HEADER    RIBONUCLEASE                            28-JUN-00   1E44              
TITLE     RIBONUCLEASE DOMAIN OF COLICIN E3 IN COMPLEX WITH ITS                 
TITLE    2 IMMUNITY PROTEIN                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLICIN E3;                                                
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: RIBONUCLEASE DOMAIN RESIDUES 456-551;                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: IMMUNITY PROTEIN;                                          
COMPND   8 CHAIN: A;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE   8 OTHER_DETAILS: CO-EXPRESSED WITH A HIS-TAGGED IMMUNITY               
SOURCE   9  PROTEIN;                                                            
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    RIBONUCLEASE, INHIBITION, PROTEIN-PROTEIN INTERACTIONS,               
KEYWDS   2 RIBOSOME INACTIVATION, TOXIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CARR,D.WALKER,R.JAMES,C.KLEANTHOUS,A.M.HEMMINGS                     
REVDAT   2   24-FEB-09 1E44    1       VERSN                                    
REVDAT   1   28-JUN-01 1E44    0                                                
JRNL        AUTH   S.CARR,D.WALKER,R.JAMES,C.KLEANTHOUS,A.M.HEMMINGS            
JRNL        TITL   INHIBITION OF A RIBOSOME INACTIVATING                        
JRNL        TITL 2 RIBONUCLEASE: THE CRYSTAL STRUCTURE OF THE                   
JRNL        TITL 3 CYTOTOXIC DOMAIN OF COLICIN E3 IN COMPLEX WITH ITS           
JRNL        TITL 4 IMMUNITY PROTEIN                                             
JRNL        REF    STRUCTURE                     V.   8   949 2000              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   10986462                                                     
JRNL        DOI    10.1016/S0969-2126(00)00186-6                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.4  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.4                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2                              
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000                         
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 14892                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 726                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1458                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 171                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.021                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.86                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E44 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5087.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9, 0.97, 0.979                   
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14892                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 72                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA CITRATE PH 5.6,                 
REMARK 280  20% ISOPROPANOL, 10% PEG 4000                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.39000            
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       50.78000            
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       50.78000            
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       25.39000            
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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.6 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     MET A    -1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY A   1   N     GLY A   1   CA      0.113                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 B  55   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
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 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    LYS B  30       -7.79   -142.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401                 
DBREF  1E44 A   -1    84  UNP    P02984   IMM3_ECOLI       1     85             
DBREF  1E44 B    1    96  UNP    P00646   CEA3_ECOLI     456    551             
SEQRES   1 A   85  MET GLY LEU LYS LEU ASP LEU THR TRP PHE ASP LYS SER          
SEQRES   2 A   85  THR GLU ASP PHE LYS GLY GLU GLU TYR SER LYS ASP PHE          
SEQRES   3 A   85  GLY ASP ASP GLY SER VAL MET GLU SER LEU GLY VAL PRO          
SEQRES   4 A   85  PHE LYS ASP ASN VAL ASN ASN GLY CYS PHE ASP VAL ILE          
SEQRES   5 A   85  ALA GLU TRP VAL PRO LEU LEU GLN PRO TYR PHE ASN HIS          
SEQRES   6 A   85  GLN ILE ASP ILE SER ASP ASN GLU TYR PHE VAL SER PHE          
SEQRES   7 A   85  ASP TYR ARG ASP GLY ASP TRP                                  
SEQRES   1 B   96  GLY PHE LYS ASP TYR GLY HIS ASP TYR HIS PRO ALA PRO          
SEQRES   2 B   96  LYS THR GLU ASN ILE LYS GLY LEU GLY ASP LEU LYS PRO          
SEQRES   3 B   96  GLY ILE PRO LYS THR PRO LYS GLN ASN GLY GLY GLY LYS          
SEQRES   4 B   96  ARG LYS ARG TRP THR GLY ASP LYS GLY ARG LYS ILE TYR          
SEQRES   5 B   96  GLU TRP ASP SER GLN HIS GLY GLU LEU GLU GLY TYR ARG          
SEQRES   6 B   96  ALA SER ASP GLY GLN HIS LEU GLY SER PHE ASP PRO LYS          
SEQRES   7 B   96  THR GLY ASN GLN LEU LYS GLY PRO ASP PRO LYS ARG ASN          
SEQRES   8 B   96  ILE LYS LYS TYR LEU                                          
HET    EDO  B 401       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    C2 H6 O2                                                     
FORMUL   4  HOH   *171(H2 O1)                                                   
HELIX    1   1 GLY A   29  GLY A   36  1                                   8    
HELIX    2   2 GLU A   53  GLN A   59  1                                   7    
HELIX    3   3 PRO A   60  PHE A   62  5                                   3    
HELIX    4   4 GLY B    1  HIS B    7  1                                   7    
HELIX    5   5 LYS B   14  ILE B   18  5                                   5    
HELIX    6   6 ILE B   92  LEU B   96  5                                   5    
SHEET    1   A 4 CYS A  47  ASP A  49  0                                        
SHEET    2   A 4 ASN A  71  TYR A  79 -1  N  VAL A  75   O  PHE A  48           
SHEET    3   A 4 LEU A   2  ASP A  10 -1  N  PHE A   9   O  GLU A  72           
SHEET    4   A 4 PHE A  16  TYR A  21 -1  N  GLU A  20   O  LEU A   6           
SHEET    1   B 4 LEU B  24  PRO B  26  0                                        
SHEET    2   B 4 ARG B  42  GLY B  45 -1  N  THR B  44   O  LYS B  25           
SHEET    3   B 4 LYS B  50  ASP B  55 -1  N  TYR B  52   O  TRP B  43           
SHEET    4   B 4 GLU B  60  ARG B  65 -1  N  TYR B  64   O  ILE B  51           
SITE     1 AC1  7 ASP A   5  GLU A  19  THR B  15  TRP B  43                    
SITE     2 AC1  7 HOH B2038  HOH B2054  HOH B2087                               
CRYST1   93.700   93.700   76.170  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010672  0.006162  0.000000        0.00000                         
SCALE2      0.000000  0.012323  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013128        0.00000                         
ATOM      1  N   GLY A   1      19.340  29.204  13.062  1.00 41.81           N  
ATOM      2  CA  GLY A   1      19.519  27.659  12.859  1.00 39.92           C  
ATOM      3  C   GLY A   1      20.740  27.261  12.024  1.00 39.14           C  
ATOM      4  O   GLY A   1      21.696  28.013  11.868  1.00 42.23           O  
ATOM      5  N   LEU A   2      20.704  26.058  11.489  1.00 41.02           N  
ATOM      6  CA  LEU A   2      21.744  25.540  10.621  1.00 40.64           C  
ATOM      7  C   LEU A   2      21.631  26.112   9.209  1.00 49.93           C  
ATOM      8  O   LEU A   2      20.542  26.023   8.592  1.00 54.86           O  
ATOM      9  CB  LEU A   2      21.566  24.035  10.539  1.00 38.24           C  
ATOM     10  CG  LEU A   2      22.298  23.411   9.401  1.00 41.94           C  
ATOM     11  CD1 LEU A   2      23.867  23.473   9.717  1.00 41.00           C  
ATOM     12  CD2 LEU A   2      21.749  21.959   9.273  1.00 38.27           C  
ATOM     13  N   LYS A   3      22.723  26.699   8.700  1.00 43.52           N  
ATOM     14  CA  LYS A   3      22.864  26.977   7.258  1.00 38.45           C  
ATOM     15  C   LYS A   3      24.062  26.200   6.677  1.00 42.57           C  
ATOM     16  O   LYS A   3      25.131  26.158   7.304  1.00 45.78           O  
ATOM     17  CB  LYS A   3      23.053  28.473   7.022  1.00 38.19           C  
ATOM     18  CG  LYS A   3      21.796  29.342   7.357  1.00 45.93           C  
ATOM     19  CD  LYS A   3      22.017  30.836   7.035  1.00 49.71           C  
ATOM     20  CE  LYS A   3      20.779  31.695   7.279  1.00 50.15           C  
ATOM     21  NZ  LYS A   3      20.361  31.689   8.712  1.00 56.62           N  
ATOM     22  N   LEU A   4      23.884  25.563   5.514  1.00 38.57           N  
ATOM     23  CA  LEU A   4      25.005  25.090   4.709  1.00 39.20           C  
ATOM     24  C   LEU A   4      25.770  26.276   4.114  1.00 43.88           C  
ATOM     25  O   LEU A   4      25.181  27.088   3.417  1.00 46.71           O  
ATOM     26  CB  LEU A   4      24.491  24.251   3.585  1.00 39.83           C  
ATOM     27  CG  LEU A   4      23.678  23.048   4.051  1.00 50.43           C  
ATOM     28  CD1 LEU A   4      23.870  21.886   3.104  1.00 50.17           C  
ATOM     29  CD2 LEU A   4      24.149  22.589   5.364  1.00 42.07           C  
ATOM     30  N   ASP A   5      27.064  26.410   4.410  1.00 42.05           N  
ATOM     31  CA  ASP A   5      27.840  27.513   3.853  1.00 36.29           C  
ATOM     32  C   ASP A   5      28.702  27.012   2.686  1.00 42.85           C  
ATOM     33  O   ASP A   5      29.656  26.264   2.880  1.00 46.38           O  
ATOM     34  CB  ASP A   5      28.678  28.111   4.955  1.00 39.89           C  
ATOM     35  CG  ASP A   5      29.508  29.285   4.489  1.00 47.17           C  
ATOM     36  OD1 ASP A   5      29.333  29.720   3.342  1.00 44.74           O  
ATOM     37  OD2 ASP A   5      30.346  29.780   5.285  1.00 41.58           O  
ATOM     38  N   LEU A   6      28.319  27.364   1.461  1.00 43.78           N  
ATOM     39  CA  LEU A   6      28.941  26.787   0.280  1.00 35.66           C  
ATOM     40  C   LEU A   6      29.946  27.717  -0.307  1.00 40.61           C  
ATOM     41  O   LEU A   6      29.683  28.879  -0.457  1.00 47.15           O  
ATOM     42  CB  LEU A   6      27.929  26.448  -0.794  1.00 36.60           C  
ATOM     43  CG  LEU A   6      28.495  25.763  -2.069  1.00 42.72           C  
ATOM     44  CD1 LEU A   6      28.881  24.306  -1.909  1.00 37.36           C  
ATOM     45  CD2 LEU A   6      27.397  25.836  -3.152  1.00 34.39           C  
ATOM     46  N   THR A   7      31.099  27.192  -0.696  1.00 39.85           N  
ATOM     47  CA  THR A   7      32.187  28.067  -1.060  1.00 29.71           C  
ATOM     48  C   THR A   7      32.911  27.397  -2.249  1.00 39.36           C  
ATOM     49  O   THR A   7      32.973  26.175  -2.326  1.00 43.06           O  
ATOM     50  CB  THR A   7      32.934  28.266   0.261  1.00 44.09           C  
ATOM     51  OG1 THR A   7      33.098  29.654   0.516  1.00 44.17           O  
ATOM     52  CG2 THR A   7      34.141  27.450   0.389  1.00 29.39           C  
ATOM     53  N   TRP A   8      33.368  28.158  -3.243  1.00 38.11           N  
ATOM     54  CA  TRP A   8      34.024  27.557  -4.393  1.00 39.53           C  
ATOM     55  C   TRP A   8      35.172  28.373  -5.035  1.00 39.26           C  
ATOM     56  O   TRP A   8      35.292  29.562  -4.836  1.00 39.31           O  
ATOM     57  CB  TRP A   8      32.986  27.124  -5.449  1.00 32.48           C  
ATOM     58  CG  TRP A   8      32.215  28.219  -6.066  1.00 43.18           C  
ATOM     59  CD1 TRP A   8      32.487  28.842  -7.239  1.00 45.40           C  
ATOM     60  CD2 TRP A   8      30.987  28.774  -5.596  1.00 46.90           C  
ATOM     61  NE1 TRP A   8      31.497  29.748  -7.548  1.00 47.64           N  
ATOM     62  CE2 TRP A   8      30.561  29.729  -6.554  1.00 49.77           C  
ATOM     63  CE3 TRP A   8      30.193  28.560  -4.462  1.00 42.84           C  
ATOM     64  CZ2 TRP A   8      29.379  30.466  -6.407  1.00 43.02           C  
ATOM     65  CZ3 TRP A   8      29.033  29.303  -4.322  1.00 41.08           C  
ATOM     66  CH2 TRP A   8      28.636  30.236  -5.287  1.00 38.95           C  
ATOM     67  N   PHE A   9      36.070  27.676  -5.731  1.00 40.64           N  
ATOM     68  CA  PHE A   9      37.404  28.205  -6.012  1.00 35.47           C  
ATOM     69  C   PHE A   9      37.869  27.674  -7.342  1.00 37.21           C  
ATOM     70  O   PHE A   9      37.455  26.587  -7.752  1.00 43.40           O  
ATOM     71  CB  PHE A   9      38.385  27.785  -4.945  1.00 29.48           C  
ATOM     72  CG  PHE A   9      37.965  28.174  -3.567  1.00 30.30           C  
ATOM     73  CD1 PHE A   9      37.058  27.401  -2.862  1.00 38.80           C  
ATOM     74  CD2 PHE A   9      38.507  29.304  -2.941  1.00 30.25           C  
ATOM     75  CE1 PHE A   9      36.702  27.736  -1.559  1.00 31.07           C  
ATOM     76  CE2 PHE A   9      38.156  29.663  -1.620  1.00 33.61           C  
ATOM     77  CZ  PHE A   9      37.253  28.876  -0.930  1.00 41.20           C  
ATOM     78  N   ASP A  10      38.667  28.465  -8.036  1.00 33.56           N  
ATOM     79  CA  ASP A  10      39.106  28.121  -9.355  1.00 35.01           C  
ATOM     80  C   ASP A  10      40.120  26.952  -9.297  1.00 39.06           C  
ATOM     81  O   ASP A  10      41.160  27.072  -8.642  1.00 37.70           O  
ATOM     82  CB  ASP A  10      39.796  29.315  -9.948  1.00 41.23           C  
ATOM     83  CG  ASP A  10      40.109  29.131 -11.410  1.00 47.73           C  
ATOM     84  OD1 ASP A  10      41.177  28.536 -11.720  1.00 49.33           O  
ATOM     85  OD2 ASP A  10      39.263  29.582 -12.238  1.00 65.88           O  
ATOM     86  N   LYS A  11      39.839  25.858  -9.979  1.00 37.18           N  
ATOM     87  CA  LYS A  11      40.772  24.736  -9.961  1.00 41.96           C  
ATOM     88  C   LYS A  11      42.177  25.108 -10.453  1.00 43.44           C  
ATOM     89  O   LYS A  11      43.174  24.528  -9.993  1.00 40.92           O  
ATOM     90  CB  LYS A  11      40.225  23.582 -10.804  1.00 47.59           C  
ATOM     91  CG  LYS A  11      39.165  22.727 -10.124  1.00 46.96           C  
ATOM     92  CD  LYS A  11      38.902  21.594 -11.070  1.00 50.46           C  
ATOM     93  CE  LYS A  11      37.912  20.618 -10.551  1.00 52.89           C  
ATOM     94  NZ  LYS A  11      37.601  19.631 -11.609  1.00 52.76           N  
ATOM     95  N   SER A  12      42.265  26.071 -11.376  1.00 43.08           N  
ATOM     96  CA  SER A  12      43.558  26.453 -11.968  1.00 40.31           C  
ATOM     97  C   SER A  12      44.369  27.344 -11.096  1.00 45.64           C  
ATOM     98  O   SER A  12      45.575  27.233 -11.107  1.00 48.20           O  
ATOM     99  CB  SER A  12      43.364  27.180 -13.272  1.00 42.40           C  
ATOM    100  OG  SER A  12      42.606  26.369 -14.131  1.00 58.68           O  
ATOM    101  N   THR A  13      43.736  28.259 -10.355  1.00 40.02           N  
ATOM    102  CA  THR A  13      44.523  29.306  -9.686  1.00 38.19           C  
ATOM    103  C   THR A  13      44.283  29.195  -8.214  1.00 42.92           C  
ATOM    104  O   THR A  13      44.961  29.834  -7.420  1.00 45.06           O  
ATOM    105  CB  THR A  13      44.100  30.803 -10.101  1.00 41.91           C  
ATOM    106  OG1 THR A  13      42.676  30.995  -9.858  1.00 39.78           O  
ATOM    107  CG2 THR A  13      44.476  31.116 -11.596  1.00 32.22           C  
ATOM    108  N   GLU A  14      43.272  28.414  -7.849  1.00 44.17           N  
ATOM    109  CA  GLU A  14      42.737  28.460  -6.498  1.00 43.52           C  
ATOM    110  C   GLU A  14      42.079  29.797  -6.077  1.00 43.31           C  
ATOM    111  O   GLU A  14      41.686  29.937  -4.920  1.00 42.68           O  
ATOM    112  CB  GLU A  14      43.833  28.066  -5.477  1.00 43.51           C  
ATOM    113  CG  GLU A  14      44.454  26.695  -5.735  1.00 43.90           C  
ATOM    114  CD  GLU A  14      45.346  26.217  -4.561  1.00 52.47           C  
ATOM    115  OE1 GLU A  14      46.213  26.980  -4.099  1.00 52.72           O  
ATOM    116  OE2 GLU A  14      45.182  25.067  -4.090  1.00 55.75           O  
ATOM    117  N   ASP A  15      41.918  30.769  -6.982  1.00 38.79           N  
ATOM    118  CA  ASP A  15      41.195  32.004  -6.578  1.00 35.97           C  
ATOM    119  C   ASP A  15      39.766  31.695  -6.135  1.00 37.20           C  
ATOM    120  O   ASP A  15      39.069  30.837  -6.710  1.00 31.69           O  
ATOM    121  CB  ASP A  15      41.061  32.999  -7.737  1.00 40.01           C  
ATOM    122  CG  ASP A  15      42.387  33.607  -8.161  1.00 41.86           C  
ATOM    123  OD1 ASP A  15      43.399  33.534  -7.394  1.00 39.00           O  
ATOM    124  OD2 ASP A  15      42.406  34.190  -9.287  1.00 50.43           O  
ATOM    125  N   PHE A  16      39.335  32.431  -5.129  1.00 32.90           N  
ATOM    126  CA  PHE A  16      37.942  32.448  -4.660  1.00 39.73           C  
ATOM    127  C   PHE A  16      37.003  32.925  -5.771  1.00 42.93           C  
ATOM    128  O   PHE A  16      37.261  33.932  -6.402  1.00 43.09           O  
ATOM    129  CB  PHE A  16      37.833  33.397  -3.449  1.00 35.72           C  
ATOM    130  CG  PHE A  16      36.429  33.694  -3.049  1.00 36.46           C  
ATOM    131  CD1 PHE A  16      35.620  32.694  -2.506  1.00 37.05           C  
ATOM    132  CD2 PHE A  16      35.895  34.986  -3.207  1.00 46.31           C  
ATOM    133  CE1 PHE A  16      34.272  32.976  -2.113  1.00 50.78           C  
ATOM    134  CE2 PHE A  16      34.578  35.290  -2.823  1.00 38.13           C  
ATOM    135  CZ  PHE A  16      33.749  34.303  -2.277  1.00 38.16           C  
ATOM    136  N   LYS A  17      35.926  32.202  -6.026  1.00 38.11           N  
ATOM    137  CA  LYS A  17      34.967  32.719  -6.964  1.00 44.53           C  
ATOM    138  C   LYS A  17      33.540  32.838  -6.457  1.00 42.73           C  
ATOM    139  O   LYS A  17      32.713  33.259  -7.197  1.00 50.14           O  
ATOM    140  CB  LYS A  17      34.893  31.902  -8.263  1.00 49.52           C  
ATOM    141  CG  LYS A  17      35.942  30.865  -8.530  1.00 53.74           C  
ATOM    142  CD  LYS A  17      36.091  30.578 -10.076  1.00 60.70           C  
ATOM    143  CE  LYS A  17      34.730  30.239 -10.755  1.00 59.07           C  
ATOM    144  NZ  LYS A  17      34.816  29.607 -12.098  1.00 57.48           N  
ATOM    145  N   GLY A  18      33.226  32.457  -5.236  1.00 42.12           N  
ATOM    146  CA  GLY A  18      31.846  32.518  -4.843  1.00 42.59           C  
ATOM    147  C   GLY A  18      31.587  31.834  -3.551  1.00 48.12           C  
ATOM    148  O   GLY A  18      32.281  30.878  -3.150  1.00 47.14           O  
ATOM    149  N   GLU A  19      30.537  32.332  -2.908  1.00 55.67           N  
ATOM    150  CA  GLU A  19      30.027  31.838  -1.614  1.00 48.96           C  
ATOM    151  C   GLU A  19      28.527  31.965  -1.673  1.00 45.20           C  
ATOM    152  O   GLU A  19      28.049  32.950  -2.169  1.00 52.25           O  
ATOM    153  CB  GLU A  19      30.582  32.679  -0.466  1.00 40.52           C  
ATOM    154  CG  GLU A  19      29.920  32.327   0.839  1.00 34.48           C  
ATOM    155  CD  GLU A  19      30.775  32.745   2.009  1.00 43.68           C  
ATOM    156  OE1 GLU A  19      31.381  33.876   1.923  1.00 55.13           O  
ATOM    157  OE2 GLU A  19      30.839  31.963   3.014  1.00 42.85           O  
ATOM    158  N   GLU A  20      27.800  30.938  -1.238  1.00 49.67           N  
ATOM    159  CA  GLU A  20      26.348  30.976  -1.066  1.00 49.20           C  
ATOM    160  C   GLU A  20      25.877  30.179   0.184  1.00 48.53           C  
ATOM    161  O   GLU A  20      26.365  29.069   0.472  1.00 45.56           O  
ATOM    162  CB  GLU A  20      25.653  30.419  -2.311  1.00 49.77           C  
ATOM    163  CG  GLU A  20      24.102  30.475  -2.278  1.00 46.00           C  
ATOM    164  CD  GLU A  20      23.415  29.905  -3.562  1.00 59.25           C  
ATOM    165  OE1 GLU A  20      24.037  29.859  -4.647  1.00 59.40           O  
ATOM    166  OE2 GLU A  20      22.232  29.518  -3.511  1.00 52.13           O  
ATOM    167  N   TYR A  21      24.927  30.758   0.924  1.00 45.64           N  
ATOM    168  CA  TYR A  21      24.325  30.061   2.064  1.00 43.22           C  
ATOM    169  C   TYR A  21      23.025  29.481   1.663  1.00 41.39           C  
ATOM    170  O   TYR A  21      22.303  30.087   0.898  1.00 43.84           O  
ATOM    171  CB  TYR A  21      24.062  30.988   3.224  1.00 33.96           C  
ATOM    172  CG  TYR A  21      25.322  31.456   3.935  1.00 43.56           C  
ATOM    173  CD1 TYR A  21      26.016  32.549   3.475  1.00 43.76           C  
ATOM    174  CD2 TYR A  21      25.820  30.789   5.077  1.00 30.70           C  
ATOM    175  CE1 TYR A  21      27.182  32.994   4.115  1.00 43.10           C  
ATOM    176  CE2 TYR A  21      26.962  31.218   5.709  1.00 33.59           C  
ATOM    177  CZ  TYR A  21      27.656  32.326   5.226  1.00 38.59           C  
ATOM    178  OH  TYR A  21      28.817  32.788   5.836  1.00 39.79           O  
ATOM    179  N   SER A  22      22.721  28.299   2.173  1.00 41.94           N  
ATOM    180  CA  SER A  22      21.401  27.755   1.989  1.00 41.91           C  
ATOM    181  C   SER A  22      20.470  28.571   2.877  1.00 48.13           C  
ATOM    182  O   SER A  22      20.908  29.337   3.736  1.00 47.08           O  
ATOM    183  CB  SER A  22      21.341  26.311   2.452  1.00 40.73           C  
ATOM    184  OG  SER A  22      21.486  26.261   3.879  1.00 40.66           O  
ATOM    185  N   LYS A  23      19.175  28.369   2.692  1.00 46.56           N  
ATOM    186  CA  LYS A  23      18.244  28.835   3.698  1.00 48.71           C  
ATOM    187  C   LYS A  23      18.494  28.123   5.029  1.00 45.91           C  
ATOM    188  O   LYS A  23      19.064  27.034   5.086  1.00 45.64           O  
ATOM    189  CB  LYS A  23      16.777  28.606   3.232  1.00 51.06           C  
ATOM    190  CG  LYS A  23      16.312  29.495   2.022  1.00 41.61           C  
ATOM    191  CD  LYS A  23      16.791  30.954   2.119  1.00 36.04           C  
ATOM    192  CE  LYS A  23      16.098  31.865   1.064  1.00 41.16           C  
ATOM    193  NZ  LYS A  23      16.590  33.288   1.148  1.00 41.72           N  
ATOM    194  N   ASP A  24      18.029  28.754   6.097  1.00 47.40           N  
ATOM    195  CA  ASP A  24      18.036  28.163   7.428  1.00 52.29           C  
ATOM    196  C   ASP A  24      17.188  26.899   7.599  1.00 51.41           C  
ATOM    197  O   ASP A  24      16.007  26.892   7.269  1.00 62.20           O  
ATOM    198  CB  ASP A  24      17.637  29.199   8.456  1.00 49.52           C  
ATOM    199  CG  ASP A  24      18.249  28.910   9.825  1.00 59.43           C  
ATOM    200  OD1 ASP A  24      17.852  27.882  10.449  1.00 53.21           O  
ATOM    201  OD2 ASP A  24      19.116  29.708  10.250  1.00 52.14           O  
ATOM    202  N   PHE A  25      17.824  25.809   8.051  1.00 52.26           N  
ATOM    203  CA  PHE A  25      17.159  24.570   8.405  1.00 44.11           C  
ATOM    204  C   PHE A  25      16.648  24.510   9.860  1.00 49.11           C  
ATOM    205  O   PHE A  25      16.292  23.434  10.305  1.00 49.95           O  
ATOM    206  CB  PHE A  25      18.116  23.406   8.248  1.00 49.14           C  
ATOM    207  CG  PHE A  25      18.463  23.086   6.836  1.00 56.18           C  
ATOM    208  CD1 PHE A  25      19.470  23.801   6.176  1.00 53.40           C  
ATOM    209  CD2 PHE A  25      17.789  22.038   6.162  1.00 47.86           C  
ATOM    210  CE1 PHE A  25      19.818  23.473   4.840  1.00 50.25           C  
ATOM    211  CE2 PHE A  25      18.115  21.706   4.857  1.00 46.41           C  
ATOM    212  CZ  PHE A  25      19.143  22.430   4.189  1.00 54.04           C  
ATOM    213  N   GLY A  26      16.644  25.615  10.614  1.00 45.77           N  
ATOM    214  CA  GLY A  26      16.280  25.524  12.021  1.00 54.57           C  
ATOM    215  C   GLY A  26      17.197  24.540  12.737  1.00 58.38           C  
ATOM    216  O   GLY A  26      18.427  24.717  12.749  1.00 56.43           O  
ATOM    217  N   ASP A  27      16.593  23.491  13.286  1.00 53.43           N  
ATOM    218  CA  ASP A  27      17.276  22.525  14.113  1.00 50.66           C  
ATOM    219  C   ASP A  27      17.165  21.179  13.540  1.00 52.84           C  
ATOM    220  O   ASP A  27      17.264  20.199  14.275  1.00 54.08           O  
ATOM    221  CB  ASP A  27      16.667  22.438  15.495  1.00 51.05           C  
ATOM    222  CG  ASP A  27      17.034  23.606  16.331  1.00 59.42           C  
ATOM    223  OD1 ASP A  27      17.864  24.415  15.859  1.00 59.42           O  
ATOM    224  OD2 ASP A  27      16.498  23.715  17.453  1.00 62.24           O  
ATOM    225  N   ASP A  28      16.910  21.112  12.245  1.00 53.70           N  
ATOM    226  CA  ASP A  28      16.814  19.827  11.585  1.00 55.57           C  
ATOM    227  C   ASP A  28      18.149  19.555  10.925  1.00 54.69           C  
ATOM    228  O   ASP A  28      18.484  20.173   9.905  1.00 58.29           O  
ATOM    229  CB  ASP A  28      15.687  19.846  10.542  1.00 49.95           C  
ATOM    230  CG  ASP A  28      15.562  18.526   9.775  1.00 62.47           C  
ATOM    231  OD1 ASP A  28      16.334  17.564  10.059  1.00 67.58           O  
ATOM    232  OD2 ASP A  28      14.694  18.441   8.870  1.00 70.90           O  
ATOM    233  N   GLY A  29      18.897  18.616  11.494  1.00 55.17           N  
ATOM    234  CA  GLY A  29      20.176  18.216  10.918  1.00 49.64           C  
ATOM    235  C   GLY A  29      20.189  17.148   9.825  1.00 56.94           C  
ATOM    236  O   GLY A  29      21.253  16.872   9.213  1.00 54.51           O  
ATOM    237  N   SER A  30      19.031  16.555   9.524  1.00 60.82           N  
ATOM    238  CA  SER A  30      19.002  15.415   8.584  1.00 57.96           C  
ATOM    239  C   SER A  30      19.716  15.660   7.240  1.00 58.06           C  
ATOM    240  O   SER A  30      20.268  14.713   6.658  1.00 57.35           O  
ATOM    241  CB  SER A  30      17.553  14.946   8.353  1.00 66.04           C  
ATOM    242  OG  SER A  30      16.688  16.038   8.089  1.00 64.96           O  
ATOM    243  N   VAL A  31      19.763  16.904   6.744  1.00 52.18           N  
ATOM    244  CA  VAL A  31      20.597  17.151   5.563  1.00 53.66           C  
ATOM    245  C   VAL A  31      22.055  16.678   5.799  1.00 55.67           C  
ATOM    246  O   VAL A  31      22.657  16.017   4.931  1.00 51.16           O  
ATOM    247  CB  VAL A  31      20.544  18.648   5.110  1.00 54.95           C  
ATOM    248  CG1 VAL A  31      21.104  19.561   6.127  1.00 54.42           C  
ATOM    249  CG2 VAL A  31      21.244  18.799   3.785  1.00 48.75           C  
ATOM    250  N   MET A  32      22.595  16.953   6.992  1.00 51.68           N  
ATOM    251  CA  MET A  32      23.896  16.387   7.351  1.00 48.40           C  
ATOM    252  C   MET A  32      23.836  14.873   7.352  1.00 52.95           C  
ATOM    253  O   MET A  32      24.752  14.207   6.854  1.00 57.51           O  
ATOM    254  CB  MET A  32      24.364  16.869   8.736  1.00 51.93           C  
ATOM    255  CG  MET A  32      24.656  18.345   8.798  1.00 40.50           C  
ATOM    256  SD  MET A  32      25.548  18.800  10.341  1.00 52.05           S  
ATOM    257  CE  MET A  32      27.036  17.635  10.264  1.00 42.41           C  
ATOM    258  N   GLU A  33      22.774  14.313   7.924  1.00 55.96           N  
ATOM    259  CA  GLU A  33      22.590  12.859   7.866  1.00 61.07           C  
ATOM    260  C   GLU A  33      22.701  12.343   6.417  1.00 63.13           C  
ATOM    261  O   GLU A  33      23.358  11.322   6.180  1.00 67.23           O  
ATOM    262  CB  GLU A  33      21.228  12.440   8.457  1.00 69.08           C  
ATOM    263  CG  GLU A  33      21.204  12.217   9.986  1.00 80.76           C  
ATOM    264  CD  GLU A  33      19.770  12.078  10.581  1.00 83.25           C  
ATOM    265  OE1 GLU A  33      18.996  11.202  10.085  1.00 89.11           O  
ATOM    266  OE2 GLU A  33      19.438  12.839  11.550  1.00 76.66           O  
ATOM    267  N   SER A  34      22.086  13.028   5.451  1.00 57.17           N  
ATOM    268  CA  SER A  34      22.089  12.529   4.059  1.00 60.47           C  
ATOM    269  C   SER A  34      23.417  12.701   3.351  1.00 61.90           C  
ATOM    270  O   SER A  34      23.709  12.003   2.359  1.00 65.99           O  
ATOM    271  CB  SER A  34      21.004  13.213   3.212  1.00 61.89           C  
ATOM    272  OG  SER A  34      21.304  14.574   2.915  1.00 63.23           O  
ATOM    273  N   LEU A  35      24.233  13.633   3.849  1.00 61.21           N  
ATOM    274  CA  LEU A  35      25.611  13.720   3.373  1.00 55.89           C  
ATOM    275  C   LEU A  35      26.500  12.629   3.974  1.00 53.00           C  
ATOM    276  O   LEU A  35      27.555  12.305   3.428  1.00 57.22           O  
ATOM    277  CB  LEU A  35      26.157  15.098   3.693  1.00 49.73           C  
ATOM    278  CG  LEU A  35      25.279  16.032   2.897  1.00 49.46           C  
ATOM    279  CD1 LEU A  35      25.535  17.431   3.328  1.00 41.56           C  
ATOM    280  CD2 LEU A  35      25.554  15.790   1.417  1.00 44.13           C  
ATOM    281  N   GLY A  36      26.059  12.044   5.086  1.00 51.69           N  
ATOM    282  CA  GLY A  36      26.874  11.035   5.751  1.00 52.31           C  
ATOM    283  C   GLY A  36      27.894  11.711   6.665  1.00 58.70           C  
ATOM    284  O   GLY A  36      29.011  11.210   6.846  1.00 62.20           O  
ATOM    285  N   VAL A  37      27.506  12.861   7.225  1.00 54.71           N  
ATOM    286  CA  VAL A  37      28.371  13.632   8.088  1.00 46.54           C  
ATOM    287  C   VAL A  37      27.756  13.605   9.443  1.00 41.40           C  
ATOM    288  O   VAL A  37      26.718  14.186   9.669  1.00 46.74           O  
ATOM    289  CB  VAL A  37      28.525  15.123   7.591  1.00 52.83           C  
ATOM    290  CG1 VAL A  37      29.436  15.900   8.510  1.00 43.92           C  
ATOM    291  CG2 VAL A  37      29.148  15.143   6.182  1.00 47.69           C  
ATOM    292  N   PRO A  38      28.392  12.892  10.374  1.00 44.03           N  
ATOM    293  CA  PRO A  38      27.907  12.770  11.770  1.00 46.64           C  
ATOM    294  C   PRO A  38      27.833  14.184  12.283  1.00 51.01           C  
ATOM    295  O   PRO A  38      28.598  15.038  11.821  1.00 52.49           O  
ATOM    296  CB  PRO A  38      29.021  12.007  12.491  1.00 41.47           C  
ATOM    297  CG  PRO A  38      29.790  11.292  11.322  1.00 47.11           C  
ATOM    298  CD  PRO A  38      29.724  12.290  10.177  1.00 41.68           C  
ATOM    299  N   PHE A  39      26.951  14.433  13.237  1.00 56.40           N  
ATOM    300  CA  PHE A  39      26.911  15.739  13.908  1.00 55.43           C  
ATOM    301  C   PHE A  39      28.134  16.026  14.754  1.00 56.10           C  
ATOM    302  O   PHE A  39      28.614  17.159  14.810  1.00 52.10           O  
ATOM    303  CB  PHE A  39      25.713  15.824  14.833  1.00 58.74           C  
ATOM    304  CG  PHE A  39      24.416  15.784  14.131  1.00 61.96           C  
ATOM    305  CD1 PHE A  39      24.360  16.005  12.771  1.00 49.22           C  
ATOM    306  CD2 PHE A  39      23.235  15.480  14.832  1.00 67.16           C  
ATOM    307  CE1 PHE A  39      23.170  15.923  12.096  1.00 57.73           C  
ATOM    308  CE2 PHE A  39      22.007  15.395  14.165  1.00 61.70           C  
ATOM    309  CZ  PHE A  39      21.972  15.614  12.794  1.00 65.86           C  
ATOM    310  N   LYS A  40      28.585  15.003  15.478  1.00 58.87           N  
ATOM    311  CA  LYS A  40      29.685  15.154  16.440  1.00 54.47           C  
ATOM    312  C   LYS A  40      30.921  15.865  15.850  1.00 50.94           C  
ATOM    313  O   LYS A  40      31.532  15.366  14.894  1.00 45.06           O  
ATOM    314  CB  LYS A  40      30.117  13.777  16.940  1.00 52.99           C  
ATOM    315  CG  LYS A  40      31.197  13.790  18.011  1.00 54.09           C  
ATOM    316  CD  LYS A  40      31.811  12.389  18.098  1.00 59.60           C  
ATOM    317  CE  LYS A  40      32.828  12.273  19.241  1.00 61.08           C  
ATOM    318  NZ  LYS A  40      32.180  12.582  20.578  1.00 68.95           N  
ATOM    319  N   ASP A  41      31.277  17.009  16.429  1.00 47.12           N  
ATOM    320  CA  ASP A  41      32.546  17.701  16.137  1.00 50.60           C  
ATOM    321  C   ASP A  41      32.563  18.280  14.712  1.00 46.66           C  
ATOM    322  O   ASP A  41      33.639  18.520  14.153  1.00 46.86           O  
ATOM    323  CB  ASP A  41      33.733  16.718  16.274  1.00 51.09           C  
ATOM    324  CG  ASP A  41      34.120  16.435  17.746  1.00 51.04           C  
ATOM    325  OD1 ASP A  41      33.798  17.264  18.628  1.00 39.59           O  
ATOM    326  OD2 ASP A  41      34.754  15.370  17.990  1.00 48.20           O  
ATOM    327  N   ASN A  42      31.374  18.437  14.118  1.00 41.69           N  
ATOM    328  CA  ASN A  42      31.296  18.825  12.747  1.00 36.80           C  
ATOM    329  C   ASN A  42      30.451  20.038  12.547  1.00 35.23           C  
ATOM    330  O   ASN A  42      30.359  20.520  11.432  1.00 40.15           O  
ATOM    331  CB  ASN A  42      30.769  17.699  11.899  1.00 39.21           C  
ATOM    332  CG  ASN A  42      31.774  16.583  11.735  1.00 48.02           C  
ATOM    333  OD1 ASN A  42      33.001  16.830  11.794  1.00 48.05           O  
ATOM    334  ND2 ASN A  42      31.275  15.330  11.512  1.00 43.91           N  
ATOM    335  N   VAL A  43      29.834  20.543  13.600  1.00 32.81           N  
ATOM    336  CA  VAL A  43      28.985  21.732  13.437  1.00 35.47           C  
ATOM    337  C   VAL A  43      29.712  22.960  14.007  1.00 36.05           C  
ATOM    338  O   VAL A  43      30.158  22.938  15.155  1.00 35.52           O  
ATOM    339  CB  VAL A  43      27.613  21.557  14.163  1.00 37.79           C  
ATOM    340  CG1 VAL A  43      26.726  22.756  13.920  1.00 31.22           C  
ATOM    341  CG2 VAL A  43      26.930  20.202  13.670  1.00 32.46           C  
ATOM    342  N   ASN A  44      29.793  24.026  13.200  1.00 38.33           N  
ATOM    343  CA  ASN A  44      30.712  25.137  13.415  1.00 38.35           C  
ATOM    344  C   ASN A  44      32.150  24.588  13.578  1.00 36.89           C  
ATOM    345  O   ASN A  44      32.837  24.938  14.504  1.00 38.46           O  
ATOM    346  CB  ASN A  44      30.300  25.941  14.661  1.00 27.69           C  
ATOM    347  CG  ASN A  44      28.961  26.648  14.477  1.00 40.40           C  
ATOM    348  OD1 ASN A  44      28.655  27.155  13.412  1.00 40.95           O  
ATOM    349  ND2 ASN A  44      28.166  26.707  15.530  1.00 40.40           N  
ATOM    350  N   ASN A  45      32.613  23.728  12.686  1.00 40.11           N  
ATOM    351  CA  ASN A  45      33.958  23.197  12.891  1.00 42.36           C  
ATOM    352  C   ASN A  45      34.601  22.772  11.593  1.00 41.84           C  
ATOM    353  O   ASN A  45      35.099  21.650  11.466  1.00 44.46           O  
ATOM    354  CB  ASN A  45      33.906  22.012  13.875  1.00 45.52           C  
ATOM    355  CG  ASN A  45      35.246  21.771  14.528  1.00 55.40           C  
ATOM    356  OD1 ASN A  45      36.006  22.747  14.749  1.00 47.31           O  
ATOM    357  ND2 ASN A  45      35.561  20.501  14.851  1.00 43.60           N  
ATOM    358  N   GLY A  46      34.554  23.654  10.593  1.00 41.30           N  
ATOM    359  CA  GLY A  46      35.284  23.347   9.387  1.00 43.28           C  
ATOM    360  C   GLY A  46      34.467  23.023   8.164  1.00 37.92           C  
ATOM    361  O   GLY A  46      33.256  22.931   8.224  1.00 38.35           O  
ATOM    362  N   CYS A  47      35.170  22.844   7.053  1.00 36.02           N  
ATOM    363  CA  CYS A  47      34.562  22.755   5.755  1.00 36.27           C  
ATOM    364  C   CYS A  47      34.950  21.383   5.222  1.00 40.67           C  
ATOM    365  O   CYS A  47      36.057  20.857   5.519  1.00 38.22           O  
ATOM    366  CB  CYS A  47      35.133  23.834   4.846  1.00 41.48           C  
ATOM    367  SG  CYS A  47      34.858  25.553   5.397  1.00 43.85           S  
ATOM    368  N   PHE A  48      34.043  20.826   4.426  1.00 36.43           N  
ATOM    369  CA  PHE A  48      34.200  19.521   3.832  1.00 39.98           C  
ATOM    370  C   PHE A  48      34.230  19.665   2.316  1.00 43.50           C  
ATOM    371  O   PHE A  48      33.507  20.499   1.740  1.00 42.67           O  
ATOM    372  CB  PHE A  48      33.031  18.658   4.273  1.00 34.48           C  
ATOM    373  CG  PHE A  48      33.020  18.417   5.728  1.00 43.06           C  
ATOM    374  CD1 PHE A  48      32.643  19.416   6.607  1.00 39.39           C  
ATOM    375  CD2 PHE A  48      33.438  17.174   6.250  1.00 46.74           C  
ATOM    376  CE1 PHE A  48      32.681  19.192   8.018  1.00 38.74           C  
ATOM    377  CE2 PHE A  48      33.471  16.951   7.633  1.00 43.17           C  
ATOM    378  CZ  PHE A  48      33.093  17.969   8.513  1.00 35.04           C  
ATOM    379  N   ASP A  49      35.095  18.874   1.684  1.00 42.97           N  
ATOM    380  CA  ASP A  49      35.167  18.776   0.233  1.00 37.15           C  
ATOM    381  C   ASP A  49      33.829  18.229  -0.292  1.00 44.25           C  
ATOM    382  O   ASP A  49      33.339  17.143   0.107  1.00 45.11           O  
ATOM    383  CB  ASP A  49      36.277  17.811  -0.159  1.00 45.41           C  
ATOM    384  CG  ASP A  49      37.628  18.284   0.297  1.00 44.43           C  
ATOM    385  OD1 ASP A  49      37.763  18.736   1.444  1.00 55.41           O  
ATOM    386  OD2 ASP A  49      38.578  18.200  -0.484  1.00 56.43           O  
ATOM    387  N   VAL A  50      33.247  18.985  -1.190  1.00 40.97           N  
ATOM    388  CA  VAL A  50      32.017  18.582  -1.808  1.00 46.34           C  
ATOM    389  C   VAL A  50      32.380  17.551  -2.842  1.00 47.19           C  
ATOM    390  O   VAL A  50      32.998  17.892  -3.860  1.00 44.23           O  
ATOM    391  CB  VAL A  50      31.343  19.779  -2.443  1.00 32.95           C  
ATOM    392  CG1 VAL A  50      30.228  19.295  -3.368  1.00 40.12           C  
ATOM    393  CG2 VAL A  50      30.763  20.690  -1.290  1.00 25.84           C  
ATOM    394  N   ILE A  51      32.056  16.275  -2.569  1.00 51.60           N  
ATOM    395  CA  ILE A  51      32.363  15.232  -3.573  1.00 47.60           C  
ATOM    396  C   ILE A  51      31.261  15.070  -4.573  1.00 47.69           C  
ATOM    397  O   ILE A  51      30.153  15.603  -4.386  1.00 49.98           O  
ATOM    398  CB  ILE A  51      32.733  13.854  -2.960  1.00 46.03           C  
ATOM    399  CG1 ILE A  51      31.668  13.292  -2.019  1.00 53.97           C  
ATOM    400  CG2 ILE A  51      34.046  14.007  -2.178  1.00 44.22           C  
ATOM    401  CD1 ILE A  51      32.215  12.018  -1.200  1.00 50.12           C  
ATOM    402  N   ALA A  52      31.579  14.406  -5.676  1.00 44.32           N  
ATOM    403  CA  ALA A  52      30.570  14.157  -6.685  1.00 49.11           C  
ATOM    404  C   ALA A  52      29.219  13.665  -6.091  1.00 54.76           C  
ATOM    405  O   ALA A  52      28.161  14.269  -6.378  1.00 57.70           O  
ATOM    406  CB  ALA A  52      31.098  13.162  -7.683  1.00 52.87           C  
ATOM    407  N   GLU A  53      29.243  12.616  -5.260  1.00 46.67           N  
ATOM    408  CA  GLU A  53      27.999  12.170  -4.607  1.00 55.23           C  
ATOM    409  C   GLU A  53      27.248  13.336  -3.973  1.00 56.40           C  
ATOM    410  O   GLU A  53      26.011  13.353  -3.884  1.00 53.77           O  
ATOM    411  CB  GLU A  53      28.254  11.175  -3.470  1.00 59.27           C  
ATOM    412  CG  GLU A  53      28.632   9.736  -3.840  1.00 76.90           C  
ATOM    413  CD  GLU A  53      29.968   9.628  -4.606  1.00 86.74           C  
ATOM    414  OE1 GLU A  53      30.939  10.376  -4.301  1.00 92.28           O  
ATOM    415  OE2 GLU A  53      30.050   8.776  -5.526  1.00 94.93           O  
ATOM    416  N   TRP A  54      27.984  14.291  -3.435  1.00 50.45           N  
ATOM    417  CA  TRP A  54      27.230  15.215  -2.616  1.00 52.08           C  
ATOM    418  C   TRP A  54      26.447  16.189  -3.470  1.00 42.16           C  
ATOM    419  O   TRP A  54      25.491  16.781  -2.975  1.00 49.63           O  
ATOM    420  CB  TRP A  54      28.152  15.983  -1.684  1.00 52.37           C  
ATOM    421  CG  TRP A  54      28.561  15.258  -0.531  1.00 51.63           C  
ATOM    422  CD1 TRP A  54      28.467  13.907  -0.314  1.00 60.56           C  
ATOM    423  CD2 TRP A  54      29.160  15.814   0.614  1.00 57.03           C  
ATOM    424  NE1 TRP A  54      28.969  13.589   0.925  1.00 60.52           N  
ATOM    425  CE2 TRP A  54      29.407  14.748   1.518  1.00 65.63           C  
ATOM    426  CE3 TRP A  54      29.535  17.109   0.973  1.00 52.27           C  
ATOM    427  CZ2 TRP A  54      30.006  14.950   2.759  1.00 60.50           C  
ATOM    428  CZ3 TRP A  54      30.134  17.303   2.200  1.00 61.52           C  
ATOM    429  CH2 TRP A  54      30.364  16.231   3.079  1.00 63.31           C  
ATOM    430  N   VAL A  55      26.880  16.387  -4.715  1.00 40.91           N  
ATOM    431  CA  VAL A  55      26.269  17.421  -5.567  1.00 49.71           C  
ATOM    432  C   VAL A  55      24.729  17.342  -5.640  1.00 49.36           C  
ATOM    433  O   VAL A  55      24.055  18.319  -5.328  1.00 56.79           O  
ATOM    434  CB  VAL A  55      26.834  17.456  -7.016  1.00 46.78           C  
ATOM    435  CG1 VAL A  55      26.264  18.713  -7.758  1.00 44.95           C  
ATOM    436  CG2 VAL A  55      28.341  17.593  -6.973  1.00 43.25           C  
ATOM    437  N   PRO A  56      24.159  16.188  -6.025  1.00 52.34           N  
ATOM    438  CA  PRO A  56      22.687  15.983  -6.129  1.00 51.51           C  
ATOM    439  C   PRO A  56      22.023  16.230  -4.770  1.00 54.19           C  
ATOM    440  O   PRO A  56      21.017  16.928  -4.670  1.00 58.66           O  
ATOM    441  CB  PRO A  56      22.546  14.510  -6.495  1.00 52.35           C  
ATOM    442  CG  PRO A  56      23.860  14.186  -7.163  1.00 57.63           C  
ATOM    443  CD  PRO A  56      24.890  14.945  -6.322  1.00 50.97           C  
ATOM    444  N   LEU A  57      22.592  15.662  -3.711  1.00 49.15           N  
ATOM    445  CA  LEU A  57      22.110  15.959  -2.366  1.00 43.24           C  
ATOM    446  C   LEU A  57      22.159  17.466  -2.020  1.00 50.57           C  
ATOM    447  O   LEU A  57      21.455  17.911  -1.124  1.00 52.43           O  
ATOM    448  CB  LEU A  57      22.952  15.191  -1.347  1.00 49.43           C  
ATOM    449  CG  LEU A  57      23.056  13.681  -1.625  1.00 60.46           C  
ATOM    450  CD1 LEU A  57      24.081  12.982  -0.700  1.00 60.69           C  
ATOM    451  CD2 LEU A  57      21.677  13.063  -1.424  1.00 60.23           C  
ATOM    452  N   LEU A  58      23.015  18.260  -2.659  1.00 48.36           N  
ATOM    453  CA  LEU A  58      23.183  19.621  -2.165  1.00 45.37           C  
ATOM    454  C   LEU A  58      22.493  20.560  -3.072  1.00 46.71           C  
ATOM    455  O   LEU A  58      22.055  21.633  -2.645  1.00 50.58           O  
ATOM    456  CB  LEU A  58      24.659  20.030  -2.128  1.00 49.62           C  
ATOM    457  CG  LEU A  58      25.501  19.368  -1.048  1.00 56.99           C  
ATOM    458  CD1 LEU A  58      26.957  19.849  -1.095  1.00 54.18           C  
ATOM    459  CD2 LEU A  58      24.880  19.683   0.289  1.00 46.68           C  
ATOM    460  N   GLN A  59      22.438  20.203  -4.359  1.00 50.19           N  
ATOM    461  CA  GLN A  59      22.049  21.196  -5.386  1.00 53.90           C  
ATOM    462  C   GLN A  59      20.654  21.809  -5.139  1.00 53.67           C  
ATOM    463  O   GLN A  59      20.437  23.022  -5.386  1.00 57.92           O  
ATOM    464  CB  GLN A  59      22.097  20.581  -6.802  1.00 53.47           C  
ATOM    465  CG  GLN A  59      21.803  21.586  -7.921  1.00 37.82           C  
ATOM    466  CD  GLN A  59      22.812  22.725  -8.024  1.00 52.86           C  
ATOM    467  OE1 GLN A  59      23.886  22.577  -8.641  1.00 46.89           O  
ATOM    468  NE2 GLN A  59      22.465  23.886  -7.440  1.00 49.91           N  
ATOM    469  N   PRO A  60      19.696  20.984  -4.648  1.00 54.41           N  
ATOM    470  CA  PRO A  60      18.312  21.430  -4.361  1.00 53.72           C  
ATOM    471  C   PRO A  60      18.261  22.609  -3.407  1.00 60.05           C  
ATOM    472  O   PRO A  60      17.213  23.226  -3.269  1.00 59.94           O  
ATOM    473  CB  PRO A  60      17.653  20.201  -3.721  1.00 52.14           C  
ATOM    474  CG  PRO A  60      18.436  19.021  -4.356  1.00 57.87           C  
ATOM    475  CD  PRO A  60      19.866  19.536  -4.363  1.00 53.66           C  
ATOM    476  N   TYR A  61      19.371  22.924  -2.724  1.00 61.03           N  
ATOM    477  CA  TYR A  61      19.329  23.994  -1.723  1.00 54.97           C  
ATOM    478  C   TYR A  61      20.066  25.211  -2.194  1.00 52.36           C  
ATOM    479  O   TYR A  61      20.139  26.192  -1.429  1.00 52.86           O  
ATOM    480  CB  TYR A  61      19.949  23.558  -0.394  1.00 49.58           C  
ATOM    481  CG  TYR A  61      19.240  22.412   0.227  1.00 51.50           C  
ATOM    482  CD1 TYR A  61      17.952  22.567   0.792  1.00 56.74           C  
ATOM    483  CD2 TYR A  61      19.809  21.136   0.186  1.00 54.84           C  
ATOM    484  CE1 TYR A  61      17.240  21.464   1.292  1.00 45.24           C  
ATOM    485  CE2 TYR A  61      19.133  20.017   0.682  1.00 56.78           C  
ATOM    486  CZ  TYR A  61      17.842  20.183   1.235  1.00 64.45           C  
ATOM    487  OH  TYR A  61      17.209  19.046   1.737  1.00 62.34           O  
ATOM    488  N   PHE A  62      20.602  25.175  -3.423  1.00 49.02           N  
ATOM    489  CA  PHE A  62      21.399  26.332  -3.916  1.00 52.91           C  
ATOM    490  C   PHE A  62      21.028  26.919  -5.290  1.00 50.83           C  
ATOM    491  O   PHE A  62      20.726  26.179  -6.213  1.00 47.88           O  
ATOM    492  CB  PHE A  62      22.905  25.981  -3.959  1.00 48.90           C  
ATOM    493  CG  PHE A  62      23.483  25.691  -2.615  1.00 49.01           C  
ATOM    494  CD1 PHE A  62      23.865  26.734  -1.780  1.00 44.02           C  
ATOM    495  CD2 PHE A  62      23.573  24.361  -2.149  1.00 45.94           C  
ATOM    496  CE1 PHE A  62      24.329  26.469  -0.484  1.00 48.17           C  
ATOM    497  CE2 PHE A  62      24.035  24.078  -0.849  1.00 40.99           C  
ATOM    498  CZ  PHE A  62      24.412  25.132  -0.016  1.00 43.34           C  
ATOM    499  N   ASN A  63      21.113  28.244  -5.420  1.00 46.63           N  
ATOM    500  CA  ASN A  63      20.979  28.906  -6.711  1.00 49.74           C  
ATOM    501  C   ASN A  63      22.145  28.546  -7.630  1.00 55.01           C  
ATOM    502  O   ASN A  63      21.955  28.335  -8.852  1.00 55.90           O  
ATOM    503  CB  ASN A  63      20.961  30.452  -6.571  1.00 49.38           C  
ATOM    504  CG  ASN A  63      19.694  30.981  -5.869  1.00 56.47           C  
ATOM    505  OD1 ASN A  63      18.669  30.285  -5.796  1.00 49.98           O  
ATOM    506  ND2 ASN A  63      19.768  32.231  -5.355  1.00 49.15           N  
ATOM    507  N   HIS A  64      23.352  28.512  -7.049  1.00 51.23           N  
ATOM    508  CA  HIS A  64      24.554  28.278  -7.810  1.00 43.90           C  
ATOM    509  C   HIS A  64      24.489  26.905  -8.422  1.00 42.29           C  
ATOM    510  O   HIS A  64      24.040  25.906  -7.811  1.00 46.02           O  
ATOM    511  CB  HIS A  64      25.779  28.370  -6.939  1.00 48.05           C  
ATOM    512  CG  HIS A  64      27.048  28.166  -7.690  1.00 54.01           C  
ATOM    513  ND1 HIS A  64      27.502  29.068  -8.632  1.00 49.13           N  
ATOM    514  CD2 HIS A  64      27.931  27.135  -7.688  1.00 44.36           C  
ATOM    515  CE1 HIS A  64      28.612  28.603  -9.176  1.00 48.39           C  
ATOM    516  NE2 HIS A  64      28.891  27.433  -8.625  1.00 54.27           N  
ATOM    517  N   GLN A  65      24.905  26.842  -9.662  1.00 39.89           N  
ATOM    518  CA  GLN A  65      24.737  25.587 -10.382  1.00 48.47           C  
ATOM    519  C   GLN A  65      26.113  24.952 -10.176  1.00 44.28           C  
ATOM    520  O   GLN A  65      27.127  25.404 -10.711  1.00 46.00           O  
ATOM    521  CB  GLN A  65      24.386  25.880 -11.884  1.00 43.84           C  
ATOM    522  CG  GLN A  65      22.996  25.394 -12.386  1.00 53.69           C  
ATOM    523  CD  GLN A  65      21.945  25.230 -11.289  1.00 56.73           C  
ATOM    524  OE1 GLN A  65      21.329  24.173 -11.176  1.00 61.28           O  
ATOM    525  NE2 GLN A  65      21.743  26.265 -10.471  1.00 58.84           N  
ATOM    526  N   ILE A  66      26.155  23.974  -9.305  1.00 47.73           N  
ATOM    527  CA  ILE A  66      27.439  23.510  -8.814  1.00 48.60           C  
ATOM    528  C   ILE A  66      28.141  22.747  -9.905  1.00 48.68           C  
ATOM    529  O   ILE A  66      27.569  21.790 -10.432  1.00 53.70           O  
ATOM    530  CB  ILE A  66      27.272  22.576  -7.637  1.00 45.11           C  
ATOM    531  CG1 ILE A  66      26.650  23.344  -6.490  1.00 44.10           C  
ATOM    532  CG2 ILE A  66      28.648  21.914  -7.304  1.00 51.27           C  
ATOM    533  CD1 ILE A  66      26.172  22.452  -5.320  1.00 44.44           C  
ATOM    534  N   ASP A  67      29.352  23.156 -10.271  1.00 46.02           N  
ATOM    535  CA  ASP A  67      30.025  22.467 -11.372  1.00 45.76           C  
ATOM    536  C   ASP A  67      31.429  21.999 -10.950  1.00 45.64           C  
ATOM    537  O   ASP A  67      32.444  22.737 -11.080  1.00 43.16           O  
ATOM    538  CB  ASP A  67      30.103  23.397 -12.588  1.00 48.54           C  
ATOM    539  CG  ASP A  67      30.829  22.762 -13.768  1.00 63.50           C  
ATOM    540  OD1 ASP A  67      31.535  21.725 -13.596  1.00 70.24           O  
ATOM    541  OD2 ASP A  67      30.713  23.315 -14.881  1.00 64.34           O  
ATOM    542  N   ILE A  68      31.491  20.781 -10.438  1.00 42.64           N  
ATOM    543  CA  ILE A  68      32.758  20.301  -9.901  1.00 50.94           C  
ATOM    544  C   ILE A  68      33.877  20.042 -10.933  1.00 50.41           C  
ATOM    545  O   ILE A  68      35.004  19.750 -10.555  1.00 56.57           O  
ATOM    546  CB  ILE A  68      32.588  19.019  -9.099  1.00 49.24           C  
ATOM    547  CG1 ILE A  68      32.045  17.910 -10.016  1.00 43.34           C  
ATOM    548  CG2 ILE A  68      31.690  19.258  -7.873  1.00 44.00           C  
ATOM    549  CD1 ILE A  68      32.054  16.562  -9.289  1.00 46.09           C  
ATOM    550  N   SER A  69      33.582  20.130 -12.217  1.00 50.86           N  
ATOM    551  CA  SER A  69      34.637  20.001 -13.188  1.00 52.08           C  
ATOM    552  C   SER A  69      35.235  21.365 -13.454  1.00 54.30           C  
ATOM    553  O   SER A  69      36.327  21.481 -14.016  1.00 56.20           O  
ATOM    554  CB  SER A  69      34.089  19.428 -14.491  1.00 56.47           C  
ATOM    555  OG  SER A  69      33.634  20.508 -15.292  1.00 59.12           O  
ATOM    556  N   ASP A  70      34.516  22.409 -13.065  1.00 51.38           N  
ATOM    557  CA  ASP A  70      35.078  23.733 -13.154  1.00 49.93           C  
ATOM    558  C   ASP A  70      35.819  24.201 -11.854  1.00 48.44           C  
ATOM    559  O   ASP A  70      36.923  24.828 -11.909  1.00 46.75           O  
ATOM    560  CB  ASP A  70      33.929  24.655 -13.503  1.00 65.50           C  
ATOM    561  CG  ASP A  70      34.322  25.717 -14.477  1.00 65.87           C  
ATOM    562  OD1 ASP A  70      35.040  25.386 -15.462  1.00 72.07           O  
ATOM    563  OD2 ASP A  70      33.890  26.869 -14.250  1.00 70.01           O  
ATOM    564  N   ASN A  71      35.221  23.885 -10.702  1.00 43.07           N  
ATOM    565  CA  ASN A  71      35.589  24.487  -9.407  1.00 44.26           C  
ATOM    566  C   ASN A  71      35.687  23.461  -8.302  1.00 40.04           C  
ATOM    567  O   ASN A  71      35.002  22.478  -8.376  1.00 42.36           O  
ATOM    568  CB  ASN A  71      34.541  25.498  -8.937  1.00 40.51           C  
ATOM    569  CG  ASN A  71      34.147  26.469 -10.024  1.00 56.50           C  
ATOM    570  OD1 ASN A  71      35.020  27.138 -10.602  1.00 50.48           O  
ATOM    571  ND2 ASN A  71      32.820  26.562 -10.318  1.00 47.01           N  
ATOM    572  N   GLU A  72      36.524  23.729  -7.280  1.00 40.22           N  
ATOM    573  CA  GLU A  72      36.541  23.001  -6.012  1.00 41.23           C  
ATOM    574  C   GLU A  72      35.483  23.602  -5.092  1.00 46.75           C  
ATOM    575  O   GLU A  72      35.487  24.815  -4.861  1.00 41.66           O  
ATOM    576  CB  GLU A  72      37.900  23.132  -5.301  1.00 44.39           C  
ATOM    577  CG  GLU A  72      39.093  22.608  -6.083  1.00 55.52           C  
ATOM    578  CD  GLU A  72      40.423  22.605  -5.287  1.00 58.29           C  
ATOM    579  OE1 GLU A  72      40.398  22.408  -4.043  1.00 44.06           O  
ATOM    580  OE2 GLU A  72      41.506  22.769  -5.943  1.00 63.77           O  
ATOM    581  N   TYR A  73      34.624  22.757  -4.534  1.00 44.03           N  
ATOM    582  CA  TYR A  73      33.586  23.184  -3.628  1.00 42.31           C  
ATOM    583  C   TYR A  73      33.845  22.693  -2.200  1.00 42.29           C  
ATOM    584  O   TYR A  73      34.399  21.630  -2.016  1.00 47.11           O  
ATOM    585  CB  TYR A  73      32.233  22.646  -4.140  1.00 42.05           C  
ATOM    586  CG  TYR A  73      31.814  23.353  -5.356  1.00 37.20           C  
ATOM    587  CD1 TYR A  73      32.337  23.002  -6.606  1.00 43.08           C  
ATOM    588  CD2 TYR A  73      30.869  24.411  -5.278  1.00 47.81           C  
ATOM    589  CE1 TYR A  73      31.904  23.698  -7.783  1.00 44.05           C  
ATOM    590  CE2 TYR A  73      30.442  25.101  -6.411  1.00 34.22           C  
ATOM    591  CZ  TYR A  73      30.943  24.749  -7.656  1.00 40.65           C  
ATOM    592  OH  TYR A  73      30.477  25.395  -8.774  1.00 38.64           O  
ATOM    593  N   PHE A  74      33.441  23.487  -1.210  1.00 37.39           N  
ATOM    594  CA  PHE A  74      33.554  23.164   0.199  1.00 36.01           C  
ATOM    595  C   PHE A  74      32.241  23.636   0.842  1.00 42.55           C  
ATOM    596  O   PHE A  74      31.664  24.647   0.391  1.00 46.04           O  
ATOM    597  CB  PHE A  74      34.730  23.916   0.797  1.00 35.58           C  
ATOM    598  CG  PHE A  74      36.031  23.503   0.215  1.00 36.96           C  
ATOM    599  CD1 PHE A  74      36.718  22.417   0.727  1.00 40.91           C  
ATOM    600  CD2 PHE A  74      36.544  24.163  -0.890  1.00 34.05           C  
ATOM    601  CE1 PHE A  74      37.945  21.973   0.152  1.00 39.01           C  
ATOM    602  CE2 PHE A  74      37.752  23.749  -1.509  1.00 40.51           C  
ATOM    603  CZ  PHE A  74      38.465  22.631  -0.973  1.00 42.63           C  
ATOM    604  N   VAL A  75      31.751  22.877   1.818  1.00 38.95           N  
ATOM    605  CA  VAL A  75      30.566  23.223   2.593  1.00 41.18           C  
ATOM    606  C   VAL A  75      30.954  23.146   4.041  1.00 38.36           C  
ATOM    607  O   VAL A  75      31.676  22.244   4.409  1.00 40.60           O  
ATOM    608  CB  VAL A  75      29.461  22.178   2.500  1.00 44.83           C  
ATOM    609  CG1 VAL A  75      28.171  22.830   2.211  1.00 35.37           C  
ATOM    610  CG2 VAL A  75      29.830  21.154   1.532  1.00 48.29           C  
ATOM    611  N   SER A  76      30.430  24.063   4.859  1.00 39.60           N  
ATOM    612  CA  SER A  76      30.507  23.935   6.317  1.00 40.31           C  
ATOM    613  C   SER A  76      29.077  23.964   6.875  1.00 42.01           C  
ATOM    614  O   SER A  76      28.141  24.382   6.198  1.00 47.26           O  
ATOM    615  CB  SER A  76      31.328  25.101   6.926  1.00 41.10           C  
ATOM    616  OG  SER A  76      30.783  26.338   6.507  1.00 38.65           O  
ATOM    617  N   PHE A  77      28.937  23.541   8.113  1.00 37.65           N  
ATOM    618  CA  PHE A  77      27.654  23.388   8.731  1.00 31.65           C  
ATOM    619  C   PHE A  77      27.641  24.384   9.809  1.00 33.75           C  
ATOM    620  O   PHE A  77      28.020  24.084  10.898  1.00 37.34           O  
ATOM    621  CB  PHE A  77      27.552  21.981   9.267  1.00 31.10           C  
ATOM    622  CG  PHE A  77      27.668  20.976   8.175  1.00 39.02           C  
ATOM    623  CD1 PHE A  77      26.637  20.842   7.230  1.00 37.08           C  
ATOM    624  CD2 PHE A  77      28.860  20.255   7.975  1.00 34.81           C  
ATOM    625  CE1 PHE A  77      26.795  20.011   6.104  1.00 40.48           C  
ATOM    626  CE2 PHE A  77      29.027  19.420   6.850  1.00 42.19           C  
ATOM    627  CZ  PHE A  77      27.985  19.301   5.912  1.00 37.79           C  
ATOM    628  N   ASP A  78      27.270  25.616   9.462  1.00 35.49           N  
ATOM    629  CA  ASP A  78      27.189  26.709  10.391  1.00 34.01           C  
ATOM    630  C   ASP A  78      25.871  26.651  11.215  1.00 43.12           C  
ATOM    631  O   ASP A  78      24.752  26.480  10.662  1.00 39.72           O  
ATOM    632  CB  ASP A  78      27.266  28.039   9.634  1.00 37.57           C  
ATOM    633  CG  ASP A  78      28.558  28.176   8.798  1.00 52.52           C  
ATOM    634  OD1 ASP A  78      29.424  27.267   8.888  1.00 45.22           O  
ATOM    635  OD2 ASP A  78      28.699  29.194   8.059  1.00 45.02           O  
ATOM    636  N   TYR A  79      25.996  26.798  12.527  1.00 42.92           N  
ATOM    637  CA  TYR A  79      24.818  26.883  13.355  1.00 44.40           C  
ATOM    638  C   TYR A  79      24.821  28.105  14.226  1.00 46.32           C  
ATOM    639  O   TYR A  79      25.755  28.301  15.021  1.00 45.07           O  
ATOM    640  CB  TYR A  79      24.663  25.656  14.238  1.00 45.64           C  
ATOM    641  CG  TYR A  79      23.349  25.735  14.980  1.00 53.91           C  
ATOM    642  CD1 TYR A  79      23.197  26.568  16.114  1.00 47.76           C  
ATOM    643  CD2 TYR A  79      22.247  24.997  14.544  1.00 49.00           C  
ATOM    644  CE1 TYR A  79      21.980  26.649  16.788  1.00 52.36           C  
ATOM    645  CE2 TYR A  79      21.033  25.061  15.213  1.00 48.77           C  
ATOM    646  CZ  TYR A  79      20.899  25.885  16.338  1.00 49.83           C  
ATOM    647  OH  TYR A  79      19.711  25.886  17.030  1.00 50.16           O  
ATOM    648  N   ARG A  80      23.780  28.932  14.086  1.00 46.59           N  
ATOM    649  CA  ARG A  80      23.626  30.114  14.974  1.00 50.51           C  
ATOM    650  C   ARG A  80      22.186  30.152  15.404  1.00 55.19           C  
ATOM    651  O   ARG A  80      21.302  29.732  14.624  1.00 56.93           O  
ATOM    652  CB  ARG A  80      23.938  31.443  14.279  1.00 38.57           C  
ATOM    653  CG  ARG A  80      25.415  31.698  14.034  1.00 55.36           C  
ATOM    654  CD  ARG A  80      25.687  32.756  12.922  1.00 51.29           C  
ATOM    655  NE  ARG A  80      27.098  33.181  12.909  1.00 55.77           N  
ATOM    656  CZ  ARG A  80      27.691  33.855  13.897  1.00 63.66           C  
ATOM    657  NH1 ARG A  80      26.983  34.195  14.961  1.00 71.88           N  
ATOM    658  NH2 ARG A  80      28.998  34.147  13.871  1.00 62.75           N  
ATOM    659  N   ASP A  81      21.954  30.638  16.630  1.00 58.25           N  
ATOM    660  CA  ASP A  81      20.607  30.702  17.190  1.00 57.37           C  
ATOM    661  C   ASP A  81      19.801  31.689  16.447  1.00 58.01           C  
ATOM    662  O   ASP A  81      20.246  32.813  16.219  1.00 59.37           O  
ATOM    663  CB  ASP A  81      20.626  31.102  18.665  1.00 55.28           C  
ATOM    664  CG  ASP A  81      21.118  29.958  19.563  1.00 57.42           C  
ATOM    665  OD1 ASP A  81      20.938  28.771  19.199  1.00 59.69           O  
ATOM    666  OD2 ASP A  81      21.677  30.246  20.627  1.00 57.67           O  
ATOM    667  N   GLY A  82      18.608  31.252  16.059  1.00 59.17           N  
ATOM    668  CA  GLY A  82      17.639  32.172  15.497  1.00 62.35           C  
ATOM    669  C   GLY A  82      17.787  32.406  14.004  1.00 67.46           C  
ATOM    670  O   GLY A  82      18.198  31.509  13.248  1.00 65.59           O  
ATOM    671  N   ASP A  83      17.439  33.632  13.606  1.00 67.80           N  
ATOM    672  CA  ASP A  83      17.514  34.114  12.235  1.00 66.28           C  
ATOM    673  C   ASP A  83      18.845  34.872  12.124  1.00 61.27           C  
ATOM    674  O   ASP A  83      19.176  35.700  12.967  1.00 59.20           O  
ATOM    675  CB  ASP A  83      16.323  35.066  11.935  1.00 64.80           C  
ATOM    676  CG  ASP A  83      16.199  35.442  10.425  1.00 68.46           C  
ATOM    677  OD1 ASP A  83      17.140  36.012   9.795  1.00 70.09           O  
ATOM    678  OD2 ASP A  83      15.125  35.165   9.853  1.00 75.39           O  
ATOM    679  N   TRP A  84      19.604  34.591  11.072  1.00 58.37           N  
ATOM    680  CA  TRP A  84      20.945  35.186  10.944  1.00 58.03           C  
ATOM    681  C   TRP A  84      21.464  35.170   9.494  1.00 58.04           C  
ATOM    682  O   TRP A  84      20.928  34.342   8.667  1.00 50.10           O  
ATOM    683  CB  TRP A  84      21.941  34.421  11.822  1.00 54.36           C  
ATOM    684  CG  TRP A  84      22.246  32.984  11.346  1.00 50.65           C  
ATOM    685  CD1 TRP A  84      21.566  31.822  11.671  1.00 53.45           C  
ATOM    686  CD2 TRP A  84      23.345  32.588  10.526  1.00 48.14           C  
ATOM    687  NE1 TRP A  84      22.186  30.741  11.112  1.00 48.76           N  
ATOM    688  CE2 TRP A  84      23.282  31.173  10.405  1.00 48.41           C  
ATOM    689  CE3 TRP A  84      24.387  33.293   9.888  1.00 40.78           C  
ATOM    690  CZ2 TRP A  84      24.221  30.439   9.675  1.00 44.29           C  
ATOM    691  CZ3 TRP A  84      25.332  32.562   9.152  1.00 49.54           C  
ATOM    692  CH2 TRP A  84      25.238  31.142   9.056  1.00 47.53           C  
ATOM    693  OXT TRP A  84      22.415  35.985   9.250  1.00 53.42           O  
TER     694      TRP A  84                                                      
ATOM    695  N   GLY B   1      21.011  16.106  21.403  1.00 44.57           N  
ATOM    696  CA  GLY B   1      20.309  16.507  20.135  1.00 59.57           C  
ATOM    697  C   GLY B   1      20.872  17.746  19.398  1.00 64.10           C  
ATOM    698  O   GLY B   1      21.787  18.415  19.876  1.00 68.77           O  
ATOM    699  N   PHE B   2      20.336  18.070  18.226  1.00 64.20           N  
ATOM    700  CA  PHE B   2      21.101  18.871  17.259  1.00 61.15           C  
ATOM    701  C   PHE B   2      21.468  20.324  17.690  1.00 58.23           C  
ATOM    702  O   PHE B   2      22.582  20.792  17.413  1.00 50.86           O  
ATOM    703  CB  PHE B   2      20.392  18.862  15.895  1.00 59.08           C  
ATOM    704  CG  PHE B   2      21.140  19.597  14.816  1.00 55.82           C  
ATOM    705  CD1 PHE B   2      22.157  18.969  14.099  1.00 53.29           C  
ATOM    706  CD2 PHE B   2      20.869  20.956  14.581  1.00 55.76           C  
ATOM    707  CE1 PHE B   2      22.903  19.684  13.165  1.00 57.49           C  
ATOM    708  CE2 PHE B   2      21.588  21.680  13.668  1.00 56.01           C  
ATOM    709  CZ  PHE B   2      22.625  21.046  12.946  1.00 57.54           C  
ATOM    710  N   LYS B   3      20.586  21.030  18.379  1.00 52.82           N  
ATOM    711  CA  LYS B   3      20.944  22.372  18.799  1.00 52.79           C  
ATOM    712  C   LYS B   3      22.161  22.273  19.706  1.00 57.56           C  
ATOM    713  O   LYS B   3      23.062  23.142  19.728  1.00 54.26           O  
ATOM    714  CB  LYS B   3      19.788  23.005  19.571  1.00 67.41           C  
ATOM    715  CG  LYS B   3      20.075  24.434  20.061  1.00 70.94           C  
ATOM    716  CD  LYS B   3      18.936  24.935  20.981  1.00 83.23           C  
ATOM    717  CE  LYS B   3      18.860  26.515  21.056  1.00 82.72           C  
ATOM    718  NZ  LYS B   3      18.452  27.195  19.731  1.00 78.15           N  
ATOM    719  N   ASP B   4      22.178  21.209  20.492  1.00 58.48           N  
ATOM    720  CA  ASP B   4      23.304  21.021  21.402  1.00 64.35           C  
ATOM    721  C   ASP B   4      24.599  20.933  20.607  1.00 55.91           C  
ATOM    722  O   ASP B   4      25.590  21.595  20.936  1.00 57.13           O  
ATOM    723  CB  ASP B   4      23.118  19.765  22.267  1.00 62.18           C  
ATOM    724  CG  ASP B   4      21.784  19.782  23.031  1.00 71.62           C  
ATOM    725  OD1 ASP B   4      21.486  20.779  23.771  1.00 60.33           O  
ATOM    726  OD2 ASP B   4      21.036  18.772  22.866  1.00 81.58           O  
ATOM    727  N   TYR B   5      24.594  20.140  19.549  1.00 52.49           N  
ATOM    728  CA  TYR B   5      25.780  20.063  18.728  1.00 54.10           C  
ATOM    729  C   TYR B   5      26.184  21.444  18.182  1.00 50.47           C  
ATOM    730  O   TYR B   5      27.360  21.765  18.118  1.00 48.19           O  
ATOM    731  CB  TYR B   5      25.576  19.070  17.603  1.00 55.19           C  
ATOM    732  CG  TYR B   5      25.617  17.652  18.085  1.00 63.39           C  
ATOM    733  CD1 TYR B   5      26.809  16.976  18.169  1.00 55.64           C  
ATOM    734  CD2 TYR B   5      24.443  16.979  18.485  1.00 73.10           C  
ATOM    735  CE1 TYR B   5      26.857  15.652  18.636  1.00 65.59           C  
ATOM    736  CE2 TYR B   5      24.482  15.648  18.947  1.00 63.33           C  
ATOM    737  CZ  TYR B   5      25.690  15.001  19.010  1.00 65.31           C  
ATOM    738  OH  TYR B   5      25.742  13.683  19.365  1.00 67.24           O  
ATOM    739  N   GLY B   6      25.191  22.261  17.828  1.00 46.44           N  
ATOM    740  CA  GLY B   6      25.465  23.572  17.295  1.00 44.71           C  
ATOM    741  C   GLY B   6      26.069  24.541  18.275  1.00 49.91           C  
ATOM    742  O   GLY B   6      26.520  25.618  17.873  1.00 52.97           O  
ATOM    743  N   HIS B   7      26.067  24.216  19.564  1.00 51.53           N  
ATOM    744  CA  HIS B   7      26.709  25.102  20.531  1.00 48.13           C  
ATOM    745  C   HIS B   7      28.014  24.523  21.053  1.00 48.34           C  
ATOM    746  O   HIS B   7      28.633  25.150  21.905  1.00 47.53           O  
ATOM    747  CB  HIS B   7      25.785  25.389  21.709  1.00 53.52           C  
ATOM    748  CG  HIS B   7      24.665  26.328  21.373  1.00 67.40           C  
ATOM    749  ND1 HIS B   7      23.435  25.893  20.928  1.00 71.16           N  
ATOM    750  CD2 HIS B   7      24.600  27.687  21.395  1.00 66.02           C  
ATOM    751  CE1 HIS B   7      22.656  26.936  20.693  1.00 68.79           C  
ATOM    752  NE2 HIS B   7      23.336  28.038  20.965  1.00 69.30           N  
ATOM    753  N   ASP B   8      28.428  23.348  20.548  1.00 37.88           N  
ATOM    754  CA  ASP B   8      29.772  22.827  20.840  1.00 51.60           C  
ATOM    755  C   ASP B   8      30.945  23.764  20.538  1.00 51.70           C  
ATOM    756  O   ASP B   8      31.940  23.776  21.270  1.00 53.18           O  
ATOM    757  CB  ASP B   8      30.046  21.498  20.111  1.00 48.12           C  
ATOM    758  CG  ASP B   8      29.255  20.362  20.699  1.00 53.99           C  
ATOM    759  OD1 ASP B   8      28.979  20.448  21.936  1.00 51.26           O  
ATOM    760  OD2 ASP B   8      28.933  19.416  19.936  1.00 54.34           O  
ATOM    761  N   TYR B   9      30.833  24.504  19.436  1.00 53.65           N  
ATOM    762  CA  TYR B   9      31.890  25.415  19.003  1.00 49.49           C  
ATOM    763  C   TYR B   9      31.340  26.775  18.642  1.00 48.99           C  
ATOM    764  O   TYR B   9      30.105  26.911  18.564  1.00 53.22           O  
ATOM    765  CB  TYR B   9      32.588  24.822  17.824  1.00 52.37           C  
ATOM    766  CG  TYR B   9      33.128  23.478  18.148  1.00 50.76           C  
ATOM    767  CD1 TYR B   9      34.263  23.353  18.929  1.00 57.35           C  
ATOM    768  CD2 TYR B   9      32.552  22.332  17.616  1.00 53.95           C  
ATOM    769  CE1 TYR B   9      34.835  22.137  19.159  1.00 55.55           C  
ATOM    770  CE2 TYR B   9      33.103  21.081  17.844  1.00 60.31           C  
ATOM    771  CZ  TYR B   9      34.251  20.998  18.611  1.00 62.28           C  
ATOM    772  OH  TYR B   9      34.833  19.787  18.795  1.00 56.42           O  
ATOM    773  N   HIS B  10      32.228  27.777  18.455  1.00 46.97           N  
ATOM    774  CA  HIS B  10      31.807  29.155  18.190  1.00 40.21           C  
ATOM    775  C   HIS B  10      31.610  29.250  16.680  1.00 47.29           C  
ATOM    776  O   HIS B  10      32.484  28.826  15.906  1.00 44.78           O  
ATOM    777  CB  HIS B  10      32.884  30.132  18.586  1.00 46.12           C  
ATOM    778  CG  HIS B  10      33.057  30.281  20.061  1.00 54.56           C  
ATOM    779  ND1 HIS B  10      32.185  31.017  20.839  1.00 59.55           N  
ATOM    780  CD2 HIS B  10      33.978  29.756  20.912  1.00 48.85           C  
ATOM    781  CE1 HIS B  10      32.560  30.937  22.108  1.00 59.56           C  
ATOM    782  NE2 HIS B  10      33.645  30.180  22.178  1.00 48.50           N  
ATOM    783  N   PRO B  11      30.453  29.779  16.239  1.00 48.45           N  
ATOM    784  CA  PRO B  11      30.176  29.902  14.796  1.00 47.04           C  
ATOM    785  C   PRO B  11      31.239  30.814  14.200  1.00 45.37           C  
ATOM    786  O   PRO B  11      31.669  31.779  14.834  1.00 44.08           O  
ATOM    787  CB  PRO B  11      28.779  30.537  14.737  1.00 42.96           C  
ATOM    788  CG  PRO B  11      28.248  30.380  16.104  1.00 51.52           C  
ATOM    789  CD  PRO B  11      29.431  30.472  17.033  1.00 43.70           C  
ATOM    790  N   ALA B  12      31.690  30.519  12.988  1.00 43.65           N  
ATOM    791  CA  ALA B  12      32.676  31.422  12.404  1.00 44.84           C  
ATOM    792  C   ALA B  12      32.009  32.756  11.956  1.00 46.05           C  
ATOM    793  O   ALA B  12      30.775  32.824  11.726  1.00 36.17           O  
ATOM    794  CB  ALA B  12      33.304  30.752  11.215  1.00 28.62           C  
ATOM    795  N   PRO B  13      32.813  33.821  11.828  1.00 43.37           N  
ATOM    796  CA  PRO B  13      32.235  35.097  11.378  1.00 40.09           C  
ATOM    797  C   PRO B  13      31.950  34.979   9.891  1.00 41.67           C  
ATOM    798  O   PRO B  13      32.703  34.348   9.156  1.00 41.16           O  
ATOM    799  CB  PRO B  13      33.323  36.089  11.655  1.00 37.66           C  
ATOM    800  CG  PRO B  13      34.591  35.246  11.543  1.00 44.08           C  
ATOM    801  CD  PRO B  13      34.205  33.977  12.275  1.00 47.46           C  
ATOM    802  N   LYS B  14      30.852  35.545   9.417  1.00 45.65           N  
ATOM    803  CA  LYS B  14      30.714  35.598   7.981  1.00 46.10           C  
ATOM    804  C   LYS B  14      31.625  36.714   7.460  1.00 45.56           C  
ATOM    805  O   LYS B  14      32.012  37.610   8.222  1.00 48.07           O  
ATOM    806  CB  LYS B  14      29.226  35.645   7.546  1.00 49.38           C  
ATOM    807  CG  LYS B  14      28.401  36.852   7.668  1.00 53.46           C  
ATOM    808  CD  LYS B  14      26.900  36.379   7.659  1.00 55.38           C  
ATOM    809  CE  LYS B  14      26.076  36.459   6.294  1.00 61.45           C  
ATOM    810  NZ  LYS B  14      24.583  35.942   6.459  1.00 64.59           N  
ATOM    811  N   THR B  15      32.105  36.545   6.224  1.00 44.66           N  
ATOM    812  CA  THR B  15      33.246  37.299   5.690  1.00 47.57           C  
ATOM    813  C   THR B  15      32.991  38.805   5.846  1.00 47.50           C  
ATOM    814  O   THR B  15      33.875  39.577   6.258  1.00 49.98           O  
ATOM    815  CB  THR B  15      33.466  36.987   4.159  1.00 46.21           C  
ATOM    816  OG1 THR B  15      33.802  35.607   3.976  1.00 46.38           O  
ATOM    817  CG2 THR B  15      34.577  37.839   3.600  1.00 38.99           C  
ATOM    818  N   GLU B  16      31.773  39.214   5.514  1.00 47.32           N  
ATOM    819  CA  GLU B  16      31.407  40.641   5.460  1.00 53.10           C  
ATOM    820  C   GLU B  16      31.512  41.315   6.836  1.00 60.02           C  
ATOM    821  O   GLU B  16      31.683  42.546   6.912  1.00 67.45           O  
ATOM    822  CB  GLU B  16      29.988  40.794   4.912  1.00 47.05           C  
ATOM    823  CG  GLU B  16      28.872  40.409   5.911  1.00 64.23           C  
ATOM    824  CD  GLU B  16      27.494  40.152   5.241  1.00 69.21           C  
ATOM    825  OE1 GLU B  16      27.252  40.685   4.140  1.00 67.75           O  
ATOM    826  OE2 GLU B  16      26.653  39.409   5.831  1.00 77.15           O  
ATOM    827  N   ASN B  17      31.428  40.518   7.915  1.00 56.50           N  
ATOM    828  CA  ASN B  17      31.472  41.053   9.280  1.00 55.36           C  
ATOM    829  C   ASN B  17      32.799  41.040   9.926  1.00 52.11           C  
ATOM    830  O   ASN B  17      32.870  41.340  11.126  1.00 51.30           O  
ATOM    831  CB  ASN B  17      30.537  40.308  10.216  1.00 51.88           C  
ATOM    832  CG  ASN B  17      29.137  40.421   9.765  1.00 55.71           C  
ATOM    833  OD1 ASN B  17      28.364  39.436   9.795  1.00 57.92           O  
ATOM    834  ND2 ASN B  17      28.778  41.629   9.296  1.00 53.26           N  
ATOM    835  N   ILE B  18      33.836  40.693   9.169  1.00 48.82           N  
ATOM    836  CA  ILE B  18      35.178  40.653   9.756  1.00 53.49           C  
ATOM    837  C   ILE B  18      35.742  42.028   9.527  1.00 54.83           C  
ATOM    838  O   ILE B  18      35.986  42.476   8.365  1.00 50.50           O  
ATOM    839  CB  ILE B  18      36.126  39.610   9.084  1.00 47.84           C  
ATOM    840  CG1 ILE B  18      35.515  38.203   9.215  1.00 48.77           C  
ATOM    841  CG2 ILE B  18      37.550  39.714   9.719  1.00 42.00           C  
ATOM    842  CD1 ILE B  18      36.380  37.010   8.590  1.00 41.61           C  
ATOM    843  N   LYS B  19      35.938  42.719  10.640  1.00 60.51           N  
ATOM    844  CA  LYS B  19      36.364  44.089  10.520  1.00 60.03           C  
ATOM    845  C   LYS B  19      37.793  44.323  10.915  1.00 60.90           C  
ATOM    846  O   LYS B  19      38.346  43.630  11.774  1.00 59.89           O  
ATOM    847  CB  LYS B  19      35.369  44.992  11.263  1.00 55.28           C  
ATOM    848  CG  LYS B  19      34.373  45.657  10.231  1.00 59.99           C  
ATOM    849  CD  LYS B  19      32.988  44.997  10.049  1.00 57.61           C  
ATOM    850  CE  LYS B  19      32.498  45.287   8.622  1.00 67.09           C  
ATOM    851  NZ  LYS B  19      31.071  45.705   8.519  1.00 66.58           N  
ATOM    852  N   GLY B  20      38.415  45.281  10.240  1.00 63.19           N  
ATOM    853  CA  GLY B  20      39.718  45.740  10.707  1.00 61.09           C  
ATOM    854  C   GLY B  20      40.947  44.994  10.236  1.00 58.63           C  
ATOM    855  O   GLY B  20      42.006  45.126  10.831  1.00 58.42           O  
ATOM    856  N   LEU B  21      40.834  44.231   9.158  1.00 58.78           N  
ATOM    857  CA  LEU B  21      41.971  43.492   8.638  1.00 53.29           C  
ATOM    858  C   LEU B  21      42.034  43.730   7.153  1.00 56.85           C  
ATOM    859  O   LEU B  21      42.778  43.047   6.420  1.00 59.79           O  
ATOM    860  CB  LEU B  21      41.781  42.016   8.921  1.00 54.82           C  
ATOM    861  CG  LEU B  21      41.742  41.689  10.412  1.00 54.32           C  
ATOM    862  CD1 LEU B  21      41.519  40.177  10.580  1.00 52.71           C  
ATOM    863  CD2 LEU B  21      43.072  42.109  11.047  1.00 44.82           C  
ATOM    864  N   GLY B  22      41.242  44.699   6.692  1.00 53.35           N  
ATOM    865  CA  GLY B  22      41.288  45.050   5.287  1.00 47.00           C  
ATOM    866  C   GLY B  22      40.289  44.241   4.524  1.00 49.22           C  
ATOM    867  O   GLY B  22      39.398  43.615   5.111  1.00 53.69           O  
ATOM    868  N   ASP B  23      40.397  44.256   3.210  1.00 51.88           N  
ATOM    869  CA  ASP B  23      39.529  43.426   2.395  1.00 55.20           C  
ATOM    870  C   ASP B  23      40.026  42.011   2.478  1.00 55.81           C  
ATOM    871  O   ASP B  23      41.233  41.745   2.431  1.00 49.00           O  
ATOM    872  CB  ASP B  23      39.544  43.884   0.938  1.00 66.44           C  
ATOM    873  CG  ASP B  23      38.758  45.200   0.728  1.00 83.73           C  
ATOM    874  OD1 ASP B  23      37.773  45.465   1.496  1.00 82.20           O  
ATOM    875  OD2 ASP B  23      39.131  45.966  -0.217  1.00 89.89           O  
ATOM    876  N   LEU B  24      39.077  41.102   2.588  1.00 48.20           N  
ATOM    877  CA  LEU B  24      39.411  39.728   2.886  1.00 46.52           C  
ATOM    878  C   LEU B  24      38.708  38.840   1.878  1.00 49.64           C  
ATOM    879  O   LEU B  24      37.587  39.147   1.440  1.00 55.86           O  
ATOM    880  CB  LEU B  24      38.945  39.379   4.285  1.00 34.32           C  
ATOM    881  CG  LEU B  24      39.662  39.977   5.443  1.00 39.14           C  
ATOM    882  CD1 LEU B  24      39.152  39.254   6.682  1.00 40.04           C  
ATOM    883  CD2 LEU B  24      41.168  39.772   5.294  1.00 35.39           C  
ATOM    884  N   LYS B  25      39.339  37.730   1.515  1.00 45.69           N  
ATOM    885  CA  LYS B  25      38.630  36.750   0.715  1.00 45.46           C  
ATOM    886  C   LYS B  25      38.802  35.377   1.213  1.00 41.97           C  
ATOM    887  O   LYS B  25      39.881  34.973   1.699  1.00 46.90           O  
ATOM    888  CB  LYS B  25      39.078  36.788  -0.748  1.00 51.30           C  
ATOM    889  CG  LYS B  25      38.424  37.943  -1.509  1.00 63.55           C  
ATOM    890  CD  LYS B  25      38.791  38.004  -2.983  1.00 76.42           C  
ATOM    891  CE  LYS B  25      37.829  38.946  -3.771  1.00 84.32           C  
ATOM    892  NZ  LYS B  25      37.299  38.250  -5.049  1.00 95.27           N  
ATOM    893  N   PRO B  26      37.730  34.622   1.135  1.00 37.62           N  
ATOM    894  CA  PRO B  26      37.896  33.254   1.612  1.00 38.64           C  
ATOM    895  C   PRO B  26      39.053  32.566   0.815  1.00 36.37           C  
ATOM    896  O   PRO B  26      39.255  32.838  -0.396  1.00 38.68           O  
ATOM    897  CB  PRO B  26      36.541  32.640   1.300  1.00 39.71           C  
ATOM    898  CG  PRO B  26      35.598  33.830   1.271  1.00 35.51           C  
ATOM    899  CD  PRO B  26      36.408  34.842   0.546  1.00 32.79           C  
ATOM    900  N   GLY B  27      39.832  31.693   1.467  1.00 38.97           N  
ATOM    901  CA  GLY B  27      40.827  30.884   0.716  1.00 32.74           C  
ATOM    902  C   GLY B  27      40.408  29.413   0.826  1.00 39.18           C  
ATOM    903  O   GLY B  27      39.673  29.026   1.747  1.00 34.50           O  
ATOM    904  N   ILE B  28      40.833  28.588  -0.115  1.00 39.84           N  
ATOM    905  CA  ILE B  28      40.683  27.160   0.063  1.00 37.88           C  
ATOM    906  C   ILE B  28      41.154  26.708   1.459  1.00 39.98           C  
ATOM    907  O   ILE B  28      42.296  26.924   1.852  1.00 40.98           O  
ATOM    908  CB  ILE B  28      41.475  26.356  -1.008  1.00 44.52           C  
ATOM    909  CG1 ILE B  28      40.997  26.745  -2.421  1.00 37.87           C  
ATOM    910  CG2 ILE B  28      41.319  24.809  -0.710  1.00 33.95           C  
ATOM    911  CD1 ILE B  28      41.610  25.886  -3.572  1.00 36.12           C  
ATOM    912  N   PRO B  29      40.255  26.073   2.214  1.00 36.84           N  
ATOM    913  CA  PRO B  29      40.548  25.589   3.567  1.00 37.32           C  
ATOM    914  C   PRO B  29      41.398  24.303   3.504  1.00 38.09           C  
ATOM    915  O   PRO B  29      41.165  23.497   2.636  1.00 43.65           O  
ATOM    916  CB  PRO B  29      39.155  25.411   4.178  1.00 31.99           C  
ATOM    917  CG  PRO B  29      38.299  25.027   2.992  1.00 23.43           C  
ATOM    918  CD  PRO B  29      38.921  25.638   1.736  1.00 28.22           C  
ATOM    919  N   LYS B  30      42.447  24.198   4.341  1.00 42.76           N  
ATOM    920  CA  LYS B  30      43.432  23.095   4.254  1.00 44.72           C  
ATOM    921  C   LYS B  30      43.964  22.540   5.597  1.00 50.19           C  
ATOM    922  O   LYS B  30      44.677  21.525   5.603  1.00 55.24           O  
ATOM    923  CB  LYS B  30      44.646  23.492   3.419  1.00 34.79           C  
ATOM    924  CG  LYS B  30      44.327  23.927   2.005  1.00 39.60           C  
ATOM    925  CD  LYS B  30      45.616  24.143   1.182  1.00 37.91           C  
ATOM    926  CE  LYS B  30      45.215  24.556  -0.230  1.00 45.50           C  
ATOM    927  NZ  LYS B  30      46.390  24.783  -1.121  1.00 46.81           N  
ATOM    928  N   THR B  31      43.637  23.176   6.718  1.00 48.01           N  
ATOM    929  CA  THR B  31      44.183  22.781   8.021  1.00 44.90           C  
ATOM    930  C   THR B  31      43.159  21.854   8.719  1.00 50.19           C  
ATOM    931  O   THR B  31      42.041  22.277   9.127  1.00 45.07           O  
ATOM    932  CB  THR B  31      44.387  23.993   8.877  1.00 39.84           C  
ATOM    933  OG1 THR B  31      45.177  24.944   8.168  1.00 42.43           O  
ATOM    934  CG2 THR B  31      45.007  23.605  10.164  1.00 32.00           C  
ATOM    935  N   PRO B  32      43.544  20.580   8.890  1.00 48.60           N  
ATOM    936  CA  PRO B  32      42.741  19.512   9.501  1.00 44.91           C  
ATOM    937  C   PRO B  32      42.631  19.805  10.928  1.00 47.48           C  
ATOM    938  O   PRO B  32      43.544  20.406  11.476  1.00 53.73           O  
ATOM    939  CB  PRO B  32      43.580  18.269   9.275  1.00 48.63           C  
ATOM    940  CG  PRO B  32      44.556  18.668   8.174  1.00 48.18           C  
ATOM    941  CD  PRO B  32      44.870  20.091   8.493  1.00 49.94           C  
ATOM    942  N   LYS B  33      41.532  19.397  11.541  1.00 46.16           N  
ATOM    943  CA  LYS B  33      41.565  19.071  12.946  1.00 54.95           C  
ATOM    944  C   LYS B  33      41.764  17.571  13.251  1.00 56.54           C  
ATOM    945  O   LYS B  33      41.492  16.708  12.415  1.00 58.71           O  
ATOM    946  CB  LYS B  33      40.319  19.628  13.622  1.00 57.63           C  
ATOM    947  CG  LYS B  33      40.398  21.177  13.642  1.00 68.17           C  
ATOM    948  CD  LYS B  33      39.864  21.819  14.955  1.00 66.99           C  
ATOM    949  CE  LYS B  33      40.936  22.021  15.992  1.00 58.97           C  
ATOM    950  NZ  LYS B  33      40.363  21.923  17.387  1.00 60.49           N  
ATOM    951  N   GLN B  34      42.267  17.252  14.443  1.00 56.93           N  
ATOM    952  CA  GLN B  34      42.334  15.846  14.843  1.00 63.30           C  
ATOM    953  C   GLN B  34      40.969  15.196  15.123  1.00 64.49           C  
ATOM    954  O   GLN B  34      40.721  14.087  14.659  1.00 72.21           O  
ATOM    955  CB  GLN B  34      43.262  15.693  16.046  1.00 62.63           C  
ATOM    956  CG  GLN B  34      44.385  14.670  15.811  1.00 62.60           C  
ATOM    957  CD  GLN B  34      45.268  15.011  14.613  1.00 66.78           C  
ATOM    958  OE1 GLN B  34      45.454  14.178  13.718  1.00 74.71           O  
ATOM    959  NE2 GLN B  34      45.819  16.237  14.586  1.00 71.64           N  
ATOM    960  N   ASN B  35      40.087  15.903  15.846  1.00 68.39           N  
ATOM    961  CA  ASN B  35      38.665  15.522  16.000  1.00 71.56           C  
ATOM    962  C   ASN B  35      37.682  16.363  15.187  1.00 75.34           C  
ATOM    963  O   ASN B  35      37.557  17.575  15.403  1.00 76.66           O  
ATOM    964  CB  ASN B  35      38.269  15.605  17.458  1.00 75.37           C  
ATOM    965  CG  ASN B  35      38.938  14.515  18.291  1.00 87.12           C  
ATOM    966  OD1 ASN B  35      40.114  14.628  18.671  1.00 90.11           O  
ATOM    967  ND2 ASN B  35      38.199  13.432  18.554  1.00 91.51           N  
ATOM    968  N   GLY B  36      36.971  15.719  14.264  1.00 73.37           N  
ATOM    969  CA  GLY B  36      36.300  16.467  13.222  1.00 66.37           C  
ATOM    970  C   GLY B  36      36.870  16.077  11.860  1.00 68.34           C  
ATOM    971  O   GLY B  36      38.106  15.799  11.730  1.00 70.98           O  
ATOM    972  N   GLY B  37      35.985  16.046  10.845  1.00 61.79           N  
ATOM    973  CA  GLY B  37      36.392  15.811   9.458  1.00 51.33           C  
ATOM    974  C   GLY B  37      36.695  17.094   8.684  1.00 56.04           C  
ATOM    975  O   GLY B  37      37.223  17.033   7.531  1.00 49.26           O  
ATOM    976  N   GLY B  38      36.419  18.252   9.332  1.00 52.33           N  
ATOM    977  CA  GLY B  38      36.523  19.544   8.649  1.00 54.54           C  
ATOM    978  C   GLY B  38      37.901  20.181   8.530  1.00 47.32           C  
ATOM    979  O   GLY B  38      38.774  19.931   9.356  1.00 51.24           O  
ATOM    980  N   LYS B  39      38.096  21.004   7.497  1.00 45.03           N  
ATOM    981  CA  LYS B  39      39.212  21.939   7.458  1.00 36.43           C  
ATOM    982  C   LYS B  39      38.801  23.373   7.889  1.00 37.55           C  
ATOM    983  O   LYS B  39      37.659  23.877   7.658  1.00 39.72           O  
ATOM    984  CB  LYS B  39      39.830  21.898   6.077  1.00 40.41           C  
ATOM    985  CG  LYS B  39      40.547  20.573   5.810  1.00 36.83           C  
ATOM    986  CD  LYS B  39      40.821  20.474   4.340  1.00 52.12           C  
ATOM    987  CE  LYS B  39      40.799  19.039   3.759  1.00 60.88           C  
ATOM    988  NZ  LYS B  39      40.460  19.126   2.253  1.00 57.39           N  
ATOM    989  N   ARG B  40      39.728  24.006   8.591  1.00 37.19           N  
ATOM    990  CA  ARG B  40      39.453  25.273   9.280  1.00 35.51           C  
ATOM    991  C   ARG B  40      39.122  26.318   8.196  1.00 34.10           C  
ATOM    992  O   ARG B  40      39.745  26.338   7.119  1.00 34.01           O  
ATOM    993  CB  ARG B  40      40.678  25.666  10.112  1.00 33.65           C  
ATOM    994  CG  ARG B  40      40.457  25.510  11.572  1.00 42.87           C  
ATOM    995  CD  ARG B  40      41.680  25.724  12.472  1.00 41.73           C  
ATOM    996  NE  ARG B  40      42.843  26.346  11.845  1.00 50.00           N  
ATOM    997  CZ  ARG B  40      43.876  26.838  12.550  1.00 53.43           C  
ATOM    998  NH1 ARG B  40      43.889  26.777  13.883  1.00 37.63           N  
ATOM    999  NH2 ARG B  40      44.895  27.401  11.922  1.00 44.00           N  
ATOM   1000  N   LYS B  41      38.101  27.128   8.438  1.00 37.31           N  
ATOM   1001  CA  LYS B  41      37.736  28.144   7.470  1.00 35.66           C  
ATOM   1002  C   LYS B  41      38.908  29.095   7.325  1.00 38.63           C  
ATOM   1003  O   LYS B  41      39.634  29.379   8.302  1.00 43.40           O  
ATOM   1004  CB  LYS B  41      36.562  28.902   7.948  1.00 39.16           C  
ATOM   1005  CG  LYS B  41      35.282  28.203   7.688  1.00 38.62           C  
ATOM   1006  CD  LYS B  41      34.170  29.176   8.005  1.00 45.50           C  
ATOM   1007  CE  LYS B  41      32.883  28.473   8.458  1.00 43.61           C  
ATOM   1008  NZ  LYS B  41      31.702  28.985   7.702  1.00 40.50           N  
ATOM   1009  N   ARG B  42      39.142  29.536   6.101  1.00 37.29           N  
ATOM   1010  CA  ARG B  42      40.316  30.337   5.795  1.00 38.36           C  
ATOM   1011  C   ARG B  42      40.005  31.607   4.957  1.00 41.52           C  
ATOM   1012  O   ARG B  42      39.138  31.589   4.056  1.00 36.95           O  
ATOM   1013  CB  ARG B  42      41.350  29.459   5.076  1.00 38.46           C  
ATOM   1014  CG  ARG B  42      42.611  30.186   4.748  1.00 44.46           C  
ATOM   1015  CD  ARG B  42      43.560  29.331   3.977  1.00 33.81           C  
ATOM   1016  NE  ARG B  42      44.283  28.467   4.900  1.00 45.66           N  
ATOM   1017  CZ  ARG B  42      45.243  27.617   4.543  1.00 36.62           C  
ATOM   1018  NH1 ARG B  42      45.633  27.518   3.282  1.00 36.62           N  
ATOM   1019  NH2 ARG B  42      45.749  26.809   5.439  1.00 40.02           N  
ATOM   1020  N   TRP B  43      40.733  32.692   5.249  1.00 42.00           N  
ATOM   1021  CA  TRP B  43      40.640  33.944   4.479  1.00 35.02           C  
ATOM   1022  C   TRP B  43      42.040  34.465   4.178  1.00 40.76           C  
ATOM   1023  O   TRP B  43      42.986  34.250   4.977  1.00 37.61           O  
ATOM   1024  CB  TRP B  43      39.913  35.009   5.299  1.00 41.15           C  
ATOM   1025  CG  TRP B  43      38.445  34.791   5.516  1.00 29.15           C  
ATOM   1026  CD1 TRP B  43      37.408  35.240   4.743  1.00 39.95           C  
ATOM   1027  CD2 TRP B  43      37.864  34.122   6.617  1.00 34.01           C  
ATOM   1028  NE1 TRP B  43      36.161  34.883   5.322  1.00 37.01           N  
ATOM   1029  CE2 TRP B  43      36.437  34.202   6.477  1.00 32.85           C  
ATOM   1030  CE3 TRP B  43      38.407  33.453   7.737  1.00 36.42           C  
ATOM   1031  CZ2 TRP B  43      35.567  33.640   7.413  1.00 36.62           C  
ATOM   1032  CZ3 TRP B  43      37.539  32.897   8.650  1.00 38.79           C  
ATOM   1033  CH2 TRP B  43      36.125  32.994   8.486  1.00 34.13           C  
ATOM   1034  N   THR B  44      42.184  35.155   3.049  1.00 40.64           N  
ATOM   1035  CA  THR B  44      43.408  35.881   2.781  1.00 36.15           C  
ATOM   1036  C   THR B  44      43.150  37.347   2.851  1.00 41.43           C  
ATOM   1037  O   THR B  44      42.052  37.827   2.552  1.00 47.29           O  
ATOM   1038  CB  THR B  44      43.989  35.566   1.412  1.00 41.91           C  
ATOM   1039  OG1 THR B  44      43.043  35.933   0.421  1.00 46.10           O  
ATOM   1040  CG2 THR B  44      44.253  34.046   1.254  1.00 44.54           C  
ATOM   1041  N   GLY B  45      44.160  38.077   3.290  1.00 46.76           N  
ATOM   1042  CA  GLY B  45      44.104  39.523   3.207  1.00 45.04           C  
ATOM   1043  C   GLY B  45      45.467  40.037   2.743  1.00 52.94           C  
ATOM   1044  O   GLY B  45      46.405  39.226   2.561  1.00 37.18           O  
ATOM   1045  N   ASP B  46      45.568  41.371   2.536  1.00 52.18           N  
ATOM   1046  CA  ASP B  46      46.821  42.039   2.173  1.00 46.34           C  
ATOM   1047  C   ASP B  46      47.419  41.356   0.904  1.00 47.25           C  
ATOM   1048  O   ASP B  46      48.577  40.873   0.848  1.00 46.31           O  
ATOM   1049  CB  ASP B  46      47.763  42.018   3.406  1.00 48.28           C  
ATOM   1050  CG  ASP B  46      48.984  42.889   3.236  1.00 60.43           C  
ATOM   1051  OD1 ASP B  46      48.968  43.738   2.323  1.00 68.55           O  
ATOM   1052  OD2 ASP B  46      49.965  42.748   4.012  1.00 63.77           O  
ATOM   1053  N   LYS B  47      46.591  41.331  -0.127  1.00 41.81           N  
ATOM   1054  CA  LYS B  47      46.982  40.758  -1.408  1.00 51.43           C  
ATOM   1055  C   LYS B  47      47.391  39.313  -1.283  1.00 53.41           C  
ATOM   1056  O   LYS B  47      48.196  38.817  -2.076  1.00 57.30           O  
ATOM   1057  CB  LYS B  47      48.128  41.556  -2.029  1.00 52.87           C  
ATOM   1058  CG  LYS B  47      47.798  43.047  -2.239  1.00 53.19           C  
ATOM   1059  CD  LYS B  47      46.553  43.249  -3.124  1.00 52.48           C  
ATOM   1060  CE  LYS B  47      46.197  44.740  -3.294  1.00 49.11           C  
ATOM   1061  NZ  LYS B  47      44.904  44.909  -4.085  1.00 47.58           N  
ATOM   1062  N   GLY B  48      46.820  38.620  -0.299  1.00 54.03           N  
ATOM   1063  CA  GLY B  48      47.226  37.241  -0.083  1.00 49.42           C  
ATOM   1064  C   GLY B  48      48.502  37.009   0.736  1.00 47.18           C  
ATOM   1065  O   GLY B  48      48.976  35.877   0.825  1.00 48.39           O  
ATOM   1066  N   ARG B  49      49.058  38.048   1.340  1.00 41.86           N  
ATOM   1067  CA  ARG B  49      50.318  37.933   2.090  1.00 49.57           C  
ATOM   1068  C   ARG B  49      49.995  37.465   3.493  1.00 49.37           C  
ATOM   1069  O   ARG B  49      50.839  36.886   4.185  1.00 40.53           O  
ATOM   1070  CB  ARG B  49      51.036  39.297   2.196  1.00 48.08           C  
ATOM   1071  CG  ARG B  49      51.905  39.636   0.999  1.00 50.60           C  
ATOM   1072  CD  ARG B  49      52.706  40.950   1.239  1.00 60.65           C  
ATOM   1073  NE  ARG B  49      51.860  42.127   1.026  1.00 58.44           N  
ATOM   1074  CZ  ARG B  49      51.727  42.707  -0.160  1.00 63.31           C  
ATOM   1075  NH1 ARG B  49      52.427  42.207  -1.180  1.00 55.10           N  
ATOM   1076  NH2 ARG B  49      50.837  43.702  -0.345  1.00 57.65           N  
ATOM   1077  N   LYS B  50      48.758  37.764   3.904  1.00 43.07           N  
ATOM   1078  CA  LYS B  50      48.203  37.317   5.170  1.00 47.84           C  
ATOM   1079  C   LYS B  50      47.057  36.273   5.023  1.00 50.97           C  
ATOM   1080  O   LYS B  50      46.131  36.403   4.164  1.00 43.02           O  
ATOM   1081  CB  LYS B  50      47.706  38.537   5.964  1.00 46.55           C  
ATOM   1082  CG  LYS B  50      48.856  39.309   6.580  1.00 49.86           C  
ATOM   1083  CD  LYS B  50      48.410  40.582   7.302  1.00 66.02           C  
ATOM   1084  CE  LYS B  50      49.633  41.480   7.656  1.00 66.95           C  
ATOM   1085  NZ  LYS B  50      49.121  42.861   7.917  1.00 72.02           N  
ATOM   1086  N   ILE B  51      47.124  35.258   5.892  1.00 51.90           N  
ATOM   1087  CA  ILE B  51      46.097  34.212   6.007  1.00 39.67           C  
ATOM   1088  C   ILE B  51      45.486  34.243   7.381  1.00 38.32           C  
ATOM   1089  O   ILE B  51      46.193  34.277   8.425  1.00 35.31           O  
ATOM   1090  CB  ILE B  51      46.735  32.828   5.791  1.00 40.49           C  
ATOM   1091  CG1 ILE B  51      47.147  32.702   4.327  1.00 41.51           C  
ATOM   1092  CG2 ILE B  51      45.759  31.705   6.085  1.00 37.16           C  
ATOM   1093  CD1 ILE B  51      47.925  31.382   4.006  1.00 35.14           C  
ATOM   1094  N   TYR B  52      44.165  34.159   7.406  1.00 37.02           N  
ATOM   1095  CA  TYR B  52      43.501  33.979   8.697  1.00 40.19           C  
ATOM   1096  C   TYR B  52      42.634  32.744   8.741  1.00 40.31           C  
ATOM   1097  O   TYR B  52      41.978  32.419   7.728  1.00 39.46           O  
ATOM   1098  CB  TYR B  52      42.638  35.197   9.011  1.00 43.30           C  
ATOM   1099  CG  TYR B  52      43.401  36.488   8.925  1.00 45.16           C  
ATOM   1100  CD1 TYR B  52      44.026  37.024  10.060  1.00 43.81           C  
ATOM   1101  CD2 TYR B  52      43.430  37.229   7.736  1.00 52.14           C  
ATOM   1102  CE1 TYR B  52      44.655  38.277  10.027  1.00 53.61           C  
ATOM   1103  CE2 TYR B  52      44.080  38.513   7.685  1.00 53.76           C  
ATOM   1104  CZ  TYR B  52      44.695  39.017   8.839  1.00 56.49           C  
ATOM   1105  OH  TYR B  52      45.439  40.177   8.796  1.00 59.40           O  
ATOM   1106  N   GLU B  53      42.585  32.087   9.908  1.00 41.47           N  
ATOM   1107  CA  GLU B  53      41.840  30.848  10.050  1.00 42.59           C  
ATOM   1108  C   GLU B  53      40.989  30.972  11.279  1.00 45.42           C  
ATOM   1109  O   GLU B  53      41.461  31.433  12.311  1.00 35.41           O  
ATOM   1110  CB  GLU B  53      42.788  29.632  10.154  1.00 35.64           C  
ATOM   1111  CG  GLU B  53      43.649  29.537   8.916  1.00 40.33           C  
ATOM   1112  CD  GLU B  53      44.025  28.101   8.557  1.00 50.30           C  
ATOM   1113  OE1 GLU B  53      44.378  27.318   9.479  1.00 45.26           O  
ATOM   1114  OE2 GLU B  53      43.980  27.770   7.344  1.00 48.46           O  
ATOM   1115  N   TRP B  54      39.716  30.581  11.150  1.00 41.38           N  
ATOM   1116  CA  TRP B  54      38.842  30.574  12.308  1.00 42.38           C  
ATOM   1117  C   TRP B  54      39.199  29.476  13.300  1.00 41.22           C  
ATOM   1118  O   TRP B  54      39.217  28.313  12.940  1.00 41.06           O  
ATOM   1119  CB  TRP B  54      37.400  30.332  11.907  1.00 37.56           C  
ATOM   1120  CG  TRP B  54      36.515  30.435  13.110  1.00 40.01           C  
ATOM   1121  CD1 TRP B  54      35.607  29.532  13.528  1.00 41.32           C  
ATOM   1122  CD2 TRP B  54      36.315  31.614  13.913  1.00 49.56           C  
ATOM   1123  NE1 TRP B  54      34.821  30.067  14.531  1.00 40.04           N  
ATOM   1124  CE2 TRP B  54      35.231  31.344  14.787  1.00 41.69           C  
ATOM   1125  CE3 TRP B  54      36.935  32.885  13.959  1.00 44.92           C  
ATOM   1126  CZ2 TRP B  54      34.740  32.297  15.720  1.00 45.15           C  
ATOM   1127  CZ3 TRP B  54      36.451  33.850  14.891  1.00 48.52           C  
ATOM   1128  CH2 TRP B  54      35.356  33.544  15.758  1.00 37.29           C  
ATOM   1129  N   ASP B  55      39.444  29.815  14.551  1.00 40.46           N  
ATOM   1130  CA  ASP B  55      39.614  28.760  15.540  1.00 44.41           C  
ATOM   1131  C   ASP B  55      38.286  28.688  16.349  1.00 45.70           C  
ATOM   1132  O   ASP B  55      37.919  29.640  17.118  1.00 36.34           O  
ATOM   1133  CB  ASP B  55      40.855  29.081  16.426  1.00 45.87           C  
ATOM   1134  CG  ASP B  55      40.869  28.360  17.793  1.00 50.60           C  
ATOM   1135  OD1 ASP B  55      39.915  27.622  18.223  1.00 51.70           O  
ATOM   1136  OD2 ASP B  55      41.882  28.566  18.474  1.00 54.68           O  
ATOM   1137  N   SER B  56      37.558  27.575  16.178  1.00 44.60           N  
ATOM   1138  CA  SER B  56      36.168  27.562  16.654  1.00 42.91           C  
ATOM   1139  C   SER B  56      36.037  27.128  18.119  1.00 47.07           C  
ATOM   1140  O   SER B  56      34.987  27.360  18.735  1.00 48.64           O  
ATOM   1141  CB  SER B  56      35.295  26.686  15.755  1.00 45.45           C  
ATOM   1142  OG  SER B  56      35.745  25.335  15.815  1.00 55.08           O  
ATOM   1143  N   GLN B  57      37.092  26.543  18.685  1.00 49.92           N  
ATOM   1144  CA  GLN B  57      37.155  26.379  20.152  1.00 52.10           C  
ATOM   1145  C   GLN B  57      37.435  27.693  20.893  1.00 49.81           C  
ATOM   1146  O   GLN B  57      36.698  28.042  21.809  1.00 43.90           O  
ATOM   1147  CB  GLN B  57      38.206  25.349  20.583  1.00 57.18           C  
ATOM   1148  CG  GLN B  57      38.191  23.994  19.833  1.00 66.31           C  
ATOM   1149  CD  GLN B  57      39.213  22.998  20.475  1.00 83.83           C  
ATOM   1150  OE1 GLN B  57      39.518  21.897  19.916  1.00 81.00           O  
ATOM   1151  NE2 GLN B  57      39.750  23.389  21.662  1.00 81.58           N  
ATOM   1152  N   HIS B  58      38.460  28.462  20.511  1.00 49.75           N  
ATOM   1153  CA  HIS B  58      38.658  29.703  21.240  1.00 46.11           C  
ATOM   1154  C   HIS B  58      37.741  30.811  20.762  1.00 48.52           C  
ATOM   1155  O   HIS B  58      37.452  31.756  21.523  1.00 50.09           O  
ATOM   1156  CB  HIS B  58      40.102  30.136  21.169  1.00 54.61           C  
ATOM   1157  CG  HIS B  58      41.046  29.146  21.778  1.00 66.71           C  
ATOM   1158  ND1 HIS B  58      41.260  27.891  21.238  1.00 76.29           N  
ATOM   1159  CD2 HIS B  58      41.849  29.224  22.869  1.00 71.39           C  
ATOM   1160  CE1 HIS B  58      42.155  27.241  21.968  1.00 75.11           C  
ATOM   1161  NE2 HIS B  58      42.530  28.027  22.961  1.00 70.15           N  
ATOM   1162  N   GLY B  59      37.261  30.691  19.505  1.00 49.80           N  
ATOM   1163  CA  GLY B  59      36.436  31.736  18.896  1.00 40.21           C  
ATOM   1164  C   GLY B  59      37.199  33.001  18.520  1.00 43.81           C  
ATOM   1165  O   GLY B  59      36.760  34.060  18.874  1.00 46.46           O  
ATOM   1166  N   GLU B  60      38.319  32.881  17.804  1.00 45.63           N  
ATOM   1167  CA  GLU B  60      39.115  34.007  17.322  1.00 50.46           C  
ATOM   1168  C   GLU B  60      39.806  33.658  15.967  1.00 48.09           C  
ATOM   1169  O   GLU B  60      39.904  32.486  15.600  1.00 47.89           O  
ATOM   1170  CB  GLU B  60      40.181  34.324  18.362  1.00 55.85           C  
ATOM   1171  CG  GLU B  60      41.111  33.175  18.556  1.00 63.23           C  
ATOM   1172  CD  GLU B  60      41.896  33.188  19.896  1.00 78.58           C  
ATOM   1173  OE1 GLU B  60      41.660  34.095  20.787  1.00 76.12           O  
ATOM   1174  OE2 GLU B  60      42.754  32.247  20.021  1.00 72.83           O  
ATOM   1175  N   LEU B  61      40.236  34.666  15.203  1.00 48.02           N  
ATOM   1176  CA  LEU B  61      41.016  34.439  14.007  1.00 42.13           C  
ATOM   1177  C   LEU B  61      42.473  34.301  14.353  1.00 46.94           C  
ATOM   1178  O   LEU B  61      43.055  35.190  14.997  1.00 51.01           O  
ATOM   1179  CB  LEU B  61      40.898  35.598  13.070  1.00 48.58           C  
ATOM   1180  CG  LEU B  61      39.569  35.665  12.393  1.00 52.33           C  
ATOM   1181  CD1 LEU B  61      39.518  36.946  11.546  1.00 49.94           C  
ATOM   1182  CD2 LEU B  61      39.379  34.371  11.562  1.00 46.59           C  
ATOM   1183  N   GLU B  62      43.078  33.218  13.889  1.00 43.09           N  
ATOM   1184  CA  GLU B  62      44.510  33.073  13.970  1.00 47.91           C  
ATOM   1185  C   GLU B  62      45.064  33.561  12.674  1.00 47.15           C  
ATOM   1186  O   GLU B  62      44.530  33.225  11.604  1.00 42.81           O  
ATOM   1187  CB  GLU B  62      44.875  31.611  14.224  1.00 55.66           C  
ATOM   1188  CG  GLU B  62      44.019  31.095  15.350  1.00 56.75           C  
ATOM   1189  CD  GLU B  62      44.799  30.346  16.350  1.00 76.68           C  
ATOM   1190  OE1 GLU B  62      45.065  29.147  16.071  1.00 79.28           O  
ATOM   1191  OE2 GLU B  62      45.143  30.952  17.404  1.00 86.75           O  
ATOM   1192  N   GLY B  63      46.108  34.394  12.768  1.00 41.78           N  
ATOM   1193  CA  GLY B  63      46.670  35.008  11.574  1.00 39.95           C  
ATOM   1194  C   GLY B  63      48.034  34.442  11.278  1.00 42.30           C  
ATOM   1195  O   GLY B  63      48.800  34.104  12.181  1.00 41.00           O  
ATOM   1196  N   TYR B  64      48.340  34.314  10.002  1.00 42.91           N  
ATOM   1197  CA  TYR B  64      49.617  33.719   9.609  1.00 45.35           C  
ATOM   1198  C   TYR B  64      50.218  34.481   8.438  1.00 46.08           C  
ATOM   1199  O   TYR B  64      49.500  35.109   7.641  1.00 42.48           O  
ATOM   1200  CB  TYR B  64      49.426  32.241   9.190  1.00 42.92           C  
ATOM   1201  CG  TYR B  64      48.862  31.401  10.299  1.00 50.05           C  
ATOM   1202  CD1 TYR B  64      47.471  31.306  10.481  1.00 38.71           C  
ATOM   1203  CD2 TYR B  64      49.694  30.718  11.184  1.00 45.28           C  
ATOM   1204  CE1 TYR B  64      46.924  30.563  11.478  1.00 44.79           C  
ATOM   1205  CE2 TYR B  64      49.143  29.956  12.209  1.00 44.76           C  
ATOM   1206  CZ  TYR B  64      47.739  29.874  12.348  1.00 50.53           C  
ATOM   1207  OH  TYR B  64      47.126  29.118  13.339  1.00 48.62           O  
ATOM   1208  N   ARG B  65      51.532  34.392   8.332  1.00 50.04           N  
ATOM   1209  CA  ARG B  65      52.237  34.978   7.220  1.00 48.60           C  
ATOM   1210  C   ARG B  65      52.164  33.957   6.119  1.00 46.14           C  
ATOM   1211  O   ARG B  65      52.735  32.864   6.255  1.00 51.29           O  
ATOM   1212  CB  ARG B  65      53.710  35.225   7.580  1.00 53.29           C  
ATOM   1213  CG  ARG B  65      54.463  36.054   6.531  1.00 58.45           C  
ATOM   1214  CD  ARG B  65      55.961  35.895   6.700  1.00 62.74           C  
ATOM   1215  NE  ARG B  65      56.407  36.253   8.049  1.00 69.65           N  
ATOM   1216  CZ  ARG B  65      57.388  35.628   8.703  1.00 73.49           C  
ATOM   1217  NH1 ARG B  65      58.035  34.621   8.139  1.00 75.98           N  
ATOM   1218  NH2 ARG B  65      57.698  35.970   9.944  1.00 79.73           N  
ATOM   1219  N   ALA B  66      51.480  34.295   5.031  1.00 41.82           N  
ATOM   1220  CA  ALA B  66      51.418  33.421   3.868  1.00 42.99           C  
ATOM   1221  C   ALA B  66      52.758  32.894   3.300  1.00 47.93           C  
ATOM   1222  O   ALA B  66      52.832  31.755   2.861  1.00 57.06           O  
ATOM   1223  CB  ALA B  66      50.649  34.083   2.781  1.00 43.07           C  
ATOM   1224  N   SER B  67      53.820  33.675   3.296  1.00 51.44           N  
ATOM   1225  CA  SER B  67      55.058  33.213   2.637  1.00 52.25           C  
ATOM   1226  C   SER B  67      55.633  31.900   3.263  1.00 53.52           C  
ATOM   1227  O   SER B  67      56.107  31.013   2.538  1.00 46.27           O  
ATOM   1228  CB  SER B  67      56.110  34.311   2.753  1.00 53.87           C  
ATOM   1229  OG  SER B  67      56.307  34.626   4.131  1.00 46.20           O  
ATOM   1230  N   ASP B  68      55.586  31.797   4.599  1.00 49.95           N  
ATOM   1231  CA  ASP B  68      56.161  30.650   5.324  1.00 54.07           C  
ATOM   1232  C   ASP B  68      55.215  30.054   6.408  1.00 49.38           C  
ATOM   1233  O   ASP B  68      55.586  29.197   7.227  1.00 50.95           O  
ATOM   1234  CB  ASP B  68      57.458  31.110   5.986  1.00 48.07           C  
ATOM   1235  CG  ASP B  68      57.211  32.096   7.097  1.00 50.81           C  
ATOM   1236  OD1 ASP B  68      56.118  32.760   7.137  1.00 55.06           O  
ATOM   1237  OD2 ASP B  68      58.119  32.196   7.942  1.00 59.45           O  
ATOM   1238  N   GLY B  69      54.005  30.564   6.470  1.00 48.66           N  
ATOM   1239  CA  GLY B  69      53.096  30.036   7.461  1.00 44.36           C  
ATOM   1240  C   GLY B  69      53.251  30.509   8.872  1.00 52.97           C  
ATOM   1241  O   GLY B  69      52.377  30.172   9.713  1.00 53.02           O  
ATOM   1242  N   GLN B  70      54.294  31.298   9.172  1.00 51.55           N  
ATOM   1243  CA  GLN B  70      54.469  31.726  10.552  1.00 44.13           C  
ATOM   1244  C   GLN B  70      53.310  32.388  11.160  1.00 49.99           C  
ATOM   1245  O   GLN B  70      52.640  33.240  10.542  1.00 46.85           O  
ATOM   1246  CB  GLN B  70      55.632  32.647  10.744  1.00 51.40           C  
ATOM   1247  CG  GLN B  70      56.938  31.905  10.898  1.00 69.03           C  
ATOM   1248  CD  GLN B  70      56.963  30.918  12.051  1.00 62.32           C  
ATOM   1249  OE1 GLN B  70      57.520  29.831  11.913  1.00 75.84           O  
ATOM   1250  NE2 GLN B  70      56.379  31.292  13.194  1.00 65.25           N  
ATOM   1251  N   HIS B  71      53.095  32.003  12.413  1.00 49.93           N  
ATOM   1252  CA  HIS B  71      51.985  32.461  13.196  1.00 46.31           C  
ATOM   1253  C   HIS B  71      52.207  33.907  13.575  1.00 48.09           C  
ATOM   1254  O   HIS B  71      53.313  34.292  13.915  1.00 50.23           O  
ATOM   1255  CB  HIS B  71      51.876  31.574  14.451  1.00 41.01           C  
ATOM   1256  CG  HIS B  71      50.966  32.128  15.500  1.00 39.86           C  
ATOM   1257  ND1 HIS B  71      49.625  32.404  15.264  1.00 51.47           N  
ATOM   1258  CD2 HIS B  71      51.190  32.452  16.790  1.00 41.14           C  
ATOM   1259  CE1 HIS B  71      49.073  32.880  16.379  1.00 50.00           C  
ATOM   1260  NE2 HIS B  71      50.006  32.915  17.315  1.00 44.51           N  
ATOM   1261  N   LEU B  72      51.139  34.682  13.590  1.00 47.79           N  
ATOM   1262  CA  LEU B  72      51.216  36.108  13.835  1.00 49.34           C  
ATOM   1263  C   LEU B  72      50.421  36.509  15.079  1.00 57.54           C  
ATOM   1264  O   LEU B  72      50.314  37.702  15.377  1.00 62.70           O  
ATOM   1265  CB  LEU B  72      50.620  36.872  12.642  1.00 42.23           C  
ATOM   1266  CG  LEU B  72      51.272  36.773  11.281  1.00 45.58           C  
ATOM   1267  CD1 LEU B  72      50.474  37.509  10.209  1.00 43.15           C  
ATOM   1268  CD2 LEU B  72      52.651  37.380  11.425  1.00 50.10           C  
ATOM   1269  N   GLY B  73      49.779  35.559  15.751  1.00 53.89           N  
ATOM   1270  CA  GLY B  73      48.831  35.944  16.790  1.00 51.91           C  
ATOM   1271  C   GLY B  73      47.355  35.804  16.414  1.00 49.18           C  
ATOM   1272  O   GLY B  73      47.042  35.280  15.378  1.00 54.51           O  
ATOM   1273  N   SER B  74      46.432  36.251  17.252  1.00 49.21           N  
ATOM   1274  CA  SER B  74      45.027  36.152  16.940  1.00 57.39           C  
ATOM   1275  C   SER B  74      44.358  37.505  16.979  1.00 54.10           C  
ATOM   1276  O   SER B  74      44.934  38.462  17.439  1.00 55.48           O  
ATOM   1277  CB  SER B  74      44.323  35.216  17.906  1.00 54.34           C  
ATOM   1278  OG  SER B  74      44.500  35.705  19.208  1.00 72.07           O  
ATOM   1279  N   PHE B  75      43.156  37.570  16.433  1.00 46.23           N  
ATOM   1280  CA  PHE B  75      42.498  38.806  16.214  1.00 44.95           C  
ATOM   1281  C   PHE B  75      41.027  38.644  16.463  1.00 53.37           C  
ATOM   1282  O   PHE B  75      40.417  37.571  16.247  1.00 55.71           O  
ATOM   1283  CB  PHE B  75      42.778  39.288  14.796  1.00 41.64           C  
ATOM   1284  CG  PHE B  75      44.262  39.304  14.478  1.00 53.31           C  
ATOM   1285  CD1 PHE B  75      44.939  38.115  14.163  1.00 49.38           C  
ATOM   1286  CD2 PHE B  75      45.019  40.460  14.647  1.00 52.22           C  
ATOM   1287  CE1 PHE B  75      46.336  38.061  14.033  1.00 46.03           C  
ATOM   1288  CE2 PHE B  75      46.428  40.408  14.515  1.00 52.49           C  
ATOM   1289  CZ  PHE B  75      47.074  39.198  14.209  1.00 57.72           C  
ATOM   1290  N   ASP B  76      40.455  39.724  16.958  1.00 54.23           N  
ATOM   1291  CA  ASP B  76      39.050  39.753  17.240  1.00 58.94           C  
ATOM   1292  C   ASP B  76      38.462  40.145  15.898  1.00 60.21           C  
ATOM   1293  O   ASP B  76      38.864  41.155  15.300  1.00 52.66           O  
ATOM   1294  CB  ASP B  76      38.785  40.825  18.294  1.00 63.45           C  
ATOM   1295  CG  ASP B  76      37.315  41.076  18.530  1.00 67.03           C  
ATOM   1296  OD1 ASP B  76      36.469  40.332  17.986  1.00 70.33           O  
ATOM   1297  OD2 ASP B  76      37.000  42.043  19.281  1.00 80.38           O  
ATOM   1298  N   PRO B  77      37.524  39.334  15.394  1.00 57.18           N  
ATOM   1299  CA  PRO B  77      36.854  39.567  14.112  1.00 59.86           C  
ATOM   1300  C   PRO B  77      35.964  40.825  14.100  1.00 67.68           C  
ATOM   1301  O   PRO B  77      35.679  41.420  13.021  1.00 66.10           O  
ATOM   1302  CB  PRO B  77      36.072  38.259  13.902  1.00 53.71           C  
ATOM   1303  CG  PRO B  77      35.733  37.876  15.311  1.00 49.46           C  
ATOM   1304  CD  PRO B  77      37.090  38.054  15.967  1.00 50.21           C  
ATOM   1305  N   LYS B  78      35.530  41.243  15.285  1.00 69.05           N  
ATOM   1306  CA  LYS B  78      34.665  42.416  15.349  1.00 73.99           C  
ATOM   1307  C   LYS B  78      35.460  43.718  15.149  1.00 72.94           C  
ATOM   1308  O   LYS B  78      34.989  44.670  14.502  1.00 73.04           O  
ATOM   1309  CB  LYS B  78      33.895  42.421  16.674  1.00 74.35           C  
ATOM   1310  CG  LYS B  78      32.621  41.589  16.609  1.00 77.77           C  
ATOM   1311  CD  LYS B  78      32.034  41.400  17.983  1.00 78.61           C  
ATOM   1312  CE  LYS B  78      32.222  39.938  18.402  1.00 91.50           C  
ATOM   1313  NZ  LYS B  78      33.651  39.405  18.245  1.00 92.08           N  
ATOM   1314  N   THR B  79      36.688  43.724  15.649  1.00 70.05           N  
ATOM   1315  CA  THR B  79      37.490  44.935  15.699  1.00 65.42           C  
ATOM   1316  C   THR B  79      38.693  44.787  14.813  1.00 64.86           C  
ATOM   1317  O   THR B  79      39.123  45.728  14.169  1.00 72.12           O  
ATOM   1318  CB  THR B  79      37.998  45.180  17.116  1.00 68.18           C  
ATOM   1319  OG1 THR B  79      39.088  44.279  17.410  1.00 70.95           O  
ATOM   1320  CG2 THR B  79      36.878  44.928  18.102  1.00 70.01           C  
ATOM   1321  N   GLY B  80      39.270  43.598  14.795  1.00 66.54           N  
ATOM   1322  CA  GLY B  80      40.515  43.418  14.069  1.00 66.06           C  
ATOM   1323  C   GLY B  80      41.729  43.600  14.970  1.00 72.31           C  
ATOM   1324  O   GLY B  80      42.878  43.633  14.474  1.00 68.53           O  
ATOM   1325  N   ASN B  81      41.481  43.715  16.284  1.00 72.97           N  
ATOM   1326  CA  ASN B  81      42.540  43.976  17.256  1.00 72.82           C  
ATOM   1327  C   ASN B  81      43.297  42.723  17.549  1.00 71.04           C  
ATOM   1328  O   ASN B  81      42.688  41.659  17.709  1.00 70.57           O  
ATOM   1329  CB  ASN B  81      41.968  44.444  18.581  1.00 79.85           C  
ATOM   1330  CG  ASN B  81      41.155  45.717  18.455  1.00 88.42           C  
ATOM   1331  OD1 ASN B  81      41.242  46.460  17.446  1.00 87.93           O  
ATOM   1332  ND2 ASN B  81      40.355  45.992  19.492  1.00 84.56           N  
ATOM   1333  N   GLN B  82      44.614  42.849  17.671  1.00 63.22           N  
ATOM   1334  CA  GLN B  82      45.403  41.714  18.103  1.00 62.53           C  
ATOM   1335  C   GLN B  82      44.990  41.312  19.518  1.00 63.30           C  
ATOM   1336  O   GLN B  82      44.766  42.167  20.347  1.00 75.79           O  
ATOM   1337  CB  GLN B  82      46.882  42.034  18.020  1.00 46.93           C  
ATOM   1338  CG  GLN B  82      47.718  40.897  18.246  1.00 57.30           C  
ATOM   1339  CD  GLN B  82      49.001  40.964  17.467  1.00 67.66           C  
ATOM   1340  OE1 GLN B  82      49.087  41.648  16.455  1.00 79.87           O  
ATOM   1341  NE2 GLN B  82      50.014  40.219  17.918  1.00 74.48           N  
ATOM   1342  N   LEU B  83      44.817  40.019  19.763  1.00 65.11           N  
ATOM   1343  CA  LEU B  83      44.457  39.517  21.082  1.00 62.31           C  
ATOM   1344  C   LEU B  83      45.629  38.744  21.664  1.00 63.10           C  
ATOM   1345  O   LEU B  83      46.126  39.099  22.725  1.00 74.14           O  
ATOM   1346  CB  LEU B  83      43.226  38.609  20.997  1.00 59.77           C  
ATOM   1347  CG  LEU B  83      41.992  39.281  20.366  1.00 60.27           C  
ATOM   1348  CD1 LEU B  83      40.830  38.310  20.218  1.00 60.95           C  
ATOM   1349  CD2 LEU B  83      41.564  40.421  21.230  1.00 67.86           C  
ATOM   1350  N   LYS B  84      46.098  37.690  21.005  1.00 61.70           N  
ATOM   1351  CA  LYS B  84      47.328  37.005  21.446  1.00 56.66           C  
ATOM   1352  C   LYS B  84      48.412  37.584  20.535  1.00 56.46           C  
ATOM   1353  O   LYS B  84      48.065  38.240  19.546  1.00 60.16           O  
ATOM   1354  CB  LYS B  84      47.199  35.464  21.272  1.00 66.29           C  
ATOM   1355  CG  LYS B  84      46.065  34.799  22.157  1.00 73.11           C  
ATOM   1356  CD  LYS B  84      45.824  33.287  21.887  1.00 75.80           C  
ATOM   1357  CE  LYS B  84      44.524  32.774  22.566  1.00 74.89           C  
ATOM   1358  NZ  LYS B  84      44.342  31.270  22.378  1.00 75.43           N  
ATOM   1359  N   GLY B  85      49.696  37.387  20.838  1.00 53.81           N  
ATOM   1360  CA  GLY B  85      50.747  37.801  19.907  1.00 51.61           C  
ATOM   1361  C   GLY B  85      51.362  36.601  19.223  1.00 55.65           C  
ATOM   1362  O   GLY B  85      50.912  35.504  19.486  1.00 63.93           O  
ATOM   1363  N   PRO B  86      52.411  36.734  18.397  1.00 59.84           N  
ATOM   1364  CA  PRO B  86      52.992  35.557  17.725  1.00 54.17           C  
ATOM   1365  C   PRO B  86      53.488  34.512  18.670  1.00 52.86           C  
ATOM   1366  O   PRO B  86      53.994  34.826  19.727  1.00 61.63           O  
ATOM   1367  CB  PRO B  86      54.168  36.118  16.905  1.00 56.74           C  
ATOM   1368  CG  PRO B  86      54.002  37.582  16.963  1.00 63.00           C  
ATOM   1369  CD  PRO B  86      53.339  37.869  18.306  1.00 56.36           C  
ATOM   1370  N   ASP B  87      53.354  33.261  18.259  1.00 57.71           N  
ATOM   1371  CA  ASP B  87      53.926  32.128  18.950  1.00 57.62           C  
ATOM   1372  C   ASP B  87      54.873  31.465  17.955  1.00 55.55           C  
ATOM   1373  O   ASP B  87      54.470  30.850  16.966  1.00 57.87           O  
ATOM   1374  CB  ASP B  87      52.800  31.214  19.423  1.00 56.55           C  
ATOM   1375  CG  ASP B  87      53.298  29.939  20.087  1.00 60.51           C  
ATOM   1376  OD1 ASP B  87      54.421  29.423  19.745  1.00 61.01           O  
ATOM   1377  OD2 ASP B  87      52.524  29.442  20.953  1.00 58.87           O  
ATOM   1378  N   PRO B  88      56.168  31.610  18.201  1.00 56.11           N  
ATOM   1379  CA  PRO B  88      57.246  31.062  17.357  1.00 56.66           C  
ATOM   1380  C   PRO B  88      57.118  29.586  17.126  1.00 53.14           C  
ATOM   1381  O   PRO B  88      57.699  29.048  16.188  1.00 49.45           O  
ATOM   1382  CB  PRO B  88      58.532  31.397  18.136  1.00 56.34           C  
ATOM   1383  CG  PRO B  88      58.130  32.562  18.985  1.00 59.08           C  
ATOM   1384  CD  PRO B  88      56.706  32.240  19.418  1.00 57.48           C  
ATOM   1385  N   LYS B  89      56.368  28.901  17.987  1.00 59.22           N  
ATOM   1386  CA  LYS B  89      56.251  27.451  17.820  1.00 59.03           C  
ATOM   1387  C   LYS B  89      55.196  27.031  16.760  1.00 61.24           C  
ATOM   1388  O   LYS B  89      55.243  25.908  16.199  1.00 60.15           O  
ATOM   1389  CB  LYS B  89      55.980  26.836  19.175  1.00 58.28           C  
ATOM   1390  CG  LYS B  89      57.113  27.100  20.140  1.00 59.65           C  
ATOM   1391  CD  LYS B  89      56.953  26.447  21.512  1.00 66.97           C  
ATOM   1392  CE  LYS B  89      57.279  24.940  21.480  1.00 67.77           C  
ATOM   1393  NZ  LYS B  89      57.118  24.395  22.862  1.00 63.43           N  
ATOM   1394  N   ARG B  90      54.312  27.979  16.447  1.00 56.01           N  
ATOM   1395  CA  ARG B  90      53.127  27.738  15.647  1.00 56.42           C  
ATOM   1396  C   ARG B  90      53.245  28.250  14.229  1.00 61.10           C  
ATOM   1397  O   ARG B  90      53.556  29.438  14.018  1.00 62.03           O  
ATOM   1398  CB  ARG B  90      51.977  28.429  16.323  1.00 52.60           C  
ATOM   1399  CG  ARG B  90      51.855  27.829  17.687  1.00 61.19           C  
ATOM   1400  CD  ARG B  90      50.483  27.969  18.196  1.00 65.40           C  
ATOM   1401  NE  ARG B  90      49.529  27.516  17.197  1.00 66.33           N  
ATOM   1402  CZ  ARG B  90      48.269  27.951  17.120  1.00 71.38           C  
ATOM   1403  NH1 ARG B  90      47.824  28.865  18.006  1.00 60.41           N  
ATOM   1404  NH2 ARG B  90      47.451  27.465  16.162  1.00 62.16           N  
ATOM   1405  N   ASN B  91      52.971  27.378  13.259  1.00 54.37           N  
ATOM   1406  CA  ASN B  91      52.826  27.825  11.878  1.00 51.55           C  
ATOM   1407  C   ASN B  91      51.850  26.946  11.068  1.00 50.47           C  
ATOM   1408  O   ASN B  91      51.485  25.882  11.551  1.00 49.90           O  
ATOM   1409  CB  ASN B  91      54.190  27.784  11.218  1.00 43.12           C  
ATOM   1410  CG  ASN B  91      54.692  26.344  11.062  1.00 42.93           C  
ATOM   1411  OD1 ASN B  91      54.252  25.617  10.175  1.00 45.17           O  
ATOM   1412  ND2 ASN B  91      55.585  25.928  11.937  1.00 49.84           N  
ATOM   1413  N   ILE B  92      51.490  27.347   9.835  1.00 43.68           N  
ATOM   1414  CA  ILE B  92      50.668  26.501   8.968  1.00 46.18           C  
ATOM   1415  C   ILE B  92      51.371  26.115   7.676  1.00 47.77           C  
ATOM   1416  O   ILE B  92      50.735  25.881   6.639  1.00 44.22           O  
ATOM   1417  CB  ILE B  92      49.277  27.147   8.636  1.00 42.25           C  
ATOM   1418  CG1 ILE B  92      49.420  28.554   8.007  1.00 47.24           C  
ATOM   1419  CG2 ILE B  92      48.494  27.342   9.907  1.00 40.47           C  
ATOM   1420  CD1 ILE B  92      47.962  29.167   7.485  1.00 35.60           C  
ATOM   1421  N   LYS B  93      52.700  26.026   7.752  1.00 48.66           N  
ATOM   1422  CA  LYS B  93      53.503  25.848   6.552  1.00 50.13           C  
ATOM   1423  C   LYS B  93      53.167  24.591   5.729  1.00 46.36           C  
ATOM   1424  O   LYS B  93      53.299  24.571   4.477  1.00 52.97           O  
ATOM   1425  CB  LYS B  93      54.994  25.870   6.936  1.00 52.31           C  
ATOM   1426  CG  LYS B  93      55.969  25.993   5.719  1.00 57.47           C  
ATOM   1427  CD  LYS B  93      57.397  25.694   6.187  1.00 71.26           C  
ATOM   1428  CE  LYS B  93      58.413  25.485   5.038  1.00 79.65           C  
ATOM   1429  NZ  LYS B  93      59.781  25.056   5.605  1.00 84.61           N  
ATOM   1430  N   LYS B  94      52.742  23.536   6.400  1.00 51.96           N  
ATOM   1431  CA  LYS B  94      52.330  22.310   5.678  1.00 55.43           C  
ATOM   1432  C   LYS B  94      50.908  22.442   5.073  1.00 54.88           C  
ATOM   1433  O   LYS B  94      50.580  21.720   4.144  1.00 58.60           O  
ATOM   1434  CB  LYS B  94      52.390  21.078   6.617  1.00 62.76           C  
ATOM   1435  CG  LYS B  94      51.498  21.213   7.879  1.00 71.84           C  
ATOM   1436  CD  LYS B  94      51.637  20.052   8.933  1.00 76.13           C  
ATOM   1437  CE  LYS B  94      50.952  18.693   8.534  1.00 74.36           C  
ATOM   1438  NZ  LYS B  94      50.999  17.672   9.708  1.00 67.17           N  
ATOM   1439  N   TYR B  95      50.093  23.379   5.579  1.00 46.03           N  
ATOM   1440  CA  TYR B  95      48.763  23.674   5.042  1.00 42.42           C  
ATOM   1441  C   TYR B  95      48.600  24.851   4.084  1.00 49.51           C  
ATOM   1442  O   TYR B  95      47.474  25.281   3.846  1.00 47.40           O  
ATOM   1443  CB  TYR B  95      47.821  23.840   6.207  1.00 37.77           C  
ATOM   1444  CG  TYR B  95      47.963  22.652   7.118  1.00 54.54           C  
ATOM   1445  CD1 TYR B  95      47.931  21.320   6.604  1.00 58.46           C  
ATOM   1446  CD2 TYR B  95      48.146  22.823   8.469  1.00 55.65           C  
ATOM   1447  CE1 TYR B  95      48.086  20.201   7.453  1.00 58.42           C  
ATOM   1448  CE2 TYR B  95      48.301  21.714   9.324  1.00 67.44           C  
ATOM   1449  CZ  TYR B  95      48.271  20.409   8.805  1.00 62.07           C  
ATOM   1450  OH  TYR B  95      48.421  19.364   9.696  1.00 68.65           O  
ATOM   1451  N   LEU B  96      49.696  25.391   3.548  1.00 46.38           N  
ATOM   1452  CA  LEU B  96      49.569  26.556   2.680  1.00 48.65           C  
ATOM   1453  C   LEU B  96      49.002  26.105   1.343  1.00 54.98           C  
ATOM   1454  O   LEU B  96      49.074  24.872   1.149  1.00 62.35           O  
ATOM   1455  CB  LEU B  96      50.940  27.235   2.488  1.00 40.09           C  
ATOM   1456  CG  LEU B  96      51.499  27.931   3.737  1.00 45.46           C  
ATOM   1457  CD1 LEU B  96      52.899  28.491   3.493  1.00 33.11           C  
ATOM   1458  CD2 LEU B  96      50.560  29.032   4.123  1.00 40.52           C  
ATOM   1459  OXT LEU B  96      48.503  26.941   0.514  1.00 56.89           O  
TER    1460      LEU B  96                                                      
HETATM 1461  C1  EDO B 401      34.942  31.653   4.784  1.00 48.55           C  
HETATM 1462  O1  EDO B 401      35.384  30.282   4.060  1.00 45.30           O  
HETATM 1463  C2  EDO B 401      33.619  32.451   4.538  1.00 52.88           C  
HETATM 1464  O2  EDO B 401      32.679  31.656   4.828  1.00 44.71           O  
HETATM 1465  O   HOH A2001      17.879  32.858   9.264  1.00 54.96           O  
HETATM 1466  O   HOH A2002      28.205  33.211  -8.840  1.00 69.36           O  
HETATM 1467  O   HOH A2003      32.547  26.487   2.909  1.00 42.70           O  
HETATM 1468  O   HOH A2004      25.932  10.137   9.632  1.00 68.17           O  
HETATM 1469  O   HOH A2005      30.795  31.169 -10.174  1.00 68.18           O  
HETATM 1470  O   HOH A2006      30.868  36.264  -3.032  1.00 69.88           O  
HETATM 1471  O   HOH A2007      25.508  36.525   2.696  1.00 63.37           O  
HETATM 1472  O   HOH A2008      32.474  37.761  -0.109  1.00 65.19           O  
HETATM 1473  O   HOH A2009      41.223  30.689 -13.807  1.00 89.33           O  
HETATM 1474  O   HOH A2010      37.624  27.577 -12.766  1.00 85.51           O  
HETATM 1475  O   HOH A2011      38.788  19.770 -14.090  1.00 56.05           O  
HETATM 1476  O   HOH A2012      39.885  25.871 -13.894  1.00 73.31           O  
HETATM 1477  O   HOH A2013      41.142  32.246 -11.469  1.00 41.16           O  
HETATM 1478  O   HOH A2014      42.510  29.728  -2.186  1.00 43.96           O  
HETATM 1479  O   HOH A2015      48.547  26.523  -2.765  1.00 59.70           O  
HETATM 1480  O   HOH A2016      44.874  28.156  -1.780  1.00 49.86           O  
HETATM 1481  O   HOH A2017      25.983  10.335  12.988  1.00 64.81           O  
HETATM 1482  O   HOH A2018      29.698  10.322  15.485  1.00 61.22           O  
HETATM 1483  O   HOH A2019      29.912  14.520  24.061  1.00 77.13           O  
HETATM 1484  O   HOH A2020      41.275  34.458  -3.988  1.00 45.04           O  
HETATM 1485  O   HOH A2021      36.675  13.838   0.218  1.00 54.40           O  
HETATM 1486  O   HOH A2022      29.148  34.656  -4.348  1.00 55.43           O  
HETATM 1487  O   HOH A2023      26.456  34.411  -4.574  1.00 75.14           O  
HETATM 1488  O   HOH A2024      26.384  34.860  -0.338  1.00 79.85           O  
HETATM 1489  O   HOH A2025      28.662  35.495   0.924  1.00 57.27           O  
HETATM 1490  O   HOH A2026      33.138  35.706   1.383  1.00 74.46           O  
HETATM 1491  O   HOH A2027      25.335  32.144  -5.291  1.00 50.28           O  
HETATM 1492  O   HOH A2028      30.739  34.521   4.883  1.00 46.02           O  
HETATM 1493  O   HOH A2029      24.028  33.769   0.571  1.00 53.87           O  
HETATM 1494  O   HOH A2030      14.232  25.886  -3.211  1.00 65.58           O  
HETATM 1495  O   HOH A2031      20.439  32.119   3.814  1.00 55.64           O  
HETATM 1496  O   HOH A2032      18.428  26.716   0.763  1.00 61.12           O  
HETATM 1497  O   HOH A2033      27.788  16.635 -10.735  1.00 69.84           O  
HETATM 1498  O   HOH A2034      13.413  25.941   9.080  1.00 62.29           O  
HETATM 1499  O   HOH A2035      36.778  16.827  -4.518  1.00 65.80           O  
HETATM 1500  O   HOH A2036      17.013  27.426  15.660  1.00 70.93           O  
HETATM 1501  O   HOH A2037      31.859  39.024  13.899  1.00 63.51           O  
HETATM 1502  O   HOH A2038      18.162  17.123  13.801  1.00 70.33           O  
HETATM 1503  O   HOH A2039      18.373  18.766   7.538  1.00 63.50           O  
HETATM 1504  O   HOH A2040      18.011  14.867  12.382  1.00 65.52           O  
HETATM 1505  O   HOH A2041      26.371  10.270   1.068  1.00 58.27           O  
HETATM 1506  O   HOH A2042      30.217  10.691   3.281  1.00 73.05           O  
HETATM 1507  O   HOH A2043      26.785  12.293  15.910  1.00 63.19           O  
HETATM 1508  O   HOH A2044      32.947  13.373  13.729  1.00 57.96           O  
HETATM 1509  O   HOH A2045      30.190  12.063  22.591  1.00 62.92           O  
HETATM 1510  O   HOH A2046      34.991  13.338  16.179  1.00 53.96           O  
HETATM 1511  O   HOH A2047      31.003  22.695  10.004  1.00 42.33           O  
HETATM 1512  O   HOH A2048      33.401  13.499  11.084  1.00 68.45           O  
HETATM 1513  O   HOH A2049      29.297  19.958  16.276  1.00 57.54           O  
HETATM 1514  O   HOH A2050      35.522  19.012  11.892  1.00 49.05           O  
HETATM 1515  O   HOH A2051      37.936  24.054  13.020  1.00 53.30           O  
HETATM 1516  O   HOH A2052      33.374  26.595  10.904  1.00 45.78           O  
HETATM 1517  O   HOH A2053      34.122  14.873   2.008  1.00 48.03           O  
HETATM 1518  O   HOH A2054      41.600  17.577  -0.472  1.00 66.20           O  
HETATM 1519  O   HOH A2055      36.384  16.655   3.453  1.00 48.00           O  
HETATM 1520  O   HOH A2056      34.516  19.873  -5.223  1.00 39.63           O  
HETATM 1521  O   HOH A2057      29.009  10.127   0.985  1.00 83.54           O  
HETATM 1522  O   HOH A2058      18.876  19.558  -7.667  1.00 56.53           O  
HETATM 1523  O   HOH A2059      16.941  25.793  -3.290  1.00 80.85           O  
HETATM 1524  O   HOH A2060      14.826  20.711   3.903  1.00 67.87           O  
HETATM 1525  O   HOH A2061      17.903  27.097  -5.527  1.00 98.75           O  
HETATM 1526  O   HOH A2062      18.169  24.623  -7.263  1.00 55.67           O  
HETATM 1527  O   HOH A2063      19.122  29.128 -10.428  1.00 54.21           O  
HETATM 1528  O   HOH A2064      26.035  31.650  -8.789  1.00 50.98           O  
HETATM 1529  O   HOH A2065      24.947  28.935 -11.597  1.00 43.89           O  
HETATM 1530  O   HOH A2066      26.658  21.484 -13.943  1.00 48.22           O  
HETATM 1531  O   HOH A2067      28.898  19.091 -10.529  1.00 50.33           O  
HETATM 1532  O   HOH A2068      33.119  28.688 -16.483  1.00 76.05           O  
HETATM 1533  O   HOH A2069      31.713  28.522 -12.457  1.00 60.16           O  
HETATM 1534  O   HOH A2070      35.828  19.732  -7.567  1.00 48.02           O  
HETATM 1535  O   HOH A2071      43.680  22.945  -4.806  1.00 54.72           O  
HETATM 1536  O   HOH A2072      42.080  21.346  -1.811  1.00 49.35           O  
HETATM 1537  O   HOH A2073      36.573  20.070  -2.886  1.00 47.80           O  
HETATM 1538  O   HOH A2074      30.789  25.272  10.451  1.00 43.19           O  
HETATM 1539  O   HOH A2075      29.059  31.585   8.028  1.00 37.86           O  
HETATM 1540  O   HOH A2076      25.973  28.463  17.655  1.00 84.74           O  
HETATM 1541  O   HOH A2077      31.486  35.321  15.453  1.00 60.32           O  
HETATM 1542  O   HOH A2078      30.034  37.128  13.993  1.00 92.45           O  
HETATM 1543  O   HOH A2079      24.587  30.447  18.536  1.00 63.15           O  
HETATM 1544  O   HOH A2080      21.146  35.498  15.420  1.00 66.58           O  
HETATM 1545  O   HOH A2081      17.402  33.132  19.807  1.00 66.19           O  
HETATM 1546  O   HOH A2082      18.849  38.020   8.327  1.00 80.26           O  
HETATM 1547  O   HOH A2083      24.337  37.517  10.131  1.00 71.34           O  
HETATM 1548  O   HOH B2001      22.755  15.079  22.503  1.00 63.38           O  
HETATM 1549  O   HOH B2002      24.568  16.809  21.896  1.00 94.59           O  
HETATM 1550  O   HOH B2003      21.692  13.728  20.461  1.00 86.21           O  
HETATM 1551  O   HOH B2004      20.335  13.366  23.794  1.00 71.21           O  
HETATM 1552  O   HOH B2005      27.135  16.932  22.058  1.00 62.52           O  
HETATM 1553  O   HOH B2006      16.460  25.841  18.986  1.00 65.55           O  
HETATM 1554  O   HOH B2007      25.009  19.114  25.340  1.00 63.23           O  
HETATM 1555  O   HOH B2008      28.300  12.662  21.219  1.00 59.83           O  
HETATM 1556  O   HOH B2009      30.928  27.325  22.222  1.00 59.87           O  
HETATM 1557  O   HOH B2010      26.973  21.981  23.645  1.00 52.99           O  
HETATM 1558  O   HOH B2011      30.270  17.671  18.829  1.00 55.24           O  
HETATM 1559  O   HOH B2012      27.751  28.099  19.510  1.00 55.74           O  
HETATM 1560  O   HOH B2013      29.071  23.923  17.483  1.00 56.96           O  
HETATM 1561  O   HOH B2014      29.664  32.495  19.903  1.00 65.04           O  
HETATM 1562  O   HOH B2015      33.145  27.718  13.284  1.00 51.16           O  
HETATM 1563  O   HOH B2016      29.188  29.729  21.357  1.00 72.11           O  
HETATM 1564  O   HOH B2017      33.194  40.806   2.274  1.00 58.30           O  
HETATM 1565  O   HOH B2018      34.814  36.980  -9.270  1.00 78.93           O  
HETATM 1566  O   HOH B2019      44.596  30.974   1.092  1.00 73.22           O  
HETATM 1567  O   HOH B2020      30.290  28.613  11.592  1.00 47.04           O  
HETATM 1568  O   HOH B2021      28.681  31.374  10.852  1.00 57.00           O  
HETATM 1569  O   HOH B2022      22.917  34.281   5.783  1.00 54.78           O  
HETATM 1570  O   HOH B2023      43.703  32.279  -1.456  1.00 48.09           O  
HETATM 1571  O   HOH B2024      34.169  45.125   6.223  1.00 83.28           O  
HETATM 1572  O   HOH B2025      29.946  37.388   4.128  1.00 53.31           O  
HETATM 1573  O   HOH B2026      29.269  37.370  11.437  1.00 54.79           O  
HETATM 1574  O   HOH B2027      47.184  31.088   0.097  1.00 58.45           O  
HETATM 1575  O   HOH B2028      28.660  45.589   7.738  1.00 83.80           O  
HETATM 1576  O   HOH B2029      39.334  46.887   7.767  1.00 62.77           O  
HETATM 1577  O   HOH B2030      39.103  43.383   7.921  1.00 62.98           O  
HETATM 1578  O   HOH B2031      45.160  41.818   6.360  1.00 62.43           O  
HETATM 1579  O   HOH B2032      41.639  40.609  -0.030  1.00 69.83           O  
HETATM 1580  O   HOH B2033      43.489  42.927   3.398  1.00 57.37           O  
HETATM 1581  O   HOH B2034      36.309  42.004   3.495  1.00 49.51           O  
HETATM 1582  O   HOH B2035      34.952  38.926  -2.672  1.00 65.73           O  
HETATM 1583  O   HOH B2036      35.040  37.425  -6.412  1.00 65.62           O  
HETATM 1584  O   HOH B2037      39.163  36.215  -5.870  1.00 73.48           O  
HETATM 1585  O   HOH B2038      37.806  28.821   3.714  1.00 42.26           O  
HETATM 1586  O   HOH B2039      44.285  28.401   0.723  1.00 39.99           O  
HETATM 1587  O   HOH B2040      44.235  19.800   2.487  1.00 53.47           O  
HETATM 1588  O   HOH B2041      42.381  25.611   6.675  1.00 44.24           O  
HETATM 1589  O   HOH B2042      38.060  23.650  16.839  1.00 77.34           O  
HETATM 1590  O   HOH B2043      43.349  14.937  10.480  1.00 57.64           O  
HETATM 1591  O   HOH B2044      40.142  13.160  12.276  1.00 93.03           O  
HETATM 1592  O   HOH B2045      37.676  19.404  17.171  1.00 56.53           O  
HETATM 1593  O   HOH B2046      40.297  18.333  17.230  1.00 49.28           O  
HETATM 1594  O   HOH B2047      39.360  13.600   9.918  1.00 65.94           O  
HETATM 1595  O   HOH B2048      37.834  13.043  13.903  1.00 84.03           O  
HETATM 1596  O   HOH B2049      37.829  18.054   5.189  1.00 71.83           O  
HETATM 1597  O   HOH B2050      39.545  17.670  10.178  1.00 58.06           O  
HETATM 1598  O   HOH B2051      38.456  21.883  11.447  1.00 59.10           O  
HETATM 1599  O   HOH B2052      41.661  21.134   0.977  1.00 48.78           O  
HETATM 1600  O   HOH B2053      42.031  25.409  15.428  1.00 58.11           O  
HETATM 1601  O   HOH B2054      31.989  31.898   7.709  1.00 41.37           O  
HETATM 1602  O   HOH B2055      36.232  26.899  10.271  1.00 46.63           O  
HETATM 1603  O   HOH B2056      41.655  34.097  -1.034  1.00 45.50           O  
HETATM 1604  O   HOH B2057      43.611  38.774  -0.141  1.00 63.57           O  
HETATM 1605  O   HOH B2058      44.840  47.958  -3.961  1.00 50.07           O  
HETATM 1606  O   HOH B2059      43.985  42.601   0.005  1.00 63.34           O  
HETATM 1607  O   HOH B2060      48.295  33.589  -0.625  1.00 55.22           O  
HETATM 1608  O   HOH B2061      53.173  36.494   3.017  1.00 54.63           O  
HETATM 1609  O   HOH B2062      46.872  44.022   7.046  1.00 64.44           O  
HETATM 1610  O   HOH B2063      47.199  41.952  10.714  1.00 60.73           O  
HETATM 1611  O   HOH B2064      37.072  26.553  12.877  1.00 89.92           O  
HETATM 1612  O   HOH B2065      39.110  25.561  15.064  1.00 64.78           O  
HETATM 1613  O   HOH B2066      39.110  19.750  22.495  1.00 65.69           O  
HETATM 1614  O   HOH B2067      36.231  28.127  25.242  1.00 65.91           O  
HETATM 1615  O   HOH B2068      34.718  26.720  23.477  1.00 68.46           O  
HETATM 1616  O   HOH B2069      35.146  34.567  21.868  1.00 70.34           O  
HETATM 1617  O   HOH B2070      39.139  35.270  22.450  1.00 67.41           O  
HETATM 1618  O   HOH B2071      46.588  32.969  18.342  1.00 78.31           O  
HETATM 1619  O   HOH B2072      55.236  39.198   8.826  1.00 63.25           O  
HETATM 1620  O   HOH B2073      55.093  32.701  14.654  1.00 59.63           O  
HETATM 1621  O   HOH B2074      52.373  39.968  14.656  1.00 53.13           O  
HETATM 1622  O   HOH B2075      32.334  44.421  14.270  1.00 69.68           O  
HETATM 1623  O   HOH B2076      44.706  44.900  13.003  1.00 76.74           O  
HETATM 1624  O   HOH B2077      42.409  44.231  21.175  1.00 71.64           O  
HETATM 1625  O   HOH B2078      38.826  43.897  20.171  1.00 83.72           O  
HETATM 1626  O   HOH B2079      41.289  32.246  24.060  1.00 58.12           O  
HETATM 1627  O   HOH B2080      50.628  33.125  20.788  1.00 82.19           O  
HETATM 1628  O   HOH B2081      53.019  28.340  23.412  1.00 58.85           O  
HETATM 1629  O   HOH B2082      59.839  30.030  14.526  1.00 60.96           O  
HETATM 1630  O   HOH B2083      56.794  27.798  13.967  1.00 56.99           O  
HETATM 1631  O   HOH B2084      53.671  23.162   9.749  1.00 61.65           O  
HETATM 1632  O   HOH B2085      54.609  25.083   1.626  1.00 66.37           O  
HETATM 1633  O   HOH B2086      48.125  21.553   1.814  1.00 78.02           O  
HETATM 1634  O   HOH B2087      33.172  28.614   4.570  1.00 38.17           O  
HETATM 1635  O   HOH B2088      35.566  27.514   2.668  1.00 38.31           O  
CONECT 1461 1462 1463                                                           
CONECT 1462 1461                                                                
CONECT 1463 1461 1464                                                           
CONECT 1464 1463                                                                
MASTER      301    0    1    6    8    0    2    6 1633    2    4   15          
END                                                                             
