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HEADER    DNA-BINDING PROTEIN                     10-JAN-97   1RMD              
TITLE     RAG1 DIMERIZATION DOMAIN                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAG1;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ZINC-BINDING DIMERIZATION DOMAIN;                          
COMPND   5 SYNONYM: V(D)J RECOMBINATION ACTIVATING PROTEIN 1;                   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21                                    
KEYWDS    RAG1, V(D)J RECOMBINATION, ANTIBODY, MAD, RING FINGER, ZINC           
KEYWDS   2 BINUCLEAR CLUSTER, ZINC FINGER, DNA-BINDING PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.F.BELLON,K.K.RODGERS,D.G.SCHATZ,J.E.COLEMAN,T.A.STEITZ              
REVDAT   3   24-FEB-09 1RMD    1       VERSN                                    
REVDAT   2   01-APR-03 1RMD    1       JRNL                                     
REVDAT   1   23-JUL-97 1RMD    0                                                
JRNL        AUTH   S.F.BELLON,K.K.RODGERS,D.G.SCHATZ,J.E.COLEMAN,               
JRNL        AUTH 2 T.A.STEITZ                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE RAG1 DIMERIZATION DOMAIN            
JRNL        TITL 2 REVEALS MULTIPLE ZINC-BINDING MOTIFS INCLUDING A             
JRNL        TITL 3 NOVEL ZINC BINUCLEAR CLUSTER.                                
JRNL        REF    NAT.STRUCT.BIOL.              V.   4   586 1997              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9228952                                                      
JRNL        DOI    10.1038/NSB0797-586                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 60.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 6970                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 668                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.20                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 29.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 372                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 43                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.042                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 911                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 52                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.70                          
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.47                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PAR.WAT                                        
REMARK   3  PARAMETER FILE  3  : PAR.ZN                                         
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOP_116_117.ZN                                 
REMARK   3  TOPOLOGY FILE  3   : TOP_118.ZN                                     
REMARK   3  TOPOLOGY FILE  4   : TOP_119.ZN                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: LOCAL SCALING USING MAXSCALE WAS          
REMARK   3  USED TO CORRECT THE HIGHLY ANISOTROPIC DATA. THE LOW OVERALL        
REMARK   3  COMPLETION OF THE DATA REFLECT THIS ANISOTROPY.                     
REMARK   4                                                                      
REMARK   4 1RMD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUN-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.35                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR          
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36957                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.61000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: BAZFAZ                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-10 % PEG 4K, 100MM HEPES, PH 7.5,      
REMARK 280  10% ETHYLENE GLYCOL                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.62000            
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       32.81000            
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       32.81000            
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       65.62000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       65.62000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  28      -66.61   -101.88                                   
REMARK 500    LYS A  55      -72.99    -78.45                                   
REMARK 500    ASP A  95       -4.35     68.78                                   
REMARK 500    ASN A  97       54.10   -119.95                                   
REMARK 500    SER A 111       -9.28    -57.49                                   
REMARK 500    SER A 115      -87.31    -68.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 117  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   2   SG                                                     
REMARK 620 2 HIS A   6   ND1 114.1                                              
REMARK 620 3 CYS A  29   SG  110.1 111.3                                        
REMARK 620 4 HIS A  31   ND1 106.3 120.9  92.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 118  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  26   SG                                                     
REMARK 620 2 CYS A  29   SG   99.2                                              
REMARK 620 3 CYS A  46   SG  106.2 106.3                                        
REMARK 620 4 CYS A  49   SG  122.8 107.6 112.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 119  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  41   SG                                                     
REMARK 620 2 HIS A  43   ND1  99.6                                              
REMARK 620 3 CYS A  61   SG  106.8 114.7                                        
REMARK 620 4 CYS A  64   SG  101.0 113.5 118.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 120  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  91   SG                                                     
REMARK 620 2 CYS A  96   SG  114.3                                              
REMARK 620 3 HIS A 108   NE2  99.3 111.3                                        
REMARK 620 4 HIS A 112   NE2 105.0 119.8 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 117                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 118                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 119                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 120                  
DBREF  1RMD A    1   116  UNP    P15919   RAG1_MOUSE     265    380             
SEQRES   1 A  116  ASN CYS SER LYS ILE HIS LEU SER THR LYS LEU LEU ALA          
SEQRES   2 A  116  VAL ASP PHE PRO ALA HIS PHE VAL LYS SER ILE SER CYS          
SEQRES   3 A  116  GLN ILE CYS GLU HIS ILE LEU ALA ASP PRO VAL GLU THR          
SEQRES   4 A  116  SER CYS LYS HIS LEU PHE CYS ARG ILE CYS ILE LEU ARG          
SEQRES   5 A  116  CYS LEU LYS VAL MET GLY SER TYR CYS PRO SER CYS ARG          
SEQRES   6 A  116  TYR PRO CYS PHE PRO THR ASP LEU GLU SER PRO VAL LYS          
SEQRES   7 A  116  SER PHE LEU ASN ILE LEU ASN SER LEU MET VAL LYS CYS          
SEQRES   8 A  116  PRO ALA GLN ASP CYS ASN GLU GLU VAL SER LEU GLU LYS          
SEQRES   9 A  116  TYR ASN HIS HIS VAL SER SER HIS LYS GLU SER LYS              
HET     ZN  A 117       1                                                       
HET     ZN  A 118       1                                                       
HET     ZN  A 119       1                                                       
HET     ZN  A 120       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    4(ZN 2+)                                                     
FORMUL   6  HOH   *52(H2 O)                                                     
HELIX    1   1 CYS A    2  LYS A    4  5                                   3    
HELIX    2   2 THR A    9  LEU A   11  5                                   3    
HELIX    3   3 ALA A   18  SER A   23  1                                   6    
HELIX    4   4 ARG A   47  VAL A   56  1                                  10    
HELIX    5   5 PRO A   70  ASP A   72  5                                   3    
HELIX    6   6 LYS A   78  SER A   86  1                                   9    
HELIX    7   7 LEU A  102  SER A  110  1                                   9    
SHEET    1   A 2 PRO A  36  GLU A  38  0                                        
SHEET    2   A 2 LEU A  44  CYS A  46 -1  N  PHE A  45   O  VAL A  37           
SHEET    1   B 2 MET A  88  LYS A  90  0                                        
SHEET    2   B 2 GLU A  99  SER A 101 -1  N  VAL A 100   O  VAL A  89           
LINK        ZN    ZN A 117                 SG  CYS A   2     1555   1555  2.31  
LINK        ZN    ZN A 117                 ND1 HIS A   6     1555   1555  1.87  
LINK        ZN    ZN A 117                 SG  CYS A  29     1555   1555  2.35  
LINK        ZN    ZN A 117                 ND1 HIS A  31     1555   1555  2.08  
LINK        ZN    ZN A 118                 SG  CYS A  26     1555   1555  2.33  
LINK        ZN    ZN A 118                 SG  CYS A  29     1555   1555  2.32  
LINK        ZN    ZN A 118                 SG  CYS A  46     1555   1555  2.24  
LINK        ZN    ZN A 118                 SG  CYS A  49     1555   1555  2.26  
LINK        ZN    ZN A 119                 SG  CYS A  41     1555   1555  2.37  
LINK        ZN    ZN A 119                 ND1 HIS A  43     1555   1555  2.07  
LINK        ZN    ZN A 119                 SG  CYS A  61     1555   1555  2.28  
LINK        ZN    ZN A 119                 SG  CYS A  64     1555   1555  2.25  
LINK        ZN    ZN A 120                 SG  CYS A  91     1555   1555  2.31  
LINK        ZN    ZN A 120                 SG  CYS A  96     1555   1555  2.39  
LINK        ZN    ZN A 120                 NE2 HIS A 108     1555   1555  1.99  
LINK        ZN    ZN A 120                 NE2 HIS A 112     1555   1555  1.96  
SITE     1 AC1  4 CYS A   2  HIS A   6  CYS A  29  HIS A  31                    
SITE     1 AC2  4 CYS A  26  CYS A  29  CYS A  46  CYS A  49                    
SITE     1 AC3  4 CYS A  41  HIS A  43  CYS A  61  CYS A  64                    
SITE     1 AC4  4 CYS A  91  CYS A  96  HIS A 108  HIS A 112                    
CRYST1   57.580   57.580   98.430  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017367  0.010027  0.000000        0.00000                         
SCALE2      0.000000  0.020054  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010160        0.00000                         
ATOM      1  N   ASN A   1       0.736  27.946  53.948  1.00 37.25           N  
ATOM      2  CA  ASN A   1       0.517  27.822  52.473  1.00 36.11           C  
ATOM      3  C   ASN A   1      -0.262  28.992  51.864  1.00 33.55           C  
ATOM      4  O   ASN A   1      -0.528  29.997  52.539  1.00 33.59           O  
ATOM      5  CB  ASN A   1      -0.208  26.506  52.166  1.00 40.18           C  
ATOM      6  CG  ASN A   1      -1.431  26.291  53.037  1.00 42.71           C  
ATOM      7  OD1 ASN A   1      -1.816  27.161  53.820  1.00 49.46           O  
ATOM      8  ND2 ASN A   1      -2.048  25.118  52.909  1.00 45.85           N  
ATOM      9  N   CYS A   2      -0.610  28.869  50.581  1.00 28.40           N  
ATOM     10  CA  CYS A   2      -1.380  29.916  49.897  1.00 28.25           C  
ATOM     11  C   CYS A   2      -2.842  29.920  50.343  1.00 26.42           C  
ATOM     12  O   CYS A   2      -3.631  30.761  49.917  1.00 27.83           O  
ATOM     13  CB  CYS A   2      -1.295  29.758  48.373  1.00 26.23           C  
ATOM     14  SG  CYS A   2      -1.810  28.164  47.735  1.00 21.06           S  
ATOM     15  N   SER A   3      -3.192  28.949  51.180  1.00 25.33           N  
ATOM     16  CA  SER A   3      -4.537  28.800  51.725  1.00 25.26           C  
ATOM     17  C   SER A   3      -4.828  29.958  52.680  1.00 24.36           C  
ATOM     18  O   SER A   3      -5.990  30.273  52.955  1.00 24.59           O  
ATOM     19  CB  SER A   3      -4.645  27.456  52.463  1.00 26.33           C  
ATOM     20  OG  SER A   3      -5.976  26.966  52.533  1.00 32.06           O  
ATOM     21  N   LYS A   4      -3.765  30.578  53.186  1.00 24.65           N  
ATOM     22  CA  LYS A   4      -3.868  31.729  54.098  1.00 26.89           C  
ATOM     23  C   LYS A   4      -4.240  32.978  53.319  1.00 27.65           C  
ATOM     24  O   LYS A   4      -4.723  33.954  53.896  1.00 27.77           O  
ATOM     25  CB  LYS A   4      -2.520  32.021  54.772  1.00 23.67           C  
ATOM     26  CG  LYS A   4      -2.152  31.070  55.872  1.00 27.40           C  
ATOM     27  CD  LYS A   4      -0.895  31.523  56.584  1.00 22.76           C  
ATOM     28  CE  LYS A   4      -0.979  31.169  58.032  1.00  9.82           C  
ATOM     29  NZ  LYS A   4       0.281  31.498  58.675  1.00 24.93           N  
ATOM     30  N   ILE A   5      -3.965  32.943  52.016  1.00 26.14           N  
ATOM     31  CA  ILE A   5      -4.198  34.069  51.130  1.00 26.27           C  
ATOM     32  C   ILE A   5      -5.186  33.814  49.995  1.00 26.60           C  
ATOM     33  O   ILE A   5      -5.635  34.767  49.335  1.00 21.76           O  
ATOM     34  CB  ILE A   5      -2.856  34.564  50.508  1.00 28.67           C  
ATOM     35  CG1 ILE A   5      -2.014  33.379  50.017  1.00 30.18           C  
ATOM     36  CG2 ILE A   5      -2.080  35.394  51.518  1.00 32.08           C  
ATOM     37  CD1 ILE A   5      -0.761  33.774  49.275  1.00 31.21           C  
ATOM     38  N   HIS A   6      -5.517  32.540  49.771  1.00 25.18           N  
ATOM     39  CA  HIS A   6      -6.431  32.157  48.697  1.00 22.43           C  
ATOM     40  C   HIS A   6      -7.803  31.677  49.167  1.00 20.05           C  
ATOM     41  O   HIS A   6      -7.946  31.192  50.281  1.00 14.95           O  
ATOM     42  CB  HIS A   6      -5.767  31.090  47.835  1.00 19.92           C  
ATOM     43  CG  HIS A   6      -4.604  31.595  47.045  1.00 20.06           C  
ATOM     44  ND1 HIS A   6      -3.770  30.734  46.359  1.00 16.46           N  
ATOM     45  CD2 HIS A   6      -4.162  32.867  46.886  1.00 20.79           C  
ATOM     46  CE1 HIS A   6      -2.840  31.497  45.817  1.00 20.77           C  
ATOM     47  NE2 HIS A   6      -3.032  32.800  46.107  1.00 21.53           N  
ATOM     48  N   LEU A   7      -8.815  31.839  48.318  1.00 15.72           N  
ATOM     49  CA  LEU A   7     -10.157  31.405  48.662  1.00 20.87           C  
ATOM     50  C   LEU A   7     -10.457  29.988  48.136  1.00 21.13           C  
ATOM     51  O   LEU A   7     -10.072  29.643  47.015  1.00 20.29           O  
ATOM     52  CB  LEU A   7     -11.184  32.403  48.120  1.00 21.07           C  
ATOM     53  CG  LEU A   7     -12.043  33.166  49.138  1.00 24.13           C  
ATOM     54  CD1 LEU A   7     -11.212  33.711  50.331  1.00 16.06           C  
ATOM     55  CD2 LEU A   7     -12.753  34.297  48.404  1.00 25.51           C  
ATOM     56  N   SER A   8     -11.105  29.168  48.966  1.00 16.69           N  
ATOM     57  CA  SER A   8     -11.479  27.798  48.601  1.00 14.82           C  
ATOM     58  C   SER A   8     -12.720  27.839  47.729  1.00 17.01           C  
ATOM     59  O   SER A   8     -13.635  28.642  47.978  1.00 18.20           O  
ATOM     60  CB  SER A   8     -11.803  26.970  49.852  1.00 16.93           C  
ATOM     61  OG  SER A   8     -12.551  25.810  49.505  1.00 15.42           O  
ATOM     62  N   THR A   9     -12.794  26.958  46.736  1.00 14.02           N  
ATOM     63  CA  THR A   9     -13.961  26.958  45.877  1.00 14.95           C  
ATOM     64  C   THR A   9     -15.260  26.583  46.626  1.00 17.29           C  
ATOM     65  O   THR A   9     -16.373  26.810  46.127  1.00 19.28           O  
ATOM     66  CB  THR A   9     -13.771  26.050  44.653  1.00 16.07           C  
ATOM     67  OG1 THR A   9     -13.493  24.718  45.080  1.00 15.85           O  
ATOM     68  CG2 THR A   9     -12.620  26.551  43.794  1.00 19.06           C  
ATOM     69  N   LYS A  10     -15.145  26.061  47.838  1.00 16.13           N  
ATOM     70  CA  LYS A  10     -16.353  25.698  48.550  1.00 21.31           C  
ATOM     71  C   LYS A  10     -17.042  26.947  49.091  1.00 19.86           C  
ATOM     72  O   LYS A  10     -18.159  26.860  49.595  1.00 21.29           O  
ATOM     73  CB  LYS A  10     -16.088  24.635  49.636  1.00 27.45           C  
ATOM     74  CG  LYS A  10     -15.299  25.115  50.841  1.00 42.69           C  
ATOM     75  CD  LYS A  10     -14.541  23.960  51.486  1.00 51.68           C  
ATOM     76  CE  LYS A  10     -13.586  24.459  52.574  1.00 55.89           C  
ATOM     77  NZ  LYS A  10     -12.623  23.389  53.000  1.00 56.88           N  
ATOM     78  N   LEU A  11     -16.404  28.113  48.943  1.00 17.01           N  
ATOM     79  CA  LEU A  11     -17.018  29.358  49.388  1.00 16.12           C  
ATOM     80  C   LEU A  11     -17.931  29.934  48.303  1.00 20.10           C  
ATOM     81  O   LEU A  11     -18.604  30.946  48.521  1.00 15.13           O  
ATOM     82  CB  LEU A  11     -15.972  30.393  49.805  1.00 15.55           C  
ATOM     83  CG  LEU A  11     -15.092  30.032  51.013  1.00 21.51           C  
ATOM     84  CD1 LEU A  11     -14.175  31.206  51.395  1.00 18.27           C  
ATOM     85  CD2 LEU A  11     -15.985  29.648  52.187  1.00 17.71           C  
ATOM     86  N   LEU A  12     -17.952  29.293  47.130  1.00 21.46           N  
ATOM     87  CA  LEU A  12     -18.799  29.750  46.024  1.00 19.76           C  
ATOM     88  C   LEU A  12     -20.258  29.611  46.414  1.00 22.19           C  
ATOM     89  O   LEU A  12     -20.693  28.546  46.865  1.00 18.17           O  
ATOM     90  CB  LEU A  12     -18.557  28.910  44.773  1.00 19.64           C  
ATOM     91  CG  LEU A  12     -17.283  29.202  43.975  1.00 25.00           C  
ATOM     92  CD1 LEU A  12     -17.075  28.155  42.870  1.00 18.26           C  
ATOM     93  CD2 LEU A  12     -17.348  30.630  43.422  1.00 18.28           C  
ATOM     94  N   ALA A  13     -21.016  30.681  46.210  1.00 21.09           N  
ATOM     95  CA  ALA A  13     -22.434  30.692  46.526  1.00 23.83           C  
ATOM     96  C   ALA A  13     -23.206  29.716  45.653  1.00 25.32           C  
ATOM     97  O   ALA A  13     -24.001  28.914  46.136  1.00 27.91           O  
ATOM     98  CB  ALA A  13     -22.992  32.093  46.339  1.00 22.64           C  
ATOM     99  N   VAL A  14     -22.959  29.789  44.358  1.00 24.82           N  
ATOM    100  CA  VAL A  14     -23.652  28.954  43.399  1.00 25.61           C  
ATOM    101  C   VAL A  14     -23.058  27.569  43.247  1.00 24.14           C  
ATOM    102  O   VAL A  14     -21.842  27.409  43.246  1.00 25.49           O  
ATOM    103  CB  VAL A  14     -23.646  29.630  42.033  1.00 25.53           C  
ATOM    104  CG1 VAL A  14     -24.455  28.823  41.050  1.00 24.61           C  
ATOM    105  CG2 VAL A  14     -24.195  31.039  42.163  1.00 24.64           C  
ATOM    106  N   ASP A  15     -23.925  26.580  43.060  1.00 22.37           N  
ATOM    107  CA  ASP A  15     -23.492  25.199  42.858  1.00 24.36           C  
ATOM    108  C   ASP A  15     -23.260  24.916  41.355  1.00 23.63           C  
ATOM    109  O   ASP A  15     -24.094  24.284  40.681  1.00 25.06           O  
ATOM    110  CB  ASP A  15     -24.547  24.246  43.430  1.00 30.13           C  
ATOM    111  CG  ASP A  15     -24.080  22.803  43.449  1.00 35.84           C  
ATOM    112  OD1 ASP A  15     -22.853  22.573  43.373  1.00 37.65           O  
ATOM    113  OD2 ASP A  15     -24.939  21.897  43.524  1.00 39.22           O  
ATOM    114  N   PHE A  16     -22.118  25.354  40.835  1.00 19.65           N  
ATOM    115  CA  PHE A  16     -21.792  25.184  39.412  1.00 18.42           C  
ATOM    116  C   PHE A  16     -21.395  23.749  39.012  1.00 17.84           C  
ATOM    117  O   PHE A  16     -21.055  22.930  39.880  1.00 16.49           O  
ATOM    118  CB  PHE A  16     -20.616  26.109  39.058  1.00 21.05           C  
ATOM    119  CG  PHE A  16     -20.948  27.584  39.046  1.00 15.67           C  
ATOM    120  CD1 PHE A  16     -21.869  28.100  38.152  1.00 16.76           C  
ATOM    121  CD2 PHE A  16     -20.293  28.457  39.908  1.00 16.73           C  
ATOM    122  CE1 PHE A  16     -22.138  29.470  38.105  1.00 20.65           C  
ATOM    123  CE2 PHE A  16     -20.550  29.827  39.875  1.00 21.29           C  
ATOM    124  CZ  PHE A  16     -21.477  30.339  38.970  1.00 17.79           C  
ATOM    125  N   PRO A  17     -21.451  23.414  37.691  1.00 15.95           N  
ATOM    126  CA  PRO A  17     -21.067  22.067  37.192  1.00  9.51           C  
ATOM    127  C   PRO A  17     -19.575  21.907  37.512  1.00 13.85           C  
ATOM    128  O   PRO A  17     -18.854  22.914  37.570  1.00 14.71           O  
ATOM    129  CB  PRO A  17     -21.296  22.183  35.695  1.00 11.22           C  
ATOM    130  CG  PRO A  17     -22.484  23.119  35.636  1.00  9.10           C  
ATOM    131  CD  PRO A  17     -22.116  24.201  36.633  1.00  6.31           C  
ATOM    132  N   ALA A  18     -19.106  20.677  37.727  1.00 11.55           N  
ATOM    133  CA  ALA A  18     -17.702  20.468  38.119  1.00 13.58           C  
ATOM    134  C   ALA A  18     -16.620  20.945  37.149  1.00 12.16           C  
ATOM    135  O   ALA A  18     -15.547  21.409  37.594  1.00 11.21           O  
ATOM    136  CB  ALA A  18     -17.442  19.021  38.486  1.00 12.60           C  
ATOM    137  N   HIS A  19     -16.872  20.833  35.846  1.00  4.09           N  
ATOM    138  CA  HIS A  19     -15.852  21.259  34.893  1.00  6.69           C  
ATOM    139  C   HIS A  19     -15.730  22.774  34.877  1.00  9.50           C  
ATOM    140  O   HIS A  19     -14.634  23.300  34.702  1.00 13.04           O  
ATOM    141  CB  HIS A  19     -16.082  20.661  33.519  1.00  4.91           C  
ATOM    142  CG  HIS A  19     -15.850  19.170  33.452  1.00 13.27           C  
ATOM    143  ND1 HIS A  19     -14.915  18.519  34.232  1.00 18.73           N  
ATOM    144  CD2 HIS A  19     -16.442  18.205  32.700  1.00 12.61           C  
ATOM    145  CE1 HIS A  19     -14.941  17.220  33.970  1.00 14.24           C  
ATOM    146  NE2 HIS A  19     -15.858  17.005  33.041  1.00 19.91           N  
ATOM    147  N   PHE A  20     -16.824  23.473  35.162  1.00  8.11           N  
ATOM    148  CA  PHE A  20     -16.767  24.922  35.196  1.00 13.45           C  
ATOM    149  C   PHE A  20     -15.997  25.352  36.453  1.00 14.14           C  
ATOM    150  O   PHE A  20     -15.194  26.282  36.402  1.00 13.12           O  
ATOM    151  CB  PHE A  20     -18.158  25.556  35.177  1.00 11.67           C  
ATOM    152  CG  PHE A  20     -18.139  27.052  35.366  1.00 15.45           C  
ATOM    153  CD1 PHE A  20     -17.752  27.897  34.325  1.00 14.62           C  
ATOM    154  CD2 PHE A  20     -18.456  27.611  36.591  1.00  9.48           C  
ATOM    155  CE1 PHE A  20     -17.679  29.285  34.505  1.00 10.89           C  
ATOM    156  CE2 PHE A  20     -18.386  29.000  36.780  1.00 15.46           C  
ATOM    157  CZ  PHE A  20     -17.995  29.835  35.732  1.00  5.13           C  
ATOM    158  N   VAL A  21     -16.253  24.682  37.573  1.00 12.16           N  
ATOM    159  CA  VAL A  21     -15.570  24.996  38.811  1.00 13.87           C  
ATOM    160  C   VAL A  21     -14.059  24.831  38.618  1.00 19.59           C  
ATOM    161  O   VAL A  21     -13.233  25.612  39.139  1.00 15.82           O  
ATOM    162  CB  VAL A  21     -15.994  24.058  39.934  1.00  9.26           C  
ATOM    163  CG1 VAL A  21     -15.089  24.276  41.164  1.00 13.80           C  
ATOM    164  CG2 VAL A  21     -17.429  24.327  40.316  1.00 13.03           C  
ATOM    165  N   LYS A  22     -13.713  23.783  37.880  1.00 18.69           N  
ATOM    166  CA  LYS A  22     -12.330  23.463  37.587  1.00 19.48           C  
ATOM    167  C   LYS A  22     -11.679  24.575  36.725  1.00 19.02           C  
ATOM    168  O   LYS A  22     -10.495  24.933  36.920  1.00 10.21           O  
ATOM    169  CB  LYS A  22     -12.308  22.122  36.862  1.00 26.95           C  
ATOM    170  CG  LYS A  22     -10.950  21.647  36.422  1.00 31.56           C  
ATOM    171  CD  LYS A  22     -10.842  21.625  34.913  1.00 36.46           C  
ATOM    172  CE  LYS A  22      -9.507  21.058  34.526  1.00 40.89           C  
ATOM    173  NZ  LYS A  22      -9.382  19.748  35.163  1.00 45.93           N  
ATOM    174  N   SER A  23     -12.484  25.141  35.815  1.00 14.81           N  
ATOM    175  CA  SER A  23     -12.033  26.192  34.902  1.00 15.27           C  
ATOM    176  C   SER A  23     -11.653  27.479  35.607  1.00 15.56           C  
ATOM    177  O   SER A  23     -10.838  28.218  35.098  1.00  9.87           O  
ATOM    178  CB  SER A  23     -13.083  26.502  33.835  1.00 15.11           C  
ATOM    179  OG  SER A  23     -14.182  27.243  34.349  1.00 20.08           O  
ATOM    180  N   ILE A  24     -12.270  27.772  36.750  1.00 14.87           N  
ATOM    181  CA  ILE A  24     -11.922  28.993  37.466  1.00 10.74           C  
ATOM    182  C   ILE A  24     -10.986  28.758  38.656  1.00 12.38           C  
ATOM    183  O   ILE A  24     -10.775  29.659  39.483  1.00 13.44           O  
ATOM    184  CB  ILE A  24     -13.191  29.813  37.840  1.00 13.14           C  
ATOM    185  CG1 ILE A  24     -14.215  28.952  38.626  1.00  6.63           C  
ATOM    186  CG2 ILE A  24     -13.841  30.307  36.542  1.00 12.80           C  
ATOM    187  CD1 ILE A  24     -13.811  28.604  40.086  1.00  2.81           C  
ATOM    188  N   SER A  25     -10.427  27.546  38.727  1.00 11.49           N  
ATOM    189  CA  SER A  25      -9.492  27.156  39.790  1.00 15.12           C  
ATOM    190  C   SER A  25      -8.010  27.110  39.327  1.00 14.28           C  
ATOM    191  O   SER A  25      -7.709  26.885  38.159  1.00 13.70           O  
ATOM    192  CB  SER A  25      -9.875  25.781  40.360  1.00 12.25           C  
ATOM    193  OG  SER A  25     -11.225  25.743  40.795  1.00 18.74           O  
ATOM    194  N   CYS A  26      -7.093  27.347  40.253  1.00 15.10           N  
ATOM    195  CA  CYS A  26      -5.668  27.287  39.953  1.00 17.94           C  
ATOM    196  C   CYS A  26      -5.309  25.814  39.806  1.00 18.73           C  
ATOM    197  O   CYS A  26      -5.532  25.030  40.716  1.00 18.49           O  
ATOM    198  CB  CYS A  26      -4.859  27.914  41.096  1.00 16.32           C  
ATOM    199  SG  CYS A  26      -3.126  27.486  41.043  1.00 17.54           S  
ATOM    200  N   GLN A  27      -4.737  25.436  38.667  1.00 26.19           N  
ATOM    201  CA  GLN A  27      -4.403  24.027  38.423  1.00 26.18           C  
ATOM    202  C   GLN A  27      -3.303  23.405  39.287  1.00 25.49           C  
ATOM    203  O   GLN A  27      -3.081  22.195  39.229  1.00 26.55           O  
ATOM    204  CB  GLN A  27      -4.185  23.765  36.933  1.00 26.70           C  
ATOM    205  CG  GLN A  27      -5.431  24.019  36.077  1.00 29.57           C  
ATOM    206  CD  GLN A  27      -6.675  23.351  36.634  1.00 29.07           C  
ATOM    207  OE1 GLN A  27      -6.839  22.140  36.542  1.00 35.32           O  
ATOM    208  NE2 GLN A  27      -7.567  24.144  37.198  1.00 30.79           N  
ATOM    209  N   ILE A  28      -2.654  24.237  40.103  1.00 23.88           N  
ATOM    210  CA  ILE A  28      -1.632  23.791  41.058  1.00 19.87           C  
ATOM    211  C   ILE A  28      -2.243  23.732  42.472  1.00 16.76           C  
ATOM    212  O   ILE A  28      -2.452  22.670  43.009  1.00 16.39           O  
ATOM    213  CB  ILE A  28      -0.415  24.741  41.079  1.00 18.25           C  
ATOM    214  CG1 ILE A  28       0.430  24.512  39.825  1.00 18.88           C  
ATOM    215  CG2 ILE A  28       0.442  24.510  42.329  1.00 20.96           C  
ATOM    216  CD1 ILE A  28       1.497  25.571  39.599  1.00 20.30           C  
ATOM    217  N   CYS A  29      -2.602  24.882  43.023  1.00 19.20           N  
ATOM    218  CA  CYS A  29      -3.154  24.959  44.361  1.00 19.74           C  
ATOM    219  C   CYS A  29      -4.640  24.635  44.509  1.00 22.70           C  
ATOM    220  O   CYS A  29      -5.101  24.404  45.626  1.00 28.44           O  
ATOM    221  CB  CYS A  29      -2.827  26.328  44.994  1.00 20.14           C  
ATOM    222  SG  CYS A  29      -3.813  27.775  44.505  1.00 19.27           S  
ATOM    223  N   GLU A  30      -5.389  24.619  43.407  1.00 22.26           N  
ATOM    224  CA  GLU A  30      -6.834  24.320  43.438  1.00 21.68           C  
ATOM    225  C   GLU A  30      -7.766  25.358  44.070  1.00 20.23           C  
ATOM    226  O   GLU A  30      -8.969  25.140  44.201  1.00 19.73           O  
ATOM    227  CB  GLU A  30      -7.091  22.952  44.058  1.00 21.41           C  
ATOM    228  CG  GLU A  30      -6.682  21.837  43.134  1.00 29.58           C  
ATOM    229  CD  GLU A  30      -6.939  20.474  43.707  1.00 34.94           C  
ATOM    230  OE1 GLU A  30      -7.954  20.283  44.412  1.00 45.72           O  
ATOM    231  OE2 GLU A  30      -6.125  19.581  43.439  1.00 37.75           O  
ATOM    232  N   HIS A  31      -7.225  26.494  44.470  1.00 18.27           N  
ATOM    233  CA  HIS A  31      -8.075  27.527  45.049  1.00 20.61           C  
ATOM    234  C   HIS A  31      -8.700  28.317  43.897  1.00 19.02           C  
ATOM    235  O   HIS A  31      -8.405  28.037  42.722  1.00 20.78           O  
ATOM    236  CB  HIS A  31      -7.222  28.460  45.911  1.00 17.40           C  
ATOM    237  CG  HIS A  31      -6.631  27.791  47.107  1.00 17.29           C  
ATOM    238  ND1 HIS A  31      -5.281  27.815  47.337  1.00 21.35           N  
ATOM    239  CD2 HIS A  31      -7.263  27.225  48.160  1.00 16.10           C  
ATOM    240  CE1 HIS A  31      -5.124  27.271  48.530  1.00 20.56           C  
ATOM    241  NE2 HIS A  31      -6.298  26.900  49.064  1.00 15.53           N  
ATOM    242  N   ILE A  32      -9.596  29.254  44.214  1.00 13.80           N  
ATOM    243  CA  ILE A  32     -10.150  30.108  43.160  1.00 16.38           C  
ATOM    244  C   ILE A  32      -8.932  30.925  42.662  1.00 19.63           C  
ATOM    245  O   ILE A  32      -8.165  31.474  43.477  1.00 16.35           O  
ATOM    246  CB  ILE A  32     -11.200  31.096  43.696  1.00 11.44           C  
ATOM    247  CG1 ILE A  32     -12.365  30.336  44.321  1.00 16.73           C  
ATOM    248  CG2 ILE A  32     -11.706  31.976  42.567  1.00  5.14           C  
ATOM    249  CD1 ILE A  32     -13.426  31.240  44.939  1.00 17.57           C  
ATOM    250  N   LEU A  33      -8.707  30.958  41.352  1.00 18.06           N  
ATOM    251  CA  LEU A  33      -7.554  31.704  40.813  1.00 19.44           C  
ATOM    252  C   LEU A  33      -7.363  33.088  41.448  1.00 17.05           C  
ATOM    253  O   LEU A  33      -8.299  33.892  41.526  1.00 15.30           O  
ATOM    254  CB  LEU A  33      -7.692  31.895  39.293  1.00 22.36           C  
ATOM    255  CG  LEU A  33      -7.565  30.666  38.401  1.00 22.49           C  
ATOM    256  CD1 LEU A  33      -8.308  30.888  37.094  1.00 21.72           C  
ATOM    257  CD2 LEU A  33      -6.111  30.370  38.166  1.00 19.58           C  
ATOM    258  N   ALA A  34      -6.150  33.366  41.898  1.00 13.30           N  
ATOM    259  CA  ALA A  34      -5.869  34.673  42.479  1.00 18.80           C  
ATOM    260  C   ALA A  34      -4.801  35.234  41.573  1.00 15.86           C  
ATOM    261  O   ALA A  34      -3.718  34.671  41.507  1.00 24.18           O  
ATOM    262  CB  ALA A  34      -5.345  34.525  43.918  1.00 16.71           C  
ATOM    263  N   ASP A  35      -5.107  36.315  40.858  1.00 20.29           N  
ATOM    264  CA  ASP A  35      -4.176  36.951  39.896  1.00 20.17           C  
ATOM    265  C   ASP A  35      -3.783  35.914  38.870  1.00 20.39           C  
ATOM    266  O   ASP A  35      -2.612  35.524  38.779  1.00 22.70           O  
ATOM    267  CB  ASP A  35      -2.920  37.459  40.612  1.00 24.63           C  
ATOM    268  CG  ASP A  35      -2.094  38.407  39.756  1.00 27.49           C  
ATOM    269  OD1 ASP A  35      -2.608  38.892  38.727  1.00 24.45           O  
ATOM    270  OD2 ASP A  35      -0.929  38.673  40.125  1.00 31.17           O  
ATOM    271  N   PRO A  36      -4.756  35.443  38.066  1.00 21.38           N  
ATOM    272  CA  PRO A  36      -4.501  34.417  37.041  1.00 18.55           C  
ATOM    273  C   PRO A  36      -3.610  34.824  35.890  1.00 18.95           C  
ATOM    274  O   PRO A  36      -3.603  35.973  35.480  1.00 21.40           O  
ATOM    275  CB  PRO A  36      -5.909  34.104  36.537  1.00 17.66           C  
ATOM    276  CG  PRO A  36      -6.590  35.445  36.623  1.00 16.88           C  
ATOM    277  CD  PRO A  36      -6.151  35.919  37.993  1.00 15.70           C  
ATOM    278  N   VAL A  37      -2.799  33.882  35.428  1.00 20.68           N  
ATOM    279  CA  VAL A  37      -1.947  34.084  34.255  1.00 21.35           C  
ATOM    280  C   VAL A  37      -2.174  32.846  33.423  1.00 21.04           C  
ATOM    281  O   VAL A  37      -2.422  31.749  33.959  1.00 23.19           O  
ATOM    282  CB  VAL A  37      -0.429  34.214  34.557  1.00 19.61           C  
ATOM    283  CG1 VAL A  37      -0.154  35.531  35.219  1.00 23.56           C  
ATOM    284  CG2 VAL A  37       0.072  33.067  35.412  1.00 22.77           C  
ATOM    285  N   GLU A  38      -2.061  33.012  32.116  1.00 17.58           N  
ATOM    286  CA  GLU A  38      -2.278  31.936  31.175  1.00 19.30           C  
ATOM    287  C   GLU A  38      -0.993  31.538  30.455  1.00 21.62           C  
ATOM    288  O   GLU A  38      -0.243  32.397  29.950  1.00 21.10           O  
ATOM    289  CB  GLU A  38      -3.348  32.367  30.162  1.00 15.37           C  
ATOM    290  CG  GLU A  38      -3.742  31.313  29.158  1.00 18.15           C  
ATOM    291  CD  GLU A  38      -4.949  31.719  28.321  1.00 15.85           C  
ATOM    292  OE1 GLU A  38      -5.532  32.772  28.570  1.00 18.33           O  
ATOM    293  OE2 GLU A  38      -5.338  30.956  27.417  1.00 23.02           O  
ATOM    294  N   THR A  39      -0.738  30.232  30.447  1.00 21.55           N  
ATOM    295  CA  THR A  39       0.425  29.668  29.779  1.00 19.90           C  
ATOM    296  C   THR A  39       0.146  29.637  28.284  1.00 21.50           C  
ATOM    297  O   THR A  39      -1.011  29.753  27.864  1.00 22.45           O  
ATOM    298  CB  THR A  39       0.712  28.219  30.245  1.00 21.90           C  
ATOM    299  OG1 THR A  39      -0.383  27.362  29.873  1.00 18.93           O  
ATOM    300  CG2 THR A  39       0.930  28.171  31.739  1.00 15.63           C  
ATOM    301  N   SER A  40       1.197  29.461  27.483  1.00 22.60           N  
ATOM    302  CA  SER A  40       1.056  29.395  26.025  1.00 23.23           C  
ATOM    303  C   SER A  40       0.045  28.297  25.658  1.00 23.52           C  
ATOM    304  O   SER A  40      -0.776  28.461  24.735  1.00 22.19           O  
ATOM    305  CB  SER A  40       2.429  29.134  25.381  1.00 24.28           C  
ATOM    306  OG  SER A  40       3.332  30.202  25.673  1.00 24.23           O  
ATOM    307  N   CYS A  41       0.026  27.246  26.478  1.00 19.73           N  
ATOM    308  CA  CYS A  41      -0.877  26.124  26.283  1.00 19.74           C  
ATOM    309  C   CYS A  41      -2.305  26.333  26.836  1.00 19.27           C  
ATOM    310  O   CYS A  41      -3.059  25.371  26.992  1.00 20.45           O  
ATOM    311  CB  CYS A  41      -0.236  24.840  26.832  1.00 17.91           C  
ATOM    312  SG  CYS A  41       0.489  25.010  28.485  1.00 15.41           S  
ATOM    313  N   LYS A  42      -2.668  27.583  27.129  1.00 18.23           N  
ATOM    314  CA  LYS A  42      -4.013  27.943  27.604  1.00 17.75           C  
ATOM    315  C   LYS A  42      -4.465  27.380  28.951  1.00 19.11           C  
ATOM    316  O   LYS A  42      -5.652  27.147  29.174  1.00 19.36           O  
ATOM    317  CB  LYS A  42      -5.066  27.582  26.550  1.00 22.39           C  
ATOM    318  CG  LYS A  42      -4.740  28.021  25.128  1.00 22.74           C  
ATOM    319  CD  LYS A  42      -5.240  29.398  24.822  1.00 27.52           C  
ATOM    320  CE  LYS A  42      -5.046  29.691  23.354  1.00 37.80           C  
ATOM    321  NZ  LYS A  42      -5.657  28.613  22.476  1.00 42.21           N  
ATOM    322  N   HIS A  43      -3.526  27.142  29.845  1.00 18.89           N  
ATOM    323  CA  HIS A  43      -3.867  26.644  31.152  1.00 13.21           C  
ATOM    324  C   HIS A  43      -3.701  27.762  32.182  1.00 17.36           C  
ATOM    325  O   HIS A  43      -2.844  28.627  32.026  1.00 14.21           O  
ATOM    326  CB  HIS A  43      -2.986  25.448  31.452  1.00 16.40           C  
ATOM    327  CG  HIS A  43      -3.300  24.276  30.588  1.00 18.66           C  
ATOM    328  ND1 HIS A  43      -2.338  23.677  29.815  1.00 24.24           N  
ATOM    329  CD2 HIS A  43      -4.473  23.647  30.399  1.00 19.72           C  
ATOM    330  CE1 HIS A  43      -2.954  22.695  29.192  1.00 24.75           C  
ATOM    331  NE2 HIS A  43      -4.248  22.639  29.516  1.00 14.35           N  
ATOM    332  N   LEU A  44      -4.509  27.730  33.244  1.00 16.82           N  
ATOM    333  CA  LEU A  44      -4.480  28.773  34.273  1.00 18.28           C  
ATOM    334  C   LEU A  44      -3.873  28.426  35.644  1.00 16.73           C  
ATOM    335  O   LEU A  44      -4.034  27.313  36.138  1.00 19.42           O  
ATOM    336  CB  LEU A  44      -5.899  29.315  34.464  1.00 17.12           C  
ATOM    337  CG  LEU A  44      -6.576  29.847  33.192  1.00 18.55           C  
ATOM    338  CD1 LEU A  44      -7.922  30.397  33.512  1.00  9.50           C  
ATOM    339  CD2 LEU A  44      -5.723  30.922  32.535  1.00 13.63           C  
ATOM    340  N   PHE A  45      -3.162  29.387  36.234  1.00 15.07           N  
ATOM    341  CA  PHE A  45      -2.525  29.248  37.562  1.00 17.27           C  
ATOM    342  C   PHE A  45      -2.378  30.640  38.184  1.00 18.21           C  
ATOM    343  O   PHE A  45      -2.218  31.630  37.460  1.00 19.09           O  
ATOM    344  CB  PHE A  45      -1.101  28.671  37.473  1.00 16.69           C  
ATOM    345  CG  PHE A  45      -0.987  27.466  36.619  1.00 19.25           C  
ATOM    346  CD1 PHE A  45      -0.770  27.593  35.253  1.00 18.52           C  
ATOM    347  CD2 PHE A  45      -1.159  26.197  37.158  1.00 20.45           C  
ATOM    348  CE1 PHE A  45      -0.727  26.472  34.419  1.00 16.38           C  
ATOM    349  CE2 PHE A  45      -1.117  25.062  36.340  1.00 22.69           C  
ATOM    350  CZ  PHE A  45      -0.903  25.206  34.952  1.00 21.31           C  
ATOM    351  N   CYS A  46      -2.420  30.719  39.519  1.00 20.99           N  
ATOM    352  CA  CYS A  46      -2.234  32.000  40.216  1.00 20.09           C  
ATOM    353  C   CYS A  46      -0.801  32.391  39.860  1.00 20.75           C  
ATOM    354  O   CYS A  46       0.074  31.523  39.862  1.00 20.57           O  
ATOM    355  CB  CYS A  46      -2.278  31.828  41.747  1.00 19.21           C  
ATOM    356  SG  CYS A  46      -3.595  30.806  42.489  1.00 20.10           S  
ATOM    357  N   ARG A  47      -0.551  33.668  39.561  1.00 25.00           N  
ATOM    358  CA  ARG A  47       0.812  34.143  39.234  1.00 26.48           C  
ATOM    359  C   ARG A  47       1.910  33.579  40.156  1.00 24.57           C  
ATOM    360  O   ARG A  47       2.965  33.198  39.675  1.00 26.66           O  
ATOM    361  CB  ARG A  47       0.871  35.681  39.268  1.00 32.22           C  
ATOM    362  CG  ARG A  47       2.275  36.312  39.243  1.00 31.34           C  
ATOM    363  CD  ARG A  47       2.805  36.600  37.833  1.00 36.45           C  
ATOM    364  NE  ARG A  47       1.882  37.366  36.992  1.00 31.64           N  
ATOM    365  CZ  ARG A  47       1.200  38.432  37.393  1.00 34.62           C  
ATOM    366  NH1 ARG A  47       1.337  38.882  38.631  1.00 36.38           N  
ATOM    367  NH2 ARG A  47       0.317  39.011  36.581  1.00 33.76           N  
ATOM    368  N   ILE A  48       1.672  33.497  41.465  1.00 23.36           N  
ATOM    369  CA  ILE A  48       2.707  32.978  42.343  1.00 27.21           C  
ATOM    370  C   ILE A  48       2.853  31.474  42.300  1.00 28.50           C  
ATOM    371  O   ILE A  48       3.955  30.951  42.464  1.00 34.52           O  
ATOM    372  CB  ILE A  48       2.545  33.394  43.843  1.00 25.77           C  
ATOM    373  CG1 ILE A  48       1.299  32.745  44.452  1.00 31.60           C  
ATOM    374  CG2 ILE A  48       2.516  34.911  43.976  1.00 24.35           C  
ATOM    375  CD1 ILE A  48       1.133  32.982  45.962  1.00 33.13           C  
ATOM    376  N   CYS A  49       1.760  30.761  42.077  1.00 26.91           N  
ATOM    377  CA  CYS A  49       1.864  29.304  42.086  1.00 25.29           C  
ATOM    378  C   CYS A  49       2.685  28.775  40.920  1.00 26.44           C  
ATOM    379  O   CYS A  49       3.556  27.914  41.101  1.00 25.67           O  
ATOM    380  CB  CYS A  49       0.481  28.658  42.119  1.00 21.26           C  
ATOM    381  SG  CYS A  49      -0.464  29.078  43.620  1.00 18.47           S  
ATOM    382  N   ILE A  50       2.449  29.347  39.745  1.00 24.93           N  
ATOM    383  CA  ILE A  50       3.146  28.909  38.546  1.00 27.53           C  
ATOM    384  C   ILE A  50       4.648  29.267  38.550  1.00 28.72           C  
ATOM    385  O   ILE A  50       5.490  28.405  38.303  1.00 26.01           O  
ATOM    386  CB  ILE A  50       2.414  29.388  37.263  1.00 18.69           C  
ATOM    387  CG1 ILE A  50       3.073  28.773  36.027  1.00 20.46           C  
ATOM    388  CG2 ILE A  50       2.332  30.908  37.214  1.00 13.36           C  
ATOM    389  CD1 ILE A  50       3.114  27.249  36.053  1.00 18.09           C  
ATOM    390  N   LEU A  51       4.982  30.494  38.935  1.00 29.33           N  
ATOM    391  CA  LEU A  51       6.378  30.902  38.963  1.00 31.12           C  
ATOM    392  C   LEU A  51       7.209  30.029  39.902  1.00 35.28           C  
ATOM    393  O   LEU A  51       8.375  29.755  39.628  1.00 34.50           O  
ATOM    394  CB  LEU A  51       6.490  32.370  39.365  1.00 29.03           C  
ATOM    395  CG  LEU A  51       6.063  33.352  38.274  1.00 27.75           C  
ATOM    396  CD1 LEU A  51       6.077  34.806  38.759  1.00 24.00           C  
ATOM    397  CD2 LEU A  51       6.997  33.169  37.103  1.00 25.41           C  
ATOM    398  N   ARG A  52       6.620  29.575  41.001  1.00 35.46           N  
ATOM    399  CA  ARG A  52       7.388  28.749  41.910  1.00 38.24           C  
ATOM    400  C   ARG A  52       7.621  27.378  41.295  1.00 40.47           C  
ATOM    401  O   ARG A  52       8.706  26.821  41.419  1.00 42.43           O  
ATOM    402  CB  ARG A  52       6.704  28.649  43.278  1.00 40.03           C  
ATOM    403  CG  ARG A  52       7.410  27.747  44.310  1.00 46.22           C  
ATOM    404  CD  ARG A  52       6.950  26.280  44.246  1.00 52.98           C  
ATOM    405  NE  ARG A  52       5.490  26.185  44.132  1.00 62.84           N  
ATOM    406  CZ  ARG A  52       4.802  25.057  43.927  1.00 65.56           C  
ATOM    407  NH1 ARG A  52       5.422  23.885  43.825  1.00 67.12           N  
ATOM    408  NH2 ARG A  52       3.487  25.113  43.742  1.00 67.46           N  
ATOM    409  N   CYS A  53       6.612  26.845  40.612  1.00 42.51           N  
ATOM    410  CA  CYS A  53       6.720  25.521  39.990  1.00 43.46           C  
ATOM    411  C   CYS A  53       7.727  25.509  38.865  1.00 41.90           C  
ATOM    412  O   CYS A  53       8.365  24.492  38.611  1.00 40.70           O  
ATOM    413  CB  CYS A  53       5.369  25.049  39.447  1.00 45.61           C  
ATOM    414  SG  CYS A  53       4.390  24.099  40.606  1.00 51.97           S  
ATOM    415  N   LEU A  54       7.834  26.637  38.171  1.00 42.28           N  
ATOM    416  CA  LEU A  54       8.768  26.768  37.063  1.00 44.14           C  
ATOM    417  C   LEU A  54      10.180  26.792  37.616  1.00 45.97           C  
ATOM    418  O   LEU A  54      11.114  26.286  36.988  1.00 48.06           O  
ATOM    419  CB  LEU A  54       8.481  28.037  36.271  1.00 41.72           C  
ATOM    420  CG  LEU A  54       7.132  28.019  35.550  1.00 40.32           C  
ATOM    421  CD1 LEU A  54       6.949  29.337  34.831  1.00 42.40           C  
ATOM    422  CD2 LEU A  54       7.045  26.838  34.571  1.00 37.85           C  
ATOM    423  N   LYS A  55      10.319  27.340  38.818  1.00 45.56           N  
ATOM    424  CA  LYS A  55      11.620  27.400  39.451  1.00 46.97           C  
ATOM    425  C   LYS A  55      11.981  26.033  40.055  1.00 45.18           C  
ATOM    426  O   LYS A  55      12.724  25.260  39.464  1.00 45.07           O  
ATOM    427  CB  LYS A  55      11.661  28.514  40.503  1.00 47.69           C  
ATOM    428  CG  LYS A  55      13.052  29.102  40.704  1.00 54.48           C  
ATOM    429  CD  LYS A  55      13.088  30.253  41.729  1.00 61.19           C  
ATOM    430  CE  LYS A  55      12.716  29.778  43.134  1.00 63.86           C  
ATOM    431  NZ  LYS A  55      13.556  28.629  43.610  1.00 64.75           N  
ATOM    432  N   VAL A  56      11.334  25.674  41.151  1.00 43.22           N  
ATOM    433  CA  VAL A  56      11.646  24.424  41.825  1.00 42.41           C  
ATOM    434  C   VAL A  56      11.429  23.117  41.080  1.00 41.23           C  
ATOM    435  O   VAL A  56      12.112  22.142  41.367  1.00 42.68           O  
ATOM    436  CB  VAL A  56      10.935  24.340  43.187  1.00 42.40           C  
ATOM    437  CG1 VAL A  56      11.198  25.617  43.988  1.00 40.43           C  
ATOM    438  CG2 VAL A  56       9.438  24.120  42.993  1.00 45.35           C  
ATOM    439  N   MET A  57      10.520  23.091  40.111  1.00 42.94           N  
ATOM    440  CA  MET A  57      10.228  21.849  39.384  1.00 45.44           C  
ATOM    441  C   MET A  57      10.748  21.717  37.956  1.00 44.98           C  
ATOM    442  O   MET A  57      11.046  20.610  37.500  1.00 46.05           O  
ATOM    443  CB  MET A  57       8.722  21.574  39.384  1.00 49.11           C  
ATOM    444  CG  MET A  57       8.174  21.034  40.693  1.00 53.61           C  
ATOM    445  SD  MET A  57       8.768  19.363  41.034  1.00 56.35           S  
ATOM    446  CE  MET A  57       7.861  18.391  39.774  1.00 56.87           C  
ATOM    447  N   GLY A  58      10.829  22.827  37.236  1.00 41.32           N  
ATOM    448  CA  GLY A  58      11.302  22.749  35.873  1.00 37.27           C  
ATOM    449  C   GLY A  58      10.476  23.635  34.975  1.00 36.38           C  
ATOM    450  O   GLY A  58       9.436  24.162  35.383  1.00 36.50           O  
ATOM    451  N   SER A  59      10.941  23.798  33.744  1.00 33.03           N  
ATOM    452  CA  SER A  59      10.250  24.636  32.792  1.00 32.83           C  
ATOM    453  C   SER A  59       9.283  23.853  31.914  1.00 32.98           C  
ATOM    454  O   SER A  59       9.468  23.725  30.698  1.00 31.09           O  
ATOM    455  CB  SER A  59      11.253  25.462  31.994  1.00 30.71           C  
ATOM    456  OG  SER A  59      11.904  26.364  32.879  1.00 28.18           O  
ATOM    457  N   TYR A  60       8.248  23.336  32.578  1.00 31.06           N  
ATOM    458  CA  TYR A  60       7.176  22.566  31.961  1.00 29.69           C  
ATOM    459  C   TYR A  60       5.845  22.846  32.658  1.00 26.56           C  
ATOM    460  O   TYR A  60       5.809  23.033  33.879  1.00 20.68           O  
ATOM    461  CB  TYR A  60       7.493  21.090  32.062  1.00 32.15           C  
ATOM    462  CG  TYR A  60       8.667  20.698  31.232  1.00 33.88           C  
ATOM    463  CD1 TYR A  60       8.619  20.778  29.838  1.00 34.07           C  
ATOM    464  CD2 TYR A  60       9.831  20.252  31.834  1.00 38.07           C  
ATOM    465  CE1 TYR A  60       9.714  20.423  29.065  1.00 37.45           C  
ATOM    466  CE2 TYR A  60      10.939  19.890  31.072  1.00 40.57           C  
ATOM    467  CZ  TYR A  60      10.870  19.975  29.698  1.00 39.48           C  
ATOM    468  OH  TYR A  60      11.974  19.622  28.974  1.00 42.02           O  
ATOM    469  N   CYS A  61       4.757  22.863  31.888  1.00 24.79           N  
ATOM    470  CA  CYS A  61       3.415  23.127  32.424  1.00 19.81           C  
ATOM    471  C   CYS A  61       2.954  22.023  33.345  1.00 18.29           C  
ATOM    472  O   CYS A  61       2.933  20.854  32.963  1.00 16.57           O  
ATOM    473  CB  CYS A  61       2.391  23.257  31.294  1.00 22.52           C  
ATOM    474  SG  CYS A  61       0.687  23.464  31.869  1.00 23.48           S  
ATOM    475  N   PRO A  62       2.527  22.378  34.567  1.00 19.09           N  
ATOM    476  CA  PRO A  62       2.062  21.358  35.516  1.00 20.38           C  
ATOM    477  C   PRO A  62       0.873  20.540  34.967  1.00 21.58           C  
ATOM    478  O   PRO A  62       0.738  19.355  35.275  1.00 20.98           O  
ATOM    479  CB  PRO A  62       1.656  22.193  36.731  1.00 21.11           C  
ATOM    480  CG  PRO A  62       2.514  23.418  36.621  1.00 17.99           C  
ATOM    481  CD  PRO A  62       2.436  23.721  35.157  1.00 17.96           C  
ATOM    482  N   SER A  63       0.027  21.175  34.152  1.00 22.27           N  
ATOM    483  CA  SER A  63      -1.141  20.516  33.572  1.00 21.56           C  
ATOM    484  C   SER A  63      -0.806  19.559  32.443  1.00 25.34           C  
ATOM    485  O   SER A  63      -1.155  18.374  32.508  1.00 26.08           O  
ATOM    486  CB  SER A  63      -2.127  21.545  33.023  1.00 23.28           C  
ATOM    487  OG  SER A  63      -2.728  22.312  34.050  1.00 32.17           O  
ATOM    488  N   CYS A  64      -0.119  20.067  31.417  1.00 23.17           N  
ATOM    489  CA  CYS A  64       0.198  19.247  30.253  1.00 21.55           C  
ATOM    490  C   CYS A  64       1.647  18.865  29.990  1.00 23.11           C  
ATOM    491  O   CYS A  64       1.922  18.054  29.100  1.00 23.72           O  
ATOM    492  CB  CYS A  64      -0.413  19.873  29.002  1.00 18.17           C  
ATOM    493  SG  CYS A  64       0.238  21.456  28.576  1.00 18.62           S  
ATOM    494  N   ARG A  65       2.573  19.461  30.739  1.00 30.01           N  
ATOM    495  CA  ARG A  65       4.011  19.156  30.629  1.00 30.85           C  
ATOM    496  C   ARG A  65       4.692  19.692  29.386  1.00 30.50           C  
ATOM    497  O   ARG A  65       5.755  19.207  28.994  1.00 31.90           O  
ATOM    498  CB  ARG A  65       4.258  17.642  30.719  1.00 36.38           C  
ATOM    499  CG  ARG A  65       3.897  16.982  32.063  1.00 47.96           C  
ATOM    500  CD  ARG A  65       3.757  15.461  31.907  1.00 51.59           C  
ATOM    501  NE  ARG A  65       2.562  15.120  31.127  1.00 59.29           N  
ATOM    502  CZ  ARG A  65       2.557  14.467  29.955  1.00 63.49           C  
ATOM    503  NH1 ARG A  65       3.694  14.053  29.384  1.00 64.67           N  
ATOM    504  NH2 ARG A  65       1.402  14.250  29.333  1.00 61.69           N  
ATOM    505  N   TYR A  66       4.074  20.678  28.753  1.00 31.64           N  
ATOM    506  CA  TYR A  66       4.632  21.292  27.540  1.00 33.68           C  
ATOM    507  C   TYR A  66       5.565  22.408  28.043  1.00 29.63           C  
ATOM    508  O   TYR A  66       5.255  23.074  29.033  1.00 26.36           O  
ATOM    509  CB  TYR A  66       3.476  21.856  26.692  1.00 39.50           C  
ATOM    510  CG  TYR A  66       3.750  22.073  25.217  1.00 47.68           C  
ATOM    511  CD1 TYR A  66       4.034  20.999  24.375  1.00 51.09           C  
ATOM    512  CD2 TYR A  66       3.678  23.360  24.654  1.00 51.26           C  
ATOM    513  CE1 TYR A  66       4.248  21.193  23.005  1.00 57.55           C  
ATOM    514  CE2 TYR A  66       3.890  23.573  23.291  1.00 54.50           C  
ATOM    515  CZ  TYR A  66       4.174  22.483  22.462  1.00 58.41           C  
ATOM    516  OH  TYR A  66       4.402  22.674  21.104  1.00 55.67           O  
ATOM    517  N   PRO A  67       6.738  22.590  27.402  1.00 29.14           N  
ATOM    518  CA  PRO A  67       7.694  23.631  27.818  1.00 27.79           C  
ATOM    519  C   PRO A  67       6.998  24.942  28.202  1.00 26.09           C  
ATOM    520  O   PRO A  67       6.162  25.442  27.459  1.00 26.65           O  
ATOM    521  CB  PRO A  67       8.585  23.773  26.595  1.00 24.48           C  
ATOM    522  CG  PRO A  67       8.628  22.357  26.083  1.00 25.99           C  
ATOM    523  CD  PRO A  67       7.196  21.919  26.169  1.00 27.18           C  
ATOM    524  N   CYS A  68       7.342  25.469  29.376  1.00 26.58           N  
ATOM    525  CA  CYS A  68       6.721  26.673  29.903  1.00 27.32           C  
ATOM    526  C   CYS A  68       7.699  27.637  30.580  1.00 26.69           C  
ATOM    527  O   CYS A  68       8.406  27.266  31.507  1.00 27.41           O  
ATOM    528  CB  CYS A  68       5.629  26.252  30.898  1.00 27.44           C  
ATOM    529  SG  CYS A  68       4.600  27.590  31.523  1.00 30.87           S  
ATOM    530  N   PHE A  69       7.683  28.899  30.161  1.00 28.36           N  
ATOM    531  CA  PHE A  69       8.584  29.892  30.728  1.00 30.91           C  
ATOM    532  C   PHE A  69       7.874  31.103  31.300  1.00 31.05           C  
ATOM    533  O   PHE A  69       6.831  31.508  30.788  1.00 35.31           O  
ATOM    534  CB  PHE A  69       9.583  30.351  29.655  1.00 33.04           C  
ATOM    535  CG  PHE A  69      10.480  29.247  29.176  1.00 32.64           C  
ATOM    536  CD1 PHE A  69      10.061  28.389  28.172  1.00 30.17           C  
ATOM    537  CD2 PHE A  69      11.703  29.014  29.795  1.00 29.83           C  
ATOM    538  CE1 PHE A  69      10.831  27.283  27.805  1.00 34.59           C  
ATOM    539  CE2 PHE A  69      12.472  27.925  29.441  1.00 36.06           C  
ATOM    540  CZ  PHE A  69      12.036  27.054  28.434  1.00 36.15           C  
ATOM    541  N   PRO A  70       8.429  31.702  32.371  1.00 28.82           N  
ATOM    542  CA  PRO A  70       7.874  32.887  33.040  1.00 30.13           C  
ATOM    543  C   PRO A  70       7.525  33.986  32.061  1.00 31.50           C  
ATOM    544  O   PRO A  70       6.501  34.659  32.193  1.00 32.13           O  
ATOM    545  CB  PRO A  70       9.007  33.312  33.954  1.00 28.28           C  
ATOM    546  CG  PRO A  70       9.490  31.975  34.446  1.00 29.68           C  
ATOM    547  CD  PRO A  70       9.545  31.146  33.158  1.00 27.98           C  
ATOM    548  N   THR A  71       8.351  34.092  31.031  1.00 31.78           N  
ATOM    549  CA  THR A  71       8.182  35.082  29.990  1.00 29.38           C  
ATOM    550  C   THR A  71       6.962  34.818  29.084  1.00 29.03           C  
ATOM    551  O   THR A  71       6.535  35.689  28.329  1.00 24.30           O  
ATOM    552  CB  THR A  71       9.488  35.185  29.176  1.00 32.95           C  
ATOM    553  OG1 THR A  71       9.343  36.178  28.161  1.00 35.00           O  
ATOM    554  CG2 THR A  71       9.880  33.825  28.570  1.00 32.44           C  
ATOM    555  N   ASP A  72       6.377  33.633  29.194  1.00 27.13           N  
ATOM    556  CA  ASP A  72       5.204  33.272  28.397  1.00 29.51           C  
ATOM    557  C   ASP A  72       3.895  33.623  29.116  1.00 30.93           C  
ATOM    558  O   ASP A  72       2.799  33.605  28.510  1.00 27.24           O  
ATOM    559  CB  ASP A  72       5.181  31.761  28.170  1.00 30.27           C  
ATOM    560  CG  ASP A  72       6.048  31.324  27.035  1.00 31.16           C  
ATOM    561  OD1 ASP A  72       5.968  31.966  25.961  1.00 30.94           O  
ATOM    562  OD2 ASP A  72       6.763  30.308  27.217  1.00 33.99           O  
ATOM    563  N   LEU A  73       4.013  33.924  30.410  1.00 28.23           N  
ATOM    564  CA  LEU A  73       2.840  34.183  31.238  1.00 28.33           C  
ATOM    565  C   LEU A  73       2.066  35.456  30.984  1.00 26.64           C  
ATOM    566  O   LEU A  73       2.527  36.544  31.310  1.00 26.81           O  
ATOM    567  CB  LEU A  73       3.199  34.026  32.718  1.00 28.42           C  
ATOM    568  CG  LEU A  73       3.190  32.590  33.287  1.00 30.31           C  
ATOM    569  CD1 LEU A  73       2.988  31.528  32.231  1.00 27.78           C  
ATOM    570  CD2 LEU A  73       4.463  32.319  34.059  1.00 26.76           C  
ATOM    571  N   GLU A  74       0.894  35.309  30.379  1.00 21.92           N  
ATOM    572  CA  GLU A  74       0.051  36.448  30.083  1.00 22.24           C  
ATOM    573  C   GLU A  74      -1.174  36.486  30.958  1.00 22.35           C  
ATOM    574  O   GLU A  74      -1.367  35.635  31.819  1.00 24.58           O  
ATOM    575  CB  GLU A  74      -0.396  36.406  28.628  1.00 25.65           C  
ATOM    576  CG  GLU A  74       0.666  36.860  27.607  1.00 37.15           C  
ATOM    577  CD  GLU A  74       1.175  38.281  27.847  1.00 39.70           C  
ATOM    578  OE1 GLU A  74       0.350  39.240  27.863  1.00 46.86           O  
ATOM    579  OE2 GLU A  74       2.405  38.431  28.029  1.00 35.23           O  
ATOM    580  N   SER A  75      -2.002  37.495  30.745  1.00 22.82           N  
ATOM    581  CA  SER A  75      -3.233  37.615  31.496  1.00 22.14           C  
ATOM    582  C   SER A  75      -4.354  36.958  30.684  1.00 22.64           C  
ATOM    583  O   SER A  75      -4.324  36.979  29.457  1.00 18.26           O  
ATOM    584  CB  SER A  75      -3.552  39.086  31.711  1.00 25.12           C  
ATOM    585  OG  SER A  75      -4.810  39.222  32.332  1.00 28.16           O  
ATOM    586  N   PRO A  76      -5.310  36.289  31.352  1.00 20.62           N  
ATOM    587  CA  PRO A  76      -6.406  35.658  30.608  1.00 17.77           C  
ATOM    588  C   PRO A  76      -7.182  36.754  29.867  1.00 16.67           C  
ATOM    589  O   PRO A  76      -7.212  37.919  30.302  1.00 13.29           O  
ATOM    590  CB  PRO A  76      -7.286  35.076  31.723  1.00 12.83           C  
ATOM    591  CG  PRO A  76      -6.326  34.787  32.796  1.00 14.49           C  
ATOM    592  CD  PRO A  76      -5.413  35.977  32.790  1.00 19.31           C  
ATOM    593  N   VAL A  77      -7.845  36.360  28.788  1.00 11.34           N  
ATOM    594  CA  VAL A  77      -8.646  37.263  27.983  1.00 14.67           C  
ATOM    595  C   VAL A  77      -9.620  38.019  28.914  1.00 18.65           C  
ATOM    596  O   VAL A  77      -9.973  37.527  29.983  1.00 20.56           O  
ATOM    597  CB  VAL A  77      -9.365  36.434  26.903  1.00 14.65           C  
ATOM    598  CG1 VAL A  77     -10.682  35.903  27.415  1.00 14.96           C  
ATOM    599  CG2 VAL A  77      -9.489  37.195  25.607  1.00 21.32           C  
ATOM    600  N   LYS A  78     -10.077  39.193  28.496  1.00 24.24           N  
ATOM    601  CA  LYS A  78     -10.962  40.016  29.327  1.00 23.92           C  
ATOM    602  C   LYS A  78     -12.268  39.351  29.750  1.00 24.57           C  
ATOM    603  O   LYS A  78     -12.639  39.402  30.930  1.00 24.17           O  
ATOM    604  CB  LYS A  78     -11.285  41.337  28.632  1.00 24.64           C  
ATOM    605  CG  LYS A  78     -12.169  42.242  29.483  1.00 30.36           C  
ATOM    606  CD  LYS A  78     -11.412  42.702  30.735  1.00 37.89           C  
ATOM    607  CE  LYS A  78     -12.271  43.555  31.677  1.00 41.89           C  
ATOM    608  NZ  LYS A  78     -13.073  44.626  30.986  1.00 47.12           N  
ATOM    609  N   SER A  79     -12.975  38.770  28.774  1.00 23.81           N  
ATOM    610  CA  SER A  79     -14.257  38.091  29.019  1.00 23.41           C  
ATOM    611  C   SER A  79     -14.163  36.994  30.051  1.00 22.05           C  
ATOM    612  O   SER A  79     -15.150  36.707  30.721  1.00 24.71           O  
ATOM    613  CB  SER A  79     -14.843  37.515  27.730  1.00 20.80           C  
ATOM    614  OG  SER A  79     -14.837  38.508  26.722  1.00 26.79           O  
ATOM    615  N   PHE A  80     -13.005  36.343  30.143  1.00 19.55           N  
ATOM    616  CA  PHE A  80     -12.838  35.299  31.150  1.00 19.16           C  
ATOM    617  C   PHE A  80     -12.671  35.984  32.486  1.00 19.28           C  
ATOM    618  O   PHE A  80     -13.284  35.595  33.476  1.00 21.01           O  
ATOM    619  CB  PHE A  80     -11.623  34.416  30.898  1.00 16.88           C  
ATOM    620  CG  PHE A  80     -11.433  33.383  31.961  1.00 16.44           C  
ATOM    621  CD1 PHE A  80     -12.289  32.286  32.038  1.00 16.88           C  
ATOM    622  CD2 PHE A  80     -10.486  33.556  32.956  1.00 12.56           C  
ATOM    623  CE1 PHE A  80     -12.197  31.381  33.107  1.00 14.74           C  
ATOM    624  CE2 PHE A  80     -10.389  32.660  34.027  1.00 13.31           C  
ATOM    625  CZ  PHE A  80     -11.242  31.579  34.102  1.00  9.67           C  
ATOM    626  N   LEU A  81     -11.831  37.012  32.516  1.00 21.19           N  
ATOM    627  CA  LEU A  81     -11.635  37.761  33.751  1.00 19.00           C  
ATOM    628  C   LEU A  81     -12.958  38.285  34.296  1.00 21.01           C  
ATOM    629  O   LEU A  81     -13.148  38.335  35.509  1.00 18.13           O  
ATOM    630  CB  LEU A  81     -10.693  38.939  33.544  1.00 16.56           C  
ATOM    631  CG  LEU A  81      -9.248  38.578  33.258  1.00 17.38           C  
ATOM    632  CD1 LEU A  81      -8.472  39.866  33.284  1.00 18.20           C  
ATOM    633  CD2 LEU A  81      -8.699  37.572  34.302  1.00 17.60           C  
ATOM    634  N   ASN A  82     -13.865  38.679  33.403  1.00 19.94           N  
ATOM    635  CA  ASN A  82     -15.165  39.195  33.829  1.00 23.79           C  
ATOM    636  C   ASN A  82     -16.023  38.153  34.538  1.00 24.83           C  
ATOM    637  O   ASN A  82     -16.707  38.468  35.517  1.00 23.24           O  
ATOM    638  CB  ASN A  82     -15.940  39.745  32.638  1.00 27.35           C  
ATOM    639  CG  ASN A  82     -15.372  41.048  32.110  1.00 25.55           C  
ATOM    640  OD1 ASN A  82     -15.799  41.531  31.062  1.00 26.78           O  
ATOM    641  ND2 ASN A  82     -14.423  41.630  32.830  1.00 23.60           N  
ATOM    642  N   ILE A  83     -15.995  36.919  34.029  1.00 21.10           N  
ATOM    643  CA  ILE A  83     -16.761  35.813  34.604  1.00 17.83           C  
ATOM    644  C   ILE A  83     -16.198  35.447  35.995  1.00 19.80           C  
ATOM    645  O   ILE A  83     -16.929  35.305  36.991  1.00 18.49           O  
ATOM    646  CB  ILE A  83     -16.729  34.608  33.644  1.00 15.62           C  
ATOM    647  CG1 ILE A  83     -17.561  34.937  32.385  1.00 15.00           C  
ATOM    648  CG2 ILE A  83     -17.229  33.383  34.346  1.00 13.59           C  
ATOM    649  CD1 ILE A  83     -17.307  34.050  31.151  1.00  5.23           C  
ATOM    650  N   LEU A  84     -14.877  35.380  36.060  1.00 21.12           N  
ATOM    651  CA  LEU A  84     -14.164  35.077  37.286  1.00 21.52           C  
ATOM    652  C   LEU A  84     -14.381  36.164  38.337  1.00 21.27           C  
ATOM    653  O   LEU A  84     -14.793  35.870  39.447  1.00 25.42           O  
ATOM    654  CB  LEU A  84     -12.672  34.964  36.984  1.00 18.68           C  
ATOM    655  CG  LEU A  84     -11.728  34.926  38.181  1.00 22.94           C  
ATOM    656  CD1 LEU A  84     -11.756  33.524  38.812  1.00 16.13           C  
ATOM    657  CD2 LEU A  84     -10.303  35.318  37.723  1.00 15.93           C  
ATOM    658  N   ASN A  85     -14.108  37.416  37.982  1.00 23.83           N  
ATOM    659  CA  ASN A  85     -14.250  38.539  38.921  1.00 25.37           C  
ATOM    660  C   ASN A  85     -15.672  38.786  39.443  1.00 26.61           C  
ATOM    661  O   ASN A  85     -15.857  39.519  40.429  1.00 25.78           O  
ATOM    662  CB  ASN A  85     -13.667  39.836  38.328  1.00 21.72           C  
ATOM    663  CG  ASN A  85     -12.143  39.869  38.367  1.00 17.00           C  
ATOM    664  OD1 ASN A  85     -11.532  39.582  39.402  1.00 19.52           O  
ATOM    665  ND2 ASN A  85     -11.520  40.230  37.241  1.00 18.15           N  
ATOM    666  N   SER A  86     -16.656  38.148  38.800  1.00 25.88           N  
ATOM    667  CA  SER A  86     -18.064  38.276  39.190  1.00 26.01           C  
ATOM    668  C   SER A  86     -18.624  37.152  40.054  1.00 24.39           C  
ATOM    669  O   SER A  86     -19.730  37.286  40.598  1.00 22.44           O  
ATOM    670  CB  SER A  86     -18.916  38.391  37.954  1.00 25.42           C  
ATOM    671  OG  SER A  86     -18.444  39.466  37.180  1.00 36.49           O  
ATOM    672  N   LEU A  87     -17.883  36.049  40.170  1.00 21.89           N  
ATOM    673  CA  LEU A  87     -18.350  34.901  40.965  1.00 25.13           C  
ATOM    674  C   LEU A  87     -18.838  35.333  42.363  1.00 25.74           C  
ATOM    675  O   LEU A  87     -18.181  36.122  43.048  1.00 29.50           O  
ATOM    676  CB  LEU A  87     -17.242  33.832  41.131  1.00 19.45           C  
ATOM    677  CG  LEU A  87     -16.568  33.150  39.944  1.00 20.31           C  
ATOM    678  CD1 LEU A  87     -15.600  32.069  40.458  1.00 15.57           C  
ATOM    679  CD2 LEU A  87     -17.610  32.532  39.021  1.00 22.11           C  
ATOM    680  N   MET A  88     -19.993  34.834  42.783  1.00 22.15           N  
ATOM    681  CA  MET A  88     -20.480  35.204  44.098  1.00 21.50           C  
ATOM    682  C   MET A  88     -19.891  34.249  45.158  1.00 23.27           C  
ATOM    683  O   MET A  88     -19.851  33.024  44.978  1.00 18.18           O  
ATOM    684  CB  MET A  88     -22.005  35.191  44.107  1.00 23.56           C  
ATOM    685  CG  MET A  88     -22.636  36.242  43.198  1.00 24.27           C  
ATOM    686  SD  MET A  88     -22.080  37.918  43.629  1.00 33.14           S  
ATOM    687  CE  MET A  88     -22.740  38.074  45.303  1.00 24.99           C  
ATOM    688  N   VAL A  89     -19.396  34.809  46.252  1.00 21.49           N  
ATOM    689  CA  VAL A  89     -18.819  33.983  47.296  1.00 24.33           C  
ATOM    690  C   VAL A  89     -19.399  34.279  48.686  1.00 23.95           C  
ATOM    691  O   VAL A  89     -19.720  35.425  49.007  1.00 22.93           O  
ATOM    692  CB  VAL A  89     -17.273  34.075  47.259  1.00 24.73           C  
ATOM    693  CG1 VAL A  89     -16.849  35.422  46.670  1.00 29.09           C  
ATOM    694  CG2 VAL A  89     -16.670  33.862  48.649  1.00 23.27           C  
ATOM    695  N   LYS A  90     -19.638  33.214  49.449  1.00 23.80           N  
ATOM    696  CA  LYS A  90     -20.172  33.309  50.794  1.00 22.73           C  
ATOM    697  C   LYS A  90     -19.071  33.594  51.806  1.00 23.20           C  
ATOM    698  O   LYS A  90     -18.237  32.727  52.113  1.00 23.38           O  
ATOM    699  CB  LYS A  90     -20.900  32.010  51.190  1.00 21.99           C  
ATOM    700  CG  LYS A  90     -22.244  31.784  50.482  1.00 29.52           C  
ATOM    701  CD  LYS A  90     -22.770  30.364  50.713  1.00 33.17           C  
ATOM    702  CE  LYS A  90     -21.729  29.329  50.271  1.00 33.76           C  
ATOM    703  NZ  LYS A  90     -22.174  27.932  50.458  1.00 32.52           N  
ATOM    704  N   CYS A  91     -19.100  34.802  52.359  1.00 23.19           N  
ATOM    705  CA  CYS A  91     -18.131  35.221  53.377  1.00 22.75           C  
ATOM    706  C   CYS A  91     -18.319  34.296  54.585  1.00 17.45           C  
ATOM    707  O   CYS A  91     -19.432  34.075  55.027  1.00 17.88           O  
ATOM    708  CB  CYS A  91     -18.382  36.683  53.761  1.00 21.78           C  
ATOM    709  SG  CYS A  91     -17.492  37.214  55.219  1.00 29.76           S  
ATOM    710  N   PRO A  92     -17.229  33.682  55.074  1.00 18.69           N  
ATOM    711  CA  PRO A  92     -17.215  32.753  56.213  1.00 17.31           C  
ATOM    712  C   PRO A  92     -17.010  33.400  57.599  1.00 18.54           C  
ATOM    713  O   PRO A  92     -16.866  32.720  58.621  1.00 16.19           O  
ATOM    714  CB  PRO A  92     -16.075  31.795  55.846  1.00 13.85           C  
ATOM    715  CG  PRO A  92     -15.060  32.742  55.241  1.00 13.62           C  
ATOM    716  CD  PRO A  92     -15.904  33.747  54.419  1.00 12.09           C  
ATOM    717  N   ALA A  93     -16.968  34.719  57.630  1.00 20.05           N  
ATOM    718  CA  ALA A  93     -16.811  35.404  58.904  1.00 26.05           C  
ATOM    719  C   ALA A  93     -18.029  35.046  59.767  1.00 28.10           C  
ATOM    720  O   ALA A  93     -19.160  35.103  59.289  1.00 25.99           O  
ATOM    721  CB  ALA A  93     -16.741  36.909  58.682  1.00 23.33           C  
ATOM    722  N   GLN A  94     -17.784  34.690  61.029  1.00 31.29           N  
ATOM    723  CA  GLN A  94     -18.825  34.306  61.991  1.00 34.99           C  
ATOM    724  C   GLN A  94     -20.075  35.194  61.999  1.00 35.18           C  
ATOM    725  O   GLN A  94     -19.973  36.407  62.148  1.00 36.82           O  
ATOM    726  CB  GLN A  94     -18.196  34.284  63.381  1.00 40.92           C  
ATOM    727  CG  GLN A  94     -19.080  33.814  64.514  1.00 48.43           C  
ATOM    728  CD  GLN A  94     -18.293  33.655  65.812  1.00 51.14           C  
ATOM    729  OE1 GLN A  94     -17.446  34.494  66.151  1.00 52.09           O  
ATOM    730  NE2 GLN A  94     -18.554  32.567  66.530  1.00 46.26           N  
ATOM    731  N   ASP A  95     -21.246  34.579  61.822  1.00 38.41           N  
ATOM    732  CA  ASP A  95     -22.538  35.281  61.807  1.00 41.86           C  
ATOM    733  C   ASP A  95     -22.837  36.207  60.637  1.00 43.09           C  
ATOM    734  O   ASP A  95     -23.920  36.801  60.560  1.00 43.18           O  
ATOM    735  CB  ASP A  95     -22.777  36.030  63.114  1.00 49.33           C  
ATOM    736  CG  ASP A  95     -23.367  35.140  64.180  1.00 55.18           C  
ATOM    737  OD1 ASP A  95     -24.607  34.946  64.168  1.00 59.22           O  
ATOM    738  OD2 ASP A  95     -22.594  34.617  65.013  1.00 59.45           O  
ATOM    739  N   CYS A  96     -21.861  36.380  59.754  1.00 43.30           N  
ATOM    740  CA  CYS A  96     -22.058  37.201  58.570  1.00 39.18           C  
ATOM    741  C   CYS A  96     -22.700  36.284  57.535  1.00 38.15           C  
ATOM    742  O   CYS A  96     -22.202  35.184  57.250  1.00 36.88           O  
ATOM    743  CB  CYS A  96     -20.729  37.728  58.041  1.00 37.17           C  
ATOM    744  SG  CYS A  96     -20.944  38.636  56.525  1.00 29.25           S  
ATOM    745  N   ASN A  97     -23.837  36.701  57.012  1.00 36.69           N  
ATOM    746  CA  ASN A  97     -24.509  35.871  56.028  1.00 41.55           C  
ATOM    747  C   ASN A  97     -24.614  36.670  54.755  1.00 39.87           C  
ATOM    748  O   ASN A  97     -25.688  36.842  54.161  1.00 39.81           O  
ATOM    749  CB  ASN A  97     -25.876  35.418  56.551  1.00 45.46           C  
ATOM    750  CG  ASN A  97     -25.758  34.518  57.784  1.00 50.18           C  
ATOM    751  OD1 ASN A  97     -25.540  33.310  57.670  1.00 49.29           O  
ATOM    752  ND2 ASN A  97     -25.873  35.118  58.971  1.00 56.91           N  
ATOM    753  N   GLU A  98     -23.454  37.139  54.334  1.00 37.52           N  
ATOM    754  CA  GLU A  98     -23.354  37.965  53.157  1.00 36.78           C  
ATOM    755  C   GLU A  98     -22.602  37.276  52.040  1.00 31.54           C  
ATOM    756  O   GLU A  98     -21.647  36.531  52.263  1.00 30.48           O  
ATOM    757  CB  GLU A  98     -22.680  39.290  53.527  1.00 41.62           C  
ATOM    758  CG  GLU A  98     -23.611  40.484  53.610  1.00 44.57           C  
ATOM    759  CD  GLU A  98     -23.351  41.455  52.475  1.00 51.60           C  
ATOM    760  OE1 GLU A  98     -23.742  41.151  51.326  1.00 55.54           O  
ATOM    761  OE2 GLU A  98     -22.722  42.507  52.717  1.00 54.82           O  
ATOM    762  N   GLU A  99     -23.078  37.516  50.833  1.00 27.11           N  
ATOM    763  CA  GLU A  99     -22.485  36.970  49.639  1.00 24.01           C  
ATOM    764  C   GLU A  99     -22.030  38.172  48.813  1.00 24.61           C  
ATOM    765  O   GLU A  99     -22.768  39.137  48.680  1.00 26.26           O  
ATOM    766  CB  GLU A  99     -23.533  36.132  48.890  1.00 17.37           C  
ATOM    767  CG  GLU A  99     -24.190  35.077  49.793  1.00 21.60           C  
ATOM    768  CD  GLU A  99     -24.978  33.992  49.044  1.00 26.22           C  
ATOM    769  OE1 GLU A  99     -25.274  34.161  47.837  1.00 32.80           O  
ATOM    770  OE2 GLU A  99     -25.310  32.957  49.669  1.00 25.37           O  
ATOM    771  N   VAL A 100     -20.800  38.142  48.306  1.00 23.33           N  
ATOM    772  CA  VAL A 100     -20.281  39.242  47.494  1.00 22.73           C  
ATOM    773  C   VAL A 100     -19.445  38.706  46.317  1.00 23.67           C  
ATOM    774  O   VAL A 100     -18.942  37.574  46.357  1.00 23.12           O  
ATOM    775  CB  VAL A 100     -19.374  40.194  48.322  1.00 24.46           C  
ATOM    776  CG1 VAL A 100     -20.163  40.899  49.401  1.00 23.70           C  
ATOM    777  CG2 VAL A 100     -18.219  39.415  48.935  1.00 26.22           C  
ATOM    778  N   SER A 101     -19.259  39.546  45.300  1.00 23.21           N  
ATOM    779  CA  SER A 101     -18.489  39.179  44.121  1.00 22.66           C  
ATOM    780  C   SER A 101     -17.016  39.086  44.484  1.00 24.59           C  
ATOM    781  O   SER A 101     -16.565  39.724  45.435  1.00 25.14           O  
ATOM    782  CB  SER A 101     -18.669  40.207  43.020  1.00 22.12           C  
ATOM    783  OG  SER A 101     -17.914  41.355  43.305  1.00 22.63           O  
ATOM    784  N   LEU A 102     -16.275  38.312  43.700  1.00 23.34           N  
ATOM    785  CA  LEU A 102     -14.858  38.096  43.922  1.00 21.08           C  
ATOM    786  C   LEU A 102     -14.069  39.393  43.949  1.00 24.68           C  
ATOM    787  O   LEU A 102     -13.154  39.543  44.759  1.00 28.23           O  
ATOM    788  CB  LEU A 102     -14.289  37.194  42.836  1.00 16.36           C  
ATOM    789  CG  LEU A 102     -12.902  36.672  43.200  1.00 18.20           C  
ATOM    790  CD1 LEU A 102     -13.047  35.750  44.410  1.00 15.32           C  
ATOM    791  CD2 LEU A 102     -12.268  35.936  42.020  1.00 15.92           C  
ATOM    792  N   GLU A 103     -14.419  40.338  43.081  1.00 25.44           N  
ATOM    793  CA  GLU A 103     -13.703  41.614  43.038  1.00 28.39           C  
ATOM    794  C   GLU A 103     -14.046  42.516  44.218  1.00 28.88           C  
ATOM    795  O   GLU A 103     -13.235  43.334  44.634  1.00 30.22           O  
ATOM    796  CB  GLU A 103     -13.958  42.333  41.719  1.00 31.94           C  
ATOM    797  CG  GLU A 103     -15.415  42.633  41.448  1.00 35.60           C  
ATOM    798  CD  GLU A 103     -15.699  43.075  40.011  1.00 37.94           C  
ATOM    799  OE1 GLU A 103     -14.758  43.181  39.172  1.00 34.14           O  
ATOM    800  OE2 GLU A 103     -16.895  43.308  39.722  1.00 41.34           O  
ATOM    801  N   LYS A 104     -15.233  42.338  44.791  1.00 27.92           N  
ATOM    802  CA  LYS A 104     -15.624  43.142  45.943  1.00 28.65           C  
ATOM    803  C   LYS A 104     -15.330  42.450  47.276  1.00 26.34           C  
ATOM    804  O   LYS A 104     -15.541  43.025  48.338  1.00 25.96           O  
ATOM    805  CB  LYS A 104     -17.105  43.527  45.861  1.00 31.82           C  
ATOM    806  CG  LYS A 104     -17.384  44.676  44.881  1.00 42.42           C  
ATOM    807  CD  LYS A 104     -18.830  45.218  44.956  1.00 48.19           C  
ATOM    808  CE  LYS A 104     -19.234  45.698  46.381  1.00 55.05           C  
ATOM    809  NZ  LYS A 104     -18.388  46.794  46.985  1.00 51.48           N  
ATOM    810  N   TYR A 105     -14.758  41.255  47.219  1.00 22.52           N  
ATOM    811  CA  TYR A 105     -14.477  40.512  48.425  1.00 24.17           C  
ATOM    812  C   TYR A 105     -13.489  41.144  49.389  1.00 26.48           C  
ATOM    813  O   TYR A 105     -13.821  41.340  50.545  1.00 28.78           O  
ATOM    814  CB  TYR A 105     -14.056  39.101  48.086  1.00 22.59           C  
ATOM    815  CG  TYR A 105     -13.988  38.200  49.287  1.00 21.82           C  
ATOM    816  CD1 TYR A 105     -15.138  37.621  49.819  1.00 20.81           C  
ATOM    817  CD2 TYR A 105     -12.764  37.877  49.856  1.00 19.26           C  
ATOM    818  CE1 TYR A 105     -15.060  36.737  50.890  1.00 22.58           C  
ATOM    819  CE2 TYR A 105     -12.675  37.000  50.916  1.00 18.53           C  
ATOM    820  CZ  TYR A 105     -13.814  36.429  51.431  1.00 21.12           C  
ATOM    821  OH  TYR A 105     -13.682  35.548  52.489  1.00 21.01           O  
ATOM    822  N   ASN A 106     -12.277  41.449  48.946  1.00 29.75           N  
ATOM    823  CA  ASN A 106     -11.302  42.070  49.844  1.00 34.70           C  
ATOM    824  C   ASN A 106     -11.812  43.329  50.530  1.00 37.34           C  
ATOM    825  O   ASN A 106     -11.424  43.633  51.654  1.00 38.52           O  
ATOM    826  CB  ASN A 106     -10.027  42.392  49.097  1.00 35.62           C  
ATOM    827  CG  ASN A 106      -9.322  41.156  48.637  1.00 39.60           C  
ATOM    828  OD1 ASN A 106      -9.894  40.065  48.650  1.00 40.86           O  
ATOM    829  ND2 ASN A 106      -8.063  41.302  48.250  1.00 42.02           N  
ATOM    830  N   HIS A 107     -12.666  44.074  49.844  1.00 38.96           N  
ATOM    831  CA  HIS A 107     -13.219  45.280  50.416  1.00 36.98           C  
ATOM    832  C   HIS A 107     -14.216  44.923  51.498  1.00 35.40           C  
ATOM    833  O   HIS A 107     -14.320  45.628  52.508  1.00 33.78           O  
ATOM    834  CB  HIS A 107     -13.907  46.130  49.352  1.00 41.59           C  
ATOM    835  CG  HIS A 107     -14.588  47.335  49.916  1.00 45.33           C  
ATOM    836  ND1 HIS A 107     -13.890  48.384  50.490  1.00 45.00           N  
ATOM    837  CD2 HIS A 107     -15.899  47.637  50.069  1.00 45.18           C  
ATOM    838  CE1 HIS A 107     -14.740  49.267  50.967  1.00 46.58           C  
ATOM    839  NE2 HIS A 107     -15.971  48.837  50.726  1.00 47.09           N  
ATOM    840  N   HIS A 108     -14.978  43.852  51.263  1.00 34.78           N  
ATOM    841  CA  HIS A 108     -15.969  43.388  52.230  1.00 32.97           C  
ATOM    842  C   HIS A 108     -15.273  42.867  53.461  1.00 35.13           C  
ATOM    843  O   HIS A 108     -15.733  43.126  54.577  1.00 40.68           O  
ATOM    844  CB  HIS A 108     -16.865  42.274  51.670  1.00 30.56           C  
ATOM    845  CG  HIS A 108     -17.694  41.582  52.722  1.00 31.68           C  
ATOM    846  ND1 HIS A 108     -18.828  42.116  53.279  1.00 30.07           N  
ATOM    847  CD2 HIS A 108     -17.518  40.387  53.341  1.00 31.24           C  
ATOM    848  CE1 HIS A 108     -19.301  41.257  54.203  1.00 28.52           C  
ATOM    849  NE2 HIS A 108     -18.545  40.184  54.287  1.00 27.49           N  
ATOM    850  N   VAL A 109     -14.197  42.104  53.276  1.00 31.57           N  
ATOM    851  CA  VAL A 109     -13.504  41.572  54.427  1.00 33.74           C  
ATOM    852  C   VAL A 109     -13.002  42.698  55.308  1.00 36.30           C  
ATOM    853  O   VAL A 109     -13.346  42.741  56.493  1.00 35.92           O  
ATOM    854  CB  VAL A 109     -12.360  40.571  54.068  1.00 33.17           C  
ATOM    855  CG1 VAL A 109     -12.946  39.350  53.393  1.00 33.15           C  
ATOM    856  CG2 VAL A 109     -11.322  41.203  53.173  1.00 35.09           C  
ATOM    857  N   SER A 110     -12.314  43.668  54.699  1.00 37.79           N  
ATOM    858  CA  SER A 110     -11.737  44.803  55.421  1.00 41.68           C  
ATOM    859  C   SER A 110     -12.809  45.609  56.127  1.00 44.42           C  
ATOM    860  O   SER A 110     -12.737  45.852  57.338  1.00 47.40           O  
ATOM    861  CB  SER A 110     -10.982  45.722  54.468  1.00 42.78           C  
ATOM    862  OG  SER A 110     -11.885  46.557  53.762  1.00 50.84           O  
ATOM    863  N   SER A 111     -13.834  45.982  55.374  1.00 44.02           N  
ATOM    864  CA  SER A 111     -14.927  46.757  55.926  1.00 45.10           C  
ATOM    865  C   SER A 111     -15.621  46.077  57.116  1.00 43.59           C  
ATOM    866  O   SER A 111     -16.446  46.694  57.779  1.00 46.57           O  
ATOM    867  CB  SER A 111     -15.932  47.076  54.823  1.00 45.68           C  
ATOM    868  OG  SER A 111     -16.439  45.886  54.239  1.00 51.83           O  
ATOM    869  N   HIS A 112     -15.292  44.816  57.383  1.00 43.66           N  
ATOM    870  CA  HIS A 112     -15.889  44.085  58.504  1.00 46.06           C  
ATOM    871  C   HIS A 112     -15.562  44.847  59.780  1.00 48.01           C  
ATOM    872  O   HIS A 112     -14.414  45.246  59.980  1.00 51.76           O  
ATOM    873  CB  HIS A 112     -15.311  42.661  58.599  1.00 44.84           C  
ATOM    874  CG  HIS A 112     -16.281  41.579  58.233  1.00 45.59           C  
ATOM    875  ND1 HIS A 112     -17.227  41.064  59.100  1.00 48.58           N  
ATOM    876  CD2 HIS A 112     -16.445  40.890  57.072  1.00 40.51           C  
ATOM    877  CE1 HIS A 112     -17.915  40.104  58.458  1.00 43.64           C  
ATOM    878  NE2 HIS A 112     -17.480  39.956  57.219  1.00 37.06           N  
ATOM    879  N   LYS A 113     -16.566  45.067  60.627  1.00 49.06           N  
ATOM    880  CA  LYS A 113     -16.373  45.796  61.887  1.00 49.63           C  
ATOM    881  C   LYS A 113     -15.670  44.911  62.930  1.00 48.39           C  
ATOM    882  O   LYS A 113     -16.108  43.796  63.201  1.00 46.16           O  
ATOM    883  CB  LYS A 113     -17.730  46.291  62.409  1.00 53.52           C  
ATOM    884  CG  LYS A 113     -17.688  47.365  63.497  1.00 58.56           C  
ATOM    885  CD  LYS A 113     -17.234  48.718  62.943  1.00 64.88           C  
ATOM    886  CE  LYS A 113     -17.370  49.835  63.998  1.00 67.80           C  
ATOM    887  NZ  LYS A 113     -16.774  51.160  63.600  1.00 64.07           N  
ATOM    888  N   GLU A 114     -14.564  45.402  63.487  1.00 50.24           N  
ATOM    889  CA  GLU A 114     -13.804  44.643  64.487  1.00 54.08           C  
ATOM    890  C   GLU A 114     -14.432  44.733  65.890  1.00 55.75           C  
ATOM    891  O   GLU A 114     -15.382  45.496  66.091  1.00 55.61           O  
ATOM    892  CB  GLU A 114     -12.349  45.136  64.539  1.00 56.18           C  
ATOM    893  CG  GLU A 114     -11.539  45.041  63.231  1.00 58.02           C  
ATOM    894  CD  GLU A 114     -10.016  45.190  63.453  1.00 61.52           C  
ATOM    895  OE1 GLU A 114      -9.579  45.289  64.617  1.00 63.05           O  
ATOM    896  OE2 GLU A 114      -9.240  45.179  62.475  1.00 60.48           O  
ATOM    897  N   SER A 115     -13.909  43.958  66.848  1.00 57.04           N  
ATOM    898  CA  SER A 115     -14.410  43.967  68.233  1.00 60.26           C  
ATOM    899  C   SER A 115     -14.097  45.294  68.957  1.00 64.33           C  
ATOM    900  O   SER A 115     -14.948  46.189  68.995  1.00 66.97           O  
ATOM    901  CB  SER A 115     -13.855  42.773  69.025  1.00 56.54           C  
ATOM    902  OG  SER A 115     -14.325  41.546  68.497  1.00 49.56           O  
ATOM    903  N   LYS A 116     -12.917  45.391  69.574  1.00 67.23           N  
ATOM    904  CA  LYS A 116     -12.447  46.605  70.266  1.00 70.68           C  
ATOM    905  C   LYS A 116     -13.443  47.331  71.180  1.00 72.84           C  
ATOM    906  O   LYS A 116     -12.991  48.296  71.847  1.00 73.36           O  
ATOM    907  CB  LYS A 116     -11.890  47.605  69.257  1.00 71.75           C  
ATOM    908  CG  LYS A 116     -10.857  47.017  68.362  1.00 73.74           C  
ATOM    909  CD  LYS A 116     -10.280  48.046  67.430  1.00 76.40           C  
ATOM    910  CE  LYS A 116      -9.353  47.345  66.476  1.00 77.72           C  
ATOM    911  NZ  LYS A 116      -8.413  48.212  65.726  1.00 78.48           N  
TER     912      LYS A 116                                                      
HETATM  913 ZN    ZN A 117      -3.674  28.883  46.574  1.00 23.28          ZN  
HETATM  914 ZN    ZN A 118      -2.582  28.847  42.854  1.00 24.14          ZN  
HETATM  915 ZN    ZN A 119      -0.311  23.240  29.837  1.00 23.33          ZN  
HETATM  916 ZN    ZN A 120     -18.665  39.074  55.936  1.00 34.77          ZN  
HETATM  917  O   HOH A 200      -8.645  41.408  37.078  1.00 32.34           O  
HETATM  918  O   HOH A 201     -22.203  34.367  53.789  1.00 28.66           O  
HETATM  919  O   HOH A 202     -21.025  31.496  42.941  1.00 11.52           O  
HETATM  920  O   HOH A 203     -10.979  23.198  42.905  1.00 35.10           O  
HETATM  921  O   HOH A 204      -6.441  21.665  28.398  1.00 22.93           O  
HETATM  922  O   HOH A 205      -7.924  33.755  27.548  1.00 17.21           O  
HETATM  923  O   HOH A 206     -12.362  39.225  25.736  1.00 29.10           O  
HETATM  924  O   HOH A 207     -16.604  39.368  68.155  1.00 48.60           O  
HETATM  925  O   HOH A 209      11.391  19.770  25.435  1.00 47.61           O  
HETATM  926  O   HOH A 210     -19.558  35.415  37.136  1.00 20.76           O  
HETATM  927  O   HOH A 211      -8.997  17.752  42.543  1.00 70.66           O  
HETATM  928  O   HOH A 212     -17.848  39.815  29.218  1.00 29.73           O  
HETATM  929  O   HOH A 213       0.354  24.858  23.327  1.00 39.34           O  
HETATM  930  O   HOH A 214     -20.053  22.709  42.510  1.00 41.65           O  
HETATM  931  O   HOH A 215      -0.550  35.214  42.541  1.00 28.15           O  
HETATM  932  O   HOH A 216       3.721  36.113  26.945  1.00 31.95           O  
HETATM  933  O   HOH A 217     -11.370  41.278  46.235  1.00 22.29           O  
HETATM  934  O   HOH A 218     -14.710  20.438  40.295  1.00 60.70           O  
HETATM  935  O   HOH A 219      -3.867  24.186  24.685  1.00 60.10           O  
HETATM  936  O   HOH A 220     -18.806  22.753  33.446  1.00 24.72           O  
HETATM  937  O   HOH A 221      -4.291  38.215  36.626  1.00 30.88           O  
HETATM  938  O   HOH A 222     -21.802  33.392  41.115  1.00 21.95           O  
HETATM  939  O   HOH A 223     -10.464  25.082  46.772  1.00 23.85           O  
HETATM  940  O   HOH A 224      -6.687  25.926  33.517  1.00  9.06           O  
HETATM  941  O   HOH A 226     -20.008  25.768  42.540  1.00 42.46           O  
HETATM  942  O   HOH A 227      -4.817  20.813  35.171  1.00 31.38           O  
HETATM  943  O   HOH A 228      -4.569  18.419  45.166  1.00 52.23           O  
HETATM  944  O   HOH A 229     -19.287  19.876  34.487  1.00 17.13           O  
HETATM  945  O   HOH A 230      -9.508  22.465  39.519  1.00 45.01           O  
HETATM  946  O   HOH A 231       0.065  35.419  58.587  1.00 41.28           O  
HETATM  947  O   HOH A 232      -8.045  28.603  55.402  1.00 72.69           O  
HETATM  948  O   HOH A 233       1.922  19.146  25.593  1.00 45.51           O  
HETATM  949  O   HOH A 234     -17.250  38.173  24.387  1.00 24.65           O  
HETATM  950  O   HOH A 235      -9.201  38.043  42.880  1.00 38.20           O  
HETATM  951  O   HOH A 236      -9.213  38.592  45.787  1.00 36.97           O  
HETATM  952  O   HOH A 237     -13.075  41.878  35.324  1.00 30.43           O  
HETATM  953  O   HOH A 238      -7.860  36.674  40.891  1.00 16.17           O  
HETATM  954  O   HOH A 239      -8.953  34.635  43.869  1.00 43.17           O  
HETATM  955  O   HOH A 240      -7.558  32.525  52.921  1.00 40.08           O  
HETATM  956  O   HOH A 241     -11.496  29.499  51.681  1.00 25.31           O  
HETATM  957  O   HOH A 242       5.209  22.297  41.811  1.00 19.13           O  
HETATM  958  O   HOH A 244      -8.278  27.167  35.413  1.00 12.83           O  
HETATM  959  O   HOH A 245      -8.077  32.807  45.674  1.00 34.04           O  
HETATM  960  O   HOH A 246       2.083  30.866  50.448  1.00 60.62           O  
HETATM  961  O   HOH A 247     -17.855  25.003  45.039  1.00 26.08           O  
HETATM  962  O   HOH A 248      -0.982  20.533  42.199  1.00 50.98           O  
HETATM  963  O   HOH A 249     -26.860  27.221  43.025  1.00 29.09           O  
HETATM  964  O   HOH A 250     -11.290  24.583  55.905  1.00 67.16           O  
HETATM  965  O   HOH A 251      10.262  34.797  25.020  1.00 57.85           O  
HETATM  966  O   HOH A 252       1.812  38.800  33.347  1.00 35.48           O  
HETATM  967  O   HOH A 253      -8.741  40.145  26.520  1.00 48.18           O  
HETATM  968  O   HOH A 254      -5.258  35.143  26.702  1.00 76.99           O  
CONECT   14  913                                                                
CONECT   44  913                                                                
CONECT  199  914                                                                
CONECT  222  913  914                                                           
CONECT  238  913                                                                
CONECT  312  915                                                                
CONECT  328  915                                                                
CONECT  356  914                                                                
CONECT  381  914                                                                
CONECT  474  915                                                                
CONECT  493  915                                                                
CONECT  709  916                                                                
CONECT  744  916                                                                
CONECT  849  916                                                                
CONECT  878  916                                                                
CONECT  913   14   44  222  238                                                 
CONECT  914  199  222  356  381                                                 
CONECT  915  312  328  474  493                                                 
CONECT  916  709  744  849  878                                                 
MASTER      297    0    4    7    4    0    4    6  967    1   19    9          
END