path: root/plip/test/pdb/3shy.pdb

HEADER    HYDROLASE/HYDROLASE INHIBITOR           17-JUN-11   3SHY              
TITLE     CRYSTAL STRUCTURE OF THE PDE5A1 CATALYTIC DOMAIN IN COMPLEX WITH NOVEL
TITLE    2 INHIBITORS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 535-860;                                      
COMPND   5 SYNONYM: PDE5A1, CGMP-BINDING CGMP-SPECIFIC PHOSPHODIESTERASE, CGB-  
COMPND   6 PDE;                                                                 
COMPND   7 EC: 3.1.4.35;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PDE5, PDE5A;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    PDE5A INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.T.CHEN,T.CHEN,Y.C.XU                                                
REVDAT   1   24-AUG-11 3SHY    0                                                
JRNL        AUTH   Z.XU,Z.LIU,T.CHEN,T.T.CHEN,Z.WANG,G.TIAN,J.SHI,X.WANG,Y.LU,  
JRNL        AUTH 2 X.YAN,G.WANG,H.JIANG,K.CHEN,S.WANG,Y.XU,J.SHEN,W.ZHU         
JRNL        TITL   UTILIZATION OF HALOGEN BOND IN LEAD OPTIMIZATION: A CASE     
JRNL        TITL 2 STUDY OF RATIONAL DESIGN OF POTENT PHOSPHODIESTERASE TYPE 5  
JRNL        TITL 3 (PDE5) INHIBITORS.                                           
JRNL        REF    J.MED.CHEM.                   V.  54  5607 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21714539                                                     
JRNL        DOI    10.1021/JM200644R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12511                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 608                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.3344 -  4.1997    0.99     3137   162  0.2103 0.2522        
REMARK   3     2  4.1997 -  3.3342    0.99     3040   162  0.1831 0.2501        
REMARK   3     3  3.3342 -  2.9129    0.97     2927   150  0.2361 0.2686        
REMARK   3     4  2.9129 -  2.6467    0.93     2799   134  0.2645 0.3097        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 51.95                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.51540                                              
REMARK   3    B22 (A**2) : 2.51540                                              
REMARK   3    B33 (A**2) : -5.03080                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           2354                                  
REMARK   3   ANGLE     :  1.191           3192                                  
REMARK   3   CHIRALITY :  0.071            368                                  
REMARK   3   PLANARITY :  0.005            403                                  
REMARK   3   DIHEDRAL  : 14.740            827                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066224.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12774                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.647                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.331                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19-20%(W/V) PEG 3350, 200MM MGSO4,       
REMARK 280  100MM TRIS-HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.97533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.95067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       87.95067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.97533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   514                                                      
REMARK 465     GLY A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     SER A   517                                                      
REMARK 465     HIS A   518                                                      
REMARK 465     HIS A   519                                                      
REMARK 465     HIS A   520                                                      
REMARK 465     HIS A   521                                                      
REMARK 465     HIS A   522                                                      
REMARK 465     HIS A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     SER A   525                                                      
REMARK 465     GLY A   526                                                      
REMARK 465     LEU A   527                                                      
REMARK 465     VAL A   528                                                      
REMARK 465     PRO A   529                                                      
REMARK 465     ARG A   530                                                      
REMARK 465     GLY A   531                                                      
REMARK 465     SER A   532                                                      
REMARK 465     HIS A   533                                                      
REMARK 465     MET A   534                                                      
REMARK 465     GLU A   535                                                      
REMARK 465     HIS A   670                                                      
REMARK 465     PRO A   671                                                      
REMARK 465     LEU A   672                                                      
REMARK 465     ALA A   673                                                      
REMARK 465     GLN A   674                                                      
REMARK 465     LEU A   675                                                      
REMARK 465     TYR A   676                                                      
REMARK 465     CYS A   677                                                      
REMARK 465     GLY A   790                                                      
REMARK 465     ASP A   791                                                      
REMARK 465     ARG A   792                                                      
REMARK 465     GLU A   793                                                      
REMARK 465     ARG A   794                                                      
REMARK 465     LYS A   795                                                      
REMARK 465     GLU A   796                                                      
REMARK 465     LEU A   797                                                      
REMARK 465     ASN A   798                                                      
REMARK 465     ILE A   799                                                      
REMARK 465     GLU A   800                                                      
REMARK 465     PRO A   801                                                      
REMARK 465     THR A   802                                                      
REMARK 465     ASP A   803                                                      
REMARK 465     LEU A   804                                                      
REMARK 465     MET A   805                                                      
REMARK 465     ASN A   806                                                      
REMARK 465     ARG A   807                                                      
REMARK 465     GLU A   808                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 536    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 538    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 540    CG   CD1  CD2                                       
REMARK 470     GLN A 541    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 543    CD1  CD2                                            
REMARK 470     GLN A 589    OE1  NE2                                            
REMARK 470     LYS A 591    CD   CE   NZ                                        
REMARK 470     GLU A 593    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 597    CZ   NH1  NH2                                       
REMARK 470     LYS A 604    CD   CE   NZ                                        
REMARK 470     LYS A 608    CD   CE   NZ                                        
REMARK 470     LYS A 633    CE   NZ                                             
REMARK 470     ASN A 636    CG   OD1  ND2                                       
REMARK 470     ASN A 662    OD1  ND2                                            
REMARK 470     SER A 663    OG                                                  
REMARK 470     TYR A 664    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 665    CB   CG1  CG2  CD1                                  
REMARK 470     GLN A 666    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG A 667    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     SER A 668    CB   OG                                             
REMARK 470     GLU A 669    CB   CG   CD   OE1  OE2                             
REMARK 470     ILE A 706    CD1                                                 
REMARK 470     GLU A 707    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 714    CG   CD   CE   NZ                                   
REMARK 470     LEU A 727    CD1  CD2                                            
REMARK 470     LYS A 730    CD   CE   NZ                                        
REMARK 470     LYS A 741    CG   CD   CE   NZ                                   
REMARK 470     ASN A 742    CG   OD1  ND2                                       
REMARK 470     GLN A 743    CD   OE1  NE2                                       
REMARK 470     LEU A 746    CG   CD1  CD2                                       
REMARK 470     GLU A 747    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 809    CG   CD   CE   NZ                                   
REMARK 470     LYS A 810    CG   CD   CE   NZ                                   
REMARK 470     ASN A 811    CG   OD1  ND2                                       
REMARK 470     LYS A 812    CG   CD   CE   NZ                                   
REMARK 470     ILE A 824    CD1                                                 
REMARK 470     LEU A 826    CD1  CD2                                            
REMARK 470     GLU A 837    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 851    CD   OE1  NE2                                       
REMARK 470     GLN A 859    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 860    OE1  NE2                                            
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    PHE A 561      150.50    -44.58                                   
REMARK 500    ASN A 583       17.35     84.25                                   
REMARK 500    GLN A 586      -72.67    -54.16                                   
REMARK 500    LYS A 630      -76.11    -85.87                                   
REMARK 500    ASN A 661       32.30    -95.46                                   
REMARK 500    ARG A 667     -114.55     41.45                                   
REMARK 500    ILE A 700        1.56    -62.07                                   
REMARK 500    ASN A 742       10.24     43.92                                   
REMARK 500    PRO A 841      -19.52    -48.92                                   
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 861  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 654   OD2                                                    
REMARK 620 2 ASP A 764   OD1 158.9                                              
REMARK 620 3 HIS A 653   NE2  81.4  83.0                                        
REMARK 620 4 HIS A 617   NE2  88.9  76.3  88.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 862  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A  11   O                                                      
REMARK 620 2 HOH A 864   O   150.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5FO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 861                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 862                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T9R   RELATED DB: PDB                                   
REMARK 900 PDE5A CATALYTIC DOMAIN COMPLEX WITH INHIBITORS                       
REMARK 900 RELATED ID: 3SHZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SIE   RELATED DB: PDB                                   
DBREF  3SHY A  535   860  UNP    O76074   PDE5A_HUMAN    535    860             
SEQADV 3SHY MET A  514  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY GLY A  515  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY SER A  516  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY SER A  517  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  518  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  519  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  520  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  521  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  522  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  523  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY SER A  524  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY SER A  525  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY GLY A  526  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY LEU A  527  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY VAL A  528  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY PRO A  529  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY ARG A  530  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY GLY A  531  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY SER A  532  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY HIS A  533  UNP  O76074              EXPRESSION TAG                 
SEQADV 3SHY MET A  534  UNP  O76074              EXPRESSION TAG                 
SEQRES   1 A  347  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  347  LEU VAL PRO ARG GLY SER HIS MET GLU GLU THR ARG GLU          
SEQRES   3 A  347  LEU GLN SER LEU ALA ALA ALA VAL VAL PRO SER ALA GLN          
SEQRES   4 A  347  THR LEU LYS ILE THR ASP PHE SER PHE SER ASP PHE GLU          
SEQRES   5 A  347  LEU SER ASP LEU GLU THR ALA LEU CYS THR ILE ARG MET          
SEQRES   6 A  347  PHE THR ASP LEU ASN LEU VAL GLN ASN PHE GLN MET LYS          
SEQRES   7 A  347  HIS GLU VAL LEU CYS ARG TRP ILE LEU SER VAL LYS LYS          
SEQRES   8 A  347  ASN TYR ARG LYS ASN VAL ALA TYR HIS ASN TRP ARG HIS          
SEQRES   9 A  347  ALA PHE ASN THR ALA GLN CYS MET PHE ALA ALA LEU LYS          
SEQRES  10 A  347  ALA GLY LYS ILE GLN ASN LYS LEU THR ASP LEU GLU ILE          
SEQRES  11 A  347  LEU ALA LEU LEU ILE ALA ALA LEU SER HIS ASP LEU ASP          
SEQRES  12 A  347  HIS ARG GLY VAL ASN ASN SER TYR ILE GLN ARG SER GLU          
SEQRES  13 A  347  HIS PRO LEU ALA GLN LEU TYR CYS HIS SER ILE MET GLU          
SEQRES  14 A  347  HIS HIS HIS PHE ASP GLN CYS LEU MET ILE LEU ASN SER          
SEQRES  15 A  347  PRO GLY ASN GLN ILE LEU SER GLY LEU SER ILE GLU GLU          
SEQRES  16 A  347  TYR LYS THR THR LEU LYS ILE ILE LYS GLN ALA ILE LEU          
SEQRES  17 A  347  ALA THR ASP LEU ALA LEU TYR ILE LYS ARG ARG GLY GLU          
SEQRES  18 A  347  PHE PHE GLU LEU ILE ARG LYS ASN GLN PHE ASN LEU GLU          
SEQRES  19 A  347  ASP PRO HIS GLN LYS GLU LEU PHE LEU ALA MET LEU MET          
SEQRES  20 A  347  THR ALA CYS ASP LEU SER ALA ILE THR LYS PRO TRP PRO          
SEQRES  21 A  347  ILE GLN GLN ARG ILE ALA GLU LEU VAL ALA THR GLU PHE          
SEQRES  22 A  347  PHE ASP GLN GLY ASP ARG GLU ARG LYS GLU LEU ASN ILE          
SEQRES  23 A  347  GLU PRO THR ASP LEU MET ASN ARG GLU LYS LYS ASN LYS          
SEQRES  24 A  347  ILE PRO SER MET GLN VAL GLY PHE ILE ASP ALA ILE CYS          
SEQRES  25 A  347  LEU GLN LEU TYR GLU ALA LEU THR HIS VAL SER GLU ASP          
SEQRES  26 A  347  CYS PHE PRO LEU LEU ASP GLY CYS ARG LYS ASN ARG GLN          
SEQRES  27 A  347  LYS TRP GLN ALA LEU ALA GLU GLN GLN                          
HET    5FO  A   1      30                                                       
HET     ZN  A 861       1                                                       
HET     MG  A 862       1                                                       
HET     MG  A   2       1                                                       
HET     MG  A   3       1                                                       
HETNAM     5FO 6-ETHYL-5-FLUORO-2-{5-[(4-METHYLPIPERAZIN-1-YL)                  
HETNAM   2 5FO  SULFONYL]-2-PROPOXYPHENYL}PYRIMIDIN-4(3H)-ONE                   
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  5FO    C20 H27 F N4 O4 S                                            
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   MG    3(MG 2+)                                                     
FORMUL   7  HOH   *12(H2 O)                                                     
HELIX    1   1 THR A  537  ALA A  546  1                                  10    
HELIX    2   2 SER A  550  LYS A  555  1                                   6    
HELIX    3   3 SER A  567  LEU A  582  1                                  16    
HELIX    4   4 ASN A  583  GLN A  589  1                                   7    
HELIX    5   5 LYS A  591  ASN A  605  1                                  15    
HELIX    6   6 ASN A  614  LYS A  630  1                                  17    
HELIX    7   7 ILE A  634  LEU A  638  5                                   5    
HELIX    8   8 THR A  639  HIS A  653  1                                  15    
HELIX    9   9 SER A  679  ASN A  694  1                                  16    
HELIX   10  10 SER A  705  THR A  723  1                                  19    
HELIX   11  11 ASP A  724  LYS A  741  1                                  18    
HELIX   12  12 ASP A  748  LEU A  765  1                                  18    
HELIX   13  13 SER A  766  LYS A  770  5                                   5    
HELIX   14  14 PRO A  771  GLN A  789  1                                  19    
HELIX   15  15 LYS A  812  ILE A  824  1                                  13    
HELIX   16  16 ILE A  824  SER A  836  1                                  13    
HELIX   17  17 CYS A  839  GLN A  860  1                                  22    
LINK         OD2 ASP A 654                ZN    ZN A 861     1555   1555  2.21  
LINK         OD1 ASP A 764                ZN    ZN A 861     1555   1555  2.27  
LINK         NE2 HIS A 653                ZN    ZN A 861     1555   1555  2.38  
LINK         NE2 HIS A 617                ZN    ZN A 861     1555   1555  2.40  
LINK        MG    MG A 862                 O   HOH A  11     1555   1555  2.61  
LINK        MG    MG A 862                 O   HOH A 864     1555   1555  2.64  
SITE     1 AC1  8 SER A 668  ALA A 779  PHE A 786  ILE A 813                    
SITE     2 AC1  8 MET A 816  GLN A 817  PHE A 820  HOH A 865                    
SITE     1 AC2  6 HIS A 617  HIS A 653  ASP A 654  ASP A 764                    
SITE     2 AC2  6  MG A 862  HOH A 864                                          
SITE     1 AC3  5 HOH A  11  HIS A 613  ASP A 654   ZN A 861                    
SITE     2 AC3  5 HOH A 864                                                     
SITE     1 AC4  1 ASP A 568                                                     
CRYST1   74.458   74.458  131.926  90.00  90.00 120.00 P 31 2 1      6          
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      0.013430  0.007754  0.000000        0.00000                         
SCALE2      0.000000  0.015508  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007580        0.00000                         
ATOM      1  N   GLU A 536     -55.723   3.872   4.784  1.00 86.68           N  
ATOM      2  CA  GLU A 536     -55.565   5.219   5.337  1.00 91.35           C  
ATOM      3  C   GLU A 536     -56.803   5.728   6.109  1.00 90.65           C  
ATOM      4  O   GLU A 536     -57.944   5.376   5.803  1.00 85.92           O  
ATOM      5  CB  GLU A 536     -55.168   6.216   4.235  1.00 79.93           C  
ATOM      6  N   THR A 537     -56.558   6.557   7.118  1.00 90.64           N  
ATOM      7  CA  THR A 537     -57.630   7.190   7.879  1.00 89.54           C  
ATOM      8  C   THR A 537     -57.911   8.591   7.336  1.00 86.16           C  
ATOM      9  O   THR A 537     -57.093   9.171   6.612  1.00 84.94           O  
ATOM     10  CB  THR A 537     -57.284   7.272   9.402  1.00 90.58           C  
ATOM     11  OG1 THR A 537     -58.240   8.103  10.074  1.00 94.75           O  
ATOM     12  CG2 THR A 537     -55.890   7.858   9.627  1.00 84.42           C  
ATOM     13  N   ARG A 538     -59.068   9.142   7.674  1.00 82.88           N  
ATOM     14  CA  ARG A 538     -59.307  10.535   7.348  1.00 85.24           C  
ATOM     15  C   ARG A 538     -58.118  11.346   7.860  1.00 86.64           C  
ATOM     16  O   ARG A 538     -57.518  12.132   7.122  1.00 83.79           O  
ATOM     17  CB  ARG A 538     -60.609  11.031   7.980  1.00 77.41           C  
ATOM     18  N   GLU A 539     -57.764  11.108   9.124  1.00 89.81           N  
ATOM     19  CA  GLU A 539     -56.752  11.895   9.835  1.00 85.93           C  
ATOM     20  C   GLU A 539     -55.368  11.834   9.193  1.00 83.21           C  
ATOM     21  O   GLU A 539     -54.631  12.835   9.183  1.00 76.53           O  
ATOM     22  CB  GLU A 539     -56.672  11.457  11.299  1.00 82.59           C  
ATOM     23  CG  GLU A 539     -55.842  12.385  12.160  1.00 85.52           C  
ATOM     24  CD  GLU A 539     -55.895  12.033  13.644  1.00 88.19           C  
ATOM     25  OE1 GLU A 539     -56.148  10.854  13.981  1.00 81.16           O  
ATOM     26  OE2 GLU A 539     -55.686  12.945  14.476  1.00 84.64           O  
ATOM     27  N   LEU A 540     -55.024  10.659   8.661  1.00 83.61           N  
ATOM     28  CA  LEU A 540     -53.760  10.483   7.946  1.00 80.66           C  
ATOM     29  C   LEU A 540     -53.720  11.366   6.714  1.00 76.97           C  
ATOM     30  O   LEU A 540     -52.741  12.073   6.502  1.00 72.47           O  
ATOM     31  CB  LEU A 540     -53.520   9.019   7.554  1.00 78.61           C  
ATOM     32  N   GLN A 541     -54.786  11.324   5.911  1.00 79.86           N  
ATOM     33  CA  GLN A 541     -54.858  12.128   4.690  1.00 79.87           C  
ATOM     34  C   GLN A 541     -54.671  13.623   4.996  1.00 78.38           C  
ATOM     35  O   GLN A 541     -53.884  14.308   4.335  1.00 75.00           O  
ATOM     36  CB  GLN A 541     -56.172  11.874   3.937  1.00 73.29           C  
ATOM     37  N   SER A 542     -55.376  14.114   6.013  1.00 75.51           N  
ATOM     38  CA  SER A 542     -55.292  15.520   6.391  1.00 77.85           C  
ATOM     39  C   SER A 542     -53.870  15.921   6.772  1.00 78.78           C  
ATOM     40  O   SER A 542     -53.362  16.939   6.275  1.00 75.24           O  
ATOM     41  CB  SER A 542     -56.244  15.845   7.552  1.00 80.98           C  
ATOM     42  OG  SER A 542     -57.333  14.933   7.611  1.00 86.83           O  
ATOM     43  N   LEU A 543     -53.234  15.142   7.659  1.00 75.94           N  
ATOM     44  CA  LEU A 543     -51.899  15.507   8.149  1.00 70.55           C  
ATOM     45  C   LEU A 543     -50.870  15.358   7.050  1.00 67.08           C  
ATOM     46  O   LEU A 543     -49.948  16.165   6.937  1.00 68.12           O  
ATOM     47  CB  LEU A 543     -51.483  14.705   9.388  1.00 73.81           C  
ATOM     48  CG  LEU A 543     -50.117  15.094   9.997  1.00 61.14           C  
ATOM     49  N   ALA A 544     -51.040  14.329   6.227  1.00 70.28           N  
ATOM     50  CA  ALA A 544     -50.159  14.121   5.076  1.00 71.95           C  
ATOM     51  C   ALA A 544     -50.229  15.293   4.101  1.00 70.51           C  
ATOM     52  O   ALA A 544     -49.194  15.775   3.630  1.00 67.46           O  
ATOM     53  CB  ALA A 544     -50.483  12.810   4.368  1.00 67.98           C  
ATOM     54  N   ALA A 545     -51.447  15.760   3.829  1.00 67.85           N  
ATOM     55  CA  ALA A 545     -51.663  16.843   2.870  1.00 69.92           C  
ATOM     56  C   ALA A 545     -51.380  18.246   3.404  1.00 70.32           C  
ATOM     57  O   ALA A 545     -51.389  19.204   2.643  1.00 69.56           O  
ATOM     58  CB  ALA A 545     -53.072  16.782   2.312  1.00 70.51           C  
ATOM     59  N   ALA A 546     -51.128  18.375   4.702  1.00 73.51           N  
ATOM     60  CA  ALA A 546     -50.967  19.702   5.312  1.00 70.32           C  
ATOM     61  C   ALA A 546     -49.655  20.410   4.961  1.00 71.22           C  
ATOM     62  O   ALA A 546     -48.757  19.825   4.369  1.00 73.81           O  
ATOM     63  CB  ALA A 546     -51.131  19.609   6.807  1.00 66.04           C  
ATOM     64  N   VAL A 547     -49.559  21.689   5.305  1.00 79.30           N  
ATOM     65  CA  VAL A 547     -48.293  22.414   5.183  1.00 75.26           C  
ATOM     66  C   VAL A 547     -47.697  22.512   6.575  1.00 76.35           C  
ATOM     67  O   VAL A 547     -48.434  22.610   7.571  1.00 74.80           O  
ATOM     68  CB  VAL A 547     -48.483  23.852   4.657  1.00 73.27           C  
ATOM     69  CG1 VAL A 547     -47.169  24.375   4.064  1.00 73.77           C  
ATOM     70  CG2 VAL A 547     -49.603  23.902   3.634  1.00 75.35           C  
ATOM     71  N   VAL A 548     -46.373  22.491   6.657  1.00 71.78           N  
ATOM     72  CA  VAL A 548     -45.715  22.492   7.955  1.00 69.31           C  
ATOM     73  C   VAL A 548     -45.088  23.859   8.213  1.00 67.69           C  
ATOM     74  O   VAL A 548     -44.042  24.191   7.636  1.00 65.49           O  
ATOM     75  CB  VAL A 548     -44.661  21.345   8.067  1.00 66.31           C  
ATOM     76  CG1 VAL A 548     -43.973  21.352   9.436  1.00 61.36           C  
ATOM     77  CG2 VAL A 548     -45.312  20.007   7.807  1.00 62.10           C  
ATOM     78  N   PRO A 549     -45.736  24.658   9.081  1.00 66.70           N  
ATOM     79  CA  PRO A 549     -45.258  26.000   9.428  1.00 60.36           C  
ATOM     80  C   PRO A 549     -43.813  25.955   9.854  1.00 60.18           C  
ATOM     81  O   PRO A 549     -43.291  24.885  10.114  1.00 64.10           O  
ATOM     82  CB  PRO A 549     -46.142  26.384  10.617  1.00 62.02           C  
ATOM     83  CG  PRO A 549     -47.431  25.646  10.364  1.00 59.71           C  
ATOM     84  CD  PRO A 549     -47.007  24.327   9.761  1.00 64.19           C  
ATOM     85  N   SER A 550     -43.179  27.112   9.933  1.00 63.69           N  
ATOM     86  CA  SER A 550     -41.801  27.210  10.375  1.00 62.95           C  
ATOM     87  C   SER A 550     -41.714  26.900  11.871  1.00 66.98           C  
ATOM     88  O   SER A 550     -42.728  26.853  12.565  1.00 66.02           O  
ATOM     89  CB  SER A 550     -41.287  28.625  10.104  1.00 62.76           C  
ATOM     90  OG  SER A 550     -39.981  28.810  10.623  1.00 69.12           O  
ATOM     91  N   ALA A 551     -40.501  26.700  12.369  1.00 66.92           N  
ATOM     92  CA  ALA A 551     -40.317  26.500  13.793  1.00 59.67           C  
ATOM     93  C   ALA A 551     -40.725  27.759  14.507  1.00 65.74           C  
ATOM     94  O   ALA A 551     -41.323  27.702  15.581  1.00 70.50           O  
ATOM     95  CB  ALA A 551     -38.875  26.170  14.108  1.00 59.00           C  
ATOM     96  N   GLN A 552     -40.392  28.906  13.922  1.00 70.03           N  
ATOM     97  CA  GLN A 552     -40.688  30.184  14.570  1.00 72.96           C  
ATOM     98  C   GLN A 552     -42.190  30.379  14.682  1.00 66.70           C  
ATOM     99  O   GLN A 552     -42.705  30.753  15.724  1.00 69.50           O  
ATOM    100  CB  GLN A 552     -40.066  31.347  13.809  1.00 75.78           C  
ATOM    101  CG  GLN A 552     -38.628  31.646  14.183  1.00 83.82           C  
ATOM    102  CD  GLN A 552     -38.064  32.819  13.384  1.00 97.22           C  
ATOM    103  OE1 GLN A 552     -38.434  33.977  13.621  1.00 89.22           O  
ATOM    104  NE2 GLN A 552     -37.174  32.521  12.421  1.00 93.18           N  
ATOM    105  N   THR A 553     -42.881  30.106  13.589  1.00 66.28           N  
ATOM    106  CA  THR A 553     -44.330  30.217  13.521  1.00 65.41           C  
ATOM    107  C   THR A 553     -44.989  29.306  14.556  1.00 69.12           C  
ATOM    108  O   THR A 553     -46.068  29.619  15.085  1.00 67.20           O  
ATOM    109  CB  THR A 553     -44.819  29.817  12.097  1.00 69.83           C  
ATOM    110  OG1 THR A 553     -44.076  30.545  11.103  1.00 69.07           O  
ATOM    111  CG2 THR A 553     -46.317  30.049  11.925  1.00 53.96           C  
ATOM    112  N   LEU A 554     -44.326  28.180  14.836  1.00 67.34           N  
ATOM    113  CA  LEU A 554     -44.857  27.168  15.738  1.00 62.10           C  
ATOM    114  C   LEU A 554     -44.365  27.364  17.169  1.00 63.17           C  
ATOM    115  O   LEU A 554     -44.946  26.827  18.120  1.00 60.19           O  
ATOM    116  CB  LEU A 554     -44.557  25.770  15.220  1.00 59.74           C  
ATOM    117  CG  LEU A 554     -45.363  25.442  13.966  1.00 60.96           C  
ATOM    118  CD1 LEU A 554     -44.918  24.128  13.384  1.00 57.35           C  
ATOM    119  CD2 LEU A 554     -46.864  25.432  14.243  1.00 52.74           C  
ATOM    120  N   LYS A 555     -43.318  28.164  17.316  1.00 60.98           N  
ATOM    121  CA  LYS A 555     -42.921  28.633  18.634  1.00 63.15           C  
ATOM    122  C   LYS A 555     -42.254  27.539  19.435  1.00 61.38           C  
ATOM    123  O   LYS A 555     -42.015  27.672  20.634  1.00 63.51           O  
ATOM    124  CB  LYS A 555     -44.144  29.148  19.383  1.00 59.57           C  
ATOM    125  CG  LYS A 555     -44.388  30.627  19.190  1.00 66.59           C  
ATOM    126  CD  LYS A 555     -45.814  30.998  19.577  1.00 68.78           C  
ATOM    127  CE  LYS A 555     -46.810  30.273  18.690  1.00 71.52           C  
ATOM    128  NZ  LYS A 555     -48.209  30.658  19.026  1.00 77.61           N  
ATOM    129  N   ILE A 556     -41.935  26.451  18.760  1.00 61.65           N  
ATOM    130  CA  ILE A 556     -41.441  25.274  19.443  1.00 57.25           C  
ATOM    131  C   ILE A 556     -39.973  25.407  19.821  1.00 58.73           C  
ATOM    132  O   ILE A 556     -39.342  24.419  20.166  1.00 62.59           O  
ATOM    133  CB  ILE A 556     -41.603  24.054  18.563  1.00 55.75           C  
ATOM    134  CG1 ILE A 556     -40.765  24.248  17.298  1.00 61.08           C  
ATOM    135  CG2 ILE A 556     -43.062  23.856  18.201  1.00 53.10           C  
ATOM    136  CD1 ILE A 556     -40.855  23.108  16.318  1.00 62.88           C  
ATOM    137  N   THR A 557     -39.423  26.617  19.767  1.00 62.21           N  
ATOM    138  CA  THR A 557     -38.019  26.819  20.135  1.00 60.96           C  
ATOM    139  C   THR A 557     -37.893  27.518  21.473  1.00 59.98           C  
ATOM    140  O   THR A 557     -36.791  27.674  22.005  1.00 59.24           O  
ATOM    141  CB  THR A 557     -37.236  27.648  19.085  1.00 60.53           C  
ATOM    142  OG1 THR A 557     -37.463  27.107  17.782  1.00 65.44           O  
ATOM    143  CG2 THR A 557     -35.737  27.584  19.378  1.00 62.56           C  
ATOM    144  N   ASP A 558     -39.024  27.954  22.012  1.00 60.47           N  
ATOM    145  CA  ASP A 558     -39.007  28.690  23.268  1.00 64.34           C  
ATOM    146  C   ASP A 558     -39.182  27.723  24.423  1.00 59.28           C  
ATOM    147  O   ASP A 558     -40.115  26.916  24.426  1.00 55.90           O  
ATOM    148  CB  ASP A 558     -40.118  29.755  23.290  1.00 66.88           C  
ATOM    149  CG  ASP A 558     -40.311  30.439  21.927  1.00 78.04           C  
ATOM    150  OD1 ASP A 558     -39.302  30.870  21.298  1.00 79.94           O  
ATOM    151  OD2 ASP A 558     -41.482  30.535  21.479  1.00 76.92           O  
ATOM    152  N   PHE A 559     -38.289  27.801  25.404  1.00 54.86           N  
ATOM    153  CA  PHE A 559     -38.446  26.986  26.595  1.00 55.50           C  
ATOM    154  C   PHE A 559     -39.811  27.168  27.262  1.00 60.37           C  
ATOM    155  O   PHE A 559     -40.272  26.294  27.998  1.00 64.64           O  
ATOM    156  CB  PHE A 559     -37.333  27.258  27.593  1.00 57.95           C  
ATOM    157  CG  PHE A 559     -36.010  26.692  27.186  1.00 61.44           C  
ATOM    158  CD1 PHE A 559     -34.974  27.529  26.796  1.00 59.34           C  
ATOM    159  CD2 PHE A 559     -35.797  25.314  27.191  1.00 60.65           C  
ATOM    160  CE1 PHE A 559     -33.745  27.004  26.422  1.00 62.97           C  
ATOM    161  CE2 PHE A 559     -34.577  24.778  26.825  1.00 57.47           C  
ATOM    162  CZ  PHE A 559     -33.546  25.625  26.433  1.00 63.13           C  
ATOM    163  N   SER A 560     -40.465  28.292  27.002  1.00 58.29           N  
ATOM    164  CA  SER A 560     -41.729  28.591  27.666  1.00 58.85           C  
ATOM    165  C   SER A 560     -42.913  28.166  26.819  1.00 54.68           C  
ATOM    166  O   SER A 560     -44.064  28.487  27.120  1.00 55.63           O  
ATOM    167  CB  SER A 560     -41.803  30.078  28.014  1.00 62.12           C  
ATOM    168  OG  SER A 560     -41.304  30.847  26.933  1.00 71.52           O  
ATOM    169  N   PHE A 561     -42.626  27.424  25.761  1.00 53.00           N  
ATOM    170  CA  PHE A 561     -43.673  26.882  24.895  1.00 50.16           C  
ATOM    171  C   PHE A 561     -44.861  26.268  25.647  1.00 51.78           C  
ATOM    172  O   PHE A 561     -44.718  25.742  26.757  1.00 51.89           O  
ATOM    173  CB  PHE A 561     -43.070  25.837  23.975  1.00 48.88           C  
ATOM    174  CG  PHE A 561     -44.070  25.130  23.139  1.00 47.76           C  
ATOM    175  CD1 PHE A 561     -44.404  25.614  21.884  1.00 48.43           C  
ATOM    176  CD2 PHE A 561     -44.683  23.978  23.602  1.00 45.57           C  
ATOM    177  CE1 PHE A 561     -45.334  24.959  21.101  1.00 48.60           C  
ATOM    178  CE2 PHE A 561     -45.615  23.317  22.833  1.00 48.53           C  
ATOM    179  CZ  PHE A 561     -45.941  23.808  21.569  1.00 51.55           C  
ATOM    180  N   SER A 562     -46.034  26.322  25.028  1.00 51.12           N  
ATOM    181  CA  SER A 562     -47.219  25.712  25.608  1.00 49.55           C  
ATOM    182  C   SER A 562     -48.189  25.217  24.541  1.00 52.66           C  
ATOM    183  O   SER A 562     -48.235  25.748  23.441  1.00 54.42           O  
ATOM    184  CB  SER A 562     -47.924  26.674  26.558  1.00 48.15           C  
ATOM    185  OG  SER A 562     -49.112  26.081  27.065  1.00 56.68           O  
ATOM    186  N   ASP A 563     -48.977  24.203  24.887  1.00 53.81           N  
ATOM    187  CA  ASP A 563     -49.765  23.482  23.902  1.00 53.21           C  
ATOM    188  C   ASP A 563     -51.261  23.570  24.138  1.00 53.64           C  
ATOM    189  O   ASP A 563     -52.021  22.932  23.421  1.00 53.50           O  
ATOM    190  CB  ASP A 563     -49.386  22.009  23.955  1.00 49.54           C  
ATOM    191  CG  ASP A 563     -49.920  21.324  25.206  1.00 55.58           C  
ATOM    192  OD1 ASP A 563     -49.367  21.582  26.296  1.00 56.43           O  
ATOM    193  OD2 ASP A 563     -50.911  20.548  25.110  1.00 56.28           O  
ATOM    194  N   PHE A 564     -51.692  24.304  25.159  1.00 52.09           N  
ATOM    195  CA  PHE A 564     -53.110  24.292  25.536  1.00 54.86           C  
ATOM    196  C   PHE A 564     -54.042  24.724  24.392  1.00 58.35           C  
ATOM    197  O   PHE A 564     -55.159  24.223  24.269  1.00 59.98           O  
ATOM    198  CB  PHE A 564     -53.382  25.174  26.763  1.00 57.38           C  
ATOM    199  CG  PHE A 564     -52.749  24.687  28.038  1.00 54.84           C  
ATOM    200  CD1 PHE A 564     -52.369  25.592  29.021  1.00 55.45           C  
ATOM    201  CD2 PHE A 564     -52.551  23.340  28.273  1.00 55.53           C  
ATOM    202  CE1 PHE A 564     -51.786  25.160  30.219  1.00 55.71           C  
ATOM    203  CE2 PHE A 564     -51.969  22.901  29.469  1.00 54.35           C  
ATOM    204  CZ  PHE A 564     -51.590  23.812  30.441  1.00 51.85           C  
ATOM    205  N   GLU A 565     -53.592  25.653  23.556  1.00 56.01           N  
ATOM    206  CA  GLU A 565     -54.433  26.147  22.469  1.00 60.30           C  
ATOM    207  C   GLU A 565     -54.329  25.324  21.184  1.00 61.53           C  
ATOM    208  O   GLU A 565     -55.014  25.612  20.199  1.00 61.71           O  
ATOM    209  CB  GLU A 565     -54.066  27.586  22.134  1.00 59.78           C  
ATOM    210  CG  GLU A 565     -52.709  27.708  21.479  1.00 60.29           C  
ATOM    211  CD  GLU A 565     -51.629  28.136  22.472  1.00 68.85           C  
ATOM    212  OE1 GLU A 565     -51.701  27.744  23.678  1.00 59.23           O  
ATOM    213  OE2 GLU A 565     -50.717  28.880  22.033  1.00 67.80           O  
ATOM    214  N   LEU A 566     -53.466  24.316  21.185  1.00 57.91           N  
ATOM    215  CA  LEU A 566     -53.222  23.533  19.988  1.00 54.74           C  
ATOM    216  C   LEU A 566     -54.201  22.388  19.864  1.00 57.48           C  
ATOM    217  O   LEU A 566     -54.621  21.803  20.864  1.00 54.20           O  
ATOM    218  CB  LEU A 566     -51.798  22.994  19.985  1.00 52.15           C  
ATOM    219  CG  LEU A 566     -50.739  24.078  20.102  1.00 56.39           C  
ATOM    220  CD1 LEU A 566     -49.358  23.525  19.823  1.00 55.26           C  
ATOM    221  CD2 LEU A 566     -51.064  25.161  19.116  1.00 62.76           C  
ATOM    222  N   SER A 567     -54.560  22.084  18.617  1.00 62.18           N  
ATOM    223  CA  SER A 567     -55.379  20.923  18.288  1.00 63.18           C  
ATOM    224  C   SER A 567     -54.444  19.740  18.129  1.00 56.81           C  
ATOM    225  O   SER A 567     -53.239  19.914  17.975  1.00 55.27           O  
ATOM    226  CB  SER A 567     -56.138  21.151  16.971  1.00 61.90           C  
ATOM    227  OG  SER A 567     -55.248  21.201  15.851  1.00 63.83           O  
ATOM    228  N   ASP A 568     -54.999  18.539  18.141  1.00 57.30           N  
ATOM    229  CA  ASP A 568     -54.184  17.363  17.876  1.00 59.33           C  
ATOM    230  C   ASP A 568     -53.394  17.533  16.608  1.00 59.29           C  
ATOM    231  O   ASP A 568     -52.180  17.339  16.606  1.00 61.58           O  
ATOM    232  CB  ASP A 568     -55.029  16.105  17.821  1.00 57.19           C  
ATOM    233  CG  ASP A 568     -55.494  15.676  19.201  1.00 65.32           C  
ATOM    234  OD1 ASP A 568     -55.024  16.283  20.193  1.00 61.30           O  
ATOM    235  OD2 ASP A 568     -56.310  14.735  19.300  1.00 69.62           O  
ATOM    236  N   LEU A 569     -54.067  17.932  15.536  1.00 59.96           N  
ATOM    237  CA  LEU A 569     -53.398  18.118  14.258  1.00 56.66           C  
ATOM    238  C   LEU A 569     -52.187  19.054  14.384  1.00 55.95           C  
ATOM    239  O   LEU A 569     -51.086  18.754  13.912  1.00 54.29           O  
ATOM    240  CB  LEU A 569     -54.398  18.654  13.244  1.00 63.40           C  
ATOM    241  CG  LEU A 569     -53.842  19.101  11.889  1.00 68.54           C  
ATOM    242  CD1 LEU A 569     -53.372  17.898  11.062  1.00 65.26           C  
ATOM    243  CD2 LEU A 569     -54.892  19.913  11.142  1.00 64.12           C  
ATOM    244  N   GLU A 570     -52.378  20.183  15.045  1.00 57.27           N  
ATOM    245  CA  GLU A 570     -51.274  21.119  15.205  1.00 60.96           C  
ATOM    246  C   GLU A 570     -50.091  20.542  15.994  1.00 58.45           C  
ATOM    247  O   GLU A 570     -48.943  20.965  15.818  1.00 57.56           O  
ATOM    248  CB  GLU A 570     -51.760  22.410  15.854  1.00 61.49           C  
ATOM    249  CG  GLU A 570     -52.911  23.077  15.109  1.00 64.62           C  
ATOM    250  CD  GLU A 570     -53.566  24.181  15.931  1.00 72.19           C  
ATOM    251  OE1 GLU A 570     -54.420  23.860  16.802  1.00 64.95           O  
ATOM    252  OE2 GLU A 570     -53.208  25.362  15.712  1.00 68.48           O  
ATOM    253  N   THR A 571     -50.355  19.585  16.871  1.00 50.80           N  
ATOM    254  CA  THR A 571     -49.250  18.968  17.579  1.00 55.76           C  
ATOM    255  C   THR A 571     -48.513  18.036  16.609  1.00 53.60           C  
ATOM    256  O   THR A 571     -47.280  17.993  16.555  1.00 51.99           O  
ATOM    257  CB  THR A 571     -49.720  18.268  18.877  1.00 56.79           C  
ATOM    258  OG1 THR A 571     -50.482  17.098  18.562  1.00 55.68           O  
ATOM    259  CG2 THR A 571     -50.586  19.224  19.692  1.00 54.17           C  
ATOM    260  N   ALA A 572     -49.291  17.338  15.802  1.00 52.22           N  
ATOM    261  CA  ALA A 572     -48.750  16.498  14.747  1.00 54.66           C  
ATOM    262  C   ALA A 572     -47.784  17.255  13.854  1.00 54.61           C  
ATOM    263  O   ALA A 572     -46.727  16.749  13.481  1.00 55.61           O  
ATOM    264  CB  ALA A 572     -49.874  15.929  13.927  1.00 59.23           C  
ATOM    265  N   LEU A 573     -48.153  18.475  13.509  1.00 55.13           N  
ATOM    266  CA  LEU A 573     -47.334  19.275  12.620  1.00 54.11           C  
ATOM    267  C   LEU A 573     -46.109  19.773  13.338  1.00 54.18           C  
ATOM    268  O   LEU A 573     -45.014  19.818  12.777  1.00 53.67           O  
ATOM    269  CB  LEU A 573     -48.157  20.444  12.103  1.00 60.73           C  
ATOM    270  CG  LEU A 573     -49.240  19.974  11.134  1.00 60.92           C  
ATOM    271  CD1 LEU A 573     -50.344  21.013  10.934  1.00 57.11           C  
ATOM    272  CD2 LEU A 573     -48.581  19.558   9.811  1.00 59.92           C  
ATOM    273  N   CYS A 574     -46.301  20.155  14.594  1.00 56.60           N  
ATOM    274  CA  CYS A 574     -45.190  20.584  15.428  1.00 55.75           C  
ATOM    275  C   CYS A 574     -44.176  19.475  15.512  1.00 54.05           C  
ATOM    276  O   CYS A 574     -42.962  19.699  15.494  1.00 53.60           O  
ATOM    277  CB  CYS A 574     -45.685  20.911  16.826  1.00 57.99           C  
ATOM    278  SG  CYS A 574     -46.487  22.529  16.954  1.00 59.22           S  
ATOM    279  N   THR A 575     -44.682  18.260  15.603  1.00 52.69           N  
ATOM    280  CA  THR A 575     -43.794  17.129  15.710  1.00 54.09           C  
ATOM    281  C   THR A 575     -43.029  16.901  14.407  1.00 56.68           C  
ATOM    282  O   THR A 575     -41.805  16.711  14.426  1.00 56.31           O  
ATOM    283  CB  THR A 575     -44.550  15.904  16.146  1.00 50.09           C  
ATOM    284  OG1 THR A 575     -45.212  16.212  17.375  1.00 53.58           O  
ATOM    285  CG2 THR A 575     -43.596  14.759  16.372  1.00 48.38           C  
ATOM    286  N   ILE A 576     -43.727  16.949  13.277  1.00 51.54           N  
ATOM    287  CA  ILE A 576     -43.026  16.844  12.017  1.00 50.07           C  
ATOM    288  C   ILE A 576     -41.981  17.933  11.891  1.00 54.12           C  
ATOM    289  O   ILE A 576     -40.879  17.703  11.398  1.00 54.38           O  
ATOM    290  CB  ILE A 576     -43.947  16.973  10.836  1.00 55.94           C  
ATOM    291  CG1 ILE A 576     -44.818  15.720  10.721  1.00 57.72           C  
ATOM    292  CG2 ILE A 576     -43.112  17.173   9.580  1.00 49.52           C  
ATOM    293  CD1 ILE A 576     -45.998  15.892   9.810  1.00 59.60           C  
ATOM    294  N   ARG A 577     -42.327  19.130  12.336  1.00 53.29           N  
ATOM    295  CA  ARG A 577     -41.386  20.225  12.240  1.00 52.33           C  
ATOM    296  C   ARG A 577     -40.115  19.929  13.046  1.00 56.11           C  
ATOM    297  O   ARG A 577     -39.008  20.349  12.671  1.00 57.64           O  
ATOM    298  CB  ARG A 577     -42.052  21.543  12.649  1.00 49.50           C  
ATOM    299  CG  ARG A 577     -41.089  22.701  12.842  1.00 52.92           C  
ATOM    300  CD  ARG A 577     -40.229  22.955  11.602  1.00 60.19           C  
ATOM    301  NE  ARG A 577     -41.041  23.136  10.394  1.00 65.82           N  
ATOM    302  CZ  ARG A 577     -40.564  23.127   9.151  1.00 57.55           C  
ATOM    303  NH1 ARG A 577     -39.272  22.935   8.934  1.00 52.30           N  
ATOM    304  NH2 ARG A 577     -41.388  23.302   8.128  1.00 56.73           N  
ATOM    305  N   MET A 578     -40.266  19.188  14.142  1.00 53.08           N  
ATOM    306  CA  MET A 578     -39.128  18.896  14.997  1.00 53.87           C  
ATOM    307  C   MET A 578     -38.148  17.948  14.322  1.00 57.64           C  
ATOM    308  O   MET A 578     -36.919  18.132  14.375  1.00 57.90           O  
ATOM    309  CB  MET A 578     -39.596  18.293  16.312  1.00 58.75           C  
ATOM    310  CG  MET A 578     -40.321  19.268  17.213  1.00 59.92           C  
ATOM    311  SD  MET A 578     -40.897  18.440  18.696  1.00 58.81           S  
ATOM    312  CE  MET A 578     -42.392  19.374  19.014  1.00 51.30           C  
ATOM    313  N   PHE A 579     -38.694  16.923  13.689  1.00 52.85           N  
ATOM    314  CA  PHE A 579     -37.851  15.979  12.992  1.00 56.70           C  
ATOM    315  C   PHE A 579     -37.160  16.684  11.855  1.00 58.81           C  
ATOM    316  O   PHE A 579     -35.983  16.441  11.586  1.00 61.44           O  
ATOM    317  CB  PHE A 579     -38.665  14.813  12.448  1.00 56.39           C  
ATOM    318  CG  PHE A 579     -38.930  13.718  13.456  1.00 59.16           C  
ATOM    319  CD1 PHE A 579     -40.037  13.775  14.293  1.00 58.33           C  
ATOM    320  CD2 PHE A 579     -38.086  12.611  13.540  1.00 58.23           C  
ATOM    321  CE1 PHE A 579     -40.296  12.755  15.198  1.00 57.49           C  
ATOM    322  CE2 PHE A 579     -38.336  11.588  14.434  1.00 51.51           C  
ATOM    323  CZ  PHE A 579     -39.441  11.663  15.271  1.00 56.74           C  
ATOM    324  N   THR A 580     -37.894  17.567  11.189  1.00 57.15           N  
ATOM    325  CA  THR A 580     -37.376  18.215  10.002  1.00 57.12           C  
ATOM    326  C   THR A 580     -36.236  19.161  10.332  1.00 61.84           C  
ATOM    327  O   THR A 580     -35.203  19.139   9.677  1.00 65.70           O  
ATOM    328  CB  THR A 580     -38.465  18.963   9.258  1.00 61.37           C  
ATOM    329  OG1 THR A 580     -39.542  18.063   8.979  1.00 59.46           O  
ATOM    330  CG2 THR A 580     -37.920  19.538   7.949  1.00 59.89           C  
ATOM    331  N   ASP A 581     -36.405  19.977  11.364  1.00 64.86           N  
ATOM    332  CA  ASP A 581     -35.388  20.978  11.690  1.00 62.91           C  
ATOM    333  C   ASP A 581     -34.174  20.410  12.386  1.00 61.22           C  
ATOM    334  O   ASP A 581     -33.143  21.063  12.488  1.00 64.34           O  
ATOM    335  CB  ASP A 581     -35.992  22.115  12.516  1.00 66.23           C  
ATOM    336  CG  ASP A 581     -36.400  23.310  11.652  1.00 71.83           C  
ATOM    337  OD1 ASP A 581     -37.044  23.103  10.586  1.00 63.24           O  
ATOM    338  OD2 ASP A 581     -36.058  24.453  12.043  1.00 75.95           O  
ATOM    339  N   LEU A 582     -34.308  19.192  12.884  1.00 65.50           N  
ATOM    340  CA  LEU A 582     -33.192  18.509  13.520  1.00 66.23           C  
ATOM    341  C   LEU A 582     -32.367  17.729  12.497  1.00 69.15           C  
ATOM    342  O   LEU A 582     -31.315  17.179  12.835  1.00 70.18           O  
ATOM    343  CB  LEU A 582     -33.700  17.587  14.620  1.00 62.65           C  
ATOM    344  CG  LEU A 582     -33.920  18.325  15.936  1.00 62.44           C  
ATOM    345  CD1 LEU A 582     -34.598  17.421  16.957  1.00 50.77           C  
ATOM    346  CD2 LEU A 582     -32.597  18.895  16.457  1.00 58.01           C  
ATOM    347  N   ASN A 583     -32.857  17.698  11.257  1.00 61.96           N  
ATOM    348  CA  ASN A 583     -32.155  17.102  10.129  1.00 64.32           C  
ATOM    349  C   ASN A 583     -32.387  15.627  10.057  1.00 68.97           C  
ATOM    350  O   ASN A 583     -31.645  14.913   9.388  1.00 70.80           O  
ATOM    351  CB  ASN A 583     -30.653  17.361  10.189  1.00 64.95           C  
ATOM    352  CG  ASN A 583     -30.300  18.756   9.776  1.00 73.26           C  
ATOM    353  OD1 ASN A 583     -30.880  19.291   8.823  1.00 73.72           O  
ATOM    354  ND2 ASN A 583     -29.365  19.376  10.499  1.00 73.62           N  
ATOM    355  N   LEU A 584     -33.421  15.173  10.750  1.00 69.52           N  
ATOM    356  CA  LEU A 584     -33.691  13.749  10.849  1.00 65.46           C  
ATOM    357  C   LEU A 584     -34.333  13.194   9.591  1.00 64.36           C  
ATOM    358  O   LEU A 584     -34.030  12.074   9.196  1.00 69.22           O  
ATOM    359  CB  LEU A 584     -34.555  13.452  12.068  1.00 62.81           C  
ATOM    360  CG  LEU A 584     -33.975  14.011  13.367  1.00 63.91           C  
ATOM    361  CD1 LEU A 584     -34.795  13.490  14.541  1.00 58.17           C  
ATOM    362  CD2 LEU A 584     -32.485  13.650  13.502  1.00 57.27           C  
ATOM    363  N   VAL A 585     -35.209  13.964   8.955  1.00 62.85           N  
ATOM    364  CA  VAL A 585     -35.861  13.485   7.735  1.00 65.90           C  
ATOM    365  C   VAL A 585     -34.833  13.378   6.610  1.00 62.04           C  
ATOM    366  O   VAL A 585     -34.773  12.397   5.878  1.00 61.21           O  
ATOM    367  CB  VAL A 585     -37.019  14.404   7.308  1.00 62.43           C  
ATOM    368  CG1 VAL A 585     -37.571  13.976   5.949  1.00 58.06           C  
ATOM    369  CG2 VAL A 585     -38.118  14.407   8.370  1.00 59.45           C  
ATOM    370  N   GLN A 586     -34.015  14.411   6.513  1.00 65.09           N  
ATOM    371  CA  GLN A 586     -32.885  14.459   5.605  1.00 66.66           C  
ATOM    372  C   GLN A 586     -31.934  13.272   5.763  1.00 67.92           C  
ATOM    373  O   GLN A 586     -31.894  12.379   4.910  1.00 67.47           O  
ATOM    374  CB  GLN A 586     -32.116  15.758   5.839  1.00 66.93           C  
ATOM    375  CG  GLN A 586     -30.777  15.828   5.141  1.00 70.36           C  
ATOM    376  CD  GLN A 586     -30.882  15.539   3.652  1.00 73.52           C  
ATOM    377  OE1 GLN A 586     -31.922  15.787   3.018  1.00 67.47           O  
ATOM    378  NE2 GLN A 586     -29.807  14.989   3.089  1.00 71.41           N  
ATOM    379  N   ASN A 587     -31.179  13.272   6.859  1.00 64.44           N  
ATOM    380  CA  ASN A 587     -30.115  12.300   7.079  1.00 65.22           C  
ATOM    381  C   ASN A 587     -30.521  10.829   7.140  1.00 64.75           C  
ATOM    382  O   ASN A 587     -29.655   9.964   7.217  1.00 67.76           O  
ATOM    383  CB  ASN A 587     -29.334  12.642   8.345  1.00 66.01           C  
ATOM    384  CG  ASN A 587     -28.651  13.983   8.261  1.00 69.30           C  
ATOM    385  OD1 ASN A 587     -28.526  14.561   7.185  1.00 73.55           O  
ATOM    386  ND2 ASN A 587     -28.189  14.483   9.400  1.00 70.61           N  
ATOM    387  N   PHE A 588     -31.814  10.539   7.120  1.00 59.14           N  
ATOM    388  CA  PHE A 588     -32.261   9.163   7.282  1.00 61.32           C  
ATOM    389  C   PHE A 588     -33.407   8.827   6.340  1.00 66.89           C  
ATOM    390  O   PHE A 588     -34.073   7.789   6.488  1.00 63.84           O  
ATOM    391  CB  PHE A 588     -32.636   8.873   8.745  1.00 59.74           C  
ATOM    392  CG  PHE A 588     -31.537   9.191   9.710  1.00 65.77           C  
ATOM    393  CD1 PHE A 588     -31.637  10.280  10.567  1.00 62.22           C  
ATOM    394  CD2 PHE A 588     -30.372   8.430   9.727  1.00 60.99           C  
ATOM    395  CE1 PHE A 588     -30.606  10.589  11.433  1.00 62.13           C  
ATOM    396  CE2 PHE A 588     -29.344   8.737  10.593  1.00 59.13           C  
ATOM    397  CZ  PHE A 588     -29.460   9.822  11.445  1.00 61.16           C  
ATOM    398  N   GLN A 589     -33.635   9.724   5.386  1.00 64.65           N  
ATOM    399  CA  GLN A 589     -34.516   9.450   4.261  1.00 64.16           C  
ATOM    400  C   GLN A 589     -35.868   8.905   4.717  1.00 66.79           C  
ATOM    401  O   GLN A 589     -36.260   7.796   4.337  1.00 65.00           O  
ATOM    402  CB  GLN A 589     -33.831   8.463   3.311  1.00 61.86           C  
ATOM    403  CG  GLN A 589     -32.321   8.739   3.108  1.00 65.80           C  
ATOM    404  CD  GLN A 589     -31.478   7.466   3.047  1.00 67.58           C  
ATOM    405  N   MET A 590     -36.578   9.681   5.534  1.00 64.72           N  
ATOM    406  CA  MET A 590     -37.901   9.258   5.977  1.00 69.35           C  
ATOM    407  C   MET A 590     -38.981   9.696   4.988  1.00 64.73           C  
ATOM    408  O   MET A 590     -39.125  10.871   4.689  1.00 65.61           O  
ATOM    409  CB  MET A 590     -38.226   9.777   7.388  1.00 65.04           C  
ATOM    410  CG  MET A 590     -37.115   9.581   8.431  1.00 66.50           C  
ATOM    411  SD  MET A 590     -37.532  10.247  10.083  1.00 64.51           S  
ATOM    412  CE  MET A 590     -36.010  10.003  10.984  1.00 57.48           C  
ATOM    413  N   LYS A 591     -39.734   8.733   4.481  1.00 62.26           N  
ATOM    414  CA  LYS A 591     -40.887   9.038   3.661  1.00 65.57           C  
ATOM    415  C   LYS A 591     -41.968   9.737   4.494  1.00 73.79           C  
ATOM    416  O   LYS A 591     -42.385   9.259   5.559  1.00 71.10           O  
ATOM    417  CB  LYS A 591     -41.439   7.769   2.994  1.00 73.28           C  
ATOM    418  CG  LYS A 591     -40.492   7.124   1.957  1.00 73.49           C  
ATOM    419  N   HIS A 592     -42.419  10.877   3.984  1.00 77.12           N  
ATOM    420  CA  HIS A 592     -43.425  11.702   4.633  1.00 67.85           C  
ATOM    421  C   HIS A 592     -44.624  10.910   5.171  1.00 64.72           C  
ATOM    422  O   HIS A 592     -45.037  11.106   6.305  1.00 61.39           O  
ATOM    423  CB  HIS A 592     -43.894  12.776   3.650  1.00 70.85           C  
ATOM    424  CG  HIS A 592     -44.582  13.933   4.299  1.00 75.75           C  
ATOM    425  ND1 HIS A 592     -43.902  14.897   5.014  1.00 75.82           N  
ATOM    426  CD2 HIS A 592     -45.892  14.275   4.352  1.00 70.69           C  
ATOM    427  CE1 HIS A 592     -44.765  15.784   5.482  1.00 74.46           C  
ATOM    428  NE2 HIS A 592     -45.979  15.430   5.093  1.00 77.37           N  
ATOM    429  N   GLU A 593     -45.192  10.028   4.359  1.00 65.73           N  
ATOM    430  CA  GLU A 593     -46.362   9.261   4.791  1.00 68.60           C  
ATOM    431  C   GLU A 593     -46.000   8.353   5.962  1.00 64.38           C  
ATOM    432  O   GLU A 593     -46.836   8.060   6.830  1.00 60.78           O  
ATOM    433  CB  GLU A 593     -46.935   8.413   3.637  1.00 64.38           C  
ATOM    434  N   VAL A 594     -44.755   7.890   5.967  1.00 57.02           N  
ATOM    435  CA  VAL A 594     -44.323   6.977   7.008  1.00 61.41           C  
ATOM    436  C   VAL A 594     -44.182   7.742   8.317  1.00 59.11           C  
ATOM    437  O   VAL A 594     -44.749   7.354   9.329  1.00 61.78           O  
ATOM    438  CB  VAL A 594     -42.995   6.286   6.650  1.00 66.97           C  
ATOM    439  CG1 VAL A 594     -42.633   5.246   7.701  1.00 60.81           C  
ATOM    440  CG2 VAL A 594     -43.094   5.653   5.279  1.00 61.44           C  
ATOM    441  N   LEU A 595     -43.432   8.834   8.292  1.00 55.23           N  
ATOM    442  CA  LEU A 595     -43.344   9.699   9.452  1.00 55.28           C  
ATOM    443  C   LEU A 595     -44.721  10.038  10.039  1.00 59.98           C  
ATOM    444  O   LEU A 595     -44.958   9.853  11.242  1.00 58.55           O  
ATOM    445  CB  LEU A 595     -42.597  10.973   9.096  1.00 53.97           C  
ATOM    446  CG  LEU A 595     -42.442  11.936  10.266  1.00 55.72           C  
ATOM    447  CD1 LEU A 595     -42.091  11.157  11.505  1.00 53.03           C  
ATOM    448  CD2 LEU A 595     -41.394  13.013   9.977  1.00 56.31           C  
ATOM    449  N   CYS A 596     -45.625  10.520   9.190  1.00 57.32           N  
ATOM    450  CA  CYS A 596     -46.949  10.941   9.637  1.00 58.53           C  
ATOM    451  C   CYS A 596     -47.691   9.791  10.288  1.00 59.04           C  
ATOM    452  O   CYS A 596     -48.343   9.946  11.327  1.00 59.03           O  
ATOM    453  CB  CYS A 596     -47.788  11.484   8.466  1.00 59.19           C  
ATOM    454  SG  CYS A 596     -47.198  13.050   7.735  1.00 63.20           S  
ATOM    455  N   ARG A 597     -47.608   8.634   9.653  1.00 56.93           N  
ATOM    456  CA  ARG A 597     -48.322   7.463  10.135  1.00 61.03           C  
ATOM    457  C   ARG A 597     -47.717   7.081  11.501  1.00 59.97           C  
ATOM    458  O   ARG A 597     -48.426   6.719  12.455  1.00 54.91           O  
ATOM    459  CB  ARG A 597     -48.208   6.338   9.092  1.00 61.11           C  
ATOM    460  CG  ARG A 597     -49.289   5.260   9.153  1.00 68.08           C  
ATOM    461  CD  ARG A 597     -49.085   4.179   8.067  1.00 73.77           C  
ATOM    462  NE  ARG A 597     -49.154   4.703   6.697  1.00 67.89           N  
ATOM    463  N   TRP A 598     -46.398   7.209  11.598  1.00 54.92           N  
ATOM    464  CA  TRP A 598     -45.711   6.887  12.830  1.00 56.45           C  
ATOM    465  C   TRP A 598     -46.214   7.750  13.972  1.00 54.78           C  
ATOM    466  O   TRP A 598     -46.485   7.257  15.056  1.00 53.20           O  
ATOM    467  CB  TRP A 598     -44.190   7.031  12.681  1.00 59.49           C  
ATOM    468  CG  TRP A 598     -43.460   6.707  13.980  1.00 57.29           C  
ATOM    469  CD1 TRP A 598     -43.183   5.469  14.473  1.00 53.72           C  
ATOM    470  CD2 TRP A 598     -42.954   7.639  14.938  1.00 58.71           C  
ATOM    471  NE1 TRP A 598     -42.527   5.564  15.656  1.00 54.37           N  
ATOM    472  CE2 TRP A 598     -42.374   6.887  15.977  1.00 59.81           C  
ATOM    473  CE3 TRP A 598     -42.933   9.040  15.020  1.00 56.43           C  
ATOM    474  CZ2 TRP A 598     -41.781   7.488  17.100  1.00 56.90           C  
ATOM    475  CZ3 TRP A 598     -42.341   9.633  16.127  1.00 56.74           C  
ATOM    476  CH2 TRP A 598     -41.773   8.857  17.154  1.00 54.90           C  
ATOM    477  N   ILE A 599     -46.331   9.043  13.709  1.00 57.15           N  
ATOM    478  CA  ILE A 599     -46.842  10.001  14.677  1.00 54.11           C  
ATOM    479  C   ILE A 599     -48.310   9.784  15.043  1.00 53.97           C  
ATOM    480  O   ILE A 599     -48.686   9.834  16.216  1.00 57.36           O  
ATOM    481  CB  ILE A 599     -46.697  11.412  14.146  1.00 56.46           C  
ATOM    482  CG1 ILE A 599     -45.218  11.735  13.931  1.00 51.00           C  
ATOM    483  CG2 ILE A 599     -47.401  12.416  15.081  1.00 54.39           C  
ATOM    484  CD1 ILE A 599     -44.985  13.057  13.269  1.00 48.22           C  
ATOM    485  N   LEU A 600     -49.158   9.549  14.059  1.00 52.28           N  
ATOM    486  CA  LEU A 600     -50.540   9.269  14.407  1.00 56.65           C  
ATOM    487  C   LEU A 600     -50.606   8.038  15.300  1.00 55.52           C  
ATOM    488  O   LEU A 600     -51.449   7.935  16.184  1.00 55.04           O  
ATOM    489  CB  LEU A 600     -51.402   9.100  13.161  1.00 58.37           C  
ATOM    490  CG  LEU A 600     -51.579  10.417  12.399  1.00 68.69           C  
ATOM    491  CD1 LEU A 600     -52.567  10.301  11.232  1.00 71.41           C  
ATOM    492  CD2 LEU A 600     -52.017  11.514  13.356  1.00 61.88           C  
ATOM    493  N   SER A 601     -49.689   7.113  15.074  1.00 54.19           N  
ATOM    494  CA  SER A 601     -49.675   5.891  15.836  1.00 54.16           C  
ATOM    495  C   SER A 601     -49.262   6.170  17.256  1.00 55.49           C  
ATOM    496  O   SER A 601     -49.879   5.679  18.209  1.00 55.89           O  
ATOM    497  CB  SER A 601     -48.702   4.888  15.221  1.00 56.67           C  
ATOM    498  OG  SER A 601     -49.290   4.254  14.109  1.00 61.35           O  
ATOM    499  N   VAL A 602     -48.195   6.941  17.404  1.00 49.86           N  
ATOM    500  CA  VAL A 602     -47.695   7.184  18.730  1.00 49.08           C  
ATOM    501  C   VAL A 602     -48.814   7.847  19.511  1.00 52.79           C  
ATOM    502  O   VAL A 602     -49.184   7.410  20.599  1.00 54.32           O  
ATOM    503  CB  VAL A 602     -46.462   8.071  18.712  1.00 53.06           C  
ATOM    504  CG1 VAL A 602     -46.152   8.562  20.136  1.00 50.47           C  
ATOM    505  CG2 VAL A 602     -45.273   7.323  18.100  1.00 49.86           C  
ATOM    506  N   LYS A 603     -49.379   8.885  18.915  1.00 53.52           N  
ATOM    507  CA  LYS A 603     -50.438   9.649  19.537  1.00 53.48           C  
ATOM    508  C   LYS A 603     -51.631   8.771  19.919  1.00 53.80           C  
ATOM    509  O   LYS A 603     -52.197   8.907  21.009  1.00 51.38           O  
ATOM    510  CB  LYS A 603     -50.846  10.767  18.586  1.00 54.58           C  
ATOM    511  CG  LYS A 603     -52.008  11.626  19.049  1.00 54.47           C  
ATOM    512  CD  LYS A 603     -52.088  12.845  18.139  1.00 57.98           C  
ATOM    513  CE  LYS A 603     -53.509  13.314  17.971  1.00 66.34           C  
ATOM    514  NZ  LYS A 603     -54.353  12.331  17.258  1.00 67.79           N  
ATOM    515  N   LYS A 604     -51.980   7.850  19.028  1.00 52.01           N  
ATOM    516  CA  LYS A 604     -53.128   6.975  19.211  1.00 51.25           C  
ATOM    517  C   LYS A 604     -52.937   6.080  20.422  1.00 56.47           C  
ATOM    518  O   LYS A 604     -53.905   5.674  21.067  1.00 59.78           O  
ATOM    519  CB  LYS A 604     -53.323   6.113  17.953  1.00 57.81           C  
ATOM    520  CG  LYS A 604     -54.538   5.174  17.964  1.00 54.12           C  
ATOM    521  N   ASN A 605     -51.682   5.763  20.720  1.00 55.05           N  
ATOM    522  CA  ASN A 605     -51.371   4.832  21.792  1.00 54.09           C  
ATOM    523  C   ASN A 605     -51.078   5.489  23.128  1.00 56.97           C  
ATOM    524  O   ASN A 605     -50.519   4.870  24.020  1.00 60.43           O  
ATOM    525  CB  ASN A 605     -50.231   3.899  21.393  1.00 56.88           C  
ATOM    526  CG  ASN A 605     -50.717   2.746  20.560  1.00 67.88           C  
ATOM    527  OD1 ASN A 605     -51.079   1.692  21.099  1.00 72.42           O  
ATOM    528  ND2 ASN A 605     -50.777   2.946  19.234  1.00 63.89           N  
ATOM    529  N   TYR A 606     -51.441   6.752  23.261  1.00 55.31           N  
ATOM    530  CA  TYR A 606     -51.559   7.329  24.574  1.00 51.53           C  
ATOM    531  C   TYR A 606     -53.044   7.305  24.878  1.00 54.84           C  
ATOM    532  O   TYR A 606     -53.852   7.312  23.953  1.00 55.41           O  
ATOM    533  CB  TYR A 606     -50.978   8.740  24.594  1.00 50.60           C  
ATOM    534  CG  TYR A 606     -49.466   8.766  24.689  1.00 50.71           C  
ATOM    535  CD1 TYR A 606     -48.828   8.671  25.928  1.00 46.26           C  
ATOM    536  CD2 TYR A 606     -48.674   8.891  23.554  1.00 49.35           C  
ATOM    537  CE1 TYR A 606     -47.464   8.701  26.035  1.00 43.38           C  
ATOM    538  CE2 TYR A 606     -47.277   8.913  23.654  1.00 47.07           C  
ATOM    539  CZ  TYR A 606     -46.688   8.809  24.901  1.00 47.34           C  
ATOM    540  OH  TYR A 606     -45.321   8.826  25.030  1.00 46.95           O  
ATOM    541  N   ARG A 607     -53.408   7.242  26.159  1.00 58.00           N  
ATOM    542  CA  ARG A 607     -54.819   7.263  26.558  1.00 61.18           C  
ATOM    543  C   ARG A 607     -55.320   8.675  26.890  1.00 69.32           C  
ATOM    544  O   ARG A 607     -54.755   9.347  27.760  1.00 68.50           O  
ATOM    545  CB  ARG A 607     -55.031   6.352  27.765  1.00 69.17           C  
ATOM    546  CG  ARG A 607     -54.905   4.884  27.435  1.00 70.44           C  
ATOM    547  CD  ARG A 607     -54.581   4.039  28.648  1.00 70.36           C  
ATOM    548  NE  ARG A 607     -54.312   2.670  28.234  1.00 75.92           N  
ATOM    549  CZ  ARG A 607     -55.239   1.836  27.764  1.00 81.81           C  
ATOM    550  NH1 ARG A 607     -56.503   2.227  27.657  1.00 79.27           N  
ATOM    551  NH2 ARG A 607     -54.901   0.606  27.404  1.00 85.44           N  
ATOM    552  N   LYS A 608     -56.377   9.123  26.209  1.00 71.84           N  
ATOM    553  CA  LYS A 608     -56.945  10.449  26.478  1.00 69.47           C  
ATOM    554  C   LYS A 608     -57.557  10.517  27.885  1.00 72.04           C  
ATOM    555  O   LYS A 608     -57.470  11.545  28.557  1.00 69.04           O  
ATOM    556  CB  LYS A 608     -57.977  10.836  25.413  1.00 68.91           C  
ATOM    557  CG  LYS A 608     -57.887  12.299  24.953  1.00 74.93           C  
ATOM    558  N   ASN A 609     -58.144   9.405  28.327  1.00 68.63           N  
ATOM    559  CA  ASN A 609     -58.760   9.305  29.650  1.00 71.45           C  
ATOM    560  C   ASN A 609     -57.810   9.522  30.858  1.00 72.80           C  
ATOM    561  O   ASN A 609     -58.254   9.609  32.006  1.00 69.82           O  
ATOM    562  CB  ASN A 609     -59.541   7.978  29.778  1.00 76.77           C  
ATOM    563  CG  ASN A 609     -58.720   6.748  29.343  1.00 82.34           C  
ATOM    564  OD1 ASN A 609     -58.668   6.382  28.148  1.00 77.31           O  
ATOM    565  ND2 ASN A 609     -58.094   6.093  30.323  1.00 77.35           N  
ATOM    566  N   VAL A 610     -56.511   9.626  30.598  1.00 69.06           N  
ATOM    567  CA  VAL A 610     -55.538   9.873  31.659  1.00 62.23           C  
ATOM    568  C   VAL A 610     -55.160  11.350  31.686  1.00 61.37           C  
ATOM    569  O   VAL A 610     -54.666  11.882  30.698  1.00 60.29           O  
ATOM    570  CB  VAL A 610     -54.272   9.027  31.456  1.00 64.10           C  
ATOM    571  CG1 VAL A 610     -53.268   9.266  32.588  1.00 62.57           C  
ATOM    572  CG2 VAL A 610     -54.640   7.549  31.357  1.00 65.53           C  
ATOM    573  N   ALA A 611     -55.383  12.005  32.822  1.00 59.74           N  
ATOM    574  CA  ALA A 611     -55.323  13.463  32.898  1.00 55.47           C  
ATOM    575  C   ALA A 611     -53.969  14.102  32.534  1.00 61.35           C  
ATOM    576  O   ALA A 611     -53.911  15.069  31.770  1.00 57.43           O  
ATOM    577  CB  ALA A 611     -55.782  13.934  34.265  1.00 59.96           C  
ATOM    578  N   TYR A 612     -52.881  13.585  33.087  1.00 59.36           N  
ATOM    579  CA  TYR A 612     -51.585  14.169  32.782  1.00 57.19           C  
ATOM    580  C   TYR A 612     -50.782  13.343  31.786  1.00 55.80           C  
ATOM    581  O   TYR A 612     -50.336  13.849  30.751  1.00 57.89           O  
ATOM    582  CB  TYR A 612     -50.767  14.354  34.058  1.00 55.42           C  
ATOM    583  CG  TYR A 612     -49.382  14.885  33.798  1.00 51.24           C  
ATOM    584  CD1 TYR A 612     -49.189  16.154  33.266  1.00 46.86           C  
ATOM    585  CD2 TYR A 612     -48.267  14.114  34.083  1.00 54.26           C  
ATOM    586  CE1 TYR A 612     -47.925  16.641  33.032  1.00 47.44           C  
ATOM    587  CE2 TYR A 612     -46.998  14.584  33.856  1.00 54.85           C  
ATOM    588  CZ  TYR A 612     -46.826  15.843  33.329  1.00 58.18           C  
ATOM    589  OH  TYR A 612     -45.537  16.292  33.127  1.00 65.99           O  
ATOM    590  N   HIS A 613     -50.571  12.079  32.126  1.00 55.49           N  
ATOM    591  CA  HIS A 613     -49.678  11.229  31.353  1.00 56.47           C  
ATOM    592  C   HIS A 613     -50.355  10.781  30.059  1.00 54.99           C  
ATOM    593  O   HIS A 613     -50.877   9.680  29.962  1.00 54.75           O  
ATOM    594  CB  HIS A 613     -49.194  10.033  32.181  1.00 52.98           C  
ATOM    595  CG  HIS A 613     -48.115  10.374  33.164  1.00 53.80           C  
ATOM    596  ND1 HIS A 613     -48.328  10.404  34.525  1.00 55.27           N  
ATOM    597  CD2 HIS A 613     -46.815  10.698  32.982  1.00 57.40           C  
ATOM    598  CE1 HIS A 613     -47.210  10.744  35.139  1.00 56.94           C  
ATOM    599  NE2 HIS A 613     -46.274  10.923  34.225  1.00 60.20           N  
ATOM    600  N   ASN A 614     -50.323  11.653  29.059  1.00 53.01           N  
ATOM    601  CA  ASN A 614     -50.961  11.382  27.790  1.00 48.44           C  
ATOM    602  C   ASN A 614     -50.161  12.020  26.678  1.00 47.32           C  
ATOM    603  O   ASN A 614     -49.105  12.598  26.922  1.00 46.92           O  
ATOM    604  CB  ASN A 614     -52.365  11.951  27.813  1.00 49.59           C  
ATOM    605  CG  ASN A 614     -52.389  13.360  28.340  1.00 51.11           C  
ATOM    606  OD1 ASN A 614     -51.640  14.229  27.873  1.00 50.26           O  
ATOM    607  ND2 ASN A 614     -53.214  13.589  29.350  1.00 51.46           N  
ATOM    608  N   TRP A 615     -50.671  11.922  25.458  1.00 43.03           N  
ATOM    609  CA  TRP A 615     -49.993  12.495  24.323  1.00 41.46           C  
ATOM    610  C   TRP A 615     -49.468  13.909  24.575  1.00 46.69           C  
ATOM    611  O   TRP A 615     -48.343  14.234  24.184  1.00 47.35           O  
ATOM    612  CB  TRP A 615     -50.917  12.490  23.110  1.00 46.65           C  
ATOM    613  CG  TRP A 615     -50.422  13.361  22.021  1.00 46.61           C  
ATOM    614  CD1 TRP A 615     -51.005  14.496  21.550  1.00 45.61           C  
ATOM    615  CD2 TRP A 615     -49.207  13.196  21.289  1.00 50.33           C  
ATOM    616  NE1 TRP A 615     -50.237  15.041  20.557  1.00 48.39           N  
ATOM    617  CE2 TRP A 615     -49.123  14.263  20.377  1.00 51.73           C  
ATOM    618  CE3 TRP A 615     -48.182  12.240  21.307  1.00 51.65           C  
ATOM    619  CZ2 TRP A 615     -48.053  14.402  19.478  1.00 56.43           C  
ATOM    620  CZ3 TRP A 615     -47.114  12.382  20.413  1.00 52.26           C  
ATOM    621  CH2 TRP A 615     -47.060  13.455  19.516  1.00 51.54           C  
ATOM    622  N   ARG A 616     -50.262  14.761  25.220  1.00 44.82           N  
ATOM    623  CA  ARG A 616     -49.823  16.141  25.378  1.00 45.69           C  
ATOM    624  C   ARG A 616     -48.542  16.223  26.191  1.00 45.38           C  
ATOM    625  O   ARG A 616     -47.665  17.051  25.919  1.00 45.87           O  
ATOM    626  CB  ARG A 616     -50.918  17.015  25.971  1.00 45.48           C  
ATOM    627  CG  ARG A 616     -52.129  17.196  25.069  1.00 47.79           C  
ATOM    628  CD  ARG A 616     -51.721  17.707  23.672  1.00 53.30           C  
ATOM    629  NE  ARG A 616     -52.867  17.856  22.770  1.00 58.90           N  
ATOM    630  CZ  ARG A 616     -53.275  19.019  22.262  1.00 55.01           C  
ATOM    631  NH1 ARG A 616     -52.627  20.136  22.562  1.00 51.29           N  
ATOM    632  NH2 ARG A 616     -54.327  19.065  21.458  1.00 47.98           N  
ATOM    633  N   HIS A 617     -48.415  15.337  27.172  1.00 46.60           N  
ATOM    634  CA  HIS A 617     -47.213  15.312  28.002  1.00 42.84           C  
ATOM    635  C   HIS A 617     -46.020  14.806  27.204  1.00 45.24           C  
ATOM    636  O   HIS A 617     -44.911  15.327  27.318  1.00 41.83           O  
ATOM    637  CB  HIS A 617     -47.430  14.450  29.242  1.00 48.44           C  
ATOM    638  CG  HIS A 617     -46.158  14.038  29.902  1.00 49.12           C  
ATOM    639  ND1 HIS A 617     -45.245  14.946  30.384  1.00 45.71           N  
ATOM    640  CD2 HIS A 617     -45.624  12.818  30.121  1.00 52.08           C  
ATOM    641  CE1 HIS A 617     -44.209  14.306  30.882  1.00 45.03           C  
ATOM    642  NE2 HIS A 617     -44.417  13.012  30.743  1.00 51.85           N  
ATOM    643  N   ALA A 618     -46.266  13.794  26.376  1.00 45.02           N  
ATOM    644  CA  ALA A 618     -45.226  13.240  25.529  1.00 42.61           C  
ATOM    645  C   ALA A 618     -44.789  14.275  24.525  1.00 42.58           C  
ATOM    646  O   ALA A 618     -43.594  14.402  24.224  1.00 43.78           O  
ATOM    647  CB  ALA A 618     -45.717  12.004  24.817  1.00 45.16           C  
ATOM    648  N   PHE A 619     -45.770  15.011  24.012  1.00 43.20           N  
ATOM    649  CA  PHE A 619     -45.514  16.048  23.032  1.00 44.60           C  
ATOM    650  C   PHE A 619     -44.667  17.154  23.633  1.00 45.50           C  
ATOM    651  O   PHE A 619     -43.713  17.610  23.014  1.00 45.24           O  
ATOM    652  CB  PHE A 619     -46.820  16.613  22.489  1.00 47.08           C  
ATOM    653  CG  PHE A 619     -46.630  17.801  21.601  1.00 50.05           C  
ATOM    654  CD1 PHE A 619     -45.881  17.698  20.434  1.00 51.50           C  
ATOM    655  CD2 PHE A 619     -47.195  19.028  21.927  1.00 47.62           C  
ATOM    656  CE1 PHE A 619     -45.699  18.802  19.601  1.00 54.83           C  
ATOM    657  CE2 PHE A 619     -47.012  20.139  21.097  1.00 52.35           C  
ATOM    658  CZ  PHE A 619     -46.267  20.026  19.936  1.00 49.25           C  
ATOM    659  N   ASN A 620     -45.000  17.551  24.859  1.00 44.24           N  
ATOM    660  CA  ASN A 620     -44.221  18.548  25.574  1.00 42.52           C  
ATOM    661  C   ASN A 620     -42.809  18.119  25.925  1.00 41.93           C  
ATOM    662  O   ASN A 620     -41.856  18.892  25.816  1.00 43.98           O  
ATOM    663  CB  ASN A 620     -44.991  19.006  26.803  1.00 42.93           C  
ATOM    664  CG  ASN A 620     -45.996  20.093  26.460  1.00 46.20           C  
ATOM    665  OD1 ASN A 620     -45.629  21.128  25.898  1.00 51.36           O  
ATOM    666  ND2 ASN A 620     -47.257  19.843  26.729  1.00 38.94           N  
ATOM    667  N   THR A 621     -42.672  16.871  26.336  1.00 42.23           N  
ATOM    668  CA  THR A 621     -41.360  16.323  26.593  1.00 41.92           C  
ATOM    669  C   THR A 621     -40.460  16.445  25.375  1.00 44.77           C  
ATOM    670  O   THR A 621     -39.318  16.921  25.493  1.00 44.39           O  
ATOM    671  CB  THR A 621     -41.452  14.884  27.044  1.00 41.74           C  
ATOM    672  OG1 THR A 621     -42.405  14.810  28.105  1.00 47.24           O  
ATOM    673  CG2 THR A 621     -40.104  14.398  27.546  1.00 39.81           C  
ATOM    674  N   ALA A 622     -40.972  16.046  24.206  1.00 41.99           N  
ATOM    675  CA  ALA A 622     -40.206  16.186  22.963  1.00 42.94           C  
ATOM    676  C   ALA A 622     -39.911  17.642  22.576  1.00 47.31           C  
ATOM    677  O   ALA A 622     -38.790  17.962  22.161  1.00 46.21           O  
ATOM    678  CB  ALA A 622     -40.877  15.463  21.834  1.00 44.29           C  
ATOM    679  N   GLN A 623     -40.903  18.522  22.719  1.00 43.79           N  
ATOM    680  CA  GLN A 623     -40.695  19.931  22.434  1.00 43.64           C  
ATOM    681  C   GLN A 623     -39.598  20.488  23.342  1.00 45.55           C  
ATOM    682  O   GLN A 623     -38.713  21.224  22.907  1.00 43.42           O  
ATOM    683  CB  GLN A 623     -42.000  20.705  22.605  1.00 47.33           C  
ATOM    684  CG  GLN A 623     -41.920  22.202  22.303  1.00 46.28           C  
ATOM    685  CD  GLN A 623     -41.255  23.008  23.403  1.00 45.65           C  
ATOM    686  OE1 GLN A 623     -41.536  22.821  24.592  1.00 48.93           O  
ATOM    687  NE2 GLN A 623     -40.378  23.923  23.011  1.00 45.91           N  
ATOM    688  N   CYS A 624     -39.629  20.112  24.612  1.00 44.71           N  
ATOM    689  CA  CYS A 624     -38.548  20.547  25.477  1.00 47.40           C  
ATOM    690  C   CYS A 624     -37.192  19.969  25.066  1.00 47.80           C  
ATOM    691  O   CYS A 624     -36.165  20.623  25.200  1.00 47.25           O  
ATOM    692  CB  CYS A 624     -38.837  20.218  26.925  1.00 47.37           C  
ATOM    693  SG  CYS A 624     -37.460  20.761  27.942  1.00 59.83           S  
ATOM    694  N   MET A 625     -37.193  18.731  24.583  1.00 49.18           N  
ATOM    695  CA  MET A 625     -35.979  18.142  24.028  1.00 51.71           C  
ATOM    696  C   MET A 625     -35.473  19.017  22.884  1.00 49.52           C  
ATOM    697  O   MET A 625     -34.314  19.439  22.841  1.00 50.31           O  
ATOM    698  CB  MET A 625     -36.243  16.711  23.533  1.00 49.60           C  
ATOM    699  CG  MET A 625     -34.982  15.989  23.004  1.00 49.19           C  
ATOM    700  SD  MET A 625     -33.684  15.772  24.254  1.00 56.40           S  
ATOM    701  CE  MET A 625     -34.507  14.691  25.423  1.00 50.64           C  
ATOM    702  N   PHE A 626     -36.372  19.293  21.961  1.00 48.02           N  
ATOM    703  CA  PHE A 626     -36.056  20.131  20.828  1.00 52.74           C  
ATOM    704  C   PHE A 626     -35.434  21.460  21.264  1.00 56.48           C  
ATOM    705  O   PHE A 626     -34.375  21.858  20.784  1.00 56.90           O  
ATOM    706  CB  PHE A 626     -37.325  20.386  20.028  1.00 53.64           C  
ATOM    707  CG  PHE A 626     -37.087  21.123  18.767  1.00 56.69           C  
ATOM    708  CD1 PHE A 626     -36.689  20.446  17.626  1.00 55.94           C  
ATOM    709  CD2 PHE A 626     -37.239  22.494  18.718  1.00 59.84           C  
ATOM    710  CE1 PHE A 626     -36.444  21.115  16.457  1.00 60.59           C  
ATOM    711  CE2 PHE A 626     -37.001  23.188  17.540  1.00 64.69           C  
ATOM    712  CZ  PHE A 626     -36.603  22.499  16.405  1.00 64.38           C  
ATOM    713  N   ALA A 627     -36.097  22.146  22.182  1.00 54.22           N  
ATOM    714  CA  ALA A 627     -35.630  23.453  22.595  1.00 55.69           C  
ATOM    715  C   ALA A 627     -34.255  23.344  23.224  1.00 55.53           C  
ATOM    716  O   ALA A 627     -33.405  24.187  23.004  1.00 57.61           O  
ATOM    717  CB  ALA A 627     -36.630  24.106  23.562  1.00 55.47           C  
ATOM    718  N   ALA A 628     -34.036  22.293  24.005  1.00 55.80           N  
ATOM    719  CA  ALA A 628     -32.742  22.100  24.648  1.00 58.49           C  
ATOM    720  C   ALA A 628     -31.681  21.770  23.602  1.00 60.94           C  
ATOM    721  O   ALA A 628     -30.499  22.012  23.809  1.00 62.39           O  
ATOM    722  CB  ALA A 628     -32.813  21.010  25.730  1.00 51.32           C  
ATOM    723  N   LEU A 629     -32.108  21.219  22.472  1.00 61.02           N  
ATOM    724  CA  LEU A 629     -31.170  20.923  21.392  1.00 63.34           C  
ATOM    725  C   LEU A 629     -30.806  22.166  20.590  1.00 64.81           C  
ATOM    726  O   LEU A 629     -29.630  22.410  20.322  1.00 67.53           O  
ATOM    727  CB  LEU A 629     -31.706  19.820  20.477  1.00 59.08           C  
ATOM    728  CG  LEU A 629     -31.645  18.449  21.158  1.00 64.27           C  
ATOM    729  CD1 LEU A 629     -32.256  17.346  20.291  1.00 61.07           C  
ATOM    730  CD2 LEU A 629     -30.220  18.104  21.575  1.00 58.75           C  
ATOM    731  N   LYS A 630     -31.816  22.948  20.221  1.00 62.71           N  
ATOM    732  CA  LYS A 630     -31.616  24.156  19.426  1.00 63.39           C  
ATOM    733  C   LYS A 630     -31.286  25.363  20.302  1.00 62.77           C  
ATOM    734  O   LYS A 630     -30.140  25.786  20.384  1.00 66.20           O  
ATOM    735  CB  LYS A 630     -32.850  24.443  18.567  1.00 65.62           C  
ATOM    736  CG  LYS A 630     -33.147  23.391  17.498  1.00 64.23           C  
ATOM    737  CD  LYS A 630     -32.035  23.302  16.466  1.00 66.62           C  
ATOM    738  CE  LYS A 630     -32.535  22.652  15.160  1.00 72.78           C  
ATOM    739  NZ  LYS A 630     -31.459  22.429  14.119  1.00 70.81           N  
ATOM    740  N   ALA A 631     -32.291  25.917  20.965  1.00 67.46           N  
ATOM    741  CA  ALA A 631     -32.069  27.063  21.846  1.00 64.71           C  
ATOM    742  C   ALA A 631     -31.035  26.750  22.939  1.00 65.72           C  
ATOM    743  O   ALA A 631     -30.186  27.579  23.262  1.00 68.30           O  
ATOM    744  CB  ALA A 631     -33.403  27.543  22.453  1.00 63.08           C  
ATOM    745  N   GLY A 632     -31.098  25.541  23.492  1.00 68.59           N  
ATOM    746  CA  GLY A 632     -30.185  25.131  24.551  1.00 69.21           C  
ATOM    747  C   GLY A 632     -28.793  24.781  24.053  1.00 69.64           C  
ATOM    748  O   GLY A 632     -27.910  24.457  24.856  1.00 67.41           O  
ATOM    749  N   LYS A 633     -28.608  24.843  22.731  1.00 66.28           N  
ATOM    750  CA  LYS A 633     -27.315  24.596  22.096  1.00 70.06           C  
ATOM    751  C   LYS A 633     -26.682  23.279  22.552  1.00 74.06           C  
ATOM    752  O   LYS A 633     -25.511  23.252  22.946  1.00 78.98           O  
ATOM    753  CB  LYS A 633     -26.353  25.769  22.345  1.00 70.52           C  
ATOM    754  CG  LYS A 633     -26.688  27.032  21.544  1.00 74.12           C  
ATOM    755  CD  LYS A 633     -25.789  28.213  21.912  1.00 74.75           C  
ATOM    756  N   ILE A 634     -27.459  22.197  22.493  1.00 69.08           N  
ATOM    757  CA  ILE A 634     -26.996  20.876  22.917  1.00 68.59           C  
ATOM    758  C   ILE A 634     -26.811  19.958  21.701  1.00 70.65           C  
ATOM    759  O   ILE A 634     -26.031  19.004  21.726  1.00 69.64           O  
ATOM    760  CB  ILE A 634     -27.965  20.255  23.945  1.00 64.88           C  
ATOM    761  CG1 ILE A 634     -27.800  20.958  25.293  1.00 67.94           C  
ATOM    762  CG2 ILE A 634     -27.721  18.757  24.091  1.00 64.01           C  
ATOM    763  CD1 ILE A 634     -28.806  20.554  26.338  1.00 63.42           C  
ATOM    764  N   GLN A 635     -27.532  20.274  20.635  1.00 65.81           N  
ATOM    765  CA  GLN A 635     -27.372  19.607  19.352  1.00 71.46           C  
ATOM    766  C   GLN A 635     -25.910  19.334  18.990  1.00 75.55           C  
ATOM    767  O   GLN A 635     -25.566  18.245  18.515  1.00 74.06           O  
ATOM    768  CB  GLN A 635     -27.984  20.488  18.277  1.00 67.04           C  
ATOM    769  CG  GLN A 635     -28.055  19.884  16.920  1.00 68.22           C  
ATOM    770  CD  GLN A 635     -28.812  20.796  15.987  1.00 72.88           C  
ATOM    771  OE1 GLN A 635     -28.863  22.013  16.210  1.00 74.03           O  
ATOM    772  NE2 GLN A 635     -29.428  20.224  14.956  1.00 65.31           N  
ATOM    773  N   ASN A 636     -25.058  20.334  19.205  1.00 74.47           N  
ATOM    774  CA  ASN A 636     -23.674  20.278  18.743  1.00 75.94           C  
ATOM    775  C   ASN A 636     -22.757  19.522  19.705  1.00 77.85           C  
ATOM    776  O   ASN A 636     -21.543  19.469  19.514  1.00 84.27           O  
ATOM    777  CB  ASN A 636     -23.135  21.689  18.456  1.00 72.38           C  
ATOM    778  N   LYS A 637     -23.338  18.929  20.739  1.00 74.11           N  
ATOM    779  CA  LYS A 637     -22.564  18.080  21.637  1.00 74.98           C  
ATOM    780  C   LYS A 637     -22.852  16.598  21.381  1.00 73.86           C  
ATOM    781  O   LYS A 637     -22.239  15.726  22.000  1.00 71.35           O  
ATOM    782  CB  LYS A 637     -22.850  18.433  23.100  1.00 76.13           C  
ATOM    783  CG  LYS A 637     -22.295  19.793  23.547  1.00 86.07           C  
ATOM    784  CD  LYS A 637     -22.553  20.067  25.041  1.00 84.49           C  
ATOM    785  CE  LYS A 637     -21.835  21.331  25.503  1.00 80.36           C  
ATOM    786  NZ  LYS A 637     -22.204  22.507  24.655  1.00 80.80           N  
ATOM    787  N   LEU A 638     -23.777  16.328  20.459  1.00 68.05           N  
ATOM    788  CA  LEU A 638     -24.288  14.982  20.238  1.00 65.42           C  
ATOM    789  C   LEU A 638     -24.250  14.548  18.764  1.00 67.25           C  
ATOM    790  O   LEU A 638     -24.168  15.383  17.860  1.00 64.60           O  
ATOM    791  CB  LEU A 638     -25.727  14.882  20.744  1.00 62.63           C  
ATOM    792  CG  LEU A 638     -26.049  15.356  22.159  1.00 64.61           C  
ATOM    793  CD1 LEU A 638     -27.515  15.123  22.461  1.00 57.65           C  
ATOM    794  CD2 LEU A 638     -25.190  14.667  23.203  1.00 66.87           C  
ATOM    795  N   THR A 639     -24.326  13.235  18.540  1.00 65.60           N  
ATOM    796  CA  THR A 639     -24.366  12.670  17.194  1.00 64.52           C  
ATOM    797  C   THR A 639     -25.793  12.658  16.683  1.00 64.82           C  
ATOM    798  O   THR A 639     -26.737  12.593  17.472  1.00 64.77           O  
ATOM    799  CB  THR A 639     -23.792  11.218  17.137  1.00 63.08           C  
ATOM    800  OG1 THR A 639     -24.678  10.293  17.796  1.00 60.63           O  
ATOM    801  CG2 THR A 639     -22.415  11.163  17.783  1.00 62.20           C  
ATOM    802  N   ASP A 640     -25.942  12.735  15.365  1.00 63.67           N  
ATOM    803  CA  ASP A 640     -27.237  12.575  14.729  1.00 65.31           C  
ATOM    804  C   ASP A 640     -28.009  11.422  15.333  1.00 59.74           C  
ATOM    805  O   ASP A 640     -29.202  11.535  15.589  1.00 61.46           O  
ATOM    806  CB  ASP A 640     -27.077  12.315  13.227  1.00 73.19           C  
ATOM    807  CG  ASP A 640     -26.799  13.580  12.436  1.00 77.52           C  
ATOM    808  OD1 ASP A 640     -27.014  14.690  12.980  1.00 77.76           O  
ATOM    809  OD2 ASP A 640     -26.380  13.456  11.264  1.00 77.17           O  
ATOM    810  N   LEU A 641     -27.336  10.301  15.542  1.00 58.49           N  
ATOM    811  CA  LEU A 641     -28.039   9.109  15.995  1.00 61.79           C  
ATOM    812  C   LEU A 641     -28.565   9.280  17.406  1.00 57.54           C  
ATOM    813  O   LEU A 641     -29.672   8.843  17.718  1.00 58.30           O  
ATOM    814  CB  LEU A 641     -27.166   7.856  15.878  1.00 62.99           C  
ATOM    815  CG  LEU A 641     -26.943   7.375  14.440  1.00 58.91           C  
ATOM    816  CD1 LEU A 641     -26.087   6.134  14.415  1.00 58.68           C  
ATOM    817  CD2 LEU A 641     -28.272   7.102  13.772  1.00 58.01           C  
ATOM    818  N   GLU A 642     -27.774   9.917  18.258  1.00 57.04           N  
ATOM    819  CA  GLU A 642     -28.229  10.221  19.607  1.00 57.73           C  
ATOM    820  C   GLU A 642     -29.492  11.073  19.562  1.00 54.84           C  
ATOM    821  O   GLU A 642     -30.459  10.832  20.277  1.00 56.46           O  
ATOM    822  CB  GLU A 642     -27.121  10.917  20.393  1.00 57.68           C  
ATOM    823  CG  GLU A 642     -26.114   9.927  20.945  1.00 64.12           C  
ATOM    824  CD  GLU A 642     -24.716  10.500  21.132  1.00 68.72           C  
ATOM    825  OE1 GLU A 642     -24.452  11.615  20.637  1.00 68.18           O  
ATOM    826  OE2 GLU A 642     -23.878   9.818  21.769  1.00 69.09           O  
ATOM    827  N   ILE A 643     -29.479  12.058  18.685  1.00 55.67           N  
ATOM    828  CA  ILE A 643     -30.562  13.013  18.595  1.00 55.65           C  
ATOM    829  C   ILE A 643     -31.832  12.336  18.117  1.00 53.59           C  
ATOM    830  O   ILE A 643     -32.912  12.506  18.699  1.00 50.98           O  
ATOM    831  CB  ILE A 643     -30.175  14.144  17.639  1.00 54.25           C  
ATOM    832  CG1 ILE A 643     -29.186  15.077  18.337  1.00 57.29           C  
ATOM    833  CG2 ILE A 643     -31.407  14.872  17.144  1.00 50.74           C  
ATOM    834  CD1 ILE A 643     -28.282  15.816  17.397  1.00 62.34           C  
ATOM    835  N   LEU A 644     -31.685  11.567  17.049  1.00 52.45           N  
ATOM    836  CA  LEU A 644     -32.789  10.828  16.477  1.00 52.37           C  
ATOM    837  C   LEU A 644     -33.431  10.008  17.591  1.00 50.60           C  
ATOM    838  O   LEU A 644     -34.651  10.015  17.786  1.00 48.97           O  
ATOM    839  CB  LEU A 644     -32.255   9.939  15.356  1.00 51.61           C  
ATOM    840  CG  LEU A 644     -33.153   8.805  14.876  1.00 54.15           C  
ATOM    841  CD1 LEU A 644     -34.500   9.335  14.433  1.00 50.53           C  
ATOM    842  CD2 LEU A 644     -32.462   8.053  13.751  1.00 55.36           C  
ATOM    843  N   ALA A 645     -32.570   9.350  18.354  1.00 50.41           N  
ATOM    844  CA  ALA A 645     -32.971   8.467  19.427  1.00 49.09           C  
ATOM    845  C   ALA A 645     -33.647   9.211  20.570  1.00 48.36           C  
ATOM    846  O   ALA A 645     -34.662   8.768  21.092  1.00 48.42           O  
ATOM    847  CB  ALA A 645     -31.764   7.720  19.924  1.00 53.22           C  
ATOM    848  N   LEU A 646     -33.074  10.340  20.966  1.00 49.46           N  
ATOM    849  CA  LEU A 646     -33.659  11.163  22.015  1.00 48.79           C  
ATOM    850  C   LEU A 646     -35.043  11.677  21.639  1.00 49.23           C  
ATOM    851  O   LEU A 646     -35.938  11.758  22.487  1.00 46.33           O  
ATOM    852  CB  LEU A 646     -32.756  12.348  22.308  1.00 48.40           C  
ATOM    853  CG  LEU A 646     -31.501  12.053  23.115  1.00 53.58           C  
ATOM    854  CD1 LEU A 646     -30.643  13.319  23.211  1.00 49.85           C  
ATOM    855  CD2 LEU A 646     -31.872  11.523  24.511  1.00 51.93           C  
ATOM    856  N   LEU A 647     -35.224  12.033  20.372  1.00 43.34           N  
ATOM    857  CA  LEU A 647     -36.492  12.588  19.981  1.00 44.72           C  
ATOM    858  C   LEU A 647     -37.565  11.513  20.030  1.00 47.59           C  
ATOM    859  O   LEU A 647     -38.665  11.739  20.535  1.00 46.61           O  
ATOM    860  CB  LEU A 647     -36.422  13.217  18.591  1.00 49.63           C  
ATOM    861  CG  LEU A 647     -37.706  14.010  18.305  1.00 53.90           C  
ATOM    862  CD1 LEU A 647     -37.738  15.224  19.225  1.00 54.52           C  
ATOM    863  CD2 LEU A 647     -37.862  14.447  16.848  1.00 53.72           C  
ATOM    864  N   ILE A 648     -37.245  10.341  19.498  1.00 48.19           N  
ATOM    865  CA  ILE A 648     -38.201   9.249  19.482  1.00 47.35           C  
ATOM    866  C   ILE A 648     -38.455   8.780  20.898  1.00 43.67           C  
ATOM    867  O   ILE A 648     -39.591   8.540  21.288  1.00 43.80           O  
ATOM    868  CB  ILE A 648     -37.687   8.069  18.665  1.00 49.32           C  
ATOM    869  CG1 ILE A 648     -37.805   8.362  17.182  1.00 47.55           C  
ATOM    870  CG2 ILE A 648     -38.480   6.817  18.980  1.00 50.27           C  
ATOM    871  CD1 ILE A 648     -36.675   7.764  16.375  1.00 48.05           C  
ATOM    872  N   ALA A 649     -37.388   8.630  21.662  1.00 42.37           N  
ATOM    873  CA  ALA A 649     -37.531   8.305  23.069  1.00 45.94           C  
ATOM    874  C   ALA A 649     -38.457   9.318  23.748  1.00 44.84           C  
ATOM    875  O   ALA A 649     -39.385   8.937  24.463  1.00 44.31           O  
ATOM    876  CB  ALA A 649     -36.167   8.254  23.761  1.00 45.73           C  
ATOM    877  N   ALA A 650     -38.217  10.605  23.522  1.00 41.63           N  
ATOM    878  CA  ALA A 650     -39.024  11.636  24.189  1.00 43.86           C  
ATOM    879  C   ALA A 650     -40.519  11.483  23.890  1.00 42.45           C  
ATOM    880  O   ALA A 650     -41.357  11.505  24.799  1.00 41.21           O  
ATOM    881  CB  ALA A 650     -38.523  13.033  23.844  1.00 41.13           C  
ATOM    882  N   LEU A 651     -40.839  11.291  22.613  1.00 44.74           N  
ATOM    883  CA  LEU A 651     -42.211  11.044  22.174  1.00 44.22           C  
ATOM    884  C   LEU A 651     -42.825   9.733  22.681  1.00 44.46           C  
ATOM    885  O   LEU A 651     -44.035   9.636  22.908  1.00 45.43           O  
ATOM    886  CB  LEU A 651     -42.265  11.085  20.653  1.00 44.57           C  
ATOM    887  CG  LEU A 651     -42.034  12.509  20.133  1.00 53.10           C  
ATOM    888  CD1 LEU A 651     -41.645  12.502  18.655  1.00 53.89           C  
ATOM    889  CD2 LEU A 651     -43.257  13.439  20.386  1.00 46.86           C  
ATOM    890  N   SER A 652     -41.986   8.732  22.886  1.00 46.55           N  
ATOM    891  CA  SER A 652     -42.478   7.402  23.185  1.00 44.83           C  
ATOM    892  C   SER A 652     -42.453   7.017  24.666  1.00 43.91           C  
ATOM    893  O   SER A 652     -43.152   6.082  25.041  1.00 43.92           O  
ATOM    894  CB  SER A 652     -41.691   6.383  22.367  1.00 47.78           C  
ATOM    895  OG  SER A 652     -41.646   6.755  20.992  1.00 49.06           O  
ATOM    896  N   HIS A 653     -41.701   7.759  25.490  1.00 39.12           N  
ATOM    897  CA  HIS A 653     -41.307   7.338  26.854  1.00 41.34           C  
ATOM    898  C   HIS A 653     -42.406   7.047  27.872  1.00 42.77           C  
ATOM    899  O   HIS A 653     -42.124   6.530  28.940  1.00 46.82           O  
ATOM    900  CB  HIS A 653     -40.367   8.363  27.498  1.00 45.35           C  
ATOM    901  CG  HIS A 653     -41.091   9.525  28.111  1.00 46.43           C  
ATOM    902  ND1 HIS A 653     -41.388  10.672  27.407  1.00 47.42           N  
ATOM    903  CD2 HIS A 653     -41.615   9.696  29.344  1.00 43.69           C  
ATOM    904  CE1 HIS A 653     -42.058  11.501  28.188  1.00 49.58           C  
ATOM    905  NE2 HIS A 653     -42.212  10.932  29.367  1.00 45.65           N  
ATOM    906  N   ASP A 654     -43.647   7.399  27.577  1.00 47.05           N  
ATOM    907  CA  ASP A 654     -44.739   7.014  28.451  1.00 44.30           C  
ATOM    908  C   ASP A 654     -45.875   6.345  27.669  1.00 45.41           C  
ATOM    909  O   ASP A 654     -47.010   6.380  28.110  1.00 47.56           O  
ATOM    910  CB  ASP A 654     -45.293   8.239  29.172  1.00 46.10           C  
ATOM    911  CG  ASP A 654     -44.545   8.589  30.448  1.00 51.04           C  
ATOM    912  OD1 ASP A 654     -43.949   7.722  31.147  1.00 55.82           O  
ATOM    913  OD2 ASP A 654     -44.589   9.783  30.779  1.00 50.61           O  
ATOM    914  N   LEU A 655     -45.595   5.743  26.518  1.00 46.11           N  
ATOM    915  CA  LEU A 655     -46.663   5.133  25.698  1.00 50.59           C  
ATOM    916  C   LEU A 655     -47.607   4.198  26.463  1.00 52.27           C  
ATOM    917  O   LEU A 655     -47.145   3.328  27.186  1.00 53.96           O  
ATOM    918  CB  LEU A 655     -46.068   4.361  24.524  1.00 47.58           C  
ATOM    919  CG  LEU A 655     -45.763   5.115  23.238  1.00 50.58           C  
ATOM    920  CD1 LEU A 655     -44.696   4.415  22.362  1.00 49.47           C  
ATOM    921  CD2 LEU A 655     -47.054   5.309  22.488  1.00 49.27           C  
ATOM    922  N   ASP A 656     -48.918   4.383  26.292  1.00 53.20           N  
ATOM    923  CA  ASP A 656     -49.943   3.497  26.857  1.00 54.27           C  
ATOM    924  C   ASP A 656     -49.991   3.537  28.392  1.00 59.62           C  
ATOM    925  O   ASP A 656     -50.516   2.635  29.040  1.00 62.85           O  
ATOM    926  CB  ASP A 656     -49.725   2.065  26.352  1.00 62.43           C  
ATOM    927  CG  ASP A 656     -50.897   1.130  26.656  1.00 66.62           C  
ATOM    928  OD1 ASP A 656     -52.068   1.528  26.472  1.00 67.33           O  
ATOM    929  OD2 ASP A 656     -50.632  -0.021  27.067  1.00 67.14           O  
ATOM    930  N   HIS A 657     -49.441   4.600  28.964  1.00 58.54           N  
ATOM    931  CA  HIS A 657     -49.482   4.843  30.405  1.00 57.85           C  
ATOM    932  C   HIS A 657     -50.930   4.989  30.962  1.00 62.99           C  
ATOM    933  O   HIS A 657     -51.792   5.621  30.362  1.00 62.72           O  
ATOM    934  CB  HIS A 657     -48.637   6.081  30.701  1.00 53.49           C  
ATOM    935  CG  HIS A 657     -48.377   6.316  32.155  1.00 55.67           C  
ATOM    936  ND1 HIS A 657     -47.105   6.470  32.666  1.00 54.22           N  
ATOM    937  CD2 HIS A 657     -49.224   6.457  33.201  1.00 52.67           C  
ATOM    938  CE1 HIS A 657     -47.182   6.678  33.968  1.00 55.96           C  
ATOM    939  NE2 HIS A 657     -48.456   6.681  34.315  1.00 52.50           N  
ATOM    940  N   ARG A 658     -51.200   4.399  32.117  1.00 65.75           N  
ATOM    941  CA  ARG A 658     -52.583   4.317  32.579  1.00 70.29           C  
ATOM    942  C   ARG A 658     -52.892   5.225  33.765  1.00 70.70           C  
ATOM    943  O   ARG A 658     -53.934   5.094  34.394  1.00 74.73           O  
ATOM    944  CB  ARG A 658     -52.930   2.875  32.934  1.00 70.74           C  
ATOM    945  CG  ARG A 658     -53.853   2.218  31.944  1.00 73.35           C  
ATOM    946  CD  ARG A 658     -53.096   1.401  30.911  1.00 79.58           C  
ATOM    947  NE  ARG A 658     -54.030   0.620  30.100  1.00 90.22           N  
ATOM    948  CZ  ARG A 658     -54.372  -0.644  30.345  1.00 91.33           C  
ATOM    949  NH1 ARG A 658     -53.837  -1.292  31.377  1.00 86.98           N  
ATOM    950  NH2 ARG A 658     -55.246  -1.260  29.551  1.00 88.88           N  
ATOM    951  N   GLY A 659     -51.992   6.152  34.057  1.00 68.89           N  
ATOM    952  CA  GLY A 659     -52.113   6.971  35.243  1.00 67.72           C  
ATOM    953  C   GLY A 659     -51.405   6.303  36.402  1.00 70.25           C  
ATOM    954  O   GLY A 659     -51.533   5.092  36.593  1.00 72.68           O  
ATOM    955  N   VAL A 660     -50.670   7.099  37.176  1.00 69.72           N  
ATOM    956  CA  VAL A 660     -49.876   6.608  38.308  1.00 77.06           C  
ATOM    957  C   VAL A 660     -50.611   5.682  39.294  1.00 83.21           C  
ATOM    958  O   VAL A 660     -49.985   4.871  39.983  1.00 84.39           O  
ATOM    959  CB  VAL A 660     -49.300   7.780  39.110  1.00 72.75           C  
ATOM    960  CG1 VAL A 660     -48.232   8.505  38.295  1.00 69.76           C  
ATOM    961  CG2 VAL A 660     -50.423   8.722  39.526  1.00 71.31           C  
ATOM    962  N   ASN A 661     -51.930   5.812  39.370  1.00 81.60           N  
ATOM    963  CA  ASN A 661     -52.715   4.995  40.284  1.00 84.51           C  
ATOM    964  C   ASN A 661     -53.314   3.739  39.635  1.00 89.31           C  
ATOM    965  O   ASN A 661     -54.398   3.296  40.016  1.00 91.08           O  
ATOM    966  CB  ASN A 661     -53.835   5.836  40.922  1.00 85.88           C  
ATOM    967  CG  ASN A 661     -53.308   6.894  41.887  1.00 86.19           C  
ATOM    968  OD1 ASN A 661     -52.318   6.680  42.591  1.00 85.18           O  
ATOM    969  ND2 ASN A 661     -53.982   8.041  41.930  1.00 81.38           N  
ATOM    970  N   ASN A 662     -52.628   3.157  38.659  1.00 89.61           N  
ATOM    971  CA  ASN A 662     -53.161   1.946  38.030  1.00 93.91           C  
ATOM    972  C   ASN A 662     -52.107   0.845  37.815  1.00 98.40           C  
ATOM    973  O   ASN A 662     -50.944   1.136  37.514  1.00 91.73           O  
ATOM    974  CB  ASN A 662     -53.926   2.291  36.741  1.00 88.65           C  
ATOM    975  CG  ASN A 662     -55.004   3.351  36.964  1.00 81.79           C  
ATOM    976  N   SER A 663     -52.528  -0.413  37.977  1.00103.73           N  
ATOM    977  CA  SER A 663     -51.598  -1.548  38.066  1.00111.04           C  
ATOM    978  C   SER A 663     -51.611  -2.518  36.873  1.00115.67           C  
ATOM    979  O   SER A 663     -52.665  -2.988  36.444  1.00111.82           O  
ATOM    980  CB  SER A 663     -51.836  -2.328  39.365  1.00105.83           C  
ATOM    981  N   TYR A 664     -50.420  -2.813  36.355  1.00121.47           N  
ATOM    982  CA  TYR A 664     -50.234  -3.817  35.312  1.00117.26           C  
ATOM    983  C   TYR A 664     -49.407  -4.977  35.881  1.00124.01           C  
ATOM    984  O   TYR A 664     -48.223  -4.810  36.196  1.00116.49           O  
ATOM    985  CB  TYR A 664     -49.537  -3.202  34.095  1.00103.73           C  
ATOM    986  N   ILE A 665     -50.038  -6.145  36.012  1.00125.55           N  
ATOM    987  CA  ILE A 665     -49.429  -7.298  36.678  1.00125.40           C  
ATOM    988  C   ILE A 665     -48.783  -8.341  35.753  1.00127.64           C  
ATOM    989  O   ILE A 665     -49.304  -8.657  34.680  1.00122.15           O  
ATOM    990  N   GLN A 666     -47.646  -8.872  36.199  1.00127.12           N  
ATOM    991  CA  GLN A 666     -46.907  -9.916  35.489  1.00120.91           C  
ATOM    992  C   GLN A 666     -45.881 -10.555  36.442  1.00126.86           C  
ATOM    993  O   GLN A 666     -45.069  -9.856  37.062  1.00120.50           O  
ATOM    994  N   ARG A 667     -45.927 -11.880  36.566  1.00125.23           N  
ATOM    995  CA  ARG A 667     -45.023 -12.599  37.465  1.00121.01           C  
ATOM    996  C   ARG A 667     -44.823 -11.895  38.815  1.00115.04           C  
ATOM    997  O   ARG A 667     -45.757 -11.772  39.614  1.00109.15           O  
ATOM    998  N   SER A 668     -43.596 -11.443  39.061  1.00110.29           N  
ATOM    999  CA  SER A 668     -43.263 -10.760  40.296  1.00105.66           C  
ATOM   1000  C   SER A 668     -42.161  -9.736  40.106  1.00110.59           C  
ATOM   1001  O   SER A 668     -41.182  -9.982  39.390  1.00103.54           O  
ATOM   1002  N   GLU A 669     -42.328  -8.579  40.746  1.00111.04           N  
ATOM   1003  CA  GLU A 669     -41.339  -7.518  40.695  1.00107.20           C  
ATOM   1004  C   GLU A 669     -40.941  -7.056  42.084  1.00110.36           C  
ATOM   1005  O   GLU A 669     -39.968  -7.546  42.663  1.00106.78           O  
ATOM   1006  N   HIS A 678     -35.601  -3.376  37.273  1.00 95.97           N  
ATOM   1007  CA  HIS A 678     -37.043  -3.606  37.269  1.00 98.50           C  
ATOM   1008  C   HIS A 678     -37.800  -2.275  37.175  1.00100.24           C  
ATOM   1009  O   HIS A 678     -38.555  -1.884  38.083  1.00 96.64           O  
ATOM   1010  CB  HIS A 678     -37.482  -4.383  38.516  1.00101.07           C  
ATOM   1011  CG  HIS A 678     -37.674  -3.519  39.725  1.00106.54           C  
ATOM   1012  ND1 HIS A 678     -36.630  -2.874  40.358  1.00108.78           N  
ATOM   1013  CD2 HIS A 678     -38.795  -3.174  40.403  1.00106.07           C  
ATOM   1014  CE1 HIS A 678     -37.098  -2.175  41.376  1.00108.83           C  
ATOM   1015  NE2 HIS A 678     -38.409  -2.339  41.425  1.00115.61           N  
ATOM   1016  N   SER A 679     -37.578  -1.562  36.079  1.00 90.45           N  
ATOM   1017  CA  SER A 679     -38.412  -0.424  35.764  1.00 74.67           C  
ATOM   1018  C   SER A 679     -39.560  -0.991  34.956  1.00 70.67           C  
ATOM   1019  O   SER A 679     -39.517  -1.009  33.726  1.00 71.45           O  
ATOM   1020  CB  SER A 679     -37.624   0.589  34.952  1.00 73.47           C  
ATOM   1021  OG  SER A 679     -36.431   0.948  35.627  1.00 76.03           O  
ATOM   1022  N   ILE A 680     -40.566  -1.491  35.663  1.00 67.50           N  
ATOM   1023  CA  ILE A 680     -41.656  -2.250  35.059  1.00 67.00           C  
ATOM   1024  C   ILE A 680     -42.300  -1.475  33.945  1.00 65.76           C  
ATOM   1025  O   ILE A 680     -42.358  -1.923  32.803  1.00 66.39           O  
ATOM   1026  CB  ILE A 680     -42.803  -2.511  36.060  1.00 73.71           C  
ATOM   1027  CG1 ILE A 680     -42.323  -2.395  37.520  1.00 83.12           C  
ATOM   1028  CG2 ILE A 680     -43.519  -3.819  35.730  1.00 63.82           C  
ATOM   1029  CD1 ILE A 680     -41.201  -3.346  37.901  1.00 88.67           C  
ATOM   1030  N   MET A 681     -42.811  -0.306  34.313  1.00 66.75           N  
ATOM   1031  CA  MET A 681     -43.511   0.584  33.403  1.00 62.10           C  
ATOM   1032  C   MET A 681     -42.712   0.961  32.162  1.00 59.13           C  
ATOM   1033  O   MET A 681     -43.204   0.859  31.036  1.00 54.35           O  
ATOM   1034  CB  MET A 681     -43.880   1.853  34.153  1.00 62.35           C  
ATOM   1035  CG  MET A 681     -45.054   1.682  35.062  1.00 62.57           C  
ATOM   1036  SD  MET A 681     -46.439   1.087  34.099  1.00 76.04           S  
ATOM   1037  CE  MET A 681     -46.287  -0.686  34.336  1.00 72.16           C  
ATOM   1038  N   GLU A 682     -41.484   1.418  32.379  1.00 56.61           N  
ATOM   1039  CA  GLU A 682     -40.692   1.920  31.288  1.00 53.15           C  
ATOM   1040  C   GLU A 682     -40.303   0.786  30.330  1.00 59.82           C  
ATOM   1041  O   GLU A 682     -40.179   0.994  29.113  1.00 58.13           O  
ATOM   1042  CB  GLU A 682     -39.504   2.773  31.768  1.00 52.47           C  
ATOM   1043  CG  GLU A 682     -39.227   2.798  33.290  1.00 67.97           C  
ATOM   1044  CD  GLU A 682     -40.263   3.548  34.143  1.00 66.58           C  
ATOM   1045  OE1 GLU A 682     -41.037   2.883  34.870  1.00 65.50           O  
ATOM   1046  OE2 GLU A 682     -40.276   4.796  34.121  1.00 66.72           O  
ATOM   1047  N   HIS A 683     -40.172  -0.428  30.851  1.00 59.09           N  
ATOM   1048  CA  HIS A 683     -39.962  -1.559  29.960  1.00 55.92           C  
ATOM   1049  C   HIS A 683     -41.155  -1.707  29.028  1.00 53.84           C  
ATOM   1050  O   HIS A 683     -41.009  -1.971  27.829  1.00 57.17           O  
ATOM   1051  CB  HIS A 683     -39.657  -2.844  30.739  1.00 56.52           C  
ATOM   1052  CG  HIS A 683     -38.201  -3.014  31.047  1.00 57.19           C  
ATOM   1053  ND1 HIS A 683     -37.293  -3.466  30.111  1.00 59.64           N  
ATOM   1054  CD2 HIS A 683     -37.485  -2.740  32.165  1.00 61.41           C  
ATOM   1055  CE1 HIS A 683     -36.082  -3.481  30.646  1.00 63.14           C  
ATOM   1056  NE2 HIS A 683     -36.171  -3.042  31.890  1.00 63.10           N  
ATOM   1057  N   HIS A 684     -42.338  -1.490  29.575  1.00 51.81           N  
ATOM   1058  CA  HIS A 684     -43.549  -1.599  28.792  1.00 53.86           C  
ATOM   1059  C   HIS A 684     -43.660  -0.470  27.759  1.00 57.55           C  
ATOM   1060  O   HIS A 684     -44.105  -0.694  26.631  1.00 57.02           O  
ATOM   1061  CB  HIS A 684     -44.763  -1.601  29.717  1.00 54.59           C  
ATOM   1062  CG  HIS A 684     -46.070  -1.715  28.997  1.00 56.57           C  
ATOM   1063  ND1 HIS A 684     -46.997  -0.695  28.970  1.00 61.43           N  
ATOM   1064  CD2 HIS A 684     -46.602  -2.724  28.269  1.00 60.18           C  
ATOM   1065  CE1 HIS A 684     -48.049  -1.074  28.265  1.00 62.47           C  
ATOM   1066  NE2 HIS A 684     -47.833  -2.302  27.828  1.00 64.34           N  
ATOM   1067  N   HIS A 685     -43.256   0.741  28.140  1.00 53.88           N  
ATOM   1068  CA  HIS A 685     -43.344   1.875  27.222  1.00 54.67           C  
ATOM   1069  C   HIS A 685     -42.443   1.628  26.038  1.00 53.20           C  
ATOM   1070  O   HIS A 685     -42.812   1.906  24.900  1.00 51.93           O  
ATOM   1071  CB  HIS A 685     -42.930   3.172  27.904  1.00 52.17           C  
ATOM   1072  CG  HIS A 685     -43.814   3.555  29.043  1.00 51.39           C  
ATOM   1073  ND1 HIS A 685     -45.179   3.380  29.007  1.00 52.60           N  
ATOM   1074  CD2 HIS A 685     -43.531   4.080  30.256  1.00 46.56           C  
ATOM   1075  CE1 HIS A 685     -45.701   3.789  30.149  1.00 50.09           C  
ATOM   1076  NE2 HIS A 685     -44.722   4.225  30.921  1.00 49.88           N  
ATOM   1077  N   PHE A 686     -41.254   1.106  26.324  1.00 54.25           N  
ATOM   1078  CA  PHE A 686     -40.329   0.705  25.274  1.00 56.07           C  
ATOM   1079  C   PHE A 686     -40.871  -0.389  24.345  1.00 55.42           C  
ATOM   1080  O   PHE A 686     -40.690  -0.327  23.135  1.00 49.72           O  
ATOM   1081  CB  PHE A 686     -38.995   0.247  25.838  1.00 48.08           C  
ATOM   1082  CG  PHE A 686     -38.084  -0.247  24.785  1.00 56.79           C  
ATOM   1083  CD1 PHE A 686     -37.520   0.639  23.878  1.00 57.30           C  
ATOM   1084  CD2 PHE A 686     -37.840  -1.602  24.635  1.00 61.44           C  
ATOM   1085  CE1 PHE A 686     -36.696   0.188  22.862  1.00 56.90           C  
ATOM   1086  CE2 PHE A 686     -37.021  -2.060  23.626  1.00 58.59           C  
ATOM   1087  CZ  PHE A 686     -36.445  -1.160  22.739  1.00 59.28           C  
ATOM   1088  N   ASP A 687     -41.508  -1.404  24.913  1.00 56.61           N  
ATOM   1089  CA  ASP A 687     -42.098  -2.433  24.076  1.00 59.85           C  
ATOM   1090  C   ASP A 687     -43.042  -1.783  23.090  1.00 57.34           C  
ATOM   1091  O   ASP A 687     -42.939  -1.964  21.868  1.00 56.82           O  
ATOM   1092  CB  ASP A 687     -42.834  -3.459  24.929  1.00 60.30           C  
ATOM   1093  CG  ASP A 687     -41.880  -4.414  25.609  1.00 75.80           C  
ATOM   1094  OD1 ASP A 687     -42.026  -4.655  26.838  1.00 77.38           O  
ATOM   1095  OD2 ASP A 687     -40.966  -4.909  24.901  1.00 78.68           O  
ATOM   1096  N   GLN A 688     -43.961  -1.018  23.652  1.00 55.64           N  
ATOM   1097  CA  GLN A 688     -44.926  -0.255  22.891  1.00 57.41           C  
ATOM   1098  C   GLN A 688     -44.230   0.534  21.780  1.00 53.96           C  
ATOM   1099  O   GLN A 688     -44.621   0.483  20.625  1.00 55.40           O  
ATOM   1100  CB  GLN A 688     -45.674   0.666  23.851  1.00 56.70           C  
ATOM   1101  CG  GLN A 688     -47.091   0.949  23.444  1.00 66.15           C  
ATOM   1102  CD  GLN A 688     -47.996  -0.269  23.501  1.00 72.29           C  
ATOM   1103  OE1 GLN A 688     -47.621  -1.329  24.018  1.00 67.51           O  
ATOM   1104  NE2 GLN A 688     -49.212  -0.116  22.971  1.00 74.83           N  
ATOM   1105  N   CYS A 689     -43.166   1.232  22.140  1.00 52.69           N  
ATOM   1106  CA  CYS A 689     -42.400   2.013  21.187  1.00 51.97           C  
ATOM   1107  C   CYS A 689     -41.893   1.180  20.006  1.00 55.49           C  
ATOM   1108  O   CYS A 689     -42.063   1.550  18.831  1.00 54.66           O  
ATOM   1109  CB  CYS A 689     -41.221   2.654  21.910  1.00 49.57           C  
ATOM   1110  SG  CYS A 689     -40.058   3.520  20.829  1.00 56.90           S  
ATOM   1111  N   LEU A 690     -41.249   0.065  20.340  1.00 53.31           N  
ATOM   1112  CA  LEU A 690     -40.673  -0.839  19.365  1.00 52.74           C  
ATOM   1113  C   LEU A 690     -41.757  -1.443  18.475  1.00 57.91           C  
ATOM   1114  O   LEU A 690     -41.612  -1.518  17.246  1.00 54.52           O  
ATOM   1115  CB  LEU A 690     -39.944  -1.956  20.086  1.00 54.57           C  
ATOM   1116  CG  LEU A 690     -39.006  -2.774  19.209  1.00 55.08           C  
ATOM   1117  CD1 LEU A 690     -38.159  -1.834  18.386  1.00 61.36           C  
ATOM   1118  CD2 LEU A 690     -38.133  -3.657  20.049  1.00 52.50           C  
ATOM   1119  N   MET A 691     -42.842  -1.885  19.101  1.00 51.46           N  
ATOM   1120  CA  MET A 691     -43.959  -2.390  18.336  1.00 52.17           C  
ATOM   1121  C   MET A 691     -44.271  -1.376  17.231  1.00 58.33           C  
ATOM   1122  O   MET A 691     -44.213  -1.703  16.045  1.00 60.52           O  
ATOM   1123  CB  MET A 691     -45.160  -2.672  19.250  1.00 56.67           C  
ATOM   1124  CG  MET A 691     -46.440  -3.125  18.555  1.00 59.30           C  
ATOM   1125  SD  MET A 691     -47.524  -1.765  18.028  1.00 89.00           S  
ATOM   1126  CE  MET A 691     -48.321  -1.326  19.587  1.00 72.89           C  
ATOM   1127  N   ILE A 692     -44.548  -0.136  17.618  1.00 57.90           N  
ATOM   1128  CA  ILE A 692     -44.864   0.909  16.650  1.00 59.69           C  
ATOM   1129  C   ILE A 692     -43.779   1.111  15.600  1.00 58.13           C  
ATOM   1130  O   ILE A 692     -44.072   1.211  14.402  1.00 59.93           O  
ATOM   1131  CB  ILE A 692     -45.155   2.255  17.330  1.00 58.80           C  
ATOM   1132  CG1 ILE A 692     -46.499   2.202  18.043  1.00 58.99           C  
ATOM   1133  CG2 ILE A 692     -45.168   3.388  16.310  1.00 54.44           C  
ATOM   1134  CD1 ILE A 692     -46.692   3.336  19.014  1.00 57.77           C  
ATOM   1135  N   LEU A 693     -42.531   1.183  16.041  1.00 54.05           N  
ATOM   1136  CA  LEU A 693     -41.438   1.376  15.098  1.00 55.97           C  
ATOM   1137  C   LEU A 693     -41.418   0.285  14.043  1.00 58.73           C  
ATOM   1138  O   LEU A 693     -41.035   0.531  12.904  1.00 61.36           O  
ATOM   1139  CB  LEU A 693     -40.109   1.384  15.828  1.00 56.88           C  
ATOM   1140  CG  LEU A 693     -39.849   2.726  16.478  1.00 57.93           C  
ATOM   1141  CD1 LEU A 693     -38.630   2.660  17.385  1.00 51.99           C  
ATOM   1142  CD2 LEU A 693     -39.680   3.739  15.370  1.00 54.53           C  
ATOM   1143  N   ASN A 694     -41.828  -0.918  14.447  1.00 60.74           N  
ATOM   1144  CA  ASN A 694     -41.816  -2.105  13.599  1.00 60.83           C  
ATOM   1145  C   ASN A 694     -43.111  -2.383  12.866  1.00 63.62           C  
ATOM   1146  O   ASN A 694     -43.207  -3.395  12.178  1.00 66.48           O  
ATOM   1147  CB  ASN A 694     -41.496  -3.334  14.432  1.00 55.46           C  
ATOM   1148  CG  ASN A 694     -40.033  -3.496  14.661  1.00 62.12           C  
ATOM   1149  OD1 ASN A 694     -39.220  -3.031  13.867  1.00 65.97           O  
ATOM   1150  ND2 ASN A 694     -39.675  -4.141  15.761  1.00 61.54           N  
ATOM   1151  N   SER A 695     -44.114  -1.525  13.037  1.00 56.33           N  
ATOM   1152  CA  SER A 695     -45.363  -1.688  12.308  1.00 58.96           C  
ATOM   1153  C   SER A 695     -45.221  -1.310  10.832  1.00 65.49           C  
ATOM   1154  O   SER A 695     -44.488  -0.381  10.474  1.00 63.28           O  
ATOM   1155  CB  SER A 695     -46.470  -0.877  12.957  1.00 60.24           C  
ATOM   1156  OG  SER A 695     -46.642  -1.312  14.291  1.00 64.86           O  
ATOM   1157  N   PRO A 696     -45.906  -2.062   9.962  1.00 69.26           N  
ATOM   1158  CA  PRO A 696     -45.962  -1.742   8.532  1.00 67.45           C  
ATOM   1159  C   PRO A 696     -46.438  -0.308   8.297  1.00 64.30           C  
ATOM   1160  O   PRO A 696     -47.499   0.092   8.786  1.00 65.14           O  
ATOM   1161  CB  PRO A 696     -46.994  -2.739   8.000  1.00 61.20           C  
ATOM   1162  CG  PRO A 696     -46.881  -3.910   8.923  1.00 62.18           C  
ATOM   1163  CD  PRO A 696     -46.551  -3.351  10.274  1.00 63.13           C  
ATOM   1164  N   GLY A 697     -45.645   0.465   7.568  1.00 60.14           N  
ATOM   1165  CA  GLY A 697     -46.047   1.808   7.207  1.00 62.19           C  
ATOM   1166  C   GLY A 697     -45.516   2.840   8.161  1.00 66.75           C  
ATOM   1167  O   GLY A 697     -45.507   4.035   7.854  1.00 69.32           O  
ATOM   1168  N   ASN A 698     -45.054   2.366   9.315  1.00 67.03           N  
ATOM   1169  CA  ASN A 698     -44.623   3.239  10.397  1.00 62.14           C  
ATOM   1170  C   ASN A 698     -43.139   3.211  10.644  1.00 61.55           C  
ATOM   1171  O   ASN A 698     -42.675   3.807  11.595  1.00 59.75           O  
ATOM   1172  CB  ASN A 698     -45.319   2.843  11.690  1.00 58.44           C  
ATOM   1173  CG  ASN A 698     -46.788   3.099  11.639  1.00 62.84           C  
ATOM   1174  OD1 ASN A 698     -47.538   2.341  11.031  1.00 71.07           O  
ATOM   1175  ND2 ASN A 698     -47.219   4.184  12.260  1.00 59.33           N  
ATOM   1176  N   GLN A 699     -42.390   2.521   9.796  1.00 59.65           N  
ATOM   1177  CA  GLN A 699     -40.990   2.262  10.102  1.00 60.82           C  
ATOM   1178  C   GLN A 699     -40.009   3.379   9.776  1.00 57.73           C  
ATOM   1179  O   GLN A 699     -39.174   3.233   8.894  1.00 56.88           O  
ATOM   1180  CB  GLN A 699     -40.557   0.972   9.433  1.00 60.53           C  
ATOM   1181  CG  GLN A 699     -41.429  -0.167   9.854  1.00 63.90           C  
ATOM   1182  CD  GLN A 699     -41.042  -1.457   9.190  1.00 70.77           C  
ATOM   1183  OE1 GLN A 699     -39.918  -1.605   8.676  1.00 62.72           O  
ATOM   1184  NE2 GLN A 699     -41.975  -2.413   9.187  1.00 72.19           N  
ATOM   1185  N   ILE A 700     -40.075   4.466  10.531  1.00 55.97           N  
ATOM   1186  CA  ILE A 700     -39.208   5.609  10.289  1.00 55.58           C  
ATOM   1187  C   ILE A 700     -37.721   5.310  10.444  1.00 57.40           C  
ATOM   1188  O   ILE A 700     -36.896   6.209  10.298  1.00 53.44           O  
ATOM   1189  CB  ILE A 700     -39.548   6.782  11.212  1.00 54.22           C  
ATOM   1190  CG1 ILE A 700     -39.569   6.299  12.671  1.00 58.98           C  
ATOM   1191  CG2 ILE A 700     -40.882   7.387  10.818  1.00 55.81           C  
ATOM   1192  CD1 ILE A 700     -39.433   7.424  13.704  1.00 56.33           C  
ATOM   1193  N   LEU A 701     -37.355   4.068  10.744  1.00 58.27           N  
ATOM   1194  CA  LEU A 701     -35.922   3.770  10.845  1.00 58.57           C  
ATOM   1195  C   LEU A 701     -35.408   2.917   9.688  1.00 60.49           C  
ATOM   1196  O   LEU A 701     -34.208   2.644   9.590  1.00 62.17           O  
ATOM   1197  CB  LEU A 701     -35.577   3.137  12.198  1.00 61.51           C  
ATOM   1198  CG  LEU A 701     -35.895   3.960  13.457  1.00 57.40           C  
ATOM   1199  CD1 LEU A 701     -35.451   3.213  14.708  1.00 52.35           C  
ATOM   1200  CD2 LEU A 701     -35.228   5.319  13.393  1.00 53.32           C  
ATOM   1201  N   SER A 702     -36.323   2.512   8.810  1.00 54.99           N  
ATOM   1202  CA  SER A 702     -35.977   1.719   7.645  1.00 52.49           C  
ATOM   1203  C   SER A 702     -34.704   2.208   6.962  1.00 56.53           C  
ATOM   1204  O   SER A 702     -33.937   1.413   6.437  1.00 59.50           O  
ATOM   1205  CB  SER A 702     -37.120   1.736   6.643  1.00 53.98           C  
ATOM   1206  OG  SER A 702     -37.195   3.001   6.022  1.00 60.90           O  
ATOM   1207  N   GLY A 703     -34.469   3.510   6.977  1.00 54.97           N  
ATOM   1208  CA  GLY A 703     -33.332   4.067   6.273  1.00 54.24           C  
ATOM   1209  C   GLY A 703     -31.961   3.913   6.900  1.00 59.09           C  
ATOM   1210  O   GLY A 703     -30.972   4.368   6.326  1.00 60.25           O  
ATOM   1211  N   LEU A 704     -31.883   3.288   8.072  1.00 58.73           N  
ATOM   1212  CA  LEU A 704     -30.599   3.097   8.736  1.00 52.52           C  
ATOM   1213  C   LEU A 704     -30.046   1.707   8.433  1.00 58.77           C  
ATOM   1214  O   LEU A 704     -30.804   0.733   8.311  1.00 57.53           O  
ATOM   1215  CB  LEU A 704     -30.759   3.233  10.247  1.00 59.53           C  
ATOM   1216  CG  LEU A 704     -31.177   4.525  10.949  1.00 57.64           C  
ATOM   1217  CD1 LEU A 704     -32.516   5.038  10.456  1.00 59.76           C  
ATOM   1218  CD2 LEU A 704     -31.215   4.275  12.445  1.00 52.56           C  
ATOM   1219  N   SER A 705     -28.724   1.608   8.331  1.00 56.69           N  
ATOM   1220  CA  SER A 705     -28.054   0.311   8.264  1.00 56.90           C  
ATOM   1221  C   SER A 705     -28.357  -0.471   9.545  1.00 62.17           C  
ATOM   1222  O   SER A 705     -28.823   0.114  10.522  1.00 64.99           O  
ATOM   1223  CB  SER A 705     -26.557   0.530   8.160  1.00 55.94           C  
ATOM   1224  OG  SER A 705     -26.052   1.111   9.349  1.00 61.73           O  
ATOM   1225  N   ILE A 706     -28.091  -1.774   9.575  1.00 62.27           N  
ATOM   1226  CA  ILE A 706     -28.296  -2.518  10.831  1.00 63.68           C  
ATOM   1227  C   ILE A 706     -27.431  -1.962  11.962  1.00 59.42           C  
ATOM   1228  O   ILE A 706     -27.870  -1.899  13.107  1.00 60.10           O  
ATOM   1229  CB  ILE A 706     -27.977  -4.043  10.727  1.00 63.23           C  
ATOM   1230  CG1 ILE A 706     -27.920  -4.506   9.282  1.00 60.59           C  
ATOM   1231  CG2 ILE A 706     -28.984  -4.867  11.542  1.00 59.45           C  
ATOM   1232  N   GLU A 707     -26.197  -1.585  11.642  1.00 53.99           N  
ATOM   1233  CA  GLU A 707     -25.277  -1.125  12.662  1.00 58.24           C  
ATOM   1234  C   GLU A 707     -25.874   0.103  13.337  1.00 60.55           C  
ATOM   1235  O   GLU A 707     -26.076   0.131  14.548  1.00 58.22           O  
ATOM   1236  CB  GLU A 707     -23.909  -0.810  12.058  1.00 53.71           C  
ATOM   1237  N   GLU A 708     -26.175   1.111  12.529  1.00 62.00           N  
ATOM   1238  CA  GLU A 708     -26.856   2.303  13.008  1.00 61.90           C  
ATOM   1239  C   GLU A 708     -28.130   1.956  13.771  1.00 56.91           C  
ATOM   1240  O   GLU A 708     -28.367   2.451  14.871  1.00 60.09           O  
ATOM   1241  CB  GLU A 708     -27.203   3.203  11.830  1.00 58.92           C  
ATOM   1242  CG  GLU A 708     -26.005   3.840  11.165  1.00 58.85           C  
ATOM   1243  CD  GLU A 708     -26.403   4.671   9.936  1.00 69.32           C  
ATOM   1244  OE1 GLU A 708     -27.424   4.341   9.275  1.00 64.88           O  
ATOM   1245  OE2 GLU A 708     -25.694   5.662   9.638  1.00 71.29           O  
ATOM   1246  N   TYR A 709     -28.937   1.099  13.171  1.00 53.48           N  
ATOM   1247  CA  TYR A 709     -30.213   0.721  13.727  1.00 56.33           C  
ATOM   1248  C   TYR A 709     -30.089   0.126  15.132  1.00 62.63           C  
ATOM   1249  O   TYR A 709     -30.852   0.463  16.049  1.00 61.01           O  
ATOM   1250  CB  TYR A 709     -30.894  -0.260  12.796  1.00 54.80           C  
ATOM   1251  CG  TYR A 709     -32.252  -0.637  13.279  1.00 57.69           C  
ATOM   1252  CD1 TYR A 709     -33.285   0.287  13.273  1.00 59.08           C  
ATOM   1253  CD2 TYR A 709     -32.506  -1.910  13.757  1.00 60.98           C  
ATOM   1254  CE1 TYR A 709     -34.549  -0.049  13.722  1.00 58.41           C  
ATOM   1255  CE2 TYR A 709     -33.757  -2.259  14.213  1.00 63.69           C  
ATOM   1256  CZ  TYR A 709     -34.779  -1.323  14.197  1.00 65.55           C  
ATOM   1257  OH  TYR A 709     -36.033  -1.669  14.657  1.00 70.34           O  
ATOM   1258  N   LYS A 710     -29.117  -0.760  15.299  1.00 61.84           N  
ATOM   1259  CA  LYS A 710     -28.903  -1.408  16.576  1.00 61.29           C  
ATOM   1260  C   LYS A 710     -28.497  -0.372  17.611  1.00 60.57           C  
ATOM   1261  O   LYS A 710     -28.989  -0.368  18.752  1.00 57.88           O  
ATOM   1262  CB  LYS A 710     -27.796  -2.446  16.450  1.00 62.03           C  
ATOM   1263  CG  LYS A 710     -28.226  -3.841  16.049  1.00 59.04           C  
ATOM   1264  CD  LYS A 710     -26.950  -4.625  15.794  1.00 64.41           C  
ATOM   1265  CE  LYS A 710     -27.186  -6.076  15.468  1.00 72.40           C  
ATOM   1266  NZ  LYS A 710     -25.863  -6.770  15.319  1.00 73.70           N  
ATOM   1267  N   THR A 711     -27.577   0.491  17.201  1.00 52.94           N  
ATOM   1268  CA  THR A 711     -27.073   1.535  18.061  1.00 56.25           C  
ATOM   1269  C   THR A 711     -28.232   2.403  18.538  1.00 60.69           C  
ATOM   1270  O   THR A 711     -28.431   2.586  19.743  1.00 58.50           O  
ATOM   1271  CB  THR A 711     -26.069   2.399  17.311  1.00 61.40           C  
ATOM   1272  OG1 THR A 711     -24.967   1.585  16.893  1.00 65.72           O  
ATOM   1273  CG2 THR A 711     -25.560   3.508  18.204  1.00 57.69           C  
ATOM   1274  N   THR A 712     -29.015   2.894  17.578  1.00 59.19           N  
ATOM   1275  CA  THR A 712     -30.176   3.739  17.852  1.00 58.57           C  
ATOM   1276  C   THR A 712     -31.171   3.116  18.833  1.00 57.42           C  
ATOM   1277  O   THR A 712     -31.628   3.770  19.771  1.00 55.06           O  
ATOM   1278  CB  THR A 712     -30.889   4.122  16.540  1.00 54.57           C  
ATOM   1279  OG1 THR A 712     -29.966   4.819  15.699  1.00 58.52           O  
ATOM   1280  CG2 THR A 712     -32.078   5.024  16.803  1.00 50.76           C  
ATOM   1281  N   LEU A 713     -31.497   1.853  18.614  1.00 57.07           N  
ATOM   1282  CA  LEU A 713     -32.403   1.144  19.501  1.00 58.53           C  
ATOM   1283  C   LEU A 713     -31.883   1.065  20.926  1.00 57.33           C  
ATOM   1284  O   LEU A 713     -32.645   1.151  21.881  1.00 54.66           O  
ATOM   1285  CB  LEU A 713     -32.622  -0.270  18.994  1.00 61.34           C  
ATOM   1286  CG  LEU A 713     -33.823  -0.479  18.095  1.00 66.27           C  
ATOM   1287  CD1 LEU A 713     -34.117  -1.970  18.056  1.00 64.88           C  
ATOM   1288  CD2 LEU A 713     -35.012   0.295  18.644  1.00 62.73           C  
ATOM   1289  N   LYS A 714     -30.583   0.859  21.067  1.00 58.06           N  
ATOM   1290  CA  LYS A 714     -30.003   0.714  22.385  1.00 58.23           C  
ATOM   1291  C   LYS A 714     -30.196   2.047  23.094  1.00 59.47           C  
ATOM   1292  O   LYS A 714     -30.704   2.102  24.216  1.00 57.21           O  
ATOM   1293  CB  LYS A 714     -28.513   0.362  22.287  1.00 59.51           C  
ATOM   1294  N   ILE A 715     -29.816   3.123  22.413  1.00 54.16           N  
ATOM   1295  CA  ILE A 715     -30.027   4.455  22.951  1.00 57.12           C  
ATOM   1296  C   ILE A 715     -31.498   4.750  23.286  1.00 54.32           C  
ATOM   1297  O   ILE A 715     -31.813   5.222  24.371  1.00 55.98           O  
ATOM   1298  CB  ILE A 715     -29.492   5.534  22.014  1.00 57.25           C  
ATOM   1299  CG1 ILE A 715     -28.006   5.304  21.731  1.00 50.78           C  
ATOM   1300  CG2 ILE A 715     -29.717   6.919  22.628  1.00 54.45           C  
ATOM   1301  CD1 ILE A 715     -27.498   6.105  20.542  1.00 54.17           C  
ATOM   1302  N   ILE A 716     -32.398   4.466  22.365  1.00 53.33           N  
ATOM   1303  CA  ILE A 716     -33.802   4.701  22.630  1.00 53.04           C  
ATOM   1304  C   ILE A 716     -34.192   3.998  23.911  1.00 53.34           C  
ATOM   1305  O   ILE A 716     -34.842   4.577  24.782  1.00 51.93           O  
ATOM   1306  CB  ILE A 716     -34.687   4.192  21.479  1.00 53.86           C  
ATOM   1307  CG1 ILE A 716     -34.512   5.070  20.238  1.00 52.45           C  
ATOM   1308  CG2 ILE A 716     -36.148   4.176  21.880  1.00 50.52           C  
ATOM   1309  CD1 ILE A 716     -35.176   4.498  19.010  1.00 50.78           C  
ATOM   1310  N   LYS A 717     -33.766   2.749  24.039  1.00 55.58           N  
ATOM   1311  CA  LYS A 717     -34.215   1.915  25.156  1.00 56.85           C  
ATOM   1312  C   LYS A 717     -33.722   2.498  26.475  1.00 55.52           C  
ATOM   1313  O   LYS A 717     -34.458   2.571  27.444  1.00 54.45           O  
ATOM   1314  CB  LYS A 717     -33.724   0.471  24.986  1.00 55.40           C  
ATOM   1315  CG  LYS A 717     -34.217  -0.481  26.057  1.00 58.82           C  
ATOM   1316  CD  LYS A 717     -33.612  -1.874  25.920  1.00 61.14           C  
ATOM   1317  CE  LYS A 717     -34.209  -2.842  26.942  1.00 61.14           C  
ATOM   1318  NZ  LYS A 717     -34.217  -4.271  26.499  1.00 61.53           N  
ATOM   1319  N   GLN A 718     -32.466   2.920  26.487  1.00 54.09           N  
ATOM   1320  CA  GLN A 718     -31.858   3.462  27.675  1.00 54.11           C  
ATOM   1321  C   GLN A 718     -32.509   4.781  28.026  1.00 55.25           C  
ATOM   1322  O   GLN A 718     -32.777   5.052  29.195  1.00 52.77           O  
ATOM   1323  CB  GLN A 718     -30.360   3.663  27.456  1.00 58.83           C  
ATOM   1324  CG  GLN A 718     -29.536   2.382  27.495  1.00 66.47           C  
ATOM   1325  CD  GLN A 718     -28.080   2.612  27.077  1.00 81.59           C  
ATOM   1326  OE1 GLN A 718     -27.785   3.453  26.205  1.00 77.30           O  
ATOM   1327  NE2 GLN A 718     -27.162   1.867  27.701  1.00 75.67           N  
ATOM   1328  N   ALA A 719     -32.760   5.599  27.007  1.00 56.06           N  
ATOM   1329  CA  ALA A 719     -33.467   6.866  27.198  1.00 52.90           C  
ATOM   1330  C   ALA A 719     -34.787   6.628  27.907  1.00 47.86           C  
ATOM   1331  O   ALA A 719     -35.059   7.214  28.947  1.00 47.08           O  
ATOM   1332  CB  ALA A 719     -33.720   7.531  25.880  1.00 49.22           C  
ATOM   1333  N   ILE A 720     -35.603   5.753  27.344  1.00 44.79           N  
ATOM   1334  CA  ILE A 720     -36.915   5.540  27.911  1.00 47.94           C  
ATOM   1335  C   ILE A 720     -36.801   5.024  29.346  1.00 51.30           C  
ATOM   1336  O   ILE A 720     -37.641   5.321  30.192  1.00 48.54           O  
ATOM   1337  CB  ILE A 720     -37.786   4.600  27.049  1.00 43.41           C  
ATOM   1338  CG1 ILE A 720     -38.047   5.243  25.693  1.00 42.25           C  
ATOM   1339  CG2 ILE A 720     -39.093   4.251  27.785  1.00 43.49           C  
ATOM   1340  CD1 ILE A 720     -39.148   4.571  24.855  1.00 47.48           C  
ATOM   1341  N   LEU A 721     -35.749   4.266  29.627  1.00 50.71           N  
ATOM   1342  CA  LEU A 721     -35.631   3.672  30.947  1.00 54.72           C  
ATOM   1343  C   LEU A 721     -35.124   4.703  31.931  1.00 52.87           C  
ATOM   1344  O   LEU A 721     -35.346   4.589  33.126  1.00 57.38           O  
ATOM   1345  CB  LEU A 721     -34.728   2.431  30.936  1.00 56.42           C  
ATOM   1346  CG  LEU A 721     -35.242   1.143  30.266  1.00 57.58           C  
ATOM   1347  CD1 LEU A 721     -34.184   0.071  30.384  1.00 61.47           C  
ATOM   1348  CD2 LEU A 721     -36.550   0.642  30.827  1.00 55.24           C  
ATOM   1349  N   ALA A 722     -34.447   5.717  31.417  1.00 50.93           N  
ATOM   1350  CA  ALA A 722     -33.950   6.775  32.260  1.00 47.89           C  
ATOM   1351  C   ALA A 722     -35.110   7.553  32.871  1.00 52.90           C  
ATOM   1352  O   ALA A 722     -34.929   8.193  33.906  1.00 57.05           O  
ATOM   1353  CB  ALA A 722     -33.020   7.689  31.479  1.00 45.00           C  
ATOM   1354  N   THR A 723     -36.297   7.475  32.254  1.00 50.53           N  
ATOM   1355  CA  THR A 723     -37.481   8.199  32.741  1.00 49.41           C  
ATOM   1356  C   THR A 723     -38.125   7.576  33.989  1.00 53.68           C  
ATOM   1357  O   THR A 723     -39.178   8.035  34.475  1.00 53.59           O  
ATOM   1358  CB  THR A 723     -38.574   8.414  31.634  1.00 49.75           C  
ATOM   1359  OG1 THR A 723     -39.263   7.179  31.345  1.00 50.40           O  
ATOM   1360  CG2 THR A 723     -37.973   9.030  30.373  1.00 45.43           C  
ATOM   1361  N   ASP A 724     -37.512   6.511  34.487  1.00 53.69           N  
ATOM   1362  CA  ASP A 724     -37.865   5.992  35.794  1.00 57.93           C  
ATOM   1363  C   ASP A 724     -37.184   6.913  36.796  1.00 58.66           C  
ATOM   1364  O   ASP A 724     -35.958   7.069  36.779  1.00 57.06           O  
ATOM   1365  CB  ASP A 724     -37.393   4.542  35.956  1.00 61.49           C  
ATOM   1366  CG  ASP A 724     -37.753   3.952  37.314  1.00 67.75           C  
ATOM   1367  OD1 ASP A 724     -38.465   4.627  38.099  1.00 67.49           O  
ATOM   1368  OD2 ASP A 724     -37.340   2.799  37.593  1.00 69.27           O  
ATOM   1369  N   LEU A 725     -37.969   7.565  37.646  1.00 56.68           N  
ATOM   1370  CA  LEU A 725     -37.348   8.466  38.604  1.00 59.96           C  
ATOM   1371  C   LEU A 725     -36.389   7.728  39.535  1.00 58.60           C  
ATOM   1372  O   LEU A 725     -35.340   8.254  39.895  1.00 59.40           O  
ATOM   1373  CB  LEU A 725     -38.391   9.270  39.366  1.00 63.85           C  
ATOM   1374  CG  LEU A 725     -38.998  10.392  38.512  1.00 60.33           C  
ATOM   1375  CD1 LEU A 725     -40.238  10.969  39.185  1.00 61.43           C  
ATOM   1376  CD2 LEU A 725     -37.971  11.489  38.202  1.00 49.29           C  
ATOM   1377  N   ALA A 726     -36.728   6.491  39.875  1.00 58.11           N  
ATOM   1378  CA  ALA A 726     -35.811   5.623  40.626  1.00 62.45           C  
ATOM   1379  C   ALA A 726     -34.425   5.491  39.978  1.00 59.58           C  
ATOM   1380  O   ALA A 726     -33.404   5.613  40.659  1.00 62.11           O  
ATOM   1381  CB  ALA A 726     -36.437   4.235  40.863  1.00 61.90           C  
ATOM   1382  N   LEU A 727     -34.383   5.239  38.671  1.00 58.98           N  
ATOM   1383  CA  LEU A 727     -33.102   5.214  37.957  1.00 60.02           C  
ATOM   1384  C   LEU A 727     -32.392   6.560  38.052  1.00 60.17           C  
ATOM   1385  O   LEU A 727     -31.167   6.633  38.176  1.00 61.28           O  
ATOM   1386  CB  LEU A 727     -33.292   4.840  36.481  1.00 64.10           C  
ATOM   1387  CG  LEU A 727     -33.170   3.373  36.063  1.00 63.54           C  
ATOM   1388  N   TYR A 728     -33.164   7.635  37.990  1.00 60.36           N  
ATOM   1389  CA  TYR A 728     -32.565   8.960  38.004  1.00 60.41           C  
ATOM   1390  C   TYR A 728     -31.888   9.258  39.352  1.00 61.10           C  
ATOM   1391  O   TYR A 728     -30.805   9.837  39.410  1.00 56.91           O  
ATOM   1392  CB  TYR A 728     -33.609  10.021  37.640  1.00 59.01           C  
ATOM   1393  CG  TYR A 728     -33.227  11.398  38.100  1.00 58.56           C  
ATOM   1394  CD1 TYR A 728     -32.203  12.109  37.471  1.00 59.03           C  
ATOM   1395  CD2 TYR A 728     -33.872  11.984  39.175  1.00 54.22           C  
ATOM   1396  CE1 TYR A 728     -31.830  13.378  37.915  1.00 60.60           C  
ATOM   1397  CE2 TYR A 728     -33.511  13.237  39.630  1.00 60.52           C  
ATOM   1398  CZ  TYR A 728     -32.492  13.938  39.004  1.00 65.40           C  
ATOM   1399  OH  TYR A 728     -32.157  15.200  39.472  1.00 64.41           O  
ATOM   1400  N   ILE A 729     -32.526   8.839  40.435  1.00 61.44           N  
ATOM   1401  CA  ILE A 729     -31.990   9.075  41.772  1.00 65.01           C  
ATOM   1402  C   ILE A 729     -30.739   8.231  42.074  1.00 66.96           C  
ATOM   1403  O   ILE A 729     -29.799   8.692  42.747  1.00 63.38           O  
ATOM   1404  CB  ILE A 729     -33.070   8.828  42.822  1.00 63.61           C  
ATOM   1405  CG1 ILE A 729     -34.084   9.972  42.770  1.00 62.37           C  
ATOM   1406  CG2 ILE A 729     -32.457   8.712  44.207  1.00 66.82           C  
ATOM   1407  CD1 ILE A 729     -35.476   9.561  43.146  1.00 57.36           C  
ATOM   1408  N   LYS A 730     -30.739   6.999  41.572  1.00 62.23           N  
ATOM   1409  CA  LYS A 730     -29.571   6.141  41.664  1.00 64.24           C  
ATOM   1410  C   LYS A 730     -28.391   6.779  40.948  1.00 67.35           C  
ATOM   1411  O   LYS A 730     -27.262   6.751  41.443  1.00 71.89           O  
ATOM   1412  CB  LYS A 730     -29.850   4.772  41.032  1.00 70.56           C  
ATOM   1413  CG  LYS A 730     -30.608   3.778  41.914  1.00 71.02           C  
ATOM   1414  N   ARG A 731     -28.642   7.363  39.784  1.00 63.92           N  
ATOM   1415  CA  ARG A 731     -27.535   7.701  38.891  1.00 64.21           C  
ATOM   1416  C   ARG A 731     -27.057   9.149  38.943  1.00 64.77           C  
ATOM   1417  O   ARG A 731     -25.991   9.478  38.423  1.00 65.80           O  
ATOM   1418  CB  ARG A 731     -27.859   7.259  37.456  1.00 63.17           C  
ATOM   1419  CG  ARG A 731     -28.112   5.754  37.369  1.00 68.76           C  
ATOM   1420  CD  ARG A 731     -27.903   5.164  35.980  1.00 75.28           C  
ATOM   1421  NE  ARG A 731     -26.526   5.265  35.495  1.00 74.12           N  
ATOM   1422  CZ  ARG A 731     -26.197   5.695  34.274  1.00 82.10           C  
ATOM   1423  NH1 ARG A 731     -27.146   6.076  33.415  1.00 75.08           N  
ATOM   1424  NH2 ARG A 731     -24.919   5.756  33.908  1.00 82.36           N  
ATOM   1425  N   ARG A 732     -27.831  10.013  39.585  1.00 65.91           N  
ATOM   1426  CA  ARG A 732     -27.555  11.441  39.515  1.00 62.94           C  
ATOM   1427  C   ARG A 732     -26.360  11.839  40.380  1.00 68.42           C  
ATOM   1428  O   ARG A 732     -25.606  12.754  40.030  1.00 69.03           O  
ATOM   1429  CB  ARG A 732     -28.795  12.242  39.900  1.00 65.72           C  
ATOM   1430  CG  ARG A 732     -29.268  11.976  41.316  1.00 69.85           C  
ATOM   1431  CD  ARG A 732     -30.249  13.021  41.741  1.00 68.42           C  
ATOM   1432  NE  ARG A 732     -30.643  12.854  43.134  1.00 76.09           N  
ATOM   1433  CZ  ARG A 732     -31.570  13.599  43.736  1.00 78.25           C  
ATOM   1434  NH1 ARG A 732     -32.195  14.557  43.052  1.00 68.85           N  
ATOM   1435  NH2 ARG A 732     -31.867  13.386  45.018  1.00 73.19           N  
ATOM   1436  N   GLY A 733     -26.190  11.152  41.508  1.00 68.08           N  
ATOM   1437  CA  GLY A 733     -25.043  11.384  42.367  1.00 70.83           C  
ATOM   1438  C   GLY A 733     -23.758  11.462  41.563  1.00 75.16           C  
ATOM   1439  O   GLY A 733     -23.036  12.469  41.609  1.00 72.50           O  
ATOM   1440  N   GLU A 734     -23.491  10.398  40.805  1.00 74.73           N  
ATOM   1441  CA  GLU A 734     -22.326  10.343  39.939  1.00 72.77           C  
ATOM   1442  C   GLU A 734     -22.246  11.553  39.019  1.00 71.50           C  
ATOM   1443  O   GLU A 734     -21.179  12.139  38.831  1.00 75.06           O  
ATOM   1444  CB  GLU A 734     -22.341   9.070  39.106  1.00 75.63           C  
ATOM   1445  CG  GLU A 734     -21.146   8.969  38.168  1.00 81.53           C  
ATOM   1446  CD  GLU A 734     -21.137   7.694  37.350  1.00 86.81           C  
ATOM   1447  OE1 GLU A 734     -22.017   6.827  37.577  1.00 85.68           O  
ATOM   1448  OE2 GLU A 734     -20.244   7.565  36.481  1.00 87.81           O  
ATOM   1449  N   PHE A 735     -23.380  11.923  38.445  1.00 70.60           N  
ATOM   1450  CA  PHE A 735     -23.448  13.066  37.536  1.00 73.61           C  
ATOM   1451  C   PHE A 735     -23.040  14.349  38.242  1.00 70.76           C  
ATOM   1452  O   PHE A 735     -22.304  15.162  37.700  1.00 69.14           O  
ATOM   1453  CB  PHE A 735     -24.871  13.196  36.975  1.00 70.75           C  
ATOM   1454  CG  PHE A 735     -25.012  14.233  35.903  1.00 65.42           C  
ATOM   1455  CD1 PHE A 735     -24.180  14.222  34.801  1.00 63.60           C  
ATOM   1456  CD2 PHE A 735     -25.997  15.210  35.990  1.00 65.16           C  
ATOM   1457  CE1 PHE A 735     -24.313  15.186  33.805  1.00 67.65           C  
ATOM   1458  CE2 PHE A 735     -26.138  16.174  35.004  1.00 65.72           C  
ATOM   1459  CZ  PHE A 735     -25.294  16.165  33.905  1.00 65.75           C  
ATOM   1460  N   PHE A 736     -23.519  14.512  39.468  1.00 72.59           N  
ATOM   1461  CA  PHE A 736     -23.235  15.707  40.254  1.00 74.99           C  
ATOM   1462  C   PHE A 736     -21.780  15.779  40.703  1.00 76.09           C  
ATOM   1463  O   PHE A 736     -21.149  16.831  40.591  1.00 76.17           O  
ATOM   1464  CB  PHE A 736     -24.182  15.794  41.456  1.00 72.27           C  
ATOM   1465  CG  PHE A 736     -25.631  15.913  41.072  1.00 70.33           C  
ATOM   1466  CD1 PHE A 736     -26.630  15.483  41.930  1.00 65.80           C  
ATOM   1467  CD2 PHE A 736     -25.991  16.446  39.836  1.00 69.49           C  
ATOM   1468  CE1 PHE A 736     -27.965  15.585  41.572  1.00 65.88           C  
ATOM   1469  CE2 PHE A 736     -27.318  16.546  39.470  1.00 67.54           C  
ATOM   1470  CZ  PHE A 736     -28.310  16.115  40.348  1.00 68.34           C  
ATOM   1471  N   GLU A 737     -21.251  14.668  41.214  1.00 76.39           N  
ATOM   1472  CA  GLU A 737     -19.815  14.578  41.500  1.00 80.00           C  
ATOM   1473  C   GLU A 737     -18.998  15.119  40.323  1.00 77.54           C  
ATOM   1474  O   GLU A 737     -18.304  16.120  40.447  1.00 79.07           O  
ATOM   1475  CB  GLU A 737     -19.401  13.131  41.799  1.00 77.45           C  
ATOM   1476  CG  GLU A 737     -20.460  12.333  42.556  1.00 84.61           C  
ATOM   1477  CD  GLU A 737     -19.986  10.949  43.015  1.00 89.61           C  
ATOM   1478  OE1 GLU A 737     -18.819  10.587  42.729  1.00 87.42           O  
ATOM   1479  OE2 GLU A 737     -20.787  10.233  43.672  1.00 84.14           O  
ATOM   1480  N   LEU A 738     -19.105  14.458  39.176  1.00 76.04           N  
ATOM   1481  CA  LEU A 738     -18.357  14.850  37.988  1.00 79.91           C  
ATOM   1482  C   LEU A 738     -18.367  16.359  37.761  1.00 84.30           C  
ATOM   1483  O   LEU A 738     -17.351  16.954  37.399  1.00 86.00           O  
ATOM   1484  CB  LEU A 738     -18.908  14.141  36.750  1.00 83.00           C  
ATOM   1485  CG  LEU A 738     -18.901  12.611  36.771  1.00 84.71           C  
ATOM   1486  CD1 LEU A 738     -19.779  12.072  35.658  1.00 85.53           C  
ATOM   1487  CD2 LEU A 738     -17.487  12.049  36.664  1.00 81.77           C  
ATOM   1488  N   ILE A 739     -19.523  16.975  37.967  1.00 82.96           N  
ATOM   1489  CA  ILE A 739     -19.662  18.409  37.762  1.00 82.07           C  
ATOM   1490  C   ILE A 739     -18.860  19.236  38.771  1.00 84.53           C  
ATOM   1491  O   ILE A 739     -18.064  20.101  38.389  1.00 82.41           O  
ATOM   1492  CB  ILE A 739     -21.129  18.821  37.836  1.00 79.19           C  
ATOM   1493  CG1 ILE A 739     -21.970  17.915  36.930  1.00 79.62           C  
ATOM   1494  CG2 ILE A 739     -21.290  20.298  37.472  1.00 81.42           C  
ATOM   1495  CD1 ILE A 739     -21.803  18.184  35.450  1.00 77.50           C  
ATOM   1496  N   ARG A 740     -19.070  18.973  40.059  1.00 84.04           N  
ATOM   1497  CA  ARG A 740     -18.445  19.792  41.089  1.00 83.35           C  
ATOM   1498  C   ARG A 740     -16.939  19.611  41.087  1.00 88.58           C  
ATOM   1499  O   ARG A 740     -16.198  20.513  41.491  1.00 91.40           O  
ATOM   1500  CB  ARG A 740     -19.026  19.497  42.470  1.00 82.99           C  
ATOM   1501  CG  ARG A 740     -18.890  18.062  42.922  1.00 84.72           C  
ATOM   1502  CD  ARG A 740     -19.468  17.890  44.317  1.00 81.89           C  
ATOM   1503  NE  ARG A 740     -19.416  16.503  44.760  1.00 82.03           N  
ATOM   1504  CZ  ARG A 740     -20.480  15.714  44.879  1.00 83.23           C  
ATOM   1505  NH1 ARG A 740     -20.326  14.460  45.291  1.00 81.11           N  
ATOM   1506  NH2 ARG A 740     -21.695  16.179  44.598  1.00 78.75           N  
ATOM   1507  N   LYS A 741     -16.490  18.448  40.620  1.00 88.59           N  
ATOM   1508  CA  LYS A 741     -15.059  18.147  40.538  1.00 87.97           C  
ATOM   1509  C   LYS A 741     -14.497  18.481  39.148  1.00 85.14           C  
ATOM   1510  O   LYS A 741     -13.507  17.899  38.721  1.00 84.37           O  
ATOM   1511  CB  LYS A 741     -14.778  16.684  40.933  1.00 78.85           C  
ATOM   1512  N   ASN A 742     -15.139  19.431  38.465  1.00 85.29           N  
ATOM   1513  CA  ASN A 742     -14.745  19.887  37.119  1.00 91.56           C  
ATOM   1514  C   ASN A 742     -14.373  18.784  36.103  1.00 92.79           C  
ATOM   1515  O   ASN A 742     -13.888  19.075  35.000  1.00 83.94           O  
ATOM   1516  CB  ASN A 742     -13.645  20.951  37.200  1.00 87.07           C  
ATOM   1517  N   GLN A 743     -14.649  17.532  36.478  1.00 90.89           N  
ATOM   1518  CA  GLN A 743     -14.302  16.343  35.696  1.00 86.70           C  
ATOM   1519  C   GLN A 743     -15.191  16.071  34.463  1.00 91.33           C  
ATOM   1520  O   GLN A 743     -14.808  15.284  33.595  1.00 95.37           O  
ATOM   1521  CB  GLN A 743     -14.311  15.092  36.601  1.00 89.13           C  
ATOM   1522  CG  GLN A 743     -13.064  14.863  37.467  1.00 86.86           C  
ATOM   1523  N   PHE A 744     -16.365  16.694  34.373  1.00 89.78           N  
ATOM   1524  CA  PHE A 744     -17.319  16.312  33.320  1.00 90.05           C  
ATOM   1525  C   PHE A 744     -16.758  16.343  31.889  1.00 90.73           C  
ATOM   1526  O   PHE A 744     -16.196  17.346  31.439  1.00 93.22           O  
ATOM   1527  CB  PHE A 744     -18.623  17.115  33.398  1.00 88.02           C  
ATOM   1528  CG  PHE A 744     -19.693  16.603  32.468  1.00 87.51           C  
ATOM   1529  CD1 PHE A 744     -20.318  15.382  32.716  1.00 84.31           C  
ATOM   1530  CD2 PHE A 744     -20.061  17.326  31.336  1.00 87.42           C  
ATOM   1531  CE1 PHE A 744     -21.298  14.893  31.862  1.00 77.45           C  
ATOM   1532  CE2 PHE A 744     -21.043  16.847  30.476  1.00 84.46           C  
ATOM   1533  CZ  PHE A 744     -21.663  15.624  30.743  1.00 78.43           C  
ATOM   1534  N   ASN A 745     -16.939  15.237  31.177  1.00 86.27           N  
ATOM   1535  CA  ASN A 745     -16.397  15.085  29.835  1.00 90.99           C  
ATOM   1536  C   ASN A 745     -17.305  14.228  28.948  1.00 92.57           C  
ATOM   1537  O   ASN A 745     -17.403  13.004  29.125  1.00 90.28           O  
ATOM   1538  CB  ASN A 745     -14.990  14.481  29.909  1.00 91.42           C  
ATOM   1539  CG  ASN A 745     -14.455  14.048  28.547  1.00 94.51           C  
ATOM   1540  OD1 ASN A 745     -14.565  14.772  27.549  1.00 93.49           O  
ATOM   1541  ND2 ASN A 745     -13.873  12.852  28.503  1.00 91.99           N  
ATOM   1542  N   LEU A 746     -17.968  14.875  27.994  1.00 88.08           N  
ATOM   1543  CA  LEU A 746     -18.934  14.185  27.147  1.00 87.40           C  
ATOM   1544  C   LEU A 746     -18.268  13.186  26.193  1.00 88.95           C  
ATOM   1545  O   LEU A 746     -18.928  12.294  25.672  1.00 88.53           O  
ATOM   1546  CB  LEU A 746     -19.812  15.189  26.380  1.00 79.55           C  
ATOM   1547  N   GLU A 747     -16.963  13.321  25.973  1.00 89.76           N  
ATOM   1548  CA  GLU A 747     -16.279  12.443  25.023  1.00 88.50           C  
ATOM   1549  C   GLU A 747     -16.133  11.023  25.569  1.00 86.08           C  
ATOM   1550  O   GLU A 747     -15.761  10.106  24.843  1.00 84.67           O  
ATOM   1551  CB  GLU A 747     -14.922  13.016  24.604  1.00 83.97           C  
ATOM   1552  N   ASP A 748     -16.448  10.838  26.846  1.00 87.64           N  
ATOM   1553  CA  ASP A 748     -16.430   9.500  27.442  1.00 87.08           C  
ATOM   1554  C   ASP A 748     -17.755   8.759  27.236  1.00 83.82           C  
ATOM   1555  O   ASP A 748     -18.814   9.248  27.610  1.00 85.58           O  
ATOM   1556  CB  ASP A 748     -16.093   9.571  28.934  1.00 82.31           C  
ATOM   1557  CG  ASP A 748     -16.208   8.225  29.621  1.00 86.58           C  
ATOM   1558  OD1 ASP A 748     -15.984   7.192  28.955  1.00 89.06           O  
ATOM   1559  OD2 ASP A 748     -16.526   8.192  30.828  1.00 89.63           O  
ATOM   1560  N   PRO A 749     -17.696   7.571  26.631  1.00 85.79           N  
ATOM   1561  CA  PRO A 749     -18.898   6.751  26.430  1.00 87.15           C  
ATOM   1562  C   PRO A 749     -19.789   6.680  27.666  1.00 81.48           C  
ATOM   1563  O   PRO A 749     -21.005   6.823  27.549  1.00 80.79           O  
ATOM   1564  CB  PRO A 749     -18.324   5.361  26.130  1.00 79.63           C  
ATOM   1565  CG  PRO A 749     -17.012   5.645  25.486  1.00 81.99           C  
ATOM   1566  CD  PRO A 749     -16.490   6.943  26.064  1.00 82.60           C  
ATOM   1567  N   HIS A 750     -19.194   6.454  28.833  1.00 84.34           N  
ATOM   1568  CA  HIS A 750     -19.980   6.209  30.038  1.00 84.57           C  
ATOM   1569  C   HIS A 750     -20.676   7.471  30.523  1.00 81.14           C  
ATOM   1570  O   HIS A 750     -21.834   7.442  30.926  1.00 73.90           O  
ATOM   1571  CB  HIS A 750     -19.115   5.637  31.154  1.00 81.18           C  
ATOM   1572  CG  HIS A 750     -19.889   5.301  32.391  1.00 88.02           C  
ATOM   1573  ND1 HIS A 750     -19.928   6.126  33.495  1.00 85.54           N  
ATOM   1574  CD2 HIS A 750     -20.668   4.233  32.692  1.00 87.48           C  
ATOM   1575  CE1 HIS A 750     -20.688   5.576  34.426  1.00 87.31           C  
ATOM   1576  NE2 HIS A 750     -21.150   4.427  33.964  1.00 83.39           N  
ATOM   1577  N   GLN A 751     -19.956   8.583  30.480  1.00 82.11           N  
ATOM   1578  CA  GLN A 751     -20.525   9.856  30.885  1.00 82.19           C  
ATOM   1579  C   GLN A 751     -21.572  10.350  29.895  1.00 77.71           C  
ATOM   1580  O   GLN A 751     -22.579  10.943  30.298  1.00 75.67           O  
ATOM   1581  CB  GLN A 751     -19.426  10.896  31.096  1.00 86.03           C  
ATOM   1582  CG  GLN A 751     -18.602  10.644  32.347  1.00 81.59           C  
ATOM   1583  CD  GLN A 751     -17.478  11.636  32.500  1.00 91.34           C  
ATOM   1584  OE1 GLN A 751     -17.559  12.773  32.019  1.00 89.88           O  
ATOM   1585  NE2 GLN A 751     -16.407  11.209  33.161  1.00 92.89           N  
ATOM   1586  N   LYS A 752     -21.329  10.099  28.609  1.00 77.49           N  
ATOM   1587  CA  LYS A 752     -22.293  10.392  27.551  1.00 76.41           C  
ATOM   1588  C   LYS A 752     -23.646   9.742  27.823  1.00 72.31           C  
ATOM   1589  O   LYS A 752     -24.679  10.400  27.869  1.00 66.87           O  
ATOM   1590  CB  LYS A 752     -21.768   9.860  26.229  1.00 76.44           C  
ATOM   1591  CG  LYS A 752     -21.553  10.921  25.201  1.00 80.13           C  
ATOM   1592  CD  LYS A 752     -22.850  11.446  24.651  1.00 71.48           C  
ATOM   1593  CE  LYS A 752     -22.549  12.306  23.442  1.00 71.72           C  
ATOM   1594  NZ  LYS A 752     -21.732  11.540  22.450  1.00 71.51           N  
ATOM   1595  N   GLU A 753     -23.626   8.433  27.994  1.00 69.80           N  
ATOM   1596  CA  GLU A 753     -24.839   7.705  28.252  1.00 71.71           C  
ATOM   1597  C   GLU A 753     -25.567   8.272  29.472  1.00 73.09           C  
ATOM   1598  O   GLU A 753     -26.801   8.253  29.537  1.00 71.70           O  
ATOM   1599  CB  GLU A 753     -24.515   6.234  28.454  1.00 71.09           C  
ATOM   1600  CG  GLU A 753     -25.665   5.434  29.007  1.00 80.82           C  
ATOM   1601  CD  GLU A 753     -25.327   3.964  29.103  1.00 89.52           C  
ATOM   1602  OE1 GLU A 753     -26.013   3.234  29.863  1.00 91.17           O  
ATOM   1603  OE2 GLU A 753     -24.364   3.547  28.414  1.00 85.85           O  
ATOM   1604  N   LEU A 754     -24.800   8.787  30.428  1.00 71.06           N  
ATOM   1605  CA  LEU A 754     -25.361   9.283  31.680  1.00 70.25           C  
ATOM   1606  C   LEU A 754     -26.030  10.642  31.466  1.00 66.73           C  
ATOM   1607  O   LEU A 754     -27.102  10.933  32.009  1.00 58.44           O  
ATOM   1608  CB  LEU A 754     -24.268   9.381  32.742  1.00 68.82           C  
ATOM   1609  CG  LEU A 754     -24.589   9.976  34.115  1.00 70.29           C  
ATOM   1610  CD1 LEU A 754     -25.575   9.123  34.929  1.00 64.84           C  
ATOM   1611  CD2 LEU A 754     -23.289  10.181  34.875  1.00 71.79           C  
ATOM   1612  N   PHE A 755     -25.385  11.467  30.658  1.00 63.99           N  
ATOM   1613  CA  PHE A 755     -25.914  12.770  30.346  1.00 59.29           C  
ATOM   1614  C   PHE A 755     -27.235  12.601  29.607  1.00 62.31           C  
ATOM   1615  O   PHE A 755     -28.219  13.276  29.912  1.00 61.65           O  
ATOM   1616  CB  PHE A 755     -24.899  13.521  29.510  1.00 57.87           C  
ATOM   1617  CG  PHE A 755     -25.406  14.787  28.932  1.00 60.91           C  
ATOM   1618  CD1 PHE A 755     -25.771  15.845  29.753  1.00 64.14           C  
ATOM   1619  CD2 PHE A 755     -25.487  14.946  27.557  1.00 62.05           C  
ATOM   1620  CE1 PHE A 755     -26.227  17.044  29.210  1.00 62.35           C  
ATOM   1621  CE2 PHE A 755     -25.945  16.143  27.004  1.00 65.53           C  
ATOM   1622  CZ  PHE A 755     -26.318  17.190  27.832  1.00 63.88           C  
ATOM   1623  N   LEU A 756     -27.267  11.675  28.653  1.00 63.43           N  
ATOM   1624  CA  LEU A 756     -28.489  11.397  27.913  1.00 56.75           C  
ATOM   1625  C   LEU A 756     -29.619  10.992  28.868  1.00 56.45           C  
ATOM   1626  O   LEU A 756     -30.764  11.378  28.676  1.00 52.80           O  
ATOM   1627  CB  LEU A 756     -28.245  10.321  26.860  1.00 59.13           C  
ATOM   1628  CG  LEU A 756     -27.167  10.608  25.804  1.00 63.38           C  
ATOM   1629  CD1 LEU A 756     -26.933   9.388  24.941  1.00 63.52           C  
ATOM   1630  CD2 LEU A 756     -27.531  11.789  24.936  1.00 61.25           C  
ATOM   1631  N   ALA A 757     -29.286  10.232  29.908  1.00 57.64           N  
ATOM   1632  CA  ALA A 757     -30.267   9.839  30.913  1.00 55.76           C  
ATOM   1633  C   ALA A 757     -30.770  11.064  31.672  1.00 56.52           C  
ATOM   1634  O   ALA A 757     -31.964  11.195  31.968  1.00 53.34           O  
ATOM   1635  CB  ALA A 757     -29.663   8.829  31.884  1.00 53.16           C  
ATOM   1636  N   MET A 758     -29.833  11.946  31.997  1.00 55.94           N  
ATOM   1637  CA  MET A 758     -30.127  13.154  32.741  1.00 56.90           C  
ATOM   1638  C   MET A 758     -30.984  14.082  31.882  1.00 56.58           C  
ATOM   1639  O   MET A 758     -32.018  14.587  32.326  1.00 52.08           O  
ATOM   1640  CB  MET A 758     -28.817  13.832  33.149  1.00 57.83           C  
ATOM   1641  CG  MET A 758     -27.968  12.980  34.063  1.00 57.97           C  
ATOM   1642  SD  MET A 758     -28.841  12.623  35.588  1.00 61.66           S  
ATOM   1643  CE  MET A 758     -28.840  10.837  35.729  1.00 56.31           C  
ATOM   1644  N   LEU A 759     -30.543  14.277  30.643  1.00 55.24           N  
ATOM   1645  CA  LEU A 759     -31.268  15.068  29.669  1.00 52.23           C  
ATOM   1646  C   LEU A 759     -32.699  14.569  29.506  1.00 53.02           C  
ATOM   1647  O   LEU A 759     -33.621  15.368  29.418  1.00 52.18           O  
ATOM   1648  CB  LEU A 759     -30.533  15.048  28.331  1.00 54.57           C  
ATOM   1649  CG  LEU A 759     -31.042  15.980  27.224  1.00 60.45           C  
ATOM   1650  CD1 LEU A 759     -31.368  17.356  27.763  1.00 59.24           C  
ATOM   1651  CD2 LEU A 759     -30.018  16.095  26.109  1.00 60.22           C  
ATOM   1652  N   MET A 760     -32.892  13.253  29.476  1.00 52.50           N  
ATOM   1653  CA  MET A 760     -34.241  12.707  29.366  1.00 48.98           C  
ATOM   1654  C   MET A 760     -35.116  13.151  30.528  1.00 48.52           C  
ATOM   1655  O   MET A 760     -36.231  13.607  30.317  1.00 46.46           O  
ATOM   1656  CB  MET A 760     -34.243  11.179  29.271  1.00 48.30           C  
ATOM   1657  CG  MET A 760     -33.932  10.615  27.882  1.00 52.23           C  
ATOM   1658  SD  MET A 760     -35.018  11.069  26.492  1.00 51.79           S  
ATOM   1659  CE  MET A 760     -36.617  10.420  26.985  1.00 41.06           C  
ATOM   1660  N   THR A 761     -34.604  13.023  31.750  1.00 50.14           N  
ATOM   1661  CA  THR A 761     -35.372  13.377  32.939  1.00 48.65           C  
ATOM   1662  C   THR A 761     -35.689  14.874  32.975  1.00 48.67           C  
ATOM   1663  O   THR A 761     -36.804  15.285  33.308  1.00 47.33           O  
ATOM   1664  CB  THR A 761     -34.666  12.935  34.227  1.00 51.35           C  
ATOM   1665  OG1 THR A 761     -34.528  11.506  34.235  1.00 51.73           O  
ATOM   1666  CG2 THR A 761     -35.486  13.355  35.442  1.00 48.91           C  
ATOM   1667  N   ALA A 762     -34.713  15.680  32.588  1.00 47.65           N  
ATOM   1668  CA  ALA A 762     -34.905  17.119  32.488  1.00 48.55           C  
ATOM   1669  C   ALA A 762     -36.085  17.526  31.588  1.00 49.63           C  
ATOM   1670  O   ALA A 762     -36.843  18.441  31.932  1.00 48.06           O  
ATOM   1671  CB  ALA A 762     -33.617  17.802  32.036  1.00 46.68           C  
ATOM   1672  N   CYS A 763     -36.244  16.869  30.441  1.00 46.02           N  
ATOM   1673  CA  CYS A 763     -37.335  17.238  29.540  1.00 48.86           C  
ATOM   1674  C   CYS A 763     -38.655  16.741  30.089  1.00 50.35           C  
ATOM   1675  O   CYS A 763     -39.674  17.420  30.002  1.00 47.57           O  
ATOM   1676  CB  CYS A 763     -37.126  16.659  28.151  1.00 46.28           C  
ATOM   1677  SG  CYS A 763     -35.643  17.254  27.384  1.00 56.39           S  
ATOM   1678  N   ASP A 764     -38.609  15.536  30.644  1.00 50.27           N  
ATOM   1679  CA  ASP A 764     -39.770  14.869  31.198  1.00 48.91           C  
ATOM   1680  C   ASP A 764     -40.375  15.720  32.312  1.00 50.15           C  
ATOM   1681  O   ASP A 764     -41.595  15.796  32.443  1.00 50.85           O  
ATOM   1682  CB  ASP A 764     -39.354  13.482  31.731  1.00 49.96           C  
ATOM   1683  CG  ASP A 764     -40.540  12.561  31.975  1.00 53.93           C  
ATOM   1684  OD1 ASP A 764     -41.666  12.961  31.620  1.00 56.69           O  
ATOM   1685  OD2 ASP A 764     -40.363  11.432  32.490  1.00 58.14           O  
ATOM   1686  N   LEU A 765     -39.530  16.364  33.113  1.00 47.56           N  
ATOM   1687  CA  LEU A 765     -40.034  17.155  34.243  1.00 51.90           C  
ATOM   1688  C   LEU A 765     -40.184  18.637  33.919  1.00 53.14           C  
ATOM   1689  O   LEU A 765     -40.446  19.436  34.819  1.00 52.80           O  
ATOM   1690  CB  LEU A 765     -39.120  17.029  35.467  1.00 49.18           C  
ATOM   1691  CG  LEU A 765     -38.748  15.616  35.932  1.00 50.13           C  
ATOM   1692  CD1 LEU A 765     -37.694  15.686  37.004  1.00 45.32           C  
ATOM   1693  CD2 LEU A 765     -39.951  14.800  36.390  1.00 43.91           C  
ATOM   1694  N   SER A 766     -40.010  18.999  32.649  1.00 47.09           N  
ATOM   1695  CA  SER A 766     -39.854  20.397  32.275  1.00 46.45           C  
ATOM   1696  C   SER A 766     -41.099  21.243  32.520  1.00 47.83           C  
ATOM   1697  O   SER A 766     -41.023  22.465  32.550  1.00 48.57           O  
ATOM   1698  CB  SER A 766     -39.375  20.526  30.822  1.00 48.51           C  
ATOM   1699  OG  SER A 766     -40.295  19.951  29.908  1.00 51.20           O  
ATOM   1700  N   ALA A 767     -42.243  20.596  32.691  1.00 44.87           N  
ATOM   1701  CA  ALA A 767     -43.454  21.313  33.038  1.00 45.45           C  
ATOM   1702  C   ALA A 767     -43.217  22.228  34.255  1.00 52.17           C  
ATOM   1703  O   ALA A 767     -43.788  23.317  34.352  1.00 51.65           O  
ATOM   1704  CB  ALA A 767     -44.560  20.341  33.312  1.00 43.63           C  
ATOM   1705  N   ILE A 768     -42.351  21.776  35.161  1.00 49.94           N  
ATOM   1706  CA  ILE A 768     -42.016  22.491  36.380  1.00 49.97           C  
ATOM   1707  C   ILE A 768     -41.264  23.797  36.101  1.00 54.15           C  
ATOM   1708  O   ILE A 768     -41.075  24.647  37.000  1.00 53.50           O  
ATOM   1709  CB  ILE A 768     -41.151  21.600  37.312  1.00 51.59           C  
ATOM   1710  CG1 ILE A 768     -41.258  22.097  38.748  1.00 50.47           C  
ATOM   1711  CG2 ILE A 768     -39.675  21.554  36.835  1.00 48.67           C  
ATOM   1712  CD1 ILE A 768     -42.662  22.159  39.254  1.00 50.32           C  
ATOM   1713  N   THR A 769     -40.825  23.962  34.859  1.00 48.42           N  
ATOM   1714  CA  THR A 769     -39.990  25.109  34.535  1.00 52.81           C  
ATOM   1715  C   THR A 769     -40.783  26.178  33.801  1.00 51.65           C  
ATOM   1716  O   THR A 769     -40.243  27.227  33.420  1.00 47.37           O  
ATOM   1717  CB  THR A 769     -38.767  24.701  33.691  1.00 51.96           C  
ATOM   1718  OG1 THR A 769     -39.210  24.211  32.423  1.00 47.85           O  
ATOM   1719  CG2 THR A 769     -37.973  23.634  34.400  1.00 49.43           C  
ATOM   1720  N   LYS A 770     -42.071  25.906  33.619  1.00 49.19           N  
ATOM   1721  CA  LYS A 770     -42.893  26.732  32.748  1.00 51.23           C  
ATOM   1722  C   LYS A 770     -43.326  28.052  33.397  1.00 54.78           C  
ATOM   1723  O   LYS A 770     -43.251  28.212  34.617  1.00 54.85           O  
ATOM   1724  CB  LYS A 770     -44.105  25.938  32.257  1.00 50.37           C  
ATOM   1725  CG  LYS A 770     -43.769  24.793  31.353  1.00 45.00           C  
ATOM   1726  CD  LYS A 770     -43.264  25.275  30.011  1.00 49.61           C  
ATOM   1727  CE  LYS A 770     -42.903  24.101  29.112  1.00 52.59           C  
ATOM   1728  NZ  LYS A 770     -42.629  24.509  27.700  1.00 56.33           N  
ATOM   1729  N   PRO A 771     -43.760  29.020  32.573  1.00 55.61           N  
ATOM   1730  CA  PRO A 771     -44.307  30.241  33.166  1.00 50.65           C  
ATOM   1731  C   PRO A 771     -45.459  29.903  34.108  1.00 54.30           C  
ATOM   1732  O   PRO A 771     -46.236  28.977  33.854  1.00 54.39           O  
ATOM   1733  CB  PRO A 771     -44.790  31.018  31.945  1.00 45.53           C  
ATOM   1734  CG  PRO A 771     -43.890  30.571  30.865  1.00 48.80           C  
ATOM   1735  CD  PRO A 771     -43.681  29.113  31.104  1.00 49.85           C  
ATOM   1736  N   TRP A 772     -45.560  30.664  35.191  1.00 58.67           N  
ATOM   1737  CA  TRP A 772     -46.453  30.340  36.298  1.00 58.97           C  
ATOM   1738  C   TRP A 772     -47.898  30.013  35.896  1.00 56.83           C  
ATOM   1739  O   TRP A 772     -48.458  29.008  36.342  1.00 57.64           O  
ATOM   1740  CB  TRP A 772     -46.394  31.453  37.343  1.00 63.19           C  
ATOM   1741  CG  TRP A 772     -47.359  31.305  38.484  1.00 65.42           C  
ATOM   1742  CD1 TRP A 772     -48.372  32.160  38.820  1.00 62.71           C  
ATOM   1743  CD2 TRP A 772     -47.397  30.243  39.441  1.00 65.12           C  
ATOM   1744  NE1 TRP A 772     -49.034  31.696  39.925  1.00 64.27           N  
ATOM   1745  CE2 TRP A 772     -48.458  30.518  40.326  1.00 67.38           C  
ATOM   1746  CE3 TRP A 772     -46.635  29.088  39.638  1.00 65.34           C  
ATOM   1747  CZ2 TRP A 772     -48.774  29.678  41.395  1.00 66.05           C  
ATOM   1748  CZ3 TRP A 772     -46.952  28.252  40.701  1.00 64.27           C  
ATOM   1749  CH2 TRP A 772     -48.010  28.552  41.564  1.00 66.49           C  
ATOM   1750  N   PRO A 773     -48.505  30.851  35.054  1.00 54.56           N  
ATOM   1751  CA  PRO A 773     -49.885  30.557  34.637  1.00 59.01           C  
ATOM   1752  C   PRO A 773     -50.006  29.184  33.988  1.00 56.62           C  
ATOM   1753  O   PRO A 773     -51.047  28.544  34.064  1.00 59.48           O  
ATOM   1754  CB  PRO A 773     -50.188  31.653  33.613  1.00 57.21           C  
ATOM   1755  CG  PRO A 773     -49.262  32.773  33.983  1.00 58.43           C  
ATOM   1756  CD  PRO A 773     -48.014  32.125  34.509  1.00 55.86           C  
ATOM   1757  N   ILE A 774     -48.931  28.722  33.373  1.00 52.77           N  
ATOM   1758  CA  ILE A 774     -48.949  27.422  32.735  1.00 53.39           C  
ATOM   1759  C   ILE A 774     -48.609  26.305  33.718  1.00 54.08           C  
ATOM   1760  O   ILE A 774     -49.328  25.297  33.812  1.00 54.10           O  
ATOM   1761  CB  ILE A 774     -48.042  27.424  31.488  1.00 56.74           C  
ATOM   1762  CG1 ILE A 774     -48.706  28.275  30.401  1.00 52.48           C  
ATOM   1763  CG2 ILE A 774     -47.793  26.015  30.981  1.00 50.81           C  
ATOM   1764  CD1 ILE A 774     -47.943  28.332  29.164  1.00 56.91           C  
ATOM   1765  N   GLN A 775     -47.531  26.495  34.470  1.00 50.46           N  
ATOM   1766  CA  GLN A 775     -47.228  25.582  35.569  1.00 54.59           C  
ATOM   1767  C   GLN A 775     -48.436  25.338  36.484  1.00 51.73           C  
ATOM   1768  O   GLN A 775     -48.707  24.208  36.865  1.00 52.16           O  
ATOM   1769  CB  GLN A 775     -45.997  26.046  36.363  1.00 55.23           C  
ATOM   1770  CG  GLN A 775     -45.853  25.427  37.753  1.00 53.00           C  
ATOM   1771  CD  GLN A 775     -45.798  23.904  37.772  1.00 49.66           C  
ATOM   1772  OE1 GLN A 775     -45.426  23.250  36.792  1.00 49.21           O  
ATOM   1773  NE2 GLN A 775     -46.182  23.331  38.902  1.00 50.17           N  
ATOM   1774  N   GLN A 776     -49.192  26.375  36.803  1.00 53.85           N  
ATOM   1775  CA  GLN A 776     -50.380  26.156  37.626  1.00 57.31           C  
ATOM   1776  C   GLN A 776     -51.341  25.174  36.996  1.00 55.13           C  
ATOM   1777  O   GLN A 776     -51.925  24.339  37.686  1.00 57.63           O  
ATOM   1778  CB  GLN A 776     -51.120  27.452  37.884  1.00 58.32           C  
ATOM   1779  CG  GLN A 776     -50.407  28.346  38.840  1.00 66.62           C  
ATOM   1780  CD  GLN A 776     -51.280  29.481  39.316  1.00 73.79           C  
ATOM   1781  OE1 GLN A 776     -51.957  29.366  40.349  1.00 75.04           O  
ATOM   1782  NE2 GLN A 776     -51.278  30.591  38.565  1.00 69.04           N  
ATOM   1783  N   ARG A 777     -51.513  25.280  35.686  1.00 53.04           N  
ATOM   1784  CA  ARG A 777     -52.499  24.467  34.999  1.00 54.19           C  
ATOM   1785  C   ARG A 777     -52.035  23.025  34.880  1.00 53.94           C  
ATOM   1786  O   ARG A 777     -52.814  22.088  35.072  1.00 53.49           O  
ATOM   1787  CB  ARG A 777     -52.809  25.062  33.627  1.00 59.43           C  
ATOM   1788  CG  ARG A 777     -53.412  26.470  33.688  1.00 57.36           C  
ATOM   1789  CD  ARG A 777     -54.891  26.476  34.109  1.00 58.43           C  
ATOM   1790  NE  ARG A 777     -55.514  27.763  33.806  1.00 61.89           N  
ATOM   1791  CZ  ARG A 777     -56.750  28.120  34.150  1.00 60.75           C  
ATOM   1792  NH1 ARG A 777     -57.533  27.293  34.834  1.00 56.19           N  
ATOM   1793  NH2 ARG A 777     -57.196  29.325  33.813  1.00 62.43           N  
ATOM   1794  N   ILE A 778     -50.754  22.839  34.588  1.00 54.53           N  
ATOM   1795  CA  ILE A 778     -50.204  21.487  34.581  1.00 53.55           C  
ATOM   1796  C   ILE A 778     -50.306  20.865  35.980  1.00 51.99           C  
ATOM   1797  O   ILE A 778     -50.834  19.772  36.129  1.00 52.14           O  
ATOM   1798  CB  ILE A 778     -48.769  21.450  33.986  1.00 53.81           C  
ATOM   1799  CG1 ILE A 778     -48.850  21.588  32.464  1.00 54.45           C  
ATOM   1800  CG2 ILE A 778     -48.070  20.140  34.272  1.00 47.97           C  
ATOM   1801  CD1 ILE A 778     -47.896  22.578  31.914  1.00 54.35           C  
ATOM   1802  N   ALA A 779     -49.841  21.580  37.001  1.00 51.30           N  
ATOM   1803  CA  ALA A 779     -49.971  21.113  38.376  1.00 51.54           C  
ATOM   1804  C   ALA A 779     -51.393  20.652  38.630  1.00 53.64           C  
ATOM   1805  O   ALA A 779     -51.645  19.689  39.344  1.00 56.77           O  
ATOM   1806  CB  ALA A 779     -49.588  22.198  39.348  1.00 48.75           C  
ATOM   1807  N   GLU A 780     -52.342  21.337  38.028  1.00 55.79           N  
ATOM   1808  CA  GLU A 780     -53.726  20.947  38.206  1.00 57.16           C  
ATOM   1809  C   GLU A 780     -54.062  19.623  37.497  1.00 60.31           C  
ATOM   1810  O   GLU A 780     -54.776  18.791  38.046  1.00 60.76           O  
ATOM   1811  CB  GLU A 780     -54.623  22.071  37.749  1.00 52.30           C  
ATOM   1812  CG  GLU A 780     -56.060  21.748  37.821  1.00 63.28           C  
ATOM   1813  CD  GLU A 780     -56.903  22.960  37.477  1.00 73.54           C  
ATOM   1814  OE1 GLU A 780     -56.293  24.060  37.342  1.00 63.21           O  
ATOM   1815  OE2 GLU A 780     -58.151  22.801  37.333  1.00 71.53           O  
ATOM   1816  N   LEU A 781     -53.540  19.423  36.288  1.00 55.65           N  
ATOM   1817  CA  LEU A 781     -53.650  18.119  35.638  1.00 55.72           C  
ATOM   1818  C   LEU A 781     -53.000  16.994  36.446  1.00 57.28           C  
ATOM   1819  O   LEU A 781     -53.567  15.913  36.590  1.00 53.80           O  
ATOM   1820  CB  LEU A 781     -53.025  18.147  34.247  1.00 55.17           C  
ATOM   1821  CG  LEU A 781     -53.687  19.032  33.196  1.00 57.64           C  
ATOM   1822  CD1 LEU A 781     -52.816  19.100  31.957  1.00 51.51           C  
ATOM   1823  CD2 LEU A 781     -55.090  18.545  32.867  1.00 54.07           C  
ATOM   1824  N   VAL A 782     -51.793  17.246  36.940  1.00 55.28           N  
ATOM   1825  CA  VAL A 782     -51.070  16.253  37.703  1.00 55.26           C  
ATOM   1826  C   VAL A 782     -51.883  15.886  38.943  1.00 60.25           C  
ATOM   1827  O   VAL A 782     -51.962  14.724  39.339  1.00 62.78           O  
ATOM   1828  CB  VAL A 782     -49.688  16.785  38.118  1.00 58.33           C  
ATOM   1829  CG1 VAL A 782     -49.026  15.851  39.107  1.00 62.63           C  
ATOM   1830  CG2 VAL A 782     -48.804  17.016  36.905  1.00 52.92           C  
ATOM   1831  N   ALA A 783     -52.504  16.887  39.547  1.00 62.63           N  
ATOM   1832  CA  ALA A 783     -53.270  16.686  40.768  1.00 63.47           C  
ATOM   1833  C   ALA A 783     -54.463  15.787  40.505  1.00 64.48           C  
ATOM   1834  O   ALA A 783     -54.800  14.936  41.325  1.00 67.85           O  
ATOM   1835  CB  ALA A 783     -53.725  18.024  41.318  1.00 60.76           C  
ATOM   1836  N   THR A 784     -55.102  15.992  39.356  1.00 61.25           N  
ATOM   1837  CA  THR A 784     -56.270  15.216  38.964  1.00 65.30           C  
ATOM   1838  C   THR A 784     -55.932  13.740  38.790  1.00 67.30           C  
ATOM   1839  O   THR A 784     -56.718  12.855  39.123  1.00 70.92           O  
ATOM   1840  CB  THR A 784     -56.833  15.715  37.627  1.00 66.03           C  
ATOM   1841  OG1 THR A 784     -57.351  17.035  37.787  1.00 65.12           O  
ATOM   1842  CG2 THR A 784     -57.939  14.795  37.120  1.00 62.27           C  
ATOM   1843  N   GLU A 785     -54.764  13.477  38.234  1.00 62.26           N  
ATOM   1844  CA  GLU A 785     -54.360  12.111  38.012  1.00 64.08           C  
ATOM   1845  C   GLU A 785     -53.964  11.478  39.337  1.00 65.04           C  
ATOM   1846  O   GLU A 785     -54.303  10.333  39.604  1.00 67.77           O  
ATOM   1847  CB  GLU A 785     -53.212  12.048  37.004  1.00 60.84           C  
ATOM   1848  CG  GLU A 785     -52.752  10.642  36.692  1.00 63.07           C  
ATOM   1849  CD  GLU A 785     -51.645  10.573  35.648  1.00 65.73           C  
ATOM   1850  OE1 GLU A 785     -50.733   9.742  35.849  1.00 63.24           O  
ATOM   1851  OE2 GLU A 785     -51.690  11.324  34.634  1.00 61.52           O  
ATOM   1852  N   PHE A 786     -53.264  12.241  40.169  1.00 65.73           N  
ATOM   1853  CA  PHE A 786     -52.779  11.750  41.461  1.00 68.91           C  
ATOM   1854  C   PHE A 786     -53.872  11.380  42.446  1.00 70.25           C  
ATOM   1855  O   PHE A 786     -53.728  10.428  43.202  1.00 72.95           O  
ATOM   1856  CB  PHE A 786     -51.849  12.771  42.129  1.00 67.39           C  
ATOM   1857  CG  PHE A 786     -50.438  12.747  41.599  1.00 74.03           C  
ATOM   1858  CD1 PHE A 786     -50.180  12.387  40.281  1.00 71.37           C  
ATOM   1859  CD2 PHE A 786     -49.366  13.064  42.423  1.00 77.28           C  
ATOM   1860  CE1 PHE A 786     -48.886  12.353  39.794  1.00 70.76           C  
ATOM   1861  CE2 PHE A 786     -48.067  13.031  41.941  1.00 77.13           C  
ATOM   1862  CZ  PHE A 786     -47.827  12.678  40.624  1.00 75.93           C  
ATOM   1863  N   PHE A 787     -54.964  12.130  42.432  1.00 71.30           N  
ATOM   1864  CA  PHE A 787     -55.899  12.088  43.540  1.00 75.54           C  
ATOM   1865  C   PHE A 787     -57.303  11.730  43.124  1.00 78.52           C  
ATOM   1866  O   PHE A 787     -58.095  11.291  43.950  1.00 85.03           O  
ATOM   1867  CB  PHE A 787     -55.921  13.441  44.249  1.00 71.44           C  
ATOM   1868  CG  PHE A 787     -54.594  13.848  44.797  1.00 71.85           C  
ATOM   1869  CD1 PHE A 787     -54.166  15.161  44.706  1.00 72.95           C  
ATOM   1870  CD2 PHE A 787     -53.768  12.909  45.410  1.00 75.33           C  
ATOM   1871  CE1 PHE A 787     -52.933  15.539  45.216  1.00 75.51           C  
ATOM   1872  CE2 PHE A 787     -52.534  13.273  45.926  1.00 74.89           C  
ATOM   1873  CZ  PHE A 787     -52.113  14.592  45.827  1.00 78.00           C  
ATOM   1874  N   ASP A 788     -57.620  11.926  41.853  1.00 75.10           N  
ATOM   1875  CA  ASP A 788     -59.001  11.765  41.417  1.00 79.64           C  
ATOM   1876  C   ASP A 788     -59.185  10.639  40.420  1.00 79.58           C  
ATOM   1877  O   ASP A 788     -60.268  10.483  39.856  1.00 85.25           O  
ATOM   1878  CB  ASP A 788     -59.540  13.066  40.810  1.00 82.12           C  
ATOM   1879  CG  ASP A 788     -59.448  14.242  41.767  1.00 89.12           C  
ATOM   1880  OD1 ASP A 788     -58.444  14.328  42.517  1.00 90.81           O  
ATOM   1881  OD2 ASP A 788     -60.380  15.077  41.770  1.00 90.10           O  
ATOM   1882  N   GLN A 789     -58.134   9.865  40.185  1.00 75.98           N  
ATOM   1883  CA  GLN A 789     -58.228   8.772  39.222  1.00 80.77           C  
ATOM   1884  C   GLN A 789     -57.534   7.548  39.789  1.00 80.28           C  
ATOM   1885  O   GLN A 789     -56.755   7.670  40.737  1.00 79.73           O  
ATOM   1886  CB  GLN A 789     -57.626   9.173  37.862  1.00 76.50           C  
ATOM   1887  CG  GLN A 789     -58.180  10.485  37.268  1.00 71.86           C  
ATOM   1888  CD  GLN A 789     -57.737  10.749  35.809  1.00 74.70           C  
ATOM   1889  OE1 GLN A 789     -58.519  11.260  34.996  1.00 73.22           O  
ATOM   1890  NE2 GLN A 789     -56.482  10.413  35.483  1.00 68.46           N  
ATOM   1891  N   LYS A 809     -56.922  17.718  50.693  1.00108.66           N  
ATOM   1892  CA  LYS A 809     -57.319  18.953  50.015  1.00109.79           C  
ATOM   1893  C   LYS A 809     -56.239  19.471  49.051  1.00101.35           C  
ATOM   1894  O   LYS A 809     -55.122  18.932  48.987  1.00 92.83           O  
ATOM   1895  CB  LYS A 809     -57.682  20.039  51.042  1.00 98.21           C  
ATOM   1896  N   LYS A 810     -56.593  20.518  48.306  1.00 98.36           N  
ATOM   1897  CA  LYS A 810     -55.649  21.227  47.442  1.00 95.32           C  
ATOM   1898  C   LYS A 810     -54.759  22.171  48.272  1.00 90.86           C  
ATOM   1899  O   LYS A 810     -53.985  22.965  47.728  1.00 81.34           O  
ATOM   1900  CB  LYS A 810     -56.402  22.000  46.347  1.00 89.72           C  
ATOM   1901  N   ASN A 811     -54.885  22.074  49.596  1.00 95.76           N  
ATOM   1902  CA  ASN A 811     -54.082  22.867  50.521  1.00 89.48           C  
ATOM   1903  C   ASN A 811     -52.674  22.295  50.671  1.00 82.47           C  
ATOM   1904  O   ASN A 811     -51.715  23.035  50.891  1.00 80.45           O  
ATOM   1905  CB  ASN A 811     -54.768  22.954  51.893  1.00 91.39           C  
ATOM   1906  N   LYS A 812     -52.558  20.977  50.538  1.00 80.27           N  
ATOM   1907  CA  LYS A 812     -51.281  20.298  50.725  1.00 78.91           C  
ATOM   1908  C   LYS A 812     -50.409  20.390  49.483  1.00 73.78           C  
ATOM   1909  O   LYS A 812     -49.214  20.095  49.535  1.00 73.18           O  
ATOM   1910  CB  LYS A 812     -51.508  18.826  51.086  1.00 81.98           C  
ATOM   1911  N   ILE A 813     -51.010  20.822  48.378  1.00 69.13           N  
ATOM   1912  CA  ILE A 813     -50.359  20.799  47.078  1.00 62.26           C  
ATOM   1913  C   ILE A 813     -49.201  21.780  46.892  1.00 62.60           C  
ATOM   1914  O   ILE A 813     -48.181  21.424  46.316  1.00 66.73           O  
ATOM   1915  CB  ILE A 813     -51.396  20.944  45.950  1.00 68.65           C  
ATOM   1916  CG1 ILE A 813     -52.097  19.601  45.731  1.00 70.31           C  
ATOM   1917  CG2 ILE A 813     -50.753  21.443  44.662  1.00 58.25           C  
ATOM   1918  CD1 ILE A 813     -53.373  19.696  44.948  1.00 73.75           C  
ATOM   1919  N   PRO A 814     -49.337  23.021  47.370  1.00 63.84           N  
ATOM   1920  CA  PRO A 814     -48.174  23.878  47.111  1.00 62.30           C  
ATOM   1921  C   PRO A 814     -46.953  23.362  47.849  1.00 64.07           C  
ATOM   1922  O   PRO A 814     -45.812  23.620  47.458  1.00 63.30           O  
ATOM   1923  CB  PRO A 814     -48.613  25.243  47.661  1.00 61.25           C  
ATOM   1924  CG  PRO A 814     -50.112  25.209  47.593  1.00 58.54           C  
ATOM   1925  CD  PRO A 814     -50.487  23.783  47.889  1.00 65.08           C  
ATOM   1926  N   SER A 815     -47.212  22.625  48.921  1.00 68.16           N  
ATOM   1927  CA  SER A 815     -46.166  22.078  49.767  1.00 66.50           C  
ATOM   1928  C   SER A 815     -45.435  20.968  49.030  1.00 64.06           C  
ATOM   1929  O   SER A 815     -44.208  20.973  48.907  1.00 61.47           O  
ATOM   1930  CB  SER A 815     -46.789  21.533  51.047  1.00 69.49           C  
ATOM   1931  OG  SER A 815     -45.880  20.691  51.734  1.00 78.91           O  
ATOM   1932  N   MET A 816     -46.209  20.013  48.541  1.00 60.49           N  
ATOM   1933  CA  MET A 816     -45.673  18.962  47.693  1.00 66.62           C  
ATOM   1934  C   MET A 816     -44.868  19.525  46.517  1.00 63.88           C  
ATOM   1935  O   MET A 816     -43.802  19.013  46.182  1.00 62.84           O  
ATOM   1936  CB  MET A 816     -46.809  18.083  47.180  1.00 67.06           C  
ATOM   1937  CG  MET A 816     -47.634  17.484  48.297  1.00 66.04           C  
ATOM   1938  SD  MET A 816     -49.080  16.613  47.685  1.00 73.94           S  
ATOM   1939  CE  MET A 816     -48.262  15.294  46.798  1.00 79.41           C  
ATOM   1940  N   GLN A 817     -45.369  20.579  45.892  1.00 57.93           N  
ATOM   1941  CA  GLN A 817     -44.655  21.140  44.756  1.00 61.70           C  
ATOM   1942  C   GLN A 817     -43.256  21.610  45.145  1.00 61.92           C  
ATOM   1943  O   GLN A 817     -42.290  21.390  44.399  1.00 58.16           O  
ATOM   1944  CB  GLN A 817     -45.449  22.273  44.099  1.00 61.49           C  
ATOM   1945  CG  GLN A 817     -46.627  21.809  43.266  1.00 60.08           C  
ATOM   1946  CD  GLN A 817     -46.264  20.678  42.325  1.00 60.77           C  
ATOM   1947  OE1 GLN A 817     -46.207  19.519  42.734  1.00 62.24           O  
ATOM   1948  NE2 GLN A 817     -46.026  21.005  41.055  1.00 55.76           N  
ATOM   1949  N   VAL A 818     -43.152  22.258  46.309  1.00 63.61           N  
ATOM   1950  CA  VAL A 818     -41.866  22.768  46.793  1.00 62.22           C  
ATOM   1951  C   VAL A 818     -40.944  21.594  47.114  1.00 60.10           C  
ATOM   1952  O   VAL A 818     -39.745  21.623  46.797  1.00 56.77           O  
ATOM   1953  CB  VAL A 818     -42.013  23.683  48.040  1.00 62.26           C  
ATOM   1954  CG1 VAL A 818     -40.648  24.112  48.531  1.00 57.72           C  
ATOM   1955  CG2 VAL A 818     -42.861  24.908  47.725  1.00 59.12           C  
ATOM   1956  N   GLY A 819     -41.521  20.556  47.719  1.00 55.33           N  
ATOM   1957  CA  GLY A 819     -40.804  19.323  47.985  1.00 56.67           C  
ATOM   1958  C   GLY A 819     -40.257  18.687  46.724  1.00 59.12           C  
ATOM   1959  O   GLY A 819     -39.094  18.301  46.650  1.00 57.74           O  
ATOM   1960  N   PHE A 820     -41.109  18.598  45.714  1.00 60.74           N  
ATOM   1961  CA  PHE A 820     -40.742  18.042  44.419  1.00 59.31           C  
ATOM   1962  C   PHE A 820     -39.613  18.854  43.770  1.00 58.14           C  
ATOM   1963  O   PHE A 820     -38.627  18.303  43.274  1.00 56.60           O  
ATOM   1964  CB  PHE A 820     -42.013  17.982  43.567  1.00 61.67           C  
ATOM   1965  CG  PHE A 820     -41.785  17.723  42.130  1.00 61.78           C  
ATOM   1966  CD1 PHE A 820     -41.092  16.605  41.713  1.00 66.23           C  
ATOM   1967  CD2 PHE A 820     -42.309  18.582  41.182  1.00 61.19           C  
ATOM   1968  CE1 PHE A 820     -40.902  16.361  40.371  1.00 64.90           C  
ATOM   1969  CE2 PHE A 820     -42.129  18.349  39.841  1.00 60.06           C  
ATOM   1970  CZ  PHE A 820     -41.424  17.237  39.430  1.00 62.74           C  
ATOM   1971  N   ILE A 821     -39.730  20.172  43.805  1.00 56.88           N  
ATOM   1972  CA  ILE A 821     -38.689  21.010  43.220  1.00 58.49           C  
ATOM   1973  C   ILE A 821     -37.362  20.843  43.947  1.00 60.27           C  
ATOM   1974  O   ILE A 821     -36.312  20.693  43.309  1.00 59.62           O  
ATOM   1975  CB  ILE A 821     -39.080  22.489  43.252  1.00 57.69           C  
ATOM   1976  CG1 ILE A 821     -40.376  22.711  42.479  1.00 58.39           C  
ATOM   1977  CG2 ILE A 821     -37.958  23.366  42.713  1.00 54.10           C  
ATOM   1978  CD1 ILE A 821     -40.790  24.159  42.436  1.00 62.45           C  
ATOM   1979  N   ASP A 822     -37.411  20.875  45.280  1.00 55.56           N  
ATOM   1980  CA  ASP A 822     -36.205  20.712  46.093  1.00 59.35           C  
ATOM   1981  C   ASP A 822     -35.512  19.371  45.917  1.00 58.84           C  
ATOM   1982  O   ASP A 822     -34.302  19.312  45.714  1.00 58.93           O  
ATOM   1983  CB  ASP A 822     -36.524  20.894  47.572  1.00 61.91           C  
ATOM   1984  CG  ASP A 822     -36.660  22.347  47.953  1.00 69.29           C  
ATOM   1985  OD1 ASP A 822     -36.300  23.203  47.099  1.00 62.91           O  
ATOM   1986  OD2 ASP A 822     -37.118  22.622  49.094  1.00 70.70           O  
ATOM   1987  N   ALA A 823     -36.299  18.306  46.007  1.00 53.63           N  
ATOM   1988  CA  ALA A 823     -35.797  16.947  45.964  1.00 51.15           C  
ATOM   1989  C   ALA A 823     -35.239  16.581  44.598  1.00 59.62           C  
ATOM   1990  O   ALA A 823     -34.204  15.925  44.501  1.00 64.24           O  
ATOM   1991  CB  ALA A 823     -36.906  15.978  46.338  1.00 51.17           C  
ATOM   1992  N   ILE A 824     -35.921  17.014  43.545  1.00 55.32           N  
ATOM   1993  CA  ILE A 824     -35.697  16.447  42.226  1.00 56.65           C  
ATOM   1994  C   ILE A 824     -35.190  17.467  41.210  1.00 61.27           C  
ATOM   1995  O   ILE A 824     -34.144  17.270  40.590  1.00 66.44           O  
ATOM   1996  CB  ILE A 824     -37.008  15.797  41.686  1.00 58.92           C  
ATOM   1997  CG1 ILE A 824     -37.487  14.680  42.617  1.00 55.61           C  
ATOM   1998  CG2 ILE A 824     -36.826  15.286  40.272  1.00 53.53           C  
ATOM   1999  N   CYS A 825     -35.920  18.564  41.053  1.00 56.20           N  
ATOM   2000  CA  CYS A 825     -35.738  19.414  39.885  1.00 56.26           C  
ATOM   2001  C   CYS A 825     -34.592  20.426  39.921  1.00 57.80           C  
ATOM   2002  O   CYS A 825     -33.846  20.525  38.941  1.00 57.08           O  
ATOM   2003  CB  CYS A 825     -37.048  20.115  39.543  1.00 60.02           C  
ATOM   2004  SG  CYS A 825     -38.449  19.005  39.621  1.00 63.79           S  
ATOM   2005  N   LEU A 826     -34.450  21.179  41.014  1.00 54.09           N  
ATOM   2006  CA  LEU A 826     -33.452  22.257  41.042  1.00 57.88           C  
ATOM   2007  C   LEU A 826     -32.030  21.782  40.735  1.00 61.33           C  
ATOM   2008  O   LEU A 826     -31.355  22.352  39.870  1.00 57.98           O  
ATOM   2009  CB  LEU A 826     -33.484  23.058  42.356  1.00 62.42           C  
ATOM   2010  CG  LEU A 826     -34.257  24.390  42.381  1.00 55.00           C  
ATOM   2011  N   GLN A 827     -31.577  20.738  41.425  1.00 61.64           N  
ATOM   2012  CA  GLN A 827     -30.221  20.243  41.197  1.00 65.33           C  
ATOM   2013  C   GLN A 827     -30.013  19.835  39.738  1.00 64.43           C  
ATOM   2014  O   GLN A 827     -29.001  20.170  39.110  1.00 63.62           O  
ATOM   2015  CB  GLN A 827     -29.902  19.080  42.129  1.00 68.27           C  
ATOM   2016  CG  GLN A 827     -29.551  19.518  43.541  1.00 75.41           C  
ATOM   2017  CD  GLN A 827     -29.294  18.341  44.475  1.00 84.15           C  
ATOM   2018  OE1 GLN A 827     -30.217  17.582  44.812  1.00 82.86           O  
ATOM   2019  NE2 GLN A 827     -28.033  18.177  44.892  1.00 74.78           N  
ATOM   2020  N   LEU A 828     -30.986  19.121  39.196  1.00 59.16           N  
ATOM   2021  CA  LEU A 828     -30.885  18.683  37.832  1.00 57.40           C  
ATOM   2022  C   LEU A 828     -30.692  19.871  36.897  1.00 58.84           C  
ATOM   2023  O   LEU A 828     -29.743  19.884  36.118  1.00 58.85           O  
ATOM   2024  CB  LEU A 828     -32.114  17.869  37.441  1.00 61.57           C  
ATOM   2025  CG  LEU A 828     -32.157  17.425  35.978  1.00 55.61           C  
ATOM   2026  CD1 LEU A 828     -31.030  16.443  35.721  1.00 59.29           C  
ATOM   2027  CD2 LEU A 828     -33.508  16.813  35.644  1.00 53.45           C  
ATOM   2028  N   TYR A 829     -31.569  20.873  36.973  1.00 56.19           N  
ATOM   2029  CA  TYR A 829     -31.468  21.997  36.042  1.00 55.92           C  
ATOM   2030  C   TYR A 829     -30.247  22.883  36.295  1.00 60.01           C  
ATOM   2031  O   TYR A 829     -29.759  23.567  35.396  1.00 59.54           O  
ATOM   2032  CB  TYR A 829     -32.744  22.825  36.013  1.00 52.14           C  
ATOM   2033  CG  TYR A 829     -33.929  22.057  35.502  1.00 53.81           C  
ATOM   2034  CD1 TYR A 829     -34.974  21.714  36.350  1.00 47.22           C  
ATOM   2035  CD2 TYR A 829     -34.000  21.655  34.161  1.00 51.57           C  
ATOM   2036  CE1 TYR A 829     -36.060  21.006  35.882  1.00 52.30           C  
ATOM   2037  CE2 TYR A 829     -35.091  20.941  33.680  1.00 45.50           C  
ATOM   2038  CZ  TYR A 829     -36.120  20.620  34.542  1.00 48.41           C  
ATOM   2039  OH  TYR A 829     -37.204  19.906  34.089  1.00 43.76           O  
ATOM   2040  N   GLU A 830     -29.757  22.871  37.526  1.00 64.06           N  
ATOM   2041  CA  GLU A 830     -28.461  23.462  37.811  1.00 65.43           C  
ATOM   2042  C   GLU A 830     -27.388  22.709  37.025  1.00 66.57           C  
ATOM   2043  O   GLU A 830     -26.687  23.294  36.200  1.00 66.72           O  
ATOM   2044  CB  GLU A 830     -28.172  23.436  39.310  1.00 62.98           C  
ATOM   2045  CG  GLU A 830     -28.356  24.791  39.969  1.00 68.69           C  
ATOM   2046  CD  GLU A 830     -28.744  24.702  41.442  1.00 76.24           C  
ATOM   2047  OE1 GLU A 830     -29.482  25.607  41.903  1.00 78.89           O  
ATOM   2048  OE2 GLU A 830     -28.321  23.739  42.133  1.00 72.94           O  
ATOM   2049  N   ALA A 831     -27.281  21.407  37.265  1.00 61.78           N  
ATOM   2050  CA  ALA A 831     -26.335  20.578  36.527  1.00 63.23           C  
ATOM   2051  C   ALA A 831     -26.406  20.805  35.015  1.00 64.68           C  
ATOM   2052  O   ALA A 831     -25.401  21.131  34.384  1.00 64.05           O  
ATOM   2053  CB  ALA A 831     -26.557  19.113  36.858  1.00 64.39           C  
ATOM   2054  N   LEU A 832     -27.601  20.638  34.447  1.00 64.76           N  
ATOM   2055  CA  LEU A 832     -27.824  20.842  33.016  1.00 64.68           C  
ATOM   2056  C   LEU A 832     -27.344  22.217  32.553  1.00 65.62           C  
ATOM   2057  O   LEU A 832     -26.916  22.403  31.410  1.00 68.31           O  
ATOM   2058  CB  LEU A 832     -29.305  20.644  32.660  1.00 62.01           C  
ATOM   2059  CG  LEU A 832     -29.738  21.137  31.264  1.00 65.09           C  
ATOM   2060  CD1 LEU A 832     -28.987  20.401  30.166  1.00 63.95           C  
ATOM   2061  CD2 LEU A 832     -31.244  21.027  31.028  1.00 55.92           C  
ATOM   2062  N   THR A 833     -27.418  23.187  33.446  1.00 66.81           N  
ATOM   2063  CA  THR A 833     -27.014  24.541  33.098  1.00 71.88           C  
ATOM   2064  C   THR A 833     -25.490  24.672  33.044  1.00 70.69           C  
ATOM   2065  O   THR A 833     -24.956  25.474  32.284  1.00 71.24           O  
ATOM   2066  CB  THR A 833     -27.646  25.569  34.061  1.00 69.03           C  
ATOM   2067  OG1 THR A 833     -28.989  25.839  33.636  1.00 68.92           O  
ATOM   2068  CG2 THR A 833     -26.862  26.859  34.063  1.00 68.17           C  
ATOM   2069  N   HIS A 834     -24.798  23.866  33.841  1.00 68.74           N  
ATOM   2070  CA  HIS A 834     -23.347  23.814  33.786  1.00 72.71           C  
ATOM   2071  C   HIS A 834     -22.887  23.208  32.468  1.00 74.87           C  
ATOM   2072  O   HIS A 834     -22.029  23.757  31.789  1.00 78.13           O  
ATOM   2073  CB  HIS A 834     -22.780  23.031  34.971  1.00 77.02           C  
ATOM   2074  CG  HIS A 834     -22.751  23.816  36.247  1.00 88.60           C  
ATOM   2075  ND1 HIS A 834     -21.817  24.801  36.494  1.00 94.34           N  
ATOM   2076  CD2 HIS A 834     -23.548  23.772  37.343  1.00 89.33           C  
ATOM   2077  CE1 HIS A 834     -22.036  25.323  37.689  1.00 98.31           C  
ATOM   2078  NE2 HIS A 834     -23.080  24.716  38.225  1.00 94.69           N  
ATOM   2079  N   VAL A 835     -23.463  22.075  32.100  1.00 73.74           N  
ATOM   2080  CA  VAL A 835     -23.212  21.518  30.784  1.00 70.46           C  
ATOM   2081  C   VAL A 835     -23.477  22.545  29.674  1.00 76.58           C  
ATOM   2082  O   VAL A 835     -22.613  22.783  28.825  1.00 75.27           O  
ATOM   2083  CB  VAL A 835     -24.060  20.272  30.563  1.00 70.90           C  
ATOM   2084  CG1 VAL A 835     -23.956  19.800  29.124  1.00 73.32           C  
ATOM   2085  CG2 VAL A 835     -23.606  19.195  31.513  1.00 73.20           C  
ATOM   2086  N   SER A 836     -24.667  23.150  29.675  1.00 75.30           N  
ATOM   2087  CA  SER A 836     -24.973  24.205  28.706  1.00 75.90           C  
ATOM   2088  C   SER A 836     -25.604  25.445  29.335  1.00 76.09           C  
ATOM   2089  O   SER A 836     -26.720  25.407  29.869  1.00 74.96           O  
ATOM   2090  CB  SER A 836     -25.847  23.696  27.551  1.00 77.23           C  
ATOM   2091  OG  SER A 836     -26.027  24.722  26.579  1.00 73.89           O  
ATOM   2092  N   GLU A 837     -24.873  26.547  29.244  1.00 74.23           N  
ATOM   2093  CA  GLU A 837     -25.317  27.817  29.783  1.00 74.30           C  
ATOM   2094  C   GLU A 837     -26.620  28.289  29.155  1.00 72.62           C  
ATOM   2095  O   GLU A 837     -27.274  29.185  29.683  1.00 71.50           O  
ATOM   2096  CB  GLU A 837     -24.233  28.880  29.580  1.00 77.50           C  
ATOM   2097  N   ASP A 838     -27.010  27.700  28.032  1.00 71.24           N  
ATOM   2098  CA  ASP A 838     -28.203  28.198  27.352  1.00 70.37           C  
ATOM   2099  C   ASP A 838     -29.484  27.496  27.780  1.00 71.32           C  
ATOM   2100  O   ASP A 838     -30.558  27.815  27.284  1.00 67.94           O  
ATOM   2101  CB  ASP A 838     -28.026  28.147  25.845  1.00 72.31           C  
ATOM   2102  CG  ASP A 838     -26.807  28.930  25.387  1.00 83.08           C  
ATOM   2103  OD1 ASP A 838     -26.988  29.998  24.748  1.00 82.34           O  
ATOM   2104  OD2 ASP A 838     -25.671  28.484  25.691  1.00 82.86           O  
ATOM   2105  N   CYS A 839     -29.358  26.547  28.707  1.00 71.26           N  
ATOM   2106  CA  CYS A 839     -30.511  25.882  29.302  1.00 64.71           C  
ATOM   2107  C   CYS A 839     -30.835  26.557  30.611  1.00 65.43           C  
ATOM   2108  O   CYS A 839     -31.617  26.046  31.410  1.00 66.94           O  
ATOM   2109  CB  CYS A 839     -30.214  24.405  29.561  1.00 63.99           C  
ATOM   2110  SG  CYS A 839     -29.834  23.457  28.094  1.00 67.69           S  
ATOM   2111  N   PHE A 840     -30.201  27.696  30.849  1.00 65.48           N  
ATOM   2112  CA  PHE A 840     -30.452  28.442  32.066  1.00 65.70           C  
ATOM   2113  C   PHE A 840     -31.933  28.793  32.210  1.00 63.59           C  
ATOM   2114  O   PHE A 840     -32.490  28.716  33.301  1.00 62.54           O  
ATOM   2115  CB  PHE A 840     -29.600  29.705  32.102  1.00 67.78           C  
ATOM   2116  CG  PHE A 840     -30.014  30.662  33.162  1.00 68.20           C  
ATOM   2117  CD1 PHE A 840     -29.672  30.432  34.493  1.00 68.31           C  
ATOM   2118  CD2 PHE A 840     -30.771  31.782  32.842  1.00 68.57           C  
ATOM   2119  CE1 PHE A 840     -30.075  31.308  35.496  1.00 64.32           C  
ATOM   2120  CE2 PHE A 840     -31.174  32.663  33.832  1.00 71.12           C  
ATOM   2121  CZ  PHE A 840     -30.827  32.423  35.164  1.00 67.38           C  
ATOM   2122  N   PRO A 841     -32.576  29.177  31.099  1.00 60.55           N  
ATOM   2123  CA  PRO A 841     -34.008  29.473  31.098  1.00 61.20           C  
ATOM   2124  C   PRO A 841     -34.853  28.405  31.761  1.00 61.81           C  
ATOM   2125  O   PRO A 841     -35.986  28.707  32.131  1.00 66.65           O  
ATOM   2126  CB  PRO A 841     -34.343  29.537  29.614  1.00 62.63           C  
ATOM   2127  CG  PRO A 841     -33.122  30.058  28.996  1.00 60.32           C  
ATOM   2128  CD  PRO A 841     -31.964  29.493  29.801  1.00 63.62           C  
ATOM   2129  N   LEU A 842     -34.334  27.192  31.907  1.00 59.85           N  
ATOM   2130  CA  LEU A 842     -35.094  26.134  32.565  1.00 57.90           C  
ATOM   2131  C   LEU A 842     -34.892  26.240  34.052  1.00 57.96           C  
ATOM   2132  O   LEU A 842     -35.833  26.087  34.823  1.00 60.14           O  
ATOM   2133  CB  LEU A 842     -34.683  24.746  32.073  1.00 54.94           C  
ATOM   2134  CG  LEU A 842     -35.156  24.363  30.664  1.00 57.19           C  
ATOM   2135  CD1 LEU A 842     -34.297  23.255  30.061  1.00 58.65           C  
ATOM   2136  CD2 LEU A 842     -36.605  23.948  30.673  1.00 53.72           C  
ATOM   2137  N   LEU A 843     -33.655  26.502  34.450  1.00 58.23           N  
ATOM   2138  CA  LEU A 843     -33.319  26.668  35.850  1.00 57.41           C  
ATOM   2139  C   LEU A 843     -34.066  27.876  36.387  1.00 62.70           C  
ATOM   2140  O   LEU A 843     -34.652  27.843  37.474  1.00 60.05           O  
ATOM   2141  CB  LEU A 843     -31.824  26.895  35.990  1.00 58.27           C  
ATOM   2142  CG  LEU A 843     -31.316  27.216  37.396  1.00 62.45           C  
ATOM   2143  CD1 LEU A 843     -31.801  26.205  38.436  1.00 57.45           C  
ATOM   2144  CD2 LEU A 843     -29.796  27.291  37.378  1.00 62.64           C  
ATOM   2145  N   ASP A 844     -34.039  28.940  35.596  1.00 60.76           N  
ATOM   2146  CA  ASP A 844     -34.733  30.167  35.913  1.00 61.18           C  
ATOM   2147  C   ASP A 844     -36.222  29.922  36.123  1.00 61.35           C  
ATOM   2148  O   ASP A 844     -36.777  30.270  37.167  1.00 60.26           O  
ATOM   2149  CB  ASP A 844     -34.515  31.174  34.783  1.00 67.85           C  
ATOM   2150  CG  ASP A 844     -34.839  32.604  35.195  1.00 72.77           C  
ATOM   2151  OD1 ASP A 844     -34.582  32.987  36.365  1.00 71.38           O  
ATOM   2152  OD2 ASP A 844     -35.360  33.346  34.336  1.00 77.67           O  
ATOM   2153  N   GLY A 845     -36.868  29.322  35.131  1.00 59.05           N  
ATOM   2154  CA  GLY A 845     -38.282  29.020  35.234  1.00 56.15           C  
ATOM   2155  C   GLY A 845     -38.614  28.248  36.493  1.00 56.61           C  
ATOM   2156  O   GLY A 845     -39.600  28.526  37.174  1.00 57.02           O  
ATOM   2157  N   CYS A 846     -37.776  27.270  36.801  1.00 56.22           N  
ATOM   2158  CA  CYS A 846     -38.006  26.379  37.932  1.00 56.83           C  
ATOM   2159  C   CYS A 846     -37.886  27.154  39.242  1.00 56.96           C  
ATOM   2160  O   CYS A 846     -38.598  26.895  40.204  1.00 59.48           O  
ATOM   2161  CB  CYS A 846     -37.000  25.212  37.882  1.00 54.54           C  
ATOM   2162  SG  CYS A 846     -37.132  23.980  39.207  1.00 57.05           S  
ATOM   2163  N   ARG A 847     -36.972  28.112  39.276  1.00 60.93           N  
ATOM   2164  CA  ARG A 847     -36.790  28.942  40.464  1.00 60.59           C  
ATOM   2165  C   ARG A 847     -37.977  29.852  40.683  1.00 58.52           C  
ATOM   2166  O   ARG A 847     -38.521  29.903  41.781  1.00 60.89           O  
ATOM   2167  CB  ARG A 847     -35.523  29.772  40.350  1.00 55.45           C  
ATOM   2168  CG  ARG A 847     -34.298  28.979  40.663  1.00 57.97           C  
ATOM   2169  CD  ARG A 847     -33.087  29.690  40.153  1.00 59.24           C  
ATOM   2170  NE  ARG A 847     -31.852  29.107  40.664  1.00 65.29           N  
ATOM   2171  CZ  ARG A 847     -30.645  29.543  40.319  1.00 65.48           C  
ATOM   2172  NH1 ARG A 847     -30.544  30.557  39.458  1.00 52.17           N  
ATOM   2173  NH2 ARG A 847     -29.555  28.961  40.817  1.00 61.55           N  
ATOM   2174  N   LYS A 848     -38.376  30.574  39.641  1.00 56.54           N  
ATOM   2175  CA  LYS A 848     -39.571  31.391  39.736  1.00 57.47           C  
ATOM   2176  C   LYS A 848     -40.742  30.565  40.272  1.00 60.67           C  
ATOM   2177  O   LYS A 848     -41.463  31.000  41.168  1.00 64.36           O  
ATOM   2178  CB  LYS A 848     -39.905  32.053  38.397  1.00 55.29           C  
ATOM   2179  CG  LYS A 848     -38.898  33.116  38.005  1.00 56.45           C  
ATOM   2180  CD  LYS A 848     -39.134  33.693  36.619  1.00 60.46           C  
ATOM   2181  CE  LYS A 848     -38.003  34.679  36.283  1.00 70.99           C  
ATOM   2182  NZ  LYS A 848     -38.007  35.208  34.884  1.00 68.60           N  
ATOM   2183  N   ASN A 849     -40.912  29.356  39.763  1.00 59.62           N  
ATOM   2184  CA  ASN A 849     -42.036  28.548  40.213  1.00 61.07           C  
ATOM   2185  C   ASN A 849     -41.927  28.141  41.656  1.00 58.80           C  
ATOM   2186  O   ASN A 849     -42.935  27.885  42.299  1.00 60.44           O  
ATOM   2187  CB  ASN A 849     -42.225  27.317  39.339  1.00 59.83           C  
ATOM   2188  CG  ASN A 849     -42.932  27.637  38.054  1.00 60.33           C  
ATOM   2189  OD1 ASN A 849     -43.832  28.481  38.034  1.00 61.42           O  
ATOM   2190  ND2 ASN A 849     -42.529  26.975  36.964  1.00 56.43           N  
ATOM   2191  N   ARG A 850     -40.706  28.056  42.163  1.00 59.47           N  
ATOM   2192  CA  ARG A 850     -40.516  27.685  43.559  1.00 60.95           C  
ATOM   2193  C   ARG A 850     -40.980  28.861  44.418  1.00 62.00           C  
ATOM   2194  O   ARG A 850     -41.686  28.683  45.421  1.00 58.61           O  
ATOM   2195  CB  ARG A 850     -39.053  27.325  43.850  1.00 56.82           C  
ATOM   2196  CG  ARG A 850     -38.875  26.582  45.159  1.00 55.79           C  
ATOM   2197  CD  ARG A 850     -37.448  26.660  45.721  1.00 55.69           C  
ATOM   2198  NE  ARG A 850     -37.355  25.968  47.012  1.00 60.69           N  
ATOM   2199  CZ  ARG A 850     -37.711  26.486  48.193  1.00 62.62           C  
ATOM   2200  NH1 ARG A 850     -37.590  25.762  49.304  1.00 60.23           N  
ATOM   2201  NH2 ARG A 850     -38.179  27.726  48.274  1.00 62.47           N  
ATOM   2202  N   GLN A 851     -40.603  30.068  43.998  1.00 59.87           N  
ATOM   2203  CA  GLN A 851     -41.066  31.271  44.675  1.00 61.87           C  
ATOM   2204  C   GLN A 851     -42.600  31.270  44.762  1.00 62.75           C  
ATOM   2205  O   GLN A 851     -43.173  31.365  45.846  1.00 64.55           O  
ATOM   2206  CB  GLN A 851     -40.532  32.528  43.976  1.00 60.90           C  
ATOM   2207  CG  GLN A 851     -40.999  33.836  44.618  1.00 66.95           C  
ATOM   2208  N   LYS A 852     -43.253  31.127  43.616  1.00 60.00           N  
ATOM   2209  CA  LYS A 852     -44.703  31.044  43.553  1.00 60.00           C  
ATOM   2210  C   LYS A 852     -45.351  30.003  44.472  1.00 62.64           C  
ATOM   2211  O   LYS A 852     -46.343  30.305  45.128  1.00 67.54           O  
ATOM   2212  CB  LYS A 852     -45.143  30.792  42.114  1.00 63.61           C  
ATOM   2213  CG  LYS A 852     -44.719  31.872  41.164  1.00 64.62           C  
ATOM   2214  CD  LYS A 852     -45.373  33.187  41.546  1.00 69.12           C  
ATOM   2215  CE  LYS A 852     -45.335  34.199  40.401  1.00 70.71           C  
ATOM   2216  NZ  LYS A 852     -45.996  35.477  40.784  1.00 67.86           N  
ATOM   2217  N   TRP A 853     -44.822  28.781  44.507  1.00 62.63           N  
ATOM   2218  CA  TRP A 853     -45.451  27.713  45.283  1.00 61.07           C  
ATOM   2219  C   TRP A 853     -45.216  27.861  46.782  1.00 62.93           C  
ATOM   2220  O   TRP A 853     -46.092  27.549  47.595  1.00 61.68           O  
ATOM   2221  CB  TRP A 853     -44.971  26.336  44.827  1.00 60.08           C  
ATOM   2222  CG  TRP A 853     -45.584  25.834  43.545  1.00 61.29           C  
ATOM   2223  CD1 TRP A 853     -44.924  25.547  42.387  1.00 60.73           C  
ATOM   2224  CD2 TRP A 853     -46.970  25.542  43.294  1.00 62.56           C  
ATOM   2225  NE1 TRP A 853     -45.807  25.099  41.431  1.00 60.19           N  
ATOM   2226  CE2 TRP A 853     -47.069  25.087  41.960  1.00 59.95           C  
ATOM   2227  CE3 TRP A 853     -48.136  25.624  44.064  1.00 62.14           C  
ATOM   2228  CZ2 TRP A 853     -48.285  24.715  41.380  1.00 60.30           C  
ATOM   2229  CZ3 TRP A 853     -49.345  25.252  43.484  1.00 63.75           C  
ATOM   2230  CH2 TRP A 853     -49.408  24.802  42.156  1.00 60.59           C  
ATOM   2231  N   GLN A 854     -44.017  28.321  47.131  1.00 66.11           N  
ATOM   2232  CA  GLN A 854     -43.614  28.557  48.518  1.00 66.30           C  
ATOM   2233  C   GLN A 854     -44.524  29.597  49.162  1.00 70.74           C  
ATOM   2234  O   GLN A 854     -45.113  29.360  50.229  1.00 69.57           O  
ATOM   2235  CB  GLN A 854     -42.150  29.027  48.552  1.00 59.99           C  
ATOM   2236  CG  GLN A 854     -41.623  29.432  49.914  1.00 64.21           C  
ATOM   2237  CD  GLN A 854     -41.791  28.353  50.982  1.00 71.40           C  
ATOM   2238  OE1 GLN A 854     -41.962  27.168  50.686  1.00 65.10           O  
ATOM   2239  NE2 GLN A 854     -41.742  28.773  52.244  1.00 76.07           N  
ATOM   2240  N   ALA A 855     -44.631  30.744  48.490  1.00 68.14           N  
ATOM   2241  CA  ALA A 855     -45.541  31.820  48.874  1.00 68.97           C  
ATOM   2242  C   ALA A 855     -46.960  31.308  49.150  1.00 71.22           C  
ATOM   2243  O   ALA A 855     -47.560  31.624  50.178  1.00 75.79           O  
ATOM   2244  CB  ALA A 855     -45.562  32.873  47.804  1.00 55.27           C  
ATOM   2245  N   LEU A 856     -47.494  30.521  48.227  1.00 65.07           N  
ATOM   2246  CA  LEU A 856     -48.773  29.869  48.442  1.00 67.73           C  
ATOM   2247  C   LEU A 856     -48.797  28.947  49.667  1.00 70.06           C  
ATOM   2248  O   LEU A 856     -49.768  28.943  50.417  1.00 71.78           O  
ATOM   2249  CB  LEU A 856     -49.172  29.079  47.196  1.00 66.97           C  
ATOM   2250  CG  LEU A 856     -49.823  29.864  46.058  1.00 68.85           C  
ATOM   2251  CD1 LEU A 856     -49.953  28.991  44.818  1.00 65.39           C  
ATOM   2252  CD2 LEU A 856     -51.191  30.428  46.478  1.00 63.20           C  
ATOM   2253  N   ALA A 857     -47.747  28.149  49.854  1.00 66.28           N  
ATOM   2254  CA  ALA A 857     -47.731  27.173  50.938  1.00 72.56           C  
ATOM   2255  C   ALA A 857     -47.698  27.880  52.293  1.00 78.66           C  
ATOM   2256  O   ALA A 857     -48.047  27.306  53.332  1.00 78.19           O  
ATOM   2257  CB  ALA A 857     -46.546  26.214  50.794  1.00 66.49           C  
ATOM   2258  N   GLU A 858     -47.277  29.137  52.258  1.00 78.13           N  
ATOM   2259  CA  GLU A 858     -47.183  29.967  53.447  1.00 82.10           C  
ATOM   2260  C   GLU A 858     -48.505  30.670  53.750  1.00 81.81           C  
ATOM   2261  O   GLU A 858     -48.804  30.975  54.908  1.00 84.67           O  
ATOM   2262  CB  GLU A 858     -46.075  31.005  53.276  1.00 78.40           C  
ATOM   2263  CG  GLU A 858     -44.671  30.466  53.438  1.00 71.63           C  
ATOM   2264  CD  GLU A 858     -43.630  31.539  53.179  1.00 82.92           C  
ATOM   2265  OE1 GLU A 858     -44.024  32.691  52.885  1.00 87.41           O  
ATOM   2266  OE2 GLU A 858     -42.418  31.242  53.258  1.00 87.63           O  
ATOM   2267  N   GLN A 859     -49.280  30.951  52.708  1.00 77.51           N  
ATOM   2268  CA  GLN A 859     -50.626  31.463  52.901  1.00 78.90           C  
ATOM   2269  C   GLN A 859     -51.478  30.345  53.516  1.00 81.25           C  
ATOM   2270  O   GLN A 859     -52.569  30.589  54.024  1.00 84.26           O  
ATOM   2271  CB  GLN A 859     -51.227  31.979  51.584  1.00 75.55           C  
ATOM   2272  N   GLN A 860     -50.962  29.118  53.483  1.00 80.56           N  
ATOM   2273  CA  GLN A 860     -51.645  27.986  54.111  1.00 84.49           C  
ATOM   2274  C   GLN A 860     -51.225  27.850  55.579  1.00 91.44           C  
ATOM   2275  O   GLN A 860     -51.038  28.850  56.286  1.00 88.17           O  
ATOM   2276  CB  GLN A 860     -51.370  26.676  53.351  1.00 84.61           C  
ATOM   2277  CG  GLN A 860     -52.199  26.472  52.062  1.00 86.72           C  
ATOM   2278  CD  GLN A 860     -53.600  25.924  52.332  1.00 84.18           C  
TER    2279      GLN A 860                                                      
HETATM 2280  CAA 5FO A   1     -49.506  19.057  42.213  1.00 66.95           C  
HETATM 2281  CAB 5FO A   1     -45.074  13.796  37.184  1.00 67.43           C  
HETATM 2282  CAC 5FO A   1     -45.396  10.564  41.879  1.00 93.11           C  
HETATM 2283  OAD 5FO A   1     -46.167  18.947  38.675  1.00 66.52           O  
HETATM 2284  OAE 5FO A   1     -42.874  13.966  45.972  1.00 85.39           O  
HETATM 2285  OAF 5FO A   1     -41.807  14.136  43.793  1.00 84.04           O  
HETATM 2286  FAG 5FO A   1     -45.016  17.241  36.823  1.00 75.09           F  
HETATM 2287  CAH 5FO A   1     -45.468  14.991  44.768  1.00 79.68           C  
HETATM 2288  CAI 5FO A   1     -46.483  15.806  44.277  1.00 78.36           C  
HETATM 2289  CAJ 5FO A   1     -44.405  15.074  42.632  1.00 74.46           C  
HETATM 2290  CAK 5FO A   1     -49.823  17.563  42.315  1.00 67.43           C  
HETATM 2291  CAL 5FO A   1     -43.965  14.677  37.776  1.00 69.43           C  
HETATM 2292  CAM 5FO A   1     -48.748  16.815  43.114  1.00 72.55           C  
HETATM 2293  CAN 5FO A   1     -43.146  10.255  42.539  1.00 99.60           C  
HETATM 2294  CAO 5FO A   1     -44.813  10.114  44.247  1.00100.43           C  
HETATM 2295  CAP 5FO A   1     -42.967  11.755  42.810  1.00 93.60           C  
HETATM 2296  CAQ 5FO A   1     -44.658  11.615  44.526  1.00 99.24           C  
HETATM 2297  NAR 5FO A   1     -44.731  15.454  39.953  1.00 73.74           N  
HETATM 2298  NAS 5FO A   1     -45.843  17.469  40.354  1.00 71.29           N  
HETATM 2299  OAT 5FO A   1     -47.459  17.037  42.465  1.00 73.84           O  
HETATM 2300  CAU 5FO A   1     -44.389  14.681  43.951  1.00 79.25           C  
HETATM 2301  CAV 5FO A   1     -46.452  16.264  42.961  1.00 74.44           C  
HETATM 2302  CAW 5FO A   1     -44.625  15.745  38.646  1.00 72.83           C  
HETATM 2303  CAX 5FO A   1     -45.123  16.953  38.149  1.00 72.30           C  
HETATM 2304  CAY 5FO A   1     -45.353  15.958  42.164  1.00 72.94           C  
HETATM 2305  CAZ 5FO A   1     -45.237  16.323  40.830  1.00 71.04           C  
HETATM 2306  CBA 5FO A   1     -45.714  17.853  39.031  1.00 67.67           C  
HETATM 2307  NBB 5FO A   1     -44.518   9.836  42.820  1.00101.84           N  
HETATM 2308  NBC 5FO A   1     -43.273  12.051  44.225  1.00100.46           N  
HETATM 2309  SBD 5FO A   1     -43.053  13.686  44.502  1.00 94.82           S  
HETATM 2310 ZN    ZN A 861     -43.081  11.191  31.566  1.00 67.10          ZN  
HETATM 2311 MG    MG A 862     -43.453   9.138  33.970  1.00 70.11          MG  
HETATM 2312 MG    MG A   2     -43.733  -1.922   5.311  1.00 79.39          MG  
HETATM 2313 MG    MG A   3     -58.501  18.457  18.617  1.00 78.02          MG  
HETATM 2314  O   HOH A   4     -38.331  31.020  26.471  1.00 63.06           O  
HETATM 2315  O   HOH A   5     -35.816   6.112   7.580  1.00 63.76           O  
HETATM 2316  O   HOH A   6     -57.441  -1.700  27.298  1.00 81.78           O  
HETATM 2317  O   HOH A   7     -57.345  17.863  15.513  1.00 68.22           O  
HETATM 2318  O   HOH A  10     -43.018  20.357  29.070  1.00 59.00           O  
HETATM 2319  O   HOH A  11     -42.076   7.003  33.358  1.00 65.79           O  
HETATM 2320  O   HOH A  16     -34.802  17.105   7.419  1.00 61.81           O  
HETATM 2321  O   HOH A  17     -44.385  29.270   8.400  1.00 58.70           O  
HETATM 2322  O   HOH A  24     -49.129  35.861  41.365  1.00 68.89           O  
HETATM 2323  O   HOH A 863     -32.320   9.726  34.439  1.00 58.32           O  
HETATM 2324  O   HOH A 864     -43.636  11.763  34.214  1.00 57.93           O  
HETATM 2325  O   HOH A 865     -46.655   9.441  46.275  1.00 92.45           O  
CONECT  642 2310                                                                
CONECT  905 2310                                                                
CONECT  913 2310                                                                
CONECT 1684 2310                                                                
CONECT 2280 2290                                                                
CONECT 2281 2291                                                                
CONECT 2282 2307                                                                
CONECT 2283 2306                                                                
CONECT 2284 2309                                                                
CONECT 2285 2309                                                                
CONECT 2286 2303                                                                
CONECT 2287 2288 2300                                                           
CONECT 2288 2287 2301                                                           
CONECT 2289 2300 2304                                                           
CONECT 2290 2280 2292                                                           
CONECT 2291 2281 2302                                                           
CONECT 2292 2290 2299                                                           
CONECT 2293 2295 2307                                                           
CONECT 2294 2296 2307                                                           
CONECT 2295 2293 2308                                                           
CONECT 2296 2294 2308                                                           
CONECT 2297 2302 2305                                                           
CONECT 2298 2305 2306                                                           
CONECT 2299 2292 2301                                                           
CONECT 2300 2287 2289 2309                                                      
CONECT 2301 2288 2299 2304                                                      
CONECT 2302 2291 2297 2303                                                      
CONECT 2303 2286 2302 2306                                                      
CONECT 2304 2289 2301 2305                                                      
CONECT 2305 2297 2298 2304                                                      
CONECT 2306 2283 2298 2303                                                      
CONECT 2307 2282 2293 2294                                                      
CONECT 2308 2295 2296 2309                                                      
CONECT 2309 2284 2285 2300 2308                                                 
CONECT 2310  642  905  913 1684                                                 
CONECT 2311 2319 2324                                                           
CONECT 2319 2311                                                                
CONECT 2324 2311                                                                
MASTER      374    0    5   17    0    0    7    6 2324    1   38   27          
END