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Database: PDB
Entry: 4GSX
LinkDB: 4GSX
Original site: 4GSX 
HEADER    VIRAL PROTEIN                           28-AUG-12   4GSX              
TITLE     HIGH RESOLUTION STRUCTURE OF DENGUE VIRUS SEROTYPE 1 SE CONTAINING    
TITLE    2 STEM                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENVELOPE PROTEIN E;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 281-691;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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: WP74;                                                        
SOURCE   6 GENE: ENVELOPE PROTEIN;                                              
SOURCE   7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   8 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    VIRAL FUSION PROTEIN, VIRAL PROTEIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.KLEIN,J.L.CHOI,S.C.HARRISON                                       
REVDAT   4   15-NOV-17 4GSX    1       REMARK                                   
REVDAT   3   06-FEB-13 4GSX    1       JRNL                                     
REVDAT   2   30-JAN-13 4GSX    1       LINK   MODRES REMARK                     
REVDAT   1   19-DEC-12 4GSX    0                                                
JRNL        AUTH   D.E.KLEIN,J.L.CHOI,S.C.HARRISON                              
JRNL        TITL   STRUCTURE OF A DENGUE VIRUS ENVELOPE PROTEIN LATE-STAGE      
JRNL        TITL 2 FUSION INTERMEDIATE.                                         
JRNL        REF    J.VIROL.                      V.  87  2287 2013              
JRNL        REFN                   ISSN 0022-538X                               
JRNL        PMID   23236058                                                     
JRNL        DOI    10.1128/JVI.02957-12                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 76852                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3879                            
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 26.1827 -  5.1529    0.91     3559   216  0.1748 0.1986        
REMARK   3     2  5.1529 -  4.0951    0.94     3645   184  0.1213 0.1660        
REMARK   3     3  4.0951 -  3.5789    0.94     3672   210  0.1313 0.1556        
REMARK   3     4  3.5789 -  3.2523    0.95     3658   191  0.1453 0.1688        
REMARK   3     5  3.2523 -  3.0196    0.95     3711   191  0.1532 0.1875        
REMARK   3     6  3.0196 -  2.8418    0.95     3687   187  0.1660 0.1908        
REMARK   3     7  2.8418 -  2.6996    0.95     3685   208  0.1702 0.2073        
REMARK   3     8  2.6996 -  2.5822    0.95     3654   181  0.1823 0.1884        
REMARK   3     9  2.5822 -  2.4829    0.94     3667   209  0.1763 0.2060        
REMARK   3    10  2.4829 -  2.3973    0.95     3687   202  0.1827 0.2119        
REMARK   3    11  2.3973 -  2.3224    0.95     3691   187  0.1867 0.1817        
REMARK   3    12  2.3224 -  2.2560    0.95     3677   190  0.1850 0.1872        
REMARK   3    13  2.2560 -  2.1966    0.94     3670   209  0.1820 0.2103        
REMARK   3    14  2.1966 -  2.1431    0.95     3648   187  0.1889 0.2077        
REMARK   3    15  2.1431 -  2.0944    0.94     3611   198  0.1881 0.2026        
REMARK   3    16  2.0944 -  2.0498    0.94     3664   190  0.1986 0.2242        
REMARK   3    17  2.0498 -  2.0088    0.94     3640   174  0.1964 0.2150        
REMARK   3    18  2.0088 -  1.9709    0.94     3634   190  0.2122 0.2328        
REMARK   3    19  1.9709 -  1.9358    0.94     3594   180  0.2232 0.2026        
REMARK   3    20  1.9358 -  1.9030    0.91     3534   173  0.2462 0.2674        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.4000                                                   
REMARK   3   OPERATOR: H,-H-K,-L                                                
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           6133                                  
REMARK   3   ANGLE     :  1.295           8291                                  
REMARK   3   CHIRALITY :  0.067            992                                  
REMARK   3   PLANARITY :  0.005           1039                                  
REMARK   3   DIHEDRAL  : 17.085           2245                                  
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 4GSX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074592.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .979                               
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY-COOLED SINGLE        
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76924                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MR PHASER                                             
REMARK 200 STARTING MODEL: PDB ENTRY 3G7T                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      146.25900            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      146.25900            
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      146.25900            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12800 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 49060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       38.78550            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -67.17846            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       77.57100            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   BIOMT1   2 -0.500000 -0.866025  0.000000      -38.78550            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -67.17846            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       38.78550            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      -67.17846            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 691  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 933  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 813  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     SER A    -4                                                      
REMARK 465     THR A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A   147                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     HIS A   149                                                      
REMARK 465     GLN A   150                                                      
REMARK 465     VAL A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     ASN A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     THR A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     GLU A   157                                                      
REMARK 465     HIS A   158                                                      
REMARK 465     ALA A   404                                                      
REMARK 465     THR A   405                                                      
REMARK 465     ALA A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     ALA A   409                                                      
REMARK 465     ARG A   410                                                      
REMARK 465     ARG A   411                                                      
REMARK 465     GLY B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     SER B    -4                                                      
REMARK 465     THR B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B   101                                                      
REMARK 465     GLY B   146                                                      
REMARK 465     ASP B   147                                                      
REMARK 465     GLN B   148                                                      
REMARK 465     HIS B   149                                                      
REMARK 465     GLN B   150                                                      
REMARK 465     VAL B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     ASN B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     THR B   155                                                      
REMARK 465     THR B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     THR B   405                                                      
REMARK 465     ALA B   406                                                      
REMARK 465     ARG B   407                                                      
REMARK 465     GLY B   408                                                      
REMARK 465     ALA B   409                                                      
REMARK 465     ARG B   410                                                      
REMARK 465     ARG B   411                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B  84    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 244    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     LYS B 247    CG   CD   CE   NZ                                   
REMARK 470     LYS B 343    CG   CD   CE   NZ                                   
REMARK 470     GLU B 362    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 385    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   774     O    HOH B   848              1.81            
REMARK 500   O    HOH B   849     O    HOH B   857              1.81            
REMARK 500   NZ   LYS A   284     O    HOH A   831              1.85            
REMARK 500   O    HOH A   858     O    HOH A   903              1.85            
REMARK 500   OE2  GLU B    49     O    HOH B   798              1.86            
REMARK 500   OE2  GLU A   309     O    HOH A   948              1.87            
REMARK 500   O    GLY B   104     O    HOH B   901              1.87            
REMARK 500   O    HOH B   700     O    HOH B   835              1.88            
REMARK 500   OD1  ASP A    71     O    HOH A   793              1.90            
REMARK 500   O    HOH B   872     O    HOH B   891              1.90            
REMARK 500   O    HOH B   632     O    HOH B   854              1.95            
REMARK 500   O    HOH B   870     O    HOH B   887              1.96            
REMARK 500   O    HOH B   821     O    HOH B   845              1.97            
REMARK 500   OG   SER B    29     O    HOH B   823              1.97            
REMARK 500   O    HOH B   744     O    HOH B   871              1.98            
REMARK 500   O    HIS B   158     O    HOH B   786              1.98            
REMARK 500   O    GLY B   328     NZ   LYS B   361              1.98            
REMARK 500   O    HOH A   922     O    HOH A   949              1.99            
REMARK 500   O    HOH B   787     O    HOH B   861              2.00            
REMARK 500   O    SER B   227     O    HOH B   834              2.03            
REMARK 500   O    LEU B   236     O    HOH B   797              2.03            
REMARK 500   O    HOH A   799     O    HOH A   901              2.04            
REMARK 500   O    HOH A   934     O    HOH A   943              2.04            
REMARK 500   O    GLY B   254     NE2  GLN B   256              2.04            
REMARK 500   OE2  GLU A    79     O    HOH A   908              2.05            
REMARK 500   O    HOH B   794     O    HOH B   895              2.05            
REMARK 500   O    HOH B   874     O    HOH B   885              2.05            
REMARK 500   OG1  THR A    69     O    HOH A   935              2.05            
REMARK 500   O    THR A   329     O    HOH A   912              2.06            
REMARK 500   O    HOH B   642     O    HOH B   744              2.08            
REMARK 500   OE1  GLU A   314     O    HOH A   945              2.09            
REMARK 500   O    HOH A   855     O    HOH A   881              2.10            
REMARK 500   O    HOH A   658     O    HOH A   953              2.10            
REMARK 500   O    LYS B   246     O    HOH B   814              2.10            
REMARK 500   OG1  THR A   142     O    HOH A   864              2.11            
REMARK 500   OE2  GLU B   229     O    HOH B   803              2.11            
REMARK 500   O    HOH B   790     O    HOH B   816              2.11            
REMARK 500   O    HOH B   884     O    HOH B   889              2.12            
REMARK 500   O    HOH B   858     O    HOH B   863              2.12            
REMARK 500   O    HOH A   886     O    HOH A   897              2.13            
REMARK 500   O    HOH A   816     O    HOH A   936              2.14            
REMARK 500   OD1  ASP B    87     O    HOH B   880              2.16            
REMARK 500   NZ   LYS A    36     OG1  THR A   293              2.16            
REMARK 500   OE1  GLU A   269     O    HOH A   844              2.17            
REMARK 500   O    HOH A   866     O    HOH A   882              2.17            
REMARK 500   OE1  GLN A   347     O    HOH A   938              2.17            
REMARK 500   O    HOH A   885     O    HOH A   952              2.18            
REMARK 500   OE1  GLU A   314     O    HOH A   951              2.19            
REMARK 500   O    HOH A   756     O    HOH A   862              2.19            
REMARK 500   OE1  GLU A    79     O    HOH A   934              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   O    HOH A   919     O    HOH A   928     3655     1.83            
REMARK 500   O    HOH A   942     O    HOH B   901     3545     1.83            
REMARK 500   O    HOH B   662     O    HOH B   662     2445     1.84            
REMARK 500   O    HOH B   678     O    HOH B   678     2445     2.01            
REMARK 500   O    HOH A   811     O    HOH B   754     3545     2.03            
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    LYS A  36       99.46    -53.03                                   
REMARK 500    ASP A 177      -36.79     73.77                                   
REMARK 500    GLU A 202     -113.56     56.59                                   
REMARK 500    LYS A 343       61.67   -111.72                                   
REMARK 500    ASN A 355       72.28   -111.59                                   
REMARK 500    HIS B  27      128.60    -36.97                                   
REMARK 500    THR B  76      -12.42    104.62                                   
REMARK 500    GLN B  77       30.02    -99.28                                   
REMARK 500    THR B  95     -177.01    179.98                                   
REMARK 500    ASN B 103       53.75     23.35                                   
REMARK 500    ALA B 168       77.88   -118.24                                   
REMARK 500    ASP B 177      -27.08     72.87                                   
REMARK 500    GLU B 202     -113.61     53.47                                   
REMARK 500    SER B 227      -79.67    -57.74                                   
REMARK 500    LYS B 291       99.53    -48.84                                   
REMARK 500    ASN B 355       73.02   -103.92                                   
REMARK 500    ASP B 360      118.03   -160.67                                   
REMARK 500    GLU B 362      -16.87     70.49                                   
REMARK 500    GLU B 384       -7.29    -56.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B   18     THR B   19                  149.87                    
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                              CD B 503  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 789   O                                                      
REMARK 620 2 HIS B 282   NE2 108.5                                              
REMARK 620 3 HIS B  27   NE2 107.5  96.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 502  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 311   OE1                                                    
REMARK 620 2 GLU B 311   OE2  53.9                                              
REMARK 620 3 ASP A  98   OD2 149.3  96.6                                        
REMARK 620 4 HOH A 710   O   100.7 153.2 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 503  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  10   OD1                                                    
REMARK 620 2 ASP A  10   OD2  50.8                                              
REMARK 620 3 HOH A 623   O   106.8 157.6                                        
REMARK 620 4 HOH A 932   O    88.7  93.6  85.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 502  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  10   OD1                                                    
REMARK 620 2 ASP B  10   OD2  49.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 503                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G7T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1OK8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1URZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GT0   RELATED DB: PDB                                   
DBREF  4GSX A    1   411  UNP    P17763   POLG_DEN1W     281    691             
DBREF  4GSX B    1   411  UNP    P17763   POLG_DEN1W     281    691             
SEQADV 4GSX GLY A  -15  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A  -14  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A  -13  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A  -12  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A  -11  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A  -10  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A   -9  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A   -8  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A   -7  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX GLY A   -6  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX SER A   -5  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX SER A   -4  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX THR A   -3  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX SER A   -2  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX ASN A   -1  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX GLY A    0  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS A  101  UNP  P17763    TRP   381 ENGINEERED MUTATION            
SEQADV 4GSX ILE A  161  UNP  P17763    THR   441 CONFLICT                       
SEQADV 4GSX GLY B  -15  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B  -14  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B  -13  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B  -12  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B  -11  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B  -10  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B   -9  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B   -8  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B   -7  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX GLY B   -6  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX SER B   -5  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX SER B   -4  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX THR B   -3  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX SER B   -2  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX ASN B   -1  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX GLY B    0  UNP  P17763              EXPRESSION TAG                 
SEQADV 4GSX HIS B  101  UNP  P17763    TRP   381 ENGINEERED MUTATION            
SEQADV 4GSX ILE B  161  UNP  P17763    THR   441 CONFLICT                       
SEQRES   1 A  427  GLY HIS HIS HIS HIS HIS HIS HIS HIS GLY SER SER THR          
SEQRES   2 A  427  SER ASN GLY MET ARG CYS VAL GLY ILE GLY ASN ARG ASP          
SEQRES   3 A  427  PHE VAL GLU GLY LEU SER GLY ALA THR TRP VAL ASP VAL          
SEQRES   4 A  427  VAL LEU GLU HIS GLY SER CYS VAL THR THR MET ALA LYS          
SEQRES   5 A  427  ASP LYS PRO THR LEU ASP ILE GLU LEU LEU LYS THR GLU          
SEQRES   6 A  427  VAL THR ASN PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU          
SEQRES   7 A  427  ALA LYS ILE SER ASN THR THR THR ASP SER ARG CYS PRO          
SEQRES   8 A  427  THR GLN GLY GLU ALA THR LEU VAL GLU GLU GLN ASP THR          
SEQRES   9 A  427  ASN PHE VAL CYS ARG ARG THR PHE VAL ASP ARG GLY HIS          
SEQRES  10 A  427  GLY ASN GLY CYS GLY LEU PHE GLY LYS GLY SER LEU ILE          
SEQRES  11 A  427  THR CYS ALA LYS PHE LYS CYS VAL THR LYS LEU GLU GLY          
SEQRES  12 A  427  LYS ILE VAL GLN TYR GLU ASN LEU LYS TYR SER VAL ILE          
SEQRES  13 A  427  VAL THR VAL HIS THR GLY ASP GLN HIS GLN VAL GLY ASN          
SEQRES  14 A  427  GLU THR THR GLU HIS GLY THR ILE ALA THR ILE THR PRO          
SEQRES  15 A  427  GLN ALA PRO THR SER GLU ILE GLN LEU THR ASP TYR GLY          
SEQRES  16 A  427  ALA LEU THR LEU ASP CYS SER PRO ARG THR GLY LEU ASP          
SEQRES  17 A  427  PHE ASN GLU MET VAL LEU LEU THR MET GLU LYS LYS SER          
SEQRES  18 A  427  TRP LEU VAL HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU          
SEQRES  19 A  427  PRO TRP THR SER GLY ALA SER THR SER GLN GLU THR TRP          
SEQRES  20 A  427  ASN ARG GLN ASP LEU LEU VAL THR PHE LYS THR ALA HIS          
SEQRES  21 A  427  ALA LYS LYS GLN GLU VAL VAL VAL LEU GLY SER GLN GLU          
SEQRES  22 A  427  GLY ALA MET HIS THR ALA LEU THR GLY ALA THR GLU ILE          
SEQRES  23 A  427  GLN THR SER GLY THR THR THR ILE PHE ALA GLY HIS LEU          
SEQRES  24 A  427  LYS CYS ARG LEU LYS MET ASP LYS LEU THR LEU LYS GLY          
SEQRES  25 A  427  MET SER TYR VAL MET CYS THR GLY SER PHE LYS LEU GLU          
SEQRES  26 A  427  LYS GLU VAL ALA GLU THR GLN HIS GLY THR VAL LEU VAL          
SEQRES  27 A  427  GLN VAL LYS TYR GLU GLY THR ASP ALA PRO CYS LYS ILE          
SEQRES  28 A  427  PRO PHE SER SER GLN ASP GLU LYS GLY VAL THR GLN ASN          
SEQRES  29 A  427  GLY ARG LEU ILE THR ALA ASN PRO ILE VAL THR ASP LYS          
SEQRES  30 A  427  GLU LYS PRO VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY          
SEQRES  31 A  427  GLU SER TYR ILE VAL VAL GLY ALA GLY GLU LYS ALA LEU          
SEQRES  32 A  427  LYS LEU SER TRP PHE LYS LYS GLY SER SER ILE GLY LYS          
SEQRES  33 A  427  MET PHE GLU ALA THR ALA ARG GLY ALA ARG ARG                  
SEQRES   1 B  427  GLY HIS HIS HIS HIS HIS HIS HIS HIS GLY SER SER THR          
SEQRES   2 B  427  SER ASN GLY MET ARG CYS VAL GLY ILE GLY ASN ARG ASP          
SEQRES   3 B  427  PHE VAL GLU GLY LEU SER GLY ALA THR TRP VAL ASP VAL          
SEQRES   4 B  427  VAL LEU GLU HIS GLY SER CYS VAL THR THR MET ALA LYS          
SEQRES   5 B  427  ASP LYS PRO THR LEU ASP ILE GLU LEU LEU LYS THR GLU          
SEQRES   6 B  427  VAL THR ASN PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU          
SEQRES   7 B  427  ALA LYS ILE SER ASN THR THR THR ASP SER ARG CYS PRO          
SEQRES   8 B  427  THR GLN GLY GLU ALA THR LEU VAL GLU GLU GLN ASP THR          
SEQRES   9 B  427  ASN PHE VAL CYS ARG ARG THR PHE VAL ASP ARG GLY HIS          
SEQRES  10 B  427  GLY ASN GLY CYS GLY LEU PHE GLY LYS GLY SER LEU ILE          
SEQRES  11 B  427  THR CYS ALA LYS PHE LYS CYS VAL THR LYS LEU GLU GLY          
SEQRES  12 B  427  LYS ILE VAL GLN TYR GLU ASN LEU LYS TYR SER VAL ILE          
SEQRES  13 B  427  VAL THR VAL HIS THR GLY ASP GLN HIS GLN VAL GLY ASN          
SEQRES  14 B  427  GLU THR THR GLU HIS GLY THR ILE ALA THR ILE THR PRO          
SEQRES  15 B  427  GLN ALA PRO THR SER GLU ILE GLN LEU THR ASP TYR GLY          
SEQRES  16 B  427  ALA LEU THR LEU ASP CYS SER PRO ARG THR GLY LEU ASP          
SEQRES  17 B  427  PHE ASN GLU MET VAL LEU LEU THR MET GLU LYS LYS SER          
SEQRES  18 B  427  TRP LEU VAL HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU          
SEQRES  19 B  427  PRO TRP THR SER GLY ALA SER THR SER GLN GLU THR TRP          
SEQRES  20 B  427  ASN ARG GLN ASP LEU LEU VAL THR PHE LYS THR ALA HIS          
SEQRES  21 B  427  ALA LYS LYS GLN GLU VAL VAL VAL LEU GLY SER GLN GLU          
SEQRES  22 B  427  GLY ALA MET HIS THR ALA LEU THR GLY ALA THR GLU ILE          
SEQRES  23 B  427  GLN THR SER GLY THR THR THR ILE PHE ALA GLY HIS LEU          
SEQRES  24 B  427  LYS CYS ARG LEU LYS MET ASP LYS LEU THR LEU LYS GLY          
SEQRES  25 B  427  MET SER TYR VAL MET CYS THR GLY SER PHE LYS LEU GLU          
SEQRES  26 B  427  LYS GLU VAL ALA GLU THR GLN HIS GLY THR VAL LEU VAL          
SEQRES  27 B  427  GLN VAL LYS TYR GLU GLY THR ASP ALA PRO CYS LYS ILE          
SEQRES  28 B  427  PRO PHE SER SER GLN ASP GLU LYS GLY VAL THR GLN ASN          
SEQRES  29 B  427  GLY ARG LEU ILE THR ALA ASN PRO ILE VAL THR ASP LYS          
SEQRES  30 B  427  GLU LYS PRO VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY          
SEQRES  31 B  427  GLU SER TYR ILE VAL VAL GLY ALA GLY GLU LYS ALA LEU          
SEQRES  32 B  427  LYS LEU SER TRP PHE LYS LYS GLY SER SER ILE GLY LYS          
SEQRES  33 B  427  MET PHE GLU ALA THR ALA ARG GLY ALA ARG ARG                  
MODRES 4GSX ASN A   67  ASN  GLYCOSYLATION SITE                                 
MODRES 4GSX ASN B   67  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 501      14                                                       
HET     CD  A 502       1                                                       
HET     CD  A 503       1                                                       
HET     CL  A 504       1                                                       
HET    NAG  B 501      14                                                       
HET     CD  B 502       1                                                       
HET     CD  B 503       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CD CADMIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4   CD    4(CD 2+)                                                     
FORMUL   6   CL    CL 1-                                                        
FORMUL  10  HOH   *666(H2 O)                                                    
HELIX    1   1 GLY A    7  ARG A    9  5                                   3    
HELIX    2   2 LEU A   82  ASP A   87  5                                   6    
HELIX    3   3 GLY A  100  GLY A  104  5                                   5    
HELIX    4   4 GLN A  131  GLU A  133  5                                   3    
HELIX    5   5 LYS A  210  ASP A  215  1                                   6    
HELIX    6   6 ARG A  233  LEU A  236  5                                   4    
HELIX    7   7 GLN A  256  LEU A  264  1                                   9    
HELIX    8   8 ALA A  382  ALA A  386  5                                   5    
HELIX    9   9 GLY B    7  ARG B    9  5                                   3    
HELIX   10  10 LEU B   82  GLN B   86  5                                   5    
HELIX   11  11 GLN B  131  GLU B  133  5                                   3    
HELIX   12  12 LYS B  210  ASP B  215  1                                   6    
HELIX   13  13 ARG B  233  LEU B  236  5                                   4    
HELIX   14  14 GLN B  256  THR B  265  1                                  10    
SHEET    1   A10 VAL A   4  GLY A   5  0                                        
SHEET    2   A10 VAL A  31  THR A  33  1  O  THR A  32   N  VAL A   4           
SHEET    3   A10 LEU A  41  THR A  51 -1  O  LEU A  41   N  THR A  33           
SHEET    4   A10 THR A 276  PHE A 279 -1  O  THR A 277   N  VAL A  50           
SHEET    5   A10 THR A 268  SER A 273 -1  N  GLN A 271   O  ILE A 278           
SHEET    6   A10 LYS A 204  HIS A 209 -1  N  LEU A 207   O  THR A 268           
SHEET    7   A10 MET A 196  MET A 201 -1  N  VAL A 197   O  VAL A 208           
SHEET    8   A10 GLY A 109  ILE A 129 -1  N  LYS A 128   O  LEU A 198           
SHEET    9   A10 LEU A 135  VAL A 143  0                                        
SHEET   10   A10 THR A 160  ILE A 164 -1  O  ALA A 162   N  VAL A 139           
SHEET    1   B 9 PHE A  90  ARG A  99  0                                        
SHEET    2   B 9 GLY A 109  ILE A 129 -1  O  GLY A 111   N  VAL A  97           
SHEET    3   B 9 MET A 196  MET A 201 -1  O  LEU A 198   N  LYS A 128           
SHEET    4   B 9 LYS A 204  HIS A 209 -1  O  VAL A 208   N  VAL A 197           
SHEET    5   B 9 THR A 268  SER A 273 -1  O  THR A 268   N  LEU A 207           
SHEET    6   B 9 THR A 276  PHE A 279 -1  O  ILE A 278   N  GLN A 271           
SHEET    7   B 9 LEU A  41  THR A  51 -1  N  VAL A  50   O  THR A 277           
SHEET    8   B 9 ALA A  54  SER A  72  0                                        
SHEET    9   B 9 TRP A 220  SER A 222 -1  O  THR A 221   N  LYS A  58           
SHEET    1   C 5 PHE A  11  GLU A  13  0                                        
SHEET    2   C 5 ALA A  18  GLU A  26 -1  O  TRP A  20   N  VAL A  12           
SHEET    3   C 5 HIS A 282  ASP A 290 -1  O  CYS A 285   N  VAL A  23           
SHEET    4   C 5 GLY A 179  PRO A 187 -1  N  ASP A 184   O  ARG A 286           
SHEET    5   C 5 THR A 170  LEU A 175 -1  N  SER A 171   O  LEU A 183           
SHEET    1   D 2 VAL A 238  PHE A 240  0                                        
SHEET    2   D 2 VAL A 250  VAL A 252 -1  O  VAL A 251   N  THR A 239           
SHEET    1   E 3 PHE A 306  LEU A 308  0                                        
SHEET    2   E 3 VAL A 320  TYR A 326 -1  O  LYS A 325   N  LYS A 307           
SHEET    3   E 3 ALA A 313  GLU A 314 -1  N  ALA A 313   O  LEU A 321           
SHEET    1   F 3 PHE A 306  LEU A 308  0                                        
SHEET    2   F 3 VAL A 320  TYR A 326 -1  O  LYS A 325   N  LYS A 307           
SHEET    3   F 3 VAL A 365  ALA A 369 -1  O  ILE A 367   N  VAL A 322           
SHEET    1   G 2 CYS A 333  LYS A 334  0                                        
SHEET    2   G 2 ILE A 357  VAL A 358 -1  O  VAL A 358   N  CYS A 333           
SHEET    1   H 3 PHE A 337  ASP A 341  0                                        
SHEET    2   H 3 GLY A 374  VAL A 380 -1  O  TYR A 377   N  GLN A 340           
SHEET    3   H 3 LEU A 387  LYS A 393 -1  O  LYS A 393   N  GLY A 374           
SHEET    1   I 5 CYS B   3  GLY B   5  0                                        
SHEET    2   I 5 CYS B  30  MET B  34  1  O  THR B  32   N  VAL B   4           
SHEET    3   I 5 THR B  40  THR B  51 -1  O  LEU B  41   N  THR B  33           
SHEET    4   I 5 LEU B 135  VAL B 143 -1  O  ILE B 140   N  GLU B  44           
SHEET    5   I 5 THR B 160  ILE B 164 -1  O  ILE B 164   N  TYR B 137           
SHEET    1   J 5 CYS B   3  GLY B   5  0                                        
SHEET    2   J 5 CYS B  30  MET B  34  1  O  THR B  32   N  VAL B   4           
SHEET    3   J 5 THR B  40  THR B  51 -1  O  LEU B  41   N  THR B  33           
SHEET    4   J 5 THR B 276  PHE B 279 -1  O  THR B 277   N  VAL B  50           
SHEET    5   J 5 THR B 272  SER B 273 -1  N  SER B 273   O  THR B 276           
SHEET    1   K 5 PHE B  11  GLU B  13  0                                        
SHEET    2   K 5 ALA B  18  GLU B  26 -1  O  TRP B  20   N  VAL B  12           
SHEET    3   K 5 HIS B 282  ASP B 290 -1  O  CYS B 285   N  VAL B  23           
SHEET    4   K 5 GLY B 179  PRO B 187 -1  N  ASP B 184   O  ARG B 286           
SHEET    5   K 5 THR B 170  LEU B 175 -1  N  LEU B 175   O  GLY B 179           
SHEET    1   L 4 PHE B  90  ASP B  98  0                                        
SHEET    2   L 4 LYS B 110  ILE B 129 -1  O  GLY B 111   N  VAL B  97           
SHEET    3   L 4 ALA B  54  SER B  72 -1  N  SER B  66   O  LYS B 118           
SHEET    4   L 4 TRP B 220  SER B 222 -1  O  THR B 221   N  LYS B  58           
SHEET    1   M 5 PHE B  90  ASP B  98  0                                        
SHEET    2   M 5 LYS B 110  ILE B 129 -1  O  GLY B 111   N  VAL B  97           
SHEET    3   M 5 MET B 196  MET B 201 -1  O  LEU B 198   N  LYS B 128           
SHEET    4   M 5 LYS B 204  HIS B 209 -1  O  VAL B 208   N  VAL B 197           
SHEET    5   M 5 GLU B 269  ILE B 270 -1  O  ILE B 270   N  SER B 205           
SHEET    1   N 2 VAL B 238  PHE B 240  0                                        
SHEET    2   N 2 VAL B 250  VAL B 252 -1  O  VAL B 251   N  THR B 239           
SHEET    1   O 3 PHE B 306  LEU B 308  0                                        
SHEET    2   O 3 VAL B 320  TYR B 326 -1  O  LYS B 325   N  LYS B 307           
SHEET    3   O 3 ALA B 313  GLU B 314 -1  N  ALA B 313   O  LEU B 321           
SHEET    1   P 3 PHE B 306  LEU B 308  0                                        
SHEET    2   P 3 VAL B 320  TYR B 326 -1  O  LYS B 325   N  LYS B 307           
SHEET    3   P 3 VAL B 365  ALA B 369 -1  O  ILE B 367   N  VAL B 322           
SHEET    1   Q 2 CYS B 333  LYS B 334  0                                        
SHEET    2   Q 2 ILE B 357  VAL B 358 -1  O  VAL B 358   N  CYS B 333           
SHEET    1   R 3 PHE B 337  ASP B 341  0                                        
SHEET    2   R 3 GLY B 374  VAL B 380 -1  O  TYR B 377   N  GLN B 340           
SHEET    3   R 3 LEU B 387  LYS B 393 -1  O  LEU B 389   N  ILE B 378           
SSBOND   1 CYS A    3    CYS A   30                          1555   1555  2.03  
SSBOND   2 CYS A   60    CYS A  121                          1555   1555  2.06  
SSBOND   3 CYS A   74    CYS A  105                          1555   1555  2.04  
SSBOND   4 CYS A   92    CYS A  116                          1555   1555  2.04  
SSBOND   5 CYS A  185    CYS A  285                          1555   1555  2.04  
SSBOND   6 CYS A  302    CYS A  333                          1555   1555  2.05  
SSBOND   7 CYS B    3    CYS B   30                          1555   1555  2.04  
SSBOND   8 CYS B   60    CYS B  121                          1555   1555  2.06  
SSBOND   9 CYS B   74    CYS B  105                          1555   1555  2.03  
SSBOND  10 CYS B   92    CYS B  116                          1555   1555  2.03  
SSBOND  11 CYS B  185    CYS B  285                          1555   1555  2.01  
SSBOND  12 CYS B  302    CYS B  333                          1555   1555  2.05  
LINK        CD    CD B 503                 O   HOH B 789     1555   1555  2.39  
LINK         NE2 HIS B 282                CD    CD B 503     1555   1555  2.42  
LINK         OE1 GLU B 311                CD    CD A 502     1555   1555  2.43  
LINK         OE2 GLU B 311                CD    CD A 502     1555   1555  2.45  
LINK         OD2 ASP A  98                CD    CD A 502     1555   1555  2.46  
LINK         NE2 HIS B  27                CD    CD B 503     1555   1555  2.48  
LINK         OD1 ASP A  10                CD    CD A 503     1555   1555  2.52  
LINK         OD1 ASP B  10                CD    CD B 502     1555   1555  2.52  
LINK         OD2 ASP A  10                CD    CD A 503     1555   1555  2.57  
LINK        CD    CD A 503                 O   HOH A 623     1555   1555  2.60  
LINK        CD    CD A 503                 O   HOH A 932     1555   1555  2.62  
LINK         OD2 ASP B  10                CD    CD B 502     1555   1555  2.65  
LINK        CD    CD A 502                 O   HOH A 710     1555   1555  2.67  
LINK         ND2 ASN A  67                 C1  NAG A 501     1555   1555  1.84  
LINK         ND2 ASN B  67                 C1  NAG B 501     1555   1555  1.80  
CISPEP   1 ALA A  331    PRO A  332          0         5.05                     
CISPEP   2 ALA B  331    PRO B  332          0         8.13                     
SITE     1 AC1  3 ASN A  67  HOH A 733  HOH A 896                               
SITE     1 AC2  4 THR A  76  ASP A  98  HOH A 710  GLU B 311                    
SITE     1 AC3  4 ASP A  10  HOH A 623  HOH A 777  HOH A 932                    
SITE     1 AC4  3 GLY A 102  HOH A 628  GLU B 311                               
SITE     1 AC5  3 ASN B  67  LYS B 118  HOH B 775                               
SITE     1 AC6  2 ASP B  10  HOH B 849                                          
SITE     1 AC7  5 HIS B  27  HIS B 282  GLU B 368  HOH B 789                    
SITE     2 AC7  5 HOH B 806                                                     
CRYST1   77.571   77.571  292.518  90.00  90.00 120.00 P 63         12          
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      0.012891  0.007443  0.000000        0.00000                         
SCALE2      0.000000  0.014886  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003419        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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