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Database: PDB
Entry: 2FIR
LinkDB: 2FIR
Original site: 2FIR 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-DEC-05   2FIR              
TITLE     CRYSTAL STRUCTURE OF DFPR-VIIA/STF                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII LIGHT CHAIN;                        
COMPND   3 CHAIN: L;                                                            
COMPND   4 EC: 3.4.21.21;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: COAGULATION FACTOR VII HEAVY CHAIN (EC 3.4.21.21);         
COMPND   8 CHAIN: H;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: TISSUE FACTOR;                                             
COMPND  12 CHAIN: T;                                                            
COMPND  13 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;  
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F7;                                                            
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: BHK/VP16;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: F7;                                                            
SOURCE  15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: BHK/VP16;                               
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: F3;                                                            
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FACTOR VIIA, SOLUBLE TISSUE FACTOR, OXYANION HOLE, SERINE PROTEASE,   
KEYWDS   2 BLOOD COAGULATION, BLOOD CLOTTING, HYDROLASE-HYDROLASE INHIBITOR     
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.P.BAJAJ,A.E.SCHMIDT,K.PADMANABHAN,M.S.BAJAJ,D.PREVOST,H.SCHREUDER   
REVDAT   4   13-JUL-11 2FIR    1       VERSN                                    
REVDAT   3   24-FEB-09 2FIR    1       VERSN                                    
REVDAT   2   05-SEP-06 2FIR    1       JRNL                                     
REVDAT   1   11-JUL-06 2FIR    0                                                
JRNL        AUTH   S.P.BAJAJ,A.E.SCHMIDT,S.AGAH,M.S.BAJAJ,K.PADMANABHAN         
JRNL        TITL   HIGH RESOLUTION STRUCTURES OF P-AMINOBENZAMIDINE- AND        
JRNL        TITL 2 BENZAMIDINE-VIIA/SOLUBLE TISSUE FACTOR: UNPREDICTED          
JRNL        TITL 3 CONFORMATION OF THE 192-193 PEPTIDE BOND AND MAPPING OF      
JRNL        TITL 4 CA2+, MG2+, NA+ AND ZN2+ SITES IN FACTOR VIIA                
JRNL        REF    J.BIOL.CHEM.                  V. 281 24873 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16757484                                                     
JRNL        DOI    10.1074/JBC.M509971200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 37933                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2045                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 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            : 4660                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 626                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB035926.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10                               
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41633                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY                : 18.900                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 100 MM MAGNESIUM           
REMARK 280  CHLORIDE, 200 MM SODIUM CHLORIDE, 10 MM CALCIUM CHLORIDE, 20 UM     
REMARK 280  ZINC CHLORIDE , PH 6.5, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 293K                                                    
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       35.01000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.16500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.49000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.16500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.01000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.49000            
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: 8960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -226.0 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     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     LYS T   159                                                      
REMARK 465     SER T   160                                                      
REMARK 465     SER T   161                                                      
REMARK 465     SER T   162                                                      
REMARK 465     SER T   163                                                      
REMARK 465     GLY T   164                                                      
REMARK 465     LYS T   165                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH L  1173     O    HOH H  1236     4556     0.52            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    HIS H 199   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA L   3       54.42   -148.06                                   
REMARK 500    PHE L   4      -86.29     37.45                                   
REMARK 500    LYS L  32      -46.93     71.40                                   
REMARK 500    SER L  67     -172.20   -173.28                                   
REMARK 500    GLN L 100     -103.05   -117.74                                   
REMARK 500    ASN H  48     -176.51   -170.14                                   
REMARK 500    SER H  54     -159.48   -147.73                                   
REMARK 500    HIS H  71      -59.49   -150.51                                   
REMARK 500    THR H  98     -162.41   -107.77                                   
REMARK 500    THR H 129C     -61.75   -120.50                                   
REMARK 500    ARG H 147       -2.04     72.27                                   
REMARK 500    ASP H 170G      -5.14     81.70                                   
REMARK 500    ARG T 135       58.78   -111.83                                   
REMARK 500    ASN T 138      -24.77     63.79                                   
REMARK 500    THR T 172     -152.54   -127.64                                   
REMARK 500    ASN T 184      103.76     52.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU L  39        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ARG T 135        23.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN T 138        24.8      L          L   OUTSIDE RANGE           
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 H 519        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH H1155        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH H1201        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH H1260        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH H1262        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH H1263        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH H1270        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH L1138        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH L1149        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH T1176        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH T1177        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH T1185        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH T1190        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH T1194        DISTANCE =  6.53 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE INHIBITOR IS COVALENTLY CONNECTED TO ACTIVE_SITE                 
REMARK 600 RESIDUE VIA A METHYLENE GROUP TO NE2 IN HIS 57 IN CHAIN H.           
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GLC L  801                                                       
REMARK 610     FUC L  901                                                       
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 H1009  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  72   O                                                      
REMARK 620 2 GLU H  75   O    83.9                                              
REMARK 620 3 HOH H1133   O    91.9  94.7                                        
REMARK 620 4 GLU H  80   OE2 174.5  94.9  82.9                                  
REMARK 620 5 GLU H  70   OE2  88.4 167.0  96.1  93.7                            
REMARK 620 6 HOH H1134   O    80.6  80.3 171.3 104.5  88.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA H1010  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR H 221   O                                                      
REMARK 620 2 HOH H1290   O   130.3                                              
REMARK 620 3 TYR H 184   O   136.3  72.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H1011  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H1135   O                                                      
REMARK 620 2 HOH H1132   O   111.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L1007  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  14  OE22                                                    
REMARK 620 2 CGU L  14  OE11  96.8                                              
REMARK 620 3 CGU L  19  OE12 143.3  95.7                                        
REMARK 620 4 CGU L  19  OE22  98.2 133.0  98.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L1004  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  16  OE21                                                    
REMARK 620 2 CGU L  16  OE11  93.0                                              
REMARK 620 3 CGU L  26  OE11  99.3  94.2                                        
REMARK 620 4 CGU L  26  OE22  86.4 175.6  90.2                                  
REMARK 620 5 HOH L1028   O   169.8  82.4  90.2  97.4                            
REMARK 620 6 HOH L1061   O    86.5  96.7 167.4  78.9  85.0                      
REMARK 620 N                    1     2     3     4     5                       
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  20  OE21                                                    
REMARK 620 2 HOH L1056   O   111.5                                              
REMARK 620 3 CGU L  16  OE11 147.1  70.5                                        
REMARK 620 4 ALA L   1   O   103.3 116.5 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  25  OE12                                                    
REMARK 620 2 CGU L  25  OE21 108.5                                              
REMARK 620 3 CGU L  29  OE11  90.3 121.1                                        
REMARK 620 4 HOH L1150   O    85.7 154.4  78.7                                  
REMARK 620 5 HOH L1054   O    99.3  81.7 151.1  75.0                            
REMARK 620 6 CGU L  29  OE21 152.4  98.4  81.0  66.9  77.9                      
REMARK 620 N                    1     2     3     4     5                       
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 CGU L  26  OE21                                                    
REMARK 620 2 HOH L1016   O    66.5                                              
REMARK 620 3 HOH L1116   O    87.3  43.3                                        
REMARK 620 4 HOH L1042   O    78.9 130.7 165.8                                  
REMARK 620 5 CGU L  29  OE12  79.2 119.1  88.7  85.5                            
REMARK 620 6 CGU L  29  OE11 109.6 104.1  61.1 120.5  43.2                      
REMARK 620 N                    1     2     3     4     5                       
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 HOH L1171   O                                                      
REMARK 620 2 HOH L1036   O    69.8                                              
REMARK 620 3 CGU L  29  OE12 109.0 160.0                                        
REMARK 620 4 HOH L1172   O   135.5 107.6  87.3                                  
REMARK 620 5 HOH L1042   O   120.1  76.2  88.2 100.9                            
REMARK 620 6 HOH L1173   O    85.1  75.9 124.1  53.0 131.7                      
REMARK 620 N                    1     2     3     4     5                       
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 CGU L   6  OE21                                                    
REMARK 620 2 HOH L1057   O   110.6                                              
REMARK 620 3 CGU L  20  OE21 148.5  65.0                                        
REMARK 620 4 HOH L1058   O   105.1  97.2 106.4                                  
REMARK 620 5 HOH L1049   O    71.9 142.7 131.8  48.9                            
REMARK 620 6 CGU L  20  OE22 138.8 109.7  50.8  78.2  81.5                      
REMARK 620 N                    1     2     3     4     5                       
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 GLN L  49   OE1                                                    
REMARK 620 2 GLY L  47   O    68.5                                              
REMARK 620 3 HOH T1025   O   152.8 130.7                                        
REMARK 620 4 HOH L1011   O   148.7  81.8  50.4                                  
REMARK 620 5 GLN L  64   O    85.3 153.6  74.7 124.5                            
REMARK 620 6 ASP L  46   OD2  79.3  85.4  83.1  89.3  92.0                      
REMARK 620 7 ASP L  63   OD2 117.9 100.1  80.9  75.4  90.0 162.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-[(3S)-6-CARBAMIMIDAMIDO-1-CHLORO-    
REMARK 630 2-OXOHEXAN-3-YL]-L-PROLINAMIDE                                       
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     0G7 H   701                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    DPN PRO ARG 0QE                                          
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 0G7 H 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC L 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC L 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 1009                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 1010                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 1011                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 1012                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 1013                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 1014                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL T 1015                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DAN   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FVIIA/STF WITH DFFR                                     
REMARK 900 RELATED ID: 2A2Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FVIIA/STF WITH P-AMINOBENZAMIDINE                       
REMARK 900 RELATED ID: 2AER   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FVIIA/STF WITH BENZAMIDINE                              
REMARK 900 RELATED ID: 2B8O   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FVIIA/STF WITH EGR                                      
DBREF  2FIR L    1   142  UNP    P08709   FA7_HUMAN       61    202             
DBREF  2FIR H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  2FIR T    6   210  UNP    P13726   TF_HUMAN        38    242             
SEQRES   1 L  142  ALA ASN ALA PHE LEU CGU CGU LEU ARG PRO GLY SER LEU          
SEQRES   2 L  142  CGU ARG CGU CYS LYS CGU CGU GLN CYS SER PHE CGU CGU          
SEQRES   3 L  142  ALA ARG CGU ILE PHE LYS ASP ALA CGU ARG THR LYS LEU          
SEQRES   4 L  142  PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER          
SEQRES   5 L  142  SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU          
SEQRES   6 L  142  GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY          
SEQRES   7 L  142  ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS          
SEQRES   8 L  142  VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP          
SEQRES   9 L  142  HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY          
SEQRES  10 L  142  TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR          
SEQRES  11 L  142  VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU              
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  205  THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER THR ASN          
SEQRES   2 T  205  PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO VAL ASN          
SEQRES   3 T  205  GLN VAL TYR THR VAL GLN ILE SER THR LYS SER GLY ASP          
SEQRES   4 T  205  TRP LYS SER LYS CYS PHE TYR THR THR ASP THR GLU CYS          
SEQRES   5 T  205  ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS GLN THR          
SEQRES   6 T  205  TYR LEU ALA ARG VAL PHE SER TYR PRO ALA GLY ASN VAL          
SEQRES   7 T  205  GLU SER THR GLY SER ALA GLY GLU PRO LEU TYR GLU ASN          
SEQRES   8 T  205  SER PRO GLU PHE THR PRO TYR LEU GLU THR ASN LEU GLY          
SEQRES   9 T  205  GLN PRO THR ILE GLN SER PHE GLU GLN VAL GLY THR LYS          
SEQRES  10 T  205  VAL ASN VAL THR VAL GLU ASP GLU ARG THR LEU VAL ARG          
SEQRES  11 T  205  ARG ASN ASN THR PHE LEU SER LEU ARG ASP VAL PHE GLY          
SEQRES  12 T  205  LYS ASP LEU ILE TYR THR LEU TYR TYR TRP LYS SER SER          
SEQRES  13 T  205  SER SER GLY LYS LYS THR ALA LYS THR ASN THR ASN GLU          
SEQRES  14 T  205  PHE LEU ILE ASP VAL ASP LYS GLY GLU ASN TYR CYS PHE          
SEQRES  15 T  205  SER VAL GLN ALA VAL ILE PRO SER ARG THR VAL ASN ARG          
SEQRES  16 T  205  LYS SER THR ASP SER PRO VAL GLU CYS MET                      
MODRES 2FIR CGU L    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR CGU L   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2FIR 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    GLC  L 801      11                                                       
HET    FUC  L 901      10                                                       
HET     MG  L1001       1                                                       
HET     CA  L1002       1                                                       
HET     CA  L1003       1                                                       
HET     MG  L1004       1                                                       
HET     CA  L1005       1                                                       
HET     CA  L1006       1                                                       
HET     MG  L1007       1                                                       
HET     CA  L1008       1                                                       
HET    0G7  H 701      30                                                       
HET     CA  H1009       1                                                       
HET     NA  H1010       1                                                       
HET     ZN  H1011       1                                                       
HET     ZN  H1012       1                                                       
HET     CL  H1013       1                                                       
HET     CL  H1014       1                                                       
HET     CL  T1015       1                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     0G7 D-PHENYLALANYL-N-[(3S)-6-CARBAMIMIDAMIDO-1-CHLORO-2-             
HETNAM   2 0G7  OXOHEXAN-3-YL]-L-PROLINAMIDE                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     0G7 D-PHE-PRO-ARG CHLOROMETHYLKETONE (PPACK)                         
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   4  GLC    C6 H12 O6                                                    
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   6   MG    3(MG 2+)                                                     
FORMUL   7   CA    6(CA 2+)                                                     
FORMUL  14  0G7    C21 H31 CL N6 O3                                             
FORMUL  16   NA    NA 1+                                                        
FORMUL  17   ZN    2(ZN 2+)                                                     
FORMUL  19   CL    3(CL 1-)                                                     
FORMUL  22  HOH   *626(H2 O)                                                    
HELIX    1   1 ALA L    3  LEU L    8  5                                   6    
HELIX    2   2 SER L   12  CYS L   17  1                                   6    
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   86  GLN L   88  5                                   3    
HELIX    6   6 ASN L   93  CYS L   98  5                                   6    
HELIX    7   7 ALA H   55  ASP H   60  5                                   6    
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 TYR H  234  MET H  242  1                                   9    
HELIX   12  12 LEU T   59  VAL T   64  1                                   6    
HELIX   13  13 THR T  101  THR T  106  1                                   6    
HELIX   14  14 ARG T  135  THR T  139  5                                   5    
HELIX   15  15 SER T  142  GLY T  148  1                                   7    
HELIX   16  16 LYS T  149  LEU T  151  5                                   3    
SHEET    1   A 2 SER L  60  ASP L  63  0                                        
SHEET    2   A 2 TYR L  68  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  TRP H 215 -1  N  TRP H 215   O  VAL H 227           
SHEET    6   E 8 PRO H 198  TYR H 203 -1  N  THR H 201   O  TYR H 208           
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 GLN T  32  THR T  40 -1  N  VAL T  36   O  LYS T  48           
SHEET    3   H 4 TYR T  71  PRO T  79 -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  ASN T 124   N  GLU T 117           
SHEET    3   I 3 GLU T 174  ASP T 178 -1  O  ILE T 177   N  VAL T 123           
SHEET    1   J 4 THR T 167  THR T 170  0                                        
SHEET    2   J 4 ILE T 152  TRP T 158 -1  N  LEU T 155   O  ALA T 168           
SHEET    3   J 4 CYS T 186  VAL T 192 -1  O  SER T 188   N  TYR T 156           
SHEET    4   J 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  2.04  
SSBOND   2 CYS L   50    CYS L   61                          1555   1555  2.05  
SSBOND   3 CYS L   55    CYS L   70                          1555   1555  2.05  
SSBOND   4 CYS L   72    CYS L   81                          1555   1555  2.05  
SSBOND   5 CYS L   91    CYS L  102                          1555   1555  2.03  
SSBOND   6 CYS L   98    CYS L  112                          1555   1555  2.02  
SSBOND   7 CYS L  114    CYS L  127                          1555   1555  2.05  
SSBOND   8 CYS L  135    CYS H  122                          1555   1555  2.04  
SSBOND   9 CYS H   22    CYS H   27                          1555   1555  2.06  
SSBOND  10 CYS H   42    CYS H   58                          1555   1555  2.03  
SSBOND  11 CYS H  168    CYS H  182                          1555   1555  2.05  
SSBOND  12 CYS H  191    CYS H  220                          1555   1555  2.03  
SSBOND  13 CYS T   49    CYS T   57                          1555   1555  2.07  
SSBOND  14 CYS T  186    CYS T  209                          1555   1555  2.04  
LINK        CA    CA H1009                 O   ASP H  72     1555   1555  2.20  
LINK        CA    CA H1009                 O   GLU H  75     1555   1555  1.98  
LINK        CA    CA H1009                 O   HOH H1133     1555   1555  1.88  
LINK        CA    CA H1009                 OE2 GLU H  80     1555   1555  2.09  
LINK        CA    CA H1009                 OE2 GLU H  70     1555   1555  2.15  
LINK        CA    CA H1009                 O   HOH H1134     1555   1555  2.36  
LINK        NA    NA H1010                 O   THR H 221     1555   1555  2.53  
LINK        NA    NA H1010                 O   HOH H1290     1555   1555  2.52  
LINK        ZN    ZN H1011                 O   HOH H1135     1555   1555  2.61  
LINK        ZN    ZN H1011                 O   HOH H1132     1555   1555  2.50  
LINK        ZN    ZN H1012                 NZ  LYS H  24     1555   1555  2.56  
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  1.34  
LINK         C   CGU L  14                 N   ARG L  15     1555   1555  1.34  
LINK        OE22 CGU L  14                MG    MG L1007     1555   1555  1.99  
LINK        OE11 CGU L  14                MG    MG L1007     1555   1555  2.03  
LINK         C   ARG L  15                 N   CGU L  16     1555   1555  1.33  
LINK        OE21 CGU L  16                MG    MG L1004     1555   1555  1.97  
LINK         C   CGU L  16                 N   CYS L  17     1555   1555  1.33  
LINK        OE11 CGU L  16                MG    MG L1004     1555   1555  1.92  
LINK         C   LYS L  18                 N   CGU L  19     1555   1555  1.34  
LINK        OE12 CGU L  19                MG    MG L1007     1555   1555  1.84  
LINK        OE22 CGU L  19                MG    MG L1007     1555   1555  1.92  
LINK         C   CGU L  19                 N   CGU L  20     1555   1555  1.33  
LINK        OE21 CGU L  20                CA    CA L1005     1555   1555  2.02  
LINK         C   CGU L  20                 N   GLN L  21     1555   1555  1.33  
LINK         C   PHE L  24                 N   CGU L  25     1555   1555  1.34  
LINK         C   CGU L  25                 N   CGU L  26     1555   1555  1.33  
LINK        OE12 CGU L  25                MG    MG L1001     1555   1555  1.88  
LINK        OE21 CGU L  25                MG    MG L1001     1555   1555  1.98  
LINK        OE11 CGU L  26                MG    MG L1004     1555   1555  1.94  
LINK         C   CGU L  26                 N   ALA L  27     1555   1555  1.33  
LINK        OE22 CGU L  26                MG    MG L1004     1555   1555  2.00  
LINK         C   ARG L  28                 N   CGU L  29     1555   1555  1.34  
LINK         C   CGU L  29                 N   ILE L  30     1555   1555  1.34  
LINK         C   ALA L  34                 N   CGU L  35     1555   1555  1.32  
LINK         C   CGU L  35                 N   ARG L  36     1555   1555  1.33  
LINK        MG    MG L1001                OE11 CGU L  29     1555   1555  2.22  
LINK        MG    MG L1001                 O   HOH L1150     1555   1555  2.77  
LINK        MG    MG L1001                 O   HOH L1054     1555   1555  2.16  
LINK        MG    MG L1001                OE21 CGU L  29     1555   1555  2.20  
LINK        CA    CA L1002                OE21 CGU L  26     1555   1555  2.17  
LINK        CA    CA L1002                 O   HOH L1016     1555   1555  3.17  
LINK        CA    CA L1002                 O   HOH L1116     1555   1555  1.89  
LINK        CA    CA L1002                 O   HOH L1042     1555   1555  2.54  
LINK        CA    CA L1002                OE12 CGU L  29     1555   1555  2.79  
LINK        CA    CA L1002                OE11 CGU L  29     1555   1555  3.09  
LINK        CA    CA L1003                 O   HOH L1171     1555   1555  2.28  
LINK        CA    CA L1003                 O   HOH L1036     1555   1555  3.04  
LINK        CA    CA L1003                OE12 CGU L  29     1555   1555  2.10  
LINK        CA    CA L1003                 O   HOH L1172     1555   1555  2.64  
LINK        CA    CA L1003                 O   HOH L1042     1555   1555  3.02  
LINK        CA    CA L1003                 O   HOH L1173     1555   1555  3.12  
LINK        MG    MG L1004                 O   HOH L1028     1555   1555  2.11  
LINK        MG    MG L1004                 O   HOH L1061     1555   1555  2.21  
LINK        CA    CA L1005                 O   HOH L1056     1555   1555  2.31  
LINK        CA    CA L1005                OE11 CGU L  16     1555   1555  2.71  
LINK        CA    CA L1005                 O   ALA L   1     1555   1555  1.89  
LINK        CA    CA L1006                OE21 CGU L   6     1555   1555  2.25  
LINK        CA    CA L1006                 O   HOH L1057     1555   1555  2.24  
LINK        CA    CA L1006                OE21 CGU L  20     1555   1555  2.63  
LINK        CA    CA L1006                 O   HOH L1058     1555   1555  3.09  
LINK        CA    CA L1006                 O   HOH L1049     1555   1555  2.81  
LINK        CA    CA L1006                OE22 CGU L  20     1555   1555  2.50  
LINK        CA    CA L1008                 OE1 GLN L  49     1555   1555  2.45  
LINK        CA    CA L1008                 O   GLY L  47     1555   1555  2.60  
LINK        CA    CA L1008                 O   HOH T1025     1555   1555  2.78  
LINK        CA    CA L1008                 O   HOH L1011     1555   1555  3.00  
LINK        CA    CA L1008                 O   GLN L  64     1555   1555  2.33  
LINK        CA    CA L1008                 OD2 ASP L  46     1555   1555  2.37  
LINK        CA    CA L1008                 OD2 ASP L  63     1555   1555  2.21  
LINK         O   TYR H 184                NA    NA H1010     1555   1555  2.72  
LINK         NE2 HIS H  57                 C3  0G7 H 701     1555   1555  1.82  
CISPEP   1 PHE H  256    PRO H  257          0         0.39                     
CISPEP   2 GLU T   26    PRO T   27          0        -0.13                     
SITE     1 AC1 17 HIS H  57  SER H 170H PRO H 170I ASP H 189                    
SITE     2 AC1 17 SER H 190  CYS H 191  LYS H 192  GLY H 193                    
SITE     3 AC1 17 SER H 195  SER H 214  TRP H 215  GLY H 216                    
SITE     4 AC1 17 GLN H 217  GLY H 219  HOH H 461  HOH H 478                    
SITE     5 AC1 17  CL H1013                                                     
SITE     1 AC2  5 GLN L  49  SER L  52  TYR L  68  HOH L1132                    
SITE     2 AC2  5 HOH L1136                                                     
SITE     1 AC3  6 GLY L  58  SER L  60  PHE L  71  CYS L  72                    
SITE     2 AC3  6 ARG T 131  PHE T 140                                          
SITE     1 AC4  4 CGU L  25  CGU L  29  HOH L1054  HOH L1150                    
SITE     1 AC5  4 CGU L  26  CGU L  29  HOH L1042  HOH L1116                    
SITE     1 AC6  5 CGU L  29  HOH L1036  HOH L1042  HOH L1171                    
SITE     2 AC6  5 HOH L1172                                                     
SITE     1 AC7  4 CGU L  16  CGU L  26  HOH L1028  HOH L1061                    
SITE     1 AC8  5 ALA L   1  CGU L  16  CGU L  20  HOH L1056                    
SITE     2 AC8  5 HOH L1057                                                     
SITE     1 AC9  5 CGU L   6  CGU L  20  HOH L1049  HOH L1057                    
SITE     2 AC9  5 HOH L1058                                                     
SITE     1 BC1  2 CGU L  14  CGU L  19                                          
SITE     1 BC2  7 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 BC2  7 GLN L  64  HOH L1011  HOH T1025                               
SITE     1 BC3  6 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     2 BC3  6 HOH H1133  HOH H1134                                          
SITE     1 BC4  9 TYR H 184  SER H 185  ASP H 186  GLY H 187                    
SITE     2 BC4  9 THR H 221  ALA H 221A HIS H 224  HOH H1198                    
SITE     3 BC4  9 HOH H1290                                                     
SITE     1 BC5  5 HIS H  76  GLU H  80  HOH H1132  HOH H1135                    
SITE     2 BC5  5 HOH H1136                                                     
SITE     1 BC6  4 LYS H  24  GLY H  69  HIS H 117  HOH H1052                    
SITE     1 BC7  2 GLY H 216  GLY H 219                                          
SITE     1 BC8  2 ARG H  84  HIS H 109                                          
SITE     1 BC9  4 GLU T 130  ARG T 144  TYR T 153  ASN T 173                    
CRYST1   70.020   80.980  126.330  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      0.014282  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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