GenomeNet

Database: PDB
Entry: 2B7D
LinkDB: 2B7D
Original site: 2B7D 
HEADER    BLOOD CLOTTING                          04-OCT-05   2B7D              
TITLE     FACTOR VIIA INHIBITORS: CHEMICAL OPTIMIZATION, PRECLINICAL            
TITLE    2 PHARMACOKINETICS, PHARMACODYNAMICS, AND EFFICACY IN A BABOON         
TITLE    3 THROMBOSIS MODEL                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: LIGHT CHAIN;                                               
COMPND   5 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, SPCA,             
COMPND   6 PROCONVERTIN, EPTACOG ALFA;                                          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND  10 CHAIN: H;                                                            
COMPND  11 FRAGMENT: HEAVY CHAIN;                                               
COMPND  12 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, SPCA,             
COMPND  13 PROCONVERTIN, EPTACOG ALFA;                                          
COMPND  14 EC: 3.4.21.21;                                                       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: TISSUE FACTOR;                                             
COMPND  18 CHAIN: T;                                                            
COMPND  19 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;  
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 GENE: F7;                                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE  10 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573;                             
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: F7;                                                            
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  19 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE  20 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573;                             
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: F3;                                                            
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SHORT HYDROGEN BOND, BLOOD CLOTTING                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.B.YOUNG,J.MORDENTI,S.TORKELSON,W.D.SHRADER,A.KOLESNIKOV,R.RAI,      
AUTHOR   2 L.LIU,H.HU,E.M.LEAHY,M.J.GREEN,P.A.SPRENGELER,B.A.KATZ,C.YU,         
AUTHOR   3 J.W.JANC,K.C.ELROD,U.M.MARZEC,S.R.HANSON                             
REVDAT   4   11-OCT-17 2B7D    1       REMARK                                   
REVDAT   3   24-FEB-09 2B7D    1       VERSN                                    
REVDAT   2   21-MAR-06 2B7D    1       JRNL                                     
REVDAT   1   14-FEB-06 2B7D    0                                                
JRNL        AUTH   W.B.YOUNG,J.MORDENTI,S.TORKELSON,W.D.SHRADER,A.KOLESNIKOV,   
JRNL        AUTH 2 R.RAI,L.LIU,H.HU,E.M.LEAHY,M.J.GREEN,P.A.SPRENGELER,         
JRNL        AUTH 3 B.A.KATZ,C.YU,J.W.JANC,K.C.ELROD,U.M.MARZEC,S.R.HANSON       
JRNL        TITL   FACTOR VIIA INHIBITORS: CHEMICAL OPTIMIZATION, PRECLINICAL   
JRNL        TITL 2 PHARMACOKINETICS, PHARMACODYNAMICS, AND EFFICACY IN AN       
JRNL        TITL 3 ARTERIAL BABOON THROMBOSIS MODEL.                            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  2037 2006              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   16412633                                                     
JRNL        DOI    10.1016/J.BMCL.2005.12.059                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 38857                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3892                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3874                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 306                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.019                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.980                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2B7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034766.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46266                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-SIGHT, ACCELRYS                                     
REMARK 200 STARTING MODEL: 1DAN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE, 16-18 % PEG 5K MME, PH    
REMARK 280  7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       34.51500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLU L     6                                                      
REMARK 465     GLU 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     GLU L    14                                                      
REMARK 465     ARG L    15                                                      
REMARK 465     GLU L    16                                                      
REMARK 465     CYS L    17                                                      
REMARK 465     LYS L    18                                                      
REMARK 465     GLU L    19                                                      
REMARK 465     GLU L    20                                                      
REMARK 465     GLN L    21                                                      
REMARK 465     CYS L    22                                                      
REMARK 465     SER L    23                                                      
REMARK 465     PHE L    24                                                      
REMARK 465     GLU L    25                                                      
REMARK 465     GLU L    26                                                      
REMARK 465     ALA L    27                                                      
REMARK 465     ARG L    28                                                      
REMARK 465     GLU 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     GLU L    35                                                      
REMARK 465     ARG L    36                                                      
REMARK 465     THR L    37                                                      
REMARK 465     LYS L    38                                                      
REMARK 465     LEU L    39                                                      
REMARK 465     PHE L    40                                                      
REMARK 465     TRP L    41                                                      
REMARK 465     ILE L    42                                                      
REMARK 465     SER L    43                                                      
REMARK 465     TYR L    44                                                      
REMARK 465     SER L    45                                                      
REMARK 465     ASP L    46                                                      
REMARK 465     GLY L    47                                                      
REMARK 465     ASP L    48                                                      
REMARK 465     LYS L   143                                                      
REMARK 465     ARG L   144                                                      
REMARK 465     ASN L   145                                                      
REMARK 465     ALA L   146                                                      
REMARK 465     SER L   147                                                      
REMARK 465     LYS L   148                                                      
REMARK 465     PRO L   149                                                      
REMARK 465     GLN L   150                                                      
REMARK 465     GLY L   151                                                      
REMARK 465     ARG L   152                                                      
REMARK 465     GLY T     2                                                      
REMARK 465     THR T     3                                                      
REMARK 465     THR T     4                                                      
REMARK 465     ASN T     5                                                      
REMARK 465     GLN T   110                                                      
REMARK 465     PRO T   111                                                      
REMARK 465     THR T   112                                                      
REMARK 465     ILE T   113                                                      
REMARK 465     GLN T   114                                                      
REMARK 465     SER T   115                                                      
REMARK 465     PHE T   116                                                      
REMARK 465     GLU T   117                                                      
REMARK 465     GLN T   118                                                      
REMARK 465     VAL T   119                                                      
REMARK 465     GLY T   120                                                      
REMARK 465     THR T   121                                                      
REMARK 465     LYS T   122                                                      
REMARK 465     VAL T   123                                                      
REMARK 465     ASN T   124                                                      
REMARK 465     VAL T   125                                                      
REMARK 465     THR T   126                                                      
REMARK 465     VAL T   127                                                      
REMARK 465     GLU T   128                                                      
REMARK 465     TYR T   156                                                      
REMARK 465     TYR T   157                                                      
REMARK 465     TRP T   158                                                      
REMARK 465     LYS T   159                                                      
REMARK 465     SER T   160                                                      
REMARK 465     SER T   161                                                      
REMARK 465     SER T   162                                                      
REMARK 465     SER T   163                                                      
REMARK 465     GLY T   164                                                      
REMARK 465     LYS T   165                                                      
REMARK 465     LYS T   166                                                      
REMARK 465     THR T   167                                                      
REMARK 465     ALA T   168                                                      
REMARK 465     LYS T   169                                                      
REMARK 465     THR T   170                                                      
REMARK 465     ASN T   171                                                      
REMARK 465     THR T   172                                                      
REMARK 465     ASN T   173                                                      
REMARK 465     GLU T   174                                                      
REMARK 465     PHE T   175                                                      
REMARK 465     LEU T   176                                                      
REMARK 465     ILE T   177                                                      
REMARK 465     ASP T   178                                                      
REMARK 465     VAL T   179                                                      
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 465     TYR T   185                                                      
REMARK 465     CYS T   186                                                      
REMARK 465     PHE T   187                                                      
REMARK 465     PRO T   206                                                      
REMARK 465     VAL T   207                                                      
REMARK 465     GLU T   208                                                      
REMARK 465     CYS T   209                                                      
REMARK 465     MET T   210                                                      
REMARK 465     GLY T   211                                                      
REMARK 465     GLN T   212                                                      
REMARK 465     GLU T   213                                                      
REMARK 465     LYS T   214                                                      
REMARK 465     GLY T   215                                                      
REMARK 465     GLU T   216                                                      
REMARK 465     PHE T   217                                                      
REMARK 465     ARG T   218                                                      
REMARK 465     GLU T   219                                                      
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   O6'  C1B H   258     O    HOH H   391              2.00            
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    CYS L 114   CA    CYS L 114   CB     -0.087                       
REMARK 500    HIS L 115   CG    HIS L 115   ND1    -0.092                       
REMARK 500    CYS H  58   CA    CYS H  58   CB     -0.095                       
REMARK 500    HIS H  71   NE2   HIS H  71   CD2    -0.082                       
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    CYS L  61   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES          
REMARK 500    CYS L 102   CA  -  CB  -  SG  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG L 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    TYR L 118   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP L 123   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    CYS L 135   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    TRP H  29   CG  -  CD1 -  NE1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TRP H  29   CD1 -  NE1 -  CE2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    TRP H  29   NE1 -  CE2 -  CZ2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TRP H  51   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    TRP H  51   CD1 -  NE1 -  CE2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    TRP H  61   CG  -  CD1 -  NE1 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    TRP H  61   CD1 -  NE1 -  CE2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    TRP H  61   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    TRP H  61   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    THR H 115   OG1 -  CB  -  CG2 ANGL. DEV. = -14.3 DEGREES          
REMARK 500    VAL H 129G  N   -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    ARG H 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TRP H 141   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    TRP H 141   CD1 -  NE1 -  CE2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TRP H 141   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG H 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG H 162   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLY H 170F  N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    CYS H 182   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TYR H 184   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    SER H 190   CA  -  CB  -  OG  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    HIS H 199   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES          
REMARK 500    TRP H 207   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    TRP H 207   CD1 -  NE1 -  CE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    TRP H 207   NE1 -  CE2 -  CZ2 ANGL. DEV. =  10.1 DEGREES          
REMARK 500    TRP H 207   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    TRP H 207   CG  -  CD2 -  CE3 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP H 215   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    TRP H 215   CD1 -  NE1 -  CE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    TRP H 215   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    TRP H 215   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG H 230   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    TRP H 237   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    TRP H 237   CD1 -  NE1 -  CE2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    TRP H 237   NE1 -  CE2 -  CZ2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    TRP H 237   NE1 -  CE2 -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG H 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TRP T  14   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    TRP T  14   CD1 -  NE1 -  CE2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    TRP T  14   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    TRP T  25   CG  -  CD1 -  NE1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TRP T  25   CD1 -  NE1 -  CE2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    TRP T  25   NE1 -  CE2 -  CZ2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    TRP T  45   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 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    SER L  52       37.28    -99.58                                   
REMARK 500    SER L  53       69.01     14.09                                   
REMARK 500    ASN L  57       35.20     38.33                                   
REMARK 500    GLN L  64     -159.59   -135.97                                   
REMARK 500    GLN L  66      -41.79    103.40                                   
REMARK 500    PRO L  74      -32.90    -38.02                                   
REMARK 500    CYS L  81       46.05     35.36                                   
REMARK 500    ASP L  86        2.17    -52.73                                   
REMARK 500    GLN L 100      -85.01   -122.74                                   
REMARK 500    LEU H  41      -73.02   -114.86                                   
REMARK 500    THR H  49      -30.42    -33.67                                   
REMARK 500    SER H  54     -157.35   -140.51                                   
REMARK 500    ALA H  56      -36.44    -38.87                                   
REMARK 500    TRP H  61       -6.91    -47.21                                   
REMARK 500    ASN H  63       32.75    -79.18                                   
REMARK 500    HIS H  71      -62.63   -142.96                                   
REMARK 500    ASP H  79      -31.67   -153.61                                   
REMARK 500    ASP H 146      -50.12    -27.88                                   
REMARK 500    LYS H 170D     -69.15    -12.81                                   
REMARK 500    ASP H 189      174.19    179.48                                   
REMARK 500    ASP H 189      173.92    179.48                                   
REMARK 500    SER H 195      139.85    -37.70                                   
REMARK 500    ARG H 204       40.96     39.89                                   
REMARK 500    SER H 214      -67.30   -122.82                                   
REMARK 500    SER H 232      -36.32    -39.64                                   
REMARK 500    PRO H 255      125.44    -32.79                                   
REMARK 500    PHE T  19       -4.44     78.81                                   
REMARK 500    CYS T  49       65.57     31.33                                   
REMARK 500    TYR T  51       58.42     33.18                                   
REMARK 500    SER T  88      -39.22    -35.87                                   
REMARK 500    ALA T  89       35.11    -97.82                                   
REMARK 500    ASN T 137       61.64     11.80                                   
REMARK 500    ASN T 138      -18.89     74.55                                   
REMARK 500    LEU T 143      -39.07    -38.49                                   
REMARK 500    SER T 195       39.58    -81.17                                   
REMARK 500    ASN T 199       62.16     24.66                                   
REMARK 500    SER T 202     -145.79    -91.92                                   
REMARK 500    THR T 203     -162.78   -109.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 NOTE THAT IN THE CRYSTAL A REACEMIC MIXTURE OF THE LIGAND            
REMARK 600 C1B WAS USED. THE PHENOLATE OXYGEN MAKES SHORT HYDROGEN              
REMARK 600 BONDS WITH THE HYDROXYL GROUP OF SER195 AND A WATER.                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C1B H 258                 
DBREF  2B7D L    1   152  UNP    P08709   FA7_HUMAN       61    212             
DBREF  2B7D H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  2B7D T    2   219  UNP    P13726   TF_HUMAN        34    251             
SEQRES   1 L  152  ALA ASN ALA PHE LEU GLU GLU LEU ARG PRO GLY SER LEU          
SEQRES   2 L  152  GLU ARG GLU CYS LYS GLU GLU GLN CYS SER PHE GLU GLU          
SEQRES   3 L  152  ALA ARG GLU ILE PHE LYS ASP ALA GLU ARG THR LYS LEU          
SEQRES   4 L  152  PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER          
SEQRES   5 L  152  SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU          
SEQRES   6 L  152  GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY          
SEQRES   7 L  152  ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS          
SEQRES   8 L  152  VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP          
SEQRES   9 L  152  HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY          
SEQRES  10 L  152  TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR          
SEQRES  11 L  152  VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU LYS          
SEQRES  12 L  152  ARG ASN ALA SER LYS PRO GLN GLY ARG                          
SEQRES   1 H  254  ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO          
SEQRES   2 H  254  TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS          
SEQRES   3 H  254  GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA          
SEQRES   4 H  254  ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU          
SEQRES   5 H  254  ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP          
SEQRES   6 H  254  GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE          
SEQRES   7 H  254  PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE          
SEQRES   8 H  254  ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP          
SEQRES   9 H  254  HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER          
SEQRES  10 H  254  GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER          
SEQRES  11 H  254  GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU          
SEQRES  12 H  254  GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN          
SEQRES  13 H  254  ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO          
SEQRES  14 H  254  ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP          
SEQRES  15 H  254  GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO          
SEQRES  16 H  254  HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY          
SEQRES  17 H  254  ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS          
SEQRES  18 H  254  PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP          
SEQRES  19 H  254  LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL          
SEQRES  20 H  254  LEU LEU ARG ALA PRO PHE PRO                                  
SEQRES   1 T  218  GLY THR THR ASN THR VAL ALA ALA TYR ASN LEU THR TRP          
SEQRES   2 T  218  LYS SER THR ASN PHE LYS THR ILE LEU GLU TRP GLU PRO          
SEQRES   3 T  218  LYS PRO VAL ASN GLN VAL TYR THR VAL GLN ILE SER THR          
SEQRES   4 T  218  LYS SER GLY ASP TRP LYS SER LYS CYS PHE TYR THR THR          
SEQRES   5 T  218  ASP THR GLU CYS ASP LEU THR ASP GLU ILE VAL LYS ASP          
SEQRES   6 T  218  VAL LYS GLN THR TYR LEU ALA ARG VAL PHE SER TYR PRO          
SEQRES   7 T  218  ALA GLY ASN VAL GLU SER THR GLY SER ALA GLY GLU PRO          
SEQRES   8 T  218  LEU TYR GLU ASN SER PRO GLU PHE THR PRO TYR LEU GLU          
SEQRES   9 T  218  THR ASN LEU GLY GLN PRO THR ILE GLN SER PHE GLU GLN          
SEQRES  10 T  218  VAL GLY THR LYS VAL ASN VAL THR VAL GLU ASP GLU ARG          
SEQRES  11 T  218  THR LEU VAL ARG ARG ASN ASN THR PHE LEU SER LEU ARG          
SEQRES  12 T  218  ASP VAL PHE GLY LYS ASP LEU ILE TYR THR LEU TYR TYR          
SEQRES  13 T  218  TRP LYS SER SER SER SER GLY LYS LYS THR ALA LYS THR          
SEQRES  14 T  218  ASN THR ASN GLU PHE LEU ILE ASP VAL ASP LYS GLY GLU          
SEQRES  15 T  218  ASN TYR CYS PHE SER VAL GLN ALA VAL ILE PRO SER ARG          
SEQRES  16 T  218  THR VAL ASN ARG LYS SER THR ASP SER PRO VAL GLU CYS          
SEQRES  17 T  218  MET GLY GLN GLU LYS GLY GLU PHE ARG GLU                      
HET    C1B  H 258      39                                                       
HETNAM     C1B (2R)-2-[5-(5-CARBAMIMIDOYL-1H-BENZOIMIDAZOL-2-YL)-6,2'-          
HETNAM   2 C1B  DIHYDROXY-5'-UREIDOMETHYL-BIPHENYL-3-YL]-SUCCINIC ACID          
FORMUL   4  C1B    C26 H24 N6 O7                                                
FORMUL   5  HOH   *306(H2 O)                                                    
HELIX    1   1 ASP L   86  GLN L   88  5                                   3    
HELIX    2   2 ASN L   93  CYS L   98  5                                   6    
HELIX    3   3 ILE L  138  GLU L  142  5                                   5    
HELIX    4   4 ALA H   55  ASP H   60  5                                   6    
HELIX    5   5 GLU H  125  THR H  129C 1                                   8    
HELIX    6   6 LEU H  129D VAL H  129G 5                                   4    
HELIX    7   7 MET H  164  SER H  170B 1                                   9    
HELIX    8   8 TYR H  234  MET H  242  1                                   9    
HELIX    9   9 LEU T   59  VAL T   64  1                                   6    
HELIX   10  10 THR T  101  THR T  106  1                                   6    
HELIX   11  11 LEU T  143  GLY T  148  1                                   6    
HELIX   12  12 LYS T  149  LEU T  151  5                                   3    
SHEET    1   A 2 SER L  60  ASP L  63  0                                        
SHEET    2   A 2 TYR L  68  PHE L  71 -1  O  PHE L  71   N  SER L  60           
SHEET    1   B 2 PHE L  76  GLU L  77  0                                        
SHEET    2   B 2 THR L  83  HIS L  84 -1  O  THR L  83   N  GLU L  77           
SHEET    1   C 2 TYR L 101  HIS L 105  0                                        
SHEET    2   C 2 THR L 108  ARG L 113 -1  O  ARG L 113   N  TYR L 101           
SHEET    1   D 2 TYR L 118  LEU L 120  0                                        
SHEET    2   D 2 CYS L 127  PRO L 129 -1  O  THR L 128   N  SER L 119           
SHEET    1   E 8 LYS H  20  VAL H  21  0                                        
SHEET    2   E 8 MET H 156  LEU H 163 -1  O  VAL H 157   N  LYS H  20           
SHEET    3   E 8 MET H 180  ALA H 183 -1  O  CYS H 182   N  LEU H 163           
SHEET    4   E 8 GLY H 226  ARG H 230 -1  O  TYR H 228   N  PHE H 181           
SHEET    5   E 8 THR H 206  TRP H 215 -1  N  TRP H 215   O  VAL H 227           
SHEET    6   E 8 PRO H 198  TYR H 203 -1  N  TYR H 203   O  THR H 206           
SHEET    7   E 8 PHE H 135  GLY H 140 -1  N  LEU H 137   O  ALA H 200           
SHEET    8   E 8 MET H 156  LEU H 163 -1  O  MET H 156   N  GLY H 140           
SHEET    1   F 8 LEU H 251  ALA H 254  0                                        
SHEET    2   F 8 GLN H  81  PRO H  91  1  N  VAL H  88   O  LEU H 252           
SHEET    3   F 8 ALA H 104  LEU H 108 -1  O  LEU H 105   N  ILE H  89           
SHEET    4   F 8 TRP H  51  SER H  54 -1  N  VAL H  52   O  LEU H 106           
SHEET    5   F 8 ALA H  39  ASN H  48 -1  N  THR H  45   O  VAL H  53           
SHEET    6   F 8 GLN H  30  VAL H  35 -1  N  VAL H  35   O  ALA H  39           
SHEET    7   F 8 LEU H  64  LEU H  68 -1  O  VAL H  67   N  LEU H  32           
SHEET    8   F 8 GLN H  81  PRO H  91 -1  O  ARG H  83   N  ALA H  66           
SHEET    1   G 3 TYR T  10  THR T  17  0                                        
SHEET    2   G 3 LYS T  20  GLU T  26 -1  O  ILE T  22   N  LYS T  15           
SHEET    3   G 3 GLU T  56  ASP T  58 -1  O  CYS T  57   N  LEU T  23           
SHEET    1   H 4 LYS T  46  THR T  52  0                                        
SHEET    2   H 4 GLN T  32  THR T  40 -1  N  VAL T  36   O  LYS T  48           
SHEET    3   H 4 TYR T  71  PRO T  79 -1  O  PHE T  76   N  THR T  35           
SHEET    4   H 4 LEU T  93  ASN T  96 -1  O  LEU T  93   N  SER T  77           
SHEET    1   I 2 ARG T 131  ARG T 136  0                                        
SHEET    2   I 2 THR T 139  SER T 142 -1  O  LEU T 141   N  THR T 132           
SHEET    1   J 2 ILE T 152  TYR T 153  0                                        
SHEET    2   J 2 ALA T 191  VAL T 192 -1  O  VAL T 192   N  ILE T 152           
SSBOND   1 CYS L   50    CYS L   61                          1555   1555  2.03  
SSBOND   2 CYS L   55    CYS L   70                          1555   1555  2.02  
SSBOND   3 CYS L   72    CYS L   81                          1555   1555  2.03  
SSBOND   4 CYS L   91    CYS L  102                          1555   1555  2.02  
SSBOND   5 CYS L   98    CYS L  112                          1555   1555  2.02  
SSBOND   6 CYS L  114    CYS L  127                          1555   1555  2.04  
SSBOND   7 CYS L  135    CYS H  122                          1555   1555  2.04  
SSBOND   8 CYS H   22    CYS H   27                          1555   1555  2.03  
SSBOND   9 CYS H   42    CYS H   58                          1555   1555  2.01  
SSBOND  10 CYS H  168    CYS H  182                          1555   1555  2.04  
SSBOND  11 CYS H  191    CYS H  220                          1555   1555  2.04  
SSBOND  12 CYS T   49    CYS T   57                          1555   1555  2.06  
CISPEP   1 PHE H  256    PRO H  257          0         7.00                     
CISPEP   2 GLU T   26    PRO T   27          0       -11.75                     
SITE     1 AC1 19 CYS H  42  HIS H  57  ASP H  60  LYS H  60A                   
SITE     2 AC1 19 ASP H 189  SER H 190  CYS H 191  LYS H 192                    
SITE     3 AC1 19 SER H 195  VAL H 213  TRP H 215  GLY H 219                    
SITE     4 AC1 19 CYS H 220  GLY H 226  HOH H 287  HOH H 298                    
SITE     5 AC1 19 HOH H 304  HOH H 385  HOH H 391                               
CRYST1   78.700   69.030   78.190  90.00  89.49  90.00 P 1 21 1      2          
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      0.012706  0.000000 -0.000113        0.00000                         
SCALE2      0.000000  0.014486  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012790        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system