HEADER    VIRAL PROTEIN                           30-JAN-09   3G21              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE ROUS SARCOMA VIRUS  
TITLE    2 CAPSID PROTEIN: LOW PH                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAG POLYPROTEIN;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 389-465;                   
COMPND   5 SYNONYM: CAPSID PROTEIN;                                             
COMPND   6 EC: 3.4.23.-;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ROUS SARCOMA VIRUS;                             
SOURCE   3 ORGANISM_COMMON: RSV-PRC;                                            
SOURCE   4 ORGANISM_TAXID: 11888;                                               
SOURCE   5 STRAIN: PRAGUE C STRAIN;                                             
SOURCE   6 GENE: GAG;                                                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3);                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PTYB11                                    
KEYWDS    ALPHA-HELICAL BUNDLE, CAPSID PROTEIN, VIRION, VIRAL PROTEIN,          
KEYWDS   2 RETROVIRUS                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.L.KINGSTON                                                          
REVDAT   2   01-NOV-23 3G21    1       REMARK                                   
REVDAT   1   02-JUN-09 3G21    0                                                
JRNL        AUTH   G.D.BAILEY,J.K.HYUN,A.K.MITRA,R.L.KINGSTON                   
JRNL        TITL   PROTON-LINKED DIMERIZATION OF A RETROVIRAL CAPSID PROTEIN    
JRNL        TITL 2 INITIATES CAPSID ASSEMBLY                                    
JRNL        REF    STRUCTURE                     V.  17   737 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19446529                                                     
JRNL        DOI    10.1016/J.STR.2009.03.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.6                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.124                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.124                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.142                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2306                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 43916                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.122                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 42426                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 596                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 4                                             
REMARK   3   SOLVENT ATOMS      : 83                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 669.09                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 583.31                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 42                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 7348                    
REMARK   3   NUMBER OF RESTRAINTS                     : 10719                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.018                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.035                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.025                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.114                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.112                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.164                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.007                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.031                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.078                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS AND KRETSINGER (BABINET SCALING)                
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF)                                                         
REMARK   4                                                                      
REMARK   4 3G21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051323.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.85503                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46299                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : 11.10                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 30.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3G1G                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M SUCCINIC ACID/KOH, PH4.3, 13-18%   
REMARK 280  PEG8000, 0.75M MAGNESIUM NITRATE, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.91667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.95833            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.95833            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       75.91667            
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: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8360 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       37.95833            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  173   CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 166   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 166   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 170   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 170   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 185   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 200   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G0V   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G1G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G1I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G26   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G28   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G29   RELATED DB: PDB                                   
DBREF  3G21 A  150   226  UNP    P03322   GAG_RSVP       389    465             
SEQRES   1 A   77  ALA GLY PRO TRP ALA ASP ILE MET GLN GLY PRO SER GLU          
SEQRES   2 A   77  SER PHE VAL ASP PHE ALA ASN ARG LEU ILE LYS ALA VAL          
SEQRES   3 A   77  GLU GLY SER ASP LEU PRO PRO SER ALA ARG ALA PRO VAL          
SEQRES   4 A   77  ILE ILE ASP CYS PHE ARG GLN LYS SER GLN PRO ASP ILE          
SEQRES   5 A   77  GLN GLN LEU ILE ARG THR ALA PRO SER THR LEU THR THR          
SEQRES   6 A   77  PRO GLY GLU ILE ILE LYS TYR VAL LEU ASP ARG GLN              
HET    NO3  A   1       4                                                       
HETNAM     NO3 NITRATE ION                                                      
FORMUL   2  NO3    N O3 1-                                                      
FORMUL   3  HOH   *83(H2 O)                                                     
HELIX    1   1 PRO A  152  ILE A  156  5                                   5    
HELIX    2   2 SER A  163  GLY A  177  1                                  15    
HELIX    3   3 PRO A  181  SER A  183  5                                   3    
HELIX    4   4 ALA A  184  SER A  197  1                                  14    
HELIX    5   5 GLN A  198  ARG A  206  1                                   9    
HELIX    6   6 THR A  214  ASP A  224  1                                  11    
SITE     1 AC1  8 HOH A 104  ASP A 200  ILE A 201  LEU A 204                    
SITE     2 AC1  8 GLY A 216  GLU A 217  LYS A 220  GLN A 226                    
CRYST1   32.179   32.179  113.875  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.031076  0.017942  0.000000        0.00000                         
SCALE2      0.000000  0.035884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008782        0.00000                         
ATOM      1  N   ALA A 150      11.227  14.398  14.549  0.50 21.38           N  
ATOM      2  CA  ALA A 150      10.891  13.231  13.778  0.50 16.28           C  
ATOM      3  C   ALA A 150       9.781  12.458  14.478  0.50 14.47           C  
ATOM      4  O   ALA A 150       9.515  12.790  15.659  0.50 18.40           O  
ATOM      5  CB  ALA A 150      12.143  12.395  13.564  0.50 19.80           C  
ATOM      6  N   GLY A 151       9.138  11.509  13.795  0.50 14.03           N  
ATOM      7  CA  GLY A 151       8.024  10.799  14.354  0.50 14.88           C  
ATOM      8  C   GLY A 151       8.399   9.784  15.414  0.50 13.54           C  
ATOM      9  O   GLY A 151       9.571   9.393  15.512  0.50 12.01           O  
ATOM     10  N   PRO A 152       7.440   9.353  16.241  1.00 15.73           N  
ATOM     11  CA  PRO A 152       7.812   8.371  17.224  1.00 12.26           C  
ATOM     12  C   PRO A 152       7.953   7.017  16.583  1.00 10.13           C  
ATOM     13  O   PRO A 152       6.975   6.312  16.346  1.00 11.41           O  
ATOM     14  CB  PRO A 152       6.764   8.386  18.304  1.00 13.98           C  
ATOM     15  CG  PRO A 152       5.572   9.006  17.664  1.00 19.67           C  
ATOM     16  CD  PRO A 152       6.111   9.786  16.508  1.00 19.88           C  
ATOM     17  N   TRP A 153       9.229   6.634  16.306  1.00  8.89           N  
ATOM     18  CA  TRP A 153       9.487   5.417  15.565  1.00  8.48           C  
ATOM     19  C   TRP A 153       8.891   4.178  16.175  1.00  7.80           C  
ATOM     20  O   TRP A 153       8.499   3.276  15.472  1.00  9.10           O  
ATOM     21  CB  TRP A 153      10.992   5.241  15.273  1.00  8.76           C  
ATOM     22  CG  TRP A 153      11.801   5.026  16.476  1.00  8.23           C  
ATOM     23  CD1 TRP A 153      12.528   5.996  17.172  1.00  8.28           C  
ATOM     24  CD2 TRP A 153      12.033   3.799  17.178  1.00  7.47           C  
ATOM     25  NE1 TRP A 153      13.171   5.440  18.240  1.00  8.20           N  
ATOM     26  CE2 TRP A 153      12.870   4.083  18.263  1.00  7.63           C  
ATOM     27  CE3 TRP A 153      11.590   2.493  17.002  1.00  7.84           C  
ATOM     28  CZ2 TRP A 153      13.289   3.135  19.155  1.00  8.11           C  
ATOM     29  CZ3 TRP A 153      11.983   1.515  17.889  1.00  8.34           C  
ATOM     30  CH2 TRP A 153      12.826   1.859  18.955  1.00  8.38           C  
ATOM     31  N   ALA A 154       8.848   4.122  17.536  1.00  7.73           N  
ATOM     32  CA  ALA A 154       8.383   2.935  18.201  1.00  8.19           C  
ATOM     33  C   ALA A 154       6.856   2.806  18.145  1.00  8.30           C  
ATOM     34  O   ALA A 154       6.344   1.715  18.531  1.00  9.03           O  
ATOM     35  CB  ALA A 154       8.918   2.880  19.622  1.00  8.56           C  
ATOM     36  N   ASP A 155       6.174   3.821  17.669  1.00  9.04           N  
ATOM     37  CA  ASP A 155       4.718   3.802  17.482  1.00 10.56           C  
ATOM     38  C   ASP A 155       4.289   3.476  16.078  1.00 10.27           C  
ATOM     39  O   ASP A 155       3.124   3.313  15.799  1.00 16.48           O  
ATOM     40  CB  ASP A 155       4.139   5.228  17.665  1.00 15.06           C  
ATOM     41  CG  ASP A 155       4.060   5.782  18.997  0.50 13.29           C  
ATOM     42  OD1 ASP A 155       4.138   4.943  19.889  0.50 15.38           O  
ATOM     43  OD2 ASP A 155       3.822   7.008  19.080  0.50 15.35           O  
ATOM     44  N   ILE A 156       5.209   3.332  15.144  1.00  8.82           N  
ATOM     45  CA  ILE A 156       4.895   3.179  13.753  1.00  9.19           C  
ATOM     46  C   ILE A 156       4.569   1.724  13.388  1.00  9.03           C  
ATOM     47  O   ILE A 156       5.326   0.796  13.704  1.00  9.10           O  
ATOM     48  CB  ILE A 156       6.032   3.691  12.882  1.00  9.48           C  
ATOM     49  CG1 ILE A 156       6.087   5.202  13.039  1.00 10.33           C  
ATOM     50  CG2 ILE A 156       5.911   3.303  11.367  1.00 11.08           C  
ATOM     51  CD1 ILE A 156       7.262   5.791  12.353  1.00 11.51           C  
ATOM     52  N   MET A 157       3.398   1.544  12.838  1.00 10.50           N  
ATOM     53  CA  MET A 157       2.899   0.221  12.441  1.00 10.38           C  
ATOM     54  C   MET A 157       2.319   0.343  11.049  1.00 10.05           C  
ATOM     55  O   MET A 157       1.764   1.351  10.674  1.00 12.70           O  
ATOM     56  CB  MET A 157       1.997  -0.419  13.437  1.00 15.73           C  
ATOM     57  CG  MET A 157       0.603   0.037  13.433  1.00 24.53           C  
ATOM     58  SD  MET A 157      -0.208  -0.710  14.875  1.00 48.85           S  
ATOM     59  CE  MET A 157       0.317  -2.420  14.873  1.00 72.85           C  
ATOM     60  N  AGLN A 158       2.368  -0.777  10.374  0.62  9.17           N  
ATOM     61  N  BGLN A 158       2.492  -0.701  10.198  0.38  9.54           N  
ATOM     62  CA AGLN A 158       1.690  -0.690   9.079  0.62  7.51           C  
ATOM     63  CA BGLN A 158       2.127  -0.847   8.783  0.38  8.36           C  
ATOM     64  C  AGLN A 158       0.176  -0.767   9.258  0.62  7.36           C  
ATOM     65  C  BGLN A 158       0.620  -0.838   8.669  0.38  7.82           C  
ATOM     66  O  AGLN A 158      -0.305  -1.768   9.724  0.62  9.16           O  
ATOM     67  O  BGLN A 158       0.009  -1.645   9.377  0.38  9.31           O  
ATOM     68  CB AGLN A 158       2.218  -1.848   8.255  0.62  7.34           C  
ATOM     69  CB BGLN A 158       2.624  -2.124   8.075  0.38  7.81           C  
ATOM     70  CG AGLN A 158       1.697  -1.813   6.833  0.62  7.72           C  
ATOM     71  CG BGLN A 158       2.232  -2.229   6.601  0.38  9.07           C  
ATOM     72  CD AGLN A 158       2.033  -3.045   6.077  0.62  7.25           C  
ATOM     73  CD BGLN A 158       2.605  -3.507   5.895  0.38  8.52           C  
ATOM     74  OE1AGLN A 158       2.753  -3.962   6.519  0.62  8.15           O  
ATOM     75  OE1BGLN A 158       3.205  -4.348   6.573  0.38  8.72           O  
ATOM     76  NE2AGLN A 158       1.453  -3.151   4.878  0.62  7.83           N  
ATOM     77  NE2BGLN A 158       2.331  -3.628   4.613  0.38 11.32           N  
ATOM     78  N  AGLY A 159      -0.467   0.321   8.809  0.62  7.87           N  
ATOM     79  N  BGLY A 159       0.064   0.080   7.841  0.38  9.23           N  
ATOM     80  CA AGLY A 159      -1.908   0.333   8.887  0.62  9.77           C  
ATOM     81  CA BGLY A 159      -1.379   0.078   7.802  0.38 10.50           C  
ATOM     82  C  AGLY A 159      -2.566  -0.427   7.760  0.62  8.68           C  
ATOM     83  C  BGLY A 159      -2.030  -1.058   7.046  0.38 11.42           C  
ATOM     84  O  AGLY A 159      -1.893  -0.811   6.782  0.62  8.47           O  
ATOM     85  O  BGLY A 159      -1.351  -1.836   6.377  0.38 10.37           O  
ATOM     86  N  APRO A 160      -3.880  -0.686   7.874  0.62 11.79           N  
ATOM     87  N  BPRO A 160      -3.358  -1.155   7.153  0.38 13.28           N  
ATOM     88  CA APRO A 160      -4.505  -1.558   6.855  0.62 14.17           C  
ATOM     89  CA BPRO A 160      -4.020  -2.318   6.584  0.38 13.79           C  
ATOM     90  C  APRO A 160      -4.665  -0.915   5.512  0.62 14.17           C  
ATOM     91  C  BPRO A 160      -3.903  -2.409   5.070  0.38 13.45           C  
ATOM     92  O  APRO A 160      -4.896  -1.607   4.523  0.62 19.59           O  
ATOM     93  O  BPRO A 160      -3.831  -3.529   4.581  0.38 21.18           O  
ATOM     94  CB APRO A 160      -5.840  -1.947   7.561  0.62 17.84           C  
ATOM     95  CB BPRO A 160      -5.483  -2.183   7.028  0.38 15.27           C  
ATOM     96  CG APRO A 160      -6.117  -0.747   8.396  0.62 17.52           C  
ATOM     97  CG BPRO A 160      -5.637  -0.746   7.395  0.38 15.65           C  
ATOM     98  CD APRO A 160      -4.773  -0.290   8.947  0.62 14.03           C  
ATOM     99  CD BPRO A 160      -4.285  -0.248   7.857  0.38 12.78           C  
ATOM    100  N  ASER A 161      -4.482   0.406   5.378  0.62 11.95           N  
ATOM    101  N  BSER A 161      -3.860  -1.296   4.367  0.38 12.48           N  
ATOM    102  CA ASER A 161      -4.469   1.014   4.031  0.62 12.08           C  
ATOM    103  CA BSER A 161      -3.749  -1.247   2.919  0.38 12.84           C  
ATOM    104  C  ASER A 161      -3.071   1.464   3.598  0.62 10.83           C  
ATOM    105  C  BSER A 161      -2.397  -0.701   2.472  0.38 11.67           C  
ATOM    106  O  ASER A 161      -2.892   2.150   2.596  0.62 12.67           O  
ATOM    107  O  BSER A 161      -2.212  -0.587   1.256  0.38 12.65           O  
ATOM    108  CB ASER A 161      -5.530   2.070   4.059  0.62 13.33           C  
ATOM    109  CB BSER A 161      -4.833  -0.376   2.233  0.38 14.65           C  
ATOM    110  OG ASER A 161      -4.962   3.128   4.754  0.62 15.02           O  
ATOM    111  OG BSER A 161      -4.738   0.965   2.721  0.38 18.04           O  
ATOM    112  N  AGLU A 162      -2.057   0.997   4.302  0.62  8.48           N  
ATOM    113  N  BGLU A 162      -1.511  -0.415   3.412  0.38  9.81           N  
ATOM    114  CA AGLU A 162      -0.675   1.265   3.954  0.62  7.91           C  
ATOM    115  CA BGLU A 162      -0.253   0.264   3.143  0.38  8.47           C  
ATOM    116  C  AGLU A 162       0.029   0.077   3.357  0.62  7.49           C  
ATOM    117  C  BGLU A 162       0.740  -0.773   2.614  0.38  8.40           C  
ATOM    118  O  AGLU A 162      -0.159  -1.043   3.807  0.62  7.82           O  
ATOM    119  O  BGLU A 162       0.772  -1.876   3.107  0.38  9.69           O  
ATOM    120  CB AGLU A 162       0.037   1.631   5.262  0.62 10.16           C  
ATOM    121  CB BGLU A 162       0.340   0.975   4.337  0.38  9.16           C  
ATOM    122  CG AGLU A 162       1.269   2.406   5.109  0.62 11.65           C  
ATOM    123  CG BGLU A 162       1.638   1.740   4.046  0.38  9.48           C  
ATOM    124  CD AGLU A 162       1.881   2.875   6.419  0.62 10.53           C  
ATOM    125  CD BGLU A 162       2.139   2.391   5.355  0.38 11.15           C  
ATOM    126  OE1AGLU A 162       1.567   2.335   7.481  0.62 10.39           O  
ATOM    127  OE1BGLU A 162       1.834   1.841   6.430  0.38 11.86           O  
ATOM    128  OE2AGLU A 162       2.737   3.764   6.315  0.62 11.93           O  
ATOM    129  OE2BGLU A 162       2.789   3.445   5.165  0.38 13.68           O  
ATOM    130  N  ASER A 163       0.834   0.317   2.307  0.62  7.25           N  
ATOM    131  N  BSER A 163       1.534  -0.402   1.623  0.38  8.57           N  
ATOM    132  CA ASER A 163       1.670  -0.743   1.805  0.62  8.42           C  
ATOM    133  CA BSER A 163       2.554  -1.302   1.118  0.38  8.75           C  
ATOM    134  C  ASER A 163       2.842  -0.955   2.747  0.62  6.81           C  
ATOM    135  C  BSER A 163       3.675  -1.396   2.168  0.38  7.49           C  
ATOM    136  O  ASER A 163       3.202  -0.140   3.591  0.62  6.86           O  
ATOM    137  O  BSER A 163       3.900  -0.456   2.963  0.38  8.10           O  
ATOM    138  CB ASER A 163       2.201  -0.285   0.434  0.62  9.73           C  
ATOM    139  CB BSER A 163       3.202  -0.877  -0.174  0.38  9.23           C  
ATOM    140  OG ASER A 163       3.041   0.815   0.557  0.62 12.69           O  
ATOM    141  OG BSER A 163       3.280   0.512  -0.133  0.38 20.72           O  
ATOM    142  N  APHE A 164       3.521  -2.057   2.529  0.62  6.65           N  
ATOM    143  N  BPHE A 164       4.369  -2.513   2.110  0.38  7.94           N  
ATOM    144  CA APHE A 164       4.737  -2.311   3.294  0.62  6.46           C  
ATOM    145  CA BPHE A 164       5.504  -2.673   2.991  0.38  7.55           C  
ATOM    146  C  APHE A 164       5.752  -1.243   3.042  0.62  5.92           C  
ATOM    147  C  BPHE A 164       6.569  -1.622   2.728  0.38  7.40           C  
ATOM    148  O  APHE A 164       6.401  -0.756   3.995  0.62  6.34           O  
ATOM    149  O  BPHE A 164       7.205  -1.045   3.614  0.38  8.14           O  
ATOM    150  CB APHE A 164       5.316  -3.692   2.941  0.62  7.13           C  
ATOM    151  CB BPHE A 164       6.066  -4.105   2.870  0.38  6.90           C  
ATOM    152  CG APHE A 164       6.625  -3.877   3.673  0.62  5.95           C  
ATOM    153  CG BPHE A 164       7.270  -4.284   3.763  0.38  6.31           C  
ATOM    154  CD1APHE A 164       6.675  -4.007   5.045  0.62  6.31           C  
ATOM    155  CD1BPHE A 164       7.132  -4.397   5.138  0.38  5.47           C  
ATOM    156  CD2APHE A 164       7.842  -3.933   3.032  0.62  7.78           C  
ATOM    157  CD2BPHE A 164       8.529  -4.326   3.144  0.38  6.95           C  
ATOM    158  CE1APHE A 164       7.846  -4.167   5.732  0.62  7.10           C  
ATOM    159  CE1BPHE A 164       8.265  -4.570   5.919  0.38  5.46           C  
ATOM    160  CE2APHE A 164       9.042  -4.064   3.712  0.62  7.95           C  
ATOM    161  CE2BPHE A 164       9.641  -4.498   3.972  0.38  6.85           C  
ATOM    162  CZ APHE A 164       9.048  -4.201   5.083  0.62  7.60           C  
ATOM    163  CZ BPHE A 164       9.510  -4.615   5.328  0.38  6.27           C  
ATOM    164  N  AVAL A 165       5.958  -0.866   1.807  0.62  6.22           N  
ATOM    165  N  BVAL A 165       6.842  -1.334   1.451  0.38  7.56           N  
ATOM    166  CA AVAL A 165       7.023   0.104   1.541  0.62  7.16           C  
ATOM    167  CA BVAL A 165       7.893  -0.362   1.158  0.38  8.25           C  
ATOM    168  C  AVAL A 165       6.660   1.464   2.145  0.62  6.84           C  
ATOM    169  C  BVAL A 165       7.557   1.016   1.697  0.38  7.27           C  
ATOM    170  O  AVAL A 165       7.533   2.185   2.624  0.62  7.57           O  
ATOM    171  O  BVAL A 165       8.372   1.796   2.256  0.38  8.56           O  
ATOM    172  CB AVAL A 165       7.432   0.146   0.058  0.62  7.68           C  
ATOM    173  CB BVAL A 165       8.204  -0.419  -0.330  0.38  8.06           C  
ATOM    174  CG1AVAL A 165       6.424   0.980  -0.742  0.62 10.05           C  
ATOM    175  CG1BVAL A 165       7.060   0.093  -1.170  0.38 11.00           C  
ATOM    176  CG2AVAL A 165       8.856   0.678  -0.051  0.62 10.01           C  
ATOM    177  CG2BVAL A 165       9.488   0.353  -0.654  0.38 10.45           C  
ATOM    178  N  AASP A 166       5.369   1.861   2.132  0.62  6.86           N  
ATOM    179  N  BASP A 166       6.318   1.440   1.610  0.38  8.30           N  
ATOM    180  CA AASP A 166       5.088   3.112   2.764  0.62  8.42           C  
ATOM    181  CA BASP A 166       5.888   2.716   2.129  0.38  8.79           C  
ATOM    182  C  AASP A 166       5.419   3.069   4.277  0.62  6.59           C  
ATOM    183  C  BASP A 166       5.956   2.742   3.671  0.38  7.44           C  
ATOM    184  O  AASP A 166       5.965   4.053   4.849  0.62  7.88           O  
ATOM    185  O  BASP A 166       6.358   3.742   4.275  0.38  9.18           O  
ATOM    186  CB AASP A 166       3.665   3.565   2.619  0.31  8.78           C  
ATOM    187  CB BASP A 166       4.490   3.128   1.619  0.19  8.75           C  
ATOM    188  CG AASP A 166       3.659   5.032   3.124  0.31  7.47           C  
ATOM    189  CG BASP A 166       4.042   4.419   2.293  0.19 10.18           C  
ATOM    190  OD1AASP A 166       4.190   5.968   2.497  0.37 13.10           O  
ATOM    191  OD1BASP A 166       4.640   5.430   1.850  0.19 14.73           O  
ATOM    192  OD2AASP A 166       3.068   5.181   4.205  0.31  7.77           O  
ATOM    193  OD2BASP A 166       3.171   4.502   3.176  0.19 13.15           O  
ATOM    194  N  APHE A 167       5.061   1.985   4.933  0.62  6.13           N  
ATOM    195  N  BPHE A 167       5.512   1.696   4.332  0.38  7.49           N  
ATOM    196  CA APHE A 167       5.503   1.760   6.339  0.62  6.62           C  
ATOM    197  CA BPHE A 167       5.585   1.584   5.795  0.38  7.99           C  
ATOM    198  C  APHE A 167       7.034   1.728   6.475  0.62  7.31           C  
ATOM    199  C  BPHE A 167       7.004   1.824   6.295  0.38  8.01           C  
ATOM    200  O  APHE A 167       7.602   2.345   7.389  0.62  5.88           O  
ATOM    201  O  BPHE A 167       7.312   2.586   7.194  0.38  7.20           O  
ATOM    202  CB APHE A 167       4.810   0.466   6.822  0.62  6.40           C  
ATOM    203  CB BPHE A 167       5.093   0.211   6.251  0.38  7.41           C  
ATOM    204  CG APHE A 167       5.514  -0.202   7.985  0.62  5.91           C  
ATOM    205  CG BPHE A 167       5.741  -0.339   7.506  0.38  5.81           C  
ATOM    206  CD1APHE A 167       5.414   0.270   9.274  0.62  6.86           C  
ATOM    207  CD1BPHE A 167       5.535   0.145   8.764  0.38  6.58           C  
ATOM    208  CD2APHE A 167       6.266  -1.339   7.756  0.62  6.78           C  
ATOM    209  CD2BPHE A 167       6.601  -1.429   7.377  0.38  6.25           C  
ATOM    210  CE1APHE A 167       6.092  -0.402  10.294  0.62  7.28           C  
ATOM    211  CE1BPHE A 167       6.163  -0.397   9.873  0.38  8.17           C  
ATOM    212  CE2APHE A 167       6.979  -2.007   8.750  0.62  7.59           C  
ATOM    213  CE2BPHE A 167       7.245  -1.985   8.471  0.38  7.61           C  
ATOM    214  CZ APHE A 167       6.858  -1.500  10.037  0.62  7.43           C  
ATOM    215  CZ BPHE A 167       7.011  -1.466   9.740  0.38  7.79           C  
ATOM    216  N   ALA A 168       7.775   1.039   5.592  1.00  7.72           N  
ATOM    217  CA  ALA A 168       9.244   0.991   5.739  1.00  7.46           C  
ATOM    218  C   ALA A 168       9.806   2.391   5.637  1.00  7.18           C  
ATOM    219  O   ALA A 168      10.686   2.783   6.402  1.00  7.46           O  
ATOM    220  CB  ALA A 168       9.881   0.063   4.741  1.00  8.88           C  
ATOM    221  N   ASN A 169       9.323   3.174   4.663  1.00  7.31           N  
ATOM    222  CA  ASN A 169       9.849   4.521   4.474  1.00  7.37           C  
ATOM    223  C   ASN A 169       9.568   5.384   5.668  1.00  7.16           C  
ATOM    224  O   ASN A 169      10.434   6.129   6.115  1.00  7.65           O  
ATOM    225  CB  ASN A 169       9.254   5.111   3.199  1.00  7.95           C  
ATOM    226  CG  ASN A 169       9.677   4.397   1.949  1.00  8.16           C  
ATOM    227  OD1 ASN A 169      10.700   3.737   1.944  1.00  9.90           O  
ATOM    228  ND2 ASN A 169       8.925   4.564   0.894  1.00  9.60           N  
ATOM    229  N   ARG A 170       8.360   5.295   6.207  1.00  7.39           N  
ATOM    230  CA AARG A 170       7.919   6.053   7.379  0.62  7.89           C  
ATOM    231  CA BARG A 170       8.098   6.210   7.332  0.38  7.94           C  
ATOM    232  C   ARG A 170       8.803   5.698   8.593  1.00  7.26           C  
ATOM    233  O   ARG A 170       9.285   6.534   9.352  1.00  8.03           O  
ATOM    234  CB AARG A 170       6.411   5.826   7.630  0.62  8.31           C  
ATOM    235  CB BARG A 170       6.648   6.421   7.692  0.38 10.73           C  
ATOM    236  CG AARG A 170       5.682   6.793   8.556  0.62 10.02           C  
ATOM    237  CG BARG A 170       5.604   6.381   6.656  0.38 10.10           C  
ATOM    238  CD AARG A 170       4.182   6.804   8.265  0.62 12.29           C  
ATOM    239  CD BARG A 170       4.152   6.314   6.964  0.38 10.90           C  
ATOM    240  NE AARG A 170       3.499   5.531   8.512  0.62 11.25           N  
ATOM    241  NE BARG A 170       3.635   5.007   7.321  0.38 10.61           N  
ATOM    242  CZ AARG A 170       3.043   5.186   9.715  0.62  9.91           C  
ATOM    243  CZ BARG A 170       3.275   4.638   8.521  0.38  9.33           C  
ATOM    244  NH1AARG A 170       3.230   5.924  10.786  0.62 10.87           N  
ATOM    245  NH1BARG A 170       3.339   5.370   9.637  0.38 13.53           N  
ATOM    246  NH2AARG A 170       2.408   4.043   9.879  0.62 11.79           N  
ATOM    247  NH2BARG A 170       2.802   3.406   8.636  0.38 12.20           N  
ATOM    248  N   LEU A 171       8.910   4.408   8.797  1.00  7.00           N  
ATOM    249  CA  LEU A 171       9.702   3.864   9.901  1.00  6.81           C  
ATOM    250  C   LEU A 171      11.144   4.319   9.840  1.00  6.54           C  
ATOM    251  O   LEU A 171      11.714   4.794  10.834  1.00  6.76           O  
ATOM    252  CB  LEU A 171       9.625   2.340   9.898  1.00  7.09           C  
ATOM    253  CG  LEU A 171      10.501   1.618  10.928  1.00  7.53           C  
ATOM    254  CD1 LEU A 171      10.001   1.850  12.354  1.00  9.39           C  
ATOM    255  CD2 LEU A 171      10.616   0.166  10.569  1.00  8.38           C  
ATOM    256  N   ILE A 172      11.762   4.141   8.675  1.00  6.34           N  
ATOM    257  CA  ILE A 172      13.171   4.449   8.531  1.00  6.53           C  
ATOM    258  C   ILE A 172      13.388   5.956   8.722  1.00  6.59           C  
ATOM    259  O   ILE A 172      14.363   6.349   9.390  1.00  7.18           O  
ATOM    260  CB  ILE A 172      13.733   3.920   7.203  1.00  6.64           C  
ATOM    261  CG1 ILE A 172      13.735   2.381   7.280  1.00  6.56           C  
ATOM    262  CG2 ILE A 172      15.102   4.483   6.912  1.00  7.77           C  
ATOM    263  CD1 ILE A 172      14.051   1.701   5.934  1.00  8.66           C  
ATOM    264  N   LYS A 173      12.549   6.791   8.147  1.00  7.41           N  
ATOM    265  CA  LYS A 173      12.700   8.245   8.362  1.00  7.85           C  
ATOM    266  C   LYS A 173      12.649   8.557   9.851  1.00  7.67           C  
ATOM    267  O   LYS A 173      13.440   9.365  10.369  1.00  8.89           O  
ATOM    268  CB  LYS A 173      11.662   8.996   7.598  1.00  9.13           C  
ATOM    269  CG  LYS A 173      11.811  10.467   7.562  0.50  8.46           C  
ATOM    270  CD  LYS A 173      10.859  11.177   6.631  0.25  7.89           C  
ATOM    271  CE  LYS A 173      10.870  12.682   6.848  0.00  8.24           C  
ATOM    272  NZ  LYS A 173       9.835  13.369   6.027  0.00  7.96           N  
ATOM    273  N   ALA A 174      11.708   7.959  10.591  1.00  7.50           N  
ATOM    274  CA  ALA A 174      11.590   8.224  12.016  1.00  7.52           C  
ATOM    275  C   ALA A 174      12.811   7.710  12.793  1.00  7.44           C  
ATOM    276  O   ALA A 174      13.288   8.371  13.710  1.00  8.43           O  
ATOM    277  CB  ALA A 174      10.301   7.627  12.546  1.00  8.69           C  
ATOM    278  N   VAL A 175      13.311   6.532  12.453  1.00  6.66           N  
ATOM    279  CA  VAL A 175      14.512   6.012  13.106  1.00  6.76           C  
ATOM    280  C   VAL A 175      15.702   6.914  12.838  1.00  6.93           C  
ATOM    281  O   VAL A 175      16.498   7.238  13.727  1.00  7.59           O  
ATOM    282  CB  VAL A 175      14.769   4.551  12.696  1.00  6.77           C  
ATOM    283  CG1 VAL A 175      16.149   4.098  13.116  1.00  8.00           C  
ATOM    284  CG2 VAL A 175      13.693   3.630  13.257  1.00  6.96           C  
ATOM    285  N   GLU A 176      15.869   7.372  11.590  1.00  7.40           N  
ATOM    286  CA  GLU A 176      16.993   8.236  11.262  1.00  7.97           C  
ATOM    287  C   GLU A 176      16.921   9.569  11.996  1.00  8.77           C  
ATOM    288  O   GLU A 176      17.955  10.166  12.285  1.00 10.59           O  
ATOM    289  CB  GLU A 176      17.037   8.481   9.743  1.00  8.87           C  
ATOM    290  CG  GLU A 176      17.396   7.235   8.966  1.00  8.73           C  
ATOM    291  CD  GLU A 176      18.823   6.754   9.148  1.00  9.17           C  
ATOM    292  OE1 GLU A 176      19.687   7.491   9.571  1.00 10.91           O  
ATOM    293  OE2 GLU A 176      19.018   5.540   8.799  1.00 10.87           O  
ATOM    294  N   GLY A 177      15.714  10.063  12.266  1.00  9.38           N  
ATOM    295  CA  GLY A 177      15.581  11.292  13.016  1.00 11.16           C  
ATOM    296  C   GLY A 177      15.610  11.164  14.510  1.00 10.54           C  
ATOM    297  O   GLY A 177      15.529  12.186  15.195  1.00 13.54           O  
ATOM    298  N   SER A 178      15.745   9.966  15.027  1.00  9.33           N  
ATOM    299  CA  SER A 178      15.766   9.674  16.449  1.00  9.46           C  
ATOM    300  C   SER A 178      17.151   9.948  17.060  1.00  9.67           C  
ATOM    301  O   SER A 178      18.095  10.190  16.351  1.00 10.30           O  
ATOM    302  CB  SER A 178      15.395   8.212  16.692  1.00  9.37           C  
ATOM    303  OG  SER A 178      16.448   7.391  16.426  1.00  9.09           O  
ATOM    304  N   ASP A 179      17.188   9.802  18.369  1.00  9.66           N  
ATOM    305  CA  ASP A 179      18.449   9.878  19.110  1.00 10.52           C  
ATOM    306  C   ASP A 179      19.150   8.538  19.205  1.00 10.30           C  
ATOM    307  O   ASP A 179      20.158   8.446  19.972  1.00 12.26           O  
ATOM    308  CB  ASP A 179      18.264  10.519  20.492  1.00 12.70           C  
ATOM    309  CG  ASP A 179      17.513   9.637  21.423  1.00 14.54           C  
ATOM    310  OD1 ASP A 179      16.979   8.570  21.002  1.00 16.53           O  
ATOM    311  OD2 ASP A 179      17.432   9.977  22.607  1.00 25.36           O  
ATOM    312  N   LEU A 180      18.841   7.455  18.570  1.00  9.87           N  
ATOM    313  CA  LEU A 180      19.471   6.201  18.618  1.00  9.89           C  
ATOM    314  C  ALEU A 180      20.902   6.389  18.081  0.61 10.19           C  
ATOM    315  C  BLEU A 180      20.907   6.363  18.070  0.39 10.20           C  
ATOM    316  O  ALEU A 180      21.114   7.155  17.145  0.61 11.53           O  
ATOM    317  O  BLEU A 180      21.141   7.061  17.085  0.39  9.90           O  
ATOM    318  CB  LEU A 180      18.747   5.181  17.789  1.00  9.58           C  
ATOM    319  CG  LEU A 180      17.365   4.777  18.320  1.00  9.08           C  
ATOM    320  CD1 LEU A 180      16.692   3.863  17.297  1.00 10.91           C  
ATOM    321  CD2 LEU A 180      17.508   4.075  19.667  1.00 14.41           C  
ATOM    322  N  APRO A 181      21.818   5.642  18.607  0.61 10.19           N  
ATOM    323  N  BPRO A 181      21.860   5.693  18.659  0.39 10.47           N  
ATOM    324  CA APRO A 181      23.159   5.611  18.012  0.61 11.36           C  
ATOM    325  CA BPRO A 181      23.224   5.650  18.101  0.39 11.20           C  
ATOM    326  C  APRO A 181      23.090   5.079  16.588  0.61  9.16           C  
ATOM    327  C  BPRO A 181      23.218   5.050  16.698  0.39 10.31           C  
ATOM    328  O  APRO A 181      22.205   4.294  16.240  0.61  8.18           O  
ATOM    329  O  BPRO A 181      22.428   4.117  16.486  0.39  8.49           O  
ATOM    330  CB APRO A 181      23.959   4.626  18.842  0.61 13.00           C  
ATOM    331  CB BPRO A 181      23.973   4.753  19.080  0.39 12.14           C  
ATOM    332  CG APRO A 181      23.013   4.003  19.760  0.61 14.00           C  
ATOM    333  CG BPRO A 181      23.173   4.792  20.342  0.39 12.53           C  
ATOM    334  CD APRO A 181      21.712   4.742  19.778  0.61 12.20           C  
ATOM    335  CD BPRO A 181      21.741   4.907  19.905  0.39 11.15           C  
ATOM    336  N   PRO A 182      24.016   5.564  15.774  1.00 10.08           N  
ATOM    337  CA  PRO A 182      23.944   5.102  14.363  1.00 10.31           C  
ATOM    338  C   PRO A 182      23.962   3.596  14.237  1.00  9.50           C  
ATOM    339  O   PRO A 182      23.229   3.043  13.406  1.00 10.21           O  
ATOM    340  CB  PRO A 182      25.201   5.746  13.747  1.00 11.98           C  
ATOM    341  CG  PRO A 182      25.339   7.027  14.550  1.00 13.98           C  
ATOM    342  CD  PRO A 182      25.006   6.631  15.955  1.00 12.53           C  
ATOM    343  N   SER A 183      24.769   2.881  15.026  1.00 10.25           N  
ATOM    344  CA ASER A 183      24.848   1.433  14.928  0.66 11.03           C  
ATOM    345  CA BSER A 183      24.816   1.433  14.836  0.34 11.21           C  
ATOM    346  C   SER A 183      23.582   0.698  15.347  1.00 10.07           C  
ATOM    347  O   SER A 183      23.413  -0.473  14.979  1.00 12.21           O  
ATOM    348  CB ASER A 183      26.036   0.920  15.760  0.66 14.87           C  
ATOM    349  CB BSER A 183      26.006   0.743  15.507  0.34 13.04           C  
ATOM    350  OG ASER A 183      25.862   1.234  17.144  0.66 19.08           O  
ATOM    351  OG BSER A 183      27.230   1.205  15.004  0.34 16.10           O  
ATOM    352  N   ALA A 184      22.715   1.348  16.089  1.00  9.11           N  
ATOM    353  CA  ALA A 184      21.462   0.739  16.521  1.00  8.88           C  
ATOM    354  C   ALA A 184      20.375   0.804  15.458  1.00  7.80           C  
ATOM    355  O   ALA A 184      19.383   0.092  15.559  1.00  8.44           O  
ATOM    356  CB  ALA A 184      20.943   1.445  17.788  1.00 10.45           C  
ATOM    357  N   ARG A 185      20.531   1.676  14.444  1.00  7.39           N  
ATOM    358  CA  ARG A 185      19.423   1.922  13.539  1.00  7.10           C  
ATOM    359  C   ARG A 185      19.014   0.676  12.775  1.00  6.87           C  
ATOM    360  O   ARG A 185      17.845   0.350  12.726  1.00  7.30           O  
ATOM    361  CB  ARG A 185      19.718   3.079  12.620  1.00  7.28           C  
ATOM    362  CG  ARG A 185      19.937   4.411  13.313  1.00  7.79           C  
ATOM    363  CD  ARG A 185      19.972   5.492  12.261  1.00 11.73           C  
ATOM    364  NE  ARG A 185      20.488   6.740  12.827  1.00 11.19           N  
ATOM    365  CZ  ARG A 185      21.586   7.386  12.496  1.00 11.17           C  
ATOM    366  NH1 ARG A 185      22.384   7.010  11.538  1.00 13.78           N  
ATOM    367  NH2 ARG A 185      21.901   8.455  13.182  1.00 13.31           N  
ATOM    368  N   ALA A 186      19.978   0.026  12.082  1.00  7.44           N  
ATOM    369  CA  ALA A 186      19.630  -1.127  11.250  1.00  7.85           C  
ATOM    370  C   ALA A 186      18.993  -2.245  12.069  1.00  7.30           C  
ATOM    371  O   ALA A 186      17.949  -2.759  11.643  1.00  7.59           O  
ATOM    372  CB  ALA A 186      20.843  -1.606  10.467  1.00  9.51           C  
ATOM    373  N   PRO A 187      19.543  -2.662  13.221  1.00  7.67           N  
ATOM    374  CA  PRO A 187      18.881  -3.736  13.959  1.00  8.06           C  
ATOM    375  C   PRO A 187      17.492  -3.348  14.454  1.00  6.89           C  
ATOM    376  O   PRO A 187      16.599  -4.193  14.490  1.00  7.80           O  
ATOM    377  CB  PRO A 187      19.869  -4.057  15.089  1.00 11.83           C  
ATOM    378  CG  PRO A 187      20.930  -3.118  15.008  1.00 14.69           C  
ATOM    379  CD  PRO A 187      20.877  -2.350  13.744  1.00  8.59           C  
ATOM    380  N   VAL A 188      17.302  -2.093  14.831  1.00  6.91           N  
ATOM    381  CA  VAL A 188      15.965  -1.609  15.220  1.00  6.63           C  
ATOM    382  C   VAL A 188      15.011  -1.694  14.055  1.00  6.39           C  
ATOM    383  O   VAL A 188      13.865  -2.157  14.196  1.00  6.51           O  
ATOM    384  CB  VAL A 188      16.065  -0.212  15.832  1.00  7.37           C  
ATOM    385  CG1 VAL A 188      14.686   0.473  15.867  1.00  8.09           C  
ATOM    386  CG2 VAL A 188      16.676  -0.281  17.227  1.00  8.87           C  
ATOM    387  N   ILE A 189      15.456  -1.236  12.879  1.00  6.04           N  
ATOM    388  CA  ILE A 189      14.604  -1.278  11.699  1.00  6.30           C  
ATOM    389  C   ILE A 189      14.198  -2.716  11.389  1.00  6.19           C  
ATOM    390  O   ILE A 189      13.009  -2.989  11.125  1.00  6.62           O  
ATOM    391  CB  ILE A 189      15.303  -0.605  10.496  1.00  6.47           C  
ATOM    392  CG1 ILE A 189      15.407   0.919  10.729  1.00  6.84           C  
ATOM    393  CG2 ILE A 189      14.571  -0.899   9.204  1.00  6.93           C  
ATOM    394  CD1 ILE A 189      16.487   1.569   9.910  1.00  7.62           C  
ATOM    395  N   ILE A 190      15.167  -3.627  11.408  1.00  6.36           N  
ATOM    396  CA  ILE A 190      14.837  -5.044  11.129  1.00  6.97           C  
ATOM    397  C   ILE A 190      13.835  -5.580  12.125  1.00  6.66           C  
ATOM    398  O   ILE A 190      12.861  -6.251  11.764  1.00  7.13           O  
ATOM    399  CB  ILE A 190      16.139  -5.877  11.106  1.00  7.63           C  
ATOM    400  CG1 ILE A 190      17.027  -5.530   9.891  1.00  9.31           C  
ATOM    401  CG2 ILE A 190      15.866  -7.383  11.207  1.00  9.27           C  
ATOM    402  CD1 ILE A 190      16.430  -6.005   8.618  1.00 11.20           C  
ATOM    403  N   ASP A 191      14.067  -5.306  13.424  1.00  6.64           N  
ATOM    404  CA  ASP A 191      13.092  -5.809  14.417  1.00  6.71           C  
ATOM    405  C   ASP A 191      11.697  -5.235  14.192  1.00  6.29           C  
ATOM    406  O   ASP A 191      10.702  -5.920  14.303  1.00  6.93           O  
ATOM    407  CB  ASP A 191      13.556  -5.513  15.846  1.00  7.20           C  
ATOM    408  CG  ASP A 191      14.583  -6.420  16.458  1.00  9.19           C  
ATOM    409  OD1 ASP A 191      15.253  -7.179  15.667  1.00 11.18           O  
ATOM    410  OD2 ASP A 191      14.749  -6.517  17.661  1.00 13.41           O  
ATOM    411  N   CYS A 192      11.633  -3.941  13.873  1.00  6.23           N  
ATOM    412  CA  CYS A 192      10.335  -3.332  13.637  1.00  6.20           C  
ATOM    413  C   CYS A 192       9.691  -3.839  12.341  1.00  6.29           C  
ATOM    414  O   CYS A 192       8.466  -3.977  12.277  1.00  6.52           O  
ATOM    415  CB  CYS A 192      10.439  -1.787  13.604  1.00  6.97           C  
ATOM    416  SG  CYS A 192      10.780  -1.095  15.265  1.00  8.05           S  
ATOM    417  N   PHE A 193      10.484  -4.150  11.299  1.00  6.07           N  
ATOM    418  CA  PHE A 193       9.908  -4.823  10.138  1.00  6.64           C  
ATOM    419  C   PHE A 193       9.202  -6.107  10.539  1.00  6.96           C  
ATOM    420  O   PHE A 193       8.120  -6.431  10.066  1.00  8.55           O  
ATOM    421  CB  PHE A 193      10.977  -5.176   9.121  1.00  7.30           C  
ATOM    422  CG  PHE A 193      11.514  -4.068   8.232  1.00  7.11           C  
ATOM    423  CD1 PHE A 193      11.054  -2.765   8.287  1.00  7.63           C  
ATOM    424  CD2 PHE A 193      12.473  -4.404   7.316  1.00  7.58           C  
ATOM    425  CE1 PHE A 193      11.543  -1.840   7.374  1.00  8.19           C  
ATOM    426  CE2 PHE A 193      12.975  -3.472   6.425  1.00  8.00           C  
ATOM    427  CZ  PHE A 193      12.504  -2.208   6.454  1.00  7.71           C  
ATOM    428  N   ARG A 194       9.870  -6.897  11.377  1.00  6.78           N  
ATOM    429  CA  ARG A 194       9.336  -8.196  11.789  1.00  7.52           C  
ATOM    430  C   ARG A 194       8.100  -8.041  12.669  1.00  7.46           C  
ATOM    431  O   ARG A 194       7.188  -8.864  12.595  1.00 10.75           O  
ATOM    432  CB  ARG A 194      10.380  -9.002  12.524  1.00  8.74           C  
ATOM    433  CG  ARG A 194      11.572  -9.402  11.699  1.00  9.27           C  
ATOM    434  CD  ARG A 194      12.654  -9.926  12.637  1.00 11.43           C  
ATOM    435  NE  ARG A 194      13.865 -10.346  11.997  1.00 11.54           N  
ATOM    436  CZ  ARG A 194      15.016 -10.508  12.614  1.00 12.20           C  
ATOM    437  NH1 ARG A 194      15.147 -10.250  13.912  1.00 18.18           N  
ATOM    438  NH2 ARG A 194      16.103 -10.881  11.995  1.00 15.76           N  
ATOM    439  N   GLN A 195       8.099  -7.050  13.549  1.00  6.73           N  
ATOM    440  CA  GLN A 195       7.101  -6.964  14.595  1.00  6.91           C  
ATOM    441  C   GLN A 195       5.897  -6.061  14.241  1.00  7.07           C  
ATOM    442  O   GLN A 195       4.853  -6.201  14.842  1.00  9.30           O  
ATOM    443  CB  GLN A 195       7.740  -6.445  15.873  1.00  7.41           C  
ATOM    444  CG  GLN A 195       8.764  -7.395  16.470  1.00  7.92           C  
ATOM    445  CD  GLN A 195       9.454  -6.816  17.661  1.00  8.62           C  
ATOM    446  OE1 GLN A 195       8.853  -6.072  18.439  1.00 10.56           O  
ATOM    447  NE2 GLN A 195      10.734  -7.136  17.869  1.00 11.17           N  
ATOM    448  N   LYS A 196       6.121  -5.081  13.354  1.00  6.68           N  
ATOM    449  CA  LYS A 196       5.175  -3.988  13.200  1.00  6.74           C  
ATOM    450  C   LYS A 196       4.523  -3.944  11.810  1.00  6.91           C  
ATOM    451  O   LYS A 196       3.678  -3.089  11.550  1.00  8.26           O  
ATOM    452  CB  LYS A 196       5.845  -2.654  13.514  1.00  7.03           C  
ATOM    453  CG  LYS A 196       6.526  -2.613  14.897  1.00  7.76           C  
ATOM    454  CD  LYS A 196       5.647  -2.827  16.063  1.00  8.29           C  
ATOM    455  CE  LYS A 196       4.772  -1.632  16.402  0.75  7.33           C  
ATOM    456  NZ  LYS A 196       5.555  -0.565  17.041  0.75  7.17           N  
ATOM    457  N   SER A 197       4.942  -4.869  10.926  1.00  7.62           N  
ATOM    458  CA ASER A 197       4.269  -4.976   9.622  0.72  7.83           C  
ATOM    459  CA BSER A 197       4.341  -5.120   9.635  0.28  8.18           C  
ATOM    460  C   SER A 197       2.971  -5.759   9.821  1.00  7.67           C  
ATOM    461  O   SER A 197       2.701  -6.362  10.859  1.00  9.77           O  
ATOM    462  CB ASER A 197       5.193  -5.639   8.637  0.72  8.01           C  
ATOM    463  CB BSER A 197       5.273  -6.053   8.861  0.28  8.44           C  
ATOM    464  OG ASER A 197       5.650  -6.892   9.093  0.72  8.42           O  
ATOM    465  OG BSER A 197       6.418  -5.295   8.443  0.28 10.29           O  
ATOM    466  N   GLN A 198       2.141  -5.725   8.792  1.00  8.01           N  
ATOM    467  CA  GLN A 198       0.889  -6.460   8.776  1.00  9.18           C  
ATOM    468  C   GLN A 198       1.189  -7.966   8.853  1.00  9.14           C  
ATOM    469  O   GLN A 198       2.239  -8.396   8.398  1.00  8.81           O  
ATOM    470  CB  GLN A 198       0.086  -6.153   7.523  1.00 10.35           C  
ATOM    471  CG  GLN A 198      -0.621  -4.789   7.561  1.00 11.35           C  
ATOM    472  CD  GLN A 198      -1.855  -4.843   8.403  1.00 14.39           C  
ATOM    473  OE1 GLN A 198      -2.599  -5.790   8.424  1.00 21.25           O  
ATOM    474  NE2 GLN A 198      -2.162  -3.768   9.080  1.00 13.95           N  
ATOM    475  N   PRO A 199       0.273  -8.771   9.389  1.00 11.77           N  
ATOM    476  CA  PRO A 199       0.582 -10.207   9.582  1.00 13.29           C  
ATOM    477  C   PRO A 199       1.010 -10.947   8.323  1.00 11.59           C  
ATOM    478  O   PRO A 199       1.933 -11.761   8.424  1.00 11.81           O  
ATOM    479  CB  PRO A 199      -0.723 -10.795  10.116  1.00 16.54           C  
ATOM    480  CG  PRO A 199      -1.326  -9.622  10.815  1.00 20.96           C  
ATOM    481  CD  PRO A 199      -1.004  -8.421   9.984  1.00 17.06           C  
ATOM    482  N   ASP A 200       0.406 -10.670   7.172  1.00 11.65           N  
ATOM    483  CA AASP A 200       0.796 -11.407   5.993  0.40 10.79           C  
ATOM    484  CA BASP A 200       0.791 -11.401   6.000  0.61 11.25           C  
ATOM    485  C   ASP A 200       2.257 -11.101   5.641  1.00  9.66           C  
ATOM    486  O   ASP A 200       2.998 -11.971   5.180  1.00 10.77           O  
ATOM    487  CB AASP A 200      -0.052 -11.064   4.780  0.40 12.27           C  
ATOM    488  CB BASP A 200      -0.134 -11.050   4.855  0.61 13.02           C  
ATOM    489  CG AASP A 200      -1.458 -11.618   4.766  0.40 14.55           C  
ATOM    490  CG BASP A 200      -0.340  -9.606   4.476  0.61 17.08           C  
ATOM    491  OD1AASP A 200      -1.794 -12.494   5.568  0.40 15.52           O  
ATOM    492  OD1BASP A 200      -0.002  -8.619   5.179  0.61 15.85           O  
ATOM    493  OD2AASP A 200      -2.245 -11.135   3.908  0.40 21.60           O  
ATOM    494  OD2BASP A 200      -0.897  -9.399   3.365  0.61 26.52           O  
ATOM    495  N   ILE A 201       2.679  -9.836   5.833  1.00  8.40           N  
ATOM    496  CA  ILE A 201       4.043  -9.423   5.542  1.00  7.95           C  
ATOM    497  C   ILE A 201       4.988  -9.979   6.579  1.00  7.34           C  
ATOM    498  O   ILE A 201       6.073 -10.440   6.228  1.00  7.77           O  
ATOM    499  CB  ILE A 201       4.132  -7.899   5.449  1.00  9.34           C  
ATOM    500  CG1 ILE A 201       3.246  -7.324   4.359  1.00 13.51           C  
ATOM    501  CG2 ILE A 201       5.589  -7.491   5.309  1.00 11.27           C  
ATOM    502  CD1 ILE A 201       3.656  -7.696   2.954  1.00 17.37           C  
ATOM    503  N   GLN A 202       4.615  -9.965   7.868  1.00  7.94           N  
ATOM    504  CA  GLN A 202       5.434 -10.609   8.856  1.00  7.96           C  
ATOM    505  C   GLN A 202       5.766 -12.041   8.479  1.00  8.05           C  
ATOM    506  O   GLN A 202       6.904 -12.534   8.598  1.00  8.24           O  
ATOM    507  CB  GLN A 202       4.716 -10.618  10.237  1.00  9.80           C  
ATOM    508  CG  GLN A 202       4.554  -9.310  10.901  1.00 11.87           C  
ATOM    509  CD  GLN A 202       3.974  -9.373  12.238  1.00 16.40           C  
ATOM    510  OE1 GLN A 202       4.448 -10.098  13.148  1.00 20.77           O  
ATOM    511  NE2 GLN A 202       3.130  -8.410  12.535  1.00 31.51           N  
ATOM    512  N   GLN A 203       4.714 -12.749   8.012  1.00  7.73           N  
ATOM    513  CA  GLN A 203       4.874 -14.133   7.620  1.00  7.97           C  
ATOM    514  C   GLN A 203       5.759 -14.277   6.386  1.00  7.74           C  
ATOM    515  O   GLN A 203       6.534 -15.228   6.287  1.00  9.13           O  
ATOM    516  CB  GLN A 203       3.501 -14.775   7.436  1.00  8.73           C  
ATOM    517  CG  GLN A 203       2.871 -15.004   8.799  1.00  9.87           C  
ATOM    518  CD  GLN A 203       1.509 -15.563   8.683  1.00 12.59           C  
ATOM    519  OE1 GLN A 203       1.206 -16.330   7.758  1.00 15.52           O  
ATOM    520  NE2 GLN A 203       0.636 -15.187   9.610  1.00 12.29           N  
ATOM    521  N   LEU A 204       5.650 -13.355   5.443  1.00  7.04           N  
ATOM    522  CA  LEU A 204       6.549 -13.425   4.298  1.00  6.70           C  
ATOM    523  C   LEU A 204       7.994 -13.159   4.713  1.00  6.81           C  
ATOM    524  O   LEU A 204       8.912 -13.839   4.261  1.00  7.33           O  
ATOM    525  CB  LEU A 204       6.086 -12.428   3.248  1.00  7.24           C  
ATOM    526  CG  LEU A 204       6.908 -12.386   1.953  1.00  7.62           C  
ATOM    527  CD1 LEU A 204       6.936 -13.742   1.272  1.00  8.62           C  
ATOM    528  CD2 LEU A 204       6.383 -11.302   1.039  1.00  8.87           C  
ATOM    529  N   ILE A 205       8.228 -12.158   5.563  1.00  6.78           N  
ATOM    530  CA  ILE A 205       9.582 -11.837   5.974  1.00  7.37           C  
ATOM    531  C   ILE A 205      10.262 -13.057   6.634  1.00  8.03           C  
ATOM    532  O   ILE A 205      11.437 -13.290   6.424  1.00  9.44           O  
ATOM    533  CB  ILE A 205       9.584 -10.607   6.895  1.00  7.34           C  
ATOM    534  CG1 ILE A 205       9.219  -9.355   6.073  1.00  7.39           C  
ATOM    535  CG2 ILE A 205      10.887 -10.408   7.597  1.00  8.93           C  
ATOM    536  CD1 ILE A 205       8.975  -8.105   6.918  1.00  8.80           C  
ATOM    537  N   ARG A 206       9.489 -13.819   7.423  1.00  8.73           N  
ATOM    538  CA  ARG A 206      10.193 -14.905   8.123  1.00 11.38           C  
ATOM    539  C   ARG A 206      10.574 -16.060   7.187  1.00 10.63           C  
ATOM    540  O   ARG A 206      11.298 -16.917   7.608  1.00 12.64           O  
ATOM    541  CB  ARG A 206       9.523 -15.222   9.434  1.00 13.18           C  
ATOM    542  CG  ARG A 206       8.256 -15.919   9.072  1.00 12.02           C  
ATOM    543  CD  ARG A 206       7.326 -15.974  10.385  1.00 13.71           C  
ATOM    544  NE  ARG A 206       6.261 -16.859  10.229  1.00 14.61           N  
ATOM    545  CZ  ARG A 206       5.199 -16.962  11.063  1.00 13.46           C  
ATOM    546  NH1 ARG A 206       5.098 -16.146  12.100  1.00 17.63           N  
ATOM    547  NH2 ARG A 206       4.265 -17.803  10.825  1.00 15.01           N  
ATOM    548  N   THR A 207      10.106 -16.037   5.920  1.00  9.35           N  
ATOM    549  CA  THR A 207      10.593 -17.026   4.918  1.00  9.77           C  
ATOM    550  C   THR A 207      11.944 -16.655   4.338  1.00  9.32           C  
ATOM    551  O   THR A 207      12.510 -17.482   3.623  1.00 10.44           O  
ATOM    552  CB  THR A 207       9.590 -17.264   3.829  1.00  9.83           C  
ATOM    553  OG1 THR A 207       9.480 -16.115   3.003  1.00  8.41           O  
ATOM    554  CG2 THR A 207       8.207 -17.625   4.375  1.00 11.49           C  
ATOM    555  N   ALA A 208      12.418 -15.422   4.521  1.00  9.36           N  
ATOM    556  CA  ALA A 208      13.616 -14.948   3.878  1.00  9.13           C  
ATOM    557  C   ALA A 208      14.856 -15.773   4.308  1.00 10.28           C  
ATOM    558  O   ALA A 208      14.937 -16.231   5.435  1.00 12.11           O  
ATOM    559  CB  ALA A 208      13.864 -13.480   4.170  1.00 10.22           C  
ATOM    560  N   PRO A 209      15.814 -15.916   3.396  1.00 11.79           N  
ATOM    561  CA  PRO A 209      17.006 -16.719   3.818  1.00 13.91           C  
ATOM    562  C   PRO A 209      17.810 -15.975   4.834  1.00 13.41           C  
ATOM    563  O   PRO A 209      17.812 -14.756   4.946  1.00 13.48           O  
ATOM    564  CB  PRO A 209      17.624 -16.963   2.428  1.00 15.51           C  
ATOM    565  CG  PRO A 209      17.257 -15.805   1.589  1.00 13.48           C  
ATOM    566  CD  PRO A 209      15.883 -15.426   2.045  1.00 10.81           C  
ATOM    567  N   SER A 210      18.590 -16.746   5.581  1.00 16.74           N  
ATOM    568  CA  SER A 210      19.424 -16.224   6.667  1.00 16.82           C  
ATOM    569  C   SER A 210      20.473 -15.268   6.138  1.00 16.70           C  
ATOM    570  O   SER A 210      21.034 -14.483   6.883  1.00 20.06           O  
ATOM    571  CB  SER A 210      20.080 -17.391   7.469  1.00 17.63           C  
ATOM    572  OG  SER A 210      20.911 -18.155   6.600  1.00 18.03           O  
ATOM    573  N   THR A 211      20.813 -15.299   4.855  1.00 16.24           N  
ATOM    574  CA  THR A 211      21.777 -14.437   4.209  1.00 19.51           C  
ATOM    575  C   THR A 211      21.289 -12.998   4.007  1.00 16.48           C  
ATOM    576  O   THR A 211      22.089 -12.111   3.846  1.00 21.96           O  
ATOM    577  CB  THR A 211      22.078 -15.112   2.835  1.00 24.72           C  
ATOM    578  OG1 THR A 211      20.878 -15.467   2.101  1.00 26.09           O  
ATOM    579  CG2 THR A 211      22.920 -16.350   3.142  1.00 29.84           C  
ATOM    580  N   LEU A 212      19.977 -12.791   4.076  1.00 14.62           N  
ATOM    581  CA  LEU A 212      19.427 -11.440   3.930  1.00 13.66           C  
ATOM    582  C   LEU A 212      19.351 -10.784   5.282  1.00 16.32           C  
ATOM    583  O   LEU A 212      18.538 -11.092   6.180  1.00 28.36           O  
ATOM    584  CB  LEU A 212      18.040 -11.434   3.298  1.00 15.66           C  
ATOM    585  CG  LEU A 212      18.020 -12.029   1.876  1.00 16.88           C  
ATOM    586  CD1 LEU A 212      16.640 -11.728   1.327  1.00 23.77           C  
ATOM    587  CD2 LEU A 212      19.134 -11.514   1.012  1.00 17.53           C  
ATOM    588  N   THR A 213      20.228  -9.790   5.499  1.00 16.12           N  
ATOM    589  CA  THR A 213      20.374  -9.217   6.824  1.00 18.73           C  
ATOM    590  C   THR A 213      20.078  -7.701   6.854  1.00 16.59           C  
ATOM    591  O   THR A 213      19.835  -7.236   7.953  1.00 23.99           O  
ATOM    592  CB  THR A 213      21.745  -9.477   7.449  1.00 22.75           C  
ATOM    593  OG1 THR A 213      22.687  -8.811   6.627  1.00 22.93           O  
ATOM    594  CG2 THR A 213      22.057 -10.967   7.446  0.25 26.83           C  
ATOM    595  N   THR A 214      20.087  -6.985   5.768  1.00 11.16           N  
ATOM    596  CA  THR A 214      19.929  -5.554   5.827  1.00  9.84           C  
ATOM    597  C   THR A 214      18.488  -5.177   5.548  1.00  7.49           C  
ATOM    598  O   THR A 214      17.734  -5.892   4.890  1.00  7.03           O  
ATOM    599  CB  THR A 214      20.780  -4.831   4.773  1.00 10.17           C  
ATOM    600  OG1 THR A 214      20.262  -5.106   3.476  1.00  9.84           O  
ATOM    601  CG2 THR A 214      22.257  -5.262   4.900  1.00 13.76           C  
ATOM    602  N   PRO A 215      18.116  -3.961   5.994  1.00  6.84           N  
ATOM    603  CA  PRO A 215      16.749  -3.471   5.658  1.00  5.99           C  
ATOM    604  C   PRO A 215      16.461  -3.492   4.179  1.00  5.41           C  
ATOM    605  O   PRO A 215      15.396  -3.909   3.735  1.00  5.71           O  
ATOM    606  CB  PRO A 215      16.682  -2.099   6.291  1.00  6.47           C  
ATOM    607  CG  PRO A 215      17.638  -2.222   7.474  1.00  8.02           C  
ATOM    608  CD  PRO A 215      18.766  -3.052   6.975  1.00  8.28           C  
ATOM    609  N   GLY A 216      17.433  -3.023   3.358  1.00  5.64           N  
ATOM    610  CA  GLY A 216      17.219  -2.994   1.925  1.00  5.78           C  
ATOM    611  C   GLY A 216      17.009  -4.391   1.317  1.00  5.97           C  
ATOM    612  O   GLY A 216      16.207  -4.540   0.415  1.00  6.35           O  
ATOM    613  N   GLU A 217      17.736  -5.381   1.820  1.00  5.90           N  
ATOM    614  CA  GLU A 217      17.544  -6.725   1.341  1.00  6.48           C  
ATOM    615  C   GLU A 217      16.149  -7.232   1.661  1.00  5.91           C  
ATOM    616  O   GLU A 217      15.511  -7.923   0.845  1.00  6.46           O  
ATOM    617  CB  GLU A 217      18.594  -7.666   1.920  1.00  7.26           C  
ATOM    618  CG  GLU A 217      19.979  -7.463   1.277  1.00  9.13           C  
ATOM    619  CD  GLU A 217      21.123  -8.059   2.078  1.00 12.78           C  
ATOM    620  OE1 GLU A 217      20.996  -8.442   3.235  1.00 11.54           O  
ATOM    621  OE2 GLU A 217      22.238  -7.998   1.488  1.00 23.85           O  
ATOM    622  N   ILE A 218      15.635  -6.918   2.863  1.00  5.87           N  
ATOM    623  CA  ILE A 218      14.282  -7.345   3.222  1.00  5.74           C  
ATOM    624  C   ILE A 218      13.221  -6.587   2.424  1.00  5.49           C  
ATOM    625  O   ILE A 218      12.218  -7.189   2.008  1.00  5.83           O  
ATOM    626  CB  ILE A 218      14.074  -7.235   4.748  1.00  6.63           C  
ATOM    627  CG1 ILE A 218      15.052  -8.153   5.499  1.00  8.66           C  
ATOM    628  CG2 ILE A 218      12.636  -7.536   5.110  1.00  6.67           C  
ATOM    629  CD1 ILE A 218      14.938  -9.635   5.141  1.00 11.48           C  
ATOM    630  N   ILE A 219      13.427  -5.290   2.190  1.00  5.61           N  
ATOM    631  CA  ILE A 219      12.501  -4.529   1.351  1.00  5.33           C  
ATOM    632  C   ILE A 219      12.419  -5.146  -0.035  1.00  5.41           C  
ATOM    633  O   ILE A 219      11.313  -5.370  -0.567  1.00  5.77           O  
ATOM    634  CB  ILE A 219      12.917  -3.049   1.297  1.00  5.59           C  
ATOM    635  CG1 ILE A 219      12.702  -2.381   2.661  1.00  5.77           C  
ATOM    636  CG2 ILE A 219      12.175  -2.308   0.187  1.00  6.91           C  
ATOM    637  CD1 ILE A 219      13.538  -1.132   2.833  1.00  6.39           C  
ATOM    638  N   LYS A 220      13.558  -5.424  -0.658  1.00  5.51           N  
ATOM    639  CA  LYS A 220      13.536  -6.034  -1.975  1.00  5.78           C  
ATOM    640  C   LYS A 220      12.878  -7.417  -1.931  1.00  5.64           C  
ATOM    641  O   LYS A 220      12.136  -7.800  -2.830  1.00  6.38           O  
ATOM    642  CB  LYS A 220      14.934  -6.132  -2.570  1.00  6.35           C  
ATOM    643  CG  LYS A 220      15.512  -4.797  -2.989  1.00  7.31           C  
ATOM    644  CD  LYS A 220      16.896  -4.896  -3.552  1.00  8.41           C  
ATOM    645  CE  LYS A 220      17.910  -5.289  -2.584  1.00 13.02           C  
ATOM    646  NZ  LYS A 220      19.274  -5.359  -3.182  1.00 18.33           N  
ATOM    647  N   TYR A 221      13.165  -8.185  -0.875  1.00  5.83           N  
ATOM    648  CA  TYR A 221      12.589  -9.527  -0.764  1.00  6.06           C  
ATOM    649  C   TYR A 221      11.074  -9.454  -0.819  1.00  5.70           C  
ATOM    650  O   TYR A 221      10.399 -10.202  -1.530  1.00  6.08           O  
ATOM    651  CB  TYR A 221      13.079 -10.178   0.546  1.00  6.47           C  
ATOM    652  CG  TYR A 221      12.586 -11.601   0.708  1.00  6.30           C  
ATOM    653  CD1 TYR A 221      13.299 -12.649   0.130  1.00  6.31           C  
ATOM    654  CD2 TYR A 221      11.467 -11.886   1.444  1.00  6.69           C  
ATOM    655  CE1 TYR A 221      12.875 -13.987   0.273  1.00  6.57           C  
ATOM    656  CE2 TYR A 221      11.017 -13.213   1.592  1.00  7.12           C  
ATOM    657  CZ  TYR A 221      11.726 -14.235   1.002  1.00  6.90           C  
ATOM    658  OH  TYR A 221      11.386 -15.573   1.045  1.00  8.88           O  
ATOM    659  N   VAL A 222      10.500  -8.558   0.009  1.00  5.89           N  
ATOM    660  CA  VAL A 222       9.057  -8.400   0.087  1.00  5.71           C  
ATOM    661  C   VAL A 222       8.493  -7.897  -1.220  1.00  5.75           C  
ATOM    662  O   VAL A 222       7.552  -8.454  -1.795  1.00  6.33           O  
ATOM    663  CB  VAL A 222       8.661  -7.503   1.278  1.00  6.29           C  
ATOM    664  CG1 VAL A 222       7.187  -7.167   1.228  1.00  7.24           C  
ATOM    665  CG2 VAL A 222       9.051  -8.164   2.604  1.00  7.31           C  
ATOM    666  N   LEU A 223       9.055  -6.775  -1.719  1.00  5.95           N  
ATOM    667  CA ALEU A 223       8.448  -6.119  -2.882  0.81  6.11           C  
ATOM    668  CA BLEU A 223       8.475  -6.153  -2.889  0.19  6.35           C  
ATOM    669  C   LEU A 223       8.526  -7.052  -4.110  1.00  6.33           C  
ATOM    670  O   LEU A 223       7.578  -7.091  -4.916  1.00  7.43           O  
ATOM    671  CB ALEU A 223       9.081  -4.764  -3.179  0.81  7.51           C  
ATOM    672  CB BLEU A 223       9.244  -4.849  -3.114  0.19  4.76           C  
ATOM    673  CG ALEU A 223       8.483  -3.568  -2.439  0.81  9.18           C  
ATOM    674  CG BLEU A 223       8.602  -3.906  -4.115  0.19  7.34           C  
ATOM    675  CD1ALEU A 223       8.304  -3.771  -0.974  0.81  8.34           C  
ATOM    676  CD1BLEU A 223       7.212  -3.499  -3.599  0.19 13.03           C  
ATOM    677  CD2ALEU A 223       9.395  -2.366  -2.738  0.81 10.93           C  
ATOM    678  CD2BLEU A 223       9.519  -2.705  -4.314  0.19  9.50           C  
ATOM    679  N   ASP A 224       9.617  -7.796  -4.236  1.00  6.31           N  
ATOM    680  CA  ASP A 224       9.810  -8.654  -5.400  1.00  6.49           C  
ATOM    681  C   ASP A 224       8.870  -9.867  -5.411  1.00  6.72           C  
ATOM    682  O   ASP A 224       8.770 -10.574  -6.406  1.00  8.00           O  
ATOM    683  CB  ASP A 224      11.221  -9.134  -5.478  1.00  7.58           C  
ATOM    684  CG  ASP A 224      12.229  -8.067  -5.735  1.00  9.40           C  
ATOM    685  OD1 ASP A 224      11.878  -6.913  -6.055  1.00 10.95           O  
ATOM    686  OD2 ASP A 224      13.461  -8.430  -5.642  1.00 10.70           O  
ATOM    687  N   ARG A 225       8.198 -10.106  -4.276  1.00  5.95           N  
ATOM    688  CA  ARG A 225       7.253 -11.217  -4.128  1.00  6.05           C  
ATOM    689  C   ARG A 225       5.821 -10.747  -4.171  1.00  7.16           C  
ATOM    690  O   ARG A 225       4.902 -11.565  -4.009  1.00  7.63           O  
ATOM    691  CB  ARG A 225       7.644 -12.042  -2.890  1.00  6.21           C  
ATOM    692  CG  ARG A 225       8.873 -12.883  -3.203  1.00  6.18           C  
ATOM    693  CD  ARG A 225       9.639 -13.333  -1.982  1.00  6.25           C  
ATOM    694  NE  ARG A 225      10.853 -14.060  -2.321  1.00  6.56           N  
ATOM    695  CZ  ARG A 225      11.933 -13.475  -2.831  1.00  6.58           C  
ATOM    696  NH1 ARG A 225      11.964 -12.162  -3.040  1.00  6.47           N  
ATOM    697  NH2 ARG A 225      13.004 -14.198  -3.139  1.00  7.60           N  
ATOM    698  N   GLN A 226       5.568  -9.474  -4.442  1.00  8.86           N  
ATOM    699  CA  GLN A 226       4.219  -8.992  -4.680  1.00  9.33           C  
ATOM    700  C   GLN A 226       3.749  -9.197  -6.147  1.00 10.28           C  
ATOM    701  O   GLN A 226       2.528  -8.884  -6.286  1.00 14.16           O  
ATOM    702  CB  GLN A 226       4.088  -7.529  -4.299  1.00 10.73           C  
ATOM    703  CG  GLN A 226       4.446  -7.341  -2.921  1.00 11.00           C  
ATOM    704  CD  GLN A 226       3.821  -8.247  -1.957  0.50  8.67           C  
ATOM    705  OE1 GLN A 226       2.592  -8.421  -1.916  0.50 10.85           O  
ATOM    706  NE2 GLN A 226       4.640  -8.912  -1.151  0.50  7.67           N  
ATOM    707  OXT GLN A 226       4.429  -9.726  -6.976  1.00 14.11           O  
TER     708      GLN A 226                                                      
HETATM  709  N   NO3 A   1      20.901  -3.373  -1.271  1.00 29.31           N  
HETATM  710  O1  NO3 A   1      21.848  -2.704  -0.751  1.00 28.52           O  
HETATM  711  O2  NO3 A   1      20.898  -3.616  -2.458  1.00 41.99           O  
HETATM  712  O3  NO3 A   1      19.984  -3.761  -0.511  1.00 33.11           O  
HETATM  713  O   HOH A   2       7.492   0.625  15.312  1.00  8.72           O  
HETATM  714  O   HOH A   3      22.705   0.995  11.686  1.00 10.20           O  
HETATM  715  O   HOH A   4      19.656   8.198  15.108  1.00 14.03           O  
HETATM  716  O   HOH A   5      12.602   6.692   4.382  1.00 13.16           O  
HETATM  717  O   HOH A   6       8.760 -11.452  10.462  1.00 17.06           O  
HETATM  718  O   HOH A   7       8.262   9.158   9.510  1.00 15.31           O  
HETATM  719  O   HOH A   8      14.538 -18.287   1.855  1.00 13.37           O  
HETATM  720  O   HOH A   9      21.862   2.179   9.320  1.00 13.93           O  
HETATM  721  O   HOH A  10      19.813   0.668   8.279  1.00 13.43           O  
HETATM  722  O   HOH A  11       0.756  -3.738  11.288  1.00 15.26           O  
HETATM  723  O   HOH A  12      21.581   4.849   9.216  1.00 15.62           O  
HETATM  724  O  AHOH A  13       5.786 -17.691   7.390  0.62 12.42           O  
HETATM  725  O  BHOH A  13       5.326 -17.765   6.498  0.38 16.23           O  
HETATM  726  O   HOH A  14       7.433  10.118   6.972  1.00 19.09           O  
HETATM  727  O   HOH A  15      17.857   6.944  23.743  1.00 17.13           O  
HETATM  728  O   HOH A  16      21.020  -4.939   9.186  1.00 16.96           O  
HETATM  729  O   HOH A  17      14.502   9.875  19.631  1.00 18.57           O  
HETATM  730  O   HOH A  18       1.229  -9.438  -8.608  1.00 21.15           O  
HETATM  731  O   HOH A  19       6.590   6.266   0.869  1.00 22.57           O  
HETATM  732  O   HOH A  22      24.691  -2.575  14.108  1.00 33.12           O  
HETATM  733  O   HOH A  23      24.718  -1.087  11.997  1.00 28.38           O  
HETATM  734  O   HOH A  25      21.170  -5.271  11.696  1.00 22.73           O  
HETATM  735  O   HOH A  26      19.542  -7.500  12.653  1.00 27.50           O  
HETATM  736  O   HOH A  27      19.087  -8.887  10.039  1.00 20.41           O  
HETATM  737  O   HOH A  28      13.088  -7.637   8.900  1.00 19.44           O  
HETATM  738  O  AHOH A  29      13.901 -11.628   9.724  0.41 19.68           O  
HETATM  739  O  BHOH A  29      14.274 -10.102   9.022  0.31  9.07           O  
HETATM  740  O  CHOH A  29      13.711 -12.753   8.035  0.29 14.21           O  
HETATM  741  O   HOH A  30      11.396 -12.734  10.462  1.00 26.88           O  
HETATM  742  O  AHOH A  33      16.473 -12.862   7.023  0.53 21.69           O  
HETATM  743  O  BHOH A  33      17.592 -13.013   8.044  0.47 20.69           O  
HETATM  744  O   HOH A  34       9.822  -5.211  -6.985  1.00 22.65           O  
HETATM  745  O   HOH A  35       9.911  11.044  10.932  1.00 19.73           O  
HETATM  746  O   HOH A  36       5.973   6.601   3.789  1.00 23.21           O  
HETATM  747  O   HOH A  37       3.069 -16.059  14.212  1.00 25.66           O  
HETATM  748  O   HOH A  38       4.273   8.086  21.363  1.00 23.57           O  
HETATM  749  O   HOH A  39       8.097   8.414   4.630  1.00 19.48           O  
HETATM  750  O   HOH A  40      26.908   3.795  16.772  1.00 21.31           O  
HETATM  751  O   HOH A  41       7.871  12.927   7.264  1.00 29.88           O  
HETATM  752  O   HOH A  42      13.993  12.050   9.714  1.00 22.08           O  
HETATM  753  O   HOH A  43       2.931 -18.081   6.306  1.00 16.67           O  
HETATM  754  O   HOH A  44      23.656   2.062   7.097  1.00 18.27           O  
HETATM  755  O   HOH A  45      14.307 -10.635  -3.692  1.00 22.68           O  
HETATM  756  O   HOH A  46      17.738  14.359  11.894  1.00 27.03           O  
HETATM  757  O  AHOH A  47       1.779   4.033  12.280  0.56 18.45           O  
HETATM  758  O  BHOH A  47       1.586   3.962  12.881  0.44 13.72           O  
HETATM  759  O   HOH A  49      -0.069 -14.833   5.443  1.00 26.74           O  
HETATM  760  O   HOH A  50      -3.785   2.650   7.350  1.00 24.79           O  
HETATM  761  O  AHOH A  51      12.256   9.177  18.156  0.38 14.76           O  
HETATM  762  O  BHOH A  51      12.244  10.191  15.464  0.62 17.91           O  
HETATM  763  O  BHOH A  52      16.937 -10.162   9.022  1.00 31.37           O  
HETATM  764  O  BHOH A  54      16.256 -20.387   2.860  1.00 20.62           O  
HETATM  765  O  BHOH A  55      18.497 -19.799   4.826  1.00 32.58           O  
HETATM  766  O  BHOH A  56      -3.543   7.590   4.513  1.00 21.09           O  
HETATM  767  O  BHOH A  57       7.870 -11.842  12.819  1.00 43.20           O  
HETATM  768  O  BHOH A  59      -1.952  -9.135   6.784  1.00 30.22           O  
HETATM  769  O   HOH A  62       6.178 -10.562  16.433  1.00 32.61           O  
HETATM  770  O   HOH A  67      27.309  -3.573  10.635  1.00 36.35           O  
HETATM  771  O   HOH A  68      15.445  14.722  13.653  1.00 32.67           O  
HETATM  772  O   HOH A  69       1.003   7.792   6.829  1.00 31.11           O  
HETATM  773  O  AHOH A  70      16.058  -9.439  -1.562  0.40 12.23           O  
HETATM  774  O  BHOH A  70      17.205  -8.942  -1.309  0.60 16.30           O  
HETATM  775  O  AHOH A  71       3.117   0.651  17.287  0.30 14.66           O  
HETATM  776  O  BHOH A  71       3.127   0.751  18.130  0.70 19.31           O  
HETATM  777  O   HOH A  72      23.949  -0.906  18.298  1.00 30.08           O  
HETATM  778  O   HOH A  73       1.998   7.089   0.629  1.00 29.92           O  
HETATM  779  O  AHOH A  74       1.284   2.975   1.361  0.35  8.39           O  
HETATM  780  O  BHOH A  74       0.458   3.390   1.673  0.65 12.25           O  
HETATM  781  O  AHOH A  76      -2.099  -2.877   4.833  0.58 18.95           O  
HETATM  782  O  BHOH A  76      -1.140  -3.606   3.871  0.42 16.78           O  
HETATM  783  O  AHOH A  84      12.410  -8.832  16.150  0.55 17.03           O  
HETATM  784  O  BHOH A  84      11.555  -9.983  16.091  0.45 18.22           O  
HETATM  785  O   HOH A  85      -0.468   5.030   3.474  1.00 26.23           O  
HETATM  786  O   HOH A  86      20.555  -7.120  15.637  1.00 34.98           O  
HETATM  787  O   HOH A  87       1.912  -5.579  13.168  1.00 38.75           O  
HETATM  788  O  AHOH A  89      19.977 -14.244  -0.992  0.68 25.36           O  
HETATM  789  O  BHOH A  89      19.316 -15.483  -2.235  0.32 23.12           O  
HETATM  790  O   HOH A  92      -1.992   9.414   6.810  1.00 42.38           O  
HETATM  791  O   HOH A  93      19.313   3.267   8.965  1.00 38.28           O  
HETATM  792  O   HOH A  95      16.889  13.166  17.528  1.00 32.30           O  
HETATM  793  O   HOH A  96      -1.132 -17.281   6.626  1.00 56.96           O  
HETATM  794  O  AHOH A  98      24.778   8.524  10.881  0.58 22.33           O  
HETATM  795  O  BHOH A  98      24.762   9.439  12.066  0.42 21.16           O  
HETATM  796  O  AHOH A  99       4.946   8.598  10.531  0.52 19.99           O  
HETATM  797  O  BHOH A  99       4.218   8.449  11.944  0.17 12.48           O  
HETATM  798  O  CHOH A  99       6.410   9.415  11.344  0.31 16.92           O  
HETATM  799  O  CHOH A 103      -0.427  -5.755  12.431  1.00 26.04           O  
HETATM  800  O  CHOH A 104      21.738  -4.011   1.482  1.00 25.45           O  
HETATM  801  O  AHOH A 105       4.941  -2.294  -0.526  0.52 11.33           O  
HETATM  802  O  BHOH A 105       5.548  -2.727  -0.689  0.47 15.97           O  
HETATM  803  O  AHOH A 106       3.271  -4.832  -0.247  0.30 11.77           O  
HETATM  804  O  BHOH A 106       2.618  -4.169   0.713  0.70 26.54           O  
HETATM  805  O   HOH A 107       1.095  -4.868   2.516  1.00 38.07           O  
HETATM  806  O  AHOH A 108       5.230  -4.988  -1.683  0.49 15.75           O  
HETATM  807  O  BHOH A 108       4.958  -4.930  -0.581  0.51 22.91           O  
HETATM  808  O   HOH A 110      -7.194  -4.014  10.631  1.00 47.93           O  
HETATM  809  O   HOH A 111      -0.644 -12.853   1.904  1.00 37.35           O  
HETATM  810  O   HOH A 112      16.926 -13.497  -1.897  1.00 28.00           O  
HETATM  811  O   HOH A 113      -0.910   2.476  11.149  1.00 33.88           O  
HETATM  812  O   HOH A 114      22.684   9.436  16.663  1.00 32.23           O  
HETATM  813  O   HOH A 227      11.365 -16.743  -1.376  1.00  9.89           O  
CONECT  709  710  711  712                                                      
CONECT  710  709                                                                
CONECT  711  709                                                                
CONECT  712  709                                                                
MASTER      239    0    1    6    0    0    2    6  683    1    4    6          
END                                                                             
