GenomeNet

Database: PDB
Entry: 1TFX
LinkDB: 1TFX
Original site: 1TFX 
HEADER    COMPLEX (SERINE PROTEASE/INHIBITOR)     21-JAN-97   1TFX              
TITLE     COMPLEX OF THE SECOND KUNITZ DOMAIN OF TISSUE FACTOR                  
TITLE    2 PATHWAY INHIBITOR WITH PORCINE TRYPSIN                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TISSUE FACTOR PATHWAY INHIBITOR;                           
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: FACTOR XA-BINDING DOMAIN, DOMAIN II;                       
COMPND  10 SYNONYM: TFPI, EPI, LACI;                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: BLOOD;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JE5505;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFLAG;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 ORGAN: BLOOD;                                                        
SOURCE  15 TISSUE: BLOOD;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: JE5505;                                    
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PFLAG                                     
KEYWDS    COMPLEX (SERINE PROTEASE/INHIBITOR), HYDROLASE, INHIBITOR,            
KEYWDS   2 BLOOD COAGULATION                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.T.STUBBS,R.HUBER                                                    
REVDAT   3   24-FEB-09 1TFX    1       VERSN                                    
REVDAT   2   01-APR-03 1TFX    1       JRNL                                     
REVDAT   1   21-JAN-98 1TFX    0                                                
JRNL        AUTH   M.J.BURGERING,L.P.ORBONS,A.VAN DER DOELEN,                   
JRNL        AUTH 2 J.MULDERS,H.J.THEUNISSEN,P.D.GROOTENHUIS,W.BODE,             
JRNL        AUTH 3 R.HUBER,M.T.STUBBS                                           
JRNL        TITL   THE SECOND KUNITZ DOMAIN OF HUMAN TISSUE FACTOR              
JRNL        TITL 2 PATHWAY INHIBITOR: CLONING, STRUCTURE                        
JRNL        TITL 3 DETERMINATION AND INTERACTION WITH FACTOR XA.                
JRNL        REF    J.MOL.BIOL.                   V. 269   395 1997              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9199408                                                      
JRNL        DOI    10.1006/JMBI.1997.1029                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.T.STUBBS,R.MORENWEISER,J.STURZEBECHER,M.BAUER,             
REMARK   1  AUTH 2 W.BODE,R.HUBER,G.P.PIECHOTTKA,G.MATSCHINER,                  
REMARK   1  AUTH 3 C.P.SOMMERHOFF,H.FRITZ,E.A.AUERSWALD                         
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT               
REMARK   1  TITL 2 LEECH-DERIVED TRYPTASE INHIBITOR IN COMPLEX WITH             
REMARK   1  TITL 3 TRYPSIN. IMPLICATIONS FOR THE STRUCTURE OF HUMAN             
REMARK   1  TITL 4 MAST CELL TRYPTASE AND ITS INHIBITION                        
REMARK   1  REF    J.BIOL.CHEM.                  V. 272 19931 1997              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.BRANDSTETTER,A.KUHNE,W.BODE,R.HUBER,                       
REMARK   1  AUTH 2 W.VON DER SAAL,K.WIRTHENSOHN,R.A.ENGH                        
REMARK   1  TITL   X-RAY STRUCTURE OF ACTIVE SITE-INHIBITED CLOTTING            
REMARK   1  TITL 2 FACTOR XA. IMPLICATIONS FOR DRUG DESIGN AND                  
REMARK   1  TITL 3 SUBSTRATE RECOGNITION                                        
REMARK   1  REF    J.BIOL.CHEM.                  V. 271 29988 1996              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.T.STUBBS II                                                
REMARK   1  TITL   STRUCTURAL ASPECTS OF FACTOR XA INHIBITION                   
REMARK   1  REF    CURR.PHARM.DES.               V.   2   543 1996              
REMARK   1  REFN                   ISSN 1381-6128                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   A.VAN DE LOCHT,M.T.STUBBS,W.BODE,T.FRIEDRICH,                
REMARK   1  AUTH 2 C.BOLLSCHWEILER,W.HOFFKEN,R.HUBER                            
REMARK   1  TITL   THE ORNITHODORIN-THROMBIN CRYSTAL STRUCTURE, A KEY           
REMARK   1  TITL 2 TO THE TAP ENIGMA?                                           
REMARK   1  REF    EMBO J.                       V.  15  6011 1996              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.T.STUBBS,R.HUBER,W.BODE                                    
REMARK   1  TITL   CRYSTAL STRUCTURES OF FACTOR XA SPECIFIC                     
REMARK   1  TITL 2 INHIBITORS IN COMPLEX WITH TRYPSIN: STRUCTURAL               
REMARK   1  TITL 3 GROUNDS FOR INHIBITION OF FACTOR XA AND                      
REMARK   1  TITL 4 SELECTIVITY AGAINST THROMBIN                                 
REMARK   1  REF    FEBS LETT.                    V. 375   103 1995              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   K.PADMANABHAN,K.P.PADMANABHAN,A.TULINSKY,C.H.PARK,           
REMARK   1  AUTH 2 W.BODE,R.HUBER,D.T.BLANKENSHIP,A.D.CARDIN,W.KISIEL           
REMARK   1  TITL   STRUCTURE OF HUMAN DES(1-45) FACTOR XA AT 2.2 A              
REMARK   1  TITL 2 RESOLUTION                                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 232   947 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13757                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 558                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
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            : 4239                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 142                                     
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) : 6.00                            
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.32                            
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TFX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.30000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PORCINE TRYPSIN MODEL FROM LDTI TRYPSIN (PDB         
REMARK 200  ENTRY 1LDT)                                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0                                   
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       20.95000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.10000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.95000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.10000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THIS STRUCTURE IS PART OF A MULTIDISCIPLINARY STUDY INTO             
REMARK 400 THE STRUCTURE AND FUNCTION OF THE SECOND DOMAIN OF TISSUE            
REMARK 400 FACTOR PATHWAY INHIBITOR, WHICH IS RESPONSIBLE FOR                   
REMARK 400 SWITCHING OFF THE EARLY STAGES OF BLOOD COAGULATION.                 
REMARK 400 COORDINATES FOR THE NMR SOLUTION STRUCTURE HAVE ALSO BEEN            
REMARK 400 DEPOSITED AS PDB ENTRY 1ADZ.                                         
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASP C   57                                                       
REMARK 475     GLY C   58                                                       
REMARK 475     ASP D   57                                                       
REMARK 475     GLY D   58                                                       
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    SER A  49      -12.54    -46.20                                   
REMARK 500    HIS A  71      -63.64   -150.49                                   
REMARK 500    ASN A 115      124.02    107.57                                   
REMARK 500    SER A 116      -66.36     65.89                                   
REMARK 500    SER A 147      -62.20   -109.13                                   
REMARK 500    ASP A 189      175.74    177.53                                   
REMARK 500    SER A 195      142.36    -39.98                                   
REMARK 500    SER A 214      -74.61   -114.69                                   
REMARK 500    ALA A 221       19.73     56.77                                   
REMARK 500    ALA A 243        4.51    -66.61                                   
REMARK 500    SER B  37       22.68   -149.98                                   
REMARK 500    HIS B  71      -58.15   -154.34                                   
REMARK 500    ASN B 115      134.20     98.20                                   
REMARK 500    SER B 116      -73.89     79.78                                   
REMARK 500    SER B 147      -72.97   -107.36                                   
REMARK 500    ASP B 189      170.85    177.58                                   
REMARK 500    SER B 214      -73.42   -132.02                                   
REMARK 500    ARG C  15       38.61    -95.83                                   
REMARK 500    TYR C  17       71.13   -117.03                                   
REMARK 500    ASN C  44      106.30   -160.60                                   
REMARK 500    GLU C  56      -70.94    -79.73                                   
REMARK 500    ASP C  57       58.92    158.84                                   
REMARK 500    ARG D  15       44.60   -102.64                                   
REMARK 500    ASN D  25       23.13    -78.50                                   
REMARK 500    GLU D  56      -75.58    -99.41                                   
REMARK 500    ASP D  57      144.38    178.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A1007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  72   O                                                      
REMARK 620 2 VAL A  75   O    94.3                                              
REMARK 620 3 GLU A  77   OE1 101.2 116.0                                        
REMARK 620 4 GLU A  80   OE2 165.4  84.4  92.4                                  
REMARK 620 5 HOH A2053   O    92.3  64.3 166.4  74.0                            
REMARK 620 6 GLU A  70   OE1  84.1 138.3 105.0  87.3  74.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  70   OE1                                                    
REMARK 620 2 ASN B  72   O    81.2                                              
REMARK 620 3 VAL B  75   O   146.3  93.2                                        
REMARK 620 4 GLU B  80   OE2  91.9 166.6  98.9                                  
REMARK 620 5 GLU B  77   OE1 102.9  90.7 110.5  79.6                            
REMARK 620 6 HOH B5053   O    73.9 112.4  77.8  76.2 155.4                      
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 A 1007                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4007                 
DBREF  1TFX A   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1TFX B   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1TFX C    1    58  UNP    P10646   TFPI1_HUMAN    121    178             
DBREF  1TFX D    1    58  UNP    P10646   TFPI1_HUMAN    121    178             
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
SEQRES   1 B  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 B  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 B  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 B  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 B  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 B  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 B  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 B  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 B  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 B  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 B  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 B  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 B  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 B  223  ALA ASN                                                      
SEQRES   1 C   58  LYS PRO ASP PHE CYS PHE LEU GLU GLU ASP PRO GLY ILE          
SEQRES   2 C   58  CYS ARG GLY TYR ILE THR ARG TYR PHE TYR ASN ASN GLN          
SEQRES   3 C   58  THR LYS GLN CYS GLU ARG PHE LYS TYR GLY GLY CYS LEU          
SEQRES   4 C   58  GLY ASN MET ASN ASN PHE GLU THR LEU GLU GLU CYS LYS          
SEQRES   5 C   58  ASN ILE CYS GLU ASP GLY                                      
SEQRES   1 D   58  LYS PRO ASP PHE CYS PHE LEU GLU GLU ASP PRO GLY ILE          
SEQRES   2 D   58  CYS ARG GLY TYR ILE THR ARG TYR PHE TYR ASN ASN GLN          
SEQRES   3 D   58  THR LYS GLN CYS GLU ARG PHE LYS TYR GLY GLY CYS LEU          
SEQRES   4 D   58  GLY ASN MET ASN ASN PHE GLU THR LEU GLU GLU CYS LYS          
SEQRES   5 D   58  ASN ILE CYS GLU ASP GLY                                      
HET     CA  A1007       1                                                       
HET     CA  B4007       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   7  HOH   *143(H2 O)                                                    
HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
HELIX    2   2 ASP A  165  SER A  171  1                                   7    
HELIX    3   3 VAL A  231  ALA A  244  5                                  14    
HELIX    4   4 ALA B   56  CYS B   58  5                                   3    
HELIX    5   5 ASP B  165  SER B  171  1                                   7    
HELIX    6   6 VAL B  231  ALA B  244  5                                  14    
HELIX    7   7 ASP C    3  PHE C    6  5                                   4    
HELIX    8   8 LEU C   48  ILE C   54  1                                   7    
HELIX    9   9 ASP D    3  PHE D    6  5                                   4    
HELIX   10  10 LEU D   48  CYS D   55  1                                   8    
SHEET    1   A 7 GLN A  81  ASN A  84  0                                        
SHEET    2   A 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    3   A 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    4   A 7 HIS A  40  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    7   A 7 ALA A  85  THR A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 6 GLN A 156  PRO A 161  0                                        
SHEET    2   B 6 GLU A 135  GLY A 140 -1  N  GLY A 140   O  GLN A 156           
SHEET    3   B 6 PRO A 198  CYS A 201 -1  N  VAL A 200   O  LEU A 137           
SHEET    4   B 6 GLN A 204  TRP A 215 -1  N  GLY A 211   O  VAL A 199           
SHEET    5   B 6 GLY A 226  LYS A 230 -1  N  THR A 229   O  ILE A 212           
SHEET    6   B 6 MET A 180  VAL A 183 -1  N  VAL A 183   O  GLY A 226           
SHEET    1   C 7 GLN B  81  ASN B  84  0                                        
SHEET    2   C 7 GLN B  64  LEU B  67 -1  N  LEU B  67   O  GLN B  81           
SHEET    3   C 7 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SHEET    4   C 7 HIS B  40  ASN B  48 -1  N  GLY B  44   O  VAL B  31           
SHEET    5   C 7 TRP B  51  SER B  54 -1  N  VAL B  53   O  SER B  45           
SHEET    6   C 7 MET B 104  LEU B 108 -1  N  ILE B 106   O  VAL B  52           
SHEET    7   C 7 ALA B  85  THR B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    1   D 2 GLU B 135  GLY B 140  0                                        
SHEET    2   D 2 GLN B 156  PRO B 161 -1  N  ALA B 160   O  CYS B 136           
SHEET    1   E 4 MET B 180  VAL B 183  0                                        
SHEET    2   E 4 GLY B 226  LYS B 230 -1  N  TYR B 228   O  ILE B 181           
SHEET    3   E 4 GLN B 204  TRP B 215 -1  N  TRP B 215   O  VAL B 227           
SHEET    4   E 4 PRO B 198  CYS B 201 -1  N  CYS B 201   O  GLN B 204           
SHEET    1   F 2 ILE C  18  ASN C  24  0                                        
SHEET    2   F 2 GLN C  29  TYR C  35 -1  N  TYR C  35   O  ILE C  18           
SHEET    1   G 2 ILE D  18  ASN D  24  0                                        
SHEET    2   G 2 GLN D  29  TYR D  35 -1  N  TYR D  35   O  ILE D  18           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.02  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.02  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   7 CYS B   22    CYS B  157                          1555   1555  2.42  
SSBOND   8 CYS B  128    CYS B  232                          1555   1555  2.40  
SSBOND   9 CYS B  136    CYS B  201                          1555   1555  2.37  
SSBOND  10 CYS B  168    CYS B  182                          1555   1555  2.47  
SSBOND  11 CYS B  191    CYS B  220                          1555   1555  2.39  
SSBOND  12 CYS C    5    CYS C   55                          1555   1555  2.03  
SSBOND  13 CYS C   14    CYS C   38                          1555   1555  2.04  
SSBOND  14 CYS C   30    CYS C   51                          1555   1555  2.03  
SSBOND  15 CYS D   14    CYS D   38                          1555   1555  2.41  
LINK        CA    CA A1007                 O   ASN A  72     1555   1555  2.20  
LINK        CA    CA A1007                 O   VAL A  75     1555   1555  2.10  
LINK        CA    CA B4007                 OE1 GLU B  70     1555   1555  2.10  
LINK        CA    CA B4007                 O   ASN B  72     1555   1555  2.19  
LINK        CA    CA B4007                 O   VAL B  75     1555   1555  2.12  
LINK        CA    CA B4007                 OE2 GLU B  80     1555   1555  2.11  
LINK        CA    CA A1007                 OE1 GLU A  77     1555   1555  2.40  
LINK        CA    CA A1007                 OE2 GLU A  80     1555   1555  2.46  
LINK        CA    CA A1007                 O   HOH A2053     1555   1555  3.25  
LINK        CA    CA A1007                 OE1 GLU A  70     1555   1555  2.98  
LINK        CA    CA B4007                 OE1 GLU B  77     1555   1555  2.87  
LINK        CA    CA B4007                 O   HOH B5053     1555   1555  3.04  
SITE     1 AC1  5 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  5 GLU A  80                                                     
SITE     1 AC2  6 GLU B  70  ASN B  72  VAL B  75  GLU B  77                    
SITE     2 AC2  6 GLU B  80  HOH B5053                                          
CRYST1   41.900   96.200  137.700  90.00  90.00  90.00 P 21 21 21    8          
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      0.023866  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010395  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007262        0.00000                         
MTRIX1   1  0.999900 -0.011400  0.000800        6.31810    1                    
MTRIX2   1  0.011300  0.975500 -0.219900      -39.90060    1                    
MTRIX3   1  0.001700  0.219900  0.975500       -7.80590    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system