408      46.384  69.158  27.408  1.00 21.26           C  
ATOM   1564  CD  LYS A 408      47.797  68.871  26.861  1.00 29.54           C  
ATOM   1565  CE  LYS A 408      48.000  69.297  25.421  1.00 22.68           C  
ATOM   1566  NZ  LYS A 408      49.490  69.535  25.151  1.00 30.22           N  
ATOM   1567  N   ASN A 409      44.600  66.112  28.729  1.00 20.80           N  
ATOM   1568  CA  ASN A 409      44.734  65.525  30.057  1.00 21.70           C  
ATOM   1569  C   ASN A 409      45.316  64.125  29.898  1.00 24.18           C  
ATOM   1570  O   ASN A 409      46.199  63.716  30.649  1.00 20.21           O  
ATOM   1571  CB  ASN A 409      43.373  65.428  30.764  1.00 20.05           C  
ATOM   1572  CG  ASN A 409      42.901  66.769  31.294  1.00 19.29           C  
ATOM   1573  OD1 ASN A 409      43.692  67.681  31.433  1.00 20.41           O  
ATOM   1574  ND2 ASN A 409      41.614  66.877  31.619  1.00 18.50           N  
ATOM   1575  N   PHE A 410      44.802  63.378  28.929  1.00 19.98           N  
ATOM   1576  CA  PHE A 410      45.306  62.025  28.710  1.00 24.12           C  
ATOM   1577  C   PHE A 410      46.804  62.003  28.387  1.00 21.50           C  
ATOM   1578  O   PHE A 410      47.564  61.230  28.978  1.00 21.87           O  
ATOM   1579  CB  PHE A 410      44.538  61.346  27.571  1.00 22.01           C  
ATOM   1580  CG  PHE A 410      45.031  59.954  27.245  1.00 28.07           C  
ATOM   1581  CD1 PHE A 410      44.523  58.848  27.911  1.00 30.63           C  
ATOM   1582  CD2 PHE A 410      45.974  59.753  26.242  1.00 24.05           C  
ATOM   1583  CE1 PHE A 410      44.941  57.558  27.571  1.00 39.71           C  
ATOM   1584  CE2 PHE A 410      46.398  58.466  25.895  1.00 25.92           C  
ATOM   1585  CZ  PHE A 410      45.881  57.377  26.554  1.00 25.67           C  
ATOM   1586  N   CYS A 411      47.228  62.837  27.438  1.00 20.22           N  
ATOM   1587  CA  CYS A 411      48.631  62.886  27.063  1.00 16.77           C  
ATOM   1588  C   CYS A 411      49.542  63.274  28.240  1.00 26.75           C  
ATOM   1589  O   CYS A 411      50.571  62.627  28.469  1.00 22.85           O  
ATOM   1590  CB  CYS A 411      48.822  63.851  25.886  1.00 18.80           C  
ATOM   1591  SG  CYS A 411      48.071  63.229  24.359  1.00 26.75           S  
ATOM   1592  N   GLU A 412      49.159  64.303  28.999  1.00 21.54           N  
ATOM   1593  CA  GLU A 412      49.966  64.738  30.152  1.00 23.18           C  
ATOM   1594  C   GLU A 412      50.067  63.628  31.184  1.00 29.76           C  
ATOM   1595  O   GLU A 412      51.132  63.416  31.753  1.00 26.62           O  
ATOM   1596  CB  GLU A 412      49.367  65.988  30.822  1.00 21.61           C  
ATOM   1597  CG  GLU A 412      49.455  67.254  29.972  1.00 32.26           C  
ATOM   1598  CD  GLU A 412      50.873  67.810  29.885  1.00 47.05           C  
ATOM   1599  OE1 GLU A 412      51.425  68.192  30.937  1.00 46.15           O  
ATOM   1600  OE2 GLU A 412      51.436  67.862  28.774  1.00 44.92           O  
ATOM   1601  N   ARG A 413      48.963  62.928  31.445  1.00 22.34           N  
ATOM   1602  CA  ARG A 413      48.998  61.842  32.418  1.00 24.12           C  
ATOM   1603  C   ARG A 413      49.906  60.698  31.940  1.00 37.31           C  
ATOM   1604  O   ARG A 413      50.684  60.149  32.724  1.00 29.36           O  
ATOM   1605  CB  ARG A 413      47.581  61.318  32.707  1.00 34.23           C  
ATOM   1606  CG  ARG A 413      46.787  62.230  33.629  1.00 53.13           C  
ATOM   1607  CD  ARG A 413      45.443  61.641  34.057  1.00 65.03           C  
ATOM   1608  NE  ARG A 413      44.388  61.762  33.043  1.00 70.35           N  
ATOM   1609  CZ  ARG A 413      44.166  60.871  32.078  1.00 69.50           C  
ATOM   1610  NH1 ARG A 413      44.925  59.786  31.989  1.00 74.68           N  
ATOM   1611  NH2 ARG A 413      43.178  61.054  31.209  1.00 29.98           N  
ATOM   1612  N   GLU A 414      49.817  60.350  30.656  1.00 25.16           N  
ATOM   1613  CA  GLU A 414      50.657  59.290  30.101  1.00 34.38           C  
ATOM   1614  C   GLU A 414      52.135  59.657  30.127  1.00 37.14           C  
ATOM   1615  O   GLU A 414      52.957  58.867  30.589  1.00 32.76           O  
ATOM   1616  CB  GLU A 414      50.261  58.975  28.656  1.00 23.78           C  
ATOM   1617  CG  GLU A 414      48.943  58.281  28.526  1.00 28.14           C  
ATOM   1618  CD  GLU A 414      48.966  56.880  29.105  1.00 27.40           C  
ATOM   1619  OE1 GLU A 414      49.819  56.082  28.687  1.00 32.15           O  
ATOM   1620  OE2 GLU A 414      48.122  56.568  29.962  1.00 37.09           O  
ATOM   1621  N   ASP A 415      52.470  60.848  29.628  1.00 32.56           N  
ATOM   1622  CA  ASP A 415      53.856  61.300  29.584  1.00 31.89           C  
ATOM   1623  C   ASP A 415      54.448  61.468  30.973  1.00 44.28           C  
ATOM   1624  O   ASP A 415      55.660  61.427  31.144  1.00 48.13           O  
ATOM   1625  CB  ASP A 415      53.987  62.632  28.844  1.00 28.24           C  
ATOM   1626  CG  ASP A 415      53.621  62.531  27.372  1.00 30.77           C  
ATOM   1627  OD1 ASP A 415      53.658  61.419  26.808  1.00 29.19           O  
ATOM   1628  OD2 ASP A 415      53.317  63.577  26.772  1.00 31.82           O  
ATOM   1629  N   ALA A 416      53.596  61.678  31.964  1.00 35.15           N  
ATOM   1630  CA  ALA A 416      54.081  61.843  33.320  1.00 52.53           C  
ATOM   1631  C   ALA A 416      54.603  60.494  33.785  1.00 61.79           C  
ATOM   1632  O   ALA A 416      55.479  60.422  34.645  1.00 64.73           O  
ATOM   1633  CB  ALA A 416      52.966  62.319  34.230  1.00 50.97           C  
ATOM   1634  N   LYS A 417      54.063  59.426  33.207  1.00 65.92           N  
ATOM   1635  CA  LYS A 417      54.485  58.079  33.561  1.00 72.79           C  
ATOM   1636  C   LYS A 417      55.948  57.889  33.174  1.00 79.57           C  
ATOM   1637  O   LYS A 417      56.272  57.705  31.998  1.00 79.15           O  
ATOM   1638  CB  LYS A 417      53.612  57.046  32.849  1.00 75.69           C  
ATOM   1639  CG  LYS A 417      52.124  57.238  33.109  1.00 85.21           C  
ATOM   1640  CD  LYS A 417      51.299  56.009  32.746  1.00 84.77           C  
ATOM   1641  CE  LYS A 417      51.427  55.642  31.277  1.00 84.91           C  
ATOM   1642  NZ  LYS A 417      50.554  54.475  30.943  1.00 92.09           N  
ATOM   1643  N   GLN A 418      56.821  57.945  34.178  1.00 81.57           N  
ATOM   1644  CA  GLN A 418      58.263  57.802  33.986  1.00 87.32           C  
ATOM   1645  C   GLN A 418      58.619  56.554  33.185  1.00 88.98           C  
ATOM   1646  O   GLN A 418      59.134  55.579  33.735  1.00 91.97           O  
ATOM   1647  CB  GLN A 418      58.972  57.751  35.345  1.00 89.68           C  
ATOM   1648  CG  GLN A 418      58.607  58.893  36.282  1.00 90.75           C  
ATOM   1649  CD  GLN A 418      58.775  60.248  35.631  1.00 91.87           C  
ATOM   1650  OE1 GLN A 418      59.830  60.556  35.079  1.00 94.83           O  
ATOM   1651  NE2 GLN A 418      57.734  61.069  35.696  1.00 92.85           N  
ATOM   1652  OXT GLN A 418      58.375  56.567  31.961  1.00 35.93           O  
TER    1653      GLN A 418                                                      
HETATM 1654 ZN    ZN A 201      21.928  60.823  23.121  1.00 27.16          ZN  
HETATM 1655  O   HOH A   1      39.556  60.616  28.531  1.00 19.07           O  
HETATM 1656  O   HOH A   2      30.823  62.247  15.612  1.00 19.34           O  
HETATM 1657  O   HOH A   3      26.510  50.963  18.922  1.00 20.07           O  
HETATM 1658  O   HOH A   4      43.722  50.106  20.269  1.00 20.37           O  
HETATM 1659  O   HOH A   5      41.370  62.479  29.648  1.00 21.64           O  
HETATM 1660  O   HOH A   6      28.039  47.368  17.197  1.00 22.47           O  
HETATM 1661  O   HOH A   7      34.556  55.296  26.294  1.00 22.83           O  
HETATM 1662  O   HOH A   8      49.635  70.351  22.487  1.00 22.83           O  
HETATM 1663  O   HOH A   9      37.322  59.917   5.300  1.00 23.23           O  
HETATM 1664  O   HOH A  10      26.081  44.295   8.485  1.00 23.78           O  
HETATM 1665  O   HOH A  11      46.335  51.194   0.333  1.00 23.84           O  
HETATM 1666  O   HOH A  12      28.308  40.957   7.469  1.00 23.87           O  
HETATM 1667  O   HOH A  13      34.829  52.208   2.830  1.00 24.11           O  
HETATM 1668  O   HOH A  14      56.085  60.359  26.015  1.00 24.53           O  
HETATM 1669  O   HOH A  15      39.872  64.387  30.979  1.00 25.07           O  
HETATM 1670  O   HOH A  16      30.903  39.909   6.637  1.00 25.40           O  
HETATM 1671  O   HOH A  17      24.467  51.209  17.210  1.00 25.63           O  
HETATM 1672  O   HOH A  18      31.788  37.025  22.553  1.00 26.29           O  
HETATM 1673  O   HOH A  19      29.006  56.679   1.850  1.00 26.40           O  
HETATM 1674  O   HOH A  20      29.687  44.359  27.079  1.00 26.45           O  
HETATM 1675  O   HOH A  21      39.154  58.136  24.463  1.00 26.54           O  
HETATM 1676  O   HOH A  22      23.737  44.722  20.997  1.00 26.73           O  
HETATM 1677  O   HOH A  23      43.749  46.828  17.208  1.00 27.04           O  
HETATM 1678  O   HOH A  24      42.844  42.492  22.451  1.00 27.09           O  
HETATM 1679  O   HOH A  25      31.614  58.241  24.895  1.00 27.39           O  
HETATM 1680  O   HOH A  26      39.417  58.310   5.887  1.00 27.80           O  
HETATM 1681  O   HOH A  27      24.050  46.630  24.527  1.00 28.32           O  
HETATM 1682  O   HOH A  28      46.097  51.712  27.059  1.00 28.39           O  
HETATM 1683  O   HOH A  29      32.127  31.058  10.870  1.00 28.46           O  
HETATM 1684  O   HOH A  30      28.997  63.719  26.107  1.00 28.47           O  
HETATM 1685  O   HOH A  31      29.833  65.839  21.604  1.00 28.72           O  
HETATM 1686  O   HOH A  32      46.557  45.384  -3.327  1.00 28.80           O  
HETATM 1687  O   HOH A  33      33.913  38.106  14.738  1.00 29.59           O  
HETATM 1688  O   HOH A  34      44.288  49.167  15.362  1.00 29.92           O  
HETATM 1689  O   HOH A  35      28.095  59.488   2.365  1.00 29.98           O  
HETATM 1690  O   HOH A  36      24.809  51.805   1.187  1.00 30.20           O  
HETATM 1691  O   HOH A  37      28.766  41.693  13.547  1.00 30.52           O  
HETATM 1692  O   HOH A  38      45.565  69.260  30.566  1.00 30.76           O  
HETATM 1693  O   HOH A  39      24.088  42.384  12.608  1.00 31.40           O  
HETATM 1694  O   HOH A  40      17.299  57.377  26.719  1.00 32.55           O  
HETATM 1695  O   HOH A  41      38.233  70.746  22.600  1.00 32.84           O  
HETATM 1696  O   HOH A  42      42.777  48.610  -1.549  1.00 32.90           O  
HETATM 1697  O   HOH A  43      40.385  58.367  29.431  1.00 33.08           O  
HETATM 1698  O   HOH A  44      34.905  67.233  27.139  1.00 33.12           O  
HETATM 1699  O   HOH A  45      48.781  45.265   2.398  1.00 33.80           O  
HETATM 1700  O   HOH A  46      46.628  42.832  13.441  1.00 34.19           O  
HETATM 1701  O   HOH A  47      24.454  43.817   6.378  1.00 34.19           O  
HETATM 1702  O   HOH A  48      44.989  52.534   9.522  1.00 34.24           O  
HETATM 1703  O   HOH A  49      40.306  32.814  10.909  1.00 34.76           O  
HETATM 1704  O   HOH A  50      33.190  41.222  -0.722  1.00 34.83           O  
HETATM 1705  O   HOH A  51      43.774  54.396  29.609  1.00 34.96           O  
HETATM 1706  O   HOH A  52      44.836  64.104  17.204  1.00 34.96           O  
HETATM 1707  O   HOH A  53      22.794  50.487  19.106  1.00 35.00           O  
HETATM 1708  O   HOH A  54      28.830  52.971  -0.466  1.00 35.43           O  
HETATM 1709  O   HOH A  55      25.473  55.269   7.100  1.00 35.50           O  
HETATM 1710  O   HOH A  56      32.985  71.690  30.221  1.00 35.66           O  
HETATM 1711  O   HOH A  57      47.170  58.977   8.725  1.00 35.78           O  
HETATM 1712  O   HOH A  58      30.934  37.049   9.391  1.00 36.03           O  
HETATM 1713  O   HOH A  59      18.567  52.343  22.283  1.00 36.18           O  
HETATM 1714  O   HOH A  60      40.058  44.365  28.111  1.00 36.49           O  
HETATM 1715  O   HOH A  61      38.140  75.825  18.017  1.00 36.51           O  
HETATM 1716  O   HOH A  62      41.369  73.366  17.615  1.00 37.34           O  
HETATM 1717  O   HOH A  63      32.157  67.035  10.588  1.00 37.35           O  
HETATM 1718  O   HOH A  64      32.311  40.027  15.685  1.00 37.38           O  
HETATM 1719  O   HOH A  65      20.951  52.079  19.882  1.00 37.55           O  
HETATM 1720  O   HOH A  66      25.634  41.965  10.088  1.00 37.68           O  
HETATM 1721  O   HOH A  67      24.806  51.533  25.922  1.00 37.80           O  
HETATM 1722  O   HOH A  68      41.669  39.740  -1.499  1.00 37.95           O  
HETATM 1723  O   HOH A  69      27.982  35.310  24.040  1.00 37.97           O  
HETATM 1724  O   HOH A  70      36.350  71.364  21.131  1.00 38.15           O  
HETATM 1725  O   HOH A  71      57.817  62.107  25.922  1.00 38.16           O  
HETATM 1726  O   HOH A  72      40.482  49.751  -1.103  1.00 38.34           O  
HETATM 1727  O   HOH A  73      40.823  58.514   3.639  1.00 38.42           O  
HETATM 1728  O   HOH A  74      49.827  52.121   4.468  1.00 38.77           O  
HETATM 1729  O   HOH A  75      38.896  72.462  13.867  1.00 38.86           O  
HETATM 1730  O   HOH A  76      21.362  42.272  19.331  1.00 39.13           O  
HETATM 1731  O   HOH A  77      19.487  49.269  14.515  1.00 39.28           O  
HETATM 1732  O   HOH A  78      29.063  68.446  21.510  1.00 39.35           O  
HETATM 1733  O   HOH A  79      24.206  46.192  -0.843  1.00 39.49           O  
HETATM 1734  O   HOH A  80      53.070  65.419  31.494  1.00 39.63           O  
HETATM 1735  O   HOH A  81      31.675  54.487  -3.654  1.00 39.66           O  
HETATM 1736  O   HOH A  82      36.316  58.858   3.231  1.00 39.92           O  
HETATM 1737  O   HOH A  83      47.266  47.928   3.668  1.00 40.13           O  
HETATM 1738  O   HOH A  84      47.375  57.475   5.971  1.00 40.51           O  
HETATM 1739  O   HOH A  85      36.539  63.275   7.701  1.00 40.95           O  
HETATM 1740  O   HOH A  86      32.730  38.213   0.804  1.00 40.98           O  
HETATM 1741  O   HOH A  87      43.035  41.605  24.946  1.00 41.07           O  
HETATM 1742  O   HOH A  88      20.034  62.121  16.241  1.00 41.19           O  
HETATM 1743  O   HOH A  89      29.535  55.530  -0.641  1.00 41.22           O  
HETATM 1744  O   HOH A  90      35.180  50.663  31.544  1.00 41.77           O  
HETATM 1745  O   HOH A  91      29.731  52.809  -3.375  1.00 41.78           O  
HETATM 1746  O   HOH A  92      32.685  38.056   3.480  1.00 41.91           O  
HETATM 1747  O   HOH A  93      48.025  41.323   1.544  1.00 41.96           O  
HETATM 1748  O   HOH A  94      19.436  60.842  27.723  1.00 42.12           O  
HETATM 1749  O   HOH A  95      43.624  33.633  12.789  1.00 42.49           O  
HETATM 1750  O   HOH A  96      32.359  56.915  27.351  1.00 42.52           O  
HETATM 1751  O   HOH A  97      18.679  44.593  11.448  1.00 42.95           O  
HETATM 1752  O   HOH A  98      47.492  51.846  29.531  1.00 43.05           O  
HETATM 1753  O   HOH A  99      32.758  48.262  -2.624  1.00 43.11           O  
HETATM 1754  O   HOH A 100      35.324  48.489  -3.368  1.00 43.25           O  
HETATM 1755  O   HOH A 101      35.332  63.341   4.628  1.00 43.39           O  
HETATM 1756  O   HOH A 102      30.703  46.694  -4.278  1.00 43.43           O  
HETATM 1757  O   HOH A 103      29.685  33.724  27.772  1.00 43.96           O  
HETATM 1758  O   HOH A 104      51.283  45.481   3.511  1.00 44.43           O  
HETATM 1759  O   HOH A 105      45.140  56.509  14.565  1.00 44.61           O  
HETATM 1760  O   HOH A 106      26.303  40.169  27.476  1.00 44.75           O  
HETATM 1761  O   HOH A 107      46.637  65.402  18.051  1.00 45.20           O  
HETATM 1762  O   HOH A 108      21.840  47.292   1.573  1.00 45.55           O  
HETATM 1763  O   HOH A 109      23.805  48.349   0.594  1.00 45.85           O  
HETATM 1764  O   HOH A 110      51.649  70.550  26.956  1.00 46.40           O  
HETATM 1765  O   HOH A 111      51.504  65.685  26.978  1.00 46.81           O  
HETATM 1766  O   HOH A 112      35.851  66.459  10.316  1.00 46.87           O  
HETATM 1767  O   HOH A 113       8.635  63.238  19.643  1.00 46.90           O  
HETATM 1768  O   HOH A 114      39.371  52.593  28.638  1.00 46.93           O  
HETATM 1769  O   HOH A 115      36.268  39.548  30.657  1.00 47.15           O  
HETATM 1770  O   HOH A 116      50.384  66.814  24.531  1.00 47.58           O  
HETATM 1771  O   HOH A 117      28.346  68.376  18.119  1.00 47.82           O  
HETATM 1772  O   HOH A 118      45.460  45.930  15.526  1.00 48.07           O  
HETATM 1773  O   HOH A 119      34.538  73.132  20.720  1.00 48.08           O  
HETATM 1774  O   HOH A 120      21.973  50.687  27.482  1.00 48.48           O  
HETATM 1775  O   HOH A 121      44.323  33.502   8.350  1.00 48.81           O  
HETATM 1776  O   HOH A 122      31.022  44.435  29.601  1.00 49.29           O  
HETATM 1777  O   HOH A 123      36.743  30.041   4.317  1.00 49.35           O  
HETATM 1778  O   HOH A 124      27.257  40.693  11.611  1.00 49.56           O  
HETATM 1779  O   HOH A 125      31.137  65.397   3.788  1.00 50.60           O  
HETATM 1780  O   HOH A 126      40.054  31.150   8.823  1.00 50.67           O  
HETATM 1781  O   HOH A 127      46.020  58.693   3.492  1.00 50.94           O  
HETATM 1782  O   HOH A 128      29.856  30.805   9.280  1.00 51.32           O  
HETATM 1783  O   HOH A 129      28.867  40.183  16.112  1.00 51.37           O  
HETATM 1784  O   HOH A 130      47.378  39.739  13.514  1.00 51.64           O  
HETATM 1785  O   HOH A 131      39.743  31.716   6.027  1.00 51.90           O  
HETATM 1786  O   HOH A 132      45.508  56.371   8.586  1.00 52.25           O  
HETATM 1787  O   HOH A 133      20.048  56.810  27.627  1.00 52.47           O  
HETATM 1788  O   HOH A 134      34.664  65.161  29.121  1.00 52.76           O  
HETATM 1789  O   HOH A 135      21.777  47.928   4.519  1.00 53.33           O  
HETATM 1790  O   HOH A 136      48.873  51.537  13.438  1.00 54.59           O  
HETATM 1791  O   HOH A 137      54.087  68.284  28.809  1.00 55.51           O  
HETATM 1792  O   HOH A 138      16.448  50.174  13.016  1.00 56.92           O  
HETATM 1793  O   HOH A 139      18.578  42.477   9.284  1.00 57.20           O  
HETATM 1794  O   HOH A 140      21.402  45.731  21.262  1.00 57.83           O  
HETATM 1795  O   HOH A 141      38.712  58.519   1.648  1.00 57.86           O  
HETATM 1796  O   HOH A 142      45.062  47.674  19.520  1.00 58.56           O  
HETATM 1797  O   HOH A 143      38.271  45.300  30.135  1.00 58.64           O  
HETATM 1798  O   HOH A 144      41.880  52.510   0.018  1.00 59.59           O  
HETATM 1799  O   HOH A 145      43.484  57.893  30.828  1.00 59.83           O  
HETATM 1800  O   HOH A 146      12.520  57.148  20.576  1.00 59.87           O  
HETATM 1801  O   HOH A 147      30.645  55.167  28.436  1.00 59.90           O  
HETATM 1802  O   HOH A 148      38.593  62.258   4.279  1.00 60.02           O  
HETATM 1803  O   HOH A 149      46.409  58.117  30.967  1.00 60.07           O  
HETATM 1804  O   HOH A 150      44.959  68.728  11.826  1.00 60.27           O  
HETATM 1805  O   HOH A 151      24.902  60.622   9.113  1.00 62.56           O  
HETATM 1806  O   HOH A 152      38.002  38.116  32.469  1.00 62.85           O  
HETATM 1807  O   HOH A 153      15.204  52.875  11.936  1.00 63.71           O  
HETATM 1808  O   HOH A 154      25.282  68.568  26.282  1.00 65.45           O  
HETATM 1809  O   HOH A 155      51.584  71.956  16.712  1.00 67.07           O  
CONECT  715 1654                                                                
CONECT  739 1654                                                                
CONECT 1169 1654                                                                
CONECT 1202 1654                                                                
CONECT 1654  715  739 1169 1202                                                 
MASTER      255    0    1    6   11    0    1    6 1808    1    5   16          
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.