HEADER    OXIDOREDUCTASE                          23-JUL-14   4U4I              
TITLE     MEGAVIRUS CHILENSIS SUPEROXIDE DISMUTASE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CU/ZN SUPEROXIDE DISMUTASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: THE LOOPS INVOLVED IN COPPER AND ZINC BINDING ARE     
COMPND   8 DISRDERED IN THE CRYSTAL STRUCTURE                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MEGAVIRUS CHILIENSIS;                           
SOURCE   3 ORGANISM_TAXID: 1094892;                                             
SOURCE   4 GENE: MG277;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: ROSETTA;                                  
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: MODIFIED PETDUET                          
KEYWDS    CU-ZN SUPEROXIDE DISMUTASE, METAL-FREE, OXIDOREDUCTASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LARTIGUE,J.-M.CLAVERIE,B.BURLAT,B.COUTARD,C.ABERGEL                 
REVDAT   3   24-DEC-14 4U4I    1       JRNL                                     
REVDAT   2   12-NOV-14 4U4I    1       JRNL                                     
REVDAT   1   05-NOV-14 4U4I    0                                                
JRNL        AUTH   A.LARTIGUE,B.BURLAT,B.COUTARD,F.CHASPOUL,J.M.CLAVERIE,       
JRNL        AUTH 2 C.ABERGEL                                                    
JRNL        TITL   THE MEGAVIRUS CHILENSIS CU,ZN-SUPEROXIDE DISMUTASE: THE      
JRNL        TITL 2 FIRST VIRAL STRUCTURE OF A TYPICAL CELLULAR COPPER           
JRNL        TITL 3 CHAPERONE-INDEPENDENT HYPERSTABLE DIMERIC ENZYME.            
JRNL        REF    J.VIROL.                      V.  89   824 2015              
JRNL        REFN                   ESSN 1098-5514                               
JRNL        PMID   25355875                                                     
JRNL        DOI    10.1128/JVI.02588-14                                         
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.LARTIGUE,N.PHILIPPE,S.JEUDY,C.ABERGEL                      
REMARK   1  TITL   PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF THE MEGAVIRUS       
REMARK   1  TITL 2 SUPEROXIDE DISMUTASE.                                        
REMARK   1  REF    ACTA CRYSTALLOGR. SECT. F     V.  68  1557 2012              
REMARK   1  REF  2 STRUCT. BIOL. CRYST. COMMUN.                                 
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   23192047                                                     
REMARK   1  DOI    10.1107/S174430911204657X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.04                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 15726                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1573                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.0461 -  4.8897    1.00     1415   157  0.2028 0.2314        
REMARK   3     2  4.8897 -  3.8823    1.00     1323   147  0.1642 0.1884        
REMARK   3     3  3.8823 -  3.3919    1.00     1293   144  0.1763 0.1934        
REMARK   3     4  3.3919 -  3.0820    1.00     1283   142  0.1775 0.2320        
REMARK   3     5  3.0820 -  2.8611    1.00     1270   142  0.1882 0.2638        
REMARK   3     6  2.8611 -  2.6925    1.00     1270   141  0.1948 0.2614        
REMARK   3     7  2.6925 -  2.5577    1.00     1270   141  0.2069 0.2717        
REMARK   3     8  2.5577 -  2.4464    1.00     1255   140  0.1948 0.2331        
REMARK   3     9  2.4464 -  2.3522    1.00     1255   139  0.1862 0.2201        
REMARK   3    10  2.3522 -  2.2710    1.00     1256   140  0.1886 0.2568        
REMARK   3    11  2.2710 -  2.2000    1.00     1263   140  0.2090 0.2767        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           1980                                  
REMARK   3   ANGLE     :  1.139           2671                                  
REMARK   3   CHIRALITY :  0.053            289                                  
REMARK   3   PLANARITY :  0.005            354                                  
REMARK   3   DIHEDRAL  : 14.254            719                                  
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 4U4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202784.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
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          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15785                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.90                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE BUFFER, 20%(W/V)    
REMARK 280  PEG 4000, 20%(V/V) MPD                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.71300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.31300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.31300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       88.06950            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.31300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.31300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.35650            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.31300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.31300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       88.06950            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.31300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.31300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       29.35650            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       58.71300            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     VAL A    78                                                      
REMARK 465     HIS A    79                                                      
REMARK 465     LYS A    80                                                      
REMARK 465     ASP A    81                                                      
REMARK 465     ILE A    82                                                      
REMARK 465     ASN A    83                                                      
REMARK 465     ILE A    84                                                      
REMARK 465     GLN A    85                                                      
REMARK 465     HIS A    86                                                      
REMARK 465     ASN A    87                                                      
REMARK 465     HIS A    88                                                      
REMARK 465     LEU A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     MSE A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     HIS A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     ASP A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     LYS A   143                                                      
REMARK 465     THR A   144                                                      
REMARK 465     THR A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     ASN A   147                                                      
REMARK 465     SER A   148                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASN B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     VAL B    78                                                      
REMARK 465     HIS B    79                                                      
REMARK 465     LYS B    80                                                      
REMARK 465     ASP B    81                                                      
REMARK 465     ILE B    82                                                      
REMARK 465     ASN B    83                                                      
REMARK 465     ILE B    84                                                      
REMARK 465     GLN B    85                                                      
REMARK 465     HIS B    86                                                      
REMARK 465     ASN B    87                                                      
REMARK 465     HIS B    88                                                      
REMARK 465     LEU B    89                                                      
REMARK 465     GLY B    90                                                      
REMARK 465     ASP B    91                                                      
REMARK 465     ASP B   133                                                      
REMARK 465     LEU B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     MSE B   136                                                      
REMARK 465     THR B   137                                                      
REMARK 465     ASN B   138                                                      
REMARK 465     HIS B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     ASP B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     LYS B   143                                                      
REMARK 465     THR B   144                                                      
REMARK 465     THR B   145                                                      
REMARK 465     GLY B   146                                                      
REMARK 465     ASN B   147                                                      
REMARK 465     SER B   148                                                      
REMARK 465     GLY B   149                                                      
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     TYR B   7    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   252     O    HOH A   253              1.84            
REMARK 500   OD1  ASN A    11     O    HOH A   201              1.98            
REMARK 500   O    HOH A   215     O    HOH A   224              2.02            
REMARK 500   O    HOH A   219     O    HOH A   234              2.10            
REMARK 500   O    HOH B   225     O    HOH B   236              2.10            
REMARK 500   O    ASP A   133     O    HOH A   202              2.16            
REMARK 500   O    HOH A   222     O    HOH A   227              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   227     O    HOH B   222     4555     1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  36      137.86   -172.68                                   
REMARK 500    ARG A 123     -162.61   -111.01                                   
REMARK 500    ASN B  63       41.38   -100.40                                   
REMARK 500    PRO B  74       12.68    -69.90                                   
REMARK 500    LEU B 112       80.58   -162.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A   35     CYS A   36                 -149.99                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4U4I A    5   161  UNP    G5CS11   G5CS11_9VIRU     2    158             
DBREF  4U4I B    5   161  UNP    G5CS11   G5CS11_9VIRU     2    158             
SEQADV 4U4I GLY A    1  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I PRO A    2  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I GLY A    3  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I SER A    4  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I GLY B    1  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I PRO B    2  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I GLY B    3  UNP  G5CS11              EXPRESSION TAG                 
SEQADV 4U4I SER B    4  UNP  G5CS11              EXPRESSION TAG                 
SEQRES   1 A  161  GLY PRO GLY SER SER ARG TYR ASP PHE PHE ASN VAL VAL          
SEQRES   2 A  161  THR ALA ILE CYS GLN LEU ASP LYS PRO HIS ASP TYR GLY          
SEQRES   3 A  161  TYR ALA ILE PHE THR GLN LEU PRO ASP CYS THR GLU ILE          
SEQRES   4 A  161  GLN PHE HIS LEU LYS ASN LEU PRO PRO GLY LYS HIS GLY          
SEQRES   5 A  161  CYS HIS ILE HIS LYS SER GLY ASP ARG ARG ASN GLY CYS          
SEQRES   6 A  161  THR SER MSE GLY PRO HIS PHE ASN PRO PHE ASN GLY VAL          
SEQRES   7 A  161  HIS LYS ASP ILE ASN ILE GLN HIS ASN HIS LEU GLY ASP          
SEQRES   8 A  161  LEU GLY ASN ILE VAL VAL ASN ASN ASN GLY GLU CYS ASN          
SEQRES   9 A  161  GLU ILE ILE CYS VAL LYS TYR LEU PRO LEU THR GLY SER          
SEQRES  10 A  161  ASN GLN ILE ILE GLY ARG GLY LEU VAL ILE HIS GLU LYS          
SEQRES  11 A  161  GLU ASP ASP LEU GLY MSE THR ASN HIS PRO ASP SER LYS          
SEQRES  12 A  161  THR THR GLY ASN SER GLY ASP ARG ILE ALA CYS GLY ILE          
SEQRES  13 A  161  ILE ALA TYR LEU ASN                                          
SEQRES   1 B  161  GLY PRO GLY SER SER ARG TYR ASP PHE PHE ASN VAL VAL          
SEQRES   2 B  161  THR ALA ILE CYS GLN LEU ASP LYS PRO HIS ASP TYR GLY          
SEQRES   3 B  161  TYR ALA ILE PHE THR GLN LEU PRO ASP CYS THR GLU ILE          
SEQRES   4 B  161  GLN PHE HIS LEU LYS ASN LEU PRO PRO GLY LYS HIS GLY          
SEQRES   5 B  161  CYS HIS ILE HIS LYS SER GLY ASP ARG ARG ASN GLY CYS          
SEQRES   6 B  161  THR SER MSE GLY PRO HIS PHE ASN PRO PHE ASN GLY VAL          
SEQRES   7 B  161  HIS LYS ASP ILE ASN ILE GLN HIS ASN HIS LEU GLY ASP          
SEQRES   8 B  161  LEU GLY ASN ILE VAL VAL ASN ASN ASN GLY GLU CYS ASN          
SEQRES   9 B  161  GLU ILE ILE CYS VAL LYS TYR LEU PRO LEU THR GLY SER          
SEQRES  10 B  161  ASN GLN ILE ILE GLY ARG GLY LEU VAL ILE HIS GLU LYS          
SEQRES  11 B  161  GLU ASP ASP LEU GLY MSE THR ASN HIS PRO ASP SER LYS          
SEQRES  12 B  161  THR THR GLY ASN SER GLY ASP ARG ILE ALA CYS GLY ILE          
SEQRES  13 B  161  ILE ALA TYR LEU ASN                                          
MODRES 4U4I MSE A   68  MET  MODIFIED RESIDUE                                   
MODRES 4U4I MSE B   68  MET  MODIFIED RESIDUE                                   
HET    MSE  A  68       8                                                       
HET    MSE  B  68       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    2(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *107(H2 O)                                                    
HELIX    1 AA1 ASN A   63  GLY A   69  5                                   7    
HELIX    2 AA2 ASN B   63  GLY B   69  5                                   7    
SHEET    1 AA1 8 ASP A  91  VAL A  97  0                                        
SHEET    2 AA1 8 GLY A  49  HIS A  56 -1  N  GLY A  49   O  VAL A  97           
SHEET    3 AA1 8 GLY A 124  HIS A 128 -1  O  HIS A 128   N  GLY A  52           
SHEET    4 AA1 8 ARG A 151  TYR A 159 -1  O  ALA A 153   N  ILE A 127           
SHEET    5 AA1 8 VAL A  13  GLN A  18 -1  N  ILE A  16   O  ALA A 158           
SHEET    6 AA1 8 GLY A  26  LEU A  33 -1  O  PHE A  30   N  ALA A  15           
SHEET    7 AA1 8 CYS A  36  LEU A  43 -1  O  GLU A  38   N  THR A  31           
SHEET    8 AA1 8 ILE A 106  VAL A 109 -1  O  ILE A 107   N  ILE A  39           
SHEET    1 AA2 8 ASN B  94  VAL B  97  0                                        
SHEET    2 AA2 8 GLY B  49  HIS B  56 -1  N  GLY B  49   O  VAL B  97           
SHEET    3 AA2 8 GLY B 124  HIS B 128 -1  O  VAL B 126   N  HIS B  54           
SHEET    4 AA2 8 ARG B 151  TYR B 159 -1  O  ALA B 153   N  ILE B 127           
SHEET    5 AA2 8 VAL B  13  GLN B  18 -1  N  ILE B  16   O  ALA B 158           
SHEET    6 AA2 8 GLY B  26  LEU B  33 -1  O  PHE B  30   N  ALA B  15           
SHEET    7 AA2 8 CYS B  36  LEU B  43 -1  O  GLN B  40   N  ILE B  29           
SHEET    8 AA2 8 ILE B 106  VAL B 109 -1  O  VAL B 109   N  THR B  37           
SSBOND   1 CYS A   36    CYS A  108                          1555   1555  2.01  
SSBOND   2 CYS A   65    CYS A  154                          1555   1555  2.08  
SSBOND   3 CYS B   36    CYS B  108                          1555   1555  2.04  
SSBOND   4 CYS B   65    CYS B  154                          1555   1555  2.07  
LINK         C   SER A  67                 N   MSE A  68     1555   1555  1.34  
LINK         C   MSE A  68                 N   GLY A  69     1555   1555  1.33  
LINK         C   SER B  67                 N   MSE B  68     1555   1555  1.33  
LINK         C   MSE B  68                 N   GLY B  69     1555   1555  1.33  
CISPEP   1 PHE A   10    ASN A   11          0        -8.34                     
CISPEP   2 LYS A   21    PRO A   22          0        -3.41                     
CISPEP   3 LYS B   21    PRO B   22          0        -1.18                     
CRYST1   70.626   70.626  117.426  90.00  90.00  90.00 P 43 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014159  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014159  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008516        0.00000                         
ATOM      1  N   PHE A   9      56.202  15.457  66.288  1.00 60.73           N  
ATOM      2  CA  PHE A   9      55.727  15.918  64.988  1.00 61.87           C  
ATOM      3  C   PHE A   9      54.266  16.390  65.021  1.00 62.06           C  
ATOM      4  O   PHE A   9      53.361  15.619  65.366  1.00 52.12           O  
ATOM      5  CB  PHE A   9      55.887  14.807  63.943  1.00 62.56           C  
ATOM      6  CG  PHE A   9      57.305  14.290  63.799  1.00 67.49           C  
ATOM      7  CD1 PHE A   9      58.381  15.165  63.718  1.00 69.81           C  
ATOM      8  CD2 PHE A   9      57.552  12.922  63.710  1.00 63.63           C  
ATOM      9  CE1 PHE A   9      59.677  14.678  63.576  1.00 73.97           C  
ATOM     10  CE2 PHE A   9      58.834  12.433  63.568  1.00 62.96           C  
ATOM     11  CZ  PHE A   9      59.898  13.307  63.499  1.00 68.59           C  
ATOM     12  N   PHE A  10      54.048  17.669  64.697  1.00 62.47           N  
ATOM     13  CA  PHE A  10      52.717  18.188  64.370  1.00 63.05           C  
ATOM     14  C   PHE A  10      52.854  18.678  62.925  1.00 67.34           C  
ATOM     15  O   PHE A  10      53.962  19.023  62.517  1.00 69.90           O  
ATOM     16  CB  PHE A  10      52.248  19.369  65.249  1.00 67.55           C  
ATOM     17  CG  PHE A  10      52.386  19.184  66.749  1.00 69.02           C  
ATOM     18  CD1 PHE A  10      53.067  18.123  67.315  1.00 68.03           C  
ATOM     19  CD2 PHE A  10      51.820  20.120  67.599  1.00 67.37           C  
ATOM     20  CE1 PHE A  10      53.186  18.003  68.686  1.00 65.20           C  
ATOM     21  CE2 PHE A  10      51.936  20.000  68.967  1.00 66.07           C  
ATOM     22  CZ  PHE A  10      52.620  18.940  69.512  1.00 63.87           C  
ATOM     23  N   ASN A  11      51.776  18.716  62.140  1.00 66.27           N  
ATOM     24  CA  ASN A  11      50.473  18.160  62.490  1.00 62.05           C  
ATOM     25  C   ASN A  11      50.089  17.171  61.401  1.00 55.99           C  
ATOM     26  O   ASN A  11      49.527  17.528  60.378  1.00 48.03           O  
ATOM     27  CB  ASN A  11      49.418  19.251  62.640  1.00 65.93           C  
ATOM     28  CG  ASN A  11      48.670  19.147  63.949  1.00 70.55           C  
ATOM     29  OD1 ASN A  11      48.989  18.298  64.786  1.00 69.79           O  
ATOM     30  ND2 ASN A  11      47.670  20.004  64.137  1.00 69.17           N  
ATOM     31  N   VAL A  12      50.403  15.917  61.666  1.00 52.84           N  
ATOM     32  CA  VAL A  12      50.598  14.909  60.650  1.00 43.95           C  
ATOM     33  C   VAL A  12      49.382  14.628  59.759  1.00 37.96           C  
ATOM     34  O   VAL A  12      48.253  14.553  60.232  1.00 39.15           O  
ATOM     35  CB  VAL A  12      51.039  13.622  61.337  1.00 41.93           C  
ATOM     36  CG1 VAL A  12      51.639  12.698  60.343  1.00 41.17           C  
ATOM     37  CG2 VAL A  12      52.063  13.961  62.427  1.00 50.09           C  
ATOM     38  N   VAL A  13      49.616  14.476  58.462  1.00 33.53           N  
ATOM     39  CA  VAL A  13      48.559  13.986  57.590  1.00 28.33           C  
ATOM     40  C   VAL A  13      48.650  12.463  57.516  1.00 26.60           C  
ATOM     41  O   VAL A  13      49.723  11.883  57.317  1.00 27.01           O  
ATOM     42  CB  VAL A  13      48.634  14.597  56.190  1.00 26.49           C  
ATOM     43  CG1 VAL A  13      47.581  13.952  55.254  1.00 24.85           C  
ATOM     44  CG2 VAL A  13      48.443  16.110  56.265  1.00 25.60           C  
ATOM     45  N   THR A  14      47.515  11.816  57.710  1.00 25.82           N  
ATOM     46  CA  THR A  14      47.456  10.367  57.665  1.00 29.88           C  
ATOM     47  C   THR A  14      46.440   9.925  56.611  1.00 25.82           C  
ATOM     48  O   THR A  14      45.371  10.522  56.501  1.00 25.57           O  
ATOM     49  CB  THR A  14      47.088   9.797  59.048  1.00 29.28           C  
ATOM     50  OG1 THR A  14      47.942  10.393  60.029  1.00 32.28           O  
ATOM     51  CG2 THR A  14      47.289   8.285  59.090  1.00 25.02           C  
ATOM     52  N   ALA A  15      46.777   8.898  55.833  1.00 23.60           N  
ATOM     53  CA  ALA A  15      45.841   8.354  54.849  1.00 25.05           C  
ATOM     54  C   ALA A  15      45.583   6.872  55.070  1.00 25.73           C  
ATOM     55  O   ALA A  15      46.400   6.162  55.646  1.00 25.42           O  
ATOM     56  CB  ALA A  15      46.353   8.590  53.415  1.00 22.41           C  
ATOM     57  N   ILE A  16      44.425   6.415  54.615  1.00 24.00           N  
ATOM     58  CA  ILE A  16      44.088   5.001  54.653  1.00 24.20           C  
ATOM     59  C   ILE A  16      43.713   4.498  53.258  1.00 27.52           C  
ATOM     60  O   ILE A  16      43.045   5.189  52.486  1.00 25.30           O  
ATOM     61  CB  ILE A  16      42.930   4.714  55.639  1.00 28.95           C  
ATOM     62  CG1 ILE A  16      42.620   3.215  55.680  1.00 29.02           C  
ATOM     63  CG2 ILE A  16      41.688   5.537  55.283  1.00 25.80           C  
ATOM     64  CD1 ILE A  16      41.629   2.826  56.756  1.00 29.54           C  
ATOM     65  N   CYS A  17      44.183   3.300  52.938  1.00 22.60           N  
ATOM     66  CA  CYS A  17      43.775   2.598  51.736  1.00 27.27           C  
ATOM     67  C   CYS A  17      43.180   1.236  52.073  1.00 27.23           C  
ATOM     68  O   CYS A  17      43.897   0.346  52.537  1.00 24.72           O  
ATOM     69  CB  CYS A  17      44.963   2.404  50.785  1.00 19.72           C  
ATOM     70  SG  CYS A  17      44.473   1.637  49.239  1.00 26.74           S  
ATOM     71  N   GLN A  18      41.883   1.049  51.841  1.00 27.11           N  
ATOM     72  CA  GLN A  18      41.330  -0.290  51.993  1.00 28.16           C  
ATOM     73  C   GLN A  18      41.495  -1.044  50.685  1.00 30.67           C  
ATOM     74  O   GLN A  18      40.925  -0.653  49.669  1.00 27.13           O  
ATOM     75  CB  GLN A  18      39.858  -0.255  52.404  1.00 28.99           C  
ATOM     76  CG  GLN A  18      39.653   0.188  53.835  1.00 36.89           C  
ATOM     77  CD  GLN A  18      38.213   0.412  54.149  1.00 39.20           C  
ATOM     78  OE1 GLN A  18      37.750   1.555  54.188  1.00 41.91           O  
ATOM     79  NE2 GLN A  18      37.479  -0.675  54.375  1.00 38.03           N  
ATOM     80  N   LEU A  19      42.270  -2.123  50.711  1.00 25.88           N  
ATOM     81  CA  LEU A  19      42.455  -2.926  49.515  1.00 26.97           C  
ATOM     82  C   LEU A  19      41.312  -3.925  49.436  1.00 31.91           C  
ATOM     83  O   LEU A  19      41.487  -5.097  49.789  1.00 28.71           O  
ATOM     84  CB  LEU A  19      43.821  -3.616  49.545  1.00 24.83           C  
ATOM     85  CG  LEU A  19      44.886  -2.532  49.381  1.00 32.16           C  
ATOM     86  CD1 LEU A  19      45.568  -2.145  50.698  1.00 26.82           C  
ATOM     87  CD2 LEU A  19      45.875  -2.888  48.287  1.00 32.27           C  
ATOM     88  N   ASP A  20      40.136  -3.448  49.000  1.00 28.02           N  
ATOM     89  CA  ASP A  20      38.935  -4.263  49.046  1.00 29.47           C  
ATOM     90  C   ASP A  20      38.419  -4.693  47.681  1.00 29.11           C  
ATOM     91  O   ASP A  20      37.301  -5.160  47.583  1.00 31.31           O  
ATOM     92  CB  ASP A  20      37.805  -3.553  49.817  1.00 30.30           C  
ATOM     93  CG  ASP A  20      37.576  -2.122  49.366  1.00 33.43           C  
ATOM     94  OD1 ASP A  20      38.133  -1.712  48.323  1.00 28.33           O  
ATOM     95  OD2 ASP A  20      36.833  -1.401  50.079  1.00 34.33           O  
ATOM     96  N   LYS A  21      39.238  -4.557  46.643  1.00 32.36           N  
ATOM     97  CA  LYS A  21      38.933  -5.163  45.354  1.00 32.41           C  
ATOM     98  C   LYS A  21      40.118  -6.004  44.915  1.00 32.78           C  
ATOM     99  O   LYS A  21      41.261  -5.628  45.176  1.00 30.36           O  
ATOM    100  CB  LYS A  21      38.607  -4.106  44.287  1.00 28.31           C  
ATOM    101  CG  LYS A  21      37.236  -3.449  44.426  1.00 29.43           C  
ATOM    102  CD  LYS A  21      36.987  -2.506  43.244  1.00 33.27           C  
ATOM    103  CE  LYS A  21      35.649  -1.784  43.344  1.00 37.57           C  
ATOM    104  NZ  LYS A  21      34.507  -2.643  42.925  1.00 44.71           N  
ATOM    105  N   PRO A  22      39.856  -7.139  44.234  1.00 32.10           N  
ATOM    106  CA  PRO A  22      38.517  -7.672  43.939  1.00 34.67           C  
ATOM    107  C   PRO A  22      37.856  -8.309  45.167  1.00 37.55           C  
ATOM    108  O   PRO A  22      36.685  -8.647  45.103  1.00 38.32           O  
ATOM    109  CB  PRO A  22      38.786  -8.725  42.851  1.00 36.06           C  
ATOM    110  CG  PRO A  22      40.184  -9.198  43.143  1.00 36.35           C  
ATOM    111  CD  PRO A  22      40.916  -7.931  43.587  1.00 33.67           C  
ATOM    112  N   HIS A  23      38.600  -8.456  46.262  1.00 34.12           N  
ATOM    113  CA  HIS A  23      38.053  -8.956  47.525  1.00 37.69           C  
ATOM    114  C   HIS A  23      38.651  -8.196  48.697  1.00 33.69           C  
ATOM    115  O   HIS A  23      39.480  -7.302  48.513  1.00 33.27           O  
ATOM    116  CB  HIS A  23      38.336 -10.447  47.712  1.00 38.81           C  
ATOM    117  CG  HIS A  23      37.843 -11.299  46.594  1.00 41.69           C  
ATOM    118  ND1 HIS A  23      36.503 -11.553  46.387  1.00 39.89           N  
ATOM    119  CD2 HIS A  23      38.509 -11.946  45.607  1.00 39.41           C  
ATOM    120  CE1 HIS A  23      36.367 -12.320  45.320  1.00 39.55           C  
ATOM    121  NE2 HIS A  23      37.568 -12.573  44.830  1.00 41.75           N  
ATOM    122  N   ASP A  24      38.257  -8.584  49.901  1.00 32.94           N  
ATOM    123  CA  ASP A  24      38.755  -7.953  51.118  1.00 33.10           C  
ATOM    124  C   ASP A  24      40.168  -8.414  51.431  1.00 32.63           C  
ATOM    125  O   ASP A  24      40.357  -9.490  51.998  1.00 30.77           O  
ATOM    126  CB  ASP A  24      37.829  -8.271  52.296  1.00 33.50           C  
ATOM    127  CG  ASP A  24      38.255  -7.580  53.575  1.00 34.96           C  
ATOM    128  OD1 ASP A  24      39.152  -6.710  53.514  1.00 35.86           O  
ATOM    129  OD2 ASP A  24      37.692  -7.903  54.645  1.00 38.28           O  
ATOM    130  N   TYR A  25      41.169  -7.612  51.069  1.00 32.41           N  
ATOM    131  CA  TYR A  25      42.548  -7.978  51.416  1.00 30.40           C  
ATOM    132  C   TYR A  25      43.144  -7.078  52.504  1.00 29.42           C  
ATOM    133  O   TYR A  25      44.369  -6.967  52.631  1.00 29.89           O  
ATOM    134  CB  TYR A  25      43.430  -7.964  50.170  1.00 29.00           C  
ATOM    135  CG  TYR A  25      42.946  -8.925  49.104  1.00 34.51           C  
ATOM    136  CD1 TYR A  25      43.144 -10.295  49.238  1.00 33.34           C  
ATOM    137  CD2 TYR A  25      42.276  -8.468  47.975  1.00 33.46           C  
ATOM    138  CE1 TYR A  25      42.694 -11.186  48.281  1.00 34.72           C  
ATOM    139  CE2 TYR A  25      41.824  -9.354  47.003  1.00 34.41           C  
ATOM    140  CZ  TYR A  25      42.035 -10.711  47.163  1.00 37.87           C  
ATOM    141  OH  TYR A  25      41.598 -11.598  46.201  1.00 36.69           O  
ATOM    142  N   GLY A  26      42.282  -6.451  53.300  1.00 29.40           N  
ATOM    143  CA  GLY A  26      42.754  -5.633  54.410  1.00 28.86           C  
ATOM    144  C   GLY A  26      43.040  -4.198  53.992  1.00 30.89           C  
ATOM    145  O   GLY A  26      42.420  -3.687  53.054  1.00 29.75           O  
ATOM    146  N   TYR A  27      43.988  -3.551  54.668  1.00 28.97           N  
ATOM    147  CA  TYR A  27      44.213  -2.127  54.456  1.00 25.87           C  
ATOM    148  C   TYR A  27      45.665  -1.692  54.718  1.00 27.96           C  
ATOM    149  O   TYR A  27      46.484  -2.487  55.186  1.00 29.19           O  
ATOM    150  CB  TYR A  27      43.245  -1.328  55.337  1.00 27.69           C  
ATOM    151  CG  TYR A  27      43.543  -1.392  56.832  1.00 31.51           C  
ATOM    152  CD1 TYR A  27      43.139  -2.487  57.605  1.00 29.72           C  
ATOM    153  CD2 TYR A  27      44.216  -0.351  57.474  1.00 28.07           C  
ATOM    154  CE1 TYR A  27      43.414  -2.544  58.979  1.00 26.08           C  
ATOM    155  CE2 TYR A  27      44.489  -0.399  58.847  1.00 26.63           C  
ATOM    156  CZ  TYR A  27      44.089  -1.495  59.585  1.00 29.71           C  
ATOM    157  OH  TYR A  27      44.359  -1.529  60.933  1.00 29.90           O  
ATOM    158  N   ALA A  28      45.986  -0.444  54.371  1.00 24.48           N  
ATOM    159  CA  ALA A  28      47.295   0.152  54.680  1.00 24.50           C  
ATOM    160  C   ALA A  28      47.121   1.593  55.187  1.00 24.46           C  
ATOM    161  O   ALA A  28      46.193   2.309  54.788  1.00 22.47           O  
ATOM    162  CB  ALA A  28      48.228   0.121  53.448  1.00 23.02           C  
ATOM    163  N   ILE A  29      48.006   2.002  56.085  1.00 21.65           N  
ATOM    164  CA  ILE A  29      47.979   3.343  56.660  1.00 23.53           C  
ATOM    165  C   ILE A  29      49.190   4.111  56.184  1.00 23.61           C  
ATOM    166  O   ILE A  29      50.316   3.620  56.316  1.00 26.85           O  
ATOM    167  CB  ILE A  29      47.980   3.312  58.215  1.00 21.89           C  
ATOM    168  CG1 ILE A  29      46.739   2.601  58.746  1.00 25.56           C  
ATOM    169  CG2 ILE A  29      47.995   4.718  58.778  1.00 21.02           C  
ATOM    170  CD1 ILE A  29      45.446   3.361  58.520  1.00 26.04           C  
ATOM    171  N   PHE A  30      48.968   5.301  55.621  1.00 24.16           N  
ATOM    172  CA  PHE A  30      50.063   6.157  55.156  1.00 24.35           C  
ATOM    173  C   PHE A  30      50.206   7.332  56.117  1.00 23.38           C  
ATOM    174  O   PHE A  30      49.223   8.007  56.422  1.00 25.38           O  
ATOM    175  CB  PHE A  30      49.819   6.713  53.739  1.00 24.37           C  
ATOM    176  CG  PHE A  30      49.768   5.681  52.639  1.00 25.70           C  
ATOM    177  CD1 PHE A  30      48.690   4.814  52.521  1.00 26.39           C  
ATOM    178  CD2 PHE A  30      50.764   5.644  51.658  1.00 25.99           C  
ATOM    179  CE1 PHE A  30      48.626   3.894  51.472  1.00 24.62           C  
ATOM    180  CE2 PHE A  30      50.705   4.727  50.603  1.00 24.82           C  
ATOM    181  CZ  PHE A  30      49.633   3.845  50.520  1.00 24.05           C  
ATOM    182  N   THR A  31      51.424   7.603  56.567  1.00 24.49           N  
ATOM    183  CA  THR A  31      51.653   8.719  57.463  1.00 28.34           C  
ATOM    184  C   THR A  31      52.759   9.629  56.923  1.00 29.70           C  
ATOM    185  O   THR A  31      53.912   9.215  56.784  1.00 29.30           O  
ATOM    186  CB  THR A  31      52.038   8.235  58.876  1.00 29.48           C  
ATOM    187  OG1 THR A  31      51.078   7.284  59.346  1.00 25.88           O  
ATOM    188  CG2 THR A  31      52.054   9.391  59.814  1.00 28.76           C  
ATOM    189  N   GLN A  32      52.400  10.869  56.627  1.00 30.79           N  
ATOM    190  CA  GLN A  32      53.329  11.822  56.014  1.00 31.03           C  
ATOM    191  C   GLN A  32      54.269  12.431  57.059  1.00 33.65           C  
ATOM    192  O   GLN A  32      53.920  13.400  57.734  1.00 32.56           O  
ATOM    193  CB  GLN A  32      52.535  12.922  55.289  1.00 33.03           C  
ATOM    194  CG  GLN A  32      53.365  13.874  54.416  1.00 37.26           C  
ATOM    195  CD  GLN A  32      52.491  14.699  53.453  1.00 38.32           C  
ATOM    196  OE1 GLN A  32      52.650  14.610  52.238  1.00 35.00           O  
ATOM    197  NE2 GLN A  32      51.576  15.516  54.004  1.00 32.85           N  
ATOM    198  N   LEU A  33      55.447  11.832  57.206  1.00 36.05           N  
ATOM    199  CA  LEU A  33      56.464  12.298  58.151  1.00 41.26           C  
ATOM    200  C   LEU A  33      57.417  13.269  57.443  1.00 41.08           C  
ATOM    201  O   LEU A  33      57.436  13.323  56.211  1.00 41.24           O  
ATOM    202  CB  LEU A  33      57.226  11.106  58.735  1.00 36.54           C  
ATOM    203  CG  LEU A  33      56.379  10.126  59.543  1.00 39.14           C  
ATOM    204  CD1 LEU A  33      57.196   8.913  59.861  1.00 38.59           C  
ATOM    205  CD2 LEU A  33      55.883  10.776  60.820  1.00 37.87           C  
ATOM    206  N   PRO A  34      58.216  14.044  58.207  1.00 43.75           N  
ATOM    207  CA  PRO A  34      58.998  15.067  57.495  1.00 45.89           C  
ATOM    208  C   PRO A  34      60.111  14.519  56.589  1.00 46.76           C  
ATOM    209  O   PRO A  34      60.398  15.128  55.560  1.00 47.45           O  
ATOM    210  CB  PRO A  34      59.580  15.914  58.628  1.00 46.46           C  
ATOM    211  CG  PRO A  34      59.584  15.012  59.820  1.00 50.77           C  
ATOM    212  CD  PRO A  34      58.388  14.127  59.670  1.00 44.89           C  
ATOM    213  N   ASP A  35      60.712  13.387  56.925  1.00 43.11           N  
ATOM    214  CA  ASP A  35      61.774  12.863  56.066  1.00 50.59           C  
ATOM    215  C   ASP A  35      61.286  11.740  55.150  1.00 50.65           C  
ATOM    216  O   ASP A  35      62.056  11.179  54.369  1.00 46.15           O  
ATOM    217  CB  ASP A  35      62.942  12.355  56.915  1.00 51.21           C  
ATOM    218  CG  ASP A  35      63.599  13.462  57.727  1.00 59.12           C  
ATOM    219  OD1 ASP A  35      63.542  14.646  57.319  1.00 58.74           O  
ATOM    220  OD2 ASP A  35      64.179  13.141  58.782  1.00 70.55           O  
ATOM    221  N   CYS A  36      59.994  11.441  55.216  1.00 48.17           N  
ATOM    222  CA  CYS A  36      59.565  10.085  54.946  1.00 42.26           C  
ATOM    223  C   CYS A  36      58.050   9.936  54.886  1.00 37.62           C  
ATOM    224  O   CYS A  36      57.353  10.493  55.718  1.00 39.14           O  
ATOM    225  CB  CYS A  36      60.111   9.202  56.070  1.00 46.11           C  
ATOM    226  SG  CYS A  36      60.640   7.617  55.575  1.00 60.32           S  
ATOM    227  N   THR A  37      57.520   9.179  53.935  1.00 37.65           N  
ATOM    228  CA  THR A  37      56.127   8.774  54.077  1.00 31.38           C  
ATOM    229  C   THR A  37      56.098   7.326  54.566  1.00 29.46           C  
ATOM    230  O   THR A  37      56.534   6.418  53.869  1.00 29.90           O  
ATOM    231  CB  THR A  37      55.335   8.933  52.789  1.00 31.62           C  
ATOM    232  OG1 THR A  37      55.151  10.331  52.528  1.00 29.84           O  
ATOM    233  CG2 THR A  37      53.948   8.268  52.931  1.00 27.25           C  
ATOM    234  N   GLU A  38      55.618   7.140  55.794  1.00 25.24           N  
ATOM    235  CA  GLU A  38      55.579   5.834  56.438  1.00 28.47           C  
ATOM    236  C   GLU A  38      54.355   5.059  55.960  1.00 27.64           C  
ATOM    237  O   GLU A  38      53.262   5.610  55.912  1.00 25.35           O  
ATOM    238  CB  GLU A  38      55.538   5.979  57.967  1.00 27.14           C  
ATOM    239  CG  GLU A  38      55.405   4.647  58.702  1.00 24.71           C  
ATOM    240  CD  GLU A  38      55.215   4.813  60.199  1.00 32.26           C  
ATOM    241  OE1 GLU A  38      54.983   5.968  60.636  1.00 26.52           O  
ATOM    242  OE2 GLU A  38      55.298   3.787  60.933  1.00 25.63           O  
ATOM    243  N   ILE A  39      54.532   3.790  55.605  1.00 26.38           N  
ATOM    244  CA  ILE A  39      53.390   2.967  55.214  1.00 25.72           C  
ATOM    245  C   ILE A  39      53.313   1.722  56.091  1.00 26.36           C  
ATOM    246  O   ILE A  39      54.204   0.890  56.075  1.00 27.04           O  
ATOM    247  CB  ILE A  39      53.453   2.560  53.721  1.00 26.51           C  
ATOM    248  CG1 ILE A  39      53.599   3.804  52.845  1.00 25.99           C  
ATOM    249  CG2 ILE A  39      52.181   1.785  53.322  1.00 25.55           C  
ATOM    250  CD1 ILE A  39      53.983   3.509  51.428  1.00 24.58           C  
ATOM    251  N   GLN A  40      52.248   1.623  56.876  1.00 26.62           N  
ATOM    252  CA  GLN A  40      52.028   0.468  57.727  1.00 27.06           C  
ATOM    253  C   GLN A  40      51.029  -0.446  57.031  1.00 24.61           C  
ATOM    254  O   GLN A  40      49.865  -0.093  56.882  1.00 23.73           O  
ATOM    255  CB  GLN A  40      51.519   0.910  59.100  1.00 26.55           C  
ATOM    256  CG  GLN A  40      52.510   1.843  59.833  1.00 28.39           C  
ATOM    257  CD  GLN A  40      51.912   2.501  61.067  1.00 34.06           C  
ATOM    258  OE1 GLN A  40      51.374   3.610  60.986  1.00 36.90           O  
ATOM    259  NE2 GLN A  40      51.976   1.806  62.215  1.00 31.59           N  
ATOM    260  N   PHE A  41      51.488  -1.600  56.570  1.00 22.13           N  
ATOM    261  CA  PHE A  41      50.592  -2.537  55.903  1.00 25.89           C  
ATOM    262  C   PHE A  41      49.852  -3.387  56.942  1.00 29.15           C  
ATOM    263  O   PHE A  41      50.418  -3.746  57.984  1.00 25.73           O  
ATOM    264  CB  PHE A  41      51.369  -3.425  54.923  1.00 25.13           C  
ATOM    265  CG  PHE A  41      51.877  -2.693  53.708  1.00 27.28           C  
ATOM    266  CD1 PHE A  41      51.081  -2.564  52.573  1.00 24.29           C  
ATOM    267  CD2 PHE A  41      53.142  -2.125  53.700  1.00 26.21           C  
ATOM    268  CE1 PHE A  41      51.546  -1.890  51.454  1.00 26.70           C  
ATOM    269  CE2 PHE A  41      53.611  -1.450  52.582  1.00 28.91           C  
ATOM    270  CZ  PHE A  41      52.811  -1.334  51.458  1.00 30.14           C  
ATOM    271  N   HIS A  42      48.575  -3.654  56.667  1.00 27.26           N  
ATOM    272  CA  HIS A  42      47.781  -4.637  57.400  1.00 28.08           C  
ATOM    273  C   HIS A  42      46.950  -5.440  56.376  1.00 30.38           C  
ATOM    274  O   HIS A  42      45.715  -5.393  56.371  1.00 23.93           O  
ATOM    275  CB  HIS A  42      46.874  -3.960  58.449  1.00 27.97           C  
ATOM    276  CG  HIS A  42      47.626  -3.183  59.491  1.00 30.61           C  
ATOM    277  ND1 HIS A  42      48.418  -3.788  60.446  1.00 28.12           N  
ATOM    278  CD2 HIS A  42      47.715  -1.847  59.723  1.00 26.96           C  
ATOM    279  CE1 HIS A  42      48.958  -2.863  61.222  1.00 31.51           C  
ATOM    280  NE2 HIS A  42      48.549  -1.676  60.805  1.00 30.89           N  
ATOM    281  N   LEU A  43      47.649  -6.152  55.493  1.00 28.72           N  
ATOM    282  CA  LEU A  43      47.006  -6.933  54.454  1.00 27.95           C  
ATOM    283  C   LEU A  43      46.705  -8.335  54.966  1.00 30.77           C  
ATOM    284  O   LEU A  43      47.281  -8.771  55.966  1.00 34.26           O  
ATOM    285  CB  LEU A  43      47.892  -7.014  53.211  1.00 23.25           C  
ATOM    286  CG  LEU A  43      48.356  -5.661  52.660  1.00 27.77           C  
ATOM    287  CD1 LEU A  43      49.092  -5.820  51.358  1.00 26.14           C  
ATOM    288  CD2 LEU A  43      47.226  -4.662  52.540  1.00 26.58           C  
ATOM    289  N   LYS A  44      45.805  -9.026  54.271  1.00 29.30           N  
ATOM    290  CA  LYS A  44      45.394 -10.388  54.617  1.00 34.89           C  
ATOM    291  C   LYS A  44      44.824 -11.075  53.363  1.00 36.36           C  
ATOM    292  O   LYS A  44      44.571 -10.403  52.351  1.00 32.32           O  
ATOM    293  CB  LYS A  44      44.354 -10.358  55.733  1.00 28.26           C  
ATOM    294  CG  LYS A  44      43.082  -9.648  55.275  1.00 33.42           C  
ATOM    295  CD  LYS A  44      42.008  -9.554  56.338  1.00 34.07           C  
ATOM    296  CE  LYS A  44      40.666  -9.224  55.698  1.00 35.30           C  
ATOM    297  NZ  LYS A  44      39.570  -8.946  56.683  1.00 45.36           N  
ATOM    298  N   ASN A  45      44.640 -12.398  53.433  1.00 34.70           N  
ATOM    299  CA  ASN A  45      44.083 -13.212  52.337  1.00 35.23           C  
ATOM    300  C   ASN A  45      44.863 -13.228  51.021  1.00 34.79           C  
ATOM    301  O   ASN A  45      44.312 -13.612  49.981  1.00 34.41           O  
ATOM    302  CB  ASN A  45      42.657 -12.756  52.022  1.00 33.94           C  
ATOM    303  CG  ASN A  45      41.771 -12.779  53.227  1.00 35.43           C  
ATOM    304  OD1 ASN A  45      41.878 -13.668  54.067  1.00 35.71           O  
ATOM    305  ND2 ASN A  45      40.893 -11.797  53.333  1.00 37.04           N  
ATOM    306  N   LEU A  46      46.129 -12.826  51.042  1.00 32.03           N  
ATOM    307  CA  LEU A  46      46.899 -12.729  49.798  1.00 30.51           C  
ATOM    308  C   LEU A  46      47.780 -13.963  49.561  1.00 33.83           C  
ATOM    309  O   LEU A  46      48.071 -14.694  50.497  1.00 34.05           O  
ATOM    310  CB  LEU A  46      47.763 -11.466  49.819  1.00 32.06           C  
ATOM    311  CG  LEU A  46      47.014 -10.137  49.658  1.00 35.31           C  
ATOM    312  CD1 LEU A  46      47.865  -8.988  50.135  1.00 28.45           C  
ATOM    313  CD2 LEU A  46      46.593  -9.918  48.202  1.00 30.22           C  
ATOM    314  N   PRO A  47      48.200 -14.197  48.306  1.00 35.97           N  
ATOM    315  CA  PRO A  47      49.220 -15.209  48.008  1.00 38.45           C  
ATOM    316  C   PRO A  47      50.550 -14.888  48.693  1.00 39.12           C  
ATOM    317  O   PRO A  47      51.029 -13.760  48.574  1.00 37.55           O  
ATOM    318  CB  PRO A  47      49.383 -15.123  46.484  1.00 34.92           C  
ATOM    319  CG  PRO A  47      48.142 -14.496  45.990  1.00 36.59           C  
ATOM    320  CD  PRO A  47      47.705 -13.546  47.081  1.00 33.90           C  
ATOM    321  N   PRO A  48      51.151 -15.868  49.385  1.00 41.56           N  
ATOM    322  CA  PRO A  48      52.430 -15.636  50.069  1.00 36.83           C  
ATOM    323  C   PRO A  48      53.548 -15.225  49.110  1.00 32.18           C  
ATOM    324  O   PRO A  48      53.486 -15.565  47.938  1.00 36.61           O  
ATOM    325  CB  PRO A  48      52.738 -16.996  50.713  1.00 41.37           C  
ATOM    326  CG  PRO A  48      51.435 -17.689  50.797  1.00 45.70           C  
ATOM    327  CD  PRO A  48      50.645 -17.232  49.602  1.00 39.59           C  
ATOM    328  N   GLY A  49      54.553 -14.503  49.608  1.00 34.91           N  
ATOM    329  CA  GLY A  49      55.716 -14.163  48.807  1.00 30.35           C  
ATOM    330  C   GLY A  49      55.844 -12.685  48.488  1.00 31.51           C  
ATOM    331  O   GLY A  49      55.107 -11.864  49.023  1.00 31.54           O  
ATOM    332  N   LYS A  50      56.787 -12.344  47.613  1.00 31.09           N  
ATOM    333  CA  LYS A  50      56.997 -10.961  47.218  1.00 32.20           C  
ATOM    334  C   LYS A  50      55.979 -10.504  46.178  1.00 36.07           C  
ATOM    335  O   LYS A  50      55.638 -11.243  45.255  1.00 33.20           O  
ATOM    336  CB  LYS A  50      58.395 -10.759  46.659  1.00 33.28           C  
ATOM    337  CG  LYS A  50      59.509 -11.122  47.596  1.00 34.75           C  
ATOM    338  CD  LYS A  50      60.807 -10.545  47.046  1.00 41.26           C  
ATOM    339  CE  LYS A  50      62.016 -11.070  47.793  1.00 48.06           C  
ATOM    340  NZ  LYS A  50      62.176 -12.534  47.575  1.00 46.45           N  
ATOM    341  N   HIS A  51      55.502  -9.276  46.338  1.00 31.32           N  
ATOM    342  CA  HIS A  51      54.551  -8.689  45.407  1.00 32.10           C  
ATOM    343  C   HIS A  51      54.905  -7.228  45.175  1.00 30.66           C  
ATOM    344  O   HIS A  51      55.143  -6.476  46.127  1.00 31.43           O  
ATOM    345  CB  HIS A  51      53.114  -8.819  45.937  1.00 31.21           C  
ATOM    346  CG  HIS A  51      52.641 -10.234  46.082  1.00 34.10           C  
ATOM    347  ND1 HIS A  51      52.287 -11.014  45.002  1.00 37.65           N  
ATOM    348  CD2 HIS A  51      52.451 -11.005  47.180  1.00 35.06           C  
ATOM    349  CE1 HIS A  51      51.911 -12.209  45.428  1.00 39.69           C  
ATOM    350  NE2 HIS A  51      52.002 -12.231  46.746  1.00 36.75           N  
ATOM    351  N   GLY A  52      54.951  -6.829  43.912  1.00 34.72           N  
ATOM    352  CA  GLY A  52      55.214  -5.446  43.554  1.00 29.86           C  
ATOM    353  C   GLY A  52      54.106  -4.560  44.088  1.00 33.68           C  
ATOM    354  O   GLY A  52      52.915  -4.888  44.017  1.00 31.80           O  
ATOM    355  N   CYS A  53      54.503  -3.437  44.658  1.00 31.42           N  
ATOM    356  CA  CYS A  53      53.542  -2.521  45.239  1.00 32.61           C  
ATOM    357  C   CYS A  53      53.695  -1.160  44.564  1.00 33.12           C  
ATOM    358  O   CYS A  53      54.768  -0.572  44.591  1.00 35.59           O  
ATOM    359  CB  CYS A  53      53.755  -2.433  46.750  1.00 31.40           C  
ATOM    360  SG  CYS A  53      52.467  -1.544  47.566  1.00 43.60           S  
ATOM    361  N   HIS A  54      52.644  -0.672  43.919  1.00 28.25           N  
ATOM    362  CA  HIS A  54      52.768   0.575  43.173  1.00 30.06           C  
ATOM    363  C   HIS A  54      51.608   1.506  43.394  1.00 26.89           C  
ATOM    364  O   HIS A  54      50.471   1.062  43.584  1.00 24.98           O  
ATOM    365  CB  HIS A  54      52.897   0.294  41.677  1.00 29.61           C  
ATOM    366  CG  HIS A  54      54.094  -0.523  41.331  1.00 33.99           C  
ATOM    367  ND1 HIS A  54      55.364   0.005  41.301  1.00 40.85           N  
ATOM    368  CD2 HIS A  54      54.226  -1.849  41.104  1.00 34.30           C  
ATOM    369  CE1 HIS A  54      56.224  -0.956  41.007  1.00 47.86           C  
ATOM    370  NE2 HIS A  54      55.559  -2.090  40.892  1.00 33.65           N  
ATOM    371  N   ILE A  55      51.904   2.804  43.364  1.00 25.26           N  
ATOM    372  CA  ILE A  55      50.850   3.806  43.231  1.00 29.46           C  
ATOM    373  C   ILE A  55      50.437   3.903  41.760  1.00 29.99           C  
ATOM    374  O   ILE A  55      51.279   3.912  40.853  1.00 27.75           O  
ATOM    375  CB  ILE A  55      51.287   5.200  43.743  1.00 29.94           C  
ATOM    376  CG1 ILE A  55      51.899   5.093  45.143  1.00 21.26           C  
ATOM    377  CG2 ILE A  55      50.082   6.155  43.761  1.00 24.71           C  
ATOM    378  CD1 ILE A  55      50.919   4.544  46.177  1.00 24.03           C  
ATOM    379  N   HIS A  56      49.131   3.953  41.531  1.00 25.43           N  
ATOM    380  CA  HIS A  56      48.613   4.103  40.197  1.00 25.31           C  
ATOM    381  C   HIS A  56      47.827   5.406  40.107  1.00 27.79           C  
ATOM    382  O   HIS A  56      47.266   5.910  41.099  1.00 24.31           O  
ATOM    383  CB  HIS A  56      47.767   2.891  39.797  1.00 26.50           C  
ATOM    384  CG  HIS A  56      48.583   1.677  39.457  1.00 29.61           C  
ATOM    385  ND1 HIS A  56      48.747   1.229  38.165  1.00 31.29           N  
ATOM    386  CD2 HIS A  56      49.300   0.833  40.244  1.00 28.02           C  
ATOM    387  CE1 HIS A  56      49.520   0.152  38.168  1.00 31.32           C  
ATOM    388  NE2 HIS A  56      49.873  -0.104  39.414  1.00 28.46           N  
ATOM    389  N   LYS A  57      47.827   5.943  38.899  1.00 26.57           N  
ATOM    390  CA  LYS A  57      47.408   7.307  38.602  1.00 32.08           C  
ATOM    391  C   LYS A  57      45.944   7.588  38.937  1.00 28.43           C  
ATOM    392  O   LYS A  57      45.621   8.628  39.486  1.00 31.32           O  
ATOM    393  CB  LYS A  57      47.665   7.598  37.114  1.00 29.88           C  
ATOM    394  CG  LYS A  57      48.172   8.998  36.823  1.00 40.81           C  
ATOM    395  CD  LYS A  57      48.264   9.287  35.308  1.00 46.86           C  
ATOM    396  CE  LYS A  57      46.932   9.075  34.574  1.00 51.57           C  
ATOM    397  NZ  LYS A  57      46.902   9.713  33.204  1.00 51.63           N  
ATOM    398  N   SER A  58      45.065   6.644  38.634  1.00 25.63           N  
ATOM    399  CA  SER A  58      43.635   6.892  38.733  1.00 27.63           C  
ATOM    400  C   SER A  58      42.998   6.219  39.955  1.00 28.75           C  
ATOM    401  O   SER A  58      43.384   5.112  40.341  1.00 27.40           O  
ATOM    402  CB  SER A  58      42.963   6.426  37.440  1.00 27.04           C  
ATOM    403  OG  SER A  58      41.565   6.453  37.550  1.00 29.94           O  
ATOM    404  N   GLY A  59      42.039   6.907  40.579  1.00 26.39           N  
ATOM    405  CA  GLY A  59      41.261   6.346  41.670  1.00 23.77           C  
ATOM    406  C   GLY A  59      40.003   5.614  41.196  1.00 28.97           C  
ATOM    407  O   GLY A  59      39.243   5.077  42.008  1.00 25.62           O  
ATOM    408  N   ASP A  60      39.795   5.596  39.880  1.00 26.98           N  
ATOM    409  CA  ASP A  60      38.636   4.955  39.234  1.00 30.09           C  
ATOM    410  C   ASP A  60      38.715   3.440  39.373  1.00 25.89           C  
ATOM    411  O   ASP A  60      39.728   2.864  39.029  1.00 26.95           O  
ATOM    412  CB  ASP A  60      38.607   5.356  37.745  1.00 25.15           C  
ATOM    413  CG  ASP A  60      37.319   4.941  37.013  1.00 29.36           C  
ATOM    414  OD1 ASP A  60      36.473   4.212  37.564  1.00 29.21           O  
ATOM    415  OD2 ASP A  60      37.170   5.348  35.838  1.00 32.26           O  
ATOM    416  N   ARG A  61      37.668   2.783  39.876  1.00 28.66           N  
ATOM    417  CA  ARG A  61      37.693   1.317  39.921  1.00 29.81           C  
ATOM    418  C   ARG A  61      36.456   0.694  39.283  1.00 35.51           C  
ATOM    419  O   ARG A  61      36.080  -0.438  39.610  1.00 34.34           O  
ATOM    420  CB  ARG A  61      37.839   0.796  41.361  1.00 29.00           C  
ATOM    421  CG  ARG A  61      39.118   1.268  42.078  1.00 28.32           C  
ATOM    422  CD  ARG A  61      39.386   0.495  43.360  1.00 27.20           C  
ATOM    423  NE  ARG A  61      38.332   0.684  44.350  1.00 23.72           N  
ATOM    424  CZ  ARG A  61      38.225  -0.022  45.473  1.00 26.78           C  
ATOM    425  NH1 ARG A  61      39.122  -0.965  45.765  1.00 26.89           N  
ATOM    426  NH2 ARG A  61      37.219   0.212  46.302  1.00 24.33           N  
ATOM    427  N   ARG A  62      35.840   1.408  38.348  1.00 32.31           N  
ATOM    428  CA  ARG A  62      34.655   0.872  37.678  1.00 32.61           C  
ATOM    429  C   ARG A  62      34.935  -0.445  36.943  1.00 30.08           C  
ATOM    430  O   ARG A  62      34.081  -1.309  36.897  1.00 33.07           O  
ATOM    431  CB  ARG A  62      34.086   1.916  36.730  1.00 31.11           C  
ATOM    432  CG  ARG A  62      33.337   3.003  37.468  1.00 28.99           C  
ATOM    433  CD  ARG A  62      32.857   4.077  36.519  1.00 28.82           C  
ATOM    434  NE  ARG A  62      33.985   4.837  36.007  1.00 35.06           N  
ATOM    435  CZ  ARG A  62      33.878   5.856  35.165  1.00 29.47           C  
ATOM    436  NH1 ARG A  62      32.681   6.230  34.738  1.00 31.36           N  
ATOM    437  NH2 ARG A  62      34.968   6.498  34.755  1.00 28.36           N  
ATOM    438  N   ASN A  63      36.138  -0.629  36.412  1.00 30.71           N  
ATOM    439  CA  ASN A  63      36.480  -1.928  35.830  1.00 38.89           C  
ATOM    440  C   ASN A  63      37.374  -2.748  36.768  1.00 38.01           C  
ATOM    441  O   ASN A  63      38.208  -3.529  36.319  1.00 41.95           O  
ATOM    442  CB  ASN A  63      37.160  -1.736  34.468  1.00 37.25           C  
ATOM    443  CG  ASN A  63      37.320  -3.032  33.696  1.00 51.34           C  
ATOM    444  OD1 ASN A  63      36.739  -4.059  34.058  1.00 55.71           O  
ATOM    445  ND2 ASN A  63      38.125  -2.995  32.628  1.00 48.76           N  
ATOM    446  N   GLY A  64      37.202  -2.579  38.075  1.00 38.65           N  
ATOM    447  CA  GLY A  64      38.097  -3.224  39.018  1.00 35.60           C  
ATOM    448  C   GLY A  64      39.447  -2.528  38.982  1.00 37.72           C  
ATOM    449  O   GLY A  64      39.511  -1.340  38.672  1.00 35.13           O  
ATOM    450  N   CYS A  65      40.525  -3.259  39.276  1.00 32.73           N  
ATOM    451  CA  CYS A  65      41.848  -2.649  39.427  1.00 30.37           C  
ATOM    452  C   CYS A  65      42.428  -2.170  38.114  1.00 33.03           C  
ATOM    453  O   CYS A  65      43.381  -1.370  38.095  1.00 30.91           O  
ATOM    454  CB  CYS A  65      42.818  -3.639  40.086  1.00 29.21           C  
ATOM    455  SG  CYS A  65      42.272  -4.154  41.743  1.00 34.56           S  
ATOM    456  N   THR A  66      41.873  -2.667  37.012  1.00 31.06           N  
ATOM    457  CA  THR A  66      42.322  -2.249  35.682  1.00 33.05           C  
ATOM    458  C   THR A  66      42.092  -0.754  35.453  1.00 28.39           C  
ATOM    459  O   THR A  66      42.860  -0.101  34.760  1.00 30.66           O  
ATOM    460  CB  THR A  66      41.600  -3.033  34.548  1.00 33.36           C  
ATOM    461  OG1 THR A  66      41.511  -4.421  34.893  1.00 48.75           O  
ATOM    462  CG2 THR A  66      42.361  -2.896  33.266  1.00 38.96           C  
ATOM    463  N   SER A  67      41.029  -0.216  36.029  1.00 31.64           N  
ATOM    464  CA  SER A  67      40.689   1.188  35.814  1.00 31.64           C  
ATOM    465  C   SER A  67      41.653   2.156  36.499  1.00 34.77           C  
ATOM    466  O   SER A  67      41.645   3.347  36.198  1.00 32.22           O  
ATOM    467  CB  SER A  67      39.287   1.475  36.324  1.00 32.45           C  
ATOM    468  OG  SER A  67      38.362   0.574  35.787  1.00 35.70           O  
HETATM  469  N   MSE A  68      42.468   1.665  37.436  1.00 29.81           N  
HETATM  470  CA  MSE A  68      43.344   2.583  38.165  1.00 32.51           C  
HETATM  471  C   MSE A  68      44.505   3.048  37.268  1.00 28.81           C  
HETATM  472  O   MSE A  68      45.348   3.843  37.688  1.00 27.55           O  
HETATM  473  CB  MSE A  68      43.850   1.944  39.459  1.00 25.04           C  
HETATM  474  CG  MSE A  68      42.729   1.322  40.292  1.00 30.32           C  
HETATM  475 SE   MSE A  68      43.061   1.336  42.234  1.00 41.26          SE  
HETATM  476  CE  MSE A  68      42.161   3.035  42.628  1.00 25.99           C  
ATOM    477  N   GLY A  69      44.528   2.576  36.026  1.00 29.26           N  
ATOM    478  CA  GLY A  69      45.489   3.080  35.049  1.00 26.60           C  
ATOM    479  C   GLY A  69      46.927   2.665  35.313  1.00 32.48           C  
ATOM    480  O   GLY A  69      47.178   1.700  36.046  1.00 32.85           O  
ATOM    481  N   PRO A  70      47.883   3.406  34.729  1.00 33.14           N  
ATOM    482  CA  PRO A  70      49.319   3.130  34.802  1.00 28.84           C  
ATOM    483  C   PRO A  70      49.962   3.576  36.105  1.00 29.91           C  
ATOM    484  O   PRO A  70      49.310   4.227  36.940  1.00 29.29           O  
ATOM    485  CB  PRO A  70      49.886   3.944  33.624  1.00 32.35           C  
ATOM    486  CG  PRO A  70      48.957   5.099  33.507  1.00 30.72           C  
ATOM    487  CD  PRO A  70      47.593   4.588  33.888  1.00 33.88           C  
ATOM    488  N   HIS A  71      51.232   3.220  36.272  1.00 29.25           N  
ATOM    489  CA  HIS A  71      52.038   3.685  37.396  1.00 32.95           C  
ATOM    490  C   HIS A  71      51.976   5.192  37.470  1.00 33.05           C  
ATOM    491  O   HIS A  71      51.969   5.868  36.443  1.00 31.89           O  
ATOM    492  CB  HIS A  71      53.501   3.241  37.267  1.00 32.94           C  
ATOM    493  CG  HIS A  71      53.694   1.760  37.380  1.00 38.59           C  
ATOM    494  ND1 HIS A  71      52.669   0.900  37.691  1.00 40.25           N  
ATOM    495  CD2 HIS A  71      54.805   0.994  37.238  1.00 41.58           C  
ATOM    496  CE1 HIS A  71      53.132  -0.342  37.726  1.00 40.47           C  
ATOM    497  NE2 HIS A  71      54.423  -0.308  37.453  1.00 42.67           N  
ATOM    498  N   PHE A  72      51.914   5.713  38.684  1.00 30.48           N  
ATOM    499  CA  PHE A  72      51.895   7.145  38.882  1.00 33.00           C  
ATOM    500  C   PHE A  72      53.330   7.640  38.999  1.00 39.17           C  
ATOM    501  O   PHE A  72      54.012   7.383  39.991  1.00 41.47           O  
ATOM    502  CB  PHE A  72      51.067   7.500  40.125  1.00 33.09           C  
ATOM    503  CG  PHE A  72      50.936   8.978  40.372  1.00 34.38           C  
ATOM    504  CD1 PHE A  72      50.383   9.812  39.408  1.00 34.00           C  
ATOM    505  CD2 PHE A  72      51.353   9.530  41.573  1.00 32.16           C  
ATOM    506  CE1 PHE A  72      50.259  11.182  39.642  1.00 35.82           C  
ATOM    507  CE2 PHE A  72      51.232  10.895  41.817  1.00 34.49           C  
ATOM    508  CZ  PHE A  72      50.691  11.723  40.846  1.00 33.07           C  
ATOM    509  N   ASN A  73      53.788   8.342  37.969  1.00 44.31           N  
ATOM    510  CA  ASN A  73      55.162   8.839  37.909  1.00 54.64           C  
ATOM    511  C   ASN A  73      55.188  10.270  37.399  1.00 54.61           C  
ATOM    512  O   ASN A  73      55.637  10.512  36.281  1.00 52.18           O  
ATOM    513  CB  ASN A  73      56.027   7.943  37.004  1.00 56.49           C  
ATOM    514  CG  ASN A  73      56.710   6.805  37.771  1.00 62.19           C  
ATOM    515  OD1 ASN A  73      56.997   6.926  38.965  1.00 62.11           O  
ATOM    516  ND2 ASN A  73      56.980   5.699  37.078  1.00 64.35           N  
ATOM    517  N   PRO A  74      54.713  11.222  38.224  1.00 52.88           N  
ATOM    518  CA  PRO A  74      54.422  12.595  37.784  1.00 57.30           C  
ATOM    519  C   PRO A  74      55.626  13.359  37.226  1.00 61.09           C  
ATOM    520  O   PRO A  74      55.479  14.079  36.230  1.00 61.69           O  
ATOM    521  CB  PRO A  74      53.902  13.271  39.062  1.00 52.21           C  
ATOM    522  CG  PRO A  74      54.403  12.436  40.181  1.00 48.90           C  
ATOM    523  CD  PRO A  74      54.439  11.035  39.659  1.00 46.22           C  
ATOM    524  N   PHE A  75      56.791  13.196  37.847  1.00 58.95           N  
ATOM    525  CA  PHE A  75      57.962  13.970  37.465  1.00 63.33           C  
ATOM    526  C   PHE A  75      58.701  13.386  36.267  1.00 69.89           C  
ATOM    527  O   PHE A  75      59.579  14.043  35.711  1.00 77.23           O  
ATOM    528  CB  PHE A  75      58.941  14.076  38.629  1.00 62.70           C  
ATOM    529  CG  PHE A  75      58.386  14.755  39.834  1.00 61.41           C  
ATOM    530  CD1 PHE A  75      58.377  16.137  39.924  1.00 61.46           C  
ATOM    531  CD2 PHE A  75      57.912  14.009  40.907  1.00 61.88           C  
ATOM    532  CE1 PHE A  75      57.881  16.769  41.061  1.00 59.21           C  
ATOM    533  CE2 PHE A  75      57.413  14.632  42.044  1.00 57.09           C  
ATOM    534  CZ  PHE A  75      57.395  16.010  42.122  1.00 58.13           C  
ATOM    535  N   ASN A  76      58.353  12.155  35.889  1.00 73.34           N  
ATOM    536  CA  ASN A  76      59.089  11.385  34.879  1.00 71.22           C  
ATOM    537  C   ASN A  76      60.560  11.183  35.260  1.00 78.29           C  
ATOM    538  O   ASN A  76      61.457  11.839  34.724  1.00 82.26           O  
ATOM    539  CB  ASN A  76      58.988  12.053  33.503  1.00 75.13           C  
ATOM    540  CG  ASN A  76      57.591  11.971  32.920  1.00 81.26           C  
ATOM    541  OD1 ASN A  76      56.799  11.104  33.301  1.00 82.20           O  
ATOM    542  ND2 ASN A  76      57.278  12.871  31.990  1.00 78.08           N  
ATOM    543  N   LEU A  89      58.539   6.964  40.673  1.00 61.49           N  
ATOM    544  CA  LEU A  89      58.675   7.085  42.122  1.00 63.28           C  
ATOM    545  C   LEU A  89      57.339   6.847  42.870  1.00 65.24           C  
ATOM    546  O   LEU A  89      57.247   7.038  44.092  1.00 60.07           O  
ATOM    547  CB  LEU A  89      59.282   8.452  42.497  1.00 69.91           C  
ATOM    548  CG  LEU A  89      60.786   8.731  42.240  1.00 74.69           C  
ATOM    549  CD1 LEU A  89      61.278   8.438  40.814  1.00 67.24           C  
ATOM    550  CD2 LEU A  89      61.148  10.158  42.629  1.00 69.55           C  
ATOM    551  N   GLY A  90      56.330   6.365  42.141  1.00 56.15           N  
ATOM    552  CA  GLY A  90      55.149   5.768  42.753  1.00 50.33           C  
ATOM    553  C   GLY A  90      55.440   4.294  43.019  1.00 49.95           C  
ATOM    554  O   GLY A  90      54.554   3.494  43.346  1.00 37.21           O  
ATOM    555  N   ASP A  91      56.718   3.957  42.841  1.00 57.36           N  
ATOM    556  CA  ASP A  91      57.283   2.639  43.094  1.00 49.96           C  
ATOM    557  C   ASP A  91      57.686   2.520  44.567  1.00 53.83           C  
ATOM    558  O   ASP A  91      58.647   3.155  45.030  1.00 49.42           O  
ATOM    559  CB  ASP A  91      58.484   2.403  42.167  1.00 51.82           C  
ATOM    560  CG  ASP A  91      59.197   1.079  42.432  1.00 61.82           C  
ATOM    561  OD1 ASP A  91      58.566   0.119  42.949  1.00 57.32           O  
ATOM    562  OD2 ASP A  91      60.409   1.004  42.112  1.00 68.33           O  
ATOM    563  N   LEU A  92      56.918   1.717  45.300  1.00 43.21           N  
ATOM    564  CA  LEU A  92      57.157   1.496  46.710  1.00 39.03           C  
ATOM    565  C   LEU A  92      58.034   0.262  46.872  1.00 38.92           C  
ATOM    566  O   LEU A  92      58.500  -0.024  47.958  1.00 38.77           O  
ATOM    567  CB  LEU A  92      55.836   1.321  47.453  1.00 32.89           C  
ATOM    568  CG  LEU A  92      54.724   2.328  47.126  1.00 36.37           C  
ATOM    569  CD1 LEU A  92      53.560   2.160  48.074  1.00 36.11           C  
ATOM    570  CD2 LEU A  92      55.207   3.762  47.142  1.00 33.63           C  
ATOM    571  N   GLY A  93      58.260  -0.452  45.771  1.00 37.35           N  
ATOM    572  CA  GLY A  93      59.029  -1.683  45.787  1.00 35.27           C  
ATOM    573  C   GLY A  93      58.170  -2.890  46.141  1.00 37.12           C  
ATOM    574  O   GLY A  93      56.949  -2.884  45.959  1.00 38.43           O  
ATOM    575  N   ASN A  94      58.805  -3.930  46.667  1.00 30.39           N  
ATOM    576  CA  ASN A  94      58.109  -5.169  46.980  1.00 30.79           C  
ATOM    577  C   ASN A  94      57.675  -5.231  48.427  1.00 33.99           C  
ATOM    578  O   ASN A  94      58.414  -4.810  49.321  1.00 34.36           O  
ATOM    579  CB  ASN A  94      59.004  -6.376  46.679  1.00 31.68           C  
ATOM    580  CG  ASN A  94      59.252  -6.568  45.203  1.00 34.34           C  
ATOM    581  OD1 ASN A  94      58.321  -6.573  44.402  1.00 32.41           O  
ATOM    582  ND2 ASN A  94      60.517  -6.734  44.832  1.00 29.46           N  
ATOM    583  N   ILE A  95      56.480  -5.761  48.663  1.00 32.33           N  
ATOM    584  CA  ILE A  95      56.116  -6.198  50.002  1.00 31.01           C  
ATOM    585  C   ILE A  95      56.238  -7.705  50.060  1.00 32.53           C  
ATOM    586  O   ILE A  95      56.285  -8.381  49.028  1.00 29.70           O  
ATOM    587  CB  ILE A  95      54.683  -5.797  50.398  1.00 31.84           C  
ATOM    588  CG1 ILE A  95      53.677  -6.536  49.516  1.00 31.74           C  
ATOM    589  CG2 ILE A  95      54.516  -4.271  50.347  1.00 29.34           C  
ATOM    590  CD1 ILE A  95      52.263  -6.280  49.862  1.00 35.33           C  
ATOM    591  N   VAL A  96      56.299  -8.231  51.275  1.00 32.82           N  
ATOM    592  CA  VAL A  96      56.328  -9.668  51.466  1.00 33.43           C  
ATOM    593  C   VAL A  96      55.079 -10.100  52.222  1.00 35.01           C  
ATOM    594  O   VAL A  96      54.785  -9.583  53.300  1.00 31.30           O  
ATOM    595  CB  VAL A  96      57.592 -10.115  52.232  1.00 33.50           C  
ATOM    596  CG1 VAL A  96      57.548 -11.609  52.510  1.00 28.73           C  
ATOM    597  CG2 VAL A  96      58.851  -9.745  51.447  1.00 25.02           C  
ATOM    598  N   VAL A  97      54.331 -11.031  51.646  1.00 28.44           N  
ATOM    599  CA  VAL A  97      53.195 -11.604  52.345  1.00 31.98           C  
ATOM    600  C   VAL A  97      53.633 -12.907  53.023  1.00 33.17           C  
ATOM    601  O   VAL A  97      54.323 -13.713  52.412  1.00 37.09           O  
ATOM    602  CB  VAL A  97      52.014 -11.870  51.385  1.00 33.12           C  
ATOM    603  CG1 VAL A  97      50.929 -12.650  52.086  1.00 29.99           C  
ATOM    604  CG2 VAL A  97      51.463 -10.547  50.813  1.00 32.07           C  
ATOM    605  N   ASN A  98      53.249 -13.093  54.282  1.00 36.04           N  
ATOM    606  CA  ASN A  98      53.546 -14.320  55.023  1.00 40.53           C  
ATOM    607  C   ASN A  98      52.769 -15.523  54.515  1.00 42.88           C  
ATOM    608  O   ASN A  98      51.827 -15.390  53.721  1.00 38.81           O  
ATOM    609  CB  ASN A  98      53.228 -14.148  56.506  1.00 38.60           C  
ATOM    610  CG  ASN A  98      54.255 -13.330  57.223  1.00 52.07           C  
ATOM    611  OD1 ASN A  98      55.456 -13.460  56.973  1.00 58.62           O  
ATOM    612  ND2 ASN A  98      53.796 -12.465  58.122  1.00 52.99           N  
ATOM    613  N   ASN A  99      53.131 -16.693  55.023  1.00 37.58           N  
ATOM    614  CA  ASN A  99      52.470 -17.915  54.615  1.00 41.80           C  
ATOM    615  C   ASN A  99      51.023 -18.012  55.068  1.00 35.85           C  
ATOM    616  O   ASN A  99      50.268 -18.819  54.540  1.00 46.98           O  
ATOM    617  CB  ASN A  99      53.263 -19.125  55.096  1.00 47.84           C  
ATOM    618  CG  ASN A  99      54.312 -19.548  54.088  1.00 58.15           C  
ATOM    619  OD1 ASN A  99      54.033 -20.344  53.186  1.00 63.21           O  
ATOM    620  ND2 ASN A  99      55.520 -19.005  54.221  1.00 61.29           N  
ATOM    621  N   ASN A 100      50.620 -17.185  56.025  1.00 39.54           N  
ATOM    622  CA  ASN A 100      49.205 -17.099  56.384  1.00 36.28           C  
ATOM    623  C   ASN A 100      48.449 -16.029  55.575  1.00 36.56           C  
ATOM    624  O   ASN A 100      47.307 -15.688  55.895  1.00 38.22           O  
ATOM    625  CB  ASN A 100      49.046 -16.818  57.883  1.00 41.67           C  
ATOM    626  CG  ASN A 100      49.641 -15.484  58.288  1.00 46.39           C  
ATOM    627  OD1 ASN A 100      50.158 -14.738  57.447  1.00 44.16           O  
ATOM    628  ND2 ASN A 100      49.583 -15.175  59.583  1.00 47.71           N  
ATOM    629  N   GLY A 101      49.087 -15.493  54.538  1.00 38.47           N  
ATOM    630  CA  GLY A 101      48.428 -14.538  53.658  1.00 36.47           C  
ATOM    631  C   GLY A 101      48.394 -13.101  54.160  1.00 36.45           C  
ATOM    632  O   GLY A 101      47.803 -12.225  53.508  1.00 35.10           O  
ATOM    633  N   GLU A 102      49.045 -12.850  55.296  1.00 35.85           N  
ATOM    634  CA  GLU A 102      49.105 -11.512  55.879  1.00 35.85           C  
ATOM    635  C   GLU A 102      50.402 -10.774  55.565  1.00 34.12           C  
ATOM    636  O   GLU A 102      51.451 -11.378  55.326  1.00 33.54           O  
ATOM    637  CB  GLU A 102      48.936 -11.574  57.404  1.00 33.63           C  
ATOM    638  CG  GLU A 102      47.618 -12.123  57.847  1.00 36.74           C  
ATOM    639  CD  GLU A 102      47.356 -11.879  59.312  1.00 47.33           C  
ATOM    640  OE1 GLU A 102      46.354 -12.414  59.828  1.00 53.74           O  
ATOM    641  OE2 GLU A 102      48.144 -11.143  59.948  1.00 50.24           O  
ATOM    642  N   CYS A 103      50.306  -9.452  55.577  1.00 28.27           N  
ATOM    643  CA  CYS A 103      51.470  -8.593  55.494  1.00 32.84           C  
ATOM    644  C   CYS A 103      51.298  -7.458  56.492  1.00 32.55           C  
ATOM    645  O   CYS A 103      50.383  -6.641  56.344  1.00 31.02           O  
ATOM    646  CB  CYS A 103      51.654  -8.034  54.080  1.00 27.97           C  
ATOM    647  SG  CYS A 103      53.056  -6.886  53.940  1.00 32.02           S  
ATOM    648  N   ASN A 104      52.146  -7.410  57.517  1.00 25.60           N  
ATOM    649  CA  ASN A 104      52.081  -6.291  58.453  1.00 31.37           C  
ATOM    650  C   ASN A 104      53.374  -5.484  58.497  1.00 31.21           C  
ATOM    651  O   ASN A 104      53.672  -4.798  59.484  1.00 31.03           O  
ATOM    652  CB  ASN A 104      51.713  -6.779  59.859  1.00 36.76           C  
ATOM    653  CG  ASN A 104      50.283  -7.314  59.936  1.00 39.41           C  
ATOM    654  OD1 ASN A 104      49.328  -6.559  60.179  1.00 35.75           O  
ATOM    655  ND2 ASN A 104      50.133  -8.625  59.744  1.00 37.89           N  
ATOM    656  N   GLU A 105      54.118  -5.536  57.402  1.00 29.92           N  
ATOM    657  CA  GLU A 105      55.396  -4.855  57.331  1.00 33.27           C  
ATOM    658  C   GLU A 105      55.229  -3.338  57.248  1.00 32.01           C  
ATOM    659  O   GLU A 105      54.149  -2.824  56.918  1.00 30.02           O  
ATOM    660  CB  GLU A 105      56.204  -5.392  56.140  1.00 34.64           C  
ATOM    661  CG  GLU A 105      56.298  -4.527  54.916  1.00 33.59           C  
ATOM    662  CD  GLU A 105      56.987  -5.264  53.746  1.00 38.15           C  
ATOM    663  OE1 GLU A 105      56.419  -6.260  53.249  1.00 34.84           O  
ATOM    664  OE2 GLU A 105      58.090  -4.859  53.322  1.00 35.09           O  
ATOM    665  N   ILE A 106      56.298  -2.630  57.588  1.00 27.07           N  
ATOM    666  CA  ILE A 106      56.316  -1.185  57.515  1.00 30.19           C  
ATOM    667  C   ILE A 106      57.462  -0.704  56.639  1.00 32.62           C  
ATOM    668  O   ILE A 106      58.590  -1.161  56.777  1.00 33.02           O  
ATOM    669  CB  ILE A 106      56.464  -0.558  58.891  1.00 28.52           C  
ATOM    670  CG1 ILE A 106      55.283  -0.941  59.783  1.00 33.46           C  
ATOM    671  CG2 ILE A 106      56.591   0.945  58.768  1.00 28.43           C  
ATOM    672  CD1 ILE A 106      55.377  -0.338  61.128  1.00 31.53           C  
ATOM    673  N   ILE A 107      57.166   0.220  55.737  1.00 31.24           N  
ATOM    674  CA  ILE A 107      58.206   0.860  54.951  1.00 34.42           C  
ATOM    675  C   ILE A 107      58.087   2.369  55.053  1.00 35.21           C  
ATOM    676  O   ILE A 107      57.049   2.903  55.460  1.00 32.99           O  
ATOM    677  CB  ILE A 107      58.134   0.453  53.482  1.00 35.16           C  
ATOM    678  CG1 ILE A 107      56.830   0.942  52.871  1.00 31.61           C  
ATOM    679  CG2 ILE A 107      58.264  -1.063  53.334  1.00 35.79           C  
ATOM    680  CD1 ILE A 107      56.748   0.698  51.368  1.00 35.76           C  
ATOM    681  N   CYS A 108      59.149   3.062  54.670  1.00 35.37           N  
ATOM    682  CA  CYS A 108      59.146   4.510  54.696  1.00 33.88           C  
ATOM    683  C   CYS A 108      59.712   4.930  53.352  1.00 38.86           C  
ATOM    684  O   CYS A 108      60.797   4.498  52.970  1.00 38.89           O  
ATOM    685  CB  CYS A 108      59.962   5.055  55.880  1.00 38.98           C  
ATOM    686  SG  CYS A 108      59.282   6.593  56.649  1.00 52.94           S  
ATOM    687  N   VAL A 109      58.953   5.724  52.605  1.00 33.64           N  
ATOM    688  CA  VAL A 109      59.350   6.109  51.261  1.00 35.34           C  
ATOM    689  C   VAL A 109      59.619   7.605  51.220  1.00 38.97           C  
ATOM    690  O   VAL A 109      58.763   8.402  51.612  1.00 36.02           O  
ATOM    691  CB  VAL A 109      58.272   5.743  50.226  1.00 36.45           C  
ATOM    692  CG1 VAL A 109      58.743   6.071  48.794  1.00 33.88           C  
ATOM    693  CG2 VAL A 109      57.896   4.259  50.349  1.00 36.14           C  
ATOM    694  N   LYS A 110      60.823   7.979  50.795  1.00 36.05           N  
ATOM    695  CA  LYS A 110      61.129   9.378  50.519  1.00 44.63           C  
ATOM    696  C   LYS A 110      60.331   9.844  49.309  1.00 42.22           C  
ATOM    697  O   LYS A 110      60.131   9.084  48.355  1.00 47.34           O  
ATOM    698  CB  LYS A 110      62.619   9.576  50.246  1.00 46.85           C  
ATOM    699  CG  LYS A 110      63.514   9.441  51.437  1.00 46.92           C  
ATOM    700  CD  LYS A 110      64.917   9.896  51.068  1.00 56.72           C  
ATOM    701  CE  LYS A 110      65.981   8.920  51.582  1.00 67.08           C  
ATOM    702  NZ  LYS A 110      65.493   8.065  52.709  1.00 69.19           N  
ATOM    703  N   TYR A 111      59.876  11.086  49.360  1.00 42.59           N  
ATOM    704  CA  TYR A 111      59.225  11.740  48.227  1.00 46.85           C  
ATOM    705  C   TYR A 111      58.002  10.967  47.735  1.00 43.83           C  
ATOM    706  O   TYR A 111      57.895  10.604  46.560  1.00 47.79           O  
ATOM    707  CB  TYR A 111      60.233  11.956  47.098  1.00 44.20           C  
ATOM    708  CG  TYR A 111      61.412  12.800  47.546  1.00 57.64           C  
ATOM    709  CD1 TYR A 111      61.268  13.733  48.573  1.00 66.01           C  
ATOM    710  CD2 TYR A 111      62.670  12.655  46.965  1.00 63.44           C  
ATOM    711  CE1 TYR A 111      62.336  14.507  49.002  1.00 72.53           C  
ATOM    712  CE2 TYR A 111      63.748  13.426  47.386  1.00 66.74           C  
ATOM    713  CZ  TYR A 111      63.574  14.352  48.402  1.00 75.51           C  
ATOM    714  OH  TYR A 111      64.635  15.123  48.825  1.00 82.99           O  
ATOM    715  N   LEU A 112      57.080  10.744  48.662  1.00 34.15           N  
ATOM    716  CA  LEU A 112      55.777  10.166  48.375  1.00 32.96           C  
ATOM    717  C   LEU A 112      54.732  11.040  49.074  1.00 28.01           C  
ATOM    718  O   LEU A 112      54.242  10.705  50.158  1.00 28.99           O  
ATOM    719  CB  LEU A 112      55.711   8.707  48.849  1.00 30.94           C  
ATOM    720  CG  LEU A 112      54.521   7.851  48.408  1.00 31.33           C  
ATOM    721  CD1 LEU A 112      54.661   7.454  46.922  1.00 29.13           C  
ATOM    722  CD2 LEU A 112      54.363   6.617  49.328  1.00 27.13           C  
ATOM    723  N   PRO A 113      54.401  12.185  48.462  1.00 28.03           N  
ATOM    724  CA  PRO A 113      53.557  13.180  49.134  1.00 30.35           C  
ATOM    725  C   PRO A 113      52.106  12.741  49.240  1.00 27.95           C  
ATOM    726  O   PRO A 113      51.558  12.206  48.273  1.00 26.81           O  
ATOM    727  CB  PRO A 113      53.687  14.418  48.230  1.00 28.32           C  
ATOM    728  CG  PRO A 113      53.975  13.837  46.875  1.00 31.44           C  
ATOM    729  CD  PRO A 113      54.801  12.611  47.107  1.00 30.41           C  
ATOM    730  N   LEU A 114      51.485  12.988  50.389  1.00 25.36           N  
ATOM    731  CA  LEU A 114      50.076  12.685  50.561  1.00 25.00           C  
ATOM    732  C   LEU A 114      49.223  13.881  50.121  1.00 28.00           C  
ATOM    733  O   LEU A 114      48.090  13.724  49.664  1.00 27.36           O  
ATOM    734  CB  LEU A 114      49.777  12.311  52.020  1.00 25.58           C  
ATOM    735  CG  LEU A 114      50.466  11.046  52.566  1.00 27.06           C  
ATOM    736  CD1 LEU A 114      49.878  10.675  53.916  1.00 25.36           C  
ATOM    737  CD2 LEU A 114      50.320   9.870  51.604  1.00 21.02           C  
ATOM    738  N   THR A 115      49.776  15.078  50.253  1.00 25.78           N  
ATOM    739  CA  THR A 115      49.025  16.292  49.944  1.00 30.16           C  
ATOM    740  C   THR A 115      49.795  17.133  48.941  1.00 30.86           C  
ATOM    741  O   THR A 115      50.976  16.887  48.690  1.00 29.03           O  
ATOM    742  CB  THR A 115      48.754  17.134  51.205  1.00 31.62           C  
ATOM    743  OG1 THR A 115      49.998  17.440  51.838  1.00 30.67           O  
ATOM    744  CG2 THR A 115      47.881  16.379  52.174  1.00 30.08           C  
ATOM    745  N   GLY A 116      49.131  18.123  48.358  1.00 31.44           N  
ATOM    746  CA  GLY A 116      49.811  19.013  47.440  1.00 33.85           C  
ATOM    747  C   GLY A 116      49.677  18.538  46.005  1.00 40.30           C  
ATOM    748  O   GLY A 116      49.025  17.523  45.725  1.00 35.02           O  
ATOM    749  N   SER A 117      50.328  19.253  45.097  1.00 42.17           N  
ATOM    750  CA  SER A 117      50.043  19.128  43.664  1.00 44.12           C  
ATOM    751  C   SER A 117      50.304  17.723  43.073  1.00 46.70           C  
ATOM    752  O   SER A 117      49.556  17.295  42.195  1.00 42.34           O  
ATOM    753  CB  SER A 117      50.837  20.194  42.895  1.00 44.36           C  
ATOM    754  OG  SER A 117      50.655  21.474  43.496  1.00 43.37           O  
ATOM    755  N   ASN A 118      51.319  16.995  43.560  1.00 37.81           N  
ATOM    756  CA  ASN A 118      51.525  15.603  43.113  1.00 37.02           C  
ATOM    757  C   ASN A 118      51.149  14.513  44.156  1.00 36.66           C  
ATOM    758  O   ASN A 118      51.736  13.421  44.209  1.00 33.67           O  
ATOM    759  CB  ASN A 118      52.969  15.434  42.673  1.00 37.65           C  
ATOM    760  CG  ASN A 118      53.285  16.276  41.451  1.00 44.85           C  
ATOM    761  OD1 ASN A 118      52.918  15.914  40.331  1.00 45.84           O  
ATOM    762  ND2 ASN A 118      53.912  17.432  41.663  1.00 42.74           N  
ATOM    763  N   GLN A 119      50.141  14.815  44.955  1.00 30.16           N  
ATOM    764  CA  GLN A 119      49.676  13.931  46.017  1.00 28.98           C  
ATOM    765  C   GLN A 119      49.221  12.557  45.525  1.00 27.80           C  
ATOM    766  O   GLN A 119      48.733  12.408  44.394  1.00 26.95           O  
ATOM    767  CB  GLN A 119      48.520  14.597  46.744  1.00 26.40           C  
ATOM    768  CG  GLN A 119      47.292  14.797  45.844  1.00 25.75           C  
ATOM    769  CD  GLN A 119      46.121  15.401  46.593  1.00 27.21           C  
ATOM    770  OE1 GLN A 119      46.069  15.367  47.820  1.00 27.62           O  
ATOM    771  NE2 GLN A 119      45.186  15.960  45.863  1.00 25.12           N  
ATOM    772  N   ILE A 120      49.333  11.553  46.390  1.00 25.56           N  
ATOM    773  CA  ILE A 120      48.791  10.243  46.047  1.00 24.28           C  
ATOM    774  C   ILE A 120      47.431   9.990  46.686  1.00 24.69           C  
ATOM    775  O   ILE A 120      46.774   8.995  46.365  1.00 23.00           O  
ATOM    776  CB  ILE A 120      49.747   9.114  46.440  1.00 22.04           C  
ATOM    777  CG1 ILE A 120      49.823   8.972  47.963  1.00 24.81           C  
ATOM    778  CG2 ILE A 120      51.120   9.371  45.822  1.00 24.84           C  
ATOM    779  CD1 ILE A 120      50.673   7.769  48.436  1.00 24.33           C  
ATOM    780  N   ILE A 121      47.006  10.866  47.594  1.00 23.91           N  
ATOM    781  CA  ILE A 121      45.644  10.780  48.113  1.00 23.66           C  
ATOM    782  C   ILE A 121      44.676  10.989  46.933  1.00 28.56           C  
ATOM    783  O   ILE A 121      44.860  11.901  46.133  1.00 22.98           O  
ATOM    784  CB  ILE A 121      45.374  11.816  49.237  1.00 25.60           C  
ATOM    785  CG1 ILE A 121      45.968  11.347  50.574  1.00 22.69           C  
ATOM    786  CG2 ILE A 121      43.886  12.028  49.424  1.00 23.92           C  
ATOM    787  CD1 ILE A 121      45.793  12.366  51.714  1.00 24.03           C  
ATOM    788  N   GLY A 122      43.679  10.113  46.805  1.00 21.66           N  
ATOM    789  CA  GLY A 122      42.739  10.191  45.710  1.00 20.37           C  
ATOM    790  C   GLY A 122      43.148   9.296  44.560  1.00 24.25           C  
ATOM    791  O   GLY A 122      42.422   9.150  43.577  1.00 24.56           O  
ATOM    792  N   ARG A 123      44.322   8.692  44.680  1.00 21.58           N  
ATOM    793  CA  ARG A 123      44.815   7.810  43.639  1.00 25.14           C  
ATOM    794  C   ARG A 123      44.820   6.368  44.145  1.00 26.22           C  
ATOM    795  O   ARG A 123      44.144   6.052  45.133  1.00 24.53           O  
ATOM    796  CB  ARG A 123      46.196   8.273  43.172  1.00 22.08           C  
ATOM    797  CG  ARG A 123      46.131   9.721  42.655  1.00 23.56           C  
ATOM    798  CD  ARG A 123      47.385  10.149  41.902  1.00 29.61           C  
ATOM    799  NE  ARG A 123      47.353  11.585  41.656  1.00 28.42           N  
ATOM    800  CZ  ARG A 123      46.694  12.161  40.652  1.00 29.34           C  
ATOM    801  NH1 ARG A 123      46.015  11.424  39.771  1.00 26.36           N  
ATOM    802  NH2 ARG A 123      46.722  13.478  40.522  1.00 26.50           N  
ATOM    803  N   GLY A 124      45.558   5.495  43.470  1.00 24.25           N  
ATOM    804  CA  GLY A 124      45.407   4.067  43.686  1.00 26.28           C  
ATOM    805  C   GLY A 124      46.633   3.359  44.214  1.00 25.25           C  
ATOM    806  O   GLY A 124      47.750   3.630  43.792  1.00 26.02           O  
ATOM    807  N   LEU A 125      46.409   2.460  45.168  1.00 26.82           N  
ATOM    808  CA  LEU A 125      47.437   1.533  45.625  1.00 27.42           C  
ATOM    809  C   LEU A 125      47.106   0.159  45.052  1.00 28.50           C  
ATOM    810  O   LEU A 125      46.008  -0.352  45.266  1.00 24.50           O  
ATOM    811  CB  LEU A 125      47.495   1.483  47.152  1.00 29.50           C  
ATOM    812  CG  LEU A 125      48.508   0.494  47.732  1.00 32.29           C  
ATOM    813  CD1 LEU A 125      49.875   0.891  47.311  1.00 24.97           C  
ATOM    814  CD2 LEU A 125      48.439   0.441  49.250  1.00 31.29           C  
ATOM    815  N   VAL A 126      48.026  -0.431  44.299  1.00 27.44           N  
ATOM    816  CA  VAL A 126      47.750  -1.728  43.685  1.00 26.07           C  
ATOM    817  C   VAL A 126      48.809  -2.742  44.113  1.00 27.81           C  
ATOM    818  O   VAL A 126      50.002  -2.442  44.080  1.00 26.13           O  
ATOM    819  CB  VAL A 126      47.697  -1.603  42.143  1.00 24.74           C  
ATOM    820  CG1 VAL A 126      47.617  -2.969  41.460  1.00 27.95           C  
ATOM    821  CG2 VAL A 126      46.522  -0.702  41.718  1.00 27.59           C  
ATOM    822  N   ILE A 127      48.371  -3.924  44.546  1.00 27.21           N  
ATOM    823  CA  ILE A 127      49.285  -5.038  44.780  1.00 25.09           C  
ATOM    824  C   ILE A 127      49.386  -5.874  43.496  1.00 30.25           C  
ATOM    825  O   ILE A 127      48.372  -6.317  42.960  1.00 30.97           O  
ATOM    826  CB  ILE A 127      48.822  -5.942  45.944  1.00 30.91           C  
ATOM    827  CG1 ILE A 127      48.489  -5.118  47.204  1.00 29.72           C  
ATOM    828  CG2 ILE A 127      49.866  -7.016  46.232  1.00 24.85           C  
ATOM    829  CD1 ILE A 127      49.592  -4.200  47.645  1.00 31.68           C  
ATOM    830  N   HIS A 128      50.596  -6.083  42.991  1.00 27.17           N  
ATOM    831  CA  HIS A 128      50.765  -6.867  41.767  1.00 29.56           C  
ATOM    832  C   HIS A 128      51.137  -8.326  42.033  1.00 34.24           C  
ATOM    833  O   HIS A 128      51.837  -8.633  43.001  1.00 29.27           O  
ATOM    834  CB  HIS A 128      51.814  -6.218  40.877  1.00 27.56           C  
ATOM    835  CG  HIS A 128      51.362  -4.923  40.278  1.00 30.72           C  
ATOM    836  ND1 HIS A 128      50.971  -4.808  38.963  1.00 37.32           N  
ATOM    837  CD2 HIS A 128      51.209  -3.692  40.826  1.00 29.10           C  
ATOM    838  CE1 HIS A 128      50.619  -3.557  38.716  1.00 36.25           C  
ATOM    839  NE2 HIS A 128      50.751  -2.861  39.832  1.00 32.84           N  
ATOM    840  N   GLU A 129      50.666  -9.217  41.163  1.00 35.69           N  
ATOM    841  CA  GLU A 129      50.929 -10.653  41.302  1.00 42.50           C  
ATOM    842  C   GLU A 129      52.424 -10.961  41.393  1.00 38.58           C  
ATOM    843  O   GLU A 129      52.882 -11.610  42.328  1.00 41.16           O  
ATOM    844  CB  GLU A 129      50.311 -11.432  40.134  1.00 43.02           C  
ATOM    845  CG  GLU A 129      50.592 -12.940  40.197  1.00 46.54           C  
ATOM    846  CD  GLU A 129      49.975 -13.611  41.426  1.00 60.78           C  
ATOM    847  OE1 GLU A 129      48.759 -13.932  41.386  1.00 61.48           O  
ATOM    848  OE2 GLU A 129      50.705 -13.823  42.432  1.00 59.43           O  
ATOM    849  N   LYS A 130      53.180 -10.465  40.429  1.00 33.80           N  
ATOM    850  CA  LYS A 130      54.611 -10.688  40.387  1.00 39.07           C  
ATOM    851  C   LYS A 130      55.385  -9.627  41.166  1.00 39.44           C  
ATOM    852  O   LYS A 130      54.912  -8.509  41.411  1.00 33.28           O  
ATOM    853  CB  LYS A 130      55.100 -10.739  38.928  1.00 42.10           C  
ATOM    854  CG  LYS A 130      54.160 -11.492  37.988  1.00 45.85           C  
ATOM    855  CD  LYS A 130      54.650 -11.463  36.543  1.00 58.24           C  
ATOM    856  CE  LYS A 130      53.949 -12.528  35.708  1.00 56.10           C  
ATOM    857  NZ  LYS A 130      52.464 -12.439  35.881  1.00 65.72           N  
ATOM    858  N   GLU A 131      56.593  -9.996  41.561  1.00 38.97           N  
ATOM    859  CA  GLU A 131      57.452  -9.081  42.280  1.00 37.37           C  
ATOM    860  C   GLU A 131      58.124  -8.166  41.277  1.00 35.04           C  
ATOM    861  O   GLU A 131      58.263  -8.532  40.114  1.00 34.09           O  
ATOM    862  CB  GLU A 131      58.488  -9.851  43.109  1.00 35.45           C  
ATOM    863  CG  GLU A 131      59.550 -10.600  42.295  1.00 37.76           C  
ATOM    864  CD  GLU A 131      60.319 -11.609  43.154  1.00 36.80           C  
ATOM    865  OE1 GLU A 131      59.750 -12.661  43.501  1.00 36.39           O  
ATOM    866  OE2 GLU A 131      61.479 -11.337  43.504  1.00 33.56           O  
ATOM    867  N   ASP A 132      58.492  -6.964  41.713  1.00 37.18           N  
ATOM    868  CA  ASP A 132      59.420  -6.127  40.949  1.00 37.48           C  
ATOM    869  C   ASP A 132      60.790  -6.796  40.904  1.00 39.76           C  
ATOM    870  O   ASP A 132      61.341  -7.170  41.942  1.00 41.38           O  
ATOM    871  CB  ASP A 132      59.576  -4.742  41.573  1.00 38.67           C  
ATOM    872  CG  ASP A 132      58.311  -3.912  41.513  1.00 40.65           C  
ATOM    873  OD1 ASP A 132      57.360  -4.289  40.794  1.00 44.67           O  
ATOM    874  OD2 ASP A 132      58.289  -2.856  42.180  1.00 44.24           O  
ATOM    875  N   ASP A 133      61.352  -6.932  39.714  1.00 43.34           N  
ATOM    876  CA  ASP A 133      62.693  -7.483  39.589  1.00 48.86           C  
ATOM    877  C   ASP A 133      63.738  -6.445  39.980  1.00 52.00           C  
ATOM    878  O   ASP A 133      64.551  -6.681  40.878  1.00 61.36           O  
ATOM    879  CB  ASP A 133      62.927  -7.981  38.162  1.00 48.62           C  
ATOM    880  CG  ASP A 133      61.989  -9.111  37.787  1.00 47.55           C  
ATOM    881  OD1 ASP A 133      61.692  -9.957  38.664  1.00 43.34           O  
ATOM    882  OD2 ASP A 133      61.532  -9.142  36.627  1.00 47.45           O  
ATOM    883  N   GLY A 149      52.214  -8.727  38.324  1.00 41.10           N  
ATOM    884  CA  GLY A 149      52.017  -8.290  36.960  1.00 49.56           C  
ATOM    885  C   GLY A 149      50.568  -7.910  36.766  1.00 55.29           C  
ATOM    886  O   GLY A 149      50.251  -6.739  36.544  1.00 56.60           O  
ATOM    887  N   ASP A 150      49.689  -8.907  36.836  1.00 54.19           N  
ATOM    888  CA  ASP A 150      48.268  -8.640  36.962  1.00 47.02           C  
ATOM    889  C   ASP A 150      47.986  -8.131  38.376  1.00 46.47           C  
ATOM    890  O   ASP A 150      48.763  -8.362  39.305  1.00 42.29           O  
ATOM    891  CB  ASP A 150      47.438  -9.882  36.657  1.00 49.91           C  
ATOM    892  CG  ASP A 150      47.062  -9.981  35.184  1.00 67.76           C  
ATOM    893  OD1 ASP A 150      47.622  -9.215  34.361  1.00 67.93           O  
ATOM    894  OD2 ASP A 150      46.198 -10.818  34.851  1.00 69.82           O  
ATOM    895  N   ARG A 151      46.857  -7.455  38.526  1.00 42.54           N  
ATOM    896  CA  ARG A 151      46.554  -6.686  39.717  1.00 36.63           C  
ATOM    897  C   ARG A 151      45.665  -7.478  40.660  1.00 38.13           C  
ATOM    898  O   ARG A 151      44.484  -7.662  40.387  1.00 38.67           O  
ATOM    899  CB  ARG A 151      45.894  -5.379  39.292  1.00 33.54           C  
ATOM    900  CG  ARG A 151      46.573  -4.785  38.059  1.00 32.44           C  
ATOM    901  CD  ARG A 151      45.983  -3.463  37.613  1.00 31.35           C  
ATOM    902  NE  ARG A 151      46.838  -2.821  36.607  1.00 28.85           N  
ATOM    903  CZ  ARG A 151      46.815  -1.523  36.331  1.00 29.59           C  
ATOM    904  NH1 ARG A 151      45.983  -0.728  36.983  1.00 27.38           N  
ATOM    905  NH2 ARG A 151      47.621  -1.013  35.404  1.00 32.08           N  
ATOM    906  N   ILE A 152      46.224  -7.951  41.772  1.00 31.35           N  
ATOM    907  CA  ILE A 152      45.490  -8.882  42.618  1.00 31.56           C  
ATOM    908  C   ILE A 152      44.786  -8.214  43.795  1.00 29.16           C  
ATOM    909  O   ILE A 152      43.961  -8.827  44.453  1.00 29.69           O  
ATOM    910  CB  ILE A 152      46.423  -9.982  43.136  1.00 37.47           C  
ATOM    911  CG1 ILE A 152      47.591  -9.371  43.911  1.00 30.27           C  
ATOM    912  CG2 ILE A 152      46.945 -10.817  41.952  1.00 34.49           C  
ATOM    913  CD1 ILE A 152      48.453 -10.395  44.581  1.00 35.05           C  
ATOM    914  N   ALA A 153      45.108  -6.952  44.050  1.00 28.64           N  
ATOM    915  CA  ALA A 153      44.463  -6.188  45.114  1.00 24.99           C  
ATOM    916  C   ALA A 153      44.643  -4.692  44.874  1.00 30.70           C  
ATOM    917  O   ALA A 153      45.728  -4.239  44.475  1.00 24.55           O  
ATOM    918  CB  ALA A 153      45.026  -6.577  46.482  1.00 25.76           C  
ATOM    919  N   CYS A 154      43.599  -3.912  45.140  1.00 29.68           N  
ATOM    920  CA  CYS A 154      43.726  -2.473  44.975  1.00 26.13           C  
ATOM    921  C   CYS A 154      42.728  -1.699  45.841  1.00 27.12           C  
ATOM    922  O   CYS A 154      41.695  -2.230  46.262  1.00 26.67           O  
ATOM    923  CB  CYS A 154      43.566  -2.107  43.500  1.00 25.25           C  
ATOM    924  SG  CYS A 154      41.916  -2.410  42.810  1.00 28.76           S  
ATOM    925  N   GLY A 155      43.039  -0.434  46.096  1.00 26.15           N  
ATOM    926  CA  GLY A 155      42.149   0.429  46.850  1.00 24.46           C  
ATOM    927  C   GLY A 155      42.457   1.878  46.539  1.00 25.92           C  
ATOM    928  O   GLY A 155      43.483   2.179  45.926  1.00 24.75           O  
ATOM    929  N   ILE A 156      41.549   2.759  46.945  1.00 23.25           N  
ATOM    930  CA  ILE A 156      41.710   4.205  46.824  1.00 24.81           C  
ATOM    931  C   ILE A 156      42.441   4.759  48.045  1.00 26.56           C  
ATOM    932  O   ILE A 156      42.127   4.389  49.190  1.00 24.49           O  
ATOM    933  CB  ILE A 156      40.330   4.909  46.695  1.00 29.02           C  
ATOM    934  CG1 ILE A 156      39.512   4.307  45.552  1.00 26.52           C  
ATOM    935  CG2 ILE A 156      40.487   6.422  46.502  1.00 24.48           C  
ATOM    936  CD1 ILE A 156      38.058   4.813  45.513  1.00 27.67           C  
ATOM    937  N   ILE A 157      43.413   5.635  47.831  1.00 20.93           N  
ATOM    938  CA  ILE A 157      44.067   6.260  48.984  1.00 21.68           C  
ATOM    939  C   ILE A 157      43.256   7.469  49.453  1.00 25.16           C  
ATOM    940  O   ILE A 157      42.995   8.397  48.680  1.00 25.05           O  
ATOM    941  CB  ILE A 157      45.505   6.661  48.665  1.00 21.29           C  
ATOM    942  CG1 ILE A 157      46.248   5.448  48.096  1.00 22.16           C  
ATOM    943  CG2 ILE A 157      46.206   7.228  49.944  1.00 19.64           C  
ATOM    944  CD1 ILE A 157      47.544   5.769  47.399  1.00 22.52           C  
ATOM    945  N   ALA A 158      42.826   7.442  50.708  1.00 22.97           N  
ATOM    946  CA  ALA A 158      41.888   8.448  51.208  1.00 25.55           C  
ATOM    947  C   ALA A 158      42.373   9.075  52.508  1.00 28.18           C  
ATOM    948  O   ALA A 158      43.225   8.492  53.181  1.00 23.44           O  
ATOM    949  CB  ALA A 158      40.523   7.830  51.416  1.00 24.68           C  
ATOM    950  N   TYR A 159      41.823  10.241  52.871  1.00 24.33           N  
ATOM    951  CA  TYR A 159      42.104  10.818  54.186  1.00 25.26           C  
ATOM    952  C   TYR A 159      41.564   9.915  55.287  1.00 27.97           C  
ATOM    953  O   TYR A 159      40.421   9.465  55.225  1.00 24.62           O  
ATOM    954  CB  TYR A 159      41.485  12.213  54.347  1.00 23.78           C  
ATOM    955  CG  TYR A 159      42.235  13.315  53.646  1.00 25.98           C  
ATOM    956  CD1 TYR A 159      43.320  13.929  54.242  1.00 26.66           C  
ATOM    957  CD2 TYR A 159      41.842  13.755  52.383  1.00 26.94           C  
ATOM    958  CE1 TYR A 159      44.013  14.942  53.591  1.00 26.37           C  
ATOM    959  CE2 TYR A 159      42.531  14.757  51.722  1.00 25.31           C  
ATOM    960  CZ  TYR A 159      43.608  15.354  52.335  1.00 27.47           C  
ATOM    961  OH  TYR A 159      44.291  16.362  51.697  1.00 24.43           O  
ATOM    962  N   LEU A 160      42.387   9.669  56.301  1.00 24.87           N  
ATOM    963  CA  LEU A 160      41.960   8.933  57.476  1.00 26.65           C  
ATOM    964  C   LEU A 160      40.977   9.796  58.245  1.00 31.22           C  
ATOM    965  O   LEU A 160      39.921   9.339  58.668  1.00 31.31           O  
ATOM    966  CB  LEU A 160      43.153   8.573  58.355  1.00 27.61           C  
ATOM    967  CG  LEU A 160      42.726   7.870  59.655  1.00 37.86           C  
ATOM    968  CD1 LEU A 160      42.272   6.417  59.375  1.00 29.77           C  
ATOM    969  CD2 LEU A 160      43.827   7.947  60.714  1.00 30.75           C  
ATOM    970  N   ASN A 161      41.338  11.061  58.406  1.00 29.68           N  
ATOM    971  CA  ASN A 161      40.475  12.019  59.076  1.00 39.28           C  
ATOM    972  C   ASN A 161      40.604  13.411  58.486  1.00 36.87           C  
ATOM    973  O   ASN A 161      39.868  14.306  58.906  1.00 47.90           O  
ATOM    974  CB  ASN A 161      40.751  12.063  60.604  1.00 34.00           C  
ATOM    975  CG  ASN A 161      42.248  12.069  60.968  1.00 44.20           C  
ATOM    976  OD1 ASN A 161      43.092  12.641  60.268  1.00 47.41           O  
ATOM    977  ND2 ASN A 161      42.571  11.441  62.102  1.00 48.97           N  
TER     978      ASN A 161                                                      
ATOM    979  N   TYR B   7      33.510  28.203  27.152  1.00 65.23           N  
ATOM    980  CA  TYR B   7      34.357  28.141  25.962  1.00 68.27           C  
ATOM    981  C   TYR B   7      35.383  27.023  26.056  1.00 55.34           C  
ATOM    982  CB  TYR B   7      35.072  29.475  25.737  1.00 64.86           C  
ATOM    983  CG  TYR B   7      34.127  30.631  25.529  1.00 77.22           C  
ATOM    984  CD1 TYR B   7      33.456  30.791  24.321  1.00 82.00           C  
ATOM    985  CD2 TYR B   7      33.905  31.563  26.537  1.00 77.07           C  
ATOM    986  CE1 TYR B   7      32.583  31.851  24.121  1.00 83.87           C  
ATOM    987  CE2 TYR B   7      33.035  32.628  26.348  1.00 83.41           C  
ATOM    988  CZ  TYR B   7      32.376  32.766  25.137  1.00 88.32           C  
ATOM    989  OH  TYR B   7      31.508  33.821  24.940  1.00 89.53           O  
ATOM    990  N   ASP B   8      36.613  27.401  26.394  1.00 53.73           N  
ATOM    991  CA  ASP B   8      37.713  26.449  26.444  1.00 46.80           C  
ATOM    992  C   ASP B   8      38.410  26.430  27.793  1.00 44.06           C  
ATOM    993  O   ASP B   8      39.163  27.346  28.116  1.00 45.24           O  
ATOM    994  CB  ASP B   8      38.727  26.767  25.358  1.00 41.66           C  
ATOM    995  CG  ASP B   8      38.265  26.337  24.017  1.00 51.90           C  
ATOM    996  OD1 ASP B   8      37.057  26.055  23.900  1.00 54.67           O  
ATOM    997  OD2 ASP B   8      39.095  26.282  23.079  1.00 58.63           O  
ATOM    998  N   PHE B   9      38.168  25.382  28.571  1.00 37.13           N  
ATOM    999  CA  PHE B   9      38.846  25.216  29.847  1.00 35.41           C  
ATOM   1000  C   PHE B   9      39.940  24.176  29.728  1.00 35.80           C  
ATOM   1001  O   PHE B   9      39.689  23.040  29.309  1.00 30.53           O  
ATOM   1002  CB  PHE B   9      37.869  24.798  30.944  1.00 36.58           C  
ATOM   1003  CG  PHE B   9      36.592  25.594  30.960  1.00 45.65           C  
ATOM   1004  CD1 PHE B   9      36.556  26.866  31.511  1.00 43.81           C  
ATOM   1005  CD2 PHE B   9      35.419  25.059  30.438  1.00 44.64           C  
ATOM   1006  CE1 PHE B   9      35.370  27.593  31.535  1.00 46.26           C  
ATOM   1007  CE2 PHE B   9      34.232  25.782  30.458  1.00 44.73           C  
ATOM   1008  CZ  PHE B   9      34.209  27.046  31.008  1.00 46.41           C  
ATOM   1009  N   PHE B  10      41.152  24.564  30.103  1.00 29.30           N  
ATOM   1010  CA  PHE B  10      42.267  23.637  30.167  1.00 32.54           C  
ATOM   1011  C   PHE B  10      42.627  23.373  31.613  1.00 35.07           C  
ATOM   1012  O   PHE B  10      42.243  24.133  32.499  1.00 36.06           O  
ATOM   1013  CB  PHE B  10      43.474  24.186  29.406  1.00 32.05           C  
ATOM   1014  CG  PHE B  10      43.222  24.349  27.949  1.00 32.64           C  
ATOM   1015  CD1 PHE B  10      43.402  23.282  27.086  1.00 34.61           C  
ATOM   1016  CD2 PHE B  10      42.753  25.558  27.441  1.00 35.33           C  
ATOM   1017  CE1 PHE B  10      43.142  23.417  25.724  1.00 33.49           C  
ATOM   1018  CE2 PHE B  10      42.500  25.706  26.085  1.00 40.23           C  
ATOM   1019  CZ  PHE B  10      42.691  24.631  25.224  1.00 32.89           C  
ATOM   1020  N   ASN B  11      43.379  22.302  31.840  1.00 35.28           N  
ATOM   1021  CA  ASN B  11      43.830  21.936  33.190  1.00 43.80           C  
ATOM   1022  C   ASN B  11      42.675  21.815  34.191  1.00 42.66           C  
ATOM   1023  O   ASN B  11      42.779  22.258  35.338  1.00 49.86           O  
ATOM   1024  CB  ASN B  11      44.866  22.946  33.706  1.00 40.26           C  
ATOM   1025  CG  ASN B  11      46.056  23.101  32.763  1.00 44.95           C  
ATOM   1026  OD1 ASN B  11      46.524  22.127  32.152  1.00 48.60           O  
ATOM   1027  ND2 ASN B  11      46.545  24.330  32.632  1.00 38.55           N  
ATOM   1028  N   VAL B  12      41.578  21.216  33.741  1.00 37.32           N  
ATOM   1029  CA  VAL B  12      40.465  20.877  34.606  1.00 36.41           C  
ATOM   1030  C   VAL B  12      40.834  19.700  35.499  1.00 35.94           C  
ATOM   1031  O   VAL B  12      41.461  18.741  35.054  1.00 41.34           O  
ATOM   1032  CB  VAL B  12      39.211  20.494  33.798  1.00 40.54           C  
ATOM   1033  CG1 VAL B  12      37.976  20.594  34.680  1.00 37.60           C  
ATOM   1034  CG2 VAL B  12      39.076  21.375  32.557  1.00 42.91           C  
ATOM   1035  N   VAL B  13      40.442  19.768  36.759  1.00 34.00           N  
ATOM   1036  CA  VAL B  13      40.575  18.620  37.645  1.00 32.77           C  
ATOM   1037  C   VAL B  13      39.215  17.920  37.700  1.00 29.06           C  
ATOM   1038  O   VAL B  13      38.182  18.571  37.883  1.00 24.85           O  
ATOM   1039  CB  VAL B  13      41.070  19.050  39.060  1.00 32.19           C  
ATOM   1040  CG1 VAL B  13      41.102  17.859  40.023  1.00 22.74           C  
ATOM   1041  CG2 VAL B  13      42.472  19.679  38.940  1.00 35.04           C  
ATOM   1042  N   THR B  14      39.225  16.604  37.497  1.00 24.55           N  
ATOM   1043  CA  THR B  14      38.007  15.793  37.497  1.00 26.53           C  
ATOM   1044  C   THR B  14      38.131  14.657  38.518  1.00 24.98           C  
ATOM   1045  O   THR B  14      39.177  13.993  38.603  1.00 23.48           O  
ATOM   1046  CB  THR B  14      37.698  15.184  36.082  1.00 26.66           C  
ATOM   1047  OG1 THR B  14      37.792  16.197  35.073  1.00 28.77           O  
ATOM   1048  CG2 THR B  14      36.292  14.606  36.037  1.00 24.61           C  
ATOM   1049  N   ALA B  15      37.066  14.438  39.286  1.00 23.09           N  
ATOM   1050  CA  ALA B  15      37.041  13.390  40.303  1.00 24.83           C  
ATOM   1051  C   ALA B  15      35.867  12.449  40.080  1.00 27.85           C  
ATOM   1052  O   ALA B  15      34.845  12.834  39.495  1.00 23.25           O  
ATOM   1053  CB  ALA B  15      36.967  13.997  41.710  1.00 21.99           C  
ATOM   1054  N   ILE B  16      36.014  11.212  40.542  1.00 24.60           N  
ATOM   1055  CA  ILE B  16      34.931  10.256  40.462  1.00 23.61           C  
ATOM   1056  C   ILE B  16      34.643   9.738  41.848  1.00 29.53           C  
ATOM   1057  O   ILE B  16      35.555   9.551  42.666  1.00 25.17           O  
ATOM   1058  CB  ILE B  16      35.258   9.076  39.517  1.00 23.33           C  
ATOM   1059  CG1 ILE B  16      34.075   8.114  39.413  1.00 26.48           C  
ATOM   1060  CG2 ILE B  16      36.531   8.347  39.956  1.00 25.26           C  
ATOM   1061  CD1 ILE B  16      34.288   6.984  38.403  1.00 28.17           C  
ATOM   1062  N   CYS B  17      33.366   9.522  42.125  1.00 22.41           N  
ATOM   1063  CA  CYS B  17      32.987   8.865  43.351  1.00 23.49           C  
ATOM   1064  C   CYS B  17      32.044   7.725  43.029  1.00 27.48           C  
ATOM   1065  O   CYS B  17      30.946   7.962  42.524  1.00 25.32           O  
ATOM   1066  CB  CYS B  17      32.322   9.847  44.319  1.00 26.76           C  
ATOM   1067  SG  CYS B  17      31.812   9.056  45.848  1.00 27.61           S  
ATOM   1068  N   GLN B  18      32.488   6.495  43.290  1.00 24.71           N  
ATOM   1069  CA  GLN B  18      31.631   5.319  43.199  1.00 27.48           C  
ATOM   1070  C   GLN B  18      30.897   5.116  44.513  1.00 30.43           C  
ATOM   1071  O   GLN B  18      31.516   4.864  45.550  1.00 27.93           O  
ATOM   1072  CB  GLN B  18      32.435   4.051  42.867  1.00 28.07           C  
ATOM   1073  CG  GLN B  18      33.032   4.010  41.474  1.00 33.65           C  
ATOM   1074  CD  GLN B  18      33.619   2.650  41.133  1.00 38.54           C  
ATOM   1075  OE1 GLN B  18      34.832   2.498  41.026  1.00 41.16           O  
ATOM   1076  NE2 GLN B  18      32.755   1.658  40.946  1.00 41.69           N  
ATOM   1077  N   LEU B  19      29.579   5.236  44.471  1.00 27.27           N  
ATOM   1078  CA  LEU B  19      28.764   5.009  45.653  1.00 28.97           C  
ATOM   1079  C   LEU B  19      28.418   3.532  45.744  1.00 33.04           C  
ATOM   1080  O   LEU B  19      27.330   3.118  45.329  1.00 35.63           O  
ATOM   1081  CB  LEU B  19      27.510   5.875  45.600  1.00 31.88           C  
ATOM   1082  CG  LEU B  19      27.973   7.314  45.766  1.00 33.80           C  
ATOM   1083  CD1 LEU B  19      27.908   8.075  44.457  1.00 32.83           C  
ATOM   1084  CD2 LEU B  19      27.252   8.019  46.898  1.00 33.56           C  
ATOM   1085  N   ASP B  20      29.368   2.749  46.261  1.00 30.16           N  
ATOM   1086  CA  ASP B  20      29.317   1.297  46.167  1.00 31.51           C  
ATOM   1087  C   ASP B  20      29.240   0.581  47.521  1.00 35.24           C  
ATOM   1088  O   ASP B  20      29.352  -0.642  47.585  1.00 35.50           O  
ATOM   1089  CB  ASP B  20      30.527   0.782  45.366  1.00 32.31           C  
ATOM   1090  CG  ASP B  20      31.868   1.235  45.944  1.00 31.67           C  
ATOM   1091  OD1 ASP B  20      31.898   1.967  46.955  1.00 30.93           O  
ATOM   1092  OD2 ASP B  20      32.908   0.835  45.382  1.00 34.13           O  
ATOM   1093  N   LYS B  21      29.043   1.343  48.592  1.00 31.42           N  
ATOM   1094  CA  LYS B  21      28.623   0.778  49.874  1.00 32.28           C  
ATOM   1095  C   LYS B  21      27.321   1.426  50.314  1.00 37.50           C  
ATOM   1096  O   LYS B  21      27.137   2.627  50.114  1.00 37.69           O  
ATOM   1097  CB  LYS B  21      29.676   0.991  50.956  1.00 30.85           C  
ATOM   1098  CG  LYS B  21      30.934   0.173  50.795  1.00 28.80           C  
ATOM   1099  CD  LYS B  21      31.886   0.530  51.910  1.00 34.83           C  
ATOM   1100  CE  LYS B  21      33.192  -0.257  51.815  1.00 40.56           C  
ATOM   1101  NZ  LYS B  21      32.968  -1.721  51.980  1.00 42.62           N  
ATOM   1102  N   PRO B  22      26.419   0.649  50.939  1.00 37.62           N  
ATOM   1103  CA  PRO B  22      26.557  -0.784  51.221  1.00 37.17           C  
ATOM   1104  C   PRO B  22      26.270  -1.640  50.009  1.00 40.99           C  
ATOM   1105  O   PRO B  22      26.507  -2.843  50.046  1.00 42.50           O  
ATOM   1106  CB  PRO B  22      25.522  -1.031  52.326  1.00 41.78           C  
ATOM   1107  CG  PRO B  22      24.515   0.042  52.155  1.00 39.71           C  
ATOM   1108  CD  PRO B  22      25.266   1.241  51.641  1.00 39.60           C  
ATOM   1109  N   HIS B  23      25.770  -1.028  48.942  1.00 38.67           N  
ATOM   1110  CA  HIS B  23      25.618  -1.738  47.678  1.00 39.41           C  
ATOM   1111  C   HIS B  23      25.918  -0.803  46.521  1.00 37.46           C  
ATOM   1112  O   HIS B  23      26.248   0.364  46.717  1.00 35.97           O  
ATOM   1113  CB  HIS B  23      24.216  -2.326  47.543  1.00 38.57           C  
ATOM   1114  CG  HIS B  23      23.873  -3.294  48.628  1.00 43.62           C  
ATOM   1115  ND1 HIS B  23      24.450  -4.545  48.717  1.00 46.21           N  
ATOM   1116  CD2 HIS B  23      23.033  -3.189  49.684  1.00 40.10           C  
ATOM   1117  CE1 HIS B  23      23.973  -5.170  49.779  1.00 48.35           C  
ATOM   1118  NE2 HIS B  23      23.116  -4.367  50.386  1.00 44.51           N  
ATOM   1119  N   ASP B  24      25.803  -1.323  45.310  1.00 39.73           N  
ATOM   1120  CA  ASP B  24      26.132  -0.555  44.124  1.00 36.94           C  
ATOM   1121  C   ASP B  24      25.016   0.428  43.768  1.00 37.90           C  
ATOM   1122  O   ASP B  24      23.980   0.038  43.227  1.00 39.62           O  
ATOM   1123  CB  ASP B  24      26.411  -1.511  42.962  1.00 39.26           C  
ATOM   1124  CG  ASP B  24      26.661  -0.790  41.651  1.00 43.16           C  
ATOM   1125  OD1 ASP B  24      27.010   0.412  41.672  1.00 42.05           O  
ATOM   1126  OD2 ASP B  24      26.518  -1.435  40.592  1.00 49.99           O  
ATOM   1127  N   TYR B  25      25.226   1.708  44.053  1.00 31.12           N  
ATOM   1128  CA  TYR B  25      24.248   2.711  43.641  1.00 32.90           C  
ATOM   1129  C   TYR B  25      24.754   3.663  42.554  1.00 34.27           C  
ATOM   1130  O   TYR B  25      24.254   4.785  42.425  1.00 32.69           O  
ATOM   1131  CB  TYR B  25      23.781   3.520  44.850  1.00 30.93           C  
ATOM   1132  CG  TYR B  25      23.163   2.644  45.916  1.00 36.17           C  
ATOM   1133  CD1 TYR B  25      21.861   2.160  45.785  1.00 37.54           C  
ATOM   1134  CD2 TYR B  25      23.891   2.272  47.037  1.00 39.70           C  
ATOM   1135  CE1 TYR B  25      21.299   1.341  46.760  1.00 37.21           C  
ATOM   1136  CE2 TYR B  25      23.338   1.455  48.016  1.00 39.67           C  
ATOM   1137  CZ  TYR B  25      22.043   0.996  47.871  1.00 40.28           C  
ATOM   1138  OH  TYR B  25      21.498   0.189  48.847  1.00 44.23           O  
ATOM   1139  N   GLY B  26      25.723   3.218  41.761  1.00 30.91           N  
ATOM   1140  CA  GLY B  26      26.247   4.053  40.693  1.00 32.38           C  
ATOM   1141  C   GLY B  26      27.382   4.958  41.134  1.00 29.66           C  
ATOM   1142  O   GLY B  26      28.132   4.620  42.054  1.00 29.75           O  
ATOM   1143  N   TYR B  27      27.508   6.114  40.482  1.00 27.68           N  
ATOM   1144  CA  TYR B  27      28.643   6.996  40.720  1.00 27.62           C  
ATOM   1145  C   TYR B  27      28.286   8.440  40.413  1.00 29.60           C  
ATOM   1146  O   TYR B  27      27.200   8.724  39.907  1.00 28.63           O  
ATOM   1147  CB  TYR B  27      29.864   6.558  39.880  1.00 24.54           C  
ATOM   1148  CG  TYR B  27      29.637   6.668  38.391  1.00 27.41           C  
ATOM   1149  CD1 TYR B  27      28.887   5.712  37.708  1.00 25.13           C  
ATOM   1150  CD2 TYR B  27      30.163   7.733  37.667  1.00 25.86           C  
ATOM   1151  CE1 TYR B  27      28.659   5.816  36.332  1.00 28.03           C  
ATOM   1152  CE2 TYR B  27      29.942   7.850  36.302  1.00 26.86           C  
ATOM   1153  CZ  TYR B  27      29.194   6.888  35.640  1.00 30.10           C  
ATOM   1154  OH  TYR B  27      28.984   7.018  34.285  1.00 31.41           O  
ATOM   1155  N   ALA B  28      29.200   9.345  40.751  1.00 24.75           N  
ATOM   1156  CA  ALA B  28      29.079  10.756  40.422  1.00 27.13           C  
ATOM   1157  C   ALA B  28      30.421  11.237  39.898  1.00 27.52           C  
ATOM   1158  O   ALA B  28      31.460  10.704  40.296  1.00 24.97           O  
ATOM   1159  CB  ALA B  28      28.648  11.579  41.660  1.00 26.01           C  
ATOM   1160  N   ILE B  29      30.393  12.229  39.006  1.00 24.96           N  
ATOM   1161  CA  ILE B  29      31.600  12.841  38.444  1.00 22.62           C  
ATOM   1162  C   ILE B  29      31.676  14.306  38.885  1.00 26.70           C  
ATOM   1163  O   ILE B  29      30.714  15.053  38.705  1.00 26.38           O  
ATOM   1164  CB  ILE B  29      31.613  12.774  36.869  1.00 26.43           C  
ATOM   1165  CG1 ILE B  29      31.540  11.332  36.362  1.00 25.90           C  
ATOM   1166  CG2 ILE B  29      32.846  13.462  36.295  1.00 24.31           C  
ATOM   1167  CD1 ILE B  29      32.829  10.534  36.539  1.00 23.14           C  
ATOM   1168  N   PHE B  30      32.800  14.713  39.470  1.00 22.59           N  
ATOM   1169  CA  PHE B  30      33.006  16.112  39.857  1.00 24.31           C  
ATOM   1170  C   PHE B  30      33.990  16.782  38.909  1.00 26.28           C  
ATOM   1171  O   PHE B  30      35.081  16.270  38.678  1.00 26.35           O  
ATOM   1172  CB  PHE B  30      33.579  16.258  41.269  1.00 23.63           C  
ATOM   1173  CG  PHE B  30      32.751  15.656  42.364  1.00 24.29           C  
ATOM   1174  CD1 PHE B  30      32.627  14.286  42.491  1.00 23.43           C  
ATOM   1175  CD2 PHE B  30      32.173  16.473  43.327  1.00 26.71           C  
ATOM   1176  CE1 PHE B  30      31.902  13.731  43.547  1.00 27.91           C  
ATOM   1177  CE2 PHE B  30      31.454  15.929  44.387  1.00 23.99           C  
ATOM   1178  CZ  PHE B  30      31.318  14.557  44.495  1.00 24.71           C  
ATOM   1179  N   THR B  31      33.644  17.956  38.415  1.00 24.52           N  
ATOM   1180  CA  THR B  31      34.514  18.657  37.495  1.00 28.72           C  
ATOM   1181  C   THR B  31      34.723  20.081  37.985  1.00 28.71           C  
ATOM   1182  O   THR B  31      33.776  20.855  38.036  1.00 30.98           O  
ATOM   1183  CB  THR B  31      33.904  18.654  36.091  1.00 28.23           C  
ATOM   1184  OG1 THR B  31      33.591  17.308  35.724  1.00 27.31           O  
ATOM   1185  CG2 THR B  31      34.858  19.234  35.087  1.00 28.95           C  
ATOM   1186  N   GLN B  32      35.945  20.435  38.361  1.00 26.64           N  
ATOM   1187  CA  GLN B  32      36.159  21.771  38.899  1.00 31.05           C  
ATOM   1188  C   GLN B  32      36.375  22.787  37.777  1.00 30.48           C  
ATOM   1189  O   GLN B  32      37.432  22.834  37.155  1.00 35.06           O  
ATOM   1190  CB  GLN B  32      37.338  21.798  39.877  1.00 30.04           C  
ATOM   1191  CG  GLN B  32      37.355  23.075  40.744  1.00 32.14           C  
ATOM   1192  CD  GLN B  32      38.442  23.058  41.818  1.00 37.45           C  
ATOM   1193  OE1 GLN B  32      39.108  22.045  42.035  1.00 36.54           O  
ATOM   1194  NE2 GLN B  32      38.639  24.197  42.477  1.00 38.99           N  
ATOM   1195  N   LEU B  33      35.344  23.581  37.522  1.00 35.96           N  
ATOM   1196  CA  LEU B  33      35.367  24.643  36.517  1.00 36.37           C  
ATOM   1197  C   LEU B  33      35.654  25.960  37.231  1.00 41.22           C  
ATOM   1198  O   LEU B  33      35.470  26.042  38.446  1.00 43.43           O  
ATOM   1199  CB  LEU B  33      34.032  24.682  35.770  1.00 34.13           C  
ATOM   1200  CG  LEU B  33      33.713  23.378  35.036  1.00 36.86           C  
ATOM   1201  CD1 LEU B  33      32.246  23.309  34.592  1.00 37.37           C  
ATOM   1202  CD2 LEU B  33      34.642  23.232  33.850  1.00 36.13           C  
ATOM   1203  N   PRO B  34      36.115  26.991  36.500  1.00 44.67           N  
ATOM   1204  CA  PRO B  34      36.582  28.222  37.161  1.00 47.69           C  
ATOM   1205  C   PRO B  34      35.582  28.913  38.085  1.00 47.65           C  
ATOM   1206  O   PRO B  34      36.022  29.610  39.001  1.00 52.69           O  
ATOM   1207  CB  PRO B  34      36.917  29.140  35.982  1.00 47.07           C  
ATOM   1208  CG  PRO B  34      37.288  28.209  34.897  1.00 45.65           C  
ATOM   1209  CD  PRO B  34      36.359  27.036  35.049  1.00 46.27           C  
ATOM   1210  N   ASP B  35      34.283  28.731  37.871  1.00 44.44           N  
ATOM   1211  CA  ASP B  35      33.298  29.440  38.680  1.00 46.28           C  
ATOM   1212  C   ASP B  35      32.504  28.537  39.613  1.00 48.17           C  
ATOM   1213  O   ASP B  35      31.797  29.025  40.492  1.00 50.52           O  
ATOM   1214  CB  ASP B  35      32.340  30.205  37.780  1.00 53.09           C  
ATOM   1215  CG  ASP B  35      33.020  31.349  37.059  1.00 59.29           C  
ATOM   1216  OD1 ASP B  35      34.012  31.890  37.603  1.00 58.47           O  
ATOM   1217  OD2 ASP B  35      32.569  31.695  35.945  1.00 65.82           O  
ATOM   1218  N   CYS B  36      32.623  27.226  39.427  1.00 42.25           N  
ATOM   1219  CA  CYS B  36      31.934  26.267  40.282  1.00 36.07           C  
ATOM   1220  C   CYS B  36      32.436  24.856  40.000  1.00 39.96           C  
ATOM   1221  O   CYS B  36      33.165  24.627  39.022  1.00 41.24           O  
ATOM   1222  CB  CYS B  36      30.414  26.333  40.069  1.00 40.31           C  
ATOM   1223  SG  CYS B  36      29.915  25.896  38.390  1.00 55.07           S  
ATOM   1224  N   THR B  37      32.052  23.921  40.864  1.00 32.91           N  
ATOM   1225  CA  THR B  37      32.343  22.517  40.659  1.00 30.75           C  
ATOM   1226  C   THR B  37      31.086  21.843  40.176  1.00 33.85           C  
ATOM   1227  O   THR B  37      30.071  21.818  40.872  1.00 33.91           O  
ATOM   1228  CB  THR B  37      32.848  21.814  41.937  1.00 31.69           C  
ATOM   1229  OG1 THR B  37      34.089  22.401  42.342  1.00 32.85           O  
ATOM   1230  CG2 THR B  37      33.082  20.338  41.676  1.00 24.44           C  
ATOM   1231  N   GLU B  38      31.162  21.311  38.964  1.00 30.75           N  
ATOM   1232  CA  GLU B  38      30.049  20.602  38.363  1.00 32.11           C  
ATOM   1233  C   GLU B  38      29.973  19.193  38.930  1.00 27.12           C  
ATOM   1234  O   GLU B  38      30.985  18.523  39.062  1.00 30.29           O  
ATOM   1235  CB  GLU B  38      30.218  20.576  36.839  1.00 30.04           C  
ATOM   1236  CG  GLU B  38      29.155  19.806  36.070  1.00 27.26           C  
ATOM   1237  CD  GLU B  38      29.508  19.700  34.603  1.00 30.21           C  
ATOM   1238  OE1 GLU B  38      30.671  20.000  34.251  1.00 30.95           O  
ATOM   1239  OE2 GLU B  38      28.633  19.331  33.799  1.00 31.21           O  
ATOM   1240  N   ILE B  39      28.780  18.751  39.299  1.00 30.19           N  
ATOM   1241  CA  ILE B  39      28.613  17.388  39.771  1.00 30.63           C  
ATOM   1242  C   ILE B  39      27.566  16.679  38.932  1.00 34.87           C  
ATOM   1243  O   ILE B  39      26.378  17.019  38.973  1.00 33.11           O  
ATOM   1244  CB  ILE B  39      28.217  17.330  41.260  1.00 29.31           C  
ATOM   1245  CG1 ILE B  39      29.119  18.263  42.070  1.00 30.71           C  
ATOM   1246  CG2 ILE B  39      28.288  15.888  41.770  1.00 22.95           C  
ATOM   1247  CD1 ILE B  39      28.801  18.330  43.548  1.00 30.77           C  
ATOM   1248  N   GLN B  40      28.028  15.699  38.156  1.00 31.48           N  
ATOM   1249  CA  GLN B  40      27.154  14.901  37.309  1.00 31.54           C  
ATOM   1250  C   GLN B  40      26.861  13.600  38.026  1.00 29.56           C  
ATOM   1251  O   GLN B  40      27.764  12.764  38.215  1.00 28.23           O  
ATOM   1252  CB  GLN B  40      27.798  14.641  35.926  1.00 28.47           C  
ATOM   1253  CG  GLN B  40      28.107  15.927  35.156  1.00 34.12           C  
ATOM   1254  CD  GLN B  40      28.999  15.716  33.920  1.00 41.31           C  
ATOM   1255  OE1 GLN B  40      28.535  15.277  32.853  1.00 42.52           O  
ATOM   1256  NE2 GLN B  40      30.278  16.036  34.063  1.00 32.53           N  
ATOM   1257  N   PHE B  41      25.607  13.430  38.440  1.00 26.30           N  
ATOM   1258  CA  PHE B  41      25.207  12.200  39.109  1.00 30.25           C  
ATOM   1259  C   PHE B  41      24.824  11.134  38.099  1.00 32.04           C  
ATOM   1260  O   PHE B  41      24.251  11.425  37.041  1.00 32.57           O  
ATOM   1261  CB  PHE B  41      24.042  12.451  40.074  1.00 32.00           C  
ATOM   1262  CG  PHE B  41      24.421  13.262  41.286  1.00 31.55           C  
ATOM   1263  CD1 PHE B  41      24.838  12.633  42.459  1.00 26.99           C  
ATOM   1264  CD2 PHE B  41      24.362  14.650  41.259  1.00 32.14           C  
ATOM   1265  CE1 PHE B  41      25.173  13.375  43.587  1.00 31.55           C  
ATOM   1266  CE2 PHE B  41      24.705  15.403  42.388  1.00 34.75           C  
ATOM   1267  CZ  PHE B  41      25.114  14.758  43.553  1.00 34.26           C  
ATOM   1268  N   HIS B  42      25.169   9.897  38.421  1.00 28.62           N  
ATOM   1269  CA  HIS B  42      24.727   8.750  37.653  1.00 31.87           C  
ATOM   1270  C   HIS B  42      24.405   7.675  38.670  1.00 31.28           C  
ATOM   1271  O   HIS B  42      25.026   6.620  38.703  1.00 31.65           O  
ATOM   1272  CB  HIS B  42      25.783   8.270  36.651  1.00 31.06           C  
ATOM   1273  CG  HIS B  42      26.130   9.278  35.599  1.00 30.15           C  
ATOM   1274  ND1 HIS B  42      25.238   9.685  34.633  1.00 31.22           N  
ATOM   1275  CD2 HIS B  42      27.279   9.954  35.356  1.00 31.60           C  
ATOM   1276  CE1 HIS B  42      25.811  10.580  33.851  1.00 30.96           C  
ATOM   1277  NE2 HIS B  42      27.056  10.753  34.260  1.00 31.12           N  
ATOM   1278  N   LEU B  43      23.425   7.968  39.510  1.00 33.10           N  
ATOM   1279  CA  LEU B  43      23.039   7.068  40.584  1.00 34.93           C  
ATOM   1280  C   LEU B  43      21.904   6.154  40.141  1.00 37.57           C  
ATOM   1281  O   LEU B  43      21.148   6.496  39.231  1.00 37.01           O  
ATOM   1282  CB  LEU B  43      22.626   7.860  41.816  1.00 28.28           C  
ATOM   1283  CG  LEU B  43      23.654   8.854  42.359  1.00 32.22           C  
ATOM   1284  CD1 LEU B  43      23.144   9.494  43.662  1.00 29.29           C  
ATOM   1285  CD2 LEU B  43      24.985   8.156  42.594  1.00 28.89           C  
ATOM   1286  N   LYS B  44      21.791   5.006  40.805  1.00 33.70           N  
ATOM   1287  CA  LYS B  44      20.826   3.968  40.465  1.00 35.90           C  
ATOM   1288  C   LYS B  44      20.466   3.147  41.712  1.00 40.19           C  
ATOM   1289  O   LYS B  44      21.138   3.258  42.742  1.00 38.58           O  
ATOM   1290  CB  LYS B  44      21.397   3.055  39.380  1.00 39.16           C  
ATOM   1291  CG  LYS B  44      22.787   2.526  39.734  1.00 41.09           C  
ATOM   1292  CD  LYS B  44      23.180   1.357  38.862  1.00 42.76           C  
ATOM   1293  CE  LYS B  44      24.434   0.672  39.369  1.00 42.99           C  
ATOM   1294  NZ  LYS B  44      24.798  -0.471  38.482  1.00 48.60           N  
ATOM   1295  N   ASN B  45      19.416   2.330  41.603  1.00 40.74           N  
ATOM   1296  CA  ASN B  45      18.947   1.426  42.666  1.00 39.47           C  
ATOM   1297  C   ASN B  45      18.614   2.105  43.998  1.00 42.74           C  
ATOM   1298  O   ASN B  45      18.641   1.464  45.052  1.00 41.52           O  
ATOM   1299  CB  ASN B  45      19.978   0.314  42.910  1.00 39.94           C  
ATOM   1300  CG  ASN B  45      20.337  -0.435  41.635  1.00 43.40           C  
ATOM   1301  OD1 ASN B  45      19.481  -0.679  40.790  1.00 50.22           O  
ATOM   1302  ND2 ASN B  45      21.603  -0.791  41.488  1.00 43.49           N  
ATOM   1303  N   LEU B  46      18.290   3.393  43.952  1.00 38.06           N  
ATOM   1304  CA  LEU B  46      17.964   4.138  45.170  1.00 43.72           C  
ATOM   1305  C   LEU B  46      16.452   4.293  45.364  1.00 47.92           C  
ATOM   1306  O   LEU B  46      15.691   4.184  44.400  1.00 44.58           O  
ATOM   1307  CB  LEU B  46      18.622   5.525  45.136  1.00 41.78           C  
ATOM   1308  CG  LEU B  46      20.128   5.554  45.405  1.00 40.11           C  
ATOM   1309  CD1 LEU B  46      20.705   6.935  45.122  1.00 36.15           C  
ATOM   1310  CD2 LEU B  46      20.409   5.118  46.847  1.00 37.89           C  
ATOM   1311  N   PRO B  47      16.018   4.543  46.615  1.00 45.06           N  
ATOM   1312  CA  PRO B  47      14.631   4.920  46.915  1.00 49.37           C  
ATOM   1313  C   PRO B  47      14.225   6.221  46.228  1.00 50.64           C  
ATOM   1314  O   PRO B  47      14.919   7.229  46.375  1.00 50.16           O  
ATOM   1315  CB  PRO B  47      14.633   5.099  48.442  1.00 47.26           C  
ATOM   1316  CG  PRO B  47      15.724   4.213  48.919  1.00 46.90           C  
ATOM   1317  CD  PRO B  47      16.788   4.262  47.840  1.00 46.25           C  
ATOM   1318  N   PRO B  48      13.117   6.201  45.473  1.00 49.87           N  
ATOM   1319  CA  PRO B  48      12.615   7.436  44.855  1.00 49.01           C  
ATOM   1320  C   PRO B  48      12.354   8.532  45.882  1.00 46.49           C  
ATOM   1321  O   PRO B  48      12.148   8.239  47.052  1.00 53.21           O  
ATOM   1322  CB  PRO B  48      11.316   6.988  44.179  1.00 46.84           C  
ATOM   1323  CG  PRO B  48      11.578   5.553  43.820  1.00 51.69           C  
ATOM   1324  CD  PRO B  48      12.461   4.998  44.930  1.00 48.55           C  
ATOM   1325  N   GLY B  49      12.375   9.784  45.442  1.00 52.29           N  
ATOM   1326  CA  GLY B  49      12.183  10.903  46.342  1.00 50.72           C  
ATOM   1327  C   GLY B  49      13.438  11.741  46.475  1.00 52.57           C  
ATOM   1328  O   GLY B  49      14.440  11.485  45.800  1.00 51.93           O  
ATOM   1329  N   LYS B  50      13.377  12.755  47.333  1.00 49.12           N  
ATOM   1330  CA  LYS B  50      14.521  13.615  47.590  1.00 51.92           C  
ATOM   1331  C   LYS B  50      15.446  12.990  48.627  1.00 51.83           C  
ATOM   1332  O   LYS B  50      14.982  12.345  49.565  1.00 50.48           O  
ATOM   1333  CB  LYS B  50      14.069  15.000  48.068  1.00 54.56           C  
ATOM   1334  CG  LYS B  50      12.934  15.612  47.272  1.00 57.92           C  
ATOM   1335  CD  LYS B  50      13.232  17.073  46.931  1.00 66.67           C  
ATOM   1336  CE  LYS B  50      11.961  17.910  46.811  1.00 71.60           C  
ATOM   1337  NZ  LYS B  50      12.257  19.370  46.705  1.00 70.53           N  
ATOM   1338  N   HIS B  51      16.753  13.185  48.453  1.00 50.44           N  
ATOM   1339  CA  HIS B  51      17.734  12.693  49.417  1.00 47.96           C  
ATOM   1340  C   HIS B  51      18.824  13.720  49.666  1.00 51.04           C  
ATOM   1341  O   HIS B  51      19.351  14.319  48.728  1.00 48.60           O  
ATOM   1342  CB  HIS B  51      18.372  11.392  48.946  1.00 46.50           C  
ATOM   1343  CG  HIS B  51      17.397  10.288  48.694  1.00 54.52           C  
ATOM   1344  ND1 HIS B  51      16.848   9.530  49.706  1.00 59.63           N  
ATOM   1345  CD2 HIS B  51      16.895   9.792  47.537  1.00 51.18           C  
ATOM   1346  CE1 HIS B  51      16.039   8.622  49.184  1.00 51.62           C  
ATOM   1347  NE2 HIS B  51      16.055   8.759  47.870  1.00 51.35           N  
ATOM   1348  N   GLY B  52      19.148  13.919  50.939  1.00 47.97           N  
ATOM   1349  CA  GLY B  52      20.222  14.801  51.333  1.00 47.38           C  
ATOM   1350  C   GLY B  52      21.553  14.289  50.817  1.00 51.24           C  
ATOM   1351  O   GLY B  52      21.780  13.082  50.685  1.00 44.79           O  
ATOM   1352  N   CYS B  53      22.446  15.221  50.522  1.00 50.69           N  
ATOM   1353  CA  CYS B  53      23.697  14.871  49.890  1.00 43.68           C  
ATOM   1354  C   CYS B  53      24.826  15.694  50.468  1.00 43.05           C  
ATOM   1355  O   CYS B  53      24.822  16.918  50.366  1.00 43.10           O  
ATOM   1356  CB  CYS B  53      23.591  15.081  48.387  1.00 48.76           C  
ATOM   1357  SG  CYS B  53      24.758  14.111  47.475  1.00 56.96           S  
ATOM   1358  N   HIS B  54      25.786  15.024  51.093  1.00 36.97           N  
ATOM   1359  CA  HIS B  54      26.841  15.741  51.789  1.00 36.57           C  
ATOM   1360  C   HIS B  54      28.225  15.116  51.672  1.00 34.72           C  
ATOM   1361  O   HIS B  54      28.397  13.891  51.622  1.00 31.04           O  
ATOM   1362  CB  HIS B  54      26.499  15.863  53.277  1.00 42.80           C  
ATOM   1363  CG  HIS B  54      25.176  16.507  53.537  1.00 49.00           C  
ATOM   1364  ND1 HIS B  54      25.041  17.855  53.788  1.00 54.53           N  
ATOM   1365  CD2 HIS B  54      23.925  15.990  53.569  1.00 47.16           C  
ATOM   1366  CE1 HIS B  54      23.764  18.140  53.967  1.00 55.29           C  
ATOM   1367  NE2 HIS B  54      23.066  17.026  53.840  1.00 50.73           N  
ATOM   1368  N   ILE B  55      29.207  16.002  51.663  1.00 33.84           N  
ATOM   1369  CA  ILE B  55      30.600  15.655  51.829  1.00 32.53           C  
ATOM   1370  C   ILE B  55      30.916  15.375  53.297  1.00 36.08           C  
ATOM   1371  O   ILE B  55      30.592  16.188  54.174  1.00 35.21           O  
ATOM   1372  CB  ILE B  55      31.497  16.797  51.326  1.00 32.44           C  
ATOM   1373  CG1 ILE B  55      31.041  17.230  49.931  1.00 31.55           C  
ATOM   1374  CG2 ILE B  55      32.971  16.365  51.341  1.00 27.98           C  
ATOM   1375  CD1 ILE B  55      31.172  16.155  48.913  1.00 31.92           C  
ATOM   1376  N   HIS B  56      31.535  14.231  53.571  1.00 31.90           N  
ATOM   1377  CA  HIS B  56      31.963  13.924  54.926  1.00 34.59           C  
ATOM   1378  C   HIS B  56      33.484  13.901  55.015  1.00 33.80           C  
ATOM   1379  O   HIS B  56      34.173  13.671  54.018  1.00 34.12           O  
ATOM   1380  CB  HIS B  56      31.345  12.603  55.394  1.00 35.76           C  
ATOM   1381  CG  HIS B  56      29.874  12.705  55.655  1.00 39.68           C  
ATOM   1382  ND1 HIS B  56      29.321  12.523  56.905  1.00 38.48           N  
ATOM   1383  CD2 HIS B  56      28.844  13.019  54.832  1.00 38.94           C  
ATOM   1384  CE1 HIS B  56      28.012  12.697  56.835  1.00 37.81           C  
ATOM   1385  NE2 HIS B  56      27.697  12.995  55.588  1.00 42.18           N  
ATOM   1386  N   LYS B  57      34.000  14.151  56.213  1.00 34.99           N  
ATOM   1387  CA  LYS B  57      35.414  14.466  56.403  1.00 37.05           C  
ATOM   1388  C   LYS B  57      36.379  13.307  56.152  1.00 32.37           C  
ATOM   1389  O   LYS B  57      37.443  13.511  55.559  1.00 32.60           O  
ATOM   1390  CB  LYS B  57      35.642  15.015  57.817  1.00 38.96           C  
ATOM   1391  CG  LYS B  57      37.066  15.530  58.040  1.00 45.88           C  
ATOM   1392  CD  LYS B  57      37.135  16.614  59.117  1.00 50.63           C  
ATOM   1393  CE  LYS B  57      36.551  16.126  60.442  1.00 59.18           C  
ATOM   1394  NZ  LYS B  57      37.319  14.976  61.015  1.00 56.48           N  
ATOM   1395  N   SER B  58      36.022  12.102  56.591  1.00 31.83           N  
ATOM   1396  CA  SER B  58      36.940  10.969  56.484  1.00 31.33           C  
ATOM   1397  C   SER B  58      36.662  10.124  55.250  1.00 31.75           C  
ATOM   1398  O   SER B  58      35.509   9.945  54.875  1.00 30.22           O  
ATOM   1399  CB  SER B  58      36.851  10.088  57.728  1.00 27.70           C  
ATOM   1400  OG  SER B  58      37.641   8.926  57.565  1.00 29.49           O  
ATOM   1401  N   GLY B  59      37.715   9.591  54.632  1.00 30.19           N  
ATOM   1402  CA  GLY B  59      37.556   8.614  53.566  1.00 28.78           C  
ATOM   1403  C   GLY B  59      37.559   7.170  54.049  1.00 27.24           C  
ATOM   1404  O   GLY B  59      37.519   6.239  53.248  1.00 25.86           O  
ATOM   1405  N   ASP B  60      37.607   6.991  55.365  1.00 29.59           N  
ATOM   1406  CA  ASP B  60      37.652   5.666  56.008  1.00 30.40           C  
ATOM   1407  C   ASP B  60      36.286   4.975  55.899  1.00 29.93           C  
ATOM   1408  O   ASP B  60      35.266   5.563  56.251  1.00 33.01           O  
ATOM   1409  CB  ASP B  60      38.071   5.845  57.476  1.00 30.64           C  
ATOM   1410  CG  ASP B  60      38.362   4.531  58.211  1.00 32.02           C  
ATOM   1411  OD1 ASP B  60      38.133   3.424  57.690  1.00 32.14           O  
ATOM   1412  OD2 ASP B  60      38.828   4.625  59.363  1.00 35.24           O  
ATOM   1413  N   ARG B  61      36.239   3.751  55.388  1.00 27.76           N  
ATOM   1414  CA  ARG B  61      34.953   3.051  55.323  1.00 34.07           C  
ATOM   1415  C   ARG B  61      35.034   1.664  55.961  1.00 35.30           C  
ATOM   1416  O   ARG B  61      34.323   0.749  55.550  1.00 38.13           O  
ATOM   1417  CB  ARG B  61      34.447   2.926  53.871  1.00 32.69           C  
ATOM   1418  CG  ARG B  61      34.150   4.261  53.170  1.00 33.61           C  
ATOM   1419  CD  ARG B  61      33.352   4.071  51.869  1.00 29.62           C  
ATOM   1420  NE  ARG B  61      34.026   3.193  50.913  1.00 31.17           N  
ATOM   1421  CZ  ARG B  61      33.495   2.796  49.757  1.00 29.79           C  
ATOM   1422  NH1 ARG B  61      32.284   3.201  49.399  1.00 28.80           N  
ATOM   1423  NH2 ARG B  61      34.177   1.999  48.953  1.00 28.32           N  
ATOM   1424  N   ARG B  62      35.887   1.514  56.973  1.00 36.59           N  
ATOM   1425  CA  ARG B  62      36.029   0.229  57.648  1.00 37.83           C  
ATOM   1426  C   ARG B  62      34.748  -0.185  58.368  1.00 37.82           C  
ATOM   1427  O   ARG B  62      34.394  -1.359  58.355  1.00 42.37           O  
ATOM   1428  CB  ARG B  62      37.205   0.265  58.623  1.00 32.52           C  
ATOM   1429  CG  ARG B  62      38.549   0.151  57.926  1.00 34.87           C  
ATOM   1430  CD  ARG B  62      39.690   0.284  58.893  1.00 37.06           C  
ATOM   1431  NE  ARG B  62      39.917   1.667  59.303  1.00 32.99           N  
ATOM   1432  CZ  ARG B  62      40.939   2.037  60.066  1.00 30.90           C  
ATOM   1433  NH1 ARG B  62      41.793   1.126  60.512  1.00 34.11           N  
ATOM   1434  NH2 ARG B  62      41.107   3.308  60.396  1.00 32.69           N  
ATOM   1435  N   ASN B  63      34.056   0.765  58.995  1.00 36.69           N  
ATOM   1436  CA  ASN B  63      32.750   0.470  59.591  1.00 44.57           C  
ATOM   1437  C   ASN B  63      31.587   0.947  58.679  1.00 37.28           C  
ATOM   1438  O   ASN B  63      30.600   1.491  59.150  1.00 44.80           O  
ATOM   1439  CB  ASN B  63      32.615   1.104  61.003  1.00 39.31           C  
ATOM   1440  CG  ASN B  63      33.848   0.843  61.924  1.00 50.80           C  
ATOM   1441  OD1 ASN B  63      34.697  -0.020  61.653  1.00 50.28           O  
ATOM   1442  ND2 ASN B  63      33.920   1.585  63.030  1.00 41.92           N  
ATOM   1443  N   GLY B  64      31.706   0.742  57.376  1.00 44.01           N  
ATOM   1444  CA  GLY B  64      30.692   1.214  56.444  1.00 39.73           C  
ATOM   1445  C   GLY B  64      30.663   2.728  56.341  1.00 41.70           C  
ATOM   1446  O   GLY B  64      31.674   3.387  56.588  1.00 42.45           O  
ATOM   1447  N   CYS B  65      29.509   3.294  55.993  1.00 34.68           N  
ATOM   1448  CA  CYS B  65      29.410   4.735  55.785  1.00 34.01           C  
ATOM   1449  C   CYS B  65      29.543   5.530  57.089  1.00 38.30           C  
ATOM   1450  O   CYS B  65      29.729   6.755  57.070  1.00 34.79           O  
ATOM   1451  CB  CYS B  65      28.084   5.074  55.084  1.00 34.25           C  
ATOM   1452  SG  CYS B  65      27.918   4.292  53.431  1.00 43.33           S  
ATOM   1453  N   THR B  66      29.458   4.837  58.221  1.00 38.82           N  
ATOM   1454  CA  THR B  66      29.570   5.491  59.531  1.00 38.73           C  
ATOM   1455  C   THR B  66      30.981   6.028  59.741  1.00 34.93           C  
ATOM   1456  O   THR B  66      31.175   7.096  60.310  1.00 35.43           O  
ATOM   1457  CB  THR B  66      29.216   4.521  60.673  1.00 42.28           C  
ATOM   1458  OG1 THR B  66      27.887   4.022  60.474  1.00 45.62           O  
ATOM   1459  CG2 THR B  66      29.295   5.224  62.029  1.00 40.08           C  
ATOM   1460  N   SER B  67      31.959   5.282  59.240  1.00 36.63           N  
ATOM   1461  CA  SER B  67      33.372   5.615  59.401  1.00 37.22           C  
ATOM   1462  C   SER B  67      33.767   6.921  58.710  1.00 35.29           C  
ATOM   1463  O   SER B  67      34.842   7.469  58.965  1.00 33.50           O  
ATOM   1464  CB  SER B  67      34.234   4.482  58.853  1.00 34.42           C  
ATOM   1465  OG  SER B  67      34.172   3.342  59.667  1.00 41.88           O  
HETATM 1466  N   MSE B  68      32.915   7.421  57.825  1.00 32.27           N  
HETATM 1467  CA  MSE B  68      33.256   8.642  57.097  1.00 34.58           C  
HETATM 1468  C   MSE B  68      33.029   9.899  57.949  1.00 35.26           C  
HETATM 1469  O   MSE B  68      33.234  11.018  57.483  1.00 36.56           O  
HETATM 1470  CB  MSE B  68      32.473   8.714  55.789  1.00 33.13           C  
HETATM 1471  CG  MSE B  68      32.633   7.466  54.919  1.00 33.46           C  
HETATM 1472 SE   MSE B  68      32.266   7.801  53.003  1.00 49.58          SE  
HETATM 1473  CE  MSE B  68      34.124   7.794  52.287  1.00 29.34           C  
ATOM   1474  N   GLY B  69      32.629   9.709  59.204  1.00 35.61           N  
ATOM   1475  CA  GLY B  69      32.609  10.795  60.172  1.00 33.24           C  
ATOM   1476  C   GLY B  69      31.582  11.887  59.917  1.00 34.12           C  
ATOM   1477  O   GLY B  69      30.584  11.657  59.239  1.00 33.06           O  
ATOM   1478  N   PRO B  70      31.824  13.084  60.475  1.00 30.25           N  
ATOM   1479  CA  PRO B  70      30.913  14.228  60.419  1.00 33.56           C  
ATOM   1480  C   PRO B  70      30.969  14.969  59.094  1.00 39.37           C  
ATOM   1481  O   PRO B  70      31.842  14.690  58.273  1.00 42.38           O  
ATOM   1482  CB  PRO B  70      31.424  15.128  61.546  1.00 37.87           C  
ATOM   1483  CG  PRO B  70      32.897  14.866  61.568  1.00 40.38           C  
ATOM   1484  CD  PRO B  70      33.050  13.396  61.236  1.00 37.37           C  
ATOM   1485  N   HIS B  71      30.043  15.904  58.902  1.00 39.49           N  
ATOM   1486  CA  HIS B  71      30.043  16.776  57.740  1.00 42.59           C  
ATOM   1487  C   HIS B  71      31.381  17.484  57.616  1.00 41.19           C  
ATOM   1488  O   HIS B  71      32.008  17.808  58.617  1.00 42.38           O  
ATOM   1489  CB  HIS B  71      28.898  17.785  57.835  1.00 45.02           C  
ATOM   1490  CG  HIS B  71      27.549  17.182  57.588  1.00 51.25           C  
ATOM   1491  ND1 HIS B  71      26.442  17.933  57.250  1.00 60.96           N  
ATOM   1492  CD2 HIS B  71      27.133  15.893  57.610  1.00 54.27           C  
ATOM   1493  CE1 HIS B  71      25.401  17.134  57.087  1.00 57.75           C  
ATOM   1494  NE2 HIS B  71      25.793  15.891  57.299  1.00 51.13           N  
ATOM   1495  N   PHE B  72      31.833  17.703  56.384  1.00 42.15           N  
ATOM   1496  CA  PHE B  72      33.152  18.290  56.168  1.00 42.19           C  
ATOM   1497  C   PHE B  72      33.073  19.799  56.038  1.00 51.53           C  
ATOM   1498  O   PHE B  72      32.225  20.342  55.333  1.00 50.70           O  
ATOM   1499  CB  PHE B  72      33.826  17.683  54.932  1.00 40.09           C  
ATOM   1500  CG  PHE B  72      35.123  18.356  54.545  1.00 43.82           C  
ATOM   1501  CD1 PHE B  72      36.168  18.456  55.445  1.00 46.49           C  
ATOM   1502  CD2 PHE B  72      35.299  18.870  53.269  1.00 41.11           C  
ATOM   1503  CE1 PHE B  72      37.358  19.068  55.081  1.00 47.85           C  
ATOM   1504  CE2 PHE B  72      36.481  19.484  52.904  1.00 41.76           C  
ATOM   1505  CZ  PHE B  72      37.513  19.580  53.803  1.00 40.14           C  
ATOM   1506  N   ASN B  73      33.981  20.455  56.749  1.00 61.16           N  
ATOM   1507  CA  ASN B  73      34.135  21.902  56.735  1.00 68.90           C  
ATOM   1508  C   ASN B  73      35.140  22.363  55.670  1.00 66.19           C  
ATOM   1509  O   ASN B  73      36.349  22.381  55.913  1.00 68.61           O  
ATOM   1510  CB  ASN B  73      34.587  22.374  58.119  1.00 69.07           C  
ATOM   1511  CG  ASN B  73      35.897  21.728  58.553  1.00 75.16           C  
ATOM   1512  OD1 ASN B  73      36.058  20.503  58.500  1.00 75.36           O  
ATOM   1513  ND2 ASN B  73      36.855  22.559  58.950  1.00 84.38           N  
ATOM   1514  N   PRO B  74      34.658  22.771  54.487  1.00 66.70           N  
ATOM   1515  CA  PRO B  74      35.644  23.179  53.474  1.00 69.54           C  
ATOM   1516  C   PRO B  74      36.335  24.492  53.848  1.00 75.06           C  
ATOM   1517  O   PRO B  74      37.017  25.119  53.024  1.00 77.10           O  
ATOM   1518  CB  PRO B  74      34.810  23.329  52.188  1.00 65.79           C  
ATOM   1519  CG  PRO B  74      33.385  22.917  52.565  1.00 65.60           C  
ATOM   1520  CD  PRO B  74      33.280  23.027  54.051  1.00 68.43           C  
ATOM   1521  N   PHE B  75      36.158  24.916  55.094  1.00 79.32           N  
ATOM   1522  CA  PHE B  75      36.725  26.176  55.540  1.00 79.25           C  
ATOM   1523  C   PHE B  75      37.742  25.959  56.684  1.00 78.98           C  
ATOM   1524  O   PHE B  75      37.477  25.244  57.656  1.00 81.53           O  
ATOM   1525  CB  PHE B  75      35.605  27.128  55.972  1.00 78.29           C  
ATOM   1526  CG  PHE B  75      34.788  27.647  54.851  1.00 82.07           C  
ATOM   1527  CD1 PHE B  75      34.083  26.800  54.022  1.00 81.14           C  
ATOM   1528  CD2 PHE B  75      34.755  29.008  54.601  1.00 83.42           C  
ATOM   1529  CE1 PHE B  75      33.359  27.285  52.975  1.00 81.64           C  
ATOM   1530  CE2 PHE B  75      34.013  29.508  53.555  1.00 83.89           C  
ATOM   1531  CZ  PHE B  75      33.316  28.634  52.743  1.00 83.25           C  
ATOM   1532  N   LEU B  92      25.714  20.812  49.329  1.00 57.84           N  
ATOM   1533  CA  LEU B  92      25.330  20.223  48.047  1.00 55.25           C  
ATOM   1534  C   LEU B  92      23.812  20.234  47.861  1.00 58.67           C  
ATOM   1535  O   LEU B  92      23.318  20.302  46.732  1.00 62.74           O  
ATOM   1536  CB  LEU B  92      25.855  18.791  47.929  1.00 48.01           C  
ATOM   1537  CG  LEU B  92      27.275  18.597  47.399  1.00 48.15           C  
ATOM   1538  CD1 LEU B  92      28.268  19.444  48.159  1.00 43.59           C  
ATOM   1539  CD2 LEU B  92      27.662  17.140  47.492  1.00 44.72           C  
ATOM   1540  N   GLY B  93      23.081  20.152  48.971  1.00 56.80           N  
ATOM   1541  CA  GLY B  93      21.632  20.199  48.944  1.00 54.41           C  
ATOM   1542  C   GLY B  93      21.025  18.830  48.734  1.00 54.51           C  
ATOM   1543  O   GLY B  93      21.625  17.813  49.088  1.00 54.51           O  
ATOM   1544  N   ASN B  94      19.828  18.805  48.159  1.00 52.38           N  
ATOM   1545  CA  ASN B  94      19.140  17.552  47.881  1.00 52.35           C  
ATOM   1546  C   ASN B  94      19.307  17.127  46.432  1.00 51.67           C  
ATOM   1547  O   ASN B  94      19.445  17.965  45.547  1.00 52.02           O  
ATOM   1548  CB  ASN B  94      17.648  17.664  48.203  1.00 50.28           C  
ATOM   1549  CG  ASN B  94      17.381  17.877  49.679  1.00 62.25           C  
ATOM   1550  OD1 ASN B  94      17.978  17.220  50.532  1.00 61.96           O  
ATOM   1551  ND2 ASN B  94      16.470  18.790  49.988  1.00 65.20           N  
ATOM   1552  N   ILE B  95      19.309  15.818  46.204  1.00 48.75           N  
ATOM   1553  CA  ILE B  95      19.144  15.267  44.871  1.00 46.25           C  
ATOM   1554  C   ILE B  95      17.787  14.600  44.793  1.00 49.04           C  
ATOM   1555  O   ILE B  95      17.229  14.185  45.810  1.00 47.31           O  
ATOM   1556  CB  ILE B  95      20.215  14.227  44.515  1.00 46.26           C  
ATOM   1557  CG1 ILE B  95      20.158  13.072  45.510  1.00 47.52           C  
ATOM   1558  CG2 ILE B  95      21.600  14.860  44.478  1.00 47.21           C  
ATOM   1559  CD1 ILE B  95      20.881  11.848  45.054  1.00 47.11           C  
ATOM   1560  N   VAL B  96      17.257  14.494  43.582  1.00 48.00           N  
ATOM   1561  CA  VAL B  96      15.994  13.810  43.378  1.00 49.46           C  
ATOM   1562  C   VAL B  96      16.242  12.496  42.651  1.00 48.82           C  
ATOM   1563  O   VAL B  96      16.827  12.472  41.565  1.00 47.12           O  
ATOM   1564  CB  VAL B  96      14.992  14.674  42.586  1.00 47.50           C  
ATOM   1565  CG1 VAL B  96      13.671  13.953  42.455  1.00 47.98           C  
ATOM   1566  CG2 VAL B  96      14.778  16.010  43.284  1.00 45.58           C  
ATOM   1567  N   VAL B  97      15.831  11.404  43.281  1.00 43.94           N  
ATOM   1568  CA  VAL B  97      15.856  10.097  42.651  1.00 44.74           C  
ATOM   1569  C   VAL B  97      14.492   9.851  42.025  1.00 47.84           C  
ATOM   1570  O   VAL B  97      13.473  10.089  42.671  1.00 46.36           O  
ATOM   1571  CB  VAL B  97      16.190   9.000  43.663  1.00 42.86           C  
ATOM   1572  CG1 VAL B  97      16.073   7.633  43.025  1.00 43.29           C  
ATOM   1573  CG2 VAL B  97      17.589   9.226  44.236  1.00 42.87           C  
ATOM   1574  N   ASN B  98      14.465   9.392  40.773  1.00 47.99           N  
ATOM   1575  CA  ASN B  98      13.194   9.212  40.072  1.00 45.12           C  
ATOM   1576  C   ASN B  98      12.593   7.842  40.359  1.00 50.93           C  
ATOM   1577  O   ASN B  98      13.129   7.078  41.163  1.00 50.39           O  
ATOM   1578  CB  ASN B  98      13.355   9.447  38.557  1.00 47.67           C  
ATOM   1579  CG  ASN B  98      14.259   8.421  37.865  1.00 54.22           C  
ATOM   1580  OD1 ASN B  98      14.439   7.288  38.327  1.00 53.70           O  
ATOM   1581  ND2 ASN B  98      14.823   8.824  36.730  1.00 50.53           N  
ATOM   1582  N   ASN B  99      11.475   7.533  39.709  1.00 56.55           N  
ATOM   1583  CA  ASN B  99      10.748   6.303  40.007  1.00 56.44           C  
ATOM   1584  C   ASN B  99      11.495   5.053  39.568  1.00 55.30           C  
ATOM   1585  O   ASN B  99      11.285   3.979  40.123  1.00 58.09           O  
ATOM   1586  CB  ASN B  99       9.361   6.338  39.368  1.00 63.93           C  
ATOM   1587  CG  ASN B  99       8.462   7.387  39.993  1.00 68.95           C  
ATOM   1588  OD1 ASN B  99       7.822   8.178  39.293  1.00 75.67           O  
ATOM   1589  ND2 ASN B  99       8.411   7.402  41.323  1.00 64.35           N  
ATOM   1590  N   ASN B 100      12.369   5.204  38.578  1.00 53.50           N  
ATOM   1591  CA  ASN B 100      13.260   4.133  38.155  1.00 52.12           C  
ATOM   1592  C   ASN B 100      14.390   3.865  39.156  1.00 52.57           C  
ATOM   1593  O   ASN B 100      15.181   2.932  38.984  1.00 52.36           O  
ATOM   1594  CB  ASN B 100      13.872   4.466  36.794  1.00 56.32           C  
ATOM   1595  CG  ASN B 100      12.838   4.559  35.694  1.00 64.77           C  
ATOM   1596  OD1 ASN B 100      12.835   5.512  34.908  1.00 71.75           O  
ATOM   1597  ND2 ASN B 100      11.953   3.567  35.627  1.00 62.70           N  
ATOM   1598  N   GLY B 101      14.488   4.703  40.182  1.00 51.11           N  
ATOM   1599  CA  GLY B 101      15.537   4.558  41.176  1.00 50.26           C  
ATOM   1600  C   GLY B 101      16.855   5.183  40.749  1.00 48.08           C  
ATOM   1601  O   GLY B 101      17.895   4.960  41.378  1.00 40.67           O  
ATOM   1602  N   GLU B 102      16.810   5.983  39.687  1.00 50.00           N  
ATOM   1603  CA  GLU B 102      18.016   6.605  39.157  1.00 45.72           C  
ATOM   1604  C   GLU B 102      18.066   8.107  39.407  1.00 44.05           C  
ATOM   1605  O   GLU B 102      17.032   8.761  39.508  1.00 45.83           O  
ATOM   1606  CB  GLU B 102      18.128   6.341  37.657  1.00 43.43           C  
ATOM   1607  CG  GLU B 102      18.366   4.896  37.290  1.00 45.18           C  
ATOM   1608  CD  GLU B 102      18.418   4.698  35.786  1.00 51.80           C  
ATOM   1609  OE1 GLU B 102      19.173   3.821  35.316  1.00 56.07           O  
ATOM   1610  OE2 GLU B 102      17.704   5.429  35.070  1.00 54.62           O  
ATOM   1611  N   CYS B 103      19.279   8.647  39.496  1.00 39.18           N  
ATOM   1612  CA  CYS B 103      19.482  10.094  39.548  1.00 39.62           C  
ATOM   1613  C   CYS B 103      20.554  10.501  38.553  1.00 40.28           C  
ATOM   1614  O   CYS B 103      21.723  10.137  38.712  1.00 38.06           O  
ATOM   1615  CB  CYS B 103      19.888  10.561  40.949  1.00 34.97           C  
ATOM   1616  SG  CYS B 103      20.284  12.358  41.046  1.00 37.14           S  
ATOM   1617  N   ASN B 104      20.158  11.277  37.550  1.00 37.70           N  
ATOM   1618  CA  ASN B 104      21.060  11.687  36.484  1.00 39.48           C  
ATOM   1619  C   ASN B 104      21.185  13.194  36.376  1.00 38.38           C  
ATOM   1620  O   ASN B 104      21.540  13.731  35.325  1.00 40.09           O  
ATOM   1621  CB  ASN B 104      20.592  11.107  35.155  1.00 38.78           C  
ATOM   1622  CG  ASN B 104      20.844   9.613  35.063  1.00 43.77           C  
ATOM   1623  OD1 ASN B 104      21.996   9.165  35.102  1.00 40.26           O  
ATOM   1624  ND2 ASN B 104      19.776   8.835  34.947  1.00 37.79           N  
ATOM   1625  N   GLU B 105      20.912  13.882  37.471  1.00 34.71           N  
ATOM   1626  CA  GLU B 105      20.930  15.330  37.436  1.00 42.09           C  
ATOM   1627  C   GLU B 105      22.339  15.884  37.541  1.00 38.95           C  
ATOM   1628  O   GLU B 105      23.292  15.185  37.887  1.00 35.23           O  
ATOM   1629  CB  GLU B 105      20.058  15.914  38.550  1.00 44.76           C  
ATOM   1630  CG  GLU B 105      20.532  15.644  39.942  1.00 46.22           C  
ATOM   1631  CD  GLU B 105      19.581  16.219  40.988  1.00 52.06           C  
ATOM   1632  OE1 GLU B 105      18.831  15.444  41.618  1.00 47.86           O  
ATOM   1633  OE2 GLU B 105      19.576  17.454  41.174  1.00 50.09           O  
ATOM   1634  N   ILE B 106      22.443  17.166  37.249  1.00 34.51           N  
ATOM   1635  CA  ILE B 106      23.700  17.868  37.293  1.00 37.94           C  
ATOM   1636  C   ILE B 106      23.490  19.104  38.138  1.00 39.33           C  
ATOM   1637  O   ILE B 106      22.519  19.827  37.953  1.00 37.13           O  
ATOM   1638  CB  ILE B 106      24.180  18.234  35.871  1.00 41.05           C  
ATOM   1639  CG1 ILE B 106      24.441  16.962  35.080  1.00 38.42           C  
ATOM   1640  CG2 ILE B 106      25.428  19.084  35.903  1.00 39.08           C  
ATOM   1641  CD1 ILE B 106      24.870  17.215  33.697  1.00 39.68           C  
ATOM   1642  N   ILE B 107      24.372  19.318  39.106  1.00 39.55           N  
ATOM   1643  CA  ILE B 107      24.337  20.549  39.870  1.00 39.85           C  
ATOM   1644  C   ILE B 107      25.709  21.183  39.765  1.00 40.59           C  
ATOM   1645  O   ILE B 107      26.647  20.553  39.282  1.00 43.53           O  
ATOM   1646  CB  ILE B 107      23.953  20.318  41.330  1.00 44.58           C  
ATOM   1647  CG1 ILE B 107      25.083  19.625  42.079  1.00 40.04           C  
ATOM   1648  CG2 ILE B 107      22.662  19.506  41.423  1.00 43.99           C  
ATOM   1649  CD1 ILE B 107      24.717  19.280  43.486  1.00 42.44           C  
ATOM   1650  N   CYS B 108      25.819  22.437  40.170  1.00 35.17           N  
ATOM   1651  CA  CYS B 108      27.100  23.116  40.144  1.00 38.07           C  
ATOM   1652  C   CYS B 108      27.215  23.869  41.456  1.00 44.18           C  
ATOM   1653  O   CYS B 108      26.327  24.642  41.818  1.00 43.50           O  
ATOM   1654  CB  CYS B 108      27.223  24.057  38.938  1.00 41.81           C  
ATOM   1655  SG  CYS B 108      28.896  24.143  38.189  1.00 53.98           S  
ATOM   1656  N   VAL B 109      28.297  23.608  42.177  1.00 37.98           N  
ATOM   1657  CA  VAL B 109      28.483  24.133  43.516  1.00 37.92           C  
ATOM   1658  C   VAL B 109      29.609  25.133  43.469  1.00 42.60           C  
ATOM   1659  O   VAL B 109      30.741  24.789  43.085  1.00 37.21           O  
ATOM   1660  CB  VAL B 109      28.797  23.007  44.514  1.00 36.36           C  
ATOM   1661  CG1 VAL B 109      29.124  23.573  45.889  1.00 38.83           C  
ATOM   1662  CG2 VAL B 109      27.621  22.037  44.584  1.00 36.65           C  
ATOM   1663  N   LYS B 110      29.302  26.371  43.845  1.00 40.03           N  
ATOM   1664  CA  LYS B 110      30.208  27.487  43.582  1.00 45.15           C  
ATOM   1665  C   LYS B 110      31.560  27.319  44.266  1.00 49.19           C  
ATOM   1666  O   LYS B 110      32.596  27.615  43.664  1.00 47.70           O  
ATOM   1667  CB  LYS B 110      29.578  28.818  44.000  1.00 45.69           C  
ATOM   1668  CG  LYS B 110      30.449  30.014  43.628  1.00 54.18           C  
ATOM   1669  CD  LYS B 110      29.828  31.346  44.031  1.00 61.96           C  
ATOM   1670  CE  LYS B 110      30.895  32.325  44.529  1.00 63.47           C  
ATOM   1671  NZ  LYS B 110      32.140  32.294  43.698  1.00 65.79           N  
ATOM   1672  N   TYR B 111      31.553  26.833  45.505  1.00 42.48           N  
ATOM   1673  CA  TYR B 111      32.798  26.623  46.234  1.00 49.50           C  
ATOM   1674  C   TYR B 111      32.903  25.179  46.702  1.00 48.54           C  
ATOM   1675  O   TYR B 111      32.218  24.778  47.641  1.00 50.95           O  
ATOM   1676  CB  TYR B 111      32.890  27.564  47.439  1.00 54.57           C  
ATOM   1677  CG  TYR B 111      34.116  27.339  48.301  1.00 58.90           C  
ATOM   1678  CD1 TYR B 111      35.351  27.887  47.950  1.00 64.67           C  
ATOM   1679  CD2 TYR B 111      34.042  26.567  49.459  1.00 65.52           C  
ATOM   1680  CE1 TYR B 111      36.484  27.685  48.734  1.00 59.98           C  
ATOM   1681  CE2 TYR B 111      35.164  26.355  50.260  1.00 67.59           C  
ATOM   1682  CZ  TYR B 111      36.385  26.914  49.893  1.00 68.63           C  
ATOM   1683  OH  TYR B 111      37.501  26.708  50.675  1.00 68.61           O  
ATOM   1684  N   LEU B 112      33.755  24.400  46.049  1.00 38.72           N  
ATOM   1685  CA  LEU B 112      33.877  22.983  46.359  1.00 36.04           C  
ATOM   1686  C   LEU B 112      35.189  22.499  45.766  1.00 33.53           C  
ATOM   1687  O   LEU B 112      35.217  21.928  44.677  1.00 31.35           O  
ATOM   1688  CB  LEU B 112      32.681  22.205  45.802  1.00 31.80           C  
ATOM   1689  CG  LEU B 112      32.393  20.815  46.359  1.00 36.21           C  
ATOM   1690  CD1 LEU B 112      32.074  20.873  47.883  1.00 36.03           C  
ATOM   1691  CD2 LEU B 112      31.258  20.177  45.581  1.00 27.98           C  
ATOM   1692  N   PRO B 113      36.296  22.755  46.469  1.00 35.00           N  
ATOM   1693  CA  PRO B 113      37.590  22.519  45.827  1.00 31.19           C  
ATOM   1694  C   PRO B 113      37.955  21.035  45.785  1.00 29.97           C  
ATOM   1695  O   PRO B 113      37.692  20.312  46.746  1.00 32.26           O  
ATOM   1696  CB  PRO B 113      38.559  23.308  46.707  1.00 29.90           C  
ATOM   1697  CG  PRO B 113      37.934  23.257  48.070  1.00 36.10           C  
ATOM   1698  CD  PRO B 113      36.435  23.257  47.852  1.00 36.74           C  
ATOM   1699  N   LEU B 114      38.553  20.593  44.683  1.00 25.43           N  
ATOM   1700  CA  LEU B 114      38.998  19.204  44.556  1.00 27.47           C  
ATOM   1701  C   LEU B 114      40.473  19.094  44.890  1.00 27.44           C  
ATOM   1702  O   LEU B 114      40.976  17.995  45.122  1.00 26.44           O  
ATOM   1703  CB  LEU B 114      38.746  18.655  43.140  1.00 23.49           C  
ATOM   1704  CG  LEU B 114      37.333  18.697  42.551  1.00 24.57           C  
ATOM   1705  CD1 LEU B 114      37.312  18.135  41.110  1.00 22.59           C  
ATOM   1706  CD2 LEU B 114      36.319  17.983  43.427  1.00 24.48           C  
ATOM   1707  N   THR B 115      41.160  20.237  44.906  1.00 23.68           N  
ATOM   1708  CA  THR B 115      42.578  20.299  45.239  1.00 29.18           C  
ATOM   1709  C   THR B 115      42.838  21.358  46.326  1.00 31.33           C  
ATOM   1710  O   THR B 115      41.976  22.192  46.599  1.00 28.00           O  
ATOM   1711  CB  THR B 115      43.430  20.636  44.003  1.00 32.16           C  
ATOM   1712  OG1 THR B 115      43.077  21.943  43.543  1.00 33.73           O  
ATOM   1713  CG2 THR B 115      43.173  19.640  42.888  1.00 33.32           C  
ATOM   1714  N   GLY B 116      44.022  21.325  46.932  1.00 27.28           N  
ATOM   1715  CA  GLY B 116      44.377  22.277  47.967  1.00 28.24           C  
ATOM   1716  C   GLY B 116      44.092  21.710  49.345  1.00 34.74           C  
ATOM   1717  O   GLY B 116      43.584  20.596  49.468  1.00 32.20           O  
ATOM   1718  N   SER B 117      44.399  22.478  50.386  1.00 36.76           N  
ATOM   1719  CA  SER B 117      44.328  21.972  51.756  1.00 38.91           C  
ATOM   1720  C   SER B 117      42.898  21.665  52.201  1.00 33.68           C  
ATOM   1721  O   SER B 117      42.686  20.816  53.054  1.00 33.84           O  
ATOM   1722  CB  SER B 117      44.977  22.962  52.730  1.00 39.87           C  
ATOM   1723  OG  SER B 117      44.253  24.171  52.796  1.00 40.68           O  
ATOM   1724  N   ASN B 118      41.917  22.326  51.598  1.00 34.05           N  
ATOM   1725  CA  ASN B 118      40.518  22.041  51.899  1.00 33.40           C  
ATOM   1726  C   ASN B 118      39.807  21.196  50.832  1.00 30.59           C  
ATOM   1727  O   ASN B 118      38.582  21.242  50.715  1.00 31.02           O  
ATOM   1728  CB  ASN B 118      39.770  23.352  52.097  1.00 42.99           C  
ATOM   1729  CG  ASN B 118      40.022  24.333  50.973  1.00 47.49           C  
ATOM   1730  OD1 ASN B 118      40.758  24.037  50.016  1.00 47.68           O  
ATOM   1731  ND2 ASN B 118      39.418  25.514  51.078  1.00 52.36           N  
ATOM   1732  N   GLN B 119      40.579  20.423  50.070  1.00 29.84           N  
ATOM   1733  CA  GLN B 119      40.048  19.599  48.977  1.00 28.64           C  
ATOM   1734  C   GLN B 119      39.105  18.535  49.506  1.00 27.20           C  
ATOM   1735  O   GLN B 119      39.262  18.080  50.642  1.00 26.45           O  
ATOM   1736  CB  GLN B 119      41.185  18.918  48.211  1.00 26.44           C  
ATOM   1737  CG  GLN B 119      41.915  17.847  49.040  1.00 25.75           C  
ATOM   1738  CD  GLN B 119      43.098  17.257  48.329  1.00 26.38           C  
ATOM   1739  OE1 GLN B 119      43.133  17.159  47.085  1.00 30.90           O  
ATOM   1740  NE2 GLN B 119      44.086  16.862  49.098  1.00 21.95           N  
ATOM   1741  N   ILE B 120      38.145  18.121  48.681  1.00 25.94           N  
ATOM   1742  CA  ILE B 120      37.253  17.029  49.054  1.00 26.77           C  
ATOM   1743  C   ILE B 120      37.675  15.697  48.448  1.00 28.50           C  
ATOM   1744  O   ILE B 120      37.098  14.657  48.766  1.00 24.86           O  
ATOM   1745  CB  ILE B 120      35.805  17.316  48.645  1.00 28.88           C  
ATOM   1746  CG1 ILE B 120      35.666  17.365  47.116  1.00 26.29           C  
ATOM   1747  CG2 ILE B 120      35.327  18.609  49.305  1.00 28.56           C  
ATOM   1748  CD1 ILE B 120      34.253  17.567  46.640  1.00 24.84           C  
ATOM   1749  N   ILE B 121      38.671  15.725  47.565  1.00 27.29           N  
ATOM   1750  CA  ILE B 121      39.245  14.487  47.060  1.00 24.11           C  
ATOM   1751  C   ILE B 121      39.938  13.788  48.215  1.00 24.91           C  
ATOM   1752  O   ILE B 121      40.688  14.417  48.968  1.00 25.90           O  
ATOM   1753  CB  ILE B 121      40.240  14.725  45.892  1.00 24.29           C  
ATOM   1754  CG1 ILE B 121      39.482  15.023  44.589  1.00 22.57           C  
ATOM   1755  CG2 ILE B 121      41.131  13.481  45.676  1.00 22.68           C  
ATOM   1756  CD1 ILE B 121      40.398  15.258  43.385  1.00 20.97           C  
ATOM   1757  N   GLY B 122      39.670  12.495  48.373  1.00 24.30           N  
ATOM   1758  CA  GLY B 122      40.214  11.739  49.492  1.00 26.15           C  
ATOM   1759  C   GLY B 122      39.234  11.651  50.651  1.00 25.16           C  
ATOM   1760  O   GLY B 122      39.467  10.940  51.632  1.00 27.10           O  
ATOM   1761  N   ARG B 123      38.127  12.373  50.529  1.00 23.50           N  
ATOM   1762  CA  ARG B 123      37.107  12.409  51.564  1.00 26.76           C  
ATOM   1763  C   ARG B 123      35.833  11.734  51.070  1.00 28.68           C  
ATOM   1764  O   ARG B 123      35.841  11.078  50.017  1.00 27.27           O  
ATOM   1765  CB  ARG B 123      36.854  13.852  51.998  1.00 24.12           C  
ATOM   1766  CG  ARG B 123      38.154  14.508  52.453  1.00 24.26           C  
ATOM   1767  CD  ARG B 123      37.944  15.788  53.223  1.00 29.45           C  
ATOM   1768  NE  ARG B 123      39.217  16.433  53.519  1.00 29.02           N  
ATOM   1769  CZ  ARG B 123      39.993  16.103  54.545  1.00 31.64           C  
ATOM   1770  NH1 ARG B 123      39.609  15.145  55.380  1.00 27.41           N  
ATOM   1771  NH2 ARG B 123      41.142  16.733  54.739  1.00 29.54           N  
ATOM   1772  N   GLY B 124      34.748  11.865  51.831  1.00 27.16           N  
ATOM   1773  CA  GLY B 124      33.552  11.091  51.541  1.00 30.35           C  
ATOM   1774  C   GLY B 124      32.357  11.813  50.944  1.00 32.31           C  
ATOM   1775  O   GLY B 124      32.105  12.973  51.222  1.00 29.15           O  
ATOM   1776  N   LEU B 125      31.614  11.113  50.102  1.00 29.99           N  
ATOM   1777  CA  LEU B 125      30.327  11.618  49.667  1.00 28.09           C  
ATOM   1778  C   LEU B 125      29.291  10.685  50.235  1.00 28.24           C  
ATOM   1779  O   LEU B 125      29.400   9.483  50.055  1.00 33.09           O  
ATOM   1780  CB  LEU B 125      30.230  11.673  48.147  1.00 28.39           C  
ATOM   1781  CG  LEU B 125      28.870  12.051  47.546  1.00 30.32           C  
ATOM   1782  CD1 LEU B 125      28.519  13.505  47.835  1.00 28.99           C  
ATOM   1783  CD2 LEU B 125      28.875  11.784  46.045  1.00 28.93           C  
ATOM   1784  N   VAL B 126      28.299  11.219  50.935  1.00 28.54           N  
ATOM   1785  CA  VAL B 126      27.277  10.363  51.542  1.00 33.28           C  
ATOM   1786  C   VAL B 126      25.882  10.770  51.111  1.00 33.41           C  
ATOM   1787  O   VAL B 126      25.539  11.947  51.195  1.00 33.10           O  
ATOM   1788  CB  VAL B 126      27.330  10.404  53.082  1.00 35.00           C  
ATOM   1789  CG1 VAL B 126      26.149   9.603  53.706  1.00 30.83           C  
ATOM   1790  CG2 VAL B 126      28.673   9.902  53.583  1.00 31.01           C  
ATOM   1791  N   ILE B 127      25.090   9.794  50.663  1.00 31.96           N  
ATOM   1792  CA  ILE B 127      23.674  10.009  50.347  1.00 38.61           C  
ATOM   1793  C   ILE B 127      22.814   9.621  51.548  1.00 43.14           C  
ATOM   1794  O   ILE B 127      22.874   8.480  52.023  1.00 42.62           O  
ATOM   1795  CB  ILE B 127      23.206   9.177  49.118  1.00 38.54           C  
ATOM   1796  CG1 ILE B 127      24.152   9.345  47.925  1.00 38.87           C  
ATOM   1797  CG2 ILE B 127      21.780   9.543  48.726  1.00 38.23           C  
ATOM   1798  CD1 ILE B 127      24.209  10.744  47.376  1.00 41.61           C  
ATOM   1799  N   HIS B 128      22.011  10.560  52.036  1.00 45.01           N  
ATOM   1800  CA  HIS B 128      21.176  10.318  53.216  1.00 48.10           C  
ATOM   1801  C   HIS B 128      19.732  10.048  52.785  1.00 52.37           C  
ATOM   1802  O   HIS B 128      19.283  10.569  51.770  1.00 49.90           O  
ATOM   1803  CB  HIS B 128      21.231  11.511  54.173  1.00 44.04           C  
ATOM   1804  CG  HIS B 128      22.616  11.881  54.619  1.00 44.87           C  
ATOM   1805  ND1 HIS B 128      23.142  11.472  55.823  1.00 52.27           N  
ATOM   1806  CD2 HIS B 128      23.573  12.640  54.028  1.00 46.93           C  
ATOM   1807  CE1 HIS B 128      24.367  11.959  55.958  1.00 46.88           C  
ATOM   1808  NE2 HIS B 128      24.651  12.670  54.885  1.00 45.10           N  
ATOM   1809  N   GLU B 129      19.000   9.236  53.543  1.00 56.55           N  
ATOM   1810  CA  GLU B 129      17.631   8.903  53.152  1.00 60.16           C  
ATOM   1811  C   GLU B 129      16.665  10.068  53.350  1.00 55.96           C  
ATOM   1812  O   GLU B 129      15.581  10.079  52.774  1.00 62.01           O  
ATOM   1813  CB  GLU B 129      17.128   7.682  53.918  1.00 62.07           C  
ATOM   1814  CG  GLU B 129      17.246   7.775  55.418  1.00 67.94           C  
ATOM   1815  CD  GLU B 129      16.689   6.542  56.109  1.00 76.68           C  
ATOM   1816  OE1 GLU B 129      17.038   5.417  55.689  1.00 80.88           O  
ATOM   1817  OE2 GLU B 129      15.903   6.695  57.070  1.00 79.05           O  
ATOM   1818  N   LYS B 130      17.071  11.047  54.151  1.00 57.72           N  
ATOM   1819  CA  LYS B 130      16.242  12.221  54.435  1.00 65.92           C  
ATOM   1820  C   LYS B 130      16.752  13.471  53.710  1.00 63.00           C  
ATOM   1821  O   LYS B 130      17.958  13.705  53.639  1.00 59.92           O  
ATOM   1822  CB  LYS B 130      16.190  12.473  55.951  1.00 67.49           C  
ATOM   1823  CG  LYS B 130      15.651  13.846  56.374  1.00 74.04           C  
ATOM   1824  CD  LYS B 130      14.192  14.049  55.951  1.00 72.20           C  
ATOM   1825  CE  LYS B 130      13.592  15.327  56.542  1.00 73.05           C  
ATOM   1826  NZ  LYS B 130      14.616  16.334  56.943  1.00 77.25           N  
ATOM   1827  N   GLU B 131      15.833  14.273  53.178  1.00 66.57           N  
ATOM   1828  CA  GLU B 131      16.204  15.521  52.514  1.00 65.33           C  
ATOM   1829  C   GLU B 131      16.671  16.575  53.523  1.00 66.87           C  
ATOM   1830  O   GLU B 131      16.469  16.432  54.731  1.00 68.24           O  
ATOM   1831  CB  GLU B 131      15.032  16.071  51.681  1.00 66.40           C  
ATOM   1832  CG  GLU B 131      13.911  16.735  52.488  1.00 71.75           C  
ATOM   1833  CD  GLU B 131      12.825  17.368  51.610  1.00 74.27           C  
ATOM   1834  OE1 GLU B 131      12.379  16.729  50.630  1.00 70.79           O  
ATOM   1835  OE2 GLU B 131      12.414  18.512  51.905  1.00 76.48           O  
ATOM   1836  N   ASP B 132      17.303  17.631  53.021  1.00 67.36           N  
ATOM   1837  CA  ASP B 132      17.742  18.733  53.872  1.00 72.41           C  
ATOM   1838  C   ASP B 132      16.600  19.713  54.107  1.00 73.26           C  
ATOM   1839  O   ASP B 132      15.707  19.843  53.269  1.00 75.37           O  
ATOM   1840  CB  ASP B 132      18.940  19.456  53.249  1.00 71.79           C  
ATOM   1841  CG  ASP B 132      20.168  18.569  53.146  1.00 69.61           C  
ATOM   1842  OD1 ASP B 132      20.387  17.750  54.069  1.00 68.62           O  
ATOM   1843  OD2 ASP B 132      20.907  18.688  52.138  1.00 68.64           O  
ATOM   1844  N   ASP B 150      20.353   7.720  59.030  1.00 67.86           N  
ATOM   1845  CA  ASP B 150      20.930   6.568  58.353  1.00 68.04           C  
ATOM   1846  C   ASP B 150      21.491   6.976  56.986  1.00 66.44           C  
ATOM   1847  O   ASP B 150      20.863   7.714  56.220  1.00 61.94           O  
ATOM   1848  CB  ASP B 150      19.890   5.448  58.202  1.00 70.67           C  
ATOM   1849  CG  ASP B 150      20.462   4.194  57.550  1.00 73.34           C  
ATOM   1850  OD1 ASP B 150      21.313   3.521  58.176  1.00 76.79           O  
ATOM   1851  OD2 ASP B 150      20.059   3.881  56.407  1.00 76.81           O  
ATOM   1852  N   ARG B 151      22.690   6.486  56.701  1.00 61.88           N  
ATOM   1853  CA  ARG B 151      23.399   6.788  55.468  1.00 53.40           C  
ATOM   1854  C   ARG B 151      23.179   5.647  54.492  1.00 53.64           C  
ATOM   1855  O   ARG B 151      23.645   4.530  54.726  1.00 54.04           O  
ATOM   1856  CB  ARG B 151      24.888   6.994  55.758  1.00 46.74           C  
ATOM   1857  CG  ARG B 151      25.131   8.030  56.851  1.00 45.97           C  
ATOM   1858  CD  ARG B 151      26.544   8.012  57.409  1.00 42.50           C  
ATOM   1859  NE  ARG B 151      26.718   9.120  58.342  1.00 43.04           N  
ATOM   1860  CZ  ARG B 151      27.894   9.593  58.742  1.00 45.97           C  
ATOM   1861  NH1 ARG B 151      29.025   9.054  58.287  1.00 40.46           N  
ATOM   1862  NH2 ARG B 151      27.937  10.619  59.589  1.00 40.77           N  
ATOM   1863  N   ILE B 152      22.470   5.919  53.400  1.00 45.15           N  
ATOM   1864  CA  ILE B 152      22.015   4.836  52.545  1.00 46.51           C  
ATOM   1865  C   ILE B 152      23.037   4.506  51.465  1.00 45.99           C  
ATOM   1866  O   ILE B 152      23.017   3.409  50.901  1.00 44.17           O  
ATOM   1867  CB  ILE B 152      20.636   5.158  51.909  1.00 51.35           C  
ATOM   1868  CG1 ILE B 152      20.704   6.356  50.957  1.00 44.79           C  
ATOM   1869  CG2 ILE B 152      19.615   5.409  53.006  1.00 50.28           C  
ATOM   1870  CD1 ILE B 152      19.441   6.557  50.121  1.00 44.36           C  
ATOM   1871  N   ALA B 153      23.942   5.441  51.195  1.00 38.58           N  
ATOM   1872  CA  ALA B 153      25.005   5.196  50.231  1.00 37.81           C  
ATOM   1873  C   ALA B 153      26.185   6.138  50.458  1.00 37.61           C  
ATOM   1874  O   ALA B 153      26.005   7.301  50.846  1.00 32.93           O  
ATOM   1875  CB  ALA B 153      24.477   5.336  48.803  1.00 37.78           C  
ATOM   1876  N   CYS B 154      27.392   5.634  50.214  1.00 32.94           N  
ATOM   1877  CA  CYS B 154      28.578   6.468  50.318  1.00 31.64           C  
ATOM   1878  C   CYS B 154      29.702   5.956  49.424  1.00 32.48           C  
ATOM   1879  O   CYS B 154      29.689   4.807  48.967  1.00 29.03           O  
ATOM   1880  CB  CYS B 154      29.057   6.532  51.771  1.00 31.54           C  
ATOM   1881  SG  CYS B 154      29.602   4.922  52.400  1.00 35.68           S  
ATOM   1882  N   GLY B 155      30.682   6.819  49.187  1.00 28.69           N  
ATOM   1883  CA  GLY B 155      31.840   6.451  48.399  1.00 29.26           C  
ATOM   1884  C   GLY B 155      32.981   7.404  48.700  1.00 28.19           C  
ATOM   1885  O   GLY B 155      32.786   8.416  49.359  1.00 25.86           O  
ATOM   1886  N   ILE B 156      34.171   7.065  48.225  1.00 23.48           N  
ATOM   1887  CA  ILE B 156      35.345   7.906  48.385  1.00 25.13           C  
ATOM   1888  C   ILE B 156      35.514   8.767  47.136  1.00 27.06           C  
ATOM   1889  O   ILE B 156      35.386   8.268  46.014  1.00 26.52           O  
ATOM   1890  CB  ILE B 156      36.610   7.041  48.621  1.00 25.95           C  
ATOM   1891  CG1 ILE B 156      36.431   6.159  49.859  1.00 25.66           C  
ATOM   1892  CG2 ILE B 156      37.841   7.903  48.778  1.00 26.11           C  
ATOM   1893  CD1 ILE B 156      37.384   4.955  49.882  1.00 31.31           C  
ATOM   1894  N   ILE B 157      35.790  10.052  47.315  1.00 24.05           N  
ATOM   1895  CA  ILE B 157      35.988  10.933  46.164  1.00 25.65           C  
ATOM   1896  C   ILE B 157      37.438  10.842  45.718  1.00 26.02           C  
ATOM   1897  O   ILE B 157      38.354  11.137  46.496  1.00 23.77           O  
ATOM   1898  CB  ILE B 157      35.611  12.387  46.496  1.00 24.77           C  
ATOM   1899  CG1 ILE B 157      34.147  12.471  46.948  1.00 28.37           C  
ATOM   1900  CG2 ILE B 157      35.849  13.310  45.291  1.00 21.80           C  
ATOM   1901  CD1 ILE B 157      33.809  13.769  47.756  1.00 26.74           C  
ATOM   1902  N   ALA B 158      37.643  10.439  44.464  1.00 23.11           N  
ATOM   1903  CA  ALA B 158      38.975  10.076  43.972  1.00 25.99           C  
ATOM   1904  C   ALA B 158      39.340  10.813  42.683  1.00 28.30           C  
ATOM   1905  O   ALA B 158      38.459  11.362  42.032  1.00 25.29           O  
ATOM   1906  CB  ALA B 158      39.041   8.572  43.745  1.00 23.15           C  
ATOM   1907  N   TYR B 159      40.622  10.828  42.304  1.00 22.82           N  
ATOM   1908  CA  TYR B 159      40.983  11.376  40.986  1.00 26.24           C  
ATOM   1909  C   TYR B 159      40.435  10.479  39.887  1.00 25.54           C  
ATOM   1910  O   TYR B 159      40.638   9.267  39.913  1.00 24.06           O  
ATOM   1911  CB  TYR B 159      42.502  11.521  40.809  1.00 24.76           C  
ATOM   1912  CG  TYR B 159      43.088  12.751  41.484  1.00 26.25           C  
ATOM   1913  CD1 TYR B 159      43.047  14.011  40.872  1.00 26.10           C  
ATOM   1914  CD2 TYR B 159      43.687  12.650  42.735  1.00 22.47           C  
ATOM   1915  CE1 TYR B 159      43.604  15.157  41.523  1.00 25.04           C  
ATOM   1916  CE2 TYR B 159      44.245  13.765  43.378  1.00 21.03           C  
ATOM   1917  CZ  TYR B 159      44.199  15.010  42.776  1.00 26.55           C  
ATOM   1918  OH  TYR B 159      44.740  16.099  43.446  1.00 22.64           O  
ATOM   1919  N   LEU B 160      39.709  11.062  38.938  1.00 24.65           N  
ATOM   1920  CA  LEU B 160      39.281  10.297  37.767  1.00 28.26           C  
ATOM   1921  C   LEU B 160      40.524  10.031  36.979  1.00 32.57           C  
ATOM   1922  O   LEU B 160      40.776   8.927  36.492  1.00 33.15           O  
ATOM   1923  CB  LEU B 160      38.288  11.062  36.907  1.00 29.92           C  
ATOM   1924  CG  LEU B 160      38.014  10.347  35.573  1.00 31.83           C  
ATOM   1925  CD1 LEU B 160      37.146   9.124  35.820  1.00 22.71           C  
ATOM   1926  CD2 LEU B 160      37.370  11.295  34.569  1.00 27.66           C  
ATOM   1927  N   ASN B 161      41.299  11.103  36.952  1.00 34.74           N  
ATOM   1928  CA  ASN B 161      42.492  11.313  36.179  1.00 45.34           C  
ATOM   1929  C   ASN B 161      42.795  10.258  35.129  1.00 49.77           C  
ATOM   1930  O   ASN B 161      42.845  10.585  33.938  1.00 58.01           O  
ATOM   1931  CB  ASN B 161      43.658  11.478  37.135  1.00 31.38           C  
ATOM   1932  CG  ASN B 161      44.962  11.408  36.444  1.00 44.12           C  
ATOM   1933  OD1 ASN B 161      45.122  11.864  35.312  1.00 61.36           O  
ATOM   1934  ND2 ASN B 161      45.921  10.809  37.105  1.00 56.81           N  
TER    1935      ASN B 161                                                      
HETATM 1936  O   HOH A 201      48.078  17.679  66.433  1.00 49.39           O  
HETATM 1937  O   HOH A 202      66.652  -6.236  40.679  1.00 57.16           O  
HETATM 1938  O   HOH A 203      59.426  -5.605  51.728  1.00 36.97           O  
HETATM 1939  O   HOH A 204      52.932 -14.614  41.888  1.00 51.44           O  
HETATM 1940  O   HOH A 205      52.688  17.020  45.678  1.00 46.61           O  
HETATM 1941  O   HOH A 206      48.894   0.503  62.045  1.00 31.12           O  
HETATM 1942  O   HOH A 207      51.816   4.894  58.603  1.00 25.43           O  
HETATM 1943  O   HOH A 208      62.912  -9.112  43.467  1.00 42.55           O  
HETATM 1944  O   HOH A 209      58.500  16.507  35.636  1.00 55.99           O  
HETATM 1945  O   HOH A 210      46.516  12.312  61.342  1.00 35.21           O  
HETATM 1946  O   HOH A 211      53.926  -9.497  57.919  1.00 40.07           O  
HETATM 1947  O   HOH A 212      36.712   3.734  33.619  1.00 34.09           O  
HETATM 1948  O   HOH A 213      52.255  -2.447  59.945  1.00 26.51           O  
HETATM 1949  O   HOH A 214      47.228  -7.818  58.652  1.00 34.85           O  
HETATM 1950  O   HOH A 215      56.814 -12.835  41.800  1.00 45.46           O  
HETATM 1951  O   HOH A 216      43.827  -4.171  61.901  1.00 34.91           O  
HETATM 1952  O   HOH A 217      52.269 -15.798  43.808  1.00 47.35           O  
HETATM 1953  O   HOH A 218      43.625  -6.453  58.077  1.00 33.99           O  
HETATM 1954  O   HOH A 219      39.562   6.667  34.604  1.00 36.56           O  
HETATM 1955  O   HOH A 220      31.588   8.318  32.796  1.00 29.87           O  
HETATM 1956  O   HOH A 221      59.881  -2.133  49.724  1.00 44.49           O  
HETATM 1957  O   HOH A 222      48.548   3.581  62.250  1.00 31.83           O  
HETATM 1958  O   HOH A 223      30.404   3.932  33.938  1.00 33.24           O  
HETATM 1959  O   HOH A 224      57.365 -12.962  39.857  1.00 54.92           O  
HETATM 1960  O   HOH A 225      45.296 -16.855  52.017  1.00 43.22           O  
HETATM 1961  O   HOH A 226      67.695  -7.598  42.961  1.00 56.99           O  
HETATM 1962  O   HOH A 227      46.840   2.252  62.368  1.00 33.37           O  
HETATM 1963  O   HOH A 228      39.754  -4.229  52.676  1.00 34.32           O  
HETATM 1964  O   HOH A 229      32.351  -0.813  43.139  1.00 38.45           O  
HETATM 1965  O   HOH A 230      39.434   1.572  48.657  1.00 28.68           O  
HETATM 1966  O   HOH A 231      40.249   3.055  50.795  1.00 27.40           O  
HETATM 1967  O   HOH A 232      45.454 -13.936  55.427  1.00 34.18           O  
HETATM 1968  O   HOH A 233      46.435  18.631  49.086  1.00 33.93           O  
HETATM 1969  O   HOH A 234      40.791   5.005  34.255  1.00 35.00           O  
HETATM 1970  O   HOH A 235      39.721  -6.243  39.770  1.00 37.70           O  
HETATM 1971  O   HOH A 236      52.507  15.448  57.182  1.00 40.65           O  
HETATM 1972  O   HOH A 237      48.394  14.784  42.331  1.00 30.49           O  
HETATM 1973  O   HOH A 238      43.154 -11.373  44.122  1.00 36.60           O  
HETATM 1974  O   HOH A 239      44.697  13.131  57.949  1.00 35.12           O  
HETATM 1975  O   HOH A 240      35.730  -6.490  49.675  1.00 44.89           O  
HETATM 1976  O   HOH A 241      37.181  -6.011  41.191  1.00 37.86           O  
HETATM 1977  O   HOH A 242      50.570  -2.118  35.410  1.00 40.33           O  
HETATM 1978  O   HOH A 243      49.370  -4.204  35.297  1.00 45.61           O  
HETATM 1979  O   HOH A 244      34.754 -10.669  47.762  1.00 50.25           O  
HETATM 1980  O   HOH A 245      39.664  -5.364  56.133  1.00 41.90           O  
HETATM 1981  O   HOH A 246      34.739  -4.100  40.416  1.00 44.23           O  
HETATM 1982  O   HOH A 247      45.351  -0.872  33.213  1.00 41.04           O  
HETATM 1983  O   HOH A 248      47.711   0.914  32.552  1.00 37.93           O  
HETATM 1984  O   HOH A 249      62.419   5.751  49.422  1.00 50.38           O  
HETATM 1985  O   HOH A 250      36.647   5.130  42.273  1.00 25.64           O  
HETATM 1986  O   HOH A 251      56.546  12.588  53.734  1.00 43.57           O  
HETATM 1987  O   HOH A 252      59.122   5.907  45.239  1.00 47.88           O  
HETATM 1988  O   HOH A 253      59.539   7.680  45.499  1.00 55.46           O  
HETATM 1989  O   HOH A 254      35.885 -10.563  50.420  1.00 46.07           O  
HETATM 1990  O   HOH A 255      58.301  10.384  38.980  1.00 55.68           O  
HETATM 1991  O   HOH A 256      60.852  11.366  39.605  1.00 64.86           O  
HETATM 1992  O   HOH A 257      39.657  -6.428  36.399  1.00 55.17           O  
HETATM 1993  O   HOH B 201      19.281   1.621  36.221  1.00 55.66           O  
HETATM 1994  O   HOH B 202      21.655   6.682  36.830  1.00 40.62           O  
HETATM 1995  O   HOH B 203      28.762  12.164  33.102  1.00 33.51           O  
HETATM 1996  O   HOH B 204      36.496  16.441  32.838  1.00 32.90           O  
HETATM 1997  O   HOH B 205      26.299  13.959  32.813  1.00 34.44           O  
HETATM 1998  O   HOH B 206      40.206  15.729  33.977  1.00 39.99           O  
HETATM 1999  O   HOH B 207      27.578   5.075  33.050  1.00 35.66           O  
HETATM 2000  O   HOH B 208      38.983   7.143  60.382  1.00 32.39           O  
HETATM 2001  O   HOH B 209      24.469  13.268  35.051  1.00 32.83           O  
HETATM 2002  O   HOH B 210      30.936  16.872  36.592  1.00 32.01           O  
HETATM 2003  O   HOH B 211      40.907  24.128  44.147  1.00 40.99           O  
HETATM 2004  O   HOH B 212      45.830  19.175  46.396  1.00 37.29           O  
HETATM 2005  O   HOH B 213      37.724   3.584  61.805  1.00 38.78           O  
HETATM 2006  O   HOH B 214      25.129   4.123  37.182  1.00 37.35           O  
HETATM 2007  O   HOH B 215      44.244   1.175  62.175  1.00 27.14           O  
HETATM 2008  O   HOH B 216      43.570  20.159  29.735  1.00 40.43           O  
HETATM 2009  O   HOH B 217      41.521  27.562  30.372  1.00 39.76           O  
HETATM 2010  O   HOH B 218      23.384  24.251  39.626  1.00 55.47           O  
HETATM 2011  O   HOH B 219      40.581  22.563  38.218  1.00 41.09           O  
HETATM 2012  O   HOH B 220      37.626   0.949  62.321  1.00 28.66           O  
HETATM 2013  O   HOH B 221      41.044  -1.954  61.283  1.00 29.85           O  
HETATM 2014  O   HOH B 222      31.495  10.960  32.583  1.00 34.75           O  
HETATM 2015  O   HOH B 223      35.125   6.139  44.323  1.00 21.82           O  
HETATM 2016  O   HOH B 224      36.733   1.318  49.500  1.00 27.06           O  
HETATM 2017  O   HOH B 225      35.324   2.220  45.647  1.00 26.73           O  
HETATM 2018  O   HOH B 226      35.408  -2.495  52.240  1.00 37.10           O  
HETATM 2019  O   HOH B 227      28.998   1.976  42.432  1.00 33.70           O  
HETATM 2020  O   HOH B 228      34.215   4.824  46.429  1.00 28.20           O  
HETATM 2021  O   HOH B 229      40.838  18.707  52.652  1.00 31.44           O  
HETATM 2022  O   HOH B 230      36.566   8.171  60.935  1.00 35.01           O  
HETATM 2023  O   HOH B 231      28.802  -2.546  45.473  1.00 44.64           O  
HETATM 2024  O   HOH B 232      38.666   4.005  52.955  1.00 28.62           O  
HETATM 2025  O   HOH B 233      30.234   2.748  39.921  1.00 39.72           O  
HETATM 2026  O   HOH B 234      31.742  -2.246  54.516  1.00 44.84           O  
HETATM 2027  O   HOH B 235      27.358   1.075  55.288  1.00 38.72           O  
HETATM 2028  O   HOH B 236      35.991   2.261  43.656  1.00 34.66           O  
HETATM 2029  O   HOH B 237      28.599  -1.173  54.220  1.00 39.38           O  
HETATM 2030  O   HOH B 238      36.563   2.280  51.546  1.00 37.42           O  
HETATM 2031  O   HOH B 239      21.190   1.689  51.175  1.00 44.53           O  
HETATM 2032  O   HOH B 240      24.349   9.522  59.922  1.00 49.67           O  
HETATM 2033  O   HOH B 241      26.961   2.371  37.031  1.00 41.57           O  
HETATM 2034  O   HOH B 242      34.763   7.265  62.932  1.00 48.97           O  
HETATM 2035  O   HOH B 243      42.562  15.948  57.318  1.00 37.35           O  
HETATM 2036  O   HOH B 244      17.693   1.932  39.536  1.00 47.45           O  
HETATM 2037  O   HOH B 245      24.877   7.398  60.730  1.00 60.56           O  
HETATM 2038  O   HOH B 246      35.673  32.794  39.475  1.00 60.59           O  
HETATM 2039  O   HOH B 247      13.521  20.475  52.271  1.00 64.22           O  
HETATM 2040  O   HOH B 248      41.781  14.721  36.950  1.00 51.02           O  
HETATM 2041  O   HOH B 249      22.801  -2.581  39.389  1.00 61.54           O  
HETATM 2042  O   HOH B 250      32.338  -1.536  40.170  1.00 58.55           O  
CONECT  226  686                                                                
CONECT  455  924                                                                
CONECT  465  469                                                                
CONECT  469  465  470                                                           
CONECT  470  469  471  473                                                      
CONECT  471  470  472  477                                                      
CONECT  472  471                                                                
CONECT  473  470  474                                                           
CONECT  474  473  475                                                           
CONECT  475  474  476                                                           
CONECT  476  475                                                                
CONECT  477  471                                                                
CONECT  686  226                                                                
CONECT  924  455                                                                
CONECT 1223 1655                                                                
CONECT 1452 1881                                                                
CONECT 1462 1466                                                                
CONECT 1466 1462 1467                                                           
CONECT 1467 1466 1468 1470                                                      
CONECT 1468 1467 1469 1474                                                      
CONECT 1469 1468                                                                
CONECT 1470 1467 1471                                                           
CONECT 1471 1470 1472                                                           
CONECT 1472 1471 1473                                                           
CONECT 1473 1472                                                                
CONECT 1474 1468                                                                
CONECT 1655 1223                                                                
CONECT 1881 1452                                                                
MASTER      385    0    2    2   16    0    0    6 2040    2   28   26          
END                                                                             
