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Database: PDB
Entry: 6IW1
LinkDB: 6IW1
Original site: 6IW1 
HEADER    VIRAL PROTEIN                           04-DEC-18   6IW1              
TITLE     CRYSTAL STRUCTURE OF YFV-17D SE IN POSTFUSION STATE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENVELOPE PROTEIN E;                                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YELLOW FEVER VIRUS (STRAIN 17D VACCINE);        
SOURCE   3 ORGANISM_COMMON: YFV;                                                
SOURCE   4 ORGANISM_TAXID: 11090;                                               
SOURCE   5 STRAIN: 17D VACCINE;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    YELLOW FEVER VIRUS, ENVELOPE PROTEIN, FLAVIVIRUS, VIRAL PROTEIN       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.S.LU,H.X.XIAO,S.H.LI,X.F.PANG                                       
REVDAT   1   13-FEB-19 6IW1    0                                                
JRNL        AUTH   X.LU,H.XIAO,S.LI,X.PANG,J.SONG,S.LIU,H.CHENG,Y.LI,X.WANG,    
JRNL        AUTH 2 C.HUANG,T.GUO,J.TER MEULEN,S.DAFFIS,J.YAN,L.DAI,Z.RAO,       
JRNL        AUTH 3 H.D.KLENK,J.QI,Y.SHI,G.F.GAO                                 
JRNL        TITL   DOUBLE LOCK OF A HUMAN NEUTRALIZING AND PROTECTIVE           
JRNL        TITL 2 MONOCLONAL ANTIBODY TARGETING THE YELLOW FEVER VIRUS         
JRNL        TITL 3 ENVELOPE.                                                    
JRNL        REF    CELL REP                      V.  26   438 2019              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   30625326                                                     
JRNL        DOI    10.1016/J.CELREP.2018.12.065                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26089                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1327                            
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 39.9588 -  6.3458    0.97     3017   159  0.2127 0.2702        
REMARK   3     2  6.3458 -  5.0401    0.99     3041   155  0.2249 0.2301        
REMARK   3     3  5.0401 -  4.4039    0.99     3017   141  0.1809 0.2020        
REMARK   3     4  4.4039 -  4.0016    1.00     3025   172  0.1889 0.2438        
REMARK   3     5  4.0016 -  3.7150    1.00     3049   141  0.2165 0.2450        
REMARK   3     6  3.7150 -  3.4961    0.97     2912   170  0.2314 0.2640        
REMARK   3     7  3.4961 -  3.3211    0.95     2849   163  0.2403 0.3007        
REMARK   3     8  3.3211 -  3.1766    0.80     2405   131  0.2595 0.2924        
REMARK   3     9  3.1766 -  3.0544    0.49     1447    95  0.2990 0.3547        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.750           
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: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           8882                                  
REMARK   3   ANGLE     :  1.151          12015                                  
REMARK   3   CHIRALITY :  0.043           1374                                  
REMARK   3   PLANARITY :  0.007           1542                                  
REMARK   3   DIHEDRAL  : 18.613           3208                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 168.5566  18.2768  34.9096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2398 T22:   0.1737                                     
REMARK   3      T33:   0.2354 T12:   0.0009                                     
REMARK   3      T13:   0.0006 T23:   0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0325 L22:   0.0712                                     
REMARK   3      L33:   1.5686 L12:  -0.0837                                     
REMARK   3      L13:  -0.1208 L23:   0.1411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:  -0.0065 S13:   0.1149                       
REMARK   3      S21:  -0.0258 S22:  -0.0128 S23:  -0.0165                       
REMARK   3      S31:  -0.2377 S32:   0.0656 S33:   0.0010                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 176.4432  -6.1631  35.5291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1583 T22:   0.1752                                     
REMARK   3      T33:   0.2144 T12:   0.0037                                     
REMARK   3      T13:   0.0443 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1928 L22:   0.3012                                     
REMARK   3      L33:   0.9616 L12:  -0.0421                                     
REMARK   3      L13:   0.1462 L23:   0.0522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0388 S12:  -0.0783 S13:  -0.0449                       
REMARK   3      S21:  -0.0389 S22:   0.0089 S23:  -0.1003                       
REMARK   3      S31:   0.0115 S32:   0.1202 S33:  -0.0094                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 151.6168  -0.9052  36.9985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1584 T22:   0.2577                                     
REMARK   3      T33:   0.2524 T12:   0.0173                                     
REMARK   3      T13:  -0.0269 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0736 L22:   0.2994                                     
REMARK   3      L33:   0.9338 L12:   0.0198                                     
REMARK   3      L13:  -0.2554 L23:  -0.0276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0372 S12:   0.0336 S13:  -0.0611                       
REMARK   3      S21:  -0.0396 S22:   0.0097 S23:   0.1509                       
REMARK   3      S31:   0.1670 S32:  -0.1627 S33:  -0.0038                       
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 6IW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300010032.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97853                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26089                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 39.90                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
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   (%): 58.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 30% V/V JEFFAMINE,   
REMARK 280  M-600, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K      
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       70.27900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.13750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.27900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.13750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12380 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     ALA A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     VAL A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     GLN A   149                                                      
REMARK 465     GLU A   150                                                      
REMARK 465     ASN A   151                                                      
REMARK 465     TRP A   152                                                      
REMARK 465     ASN A   153                                                      
REMARK 465     THR A   154                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     GLY A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     SER A   395                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     VAL B   145                                                      
REMARK 465     GLY B   146                                                      
REMARK 465     ALA B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     GLN B   149                                                      
REMARK 465     GLU B   150                                                      
REMARK 465     ASN B   151                                                      
REMARK 465     TRP B   152                                                      
REMARK 465     ASN B   153                                                      
REMARK 465     THR B   154                                                      
REMARK 465     GLY B   393                                                      
REMARK 465     SER B   394                                                      
REMARK 465     SER B   395                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     VAL C   145                                                      
REMARK 465     GLY C   146                                                      
REMARK 465     ALA C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     GLN C   149                                                      
REMARK 465     GLU C   150                                                      
REMARK 465     ASN C   151                                                      
REMARK 465     TRP C   152                                                      
REMARK 465     ASN C   153                                                      
REMARK 465     THR C   154                                                      
REMARK 465     ASP C   339                                                      
REMARK 465     LEU C   340                                                      
REMARK 465     THR C   341                                                      
REMARK 465     ALA C   342                                                      
REMARK 465     ALA C   343                                                      
REMARK 465     GLY C   393                                                      
REMARK 465     SER C   394                                                      
REMARK 465     SER C   395                                                      
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   OD1  ASP A   267     NZ   LYS A   275              1.25            
REMARK 500   SG   CYS B     3     CB   CYS B    30              1.92            
REMARK 500   SG   CYS C   300     CB   CYS C   330              2.13            
REMARK 500   CG   ASP A   267     NZ   LYS A   275              2.15            
REMARK 500   O    VAL B   324     N    ASP B   360              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER B 221   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    HIS B 277   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    PRO C 329   C   -  N   -  CA  ANGL. DEV. = -11.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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    GLU A 199     -126.98     55.23                                   
REMARK 500    HIS A 238     -156.97   -103.97                                   
REMARK 500    LYS A 266     -128.60    -99.04                                   
REMARK 500    THR A 268       -2.48    -56.01                                   
REMARK 500    ASN A 269      -65.84   -136.04                                   
REMARK 500    LYS A 303       83.37     54.71                                   
REMARK 500    LYS A 326      -52.20   -135.18                                   
REMARK 500    ALA A 328     -120.51    -74.59                                   
REMARK 500    GLU B 199     -127.34     56.18                                   
REMARK 500    HIS B 238     -155.74   -102.04                                   
REMARK 500    LYS B 303       84.49     57.90                                   
REMARK 500    ALA B 328      165.02    149.02                                   
REMARK 500    GLU C 199     -126.28     55.24                                   
REMARK 500    HIS C 238     -156.68   -101.57                                   
REMARK 500    ASP C 267      171.74     68.38                                   
REMARK 500    ASN C 269      -73.21    -74.40                                   
REMARK 500    HIS C 277      -38.32     59.59                                   
REMARK 500    LYS C 303       89.06     63.50                                   
REMARK 500    ALA C 328     -144.06     63.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6IW1 A    1   395  UNP    P03314   POLG_YEFV1     286    680             
DBREF  6IW1 B    1   395  UNP    P03314   POLG_YEFV1     286    680             
DBREF  6IW1 C    1   395  UNP    P03314   POLG_YEFV1     286    680             
SEQRES   1 A  395  ALA HIS CYS ILE GLY ILE THR ASP ARG ASP PHE ILE GLU          
SEQRES   2 A  395  GLY VAL HIS GLY GLY THR TRP VAL SER ALA THR LEU GLU          
SEQRES   3 A  395  GLN ASP LYS CYS VAL THR VAL MET ALA PRO ASP LYS PRO          
SEQRES   4 A  395  SER LEU ASP ILE SER LEU GLU THR VAL ALA ILE ASP ARG          
SEQRES   5 A  395  PRO ALA GLU VAL ARG LYS VAL CYS TYR ASN ALA VAL LEU          
SEQRES   6 A  395  THR HIS VAL LYS ILE ASN ASP LYS CYS PRO SER THR GLY          
SEQRES   7 A  395  GLU ALA HIS LEU ALA GLU GLU ASN GLU GLY ASP ASN ALA          
SEQRES   8 A  395  CYS LYS ARG THR TYR SER ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 A  395  CYS GLY LEU PHE GLY LYS GLY SER ILE VAL ALA CYS ALA          
SEQRES  10 A  395  LYS PHE THR CYS ALA LYS SER MET SER LEU PHE GLU VAL          
SEQRES  11 A  395  ASP GLN THR LYS ILE GLN TYR VAL ILE ARG ALA GLN LEU          
SEQRES  12 A  395  HIS VAL GLY ALA LYS GLN GLU ASN TRP ASN THR ASP ILE          
SEQRES  13 A  395  LYS THR LEU LYS PHE ASP ALA LEU SER GLY SER GLN GLU          
SEQRES  14 A  395  VAL GLU PHE ILE GLY TYR GLY LYS ALA THR LEU GLU CYS          
SEQRES  15 A  395  GLN VAL GLN THR ALA VAL ASP PHE GLY ASN SER TYR ILE          
SEQRES  16 A  395  ALA GLU MET GLU THR GLU SER TRP ILE VAL ASP ARG GLN          
SEQRES  17 A  395  TRP ALA GLN ASP LEU THR LEU PRO TRP GLN SER GLY SER          
SEQRES  18 A  395  GLY GLY VAL TRP ARG GLU MET HIS HIS LEU VAL GLU PHE          
SEQRES  19 A  395  GLU PRO PRO HIS ALA ALA THR ILE ARG VAL LEU ALA LEU          
SEQRES  20 A  395  GLY ASN GLN GLU GLY SER LEU LYS THR ALA LEU THR GLY          
SEQRES  21 A  395  ALA MET ARG VAL THR LYS ASP THR ASN ASP ASN ASN LEU          
SEQRES  22 A  395  TYR LYS LEU HIS GLY GLY HIS VAL SER CYS ARG VAL LYS          
SEQRES  23 A  395  LEU SER ALA LEU THR LEU LYS GLY THR SER TYR LYS ILE          
SEQRES  24 A  395  CYS THR ASP LYS MET PHE PHE VAL LYS ASN PRO THR ASP          
SEQRES  25 A  395  THR GLY HIS GLY THR VAL VAL MET GLN VAL LYS VAL SER          
SEQRES  26 A  395  LYS GLY ALA PRO CYS ARG ILE PRO VAL ILE VAL ALA ASP          
SEQRES  27 A  395  ASP LEU THR ALA ALA ILE ASN LYS GLY ILE LEU VAL THR          
SEQRES  28 A  395  VAL ASN PRO ILE ALA SER THR ASN ASP ASP GLU VAL LEU          
SEQRES  29 A  395  ILE GLU VAL ASN PRO PRO PHE GLY ASP SER TYR ILE ILE          
SEQRES  30 A  395  VAL GLY ARG GLY ASP SER ARG LEU THR TYR GLN TRP HIS          
SEQRES  31 A  395  LYS GLU GLY SER SER                                          
SEQRES   1 B  395  ALA HIS CYS ILE GLY ILE THR ASP ARG ASP PHE ILE GLU          
SEQRES   2 B  395  GLY VAL HIS GLY GLY THR TRP VAL SER ALA THR LEU GLU          
SEQRES   3 B  395  GLN ASP LYS CYS VAL THR VAL MET ALA PRO ASP LYS PRO          
SEQRES   4 B  395  SER LEU ASP ILE SER LEU GLU THR VAL ALA ILE ASP ARG          
SEQRES   5 B  395  PRO ALA GLU VAL ARG LYS VAL CYS TYR ASN ALA VAL LEU          
SEQRES   6 B  395  THR HIS VAL LYS ILE ASN ASP LYS CYS PRO SER THR GLY          
SEQRES   7 B  395  GLU ALA HIS LEU ALA GLU GLU ASN GLU GLY ASP ASN ALA          
SEQRES   8 B  395  CYS LYS ARG THR TYR SER ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 B  395  CYS GLY LEU PHE GLY LYS GLY SER ILE VAL ALA CYS ALA          
SEQRES  10 B  395  LYS PHE THR CYS ALA LYS SER MET SER LEU PHE GLU VAL          
SEQRES  11 B  395  ASP GLN THR LYS ILE GLN TYR VAL ILE ARG ALA GLN LEU          
SEQRES  12 B  395  HIS VAL GLY ALA LYS GLN GLU ASN TRP ASN THR ASP ILE          
SEQRES  13 B  395  LYS THR LEU LYS PHE ASP ALA LEU SER GLY SER GLN GLU          
SEQRES  14 B  395  VAL GLU PHE ILE GLY TYR GLY LYS ALA THR LEU GLU CYS          
SEQRES  15 B  395  GLN VAL GLN THR ALA VAL ASP PHE GLY ASN SER TYR ILE          
SEQRES  16 B  395  ALA GLU MET GLU THR GLU SER TRP ILE VAL ASP ARG GLN          
SEQRES  17 B  395  TRP ALA GLN ASP LEU THR LEU PRO TRP GLN SER GLY SER          
SEQRES  18 B  395  GLY GLY VAL TRP ARG GLU MET HIS HIS LEU VAL GLU PHE          
SEQRES  19 B  395  GLU PRO PRO HIS ALA ALA THR ILE ARG VAL LEU ALA LEU          
SEQRES  20 B  395  GLY ASN GLN GLU GLY SER LEU LYS THR ALA LEU THR GLY          
SEQRES  21 B  395  ALA MET ARG VAL THR LYS ASP THR ASN ASP ASN ASN LEU          
SEQRES  22 B  395  TYR LYS LEU HIS GLY GLY HIS VAL SER CYS ARG VAL LYS          
SEQRES  23 B  395  LEU SER ALA LEU THR LEU LYS GLY THR SER TYR LYS ILE          
SEQRES  24 B  395  CYS THR ASP LYS MET PHE PHE VAL LYS ASN PRO THR ASP          
SEQRES  25 B  395  THR GLY HIS GLY THR VAL VAL MET GLN VAL LYS VAL SER          
SEQRES  26 B  395  LYS GLY ALA PRO CYS ARG ILE PRO VAL ILE VAL ALA ASP          
SEQRES  27 B  395  ASP LEU THR ALA ALA ILE ASN LYS GLY ILE LEU VAL THR          
SEQRES  28 B  395  VAL ASN PRO ILE ALA SER THR ASN ASP ASP GLU VAL LEU          
SEQRES  29 B  395  ILE GLU VAL ASN PRO PRO PHE GLY ASP SER TYR ILE ILE          
SEQRES  30 B  395  VAL GLY ARG GLY ASP SER ARG LEU THR TYR GLN TRP HIS          
SEQRES  31 B  395  LYS GLU GLY SER SER                                          
SEQRES   1 C  395  ALA HIS CYS ILE GLY ILE THR ASP ARG ASP PHE ILE GLU          
SEQRES   2 C  395  GLY VAL HIS GLY GLY THR TRP VAL SER ALA THR LEU GLU          
SEQRES   3 C  395  GLN ASP LYS CYS VAL THR VAL MET ALA PRO ASP LYS PRO          
SEQRES   4 C  395  SER LEU ASP ILE SER LEU GLU THR VAL ALA ILE ASP ARG          
SEQRES   5 C  395  PRO ALA GLU VAL ARG LYS VAL CYS TYR ASN ALA VAL LEU          
SEQRES   6 C  395  THR HIS VAL LYS ILE ASN ASP LYS CYS PRO SER THR GLY          
SEQRES   7 C  395  GLU ALA HIS LEU ALA GLU GLU ASN GLU GLY ASP ASN ALA          
SEQRES   8 C  395  CYS LYS ARG THR TYR SER ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 C  395  CYS GLY LEU PHE GLY LYS GLY SER ILE VAL ALA CYS ALA          
SEQRES  10 C  395  LYS PHE THR CYS ALA LYS SER MET SER LEU PHE GLU VAL          
SEQRES  11 C  395  ASP GLN THR LYS ILE GLN TYR VAL ILE ARG ALA GLN LEU          
SEQRES  12 C  395  HIS VAL GLY ALA LYS GLN GLU ASN TRP ASN THR ASP ILE          
SEQRES  13 C  395  LYS THR LEU LYS PHE ASP ALA LEU SER GLY SER GLN GLU          
SEQRES  14 C  395  VAL GLU PHE ILE GLY TYR GLY LYS ALA THR LEU GLU CYS          
SEQRES  15 C  395  GLN VAL GLN THR ALA VAL ASP PHE GLY ASN SER TYR ILE          
SEQRES  16 C  395  ALA GLU MET GLU THR GLU SER TRP ILE VAL ASP ARG GLN          
SEQRES  17 C  395  TRP ALA GLN ASP LEU THR LEU PRO TRP GLN SER GLY SER          
SEQRES  18 C  395  GLY GLY VAL TRP ARG GLU MET HIS HIS LEU VAL GLU PHE          
SEQRES  19 C  395  GLU PRO PRO HIS ALA ALA THR ILE ARG VAL LEU ALA LEU          
SEQRES  20 C  395  GLY ASN GLN GLU GLY SER LEU LYS THR ALA LEU THR GLY          
SEQRES  21 C  395  ALA MET ARG VAL THR LYS ASP THR ASN ASP ASN ASN LEU          
SEQRES  22 C  395  TYR LYS LEU HIS GLY GLY HIS VAL SER CYS ARG VAL LYS          
SEQRES  23 C  395  LEU SER ALA LEU THR LEU LYS GLY THR SER TYR LYS ILE          
SEQRES  24 C  395  CYS THR ASP LYS MET PHE PHE VAL LYS ASN PRO THR ASP          
SEQRES  25 C  395  THR GLY HIS GLY THR VAL VAL MET GLN VAL LYS VAL SER          
SEQRES  26 C  395  LYS GLY ALA PRO CYS ARG ILE PRO VAL ILE VAL ALA ASP          
SEQRES  27 C  395  ASP LEU THR ALA ALA ILE ASN LYS GLY ILE LEU VAL THR          
SEQRES  28 C  395  VAL ASN PRO ILE ALA SER THR ASN ASP ASP GLU VAL LEU          
SEQRES  29 C  395  ILE GLU VAL ASN PRO PRO PHE GLY ASP SER TYR ILE ILE          
SEQRES  30 C  395  VAL GLY ARG GLY ASP SER ARG LEU THR TYR GLN TRP HIS          
SEQRES  31 C  395  LYS GLU GLY SER SER                                          
HELIX    1 AA1 LEU A   82  ASN A   86  5                                   5    
HELIX    2 AA2 GLY A  100  GLY A  104  5                                   5    
HELIX    3 AA3 ASP A  131  LYS A  134  5                                   4    
HELIX    4 AA4 ARG A  207  ASP A  212  1                                   6    
HELIX    5 AA5 GLU A  227  HIS A  230  5                                   4    
HELIX    6 AA6 GLN A  250  LEU A  258  1                                   9    
HELIX    7 AA7 ARG A  380  ARG A  384  5                                   5    
HELIX    8 AA8 LEU B   82  ASN B   86  5                                   5    
HELIX    9 AA9 GLY B  100  GLY B  104  5                                   5    
HELIX   10 AB1 ASP B  131  LYS B  134  5                                   4    
HELIX   11 AB2 ARG B  207  ASP B  212  1                                   6    
HELIX   12 AB3 GLU B  227  HIS B  230  5                                   4    
HELIX   13 AB4 GLN B  250  LEU B  258  1                                   9    
HELIX   14 AB5 THR B  259  ALA B  261  5                                   3    
HELIX   15 AB6 ARG B  380  ARG B  384  5                                   5    
HELIX   16 AB7 LEU C   82  ASN C   86  5                                   5    
HELIX   17 AB8 GLY C  100  GLY C  104  5                                   5    
HELIX   18 AB9 ASP C  131  LYS C  134  5                                   4    
HELIX   19 AC1 ARG C  207  ASP C  212  1                                   6    
HELIX   20 AC2 GLU C  227  HIS C  230  5                                   4    
HELIX   21 AC3 GLN C  250  LEU C  258  1                                   9    
HELIX   22 AC4 THR C  259  ALA C  261  5                                   3    
HELIX   23 AC5 ARG C  380  ARG C  384  5                                   5    
SHEET    1 AA1 5 ILE A   4  GLY A   5  0                                        
SHEET    2 AA1 5 CYS A  30  ALA A  35  1  O  THR A  32   N  ILE A   4           
SHEET    3 AA1 5 LYS A  38  ASP A  51 -1  O  ILE A  43   N  VAL A  31           
SHEET    4 AA1 5 GLN A 136  LEU A 143 -1  O  GLN A 136   N  ALA A  49           
SHEET    5 AA1 5 ILE A 156  ASP A 162 -1  O  LEU A 159   N  ILE A 139           
SHEET    1 AA2 4 ILE A   4  GLY A   5  0                                        
SHEET    2 AA2 4 CYS A  30  ALA A  35  1  O  THR A  32   N  ILE A   4           
SHEET    3 AA2 4 LYS A  38  ASP A  51 -1  O  ILE A  43   N  VAL A  31           
SHEET    4 AA2 4 LEU A 273  LYS A 275 -1  O  TYR A 274   N  ILE A  50           
SHEET    1 AA3 6 SER A 167  PHE A 172  0                                        
SHEET    2 AA3 6 GLY A 176  VAL A 184 -1  O  ALA A 178   N  VAL A 170           
SHEET    3 AA3 6 VAL A 281  SER A 288 -1  O  LYS A 286   N  THR A 179           
SHEET    4 AA3 6 GLY A  18  LEU A  25 -1  N  VAL A  21   O  VAL A 285           
SHEET    5 AA3 6 PHE A  11  GLU A  13 -1  N  ILE A  12   O  TRP A  20           
SHEET    6 AA3 6 HIS B  16  GLY B  17 -1  O  HIS B  16   N  GLU A  13           
SHEET    1 AA4 4 ASN A  90  ARG A  99  0                                        
SHEET    2 AA4 4 GLY A 109  GLU A 129 -1  O  GLY A 109   N  ARG A  99           
SHEET    3 AA4 4 SER A 193  MET A 198 -1  O  GLU A 197   N  SER A 126           
SHEET    4 AA4 4 GLU A 201  ASP A 206 -1  O  VAL A 205   N  TYR A 194           
SHEET    1 AA5 4 ASN A  90  ARG A  99  0                                        
SHEET    2 AA5 4 GLY A 109  GLU A 129 -1  O  GLY A 109   N  ARG A  99           
SHEET    3 AA5 4 ALA A  54  ASP A  72 -1  N  VAL A  59   O  MET A 125           
SHEET    4 AA5 4 TRP A 217  SER A 219 -1  O  GLN A 218   N  LYS A  58           
SHEET    1 AA6 2 VAL A 232  PHE A 234  0                                        
SHEET    2 AA6 2 VAL A 244  ALA A 246 -1  O  LEU A 245   N  GLU A 233           
SHEET    1 AA7 3 LYS A 298  ILE A 299  0                                        
SHEET    2 AA7 3 CYS A 330  ARG A 331  1  O  ARG A 331   N  LYS A 298           
SHEET    3 AA7 3 ILE A 355  ALA A 356 -1  O  ALA A 356   N  CYS A 330           
SHEET    1 AA8 4 MET A 304  ASP A 312  0                                        
SHEET    2 AA8 4 VAL A 318  VAL A 324 -1  O  VAL A 319   N  THR A 311           
SHEET    3 AA8 4 VAL A 363  ASN A 368 -1  O  VAL A 367   N  VAL A 318           
SHEET    4 AA8 4 ILE A 348  LEU A 349 -1  N  ILE A 348   O  ASN A 368           
SHEET    1 AA9 3 VAL A 334  ALA A 337  0                                        
SHEET    2 AA9 3 GLY A 372  VAL A 378 -1  O  TYR A 375   N  ALA A 337           
SHEET    3 AA9 3 LEU A 385  LYS A 391 -1  O  TRP A 389   N  SER A 374           
SHEET    1 AB1 5 ILE B   4  GLY B   5  0                                        
SHEET    2 AB1 5 CYS B  30  ALA B  35  1  O  THR B  32   N  ILE B   4           
SHEET    3 AB1 5 LYS B  38  ASP B  51 -1  O  ILE B  43   N  VAL B  31           
SHEET    4 AB1 5 GLN B 136  LEU B 143 -1  O  GLN B 136   N  ALA B  49           
SHEET    5 AB1 5 ILE B 156  ASP B 162 -1  O  LEU B 159   N  ILE B 139           
SHEET    1 AB2 5 ILE B   4  GLY B   5  0                                        
SHEET    2 AB2 5 CYS B  30  ALA B  35  1  O  THR B  32   N  ILE B   4           
SHEET    3 AB2 5 LYS B  38  ASP B  51 -1  O  ILE B  43   N  VAL B  31           
SHEET    4 AB2 5 LEU B 273  LYS B 275 -1  O  TYR B 274   N  ILE B  50           
SHEET    5 AB2 5 THR B 265  LYS B 266 -1  N  THR B 265   O  LYS B 275           
SHEET    1 AB3 6 SER B 167  PHE B 172  0                                        
SHEET    2 AB3 6 GLY B 176  VAL B 184 -1  O  LEU B 180   N  GLN B 168           
SHEET    3 AB3 6 HIS B 280  LEU B 287 -1  O  LYS B 286   N  THR B 179           
SHEET    4 AB3 6 THR B  19  GLU B  26 -1  N  VAL B  21   O  VAL B 285           
SHEET    5 AB3 6 PHE B  11  GLU B  13 -1  N  ILE B  12   O  TRP B  20           
SHEET    6 AB3 6 HIS C  16  GLY C  17 -1  O  HIS C  16   N  GLU B  13           
SHEET    1 AB4 4 ASN B  90  ARG B  99  0                                        
SHEET    2 AB4 4 GLY B 109  GLU B 129 -1  O  GLY B 109   N  ARG B  99           
SHEET    3 AB4 4 ALA B  54  ASP B  72 -1  N  VAL B  59   O  MET B 125           
SHEET    4 AB4 4 TRP B 217  SER B 219 -1  O  GLN B 218   N  LYS B  58           
SHEET    1 AB5 5 ASN B  90  ARG B  99  0                                        
SHEET    2 AB5 5 GLY B 109  GLU B 129 -1  O  GLY B 109   N  ARG B  99           
SHEET    3 AB5 5 SER B 193  MET B 198 -1  O  GLU B 197   N  SER B 126           
SHEET    4 AB5 5 GLU B 201  ASP B 206 -1  O  VAL B 205   N  TYR B 194           
SHEET    5 AB5 5 MET B 262  ARG B 263 -1  O  MET B 262   N  ILE B 204           
SHEET    1 AB6 2 VAL B 232  PHE B 234  0                                        
SHEET    2 AB6 2 VAL B 244  ALA B 246 -1  O  LEU B 245   N  GLU B 233           
SHEET    1 AB7 3 LYS B 298  ILE B 299  0                                        
SHEET    2 AB7 3 CYS B 330  ARG B 331  1  O  ARG B 331   N  LYS B 298           
SHEET    3 AB7 3 ILE B 355  ALA B 356 -1  O  ALA B 356   N  CYS B 330           
SHEET    1 AB8 4 MET B 304  ASP B 312  0                                        
SHEET    2 AB8 4 VAL B 318  VAL B 324 -1  O  GLN B 321   N  LYS B 308           
SHEET    3 AB8 4 ASP B 361  ASN B 368 -1  O  VAL B 367   N  VAL B 318           
SHEET    4 AB8 4 ILE B 348  LEU B 349 -1  N  ILE B 348   O  ASN B 368           
SHEET    1 AB9 3 VAL B 334  ALA B 337  0                                        
SHEET    2 AB9 3 GLY B 372  VAL B 378 -1  O  ILE B 377   N  ILE B 335           
SHEET    3 AB9 3 LEU B 385  LYS B 391 -1  O  TRP B 389   N  SER B 374           
SHEET    1 AC1 5 ILE C   4  GLY C   5  0                                        
SHEET    2 AC1 5 CYS C  30  VAL C  33  1  O  THR C  32   N  ILE C   4           
SHEET    3 AC1 5 LEU C  41  ASP C  51 -1  O  ILE C  43   N  VAL C  31           
SHEET    4 AC1 5 GLN C 136  LEU C 143 -1  O  GLN C 136   N  ALA C  49           
SHEET    5 AC1 5 ILE C 156  ASP C 162 -1  O  LEU C 159   N  ILE C 139           
SHEET    1 AC2 4 ILE C   4  GLY C   5  0                                        
SHEET    2 AC2 4 CYS C  30  VAL C  33  1  O  THR C  32   N  ILE C   4           
SHEET    3 AC2 4 LEU C  41  ASP C  51 -1  O  ILE C  43   N  VAL C  31           
SHEET    4 AC2 4 LEU C 273  LYS C 275 -1  O  TYR C 274   N  ILE C  50           
SHEET    1 AC3 5 PHE C  11  GLU C  13  0                                        
SHEET    2 AC3 5 THR C  19  LEU C  25 -1  O  TRP C  20   N  ILE C  12           
SHEET    3 AC3 5 HIS C 280  LEU C 287 -1  O  VAL C 285   N  VAL C  21           
SHEET    4 AC3 5 GLY C 176  GLN C 185 -1  N  THR C 179   O  LYS C 286           
SHEET    5 AC3 5 SER C 167  PHE C 172 -1  N  GLN C 168   O  LEU C 180           
SHEET    1 AC4 4 ASN C  90  ARG C  99  0                                        
SHEET    2 AC4 4 GLY C 109  GLU C 129 -1  O  GLY C 109   N  ARG C  99           
SHEET    3 AC4 4 ALA C  54  ASP C  72 -1  N  VAL C  59   O  MET C 125           
SHEET    4 AC4 4 TRP C 217  SER C 219 -1  O  GLN C 218   N  LYS C  58           
SHEET    1 AC5 5 ASN C  90  ARG C  99  0                                        
SHEET    2 AC5 5 GLY C 109  GLU C 129 -1  O  GLY C 109   N  ARG C  99           
SHEET    3 AC5 5 SER C 193  MET C 198 -1  O  GLU C 197   N  SER C 126           
SHEET    4 AC5 5 GLU C 201  ASP C 206 -1  O  VAL C 205   N  TYR C 194           
SHEET    5 AC5 5 MET C 262  VAL C 264 -1  O  VAL C 264   N  SER C 202           
SHEET    1 AC6 2 VAL C 232  PHE C 234  0                                        
SHEET    2 AC6 2 VAL C 244  ALA C 246 -1  O  LEU C 245   N  GLU C 233           
SHEET    1 AC7 3 LYS C 298  ILE C 299  0                                        
SHEET    2 AC7 3 CYS C 330  ARG C 331  1  O  ARG C 331   N  LYS C 298           
SHEET    3 AC7 3 ILE C 355  ALA C 356 -1  O  ALA C 356   N  CYS C 330           
SHEET    1 AC8 4 ASP C 302  ASP C 312  0                                        
SHEET    2 AC8 4 VAL C 318  LYS C 326 -1  O  VAL C 319   N  THR C 311           
SHEET    3 AC8 4 VAL C 363  ASN C 368 -1  O  VAL C 367   N  VAL C 318           
SHEET    4 AC8 4 ILE C 348  LEU C 349 -1  N  ILE C 348   O  ASN C 368           
SHEET    1 AC9 3 VAL C 334  ALA C 337  0                                        
SHEET    2 AC9 3 GLY C 372  VAL C 378 -1  O  TYR C 375   N  ALA C 337           
SHEET    3 AC9 3 LEU C 385  LYS C 391 -1  O  LEU C 385   N  VAL C 378           
SSBOND   1 CYS A    3    CYS A   30                          1555   1555  2.03  
SSBOND   2 CYS A   60    CYS A  121                          1555   1555  2.04  
SSBOND   3 CYS A   74    CYS A  105                          1555   1555  2.03  
SSBOND   4 CYS A   92    CYS A  116                          1555   1555  2.03  
SSBOND   5 CYS A  182    CYS A  283                          1555   1555  2.02  
SSBOND   6 CYS A  300    CYS A  330                          1555   1555  2.03  
SSBOND   7 CYS B    3    CYS B   30                          1555   1555  2.03  
SSBOND   8 CYS B   60    CYS B  121                          1555   1555  2.03  
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  182    CYS B  283                          1555   1555  2.02  
SSBOND  12 CYS B  300    CYS B  330                          1555   1555  2.00  
SSBOND  13 CYS C    3    CYS C   30                          1555   1555  2.03  
SSBOND  14 CYS C   60    CYS C  121                          1555   1555  2.04  
SSBOND  15 CYS C   74    CYS C  105                          1555   1555  2.03  
SSBOND  16 CYS C   92    CYS C  116                          1555   1555  2.03  
SSBOND  17 CYS C  182    CYS C  283                          1555   1555  2.03  
SSBOND  18 CYS C  300    CYS C  330                          1555   1555  2.03  
CISPEP   1 LYS B  326    GLY B  327          0       -19.27                     
CRYST1  140.558   88.275  128.953  90.00 107.06  90.00 C 1 2 1      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      0.007115  0.000000  0.002183        0.00000                         
SCALE2      0.000000  0.011328  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008112        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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