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Database: PDB
Entry: 1WSS
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HEADER    HYDROLASE/BLOOD CLOTTING                10-NOV-04   1WSS              
TITLE     HUMAN FACTOR VIIA-TISSUE FACTOR IN COMPLEX WITH PEPTIDE-MIMETIC       
TITLE    2 INHIBITOR THAT HAS TWO CHARGED GROUPS IN P2 AND P4                   
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-BLOOD CLOTTING 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,Y.ONO,T.ESAKI,H.SATO,Y.WATANABE,     
AUTHOR   3 S.ITOH,M.OHTA,T.KOZONO                                               
REVDAT   4   23-JUL-14 1WSS    1       TITLE  VERSN                             
REVDAT   3   24-FEB-09 1WSS    1       VERSN                                    
REVDAT   2   04-APR-06 1WSS    1       JRNL                                     
REVDAT   1   10-NOV-05 1WSS    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,Y.ONO,T.ESAKI,     
JRNL        AUTH 3 H.SATO,Y.WATANABE,S.ITOH,M.OHTA,T.KOZONO                     
JRNL        TITL   STRUCTURE OF HUMAN FACTOR VIIA/TISSUE FACTOR IN COMPLEX WITH 
JRNL        TITL 2 A PEPTIDE-MIMETIC INHIBITOR: HIGH SELECTIVITY AGAINST        
JRNL        TITL 3 THROMBIN BY INTRODUCING TWO CHARGED GROUPS IN P2 AND P4.     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  61   169 2005              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   16510984                                                     
JRNL        DOI    10.1107/S1744309105000047                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1732189.920                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 23023                          
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                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1588                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2095                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 162                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
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          : 71                                      
REMARK   3   SOLVENT ATOMS            : 319                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.66000                                              
REMARK   3    B22 (A**2) : 0.67000                                              
REMARK   3    B33 (A**2) : -3.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.09                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.500                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.780                           
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) : 1.400 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.360 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.960 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.910 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : BABINET                                              
REMARK   3   KSOL        : 0.80                                                 
REMARK   3   BSOL        : 280.00                                               
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : 180.X.PARAM                                    
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
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: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1WSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023957.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL40B2                             
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25939                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1DAN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, SODIUM CHLORIDE, CACODYLATE,   
REMARK 280  CALCIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, 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       35.78000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.76000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.76000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.78000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.15000            
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: 8030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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       -9.12     72.43                                   
REMARK 500    LYS L  32      -65.24     69.35                                   
REMARK 500    SER L  67      174.27    178.73                                   
REMARK 500    LEU L  89       49.47    -77.06                                   
REMARK 500    GLN L 100      -95.08   -123.45                                   
REMARK 500    THR L 108     -177.31    -65.44                                   
REMARK 500    LEU H  41      -51.41   -129.21                                   
REMARK 500    HIS H  71      -67.51   -156.45                                   
REMARK 500    THR H  98     -169.32   -103.67                                   
REMARK 500    THR H 129C     -68.17   -122.71                                   
REMARK 500    ASP H 189      167.90    179.25                                   
REMARK 500    SER H 195      137.56    -39.21                                   
REMARK 500    SER H 214      -62.71   -124.12                                   
REMARK 500    PHE T  19       -4.52     78.23                                   
REMARK 500    PRO T  29      128.91    -39.65                                   
REMARK 500    TYR T  51       41.29     39.20                                   
REMARK 500    ASP T  66       89.52   -170.97                                   
REMARK 500    SER T 115      176.96    174.27                                   
REMARK 500    ARG T 136      117.04   -167.16                                   
REMARK 500    THR T 172     -152.57   -120.00                                   
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 H2186        DISTANCE =  5.28 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     3CB H  2001                                                      
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 H1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  75   O                                                      
REMARK 620 2 GLU H  70   OE1 144.9                                              
REMARK 620 3 HOH H2094   O    99.7 114.3                                        
REMARK 620 4 ASP H  72   O    77.7  91.3  93.2                                  
REMARK 620 5 GLU H  70   OE2 170.9  44.2  71.4 104.5                            
REMARK 620 6 GLU H  80   OE2 111.4  88.9  70.6 162.2  64.1                      
REMARK 620 7 GLU H  80   OE1  80.7 101.2  99.4 156.6  98.2  39.4                
REMARK 620 8 HOH H2105   O    71.6  73.5 168.0  77.1 117.5 119.8  87.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L  63   OD1                                                    
REMARK 620 2 ASP L  63   OD2  45.9                                              
REMARK 620 3 GLN L  64   O    81.1  93.4                                        
REMARK 620 4 ASP L  46   OD2 153.4 154.5  80.7                                  
REMARK 620 5 GLY L  47   O    96.5 115.4 137.3  84.1                            
REMARK 620 6 HOH L1113   O   110.0  64.1 103.9  93.1 116.6                      
REMARK 620 7 GLN L  49   OE1  81.9 127.7  72.0  74.2  65.5 167.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  26  OE12                                                    
REMARK 620 2 CGU L   7  OE22  86.1                                              
REMARK 620 3 CGU L  29  OE21  98.1 174.5                                        
REMARK 620 4 CGU L   7  OE12  97.8  61.2 121.4                                  
REMARK 620 5 CGU L  29  OE22  94.5 139.3  44.2  78.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE11                                                    
REMARK 620 2 HOH L1084   O   124.7                                              
REMARK 620 3 CGU L   7  OE12  43.7  88.6                                        
REMARK 620 4 CGU L  29  OE22 115.3  65.0  78.7                                  
REMARK 620 5 CGU L  26  OE11  70.5 141.0  82.2  76.0                            
REMARK 620 6 HOH L1083   O    74.1  81.4  90.0 144.5 136.0                      
REMARK 620 7 HOH L1067   O   145.6  88.0 164.9  86.6  91.3 104.0                
REMARK 620 8 CGU L  16  OE21  81.3 140.2 124.6 135.8  71.8  77.9  65.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE11                                                    
REMARK 620 2 CGU L  26  OE22 135.5                                              
REMARK 620 3 ASN L   2   OD1  61.8  92.4                                        
REMARK 620 4 CGU L  26  OE11  71.2  67.9  77.8                                  
REMARK 620 5 CGU L   6  OE11  70.9 149.5  89.3 141.7                            
REMARK 620 6 CGU L  16  OE11 133.8  84.5 155.6 122.6  81.5                      
REMARK 620 7 ALA L   1   O   132.0  71.0  81.6 132.7  79.2  74.5                
REMARK 620 8 CGU L  16  OE21  87.9  95.4 142.7  71.7 101.5  61.7 135.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH L1106   O                                                      
REMARK 620 2 CGU L  16  OE12 165.7                                              
REMARK 620 3 CGU L   6  OE22 106.4  60.8                                        
REMARK 620 4 CGU L   6  OE11 104.7  78.8  73.8                                  
REMARK 620 5 CGU L  20  OE22  79.9 104.5 135.6 148.6                            
REMARK 620 6 CGU L  20  OE21  94.6  80.0  91.6 158.3  44.1                      
REMARK 620 7 CGU L  16  OE11 150.7  42.7 102.8  82.5  80.0  85.4                
REMARK 620 8 ALA L   1   O    78.7 115.6 156.5  82.7  67.5 111.1  74.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  19  OE21                                                    
REMARK 620 2 CGU L  19  OE12  84.1                                              
REMARK 620 3 CGU L  14  OE21  85.8  97.1                                        
REMARK 620 4 CGU L  14  OE12  83.1 165.8  75.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  20  OE11                                                    
REMARK 620 2 CGU L  20  OE21  77.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1009  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  25  OE11                                                    
REMARK 620 2 CGU L  29  OE21  84.1                                              
REMARK 620 3 CGU L  25  OE22  81.3  82.5                                        
REMARK 620 4 CGU L  29  OE11 157.4  74.1  89.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 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 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1009                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3CB H 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WQV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER INHIBITOR.                   
REMARK 900 RELATED ID: 1DAN   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH IRREVERSIBLE INHIBITOR.              
DBREF  1WSS L    1   152  UNP    P08709   FA7_HUMAN       61    212             
DBREF  1WSS H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  1WSS 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 1WSS SER L   52  SER  GLYCOSYLATION SITE                                 
MODRES 1WSS SER L   60  SER  GLYCOSYLATION SITE                                 
MODRES 1WSS CGU L    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS CGU L   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WSS 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  H1001       1                                                       
HET     CA  L1002       1                                                       
HET     CA  L1003       1                                                       
HET     CA  L1004       1                                                       
HET     CA  L1005       1                                                       
HET     CA  L1006       1                                                       
HET     CA  L1007       1                                                       
HET     CA  L1008       1                                                       
HET     CA  L1009       1                                                       
HET    3CB  H2001      41                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     3CB N-[(3-CARBOXYBENZYL)SULFONYL]ISOLEUCYL-N~1~-{4-                  
HETNAM   2 3CB  [AMINO(IMINO)METHYL]BENZYL}-5-IMINOORNITHINAMIDE                
HETSYN     3CB 3-({1-[3-CARBAMIMIDOYL-1-(4-CARBAMIMIDOYL-                       
HETSYN   2 3CB  BENZYLCARBAMOYL)-PROPYLCARBAMOYL]-2-METHYL-                     
HETSYN   3 3CB  BUTYLSULFAMOYL}-METHYL)-BENZOIC ACID                            
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  3CB    C27 H37 N7 O6 S                                              
FORMUL  16  HOH   *319(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 ASN L   93  CYS L   98  5                                   6    
HELIX    6   6 ILE L  138  GLU L  142  5                                   5    
HELIX    7   7 ALA H   56  ASP H   60  5                                   5    
HELIX    8   8 GLU H  125  THR H  129C 1                                   8    
HELIX    9   9 LEU H  129D VAL H  129G 5                                   4    
HELIX   10  10 MET H  164  SER H  170B 1                                   9    
HELIX   11  11 CYS H  191  SER H  195  5                                   5    
HELIX   12  12 TYR H  234  ARG H  243  1                                  10    
HELIX   13  13 LEU T   59  VAL T   64  1                                   6    
HELIX   14  14 THR T  101  THR T  106  1                                   6    
HELIX   15  15 LEU T  143  GLY T  148  1                                   6    
HELIX   16  16 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  ARG L 113   N  TYR L 101           
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  TRP H 215 -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  LEU H 158   N  VAL H 138           
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  VAL H  85   N  LEU H  64           
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  VAL T 119  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  ILE T 177   N  VAL T 123           
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  2.04  
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  2.04  
SSBOND  12 CYS H  191    CYS H  220                          1555   1555  2.03  
SSBOND  13 CYS T   49    CYS T   57                          1555   1555  2.62  
SSBOND  14 CYS T  186    CYS T  209                          1555   1555  2.70  
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 H1001                 O   GLU H  75     1555   1555  2.65  
LINK        CA    CA H1001                 OE1 GLU H  70     1555   1555  2.72  
LINK        CA    CA H1001                 O   HOH H2094     1555   1555  2.93  
LINK        CA    CA H1001                 O   ASP H  72     1555   1555  2.71  
LINK        CA    CA H1001                 OE2 GLU H  70     1555   1555  2.97  
LINK        CA    CA H1001                 OE2 GLU H  80     1555   1555  2.94  
LINK        CA    CA H1001                 OE1 GLU H  80     1555   1555  3.31  
LINK        CA    CA H1001                 O   HOH H2105     1555   1555  2.78  
LINK         C   LEU L   5                 N   CGU L   6     1555   1555  1.32  
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  1.33  
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  1.32  
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 L1002                 OD1 ASP L  63     1555   1555  2.80  
LINK        CA    CA L1002                 OD2 ASP L  63     1555   1555  2.73  
LINK        CA    CA L1002                 O   GLN L  64     1555   1555  2.63  
LINK        CA    CA L1002                 OD2 ASP L  46     1555   1555  2.68  
LINK        CA    CA L1002                 O   GLY L  47     1555   1555  2.79  
LINK        CA    CA L1002                 O   HOH L1113     1555   1555  3.10  
LINK        CA    CA L1002                 OE1 GLN L  49     1555   1555  2.63  
LINK        CA    CA L1003                OE12 CGU L  26     1555   1555  2.99  
LINK        CA    CA L1003                OE22 CGU L   7     1555   1555  2.78  
LINK        CA    CA L1003                OE21 CGU L  29     1555   1555  2.70  
LINK        CA    CA L1003                OE12 CGU L   7     1555   1555  2.68  
LINK        CA    CA L1003                OE22 CGU L  29     1555   1555  2.92  
LINK        CA    CA L1004                OE11 CGU L   7     1555   1555  2.86  
LINK        CA    CA L1004                 O   HOH L1084     1555   1555  2.83  
LINK        CA    CA L1004                OE12 CGU L   7     1555   1555  2.90  
LINK        CA    CA L1004                OE22 CGU L  29     1555   1555  2.69  
LINK        CA    CA L1004                OE11 CGU L  26     1555   1555  2.79  
LINK        CA    CA L1004                 O   HOH L1083     1555   1555  2.79  
LINK        CA    CA L1004                 O   HOH L1067     1555   1555  2.87  
LINK        CA    CA L1004                OE21 CGU L  16     1555   1555  2.91  
LINK        CA    CA L1005                OE11 CGU L   7     1555   1555  2.64  
LINK        CA    CA L1005                OE22 CGU L  26     1555   1555  2.66  
LINK        CA    CA L1005                 OD1 ASN L   2     1555   1555  2.81  
LINK        CA    CA L1005                OE11 CGU L  26     1555   1555  2.94  
LINK        CA    CA L1005                OE11 CGU L   6     1555   1555  2.91  
LINK        CA    CA L1005                OE11 CGU L  16     1555   1555  2.74  
LINK        CA    CA L1005                 O   ALA L   1     1555   1555  2.89  
LINK        CA    CA L1005                OE21 CGU L  16     1555   1555  2.77  
LINK        CA    CA L1006                 O   HOH L1106     1555   1555  2.88  
LINK        CA    CA L1006                OE12 CGU L  16     1555   1555  3.07  
LINK        CA    CA L1006                OE22 CGU L   6     1555   1555  2.85  
LINK        CA    CA L1006                OE11 CGU L   6     1555   1555  2.77  
LINK        CA    CA L1006                OE22 CGU L  20     1555   1555  2.97  
LINK        CA    CA L1006                OE21 CGU L  20     1555   1555  2.80  
LINK        CA    CA L1006                OE11 CGU L  16     1555   1555  2.83  
LINK        CA    CA L1006                 O   ALA L   1     1555   1555  2.82  
LINK        CA    CA L1007                OE21 CGU L  19     1555   1555  3.04  
LINK        CA    CA L1007                OE12 CGU L  19     1555   1555  2.79  
LINK        CA    CA L1007                OE21 CGU L  14     1555   1555  2.72  
LINK        CA    CA L1007                OE12 CGU L  14     1555   1555  2.93  
LINK        CA    CA L1008                OE11 CGU L  20     1555   1555  3.01  
LINK        CA    CA L1008                OE21 CGU L  20     1555   1555  2.79  
LINK        CA    CA L1009                OE11 CGU L  25     1555   1555  2.73  
LINK        CA    CA L1009                OE21 CGU L  29     1555   1555  2.58  
LINK        CA    CA L1009                OE22 CGU L  25     1555   1555  2.91  
LINK        CA    CA L1009                OE11 CGU L  29     1555   1555  2.93  
CISPEP   1 PHE H  256    PRO H  257          0         0.15                     
CISPEP   2 GLU T   26    PRO T   27          0        -0.05                     
SITE     1 AC1  3 GLN L  49  SER L  52  TYR L  68                               
SITE     1 AC2  6 GLY L  58  SER L  60  PHE L  71  CYS L  72                    
SITE     2 AC2  6 HOH L1092  ARG T 131                                          
SITE     1 AC3  6 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     2 AC3  6 HOH H2094  HOH H2105                                          
SITE     1 AC4  5 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 AC4  5 GLN L  64                                                     
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 L1067  HOH L1083  HOH L1084                               
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  5 ALA L   1  CGU L   6  CGU L  16  CGU L  20                    
SITE     2 AC8  5 HOH L1106                                                     
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 18 HIS H  57  ASP H  60  TYR H  94  GLY H  97                    
SITE     2 BC3 18 THR H  98  THR H  99  ASP H 146  ASP H 189                    
SITE     3 BC3 18 SER H 190  SER H 195  VAL H 213  SER H 214                    
SITE     4 BC3 18 TRP H 215  GLY H 216  GLY H 219  GLY H 226                    
SITE     5 BC3 18 HOH H2054  HOH H2162                                          
CRYST1   71.560   82.300  123.520  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      0.013974  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012151  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008096        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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