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Database: PDB
Entry: 1FAK
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HEADER    BLOOD CLOTTING                          28-DEC-98   1FAK              
TITLE     HUMAN TISSUE FACTOR COMPLEXED WITH COAGULATION FACTOR VIIA            
TITLE    2 INHIBITED WITH A BPTI-MUTANT                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (BLOOD COAGULATION FACTOR VIIA);                   
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: LIGHT CHAIN;                                               
COMPND   5 EC: 3.4.21.21;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN (BLOOD COAGULATION FACTOR VIIA);                   
COMPND   9 CHAIN: H;                                                            
COMPND  10 FRAGMENT: HEAVY CHAIN;                                               
COMPND  11 EC: 3.4.21.21;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PROTEIN (SOLUBLE TISSUE FACTOR);                           
COMPND  15 CHAIN: T;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: PROTEIN (5L15);                                            
COMPND  19 CHAIN: I;                                                            
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: KIDNEY CELLS (BHK);                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: KIDNEY CELLS (BHK);                     
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 SYNTHETIC: YES;                                                      
SOURCE  25 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
KEYWDS    COMPLEX(SERINE PROTEASE/COFACTOR/LIGAND), BLOOD COAGULATION,          
KEYWDS   2 SERINE PROTEASE, COMPLEX, CO-FACTOR, RECEPTOR ENZYME,                
KEYWDS   3 INHIBITOR, GLA, EGF, COMPLEX (SERINE                                 
KEYWDS   4 PROTEASE/COFACTOR/LIGAND), BLOOD CLOTTING                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ZHANG,R.ST CHARLES,A.TULINSKY                                       
REVDAT   3   24-FEB-09 1FAK    1       VERSN                                    
REVDAT   2   10-JAN-01 1FAK    1       SOURCE REMARK MODRES                     
REVDAT   1   03-DEC-99 1FAK    0                                                
JRNL        AUTH   E.ZHANG,R.ST CHARLES,A.TULINSKY                              
JRNL        TITL   STRUCTURE OF EXTRACELLULAR TISSUE FACTOR COMPLEXED           
JRNL        TITL 2 WITH FACTOR VIIA INHIBITED WITH A BPTI MUTANT.               
JRNL        REF    J.MOL.BIOL.                   V. 285  2089 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9925787                                                      
JRNL        DOI    10.1006/JMBI.1998.2452                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 49719                          
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 + TEST SET) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4716                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 340                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.022 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.041 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.054 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.013 ; 0.015               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.219 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.195 ; 0.600               
REMARK   3    MULTIPLE TORSION                (A) : 0.238 ; 0.600               
REMARK   3    H-BOND (X...Y)                  (A) : 0.247 ; 0.600               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.100 ; 1.500               
REMARK   3    STAGGERED                 (DEGREES) : 21.000; 20.000              
REMARK   3    TRANSVERSE                (DEGREES) : 20.900; 25.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.450 ; 1.500               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.140 ; 2.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 3.830 ; 3.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 4.920 ; 5.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FAK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB007343.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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) : 0.89                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 2.350                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.6                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.65000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.65000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       31.74500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       95.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       31.74500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       95.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       87.65000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       31.74500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       95.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       87.65000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       31.74500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       95.00000            
REMARK 290   SMTRY3   8  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T, I                            
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     ALA L     1                                                      
REMARK 465     ASN L     2                                                      
REMARK 465     ALA L     3                                                      
REMARK 465     PHE L     4                                                      
REMARK 465     LEU L     5                                                      
REMARK 465     CGU L     6                                                      
REMARK 465     CGU L     7                                                      
REMARK 465     LEU L     8                                                      
REMARK 465     ARG L     9                                                      
REMARK 465     PRO L    10                                                      
REMARK 465     GLY L    11                                                      
REMARK 465     SER L    12                                                      
REMARK 465     LEU L    13                                                      
REMARK 465     CGU L    14                                                      
REMARK 465     ARG L    15                                                      
REMARK 465     CGU L    16                                                      
REMARK 465     CYS L    17                                                      
REMARK 465     LYS L    18                                                      
REMARK 465     CGU L    19                                                      
REMARK 465     CGU L    20                                                      
REMARK 465     GLN L    21                                                      
REMARK 465     CYS L    22                                                      
REMARK 465     SER L    23                                                      
REMARK 465     PHE L    24                                                      
REMARK 465     CGU L    25                                                      
REMARK 465     CGU L    26                                                      
REMARK 465     ALA L    27                                                      
REMARK 465     ARG L    28                                                      
REMARK 465     CGU L    29                                                      
REMARK 465     ILE L    30                                                      
REMARK 465     PHE L    31                                                      
REMARK 465     LYS L    32                                                      
REMARK 465     ASP L    33                                                      
REMARK 465     ALA L    34                                                      
REMARK 465     CGU L    35                                                      
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     VAL H   170E                                                     
REMARK 465     GLY H   170F                                                     
REMARK 465     ASP H   170G                                                     
REMARK 465     ASN T     5                                                      
REMARK 465     GLY T    81                                                      
REMARK 465     ASN T    82                                                      
REMARK 465     VAL T    83                                                      
REMARK 465     GLU T    84                                                      
REMARK 465     SER T    85                                                      
REMARK 465     THR T    86                                                      
REMARK 465     GLY T    87                                                      
REMARK 465     SER T    88                                                      
REMARK 465     ALA T    89                                                      
REMARK 465     VAL T   119                                                      
REMARK 465     GLY T   120                                                      
REMARK 465     THR T   121                                                      
REMARK 465     LYS T   159                                                      
REMARK 465     SER T   160                                                      
REMARK 465     SER T   161                                                      
REMARK 465     SER T   162                                                      
REMARK 465     SER T   163                                                      
REMARK 465     ASP T   180                                                      
REMARK 465     LYS T   181                                                      
REMARK 465     GLY T   182                                                      
REMARK 465     GLU T   183                                                      
REMARK 465     ASN T   184                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU I     7     NZ   LYS I    41              2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER H  92   CB    SER H  92   OG      0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG L  36   CD  -  NE  -  CZ  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ARG L  36   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG L  36   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ASP L  46   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG L  79   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG L  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    HIS L  84   CA  -  CB  -  CG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    GLU L  94   CG  -  CD  -  OE2 ANGL. DEV. =  12.2 DEGREES          
REMARK 500    GLU L  99   CG  -  CD  -  OE1 ANGL. DEV. =  13.2 DEGREES          
REMARK 500    GLU L  99   CG  -  CD  -  OE2 ANGL. DEV. = -13.8 DEGREES          
REMARK 500    TYR L 101   CB  -  CG  -  CD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    TYR L 101   CB  -  CG  -  CD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    CYS L 112   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG L 113   CA  -  CB  -  CG  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ASP L 123   CB  -  CG  -  OD1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    CYS L 135   CA  -  CB  -  SG  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ALA H  39   N   -  CA  -  CB  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ALA H  39   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    SER H  54   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG H  62   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG H  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    GLU H  80   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG H  83   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG H  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    VAL H  85   CA  -  CB  -  CG1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ASN H 100   CB  -  CA  -  C   ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ARG H 107   CD  -  NE  -  CZ  ANGL. DEV. =  25.9 DEGREES          
REMARK 500    ARG H 107   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG H 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP H 116   CB  -  CG  -  OD1 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ASP H 116   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    GLU H 125   OE1 -  CD  -  OE2 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG H 126   CD  -  NE  -  CZ  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG H 126   NE  -  CZ  -  NH1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ARG H 134   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    THR H 151   CA  -  CB  -  CG2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG H 170C  CD  -  NE  -  CZ  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG H 170C  NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    PHE H 181   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    TYR H 184   CB  -  CG  -  CD2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    SER H 185   N   -  CA  -  CB  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    SER H 185   CA  -  CB  -  OG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ASP H 186   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG H 204   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    GLN H 217   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    GLN H 217   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG H 243   CD  -  NE  -  CZ  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG H 243   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG H 243   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG H 247   CD  -  NE  -  CZ  ANGL. DEV. =  12.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 ANGLE DEVIATIONS.                             
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    GLN L 100     -104.54   -115.92                                   
REMARK 500    LYS H  24      117.94    -37.83                                   
REMARK 500    CYS H  27       53.77   -142.95                                   
REMARK 500    ASN H  48     -176.24   -177.94                                   
REMARK 500    SER H  54     -157.89   -148.80                                   
REMARK 500    HIS H  71      -57.82   -142.23                                   
REMARK 500    PRO H 170I     174.03    -57.21                                   
REMARK 500    ASP H 189     -177.10   -171.37                                   
REMARK 500    ARG H 204       49.43     38.74                                   
REMARK 500    SER H 214      -75.68   -126.52                                   
REMARK 500    ASN T  11       63.56     61.66                                   
REMARK 500    PHE T  19       -6.58     77.33                                   
REMARK 500    PRO T  92      167.62    -48.54                                   
REMARK 500    ASN I  44      116.11   -164.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG H 134         0.10    SIDE_CHAIN                              
REMARK 500    ARG H 230         0.08    SIDE_CHAIN                              
REMARK 500    ARG I  53         0.10    SIDE_CHAIN                              
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 H 258  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  70   OE1                                                    
REMARK 620 2 GLU H  75   O   139.1                                              
REMARK 620 3 ASP H  72   O    78.7  67.7                                        
REMARK 620 4 HOH H 281   O    81.2 111.0  75.8                                  
REMARK 620 5 HOH H 295   O    84.0  69.2  82.0 155.3                            
REMARK 620 6 GLU H  80   OE2 111.2 102.9 170.1 105.7  98.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L  63   OD2                                                    
REMARK 620 2 HOH L 669   O    85.0                                              
REMARK 620 3 GLN L  64   O    92.6  84.1                                        
REMARK 620 4 GLY L  47   O   106.9 111.2 155.8                                  
REMARK 620 5 ASP L  63   OD1  50.2 131.2  80.3 101.0                            
REMARK 620 6 GLN L  49   OE1 118.8 146.8  72.8  85.1  68.7                      
REMARK 620 7 ASP L  46   OD2 162.7  77.7  86.4  79.2 145.9  77.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC L 600                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC L 601                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 602                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 258                  
DBREF  1FAK L    1   152  UNP    P08709   FA7_HUMAN       61    212             
DBREF  1FAK H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  1FAK T    5   210  UNP    P13726   TF_HUMAN        37    242             
DBREF  1FAK I    1    55  UNP    P00974   BPT1_BOVIN      37     90             
SEQADV 1FAK ASP I   11  UNP  P00974    THR    46 CONFLICT                       
SEQADV 1FAK ARG I   15  UNP  P00974    LYS    50 CONFLICT                       
SEQADV 1FAK LEU I   17  UNP  P00974    ARG    52 CONFLICT                       
SEQADV 1FAK HIS I   18  UNP  P00974    ILE    53 CONFLICT                       
SEQADV 1FAK LEU I   19  UNP  P00974    ILE    54 CONFLICT                       
SEQADV 1FAK TYR I   34  UNP  P00974    VAL    69 CONFLICT                       
SEQADV 1FAK LEU I   39  UNP  P00974    ARG    74 CONFLICT                       
SEQADV 1FAK GLU I   46  UNP  P00974    LYS    81 CONFLICT                       
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  206  ASN THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER THR          
SEQRES   2 T  206  ASN PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO VAL          
SEQRES   3 T  206  ASN GLN VAL TYR THR VAL GLN ILE SER THR LYS SER GLY          
SEQRES   4 T  206  ASP TRP LYS SER LYS CYS PHE TYR THR THR ASP THR GLU          
SEQRES   5 T  206  CYS ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS GLN          
SEQRES   6 T  206  THR TYR LEU ALA ARG VAL PHE SER TYR PRO ALA GLY ASN          
SEQRES   7 T  206  VAL GLU SER THR GLY SER ALA GLY GLU PRO LEU TYR GLU          
SEQRES   8 T  206  ASN SER PRO GLU PHE THR PRO TYR LEU GLU THR ASN LEU          
SEQRES   9 T  206  GLY GLN PRO THR ILE GLN SER PHE GLU GLN VAL GLY THR          
SEQRES  10 T  206  LYS VAL ASN VAL THR VAL GLU ASP GLU ARG THR LEU VAL          
SEQRES  11 T  206  ARG ARG ASN ASN THR PHE LEU SER LEU ARG ASP VAL PHE          
SEQRES  12 T  206  GLY LYS ASP LEU ILE TYR THR LEU TYR TYR TRP LYS SER          
SEQRES  13 T  206  SER SER SER GLY LYS LYS THR ALA LYS THR ASN THR ASN          
SEQRES  14 T  206  GLU PHE LEU ILE ASP VAL ASP LYS GLY GLU ASN TYR CYS          
SEQRES  15 T  206  PHE SER VAL GLN ALA VAL ILE PRO SER ARG THR VAL ASN          
SEQRES  16 T  206  ARG LYS SER THR ASP SER PRO VAL GLU CYS MET                  
SEQRES   1 I   55  ALA PRO ASP PHE CYS LEU GLU PRO PRO TYR ASP GLY PRO          
SEQRES   2 I   55  CYS ARG ALA LEU HIS LEU ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 I   55  ALA GLY LEU CYS GLN THR PHE TYR TYR GLY GLY CYS LEU          
SEQRES   4 I   55  ALA LYS ARG ASN ASN PHE GLU SER ALA GLU ASP CYS MET          
SEQRES   5 I   55  ARG THR CYS                                                  
MODRES 1FAK SER L   52  SER  GLYCOSYLATION SITE                                 
MODRES 1FAK SER L   60  SER  GLYCOSYLATION SITE                                 
HET    GLC  L 600      11                                                       
HET    FUC  L 601      10                                                       
HET     CA  L 602       1                                                       
HET     CA  H 258       1                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   5  GLC    C6 H12 O6                                                    
FORMUL   6  FUC    C6 H12 O5                                                    
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL   9  HOH   *340(H2 O)                                                    
HELIX    1   1 THR L   37  TYR L   44  1                                   8    
HELIX    2   2 GLN L   49  SER L   52  5                                   4    
HELIX    3   3 GLU L   94  GLY L   97  5                                   4    
HELIX    4   4 ALA H   56  PHE H   59  5                                   4    
HELIX    5   5 ARG H  126  ARG H  129B 1                                   6    
HELIX    6   6 LEU H  129D PHE H  129F 5                                   3    
HELIX    7   7 THR H  165  GLN H  170A 1                                   7    
HELIX    8   8 VAL H  231  GLN H  233  5                                   3    
HELIX    9   9 ILE H  235  ARG H  243  1                                   9    
HELIX   10  10 THR T   60  LYS T   65  1                                   6    
HELIX   11  11 PRO T  102  GLU T  105  1                                   4    
HELIX   12  12 LEU T  143  ASP T  150  1                                   8    
HELIX   13  13 ASP I    3  LEU I    6  5                                   4    
HELIX   14  14 ALA I   48  ARG I   53  1                                   6    
SHEET    1   A 2 SER L  60  GLN L  64  0                                        
SHEET    2   A 2 SER L  67  PHE L  71 -1  N  PHE L  71   O  SER L  60           
SHEET    1   B 2 TYR L 101  SER L 103  0                                        
SHEET    2   B 2 SER L 111  ARG L 113 -1  N  ARG L 113   O  TYR L 101           
SHEET    1   C 2 TYR L 118  LEU L 120  0                                        
SHEET    2   C 2 CYS L 127  PRO L 129 -1  N  THR L 128   O  SER L 119           
SHEET    1   D 4 GLN H  81  ARG H  84  0                                        
SHEET    2   D 4 LEU H  64  LEU H  68 -1  N  LEU H  68   O  GLN H  81           
SHEET    3   D 4 GLN H  30  VAL H  35 -1  N  LEU H  34   O  ILE H  65           
SHEET    4   D 4 ALA H  39  THR H  45 -1  N  GLY H  44   O  VAL H  31           
SHEET    1   E 4 TRP H  51  SER H  54  0                                        
SHEET    2   E 4 ALA H 104  LEU H 108 -1  N  LEU H 106   O  VAL H  52           
SHEET    3   E 4 VAL H  85  PRO H  91 -1  N  ILE H  89   O  LEU H 105           
SHEET    4   E 4 LEU H 251  ALA H 254  1  N  LEU H 252   O  VAL H  88           
SHEET    1   F 2 PHE H 135  GLY H 140  0                                        
SHEET    2   F 2 MET H 156  PRO H 161 -1  N  VAL H 160   O  SER H 136           
SHEET    1   G 4 MET H 180  ALA H 183  0                                        
SHEET    2   G 4 GLY H 226  ARG H 230 -1  N  TYR H 228   O  PHE H 181           
SHEET    3   G 4 THR H 206  TRP H 215 -1  N  TRP H 215   O  VAL H 227           
SHEET    4   G 4 PRO H 198  TYR H 203 -1  N  TYR H 203   O  THR H 206           
SHEET    1   H 3 THR T  13  THR T  17  0                                        
SHEET    2   H 3 LYS T  20  GLU T  24 -1  N  GLU T  24   O  THR T  13           
SHEET    3   H 3 GLU T  56  ASP T  58 -1  N  CYS T  57   O  LEU T  23           
SHEET    1   I 4 LYS T  46  LYS T  48  0                                        
SHEET    2   I 4 GLN T  32  THR T  40 -1  N  ILE T  38   O  LYS T  46           
SHEET    3   I 4 TYR T  71  PRO T  79 -1  N  TYR T  78   O  VAL T  33           
SHEET    4   I 4 LEU T  93  ASN T  96 -1  N  GLU T  95   O  VAL T  75           
SHEET    1   J 3 GLU T 174  ILE T 177  0                                        
SHEET    2   J 3 VAL T 123  VAL T 127 -1  N  VAL T 125   O  PHE T 175           
SHEET    3   J 3 ILE T 113  GLU T 117 -1  N  GLU T 117   O  ASN T 124           
SHEET    1   K 3 CYS T 186  VAL T 192  0                                        
SHEET    2   K 3 ILE T 152  TRP T 158 -1  N  TRP T 158   O  CYS T 186           
SHEET    3   K 3 LYS T 166  THR T 170 -1  N  THR T 170   O  TYR T 153           
SHEET    1   L 2 HIS I  18  ASN I  24  0                                        
SHEET    2   L 2 LEU I  29  TYR I  35 -1  N  TYR I  35   O  HIS I  18           
SSBOND   1 CYS L   50    CYS L   61                          1555   1555  2.01  
SSBOND   2 CYS L   55    CYS L   70                          1555   1555  2.09  
SSBOND   3 CYS L   72    CYS L   81                          1555   1555  2.17  
SSBOND   4 CYS L   91    CYS L  102                          1555   1555  2.05  
SSBOND   5 CYS L   98    CYS L  112                          1555   1555  2.01  
SSBOND   6 CYS L  114    CYS L  127                          1555   1555  2.01  
SSBOND   7 CYS L  135    CYS H  122                          1555   1555  1.91  
SSBOND   8 CYS H   22    CYS H   27                          1555   1555  2.01  
SSBOND   9 CYS H   42    CYS H   58                          1555   1555  2.07  
SSBOND  10 CYS H  168    CYS H  182                          1555   1555  2.05  
SSBOND  11 CYS H  191    CYS H  220                          1555   1555  2.11  
SSBOND  12 CYS T   49    CYS T   57                          1555   1555  2.14  
SSBOND  13 CYS T  186    CYS T  209                          1555   1555  2.08  
SSBOND  14 CYS I    5    CYS I   55                          1555   1555  2.01  
SSBOND  15 CYS I   14    CYS I   38                          1555   1555  2.03  
LINK         C1  GLC L 600                 OG  SER L  52     1555   1555  1.37  
LINK         C1  FUC L 601                 OG  SER L  60     1555   1555  1.42  
LINK        CA    CA H 258                 OE1 GLU H  70     1555   1555  2.52  
LINK        CA    CA H 258                 O   GLU H  75     1555   1555  2.11  
LINK        CA    CA H 258                 O   ASP H  72     1555   1555  2.43  
LINK        CA    CA H 258                 O   HOH H 281     1555   1555  2.38  
LINK        CA    CA H 258                 O   HOH H 295     1555   1555  3.02  
LINK        CA    CA H 258                 OE2 GLU H  80     1555   1555  2.22  
LINK        CA    CA L 602                 OD2 ASP L  63     1555   1555  2.22  
LINK        CA    CA L 602                 O   HOH L 669     1555   1555  1.97  
LINK        CA    CA L 602                 O   GLN L  64     1555   1555  2.55  
LINK        CA    CA L 602                 O   GLY L  47     1555   1555  2.20  
LINK        CA    CA L 602                 OD1 ASP L  63     1555   1555  2.76  
LINK        CA    CA L 602                 OE1 GLN L  49     1555   1555  2.48  
LINK        CA    CA L 602                 OD2 ASP L  46     1555   1555  2.93  
CISPEP   1 PHE H  256    PRO H  257          0         0.79                     
CISPEP   2 GLU T   26    PRO T   27          0         0.73                     
SITE     1 AC1  6 GLN L  49  SER L  52  PRO L  54  HOH L 646                    
SITE     2 AC1  6 HOH L 662  HOH L 668                                          
SITE     1 AC2  2 GLY L  58  SER L  60                                          
SITE     1 AC3  6 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 AC3  6 GLN L  64  HOH L 669                                          
SITE     1 AC4  6 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     2 AC4  6 HOH H 281  HOH H 295                                          
CRYST1   63.490  190.000  175.300  90.00  90.00  90.00 C 2 2 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      0.015750  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005263  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system