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Database: PDB
Entry: 4OIG
LinkDB: 4OIG
Original site: 4OIG 
HEADER    VIRAL PROTEIN                           19-JAN-14   4OIG              
TITLE     DENGUE VIRUS NON-STRUCTURAL PROTEIN NS1                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL PROTEIN 1, NS1;                             
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 947-1127;                                     
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 1;                                 
SOURCE   3 ORGANISM_COMMON: DENV-1;                                             
SOURCE   4 ORGANISM_TAXID: 11059;                                               
SOURCE   5 STRAIN: NAURU/WEST PAC/1974;                                         
SOURCE   6 GENE: NS1;                                                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET21(A)+                                 
KEYWDS    DENGUE VIRUS, NON-STRUCTURAL PROTEIN, NS1, FLAVIVIRUS VIRAL PROTEIN,  
KEYWDS   2 STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS    
KEYWDS   3 DISEASES, CSGID, VIRAL PROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.EDELING,D.H.FREMONT,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS  
AUTHOR   2 DISEASES (CSGID)                                                     
REVDAT   4   22-NOV-17 4OIG    1       REMARK                                   
REVDAT   3   23-APR-14 4OIG    1       JRNL                                     
REVDAT   2   02-APR-14 4OIG    1       JRNL                                     
REVDAT   1   05-MAR-14 4OIG    0                                                
JRNL        AUTH   M.A.EDELING,M.S.DIAMOND,D.H.FREMONT                          
JRNL        TITL   STRUCTURAL BASIS OF FLAVIVIRUS NS1 ASSEMBLY AND ANTIBODY     
JRNL        TITL 2 RECOGNITION.                                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  4285 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24594604                                                     
JRNL        DOI    10.1073/PNAS.1322036111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.2_869                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 23632                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1182                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.9080 -  5.3442    1.00     2889   152  0.2191 0.2667        
REMARK   3     2  5.3442 -  4.2554    1.00     2814   149  0.1656 0.1881        
REMARK   3     3  4.2554 -  3.7215    1.00     2840   149  0.1900 0.2475        
REMARK   3     4  3.7215 -  3.3831    1.00     2788   147  0.2139 0.2452        
REMARK   3     5  3.3831 -  3.1416    1.00     2825   149  0.2374 0.2775        
REMARK   3     6  3.1416 -  2.9570    1.00     2783   146  0.2586 0.3209        
REMARK   3     7  2.9570 -  2.8093    1.00     2827   149  0.2806 0.3639        
REMARK   3     8  2.8093 -  2.6900    0.96     2684   141  0.3548 0.4393        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 27.42                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.900            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.38140                                             
REMARK   3    B22 (A**2) : 1.90480                                              
REMARK   3    B33 (A**2) : 0.47660                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.38770                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5780                                  
REMARK   3   ANGLE     :  1.166           7820                                  
REMARK   3   CHIRALITY :  0.049            828                                  
REMARK   3   PLANARITY :  0.004            972                                  
REMARK   3   DIHEDRAL  : 10.637           2088                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OIG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084533.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NOIR-1                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23633                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12MG/ML IN 20% PEG 4K, 0.2 M MAGNESIUM   
REMARK 280  SULFATE, 10% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       54.58750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.98100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.58750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.98100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A   168                                                      
REMARK 465     ALA A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     MSE A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     TYR A   175                                                      
REMARK 465     THR A   176                                                      
REMARK 465     GLN A   177                                                      
REMARK 465     MSE B   168                                                      
REMARK 465     ALA B   169                                                      
REMARK 465     SER B   170                                                      
REMARK 465     MSE B   171                                                      
REMARK 465     ARG B   172                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     TYR B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     GLN B   177                                                      
REMARK 465     MSE D   168                                                      
REMARK 465     ALA D   169                                                      
REMARK 465     SER D   170                                                      
REMARK 465     MSE D   171                                                      
REMARK 465     ARG D   172                                                      
REMARK 465     ASP D   173                                                      
REMARK 465     SER D   174                                                      
REMARK 465     TYR D   175                                                      
REMARK 465     THR D   176                                                      
REMARK 465     GLN D   177                                                      
REMARK 465     MSE E   168                                                      
REMARK 465     ALA E   169                                                      
REMARK 465     SER E   170                                                      
REMARK 465     MSE E   171                                                      
REMARK 465     ARG E   172                                                      
REMARK 465     ASP E   173                                                      
REMARK 465     SER E   174                                                      
REMARK 465     TYR E   175                                                      
REMARK 465     THR E   176                                                      
REMARK 465     GLN E   177                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA E   265     OG   SER E   348              2.05            
REMARK 500   OG   SER E   216     O    HOH E   543              2.19            
REMARK 500   NE1  TRP E   210     O3   SO4 E   401              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER D   351     OE1  GLU E   343     3555     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 190     -123.74     55.59                                   
REMARK 500    ASP A 197     -154.36   -150.14                                   
REMARK 500    GLU A 208      -57.95     70.14                                   
REMARK 500    ASP B 190     -123.89     55.83                                   
REMARK 500    GLU B 208      -57.38     69.80                                   
REMARK 500    LEU B 345      141.46   -171.45                                   
REMARK 500    ASP D 190     -124.10     55.57                                   
REMARK 500    ASP D 197     -153.18   -150.50                                   
REMARK 500    GLU D 208      -57.94     69.71                                   
REMARK 500    ASP E 190     -123.95     56.14                                   
REMARK 500    ASP E 197     -151.68   -150.49                                   
REMARK 500    GLU E 208      -57.04     69.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OIE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OII   RELATED DB: PDB                                   
REMARK 900 RELATED ID: CSGID-IDP00269   RELATED DB: TARGETTRACK                 
DBREF  4OIG A  172   352  UNP    P17763   POLG_DEN1W     947   1127             
DBREF  4OIG B  172   352  UNP    P17763   POLG_DEN1W     947   1127             
DBREF  4OIG D  172   352  UNP    P17763   POLG_DEN1W     947   1127             
DBREF  4OIG E  172   352  UNP    P17763   POLG_DEN1W     947   1127             
SEQADV 4OIG MSE A  168  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG ALA A  169  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG SER A  170  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE A  171  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE B  168  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG ALA B  169  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG SER B  170  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE B  171  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE D  168  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG ALA D  169  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG SER D  170  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE D  171  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE E  168  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG ALA E  169  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG SER E  170  UNP  P17763              EXPRESSION TAG                 
SEQADV 4OIG MSE E  171  UNP  P17763              EXPRESSION TAG                 
SEQRES   1 A  185  MSE ALA SER MSE ARG ASP SER TYR THR GLN VAL CYS ASP          
SEQRES   2 A  185  HIS ARG LEU MSE SER ALA ALA ILE LYS ASP SER LYS ALA          
SEQRES   3 A  185  VAL HIS ALA ASP MSE GLY TYR TRP ILE GLU SER GLU LYS          
SEQRES   4 A  185  ASN GLU THR TRP LYS LEU ALA ARG ALA SER PHE ILE GLU          
SEQRES   5 A  185  VAL LYS THR CYS ILE TRP PRO LYS SER HIS THR LEU TRP          
SEQRES   6 A  185  SER ASN GLY VAL LEU GLU SER GLU MSE ILE ILE PRO LYS          
SEQRES   7 A  185  ILE TYR GLY GLY PRO ILE SER GLN HIS ASN TYR ARG PRO          
SEQRES   8 A  185  GLY TYR PHE THR GLN THR ALA GLY PRO TRP HIS LEU GLY          
SEQRES   9 A  185  LYS LEU GLU LEU ASP PHE ASP LEU CYS GLU GLY THR THR          
SEQRES  10 A  185  VAL VAL VAL ASP GLU HIS CYS GLY ASN ARG GLY PRO SER          
SEQRES  11 A  185  LEU ARG THR THR THR VAL THR GLY LYS THR ILE HIS GLU          
SEQRES  12 A  185  TRP CYS CYS ARG SER CYS THR LEU PRO PRO LEU ARG PHE          
SEQRES  13 A  185  LYS GLY GLU ASP GLY CYS TRP TYR GLY MSE GLU ILE ARG          
SEQRES  14 A  185  PRO VAL LYS GLU LYS GLU GLU ASN LEU VAL LYS SER MSE          
SEQRES  15 A  185  VAL SER ALA                                                  
SEQRES   1 B  185  MSE ALA SER MSE ARG ASP SER TYR THR GLN VAL CYS ASP          
SEQRES   2 B  185  HIS ARG LEU MSE SER ALA ALA ILE LYS ASP SER LYS ALA          
SEQRES   3 B  185  VAL HIS ALA ASP MSE GLY TYR TRP ILE GLU SER GLU LYS          
SEQRES   4 B  185  ASN GLU THR TRP LYS LEU ALA ARG ALA SER PHE ILE GLU          
SEQRES   5 B  185  VAL LYS THR CYS ILE TRP PRO LYS SER HIS THR LEU TRP          
SEQRES   6 B  185  SER ASN GLY VAL LEU GLU SER GLU MSE ILE ILE PRO LYS          
SEQRES   7 B  185  ILE TYR GLY GLY PRO ILE SER GLN HIS ASN TYR ARG PRO          
SEQRES   8 B  185  GLY TYR PHE THR GLN THR ALA GLY PRO TRP HIS LEU GLY          
SEQRES   9 B  185  LYS LEU GLU LEU ASP PHE ASP LEU CYS GLU GLY THR THR          
SEQRES  10 B  185  VAL VAL VAL ASP GLU HIS CYS GLY ASN ARG GLY PRO SER          
SEQRES  11 B  185  LEU ARG THR THR THR VAL THR GLY LYS THR ILE HIS GLU          
SEQRES  12 B  185  TRP CYS CYS ARG SER CYS THR LEU PRO PRO LEU ARG PHE          
SEQRES  13 B  185  LYS GLY GLU ASP GLY CYS TRP TYR GLY MSE GLU ILE ARG          
SEQRES  14 B  185  PRO VAL LYS GLU LYS GLU GLU ASN LEU VAL LYS SER MSE          
SEQRES  15 B  185  VAL SER ALA                                                  
SEQRES   1 D  185  MSE ALA SER MSE ARG ASP SER TYR THR GLN VAL CYS ASP          
SEQRES   2 D  185  HIS ARG LEU MSE SER ALA ALA ILE LYS ASP SER LYS ALA          
SEQRES   3 D  185  VAL HIS ALA ASP MSE GLY TYR TRP ILE GLU SER GLU LYS          
SEQRES   4 D  185  ASN GLU THR TRP LYS LEU ALA ARG ALA SER PHE ILE GLU          
SEQRES   5 D  185  VAL LYS THR CYS ILE TRP PRO LYS SER HIS THR LEU TRP          
SEQRES   6 D  185  SER ASN GLY VAL LEU GLU SER GLU MSE ILE ILE PRO LYS          
SEQRES   7 D  185  ILE TYR GLY GLY PRO ILE SER GLN HIS ASN TYR ARG PRO          
SEQRES   8 D  185  GLY TYR PHE THR GLN THR ALA GLY PRO TRP HIS LEU GLY          
SEQRES   9 D  185  LYS LEU GLU LEU ASP PHE ASP LEU CYS GLU GLY THR THR          
SEQRES  10 D  185  VAL VAL VAL ASP GLU HIS CYS GLY ASN ARG GLY PRO SER          
SEQRES  11 D  185  LEU ARG THR THR THR VAL THR GLY LYS THR ILE HIS GLU          
SEQRES  12 D  185  TRP CYS CYS ARG SER CYS THR LEU PRO PRO LEU ARG PHE          
SEQRES  13 D  185  LYS GLY GLU ASP GLY CYS TRP TYR GLY MSE GLU ILE ARG          
SEQRES  14 D  185  PRO VAL LYS GLU LYS GLU GLU ASN LEU VAL LYS SER MSE          
SEQRES  15 D  185  VAL SER ALA                                                  
SEQRES   1 E  185  MSE ALA SER MSE ARG ASP SER TYR THR GLN VAL CYS ASP          
SEQRES   2 E  185  HIS ARG LEU MSE SER ALA ALA ILE LYS ASP SER LYS ALA          
SEQRES   3 E  185  VAL HIS ALA ASP MSE GLY TYR TRP ILE GLU SER GLU LYS          
SEQRES   4 E  185  ASN GLU THR TRP LYS LEU ALA ARG ALA SER PHE ILE GLU          
SEQRES   5 E  185  VAL LYS THR CYS ILE TRP PRO LYS SER HIS THR LEU TRP          
SEQRES   6 E  185  SER ASN GLY VAL LEU GLU SER GLU MSE ILE ILE PRO LYS          
SEQRES   7 E  185  ILE TYR GLY GLY PRO ILE SER GLN HIS ASN TYR ARG PRO          
SEQRES   8 E  185  GLY TYR PHE THR GLN THR ALA GLY PRO TRP HIS LEU GLY          
SEQRES   9 E  185  LYS LEU GLU LEU ASP PHE ASP LEU CYS GLU GLY THR THR          
SEQRES  10 E  185  VAL VAL VAL ASP GLU HIS CYS GLY ASN ARG GLY PRO SER          
SEQRES  11 E  185  LEU ARG THR THR THR VAL THR GLY LYS THR ILE HIS GLU          
SEQRES  12 E  185  TRP CYS CYS ARG SER CYS THR LEU PRO PRO LEU ARG PHE          
SEQRES  13 E  185  LYS GLY GLU ASP GLY CYS TRP TYR GLY MSE GLU ILE ARG          
SEQRES  14 E  185  PRO VAL LYS GLU LYS GLU GLU ASN LEU VAL LYS SER MSE          
SEQRES  15 E  185  VAL SER ALA                                                  
MODRES 4OIG MSE A  184  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE A  198  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE A  241  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE A  333  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE A  349  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE B  184  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE B  198  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE B  241  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE B  333  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE B  349  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE D  184  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE D  198  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE D  241  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE D  333  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE D  349  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE E  184  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE E  198  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE E  241  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE E  333  MET  SELENOMETHIONINE                                   
MODRES 4OIG MSE E  349  MET  SELENOMETHIONINE                                   
HET    MSE  A 184       8                                                       
HET    MSE  A 198       8                                                       
HET    MSE  A 241       8                                                       
HET    MSE  A 333       8                                                       
HET    MSE  A 349       8                                                       
HET    MSE  B 184       8                                                       
HET    MSE  B 198       8                                                       
HET    MSE  B 241       8                                                       
HET    MSE  B 333       8                                                       
HET    MSE  B 349       8                                                       
HET    MSE  D 184       8                                                       
HET    MSE  D 198       8                                                       
HET    MSE  D 241       8                                                       
HET    MSE  D 333       8                                                       
HET    MSE  D 349       8                                                       
HET    MSE  E 184       8                                                       
HET    MSE  E 198       8                                                       
HET    MSE  E 241       8                                                       
HET    MSE  E 333       8                                                       
HET    MSE  E 349       8                                                       
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    SO4  D 401       5                                                       
HET    SO4  D 402       5                                                       
HET    SO4  D 403       5                                                       
HET    SO4  D 404       5                                                       
HET    SO4  E 401       5                                                       
HET    SO4  E 402       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   5  SO4    14(O4 S 2-)                                                  
FORMUL  19  HOH   *145(H2 O)                                                    
HELIX    1   1 PRO A  226  THR A  230  5                                   5    
HELIX    2   2 LEU A  237  MSE A  241  5                                   5    
HELIX    3   3 PRO A  244  GLY A  248  5                                   5    
HELIX    4   4 SER A  252  TYR A  256  5                                   5    
HELIX    5   5 PRO A  267  GLY A  271  5                                   5    
HELIX    6   6 ASP B  180  MSE B  184  5                                   5    
HELIX    7   7 PRO B  226  THR B  230  5                                   5    
HELIX    8   8 LEU B  237  MSE B  241  5                                   5    
HELIX    9   9 PRO B  244  GLY B  248  5                                   5    
HELIX   10  10 SER B  252  TYR B  256  5                                   5    
HELIX   11  11 PRO B  267  GLY B  271  5                                   5    
HELIX   12  12 ASP D  180  MSE D  184  5                                   5    
HELIX   13  13 PRO D  226  THR D  230  5                                   5    
HELIX   14  14 LEU D  237  MSE D  241  5                                   5    
HELIX   15  15 PRO D  244  GLY D  248  5                                   5    
HELIX   16  16 SER D  252  TYR D  256  5                                   5    
HELIX   17  17 PRO D  267  GLY D  271  5                                   5    
HELIX   18  18 ASP E  180  MSE E  184  5                                   5    
HELIX   19  19 PRO E  226  THR E  230  5                                   5    
HELIX   20  20 LEU E  237  MSE E  241  5                                   5    
HELIX   21  21 PRO E  244  GLY E  248  5                                   5    
HELIX   22  22 SER E  252  TYR E  256  5                                   5    
HELIX   23  23 PRO E  267  GLY E  271  5                                   5    
SHEET    1   A15 LEU A 298  ARG A 299  0                                        
SHEET    2   A15 CYS A 329  TYR A 331 -1  O  TYR A 331   N  LEU A 298           
SHEET    3   A15 LEU A 321  LYS A 324 -1  N  PHE A 323   O  TRP A 330           
SHEET    4   A15 LEU A 273  PHE A 277 -1  N  ASP A 276   O  ARG A 322           
SHEET    5   A15 TRP A 210  PHE A 217 -1  N  PHE A 217   O  LEU A 273           
SHEET    6   A15 TYR A 200  LYS A 206 -1  N  GLU A 203   O  ARG A 214           
SHEET    7   A15 LYS A 192  ALA A 196 -1  N  ALA A 193   O  SER A 204           
SHEET    8   A15 SER A 185  LYS A 189 -1  N  SER A 185   O  ALA A 196           
SHEET    9   A15 SER B 185  LYS B 189 -1  O  ALA B 186   N  ILE A 188           
SHEET   10   A15 LYS B 192  ALA B 196 -1  O  ALA B 196   N  SER B 185           
SHEET   11   A15 TYR B 200  LYS B 206 -1  O  SER B 204   N  ALA B 193           
SHEET   12   A15 TRP B 210  PHE B 217 -1  O  ALA B 213   N  GLU B 203           
SHEET   13   A15 LEU B 273  PHE B 277 -1  O  LEU B 273   N  PHE B 217           
SHEET   14   A15 LEU B 321  LYS B 324 -1  O  ARG B 322   N  ASP B 276           
SHEET   15   A15 CYS B 329  TYR B 331 -1  O  TRP B 330   N  PHE B 323           
SHEET    1   B 3 THR A 284  VAL A 287  0                                        
SHEET    2   B 3 GLU A 310  CYS A 313  1  O  TRP A 311   N  THR A 284           
SHEET    3   B 3 ARG A 336  PRO A 337 -1  O  ARG A 336   N  CYS A 312           
SHEET    1   C 3 THR B 284  VAL B 287  0                                        
SHEET    2   C 3 GLU B 310  CYS B 313  1  O  TRP B 311   N  THR B 284           
SHEET    3   C 3 ILE B 335  PRO B 337 -1  O  ARG B 336   N  CYS B 312           
SHEET    1   D16 LEU D 298  ARG D 299  0                                        
SHEET    2   D16 CYS D 329  TYR D 331 -1  O  TYR D 331   N  LEU D 298           
SHEET    3   D16 LEU D 321  LYS D 324 -1  N  PHE D 323   O  TRP D 330           
SHEET    4   D16 LEU D 273  PHE D 277 -1  N  ASP D 276   O  ARG D 322           
SHEET    5   D16 TRP D 210  PHE D 217 -1  N  PHE D 217   O  LEU D 273           
SHEET    6   D16 TYR D 200  LYS D 206 -1  N  GLU D 203   O  ALA D 213           
SHEET    7   D16 LYS D 192  ALA D 196 -1  N  ALA D 193   O  SER D 204           
SHEET    8   D16 SER D 185  LYS D 189 -1  N  SER D 185   O  ALA D 196           
SHEET    9   D16 SER E 185  LYS E 189 -1  O  ILE E 188   N  ALA D 186           
SHEET   10   D16 LYS E 192  ALA E 196 -1  O  ALA E 196   N  SER E 185           
SHEET   11   D16 TYR E 200  LYS E 206 -1  O  SER E 204   N  ALA E 193           
SHEET   12   D16 TRP E 210  PHE E 217 -1  O  SER E 216   N  TRP E 201           
SHEET   13   D16 LEU E 273  PHE E 277 -1  O  LEU E 275   N  ALA E 215           
SHEET   14   D16 LEU E 321  LYS E 324 -1  O  ARG E 322   N  ASP E 276           
SHEET   15   D16 CYS E 329  TYR E 331 -1  O  TRP E 330   N  PHE E 323           
SHEET   16   D16 LEU E 298  ARG E 299 -1  N  LEU E 298   O  TYR E 331           
SHEET    1   E 3 THR D 284  VAL D 287  0                                        
SHEET    2   E 3 GLU D 310  CYS D 313  1  O  TRP D 311   N  THR D 284           
SHEET    3   E 3 ILE D 335  PRO D 337 -1  O  ARG D 336   N  CYS D 312           
SHEET    1   F 3 THR E 284  VAL E 287  0                                        
SHEET    2   F 3 GLU E 310  CYS E 313  1  O  TRP E 311   N  THR E 284           
SHEET    3   F 3 ILE E 335  PRO E 337 -1  O  ARG E 336   N  CYS E 312           
SSBOND   1 CYS A  179    CYS A  223                          1555   1555  2.04  
SSBOND   2 CYS A  280    CYS A  329                          1555   1555  2.04  
SSBOND   3 CYS A  291    CYS A  312                          1555   1555  2.03  
SSBOND   4 CYS A  313    CYS A  316                          1555   1555  2.03  
SSBOND   5 CYS B  179    CYS B  223                          1555   1555  2.03  
SSBOND   6 CYS B  280    CYS B  329                          1555   1555  2.03  
SSBOND   7 CYS B  291    CYS B  312                          1555   1555  2.05  
SSBOND   8 CYS B  313    CYS B  316                          1555   1555  2.03  
SSBOND   9 CYS D  179    CYS D  223                          1555   1555  2.03  
SSBOND  10 CYS D  280    CYS D  329                          1555   1555  2.03  
SSBOND  11 CYS D  291    CYS D  312                          1555   1555  2.04  
SSBOND  12 CYS D  313    CYS D  316                          1555   1555  2.04  
SSBOND  13 CYS E  179    CYS E  223                          1555   1555  2.03  
SSBOND  14 CYS E  280    CYS E  329                          1555   1555  2.02  
SSBOND  15 CYS E  291    CYS E  312                          1555   1555  2.03  
SSBOND  16 CYS E  313    CYS E  316                          1555   1555  2.03  
LINK         C   LEU A 183                 N   MSE A 184     1555   1555  1.33  
LINK         C   MSE A 184                 N   SER A 185     1555   1555  1.33  
LINK         C   ASP A 197                 N   MSE A 198     1555   1555  1.33  
LINK         C   MSE A 198                 N   GLY A 199     1555   1555  1.33  
LINK         C   GLU A 240                 N   MSE A 241     1555   1555  1.33  
LINK         C   MSE A 241                 N   ILE A 242     1555   1555  1.33  
LINK         C   GLY A 332                 N   MSE A 333     1555   1555  1.33  
LINK         C   MSE A 333                 N   GLU A 334     1555   1555  1.33  
LINK         C   SER A 348                 N   MSE A 349     1555   1555  1.33  
LINK         C   MSE A 349                 N   VAL A 350     1555   1555  1.33  
LINK         C   LEU B 183                 N   MSE B 184     1555   1555  1.33  
LINK         C   MSE B 184                 N   SER B 185     1555   1555  1.33  
LINK         C   ASP B 197                 N   MSE B 198     1555   1555  1.33  
LINK         C   MSE B 198                 N   GLY B 199     1555   1555  1.33  
LINK         C   GLU B 240                 N   MSE B 241     1555   1555  1.33  
LINK         C   MSE B 241                 N   ILE B 242     1555   1555  1.33  
LINK         C   GLY B 332                 N   MSE B 333     1555   1555  1.33  
LINK         C   MSE B 333                 N   GLU B 334     1555   1555  1.33  
LINK         C   SER B 348                 N   MSE B 349     1555   1555  1.32  
LINK         C   MSE B 349                 N   VAL B 350     1555   1555  1.32  
LINK         C   LEU D 183                 N   MSE D 184     1555   1555  1.33  
LINK         C   MSE D 184                 N   SER D 185     1555   1555  1.33  
LINK         C   ASP D 197                 N   MSE D 198     1555   1555  1.33  
LINK         C   MSE D 198                 N   GLY D 199     1555   1555  1.33  
LINK         C   GLU D 240                 N   MSE D 241     1555   1555  1.33  
LINK         C   MSE D 241                 N   ILE D 242     1555   1555  1.33  
LINK         C   GLY D 332                 N   MSE D 333     1555   1555  1.32  
LINK         C   MSE D 333                 N   GLU D 334     1555   1555  1.33  
LINK         C   SER D 348                 N   MSE D 349     1555   1555  1.33  
LINK         C   MSE D 349                 N   VAL D 350     1555   1555  1.33  
LINK         C   LEU E 183                 N   MSE E 184     1555   1555  1.33  
LINK         C   MSE E 184                 N   SER E 185     1555   1555  1.33  
LINK         C   ASP E 197                 N   MSE E 198     1555   1555  1.33  
LINK         C   MSE E 198                 N   GLY E 199     1555   1555  1.33  
LINK         C   GLU E 240                 N   MSE E 241     1555   1555  1.33  
LINK         C   MSE E 241                 N   ILE E 242     1555   1555  1.33  
LINK         C   GLY E 332                 N   MSE E 333     1555   1555  1.33  
LINK         C   MSE E 333                 N   GLU E 334     1555   1555  1.33  
LINK         C   SER E 348                 N   MSE E 349     1555   1555  1.33  
LINK         C   MSE E 349                 N   VAL E 350     1555   1555  1.33  
CISPEP   1 LEU A  318    PRO A  319          0        -1.19                     
CISPEP   2 LEU B  318    PRO B  319          0        -0.06                     
CISPEP   3 LEU D  318    PRO D  319          0         0.21                     
CISPEP   4 LEU E  318    PRO E  319          0        -0.85                     
SITE     1 AC1  4 TRP A 232  ASN A 234  LYS B 227  ASN E 293                    
SITE     1 AC2  6 ASN A 234  GLY A 235  HOH A 522  HOH A 524                    
SITE     2 AC2  6 ASN B 234  GLY B 235                                          
SITE     1 AC3  7 LYS A 206  TRP A 210  HOH A 528  HIS B 181                    
SITE     2 AC3  7 PRO B 226  SER B 228  HIS B 229                               
SITE     1 AC4  5 HIS A 181  SER A 228  HIS A 229  LYS B 206                    
SITE     2 AC4  5 TRP B 210                                                     
SITE     1 AC5  5 ASN A 293  HOH A 530  LYS D 227  TRP E 232                    
SITE     2 AC5  5 ASN E 234                                                     
SITE     1 AC6  6 ILE A 308  HIS A 309  GLU A 310  LYS A 339                    
SITE     2 AC6  6 GLU A 340  HOH A 513                                          
SITE     1 AC7  7 ILE B 308  HIS B 309  GLU B 310  LYS B 339                    
SITE     2 AC7  7 HOH B 528  HOH B 532  HIS D 290                               
SITE     1 AC8  3 LYS A 227  TRP B 232  ASN B 234                               
SITE     1 AC9  6 ASN D 234  GLY D 235  HOH D 518  ASN E 234                    
SITE     2 AC9  6 GLY E 235  HOH E 508                                          
SITE     1 BC1  3 TRP D 232  ASN D 234  LYS E 227                               
SITE     1 BC2  7 HIS B 290  ILE D 308  HIS D 309  GLU D 310                    
SITE     2 BC2  7 LYS D 339  GLU D 340  HOH D 515                               
SITE     1 BC3  6 LYS D 206  TRP D 210  HOH D 517  HIS E 181                    
SITE     2 BC3  6 SER E 228  HIS E 229                                          
SITE     1 BC4  5 HIS D 181  SER D 228  HIS D 229  LYS E 206                    
SITE     2 BC4  5 TRP E 210                                                     
SITE     1 BC5  6 LYS E 306  ILE E 308  HIS E 309  GLU E 310                    
SITE     2 BC5  6 LYS E 339  HOH E 506                                          
CRYST1  109.175   81.962   97.189  90.00  97.78  90.00 C 1 2 1      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009160  0.000000  0.001252        0.00000                         
SCALE2      0.000000  0.012201  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010385        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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