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Database: PDB
Entry: 2AEI
LinkDB: 2AEI
Original site: 2AEI 
HEADER    HYDROLASE                               22-JUL-05   2AEI              
TITLE     CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF FACTOR VIIA/TISSUE FACTOR   
TITLE    2 AND 2-[[6-[3-(AMINOIMINOMETHYL)PHENOXY]-3,5-DIFLURO-4-[(1-METHYL-3-  
TITLE    3 PHENYLPROPYL)AMINO]-2-PYRIDINYL]OXY]-BENZOIC ACID                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: 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: 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 33-243;                                           
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 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_ORGAN: KIDNEY;                                     
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_ORGAN: KIDNEY;                                     
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: SACCHAROMYCES CEREVISIAE;                         
SOURCE  25 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    BLOOD COAGULATION, SERINE PROTEASE, THROMBOSIS, GLA, PYRIDINE,        
KEYWDS   2 BENZAMIDINE, TISSUE FACTOR, COFACTOR, ENZYME INHIBITOR COMPLEX,      
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ADLER,M.WHITLOW                                                     
REVDAT   3   13-JUL-11 2AEI    1       VERSN                                    
REVDAT   2   24-FEB-09 2AEI    1       VERSN                                    
REVDAT   1   01-AUG-06 2AEI    0                                                
JRNL        AUTH   J.T.KOHRT,K.J.FILIPSKI,W.L.CODY,C.CAI,D.A.DUDLEY,            
JRNL        AUTH 2 C.A.VAN HUIS,J.A.WILLARDSEN,S.T.RAPUNDALO,K.SAIYA-CORK,      
JRNL        AUTH 3 R.J.LEADLEY,L.NARASIMHAN,E.ZHANG,M.WHITLOW,M.ADLER,K.MCLEAN, 
JRNL        AUTH 4 Y.L.CHOU,C.MCKNIGHT,D.O.ARNAIZ,K.J.SHAW,D.R.LIGHT,           
JRNL        AUTH 5 J.J.EDMUNDS                                                  
JRNL        TITL   THE DISCOVERY OF FLUOROPYRIDINE-BASED INHIBITORS OF THE      
JRNL        TITL 2 FACTOR VIIA/TF COMPLEX.                                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  15  4752 2005              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   16125385                                                     
JRNL        DOI    10.1016/J.BMCL.2005.07.059                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52                           
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)   (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21278                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 759                             
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) : 2.52                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.63                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1388                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2529                       
REMARK   3   BIN FREE R VALUE                    : 0.2718                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 64                           
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            : 4679                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -12.17230                                            
REMARK   3    B22 (A**2) : 5.23530                                              
REMARK   3    B33 (A**2) : 6.93700                                              
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.34                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
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 2AEI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033797.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.080                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21938                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
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: MERLOT                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DAN USING SEPARATE REPLACEMENTS FOR EA    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000,CACODYLATE, GLYCEROL, PH 5.0,   
REMARK 280  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       35.10750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.96800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.24800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.96800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.10750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.24800            
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: 7150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 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    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   160                                                      
REMARK 465     SER T   161                                                      
REMARK 465     SER T   162                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE L   4    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG L    9   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU H  245   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG H  247   CG   CD   NE   CZ   NH1  NH2                        
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    GLY L  47   N   -  CA  -  C   ANGL. DEV. =  15.1 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    PHE L   4      -74.62    -32.70                                   
REMARK 500    CGU L   7        8.74    -64.11                                   
REMARK 500    CGU L  14      -77.41    -71.14                                   
REMARK 500    ILE L  30      -70.10    -89.11                                   
REMARK 500    LYS L  32      -56.33     62.51                                   
REMARK 500    ASN L  57       24.38     38.12                                   
REMARK 500    SER L  67     -177.55    179.65                                   
REMARK 500    LEU L  89       64.86    -64.14                                   
REMARK 500    GLN L 100      -93.87   -123.34                                   
REMARK 500    THR L 106      -80.59    -64.66                                   
REMARK 500    TYR L 133       78.92   -118.79                                   
REMARK 500    CYS H  27       49.85   -146.16                                   
REMARK 500    LEU H  41      -75.45   -109.53                                   
REMARK 500    ASN H  48     -148.03   -170.69                                   
REMARK 500    HIS H  71      -55.24   -144.59                                   
REMARK 500    THR H 129C     -59.91   -121.50                                   
REMARK 500    ARG H 147       -0.60     68.98                                   
REMARK 500    LYS H 170D      83.05    -63.00                                   
REMARK 500    ASP H 189      161.41    170.08                                   
REMARK 500    SER H 195      143.99    -37.26                                   
REMARK 500    SER H 214      -68.87   -120.73                                   
REMARK 500    PRO H 246      101.03    -59.20                                   
REMARK 500    PHE T  19       -3.74     82.33                                   
REMARK 500    LYS T  41      -33.75    -34.66                                   
REMARK 500    ASP T  66       90.06   -170.97                                   
REMARK 500    PHE T 116       87.06   -153.08                                   
REMARK 500    ARG T 136      113.57   -164.81                                   
REMARK 500    ASN T 138      -23.46     64.32                                   
REMARK 500    THR T 172     -155.46   -142.52                                   
REMARK 500    LYS T 181       89.63    -64.42                                   
REMARK 500    SER T 188      127.49    174.33                                   
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    CYS L 135        23.2      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 678        DISTANCE =  5.05 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 510  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  75   O                                                      
REMARK 620 2 GLU H  70   OE2 179.5                                              
REMARK 620 3 GLU H  70   OE1 137.8  41.7                                        
REMARK 620 4 ASP H  72   O   101.0  79.2  94.3                                  
REMARK 620 5 GLU H  80   OE2  97.4  82.4  76.0 160.5                            
REMARK 620 6 HOH H 632   O   102.4  78.0 117.6  87.2  82.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE12                                                    
REMARK 620 2 CGU L  26  OE11 130.0                                              
REMARK 620 3 CGU L  29  OE22 103.0  98.5                                        
REMARK 620 4 CGU L  25  OE21 111.5 118.2  70.3                                  
REMARK 620 5 CGU L   7  OE21  83.1  52.3  89.8 157.2                            
REMARK 620 6 CGU L   7  OE11  50.2  93.8 151.0 125.6  77.2                      
REMARK 620 7 CGU L  29  OE21  98.0  72.1  39.4 108.4  50.5 123.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  25  OE12                                                    
REMARK 620 2 CGU L  29  OE12 134.6                                              
REMARK 620 3 CGU L  25  OE21 102.5 104.7                                        
REMARK 620 4 CGU L  29  OE11  97.1  41.7 141.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  19  OE12                                                    
REMARK 620 2 CGU L  20  OE12 128.4                                              
REMARK 620 3 CGU L  20  OE22 112.8  95.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   6  OE22                                                    
REMARK 620 2 CGU L  16  OE22 113.8                                              
REMARK 620 3 CGU L  20  OE21 110.3 107.3                                        
REMARK 620 4 CGU L  16  OE21 119.7  63.7 128.6                                  
REMARK 620 5 CGU L   6  OE21  53.0 156.4  96.1 103.8                            
REMARK 620 6 ALA L   1   O   106.4 120.8  96.8  59.1  57.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  26  OE21                                                    
REMARK 620 2 CGU L   6  OE11 159.2                                              
REMARK 620 3 CGU L  16  OE21  97.2  98.1                                        
REMARK 620 4 CGU L   7  OE21  96.2  80.7 140.8                                  
REMARK 620 5 ASN L   2   OD1  77.9  81.6 148.1  70.8                            
REMARK 620 6 CGU L   6  OE12 164.2  36.4  69.6  89.6 117.8                      
REMARK 620 7 ALA L   1   O    79.7  92.7  68.8 150.1  79.4 102.3                
REMARK 620 8 CGU L  16  OE12  92.1 104.3  80.6  62.3 130.7  77.6 146.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L   7  OE22                                                    
REMARK 620 2 CGU L   7  OE21  69.3                                              
REMARK 620 3 CGU L  16  OE12 117.6  83.2                                        
REMARK 620 4 CGU L  29  OE21  93.9  99.7 146.8                                  
REMARK 620 5 CGU L  16  OE11 136.5 126.1  43.9 118.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 509  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN L  49   OE1                                                    
REMARK 620 2 GLY L  47   O    86.6                                              
REMARK 620 3 ASP L  46   O   104.4  68.6                                        
REMARK 620 4 ASP L  63   OD2 110.1  74.4 126.8                                  
REMARK 620 5 ASP L  63   OD1  64.2  80.7 148.1  46.8                            
REMARK 620 6 GLN L  64   O    91.7 164.9 126.2  92.2  85.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC H 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 03R H 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DAN   RELATED DB: PDB                                   
REMARK 900 ORIGINAL FACTOR VIIA/TISSUE FACTOR                                   
REMARK 900 RELATED ID: 1Z6J   RELATED DB: PDB                                   
REMARK 900 FACTOR VIIA/TISSUE FACTOR W/ INHIBITOR                               
REMARK 900 RELATED ID: 1W0Y   RELATED DB: PDB                                   
REMARK 900 FACTOR VIIA/TISSUE FACTOR W/ INHIBITOR                               
REMARK 900 RELATED ID: 1W2K   RELATED DB: PDB                                   
REMARK 900 FACTOR VIIA/TISSUE FACTOR W/ INHIBITOR                               
REMARK 900 RELATED ID: 1YGC   RELATED DB: PDB                                   
REMARK 900 FACTOR VIIA W/ INHIBITOR                                             
DBREF  2AEI L    1   152  UNP    P08709   FA7_HUMAN       61    212             
DBREF  2AEI H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  2AEI T    1   211  UNP    P13726   TF_HUMAN        33    243             
SEQADV 2AEI CGU L    6  UNP  P08709    GLU    66 MODIFIED RESIDUE               
SEQADV 2AEI CGU L    7  UNP  P08709    GLU    67 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   14  UNP  P08709    GLU    74 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   16  UNP  P08709    GLU    76 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   19  UNP  P08709    GLU    79 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   20  UNP  P08709    GLU    80 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   25  UNP  P08709    GLU    85 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   26  UNP  P08709    GLU    86 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   29  UNP  P08709    GLU    89 MODIFIED RESIDUE               
SEQADV 2AEI CGU L   35  UNP  P08709    GLU    95 MODIFIED RESIDUE               
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  211  SER GLY THR THR ASN THR VAL ALA ALA TYR ASN LEU THR          
SEQRES   2 T  211  TRP LYS SER THR ASN PHE LYS THR ILE LEU GLU TRP GLU          
SEQRES   3 T  211  PRO LYS PRO VAL ASN GLN VAL TYR THR VAL GLN ILE SER          
SEQRES   4 T  211  THR LYS SER GLY ASP TRP LYS SER LYS CYS PHE TYR THR          
SEQRES   5 T  211  THR ASP THR GLU CYS ASP LEU THR ASP GLU ILE VAL LYS          
SEQRES   6 T  211  ASP VAL LYS GLN THR TYR LEU ALA ARG VAL PHE SER TYR          
SEQRES   7 T  211  PRO ALA GLY ASN VAL GLU SER THR GLY SER ALA GLY GLU          
SEQRES   8 T  211  PRO LEU TYR GLU ASN SER PRO GLU PHE THR PRO TYR LEU          
SEQRES   9 T  211  GLU THR ASN LEU GLY GLN PRO THR ILE GLN SER PHE GLU          
SEQRES  10 T  211  GLN VAL GLY THR LYS VAL ASN VAL THR VAL GLU ASP GLU          
SEQRES  11 T  211  ARG THR LEU VAL ARG ARG ASN ASN THR PHE LEU SER LEU          
SEQRES  12 T  211  ARG ASP VAL PHE GLY LYS ASP LEU ILE TYR THR LEU TYR          
SEQRES  13 T  211  TYR TRP LYS SER SER SER SER GLY LYS LYS THR ALA LYS          
SEQRES  14 T  211  THR ASN THR ASN GLU PHE LEU ILE ASP VAL ASP LYS GLY          
SEQRES  15 T  211  GLU ASN TYR CYS PHE SER VAL GLN ALA VAL ILE PRO SER          
SEQRES  16 T  211  ARG THR VAL ASN ARG LYS SER THR ASP SER PRO VAL GLU          
SEQRES  17 T  211  CYS MET GLY                                                  
MODRES 2AEI CGU L    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI CGU L   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2AEI 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     CA  L 501       1                                                       
HET     CA  L 502       1                                                       
HET     CA  L 503       1                                                       
HET     CA  L 504       1                                                       
HET     CA  L 505       1                                                       
HET     CA  L 506       1                                                       
HET     CA  L 509       1                                                       
HET     CA  H 510       1                                                       
HET    CAC  H 511       5                                                       
HET    03R  H 500      39                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     CAC CACODYLATE ION                                                   
HETNAM     03R 2-({6-{3-[AMINO(IMINO)METHYL]PHENOXY}-3,5-DIFLUORO-4-            
HETNAM   2 03R  [(1-METHYL-3-PHENYLPROPYL)AMINO]-2-PYRIDINYL}OXY)               
HETNAM   3 03R  BENZOIC ACID                                                    
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   4   CA    8(CA 2+)                                                     
FORMUL  12  CAC    C2 H6 AS O2 1-                                               
FORMUL  13  03R    C29 H26 F2 N4 O4                                             
FORMUL  14  HOH   *81(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  ASP L   46  1                                  14    
HELIX    5   5 ASP L   48  SER L   53  5                                   6    
HELIX    6   6 ASP L   86  GLN L   88  5                                   3    
HELIX    7   7 ASN L   93  CYS L   98  5                                   6    
HELIX    8   8 ALA H   55  ASP H   60  5                                   6    
HELIX    9   9 GLU H  125  THR H  129C 1                                   8    
HELIX   10  10 LEU H  129D VAL H  129G 5                                   4    
HELIX   11  11 MET H  164  GLN H  170A 1                                   8    
HELIX   12  12 TYR H  234  SER H  244  1                                  11    
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  ASP L  63  0                                        
SHEET    2   A 2 TYR L  68  PHE L  71 -1  O  ILE L  69   N  LYS L  62           
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  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  ARG H 107   N  ALA H  86           
SHEET    4   F 8 TRP H  51  SER H  54 -1  N  SER H  54   O  ALA H 104           
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  GLU T  24   N  THR T  13           
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  ILE T  38   O  LYS T  46           
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  GLU T  95   N  VAL T  75           
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  PHE T 175   N  VAL T 125           
SHEET    1   J 2 ARG T 131  ARG T 136  0                                        
SHEET    2   J 2 THR T 139  SER T 142 -1  O  LEU T 141   N  VAL T 134           
SHEET    1   K 4 LYS T 166  THR T 170  0                                        
SHEET    2   K 4 ILE T 152  TRP T 158 -1  N  TYR T 153   O  THR T 170           
SHEET    3   K 4 CYS T 186  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  2.04  
SSBOND   2 CYS L   50    CYS L   61                          1555   1555  2.04  
SSBOND   3 CYS L   55    CYS L   70                          1555   1555  2.03  
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  2.04  
SSBOND   7 CYS L  114    CYS L  127                          1555   1555  2.03  
SSBOND   8 CYS L  135    CYS H  122                          1555   1555  2.04  
SSBOND   9 CYS H   22    CYS H   27                          1555   1555  2.05  
SSBOND  10 CYS H   42    CYS H   58                          1555   1555  2.02  
SSBOND  11 CYS H  168    CYS H  182                          1555   1555  2.04  
SSBOND  12 CYS H  191    CYS H  220                          1555   1555  2.02  
SSBOND  13 CYS T   49    CYS T   57                          1555   1555  2.04  
SSBOND  14 CYS T  186    CYS T  209                          1555   1555  2.04  
LINK        CA    CA H 510                 O   GLU H  75     1555   1555  1.61  
LINK        CA    CA L 502                OE12 CGU L   7     1555   1555  1.67  
LINK        CA    CA L 501                OE12 CGU L  25     1555   1555  1.68  
LINK        CA    CA L 501                OE12 CGU L  29     1555   1555  1.67  
LINK        CA    CA L 506                OE12 CGU L  19     1555   1555  1.68  
LINK        CA    CA L 506                OE12 CGU L  20     1555   1555  1.68  
LINK        CA    CA L 505                OE22 CGU L   6     1555   1555  1.70  
LINK        CA    CA L 504                OE21 CGU L  26     1555   1555  1.70  
LINK        CA    CA H 510                 OE2 GLU H  70     1555   1555  2.48  
LINK        CA    CA H 510                 OE1 GLU H  70     1555   1555  3.28  
LINK        CA    CA H 510                 O   ASP H  72     1555   1555  2.20  
LINK        CA    CA H 510                 OE2 GLU H  80     1555   1555  2.41  
LINK        CA    CA H 510                 O   HOH H 632     1555   1555  1.74  
LINK         C   LEU L   5                 N   CGU L   6     1555   1555  1.34  
LINK         C   CGU L   6                 N   CGU L   7     1555   1555  1.33  
LINK        OE11 CGU L   6                CA    CA L 504     1555   1555  1.72  
LINK        OE22 CGU L   7                CA    CA L 503     1555   1555  1.92  
LINK        OE21 CGU L   7                CA    CA L 503     1555   1555  1.83  
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        OE12 CGU L  16                CA    CA L 503     1555   1555  1.92  
LINK        OE21 CGU L  16                CA    CA L 504     1555   1555  1.76  
LINK        OE22 CGU L  16                CA    CA L 505     1555   1555  1.73  
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        OE21 CGU L  20                CA    CA L 505     1555   1555  1.71  
LINK         C   CGU L  20                 N   GLN L  21     1555   1555  1.33  
LINK        OE22 CGU L  20                CA    CA L 506     1555   1555  1.74  
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        OE21 CGU L  25                CA    CA L 501     1555   1555  1.78  
LINK         C   CGU L  26                 N   ALA L  27     1555   1555  1.33  
LINK        OE11 CGU L  26                CA    CA L 502     1555   1555  1.70  
LINK         C   ARG L  28                 N   CGU L  29     1555   1555  1.33  
LINK         C   CGU L  29                 N   ILE L  30     1555   1555  1.34  
LINK        OE22 CGU L  29                CA    CA L 502     1555   1555  1.72  
LINK        OE21 CGU L  29                CA    CA L 503     1555   1555  1.82  
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        CA    CA L 501                OE11 CGU L  29     1555   1555  3.11  
LINK        CA    CA L 502                OE21 CGU L  25     1555   1555  3.33  
LINK        CA    CA L 502                OE21 CGU L   7     1555   1555  3.28  
LINK        CA    CA L 502                OE11 CGU L   7     1555   1555  2.84  
LINK        CA    CA L 502                OE21 CGU L  29     1555   1555  3.24  
LINK        CA    CA L 503                OE11 CGU L  16     1555   1555  3.09  
LINK        CA    CA L 504                OE21 CGU L   7     1555   1555  2.45  
LINK        CA    CA L 504                 OD1 ASN L   2     1555   1555  2.32  
LINK        CA    CA L 504                OE12 CGU L   6     1555   1555  3.31  
LINK        CA    CA L 504                 O   ALA L   1     1555   1555  2.64  
LINK        CA    CA L 504                OE12 CGU L  16     1555   1555  2.37  
LINK        CA    CA L 505                OE21 CGU L  16     1555   1555  2.26  
LINK        CA    CA L 505                OE21 CGU L   6     1555   1555  2.73  
LINK        CA    CA L 505                 O   ALA L   1     1555   1555  2.88  
LINK        CA    CA L 509                 OE1 GLN L  49     1555   1555  2.05  
LINK        CA    CA L 509                 O   GLY L  47     1555   1555  1.87  
LINK        CA    CA L 509                 O   ASP L  46     1555   1555  2.35  
LINK        CA    CA L 509                 OD2 ASP L  63     1555   1555  2.74  
LINK        CA    CA L 509                 OD1 ASP L  63     1555   1555  2.71  
LINK        CA    CA L 509                 O   GLN L  64     1555   1555  1.75  
CISPEP   1 PHE H  256    PRO H  257          0        -0.33                     
CISPEP   2 GLU T   26    PRO T   27          0         0.20                     
SITE     1 AC1  2 CGU L  25  CGU L  29                                          
SITE     1 AC2  4 CGU L   7  CGU L  25  CGU L  26  CGU L  29                    
SITE     1 AC3  5 CGU L   7  CGU L  16  CGU L  26  CGU L  29                    
SITE     2 AC3  5  CA L 504                                                     
SITE     1 AC4  8 ALA L   1  ASN L   2  CGU L   6  CGU L   7                    
SITE     2 AC4  8 CGU L  16  CGU L  26   CA L 503   CA L 505                    
SITE     1 AC5  5 ALA L   1  CGU L   6  CGU L  16  CGU L  20                    
SITE     2 AC5  5  CA L 504                                                     
SITE     1 AC6  2 CGU L  19  CGU L  20                                          
SITE     1 AC7  5 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 AC7  5 GLN L  64                                                     
SITE     1 AC8  5 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     2 AC8  5 HOH H 632                                                     
SITE     1 AC9  6 CYS H 168  SER H 170B GLN H 217  GLY H 223                    
SITE     2 AC9  6 HIS H 224  PHE H 225                                          
SITE     1 BC1 15 HIS H  57  THR H  98  THR H  99  ASP H 189                    
SITE     2 BC1 15 SER H 190  CYS H 191  LYS H 192  GLY H 193                    
SITE     3 BC1 15 SER H 195  SER H 214  TRP H 215  GLY H 216                    
SITE     4 BC1 15 GLN H 217  GLY H 219  CYS H 220                               
CRYST1   70.215   80.496  125.936  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      0.014242  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012423  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007941        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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