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Database: PDB
Entry: 1WQV
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Original site: 1WQV 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           02-OCT-04   1WQV              
TITLE     HUMAN FACTOR VIIA-TISSUE FACTOR COMPLEXED WITH PROPYLSULFONAMIDE-D-   
TITLE    2 THR-MET-P-AMINOBENZAMIDINE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: FACTOR VII LIGHT CHAIN;                                    
COMPND   5 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, SPCA,             
COMPND   6 PROCONVERTIN, EPTACOG ALFA;                                          
COMPND   7 EC: 3.4.21.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND  11 CHAIN: H;                                                            
COMPND  12 FRAGMENT: FACTOR VII HEAVY CHAIN;                                    
COMPND  13 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, SPCA,             
COMPND  14 PROCONVERTIN, EPTACOG ALFA;                                          
COMPND  15 EC: 3.4.21.21;                                                       
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: TISSUE FACTOR;                                             
COMPND  19 CHAIN: T;                                                            
COMPND  20 FRAGMENT: RESIDUES 1-218;                                            
COMPND  21 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;  
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 EXPRESSION_SYSTEM_STRAIN: JM-109;                                    
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  25 EXPRESSION_SYSTEM_PLASMID: PKK223-3                                  
KEYWDS    SERINE PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KADONO,A.SAKAMOTO,Y.KIKUCHI,M.OH-EDA,N.YABUTA,T.KOGA,K.HATTORI,     
AUTHOR   2 T.SHIRAISHI,M.HARAMURA,H.KODAMA                                      
REVDAT   3   13-JUL-11 1WQV    1       VERSN                                    
REVDAT   2   24-FEB-09 1WQV    1       VERSN                                    
REVDAT   1   02-OCT-05 1WQV    0                                                
JRNL        AUTH   S.KADONO,A.SAKAMOTO,Y.KIKUCHI,M.OH-EDA,N.YABUTA,T.KOGA,      
JRNL        AUTH 2 K.HATTORI,T.SHIRAISHI,M.HARAMURA,H.KODAMA,T.ESAKI,H.SATO,    
JRNL        AUTH 3 Y.WATANABE,S.ITOH,M.OHTA,T.KOZONO                            
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN FACTOR VIIA/TISSUE FACTOR IN      
JRNL        TITL 2 COMPLEX WITH PEPTIDE MIMETIC INHIBITOR                       
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 324  1227 2004              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   15504346                                                     
JRNL        DOI    10.1016/J.BBRC.2004.09.182                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1728720.430                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24121                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1648                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : NULL                 
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4665                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 328                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.360 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.280 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.960 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.860 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PARAHCSDX.CGU                                  
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : 132.X.PARAM                                    
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1WQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023892.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27554                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNX 2002                                              
REMARK 200 STARTING MODEL: PDB ENTRY 1DAN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, SODIUM CHLORIDE, CACODYLATE,   
REMARK 280  CALCIUM CHLORIDE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       35.69500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.75500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.75500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.69500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.21000            
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: 7900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T                               
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     LYS L   143                                                      
REMARK 465     ARG L   144                                                      
REMARK 465     ASN L   145                                                      
REMARK 465     ALA L   146                                                      
REMARK 465     SER L   147                                                      
REMARK 465     LYS L   148                                                      
REMARK 465     PRO L   149                                                      
REMARK 465     GLN L   150                                                      
REMARK 465     GLY L   151                                                      
REMARK 465     ARG L   152                                                      
REMARK 465     SER T     1                                                      
REMARK 465     GLY T     2                                                      
REMARK 465     THR T     3                                                      
REMARK 465     THR T     4                                                      
REMARK 465     ASN T     5                                                      
REMARK 465     ALA T    80                                                      
REMARK 465     GLY T    81                                                      
REMARK 465     ASN T    82                                                      
REMARK 465     VAL T    83                                                      
REMARK 465     GLU T    84                                                      
REMARK 465     SER T    85                                                      
REMARK 465     THR T    86                                                      
REMARK 465     GLY T    87                                                      
REMARK 465     SER T    88                                                      
REMARK 465     ALA T    89                                                      
REMARK 465     GLY T    90                                                      
REMARK 465     SER T   161                                                      
REMARK 465     SER T   162                                                      
REMARK 465     SER T   163                                                      
REMARK 465     GLY T   211                                                      
REMARK 465     GLN T   212                                                      
REMARK 465     GLU T   213                                                      
REMARK 465     LYS T   214                                                      
REMARK 465     GLY T   215                                                      
REMARK 465     GLU T   216                                                      
REMARK 465     PHE T   217                                                      
REMARK 465     ARG T   218                                                      
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    LEU L   5       -8.29     72.33                                   
REMARK 500    LYS L  32      -76.46     70.24                                   
REMARK 500    SER L  67     -176.72    176.18                                   
REMARK 500    ALA L  75       23.05    -79.78                                   
REMARK 500    GLN L 100      -86.54   -124.57                                   
REMARK 500    THR L 108     -175.59    -65.61                                   
REMARK 500    ILE L 140        4.66    -68.95                                   
REMARK 500    HIS H  71      -61.68   -162.90                                   
REMARK 500    THR H 129C     -65.96   -124.15                                   
REMARK 500    ARG H 147       -6.69     76.12                                   
REMARK 500    PHE H 181      141.59   -173.90                                   
REMARK 500    SER H 214      -65.15   -121.33                                   
REMARK 500    PHE T  19       -1.31     82.16                                   
REMARK 500    PRO T  29      132.17    -34.59                                   
REMARK 500    THR T  55       40.93   -108.83                                   
REMARK 500    ASP T  66       95.84   -167.70                                   
REMARK 500    SER T 115     -175.63    171.92                                   
REMARK 500    PHE T 116      120.39   -171.69                                   
REMARK 500    THR T 172     -151.57   -128.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H1080        DISTANCE =  5.19 ANGSTROMS                       
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                              CA H 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  75   O                                                      
REMARK 620 2 GLU H  70   OE2 166.1                                              
REMARK 620 3 GLU H  70   OE1 147.5  45.7                                        
REMARK 620 4 HOH H1095   O    92.5  76.5 119.0                                  
REMARK 620 5 ASP H  72   O    73.9 114.2  96.1  90.7                            
REMARK 620 6 HOH H1108   O    76.5 114.8  71.6 168.7  83.9                      
REMARK 620 7 GLU H  80   OE1  85.0  86.2 102.8  88.3 158.8  93.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH L1109   O                                                      
REMARK 620 2 ASP L  63   OD2  76.1                                              
REMARK 620 3 ASP L  63   OD1 121.0  46.5                                        
REMARK 620 4 GLN L  64   O   102.5  99.2  78.6                                  
REMARK 620 5 GLN L  49   OE1 160.2 123.4  77.7  73.2                            
REMARK 620 6 ASP L  46   OD2  95.3 169.1 143.3  89.0  65.7                      
REMARK 620 7 GLY L  47   O   104.0  97.3  96.5 151.4  78.2  78.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  26  OE12                                                    
REMARK 620 2 CGU L  29  OE22  93.2                                              
REMARK 620 3 CGU L  29  OE21 102.7  47.3                                        
REMARK 620 4 CGU L   7  OE22  81.4 144.1 168.3                                  
REMARK 620 5 CGU L   7  OE12  96.0  80.3 124.5  65.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE12                                                    
REMARK 620 2 CGU L   7  OE11  44.4                                              
REMARK 620 3 CGU L  26  OE11  83.2  67.1                                        
REMARK 620 4 HOH L1083   O    83.1 119.8 146.3                                  
REMARK 620 5 CGU L  29  OE22  78.8 112.5  74.4  72.8                            
REMARK 620 6 CGU L  16  OE21 119.5  76.2  83.1 130.2 149.3                      
REMARK 620 7 HOH L1082   O    86.0  78.5 140.1  69.0 140.2  69.3                
REMARK 620 8 HOH L1066   O   167.8 145.1  94.8  92.1  89.1  72.0 102.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE11                                                    
REMARK 620 2 CGU L  26  OE22 134.1                                              
REMARK 620 3 CGU L  26  OE11  70.0  70.8                                        
REMARK 620 4 ASN L   2   OD1  58.6  88.9  74.9                                  
REMARK 620 5 CGU L  16  OE21  87.0 109.9  81.8 143.2                            
REMARK 620 6 CGU L   6  OE11  75.2 143.4 144.5  92.9  89.8                      
REMARK 620 7 CGU L  16  OE11 138.8  84.7 126.8 152.9  62.9  77.2                
REMARK 620 8 ALA L   1   O   128.6  67.7 132.0  81.2 134.8  76.5  72.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  20  OE22                                                    
REMARK 620 2 CGU L  20  OE21  46.2                                              
REMARK 620 3 CGU L  16  OE12  90.4  79.9                                        
REMARK 620 4 CGU L   6  OE22 137.4  91.8  72.9                                  
REMARK 620 5 CGU L   6  OE11 143.8 154.2  76.8  71.0                            
REMARK 620 6 CGU L  16  OE11  71.8  95.1  44.2 113.7  75.6                      
REMARK 620 7 ALA L   1   O    75.5 120.8 114.3 147.1  79.4  70.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  19  OE21                                                    
REMARK 620 2 CGU L  19  OE12  69.8                                              
REMARK 620 3 CGU L  14  OE12  68.0 137.3                                        
REMARK 620 4 CGU L  14  OE21  71.6  92.7  80.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 508  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  20  OE21                                                    
REMARK 620 2 CGU L  20  OE11  70.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 509  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  25  OE22                                                    
REMARK 620 2 CGU L  25  OE11  83.5                                              
REMARK 620 3 CGU L  29  OE21  75.9  84.3                                        
REMARK 620 N                    1     2                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-[DIHYDROXY(PROPYL)-LAMBDA~4~-SULFANYL]THREONYL-N~   
REMARK 630 1~-{4-[AMINO(IMINO)METHYL]BENZYL}METHIONINAMIDE                      
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     PSM H  1001                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    0TH MET 00S                                              
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC L 1052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC L 1060                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSM H 1001                
DBREF  1WQV L    1   152  UNP    P08709   FA7_HUMAN       61    212             
DBREF  1WQV H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  1WQV T    1   218  UNP    P13726   TF_HUMAN        33    250             
SEQRES   1 L  152  ALA ASN ALA PHE LEU CGU CGU LEU ARG PRO GLY SER LEU          
SEQRES   2 L  152  CGU ARG CGU CYS LYS CGU CGU GLN CYS SER PHE CGU CGU          
SEQRES   3 L  152  ALA ARG CGU ILE PHE LYS ASP ALA CGU ARG THR LYS LEU          
SEQRES   4 L  152  PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER          
SEQRES   5 L  152  SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU          
SEQRES   6 L  152  GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY          
SEQRES   7 L  152  ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS          
SEQRES   8 L  152  VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP          
SEQRES   9 L  152  HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY          
SEQRES  10 L  152  TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR          
SEQRES  11 L  152  VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU LYS          
SEQRES  12 L  152  ARG ASN ALA SER LYS PRO GLN GLY ARG                          
SEQRES   1 H  254  ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO          
SEQRES   2 H  254  TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS          
SEQRES   3 H  254  GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA          
SEQRES   4 H  254  ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU          
SEQRES   5 H  254  ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP          
SEQRES   6 H  254  GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE          
SEQRES   7 H  254  PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE          
SEQRES   8 H  254  ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP          
SEQRES   9 H  254  HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER          
SEQRES  10 H  254  GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER          
SEQRES  11 H  254  GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU          
SEQRES  12 H  254  GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN          
SEQRES  13 H  254  ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO          
SEQRES  14 H  254  ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP          
SEQRES  15 H  254  GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO          
SEQRES  16 H  254  HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY          
SEQRES  17 H  254  ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS          
SEQRES  18 H  254  PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP          
SEQRES  19 H  254  LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL          
SEQRES  20 H  254  LEU LEU ARG ALA PRO PHE PRO                                  
SEQRES   1 T  218  SER GLY THR THR ASN THR VAL ALA ALA TYR ASN LEU THR          
SEQRES   2 T  218  TRP LYS SER THR ASN PHE LYS THR ILE LEU GLU TRP GLU          
SEQRES   3 T  218  PRO LYS PRO VAL ASN GLN VAL TYR THR VAL GLN ILE SER          
SEQRES   4 T  218  THR LYS SER GLY ASP TRP LYS SER LYS CYS PHE TYR THR          
SEQRES   5 T  218  THR ASP THR GLU CYS ASP LEU THR ASP GLU ILE VAL LYS          
SEQRES   6 T  218  ASP VAL LYS GLN THR TYR LEU ALA ARG VAL PHE SER TYR          
SEQRES   7 T  218  PRO ALA GLY ASN VAL GLU SER THR GLY SER ALA GLY GLU          
SEQRES   8 T  218  PRO LEU TYR GLU ASN SER PRO GLU PHE THR PRO TYR LEU          
SEQRES   9 T  218  GLU THR ASN LEU GLY GLN PRO THR ILE GLN SER PHE GLU          
SEQRES  10 T  218  GLN VAL GLY THR LYS VAL ASN VAL THR VAL GLU ASP GLU          
SEQRES  11 T  218  ARG THR LEU VAL ARG ARG ASN ASN THR PHE LEU SER LEU          
SEQRES  12 T  218  ARG ASP VAL PHE GLY LYS ASP LEU ILE TYR THR LEU TYR          
SEQRES  13 T  218  TYR TRP LYS SER SER SER SER GLY LYS LYS THR ALA LYS          
SEQRES  14 T  218  THR ASN THR ASN GLU PHE LEU ILE ASP VAL ASP LYS GLY          
SEQRES  15 T  218  GLU ASN TYR CYS PHE SER VAL GLN ALA VAL ILE PRO SER          
SEQRES  16 T  218  ARG THR VAL ASN ARG LYS SER THR ASP SER PRO VAL GLU          
SEQRES  17 T  218  CYS MET GLY GLN GLU LYS GLY GLU PHE ARG                      
MODRES 1WQV SER L   52  SER  GLYCOSYLATION SITE                                 
MODRES 1WQV SER L   60  SER  GLYCOSYLATION SITE                                 
MODRES 1WQV CGU L    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WQV CGU L   35  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
HET    CGU  L   6      12                                                       
HET    CGU  L   7      12                                                       
HET    CGU  L  14      12                                                       
HET    CGU  L  16      12                                                       
HET    CGU  L  19      12                                                       
HET    CGU  L  20      12                                                       
HET    CGU  L  25      12                                                       
HET    CGU  L  26      12                                                       
HET    CGU  L  29      12                                                       
HET    CGU  L  35      12                                                       
HET    BGC  L1052      11                                                       
HET    FUC  L1060      10                                                       
HET     CA  H 501       1                                                       
HET     CA  L 502       1                                                       
HET     CA  L 503       1                                                       
HET     CA  L 504       1                                                       
HET     CA  L 505       1                                                       
HET     CA  L 506       1                                                       
HET     CA  L 507       1                                                       
HET     CA  L 508       1                                                       
HET     CA  L 509       1                                                       
HET    PSM  H1001      32                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     PSM N-[DIHYDROXY(PROPYL)-LAMBDA~4~-SULFANYL]THREONYL-N~1~-           
HETNAM   2 PSM  {4-[AMINO(IMINO)METHYL]BENZYL}METHIONINAMIDE                    
HETSYN     PSM N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-                        
HETSYN   2 PSM  METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-                
HETSYN   3 PSM  BUTYRAMID                                                       
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   4  BGC    C6 H12 O6                                                    
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   6   CA    9(CA 2+)                                                     
FORMUL  15  PSM    C20 H33 N5 O5 S2                                             
FORMUL  16  HOH   *328(H2 O)                                                    
HELIX    1   1 LEU L    5  ARG L    9  5                                   5    
HELIX    2   2 SER L   12  LYS L   18  1                                   7    
HELIX    3   3 SER L   23  LYS L   32  1                                  10    
HELIX    4   4 ASP L   33  SER L   45  1                                  13    
HELIX    5   5 ASP L   48  SER L   53  5                                   6    
HELIX    6   6 ASP L   86  GLN L   88  5                                   3    
HELIX    7   7 ASN L   93  CYS L   98  5                                   6    
HELIX    8   8 ILE L  138  GLU L  142  5                                   5    
HELIX    9   9 ALA H   55  ASP H   60  5                                   6    
HELIX   10  10 ASN H   60D ARG H   62  5                                   3    
HELIX   11  11 GLU H  125  THR H  129C 1                                   8    
HELIX   12  12 LEU H  129D VAL H  129G 5                                   4    
HELIX   13  13 MET H  164  SER H  170B 1                                   9    
HELIX   14  14 CYS H  191  SER H  195  5                                   5    
HELIX   15  15 TYR H  234  ARG H  243  1                                  10    
HELIX   16  16 LEU T   59  VAL T   64  1                                   6    
HELIX   17  17 THR T  101  THR T  106  1                                   6    
HELIX   18  18 LEU T  143  GLY T  148  1                                   6    
HELIX   19  19 LYS T  149  LEU T  151  5                                   3    
SHEET    1   A 2 SER L  60  GLN L  64  0                                        
SHEET    2   A 2 SER L  67  PHE L  71 -1  O  PHE L  71   N  SER L  60           
SHEET    1   B 2 PHE L  76  GLU L  77  0                                        
SHEET    2   B 2 THR L  83  HIS L  84 -1  O  THR L  83   N  GLU L  77           
SHEET    1   C 2 TYR L 101  SER L 103  0                                        
SHEET    2   C 2 SER L 111  ARG L 113 -1  O  SER L 111   N  SER L 103           
SHEET    1   D 2 TYR L 118  LEU L 120  0                                        
SHEET    2   D 2 CYS L 127  PRO L 129 -1  O  THR L 128   N  SER L 119           
SHEET    1   E 8 LYS H  20  VAL H  21  0                                        
SHEET    2   E 8 MET H 156  LEU H 163 -1  O  VAL H 157   N  LYS H  20           
SHEET    3   E 8 MET H 180  ALA H 183 -1  O  CYS H 182   N  LEU H 163           
SHEET    4   E 8 GLY H 226  ARG H 230 -1  O  TYR H 228   N  PHE H 181           
SHEET    5   E 8 THR H 206  GLY H 216 -1  N  TRP H 215   O  VAL H 227           
SHEET    6   E 8 PRO H 198  TYR H 203 -1  N  TYR H 203   O  THR H 206           
SHEET    7   E 8 PHE H 135  GLY H 140 -1  N  LEU H 137   O  ALA H 200           
SHEET    8   E 8 MET H 156  LEU H 163 -1  O  VAL H 160   N  SER H 136           
SHEET    1   F 8 LEU H 251  ALA H 254  0                                        
SHEET    2   F 8 GLN H  81  PRO H  91  1  N  ILE H  90   O  LEU H 252           
SHEET    3   F 8 ALA H 104  LEU H 108 -1  O  LEU H 105   N  ILE H  89           
SHEET    4   F 8 TRP H  51  SER H  54 -1  N  VAL H  52   O  LEU H 106           
SHEET    5   F 8 ALA H  39  LEU H  46 -1  N  THR H  45   O  VAL H  53           
SHEET    6   F 8 GLN H  30  VAL H  35 -1  N  LEU H  33   O  CYS H  42           
SHEET    7   F 8 LEU H  64  LEU H  68 -1  O  ILE H  65   N  LEU H  34           
SHEET    8   F 8 GLN H  81  PRO H  91 -1  O  GLN H  81   N  LEU H  68           
SHEET    1   G 3 TYR T  10  THR T  17  0                                        
SHEET    2   G 3 LYS T  20  GLU T  26 -1  O  ILE T  22   N  LYS T  15           
SHEET    3   G 3 GLU T  56  ASP T  58 -1  O  CYS T  57   N  LEU T  23           
SHEET    1   H 4 LYS T  46  THR T  52  0                                        
SHEET    2   H 4 VAL T  33  THR T  40 -1  N  VAL T  36   O  LYS T  48           
SHEET    3   H 4 TYR T  71  TYR T  78 -1  O  PHE T  76   N  THR T  35           
SHEET    4   H 4 LEU T  93  ASN T  96 -1  O  LEU T  93   N  SER T  77           
SHEET    1   I 3 ILE T 113  GLN T 118  0                                        
SHEET    2   I 3 LYS T 122  VAL T 127 -1  O  THR T 126   N  SER T 115           
SHEET    3   I 3 GLU T 174  ASP T 178 -1  O  PHE T 175   N  VAL T 125           
SHEET    1   J 2 ARG T 131  ARG T 135  0                                        
SHEET    2   J 2 PHE T 140  SER T 142 -1  O  LEU T 141   N  THR T 132           
SHEET    1   K 4 LYS T 166  THR T 170  0                                        
SHEET    2   K 4 ILE T 152  LYS T 159 -1  N  LEU T 155   O  ALA T 168           
SHEET    3   K 4 TYR T 185  VAL T 192 -1  O  VAL T 192   N  ILE T 152           
SHEET    4   K 4 GLU T 208  CYS T 209 -1  O  GLU T 208   N  PHE T 187           
SSBOND   1 CYS L   17    CYS L   22                          1555   1555  2.03  
SSBOND   2 CYS L   50    CYS L   61                          1555   1555  2.03  
SSBOND   3 CYS L   55    CYS L   70                          1555   1555  2.03  
SSBOND   4 CYS L   72    CYS L   81                          1555   1555  2.03  
SSBOND   5 CYS L   91    CYS L  102                          1555   1555  2.03  
SSBOND   6 CYS L   98    CYS L  112                          1555   1555  2.03  
SSBOND   7 CYS L  114    CYS L  127                          1555   1555  2.03  
SSBOND   8 CYS L  135    CYS H  122                          1555   1555  2.03  
SSBOND   9 CYS H   22    CYS H   27                          1555   1555  2.03  
SSBOND  10 CYS H   42    CYS H   58                          1555   1555  2.03  
SSBOND  11 CYS H  168    CYS H  182                          1555   1555  2.03  
SSBOND  12 CYS H  191    CYS H  220                          1555   1555  2.04  
SSBOND  13 CYS T   49    CYS T   57                          1555   1555  2.64  
SSBOND  14 CYS T  186    CYS T  209                          1555   1555  2.77  
LINK         OG  SER L  52                 C1  BGC L1052     1555   1555  1.44  
LINK         OG  SER L  60                 C1  FUC L1060     1555   1555  1.43  
LINK        CA    CA H 501                 O   GLU H  75     1555   1555  2.67  
LINK        CA    CA H 501                 OE2 GLU H  70     1555   1555  2.90  
LINK        CA    CA H 501                 OE1 GLU H  70     1555   1555  2.73  
LINK        CA    CA H 501                 O   HOH H1095     1555   1555  2.83  
LINK        CA    CA H 501                 O   ASP H  72     1555   1555  2.64  
LINK        CA    CA H 501                 O   HOH H1108     1555   1555  2.82  
LINK        CA    CA H 501                 OE1 GLU H  80     1555   1555  2.68  
LINK         C   LEU L   5                 N   CGU L   6     1555   1555  1.33  
LINK         C   CGU L   6                 N   CGU L   7     1555   1555  1.33  
LINK         C   CGU L   7                 N   LEU L   8     1555   1555  1.33  
LINK         C   LEU L  13                 N   CGU L  14     1555   1555  1.33  
LINK         C   CGU L  14                 N   ARG L  15     1555   1555  1.32  
LINK         C   ARG L  15                 N   CGU L  16     1555   1555  1.33  
LINK         C   CGU L  16                 N   CYS L  17     1555   1555  1.33  
LINK         C   LYS L  18                 N   CGU L  19     1555   1555  1.33  
LINK         C   CGU L  19                 N   CGU L  20     1555   1555  1.33  
LINK         C   CGU L  20                 N   GLN L  21     1555   1555  1.33  
LINK         C   PHE L  24                 N   CGU L  25     1555   1555  1.33  
LINK         C   CGU L  25                 N   CGU L  26     1555   1555  1.33  
LINK         C   CGU L  26                 N   ALA L  27     1555   1555  1.33  
LINK         C   ARG L  28                 N   CGU L  29     1555   1555  1.33  
LINK         C   CGU L  29                 N   ILE L  30     1555   1555  1.33  
LINK         C   ALA L  34                 N   CGU L  35     1555   1555  1.33  
LINK         C   CGU L  35                 N   ARG L  36     1555   1555  1.33  
LINK        CA    CA L 502                 O   HOH L1109     1555   1555  3.00  
LINK        CA    CA L 502                 OD2 ASP L  63     1555   1555  2.74  
LINK        CA    CA L 502                 OD1 ASP L  63     1555   1555  2.85  
LINK        CA    CA L 502                 O   GLN L  64     1555   1555  2.63  
LINK        CA    CA L 502                 OE1 GLN L  49     1555   1555  2.70  
LINK        CA    CA L 502                 OD2 ASP L  46     1555   1555  2.60  
LINK        CA    CA L 502                 O   GLY L  47     1555   1555  2.58  
LINK        CA    CA L 503                OE12 CGU L  26     1555   1555  3.07  
LINK        CA    CA L 503                OE22 CGU L  29     1555   1555  2.77  
LINK        CA    CA L 503                OE21 CGU L  29     1555   1555  2.72  
LINK        CA    CA L 503                OE22 CGU L   7     1555   1555  2.74  
LINK        CA    CA L 503                OE12 CGU L   7     1555   1555  2.67  
LINK        CA    CA L 504                OE12 CGU L   7     1555   1555  2.81  
LINK        CA    CA L 504                OE11 CGU L   7     1555   1555  2.97  
LINK        CA    CA L 504                OE11 CGU L  26     1555   1555  2.66  
LINK        CA    CA L 504                 O   HOH L1083     1555   1555  2.90  
LINK        CA    CA L 504                OE22 CGU L  29     1555   1555  2.72  
LINK        CA    CA L 504                OE21 CGU L  16     1555   1555  2.95  
LINK        CA    CA L 504                 O   HOH L1082     1555   1555  2.73  
LINK        CA    CA L 504                 O   HOH L1066     1555   1555  2.85  
LINK        CA    CA L 505                OE11 CGU L   7     1555   1555  2.51  
LINK        CA    CA L 505                OE22 CGU L  26     1555   1555  2.59  
LINK        CA    CA L 505                OE11 CGU L  26     1555   1555  2.90  
LINK        CA    CA L 505                 OD1 ASN L   2     1555   1555  2.84  
LINK        CA    CA L 505                OE21 CGU L  16     1555   1555  2.79  
LINK        CA    CA L 505                OE11 CGU L   6     1555   1555  2.79  
LINK        CA    CA L 505                OE11 CGU L  16     1555   1555  2.58  
LINK        CA    CA L 505                 O   ALA L   1     1555   1555  2.79  
LINK        CA    CA L 506                OE22 CGU L  20     1555   1555  2.85  
LINK        CA    CA L 506                OE21 CGU L  20     1555   1555  2.75  
LINK        CA    CA L 506                OE12 CGU L  16     1555   1555  3.03  
LINK        CA    CA L 506                OE22 CGU L   6     1555   1555  2.64  
LINK        CA    CA L 506                OE11 CGU L   6     1555   1555  2.71  
LINK        CA    CA L 506                OE11 CGU L  16     1555   1555  2.76  
LINK        CA    CA L 506                 O   ALA L   1     1555   1555  2.70  
LINK        CA    CA L 507                OE21 CGU L  19     1555   1555  3.03  
LINK        CA    CA L 507                OE12 CGU L  19     1555   1555  2.70  
LINK        CA    CA L 507                OE12 CGU L  14     1555   1555  2.82  
LINK        CA    CA L 507                OE21 CGU L  14     1555   1555  2.86  
LINK        CA    CA L 508                OE21 CGU L  20     1555   1555  2.71  
LINK        CA    CA L 508                OE11 CGU L  20     1555   1555  2.94  
LINK        CA    CA L 509                OE22 CGU L  25     1555   1555  3.05  
LINK        CA    CA L 509                OE11 CGU L  25     1555   1555  2.91  
LINK        CA    CA L 509                OE21 CGU L  29     1555   1555  2.85  
CISPEP   1 PHE H  256    PRO H  257          0         0.09                     
CISPEP   2 GLU T   26    PRO T   27          0        -0.16                     
SITE     1 AC1  3 GLN L  49  SER L  52  TYR L  68                               
SITE     1 AC2  4 SER L  60  PHE L  71  CYS L  72  ARG T 131                    
SITE     1 AC3  6 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     2 AC3  6 HOH H1095  HOH H1108                                          
SITE     1 AC4  6 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 AC4  6 GLN L  64  HOH L1109                                          
SITE     1 AC5  3 CGU L   7  CGU L  26  CGU L  29                               
SITE     1 AC6  7 CGU L   7  CGU L  16  CGU L  26  CGU L  29                    
SITE     2 AC6  7 HOH L1066  HOH L1082  HOH L1083                               
SITE     1 AC7  6 ALA L   1  ASN L   2  CGU L   6  CGU L   7                    
SITE     2 AC7  6 CGU L  16  CGU L  26                                          
SITE     1 AC8  4 ALA L   1  CGU L   6  CGU L  16  CGU L  20                    
SITE     1 AC9  2 CGU L  14  CGU L  19                                          
SITE     1 BC1  1 CGU L  20                                                     
SITE     1 BC2  3 CGU L  25  ARG L  28  CGU L  29                               
SITE     1 BC3 16 HIS H  57  THR H  98  THR H  99  ASP H 102                    
SITE     2 BC3 16 ASP H 189  SER H 190  CYS H 191  SER H 195                    
SITE     3 BC3 16 VAL H 213  SER H 214  TRP H 215  GLY H 216                    
SITE     4 BC3 16 GLY H 219  GLY H 226  HOH H1054  HOH H1175                    
CRYST1   71.390   82.420  123.510  90.00  90.00  90.00 P 21 21 21    4          
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      0.014008  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008097        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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