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Database: PDB
Entry: 1XKA
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Original site: 1XKA 
HEADER    BLOOD COAGULATION FACTOR                19-MAR-98   1XKA              
TITLE     FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S)-(3'-     
TITLE    2 AMIDINO-3-BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BLOOD COAGULATION FACTOR XA;                               
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: PROTEOLYTIC CLEAVAGE PRODUCT, GLA DOMAIN;                  
COMPND   5 SYNONYM: STUART FACTOR;                                              
COMPND   6 EC: 3.4.21.6;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BLOOD COAGULATION FACTOR XA;                               
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: PROTEOLYTIC CLEAVAGE PRODUCT, GLA DOMAIN;                  
COMPND  11 SYNONYM: STUART FACTOR;                                              
COMPND  12 EC: 3.4.21.6                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 TISSUE: BLOOD                                                        
KEYWDS    BLOOD COAGULATION FACTOR, SERINE PROTEINASE, EPIDERMAL GROWTH FACTOR  
KEYWDS   2 LIKE DOMAIN                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KAMATA,S.H.KIM                                                      
REVDAT   3   20-JUN-12 1XKA    1       HETNAM VERSN                             
REVDAT   2   24-FEB-09 1XKA    1       VERSN                                    
REVDAT   1   23-MAR-99 1XKA    0                                                
JRNL        AUTH   K.KAMATA,H.KAWAMOTO,T.HONMA,T.IWAMA,S.H.KIM                  
JRNL        TITL   STRUCTURAL BASIS FOR CHEMICAL INHIBITION OF HUMAN BLOOD      
JRNL        TITL 2 COAGULATION FACTOR XA.                                       
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  95  6630 1998              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9618463                                                      
JRNL        DOI    10.1073/PNAS.95.12.6630                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.BRANDSTETTER,A.KUHNE,W.BODE,R.HUBER,W.VON DER SAAL,        
REMARK   1  AUTH 2 K.WIRTHENSOHN,R.A.ENGH                                       
REMARK   1  TITL   X-RAY STRUCTURE OF ACTIVE SITE-INHIBITED CLOTTING FACTOR XA. 
REMARK   1  TITL 2 IMPLICATIONS FOR DRUG DESIGN AND SUBSTRATE RECOGNITION       
REMARK   1  REF    J.BIOL.CHEM.                  V. 271 29988 1996              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.PADMANABHAN,K.P.PADMANABHAN,A.TULINSKY,C.H.PARK,W.BODE,    
REMARK   1  AUTH 2 R.HUBER,D.T.BLANKENSHIP,A.D.CARDIN,W.KISIEL                  
REMARK   1  TITL   STRUCTURE OF HUMAN DES(1-45) FACTOR XA AT 2.2 A RESOLUTION   
REMARK   1  REF    J.MOL.BIOL.                   V. 232   947 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14081                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : 0.287                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1410                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1532                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 167                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2550                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 210                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.10                          
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.60                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.210 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.040 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.970 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.170 ; 2.500                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0086                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14542                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.13500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1HCG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.75000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.70000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.70000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.75000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS L    45                                                      
REMARK 465     ASP L    46                                                      
REMARK 465     GLY L    47                                                      
REMARK 465     ASP L    48                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU L    82     O    HOH C   582     2564     1.97            
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    THR L  52       -7.95    -57.95                                   
REMARK 500    LEU L  65     -118.53   -109.20                                   
REMARK 500    LEU L  73     -139.27    -70.92                                   
REMARK 500    ARG L  86      105.11    -44.16                                   
REMARK 500    GLN L  98     -114.27   -135.19                                   
REMARK 500    LYS L 122      -50.36   -130.38                                   
REMARK 500    ASP C  24      121.64    -34.42                                   
REMARK 500    PHE C  41       -4.31   -142.55                                   
REMARK 500    SER C  48     -176.70   -174.51                                   
REMARK 500    VAL C 213      109.70    -57.63                                   
REMARK 500    SER C 214      -64.17   -100.98                                   
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 C 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  72   O                                                      
REMARK 620 2 GLU C  80   OE2 138.6                                              
REMARK 620 3 ASP C  70   OD1  69.0  97.0                                        
REMARK 620 4 GLN C  75   O    78.3  94.1 141.4                                  
REMARK 620 5 GLU C  77   OE2  79.8  58.8  71.2  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PP C 500                 
DBREF  1XKA L   45   139  UNP    P00742   FA10_HUMAN      85    179             
DBREF  1XKA C   16   245  UNP    P00742   FA10_HUMAN     235    469             
SEQADV 1XKA BHD L   63  UNP  P00742    ASP   103 MODIFIED RESIDUE               
SEQRES   1 L   95  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 L   95  GLN GLY LYS CYS LYS BHD GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 L   95  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 L   95  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 L   95  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 L   95  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 L   95  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 L   95  THR LEU GLU ARG                                              
SEQRES   1 C  235  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 C  235  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 C  235  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 C  235  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 C  235  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 C  235  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 C  235  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 C  235  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 C  235  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 C  235  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 C  235  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 C  235  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 C  235  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 C  235  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 C  235  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 C  235  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 C  235  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 C  235  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 C  235  ARG                                                          
MODRES 1XKA BHD L   63  ASP  (3S)-3-HYDROXY-L-ASPARTIC ACID                     
HET    BHD  L  63       9                                                       
HET     CA  C 501       1                                                       
HET    4PP  C 500      29                                                       
HETNAM     BHD (3S)-3-HYDROXY-L-ASPARTIC ACID                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     4PP (2S)-(3'-AMIDINO-3-BIPHENYL)-5-(4-PYRIDYLAMINO)                  
HETNAM   2 4PP  PENTANOIC ACID                                                  
HETSYN     BHD BETA-HYDROXYASPARTIC ACID                                        
FORMUL   1  BHD    C4 H7 N O5                                                   
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  4PP    C23 H24 N4 O2                                                
FORMUL   5  HOH   *210(H2 O)                                                    
HELIX    1   1 ASP L   92  ASP L   95  5                                   4    
HELIX    2   2 ALA C   56  TYR C   60  5                                   5    
HELIX    3   3 ARG C  125  THR C  131  1                                   7    
HELIX    4   4 ARG C  165  SER C  171  1                                   7    
HELIX    5   5 VAL C  231  ALA C  233  5                                   3    
HELIX    6   6 LEU C  235  LYS C  243  1                                   9    
SHEET    1   A 2 LYS L  60  LYS L  62  0                                        
SHEET    2   A 2 THR L  69  THR L  71 -1  N  THR L  71   O  LYS L  60           
SHEET    1   B 2 PHE L  99  GLU L 102  0                                        
SHEET    2   B 2 VAL L 107  SER L 110 -1  N  SER L 110   O  PHE L  99           
SHEET    1   C 2 TYR L 115  LEU L 117  0                                        
SHEET    2   C 2 CYS L 124  PRO L 126 -1  N  ILE L 125   O  THR L 116           
SHEET    1   D 4 ALA C  81  HIS C  83  0                                        
SHEET    2   D 4 PHE C  64  VAL C  68 -1  N  VAL C  68   O  ALA C  81           
SHEET    3   D 4 GLN C  30  ASN C  35 -1  N  ILE C  34   O  LYS C  65           
SHEET    4   D 4 GLY C  40  THR C  45 -1  N  GLY C  44   O  ALA C  31           
SHEET    1   E 3 TYR C  51  THR C  54  0                                        
SHEET    2   E 3 ALA C 104  LEU C 108 -1  N  LEU C 106   O  ILE C  52           
SHEET    3   E 3 VAL C  85  LYS C  90 -1  N  ILE C  89   O  VAL C 105           
SHEET    1   F 2 THR C 135  GLY C 140  0                                        
SHEET    2   F 2 LYS C 156  PRO C 161 -1  N  VAL C 160   O  GLY C 136           
SHEET    1   G 4 MET C 180  ALA C 183  0                                        
SHEET    2   G 4 GLY C 226  LYS C 230 -1  N  TYR C 228   O  PHE C 181           
SHEET    3   G 4 THR C 206  TRP C 215 -1  N  TRP C 215   O  ILE C 227           
SHEET    4   G 4 PRO C 198  PHE C 203 -1  N  PHE C 203   O  THR C 206           
SSBOND   1 CYS L   50    CYS L   61                          1555   1555  2.04  
SSBOND   2 CYS L   55    CYS L   70                          1555   1555  2.03  
SSBOND   3 CYS L   72    CYS L   81                          1555   1555  2.03  
SSBOND   4 CYS L   89    CYS L  100                          1555   1555  2.04  
SSBOND   5 CYS L   96    CYS L  109                          1555   1555  2.02  
SSBOND   6 CYS L  111    CYS L  124                          1555   1555  2.02  
SSBOND   7 CYS L  132    CYS C  122                          1555   1555  2.03  
SSBOND   8 CYS C   22    CYS C   27                          1555   1555  2.02  
SSBOND   9 CYS C   42    CYS C   58                          1555   1555  2.02  
SSBOND  10 CYS C  168    CYS C  182                          1555   1555  2.02  
SSBOND  11 CYS C  191    CYS C  220                          1555   1555  2.03  
LINK         C   LYS L  62                 N   BHD L  63     1555   1555  1.33  
LINK         C   BHD L  63                 N   GLY L  64     1555   1555  1.33  
LINK        CA    CA C 501                 O   ASN C  72     1555   1555  2.66  
LINK        CA    CA C 501                 OE2 GLU C  80     1555   1555  2.81  
LINK        CA    CA C 501                 OD1 ASP C  70     1555   1555  2.83  
LINK        CA    CA C 501                 O   GLN C  75     1555   1555  2.52  
LINK        CA    CA C 501                 OE2 GLU C  77     1555   1555  3.39  
SITE     1 AC1  5 ASP C  70  ASN C  72  GLN C  75  GLU C  77                    
SITE     2 AC1  5 GLU C  80                                                     
SITE     1 AC2 20 GLU C  97  THR C  98  TYR C  99  PHE C 174                    
SITE     2 AC2 20 ASP C 189  ALA C 190  GLN C 192  SER C 195                    
SITE     3 AC2 20 TRP C 215  GLY C 216  GLY C 218  CYS C 220                    
SITE     4 AC2 20 GLY C 226  HOH C 517  HOH C 519  HOH C 578                    
SITE     5 AC2 20 HOH C 583  GLN L  56  LYS L  79  ASN L  80                    
CRYST1   61.500   65.800   81.400  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016260  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015198  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012285        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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