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Database: PDB
Entry: 2VH0
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Original site: 2VH0 
HEADER    HYDROLASE                               16-NOV-07   2VH0              
TITLE     STRUCTURE AND PROPERTY BASED DESIGN OF FACTOR XA INHIBITORS:BIARYL    
TITLE    2 PYRROLIDIN-2-ONES INCORPORATING BASIC HETEROCYCLIC MOTIFS            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIVATED FACTOR XA HEAVY CHAIN;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ACTIVATED DESGLA, RESIDUES 235-488;                        
COMPND   5 SYNONYM: STUART FACTOR, STUART-PROWER FACTOR;                        
COMPND   6 EC: 3.4.21.6;                                                        
COMPND   7 OTHER_DETAILS: DISULPHIDE LINKED TO OTHER CHAIN;                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ACTIVATED FACTOR XA LIGHT CHAIN;                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: ACTIVATED DESGLA, RESIDUES 46-179;                         
COMPND  12 SYNONYM: STUART FACTOR, STUART-PROWER FACTOR;                        
COMPND  13 EC: 3.4.21.6;                                                        
COMPND  14 OTHER_DETAILS: DISULPHIDE LINKED TO OTHER CHAIN                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 OTHER_DETAILS: PURCHASED FROM ENZYME RESEARCH LABS. ISOLATED FROM    
SOURCE   6 HUMAN BLOOD;                                                         
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 OTHER_DETAILS: PURCHASED FROM ENZYME RESEARCH LABS. ISOLATED FROM    
SOURCE  12 HUMAN BLOOD                                                          
KEYWDS    SERINE PROTEASE, EGF-LIKE DOMAIN, BLOOD COAGULATION, POLYMORPHISM,    
KEYWDS   2 GLYCOPROTEIN, HYDROXYLATION, GAMMA-CARBOXYGLUTAMIC ACID, CALCIUM,    
KEYWDS   3 ZYMOGEN, COMPLEX, PROTEASE, HYDROLASE, CLEAVAGE ON PAIR OF BASIC     
KEYWDS   4 RESIDUES                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.YOUNG,A.D.BORTHWICK,D.BROWN,C.L.BURNS-KURTIS,M.CAMPBELL,C.CHAN,   
AUTHOR   2 M.CHARBAUT,M.A.CONVERY,H.DIALLO,E.HORTENSE,W.R.IRVING,H.A.KELLY,     
AUTHOR   3 N.P.KING,S.KLEANTHOUS,A.M.MASON,A.J.PATEMAN,A.PATIKIS,I.L.PINTO,     
AUTHOR   4 D.R.POLLARD,S.SENGER,G.P.SHAH,J.R.TOOMEY,N.S.WATSON,H.E.WESTON,      
AUTHOR   5 P.ZHOU                                                               
REVDAT   4   08-MAY-19 2VH0    1       REMARK                                   
REVDAT   3   23-JAN-19 2VH0    1       JRNL   FORMUL                            
REVDAT   2   24-FEB-09 2VH0    1       VERSN                                    
REVDAT   1   25-NOV-08 2VH0    0                                                
JRNL        AUTH   R.J.YOUNG,A.D.BORTHWICK,D.BROWN,C.L.BURNS-KURTIS,M.CAMPBELL, 
JRNL        AUTH 2 C.CHAN,M.CHARBAUT,M.A.CONVERY,H.DIALLO,E.HORTENSE,           
JRNL        AUTH 3 W.R.IRVING,H.A.KELLY,N.P.KING,S.KLEANTHOUS,A.M.MASON,        
JRNL        AUTH 4 A.J.PATEMAN,A.N.PATIKIS,I.L.PINTO,D.R.POLLARD,S.SENGER,      
JRNL        AUTH 5 G.P.SHAH,J.R.TOOMEY,N.S.WATSON,H.E.WESTON,P.ZHOU             
JRNL        TITL   STRUCTURE AND PROPERTY BASED DESIGN OF FACTOR XA INHIBITORS: 
JRNL        TITL 2 BIARYL PYRROLIDIN-2-ONES INCORPORATING BASIC HETEROCYCLIC    
JRNL        TITL 3 MOTIFS.                                                      
JRNL        REF    BIOORG. MED. CHEM. LETT.      V.  18    28 2008              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   18053714                                                     
JRNL        DOI    10.1016/J.BMCL.2007.11.019                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0006                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 33755                          
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 + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1779                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2442                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2226                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 232                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.88000                                              
REMARK   3    B22 (A**2) : -1.79000                                             
REMARK   3    B33 (A**2) : 0.91000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.072         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.170         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2348 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3168 ; 1.650 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   288 ; 3.984 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;27.436 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   401 ;10.912 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;17.603 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   335 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1785 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   994 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1604 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   199 ; 0.139 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1471 ; 1.940 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2289 ; 3.135 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1001 ; 4.227 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   879 ; 6.175 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2VH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290034448.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.85                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35548                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
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: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION WAS CARRIED OUT USING    
REMARK 280  THE HANGING DROP VAPOUR DIFFUSION METHOD IN 2UL DROPS CONTAINING    
REMARK 280  A 1:1 MIXTURE OF PROTEIN AND WELL SOLUTION. WELL SOLUTION           
REMARK 280  CONTAINED 16-20% PEG 6K, 50MM MES-NAOH (PH5.7-6.0), 5MM CACL2       
REMARK 280  AND 50MM NACL., PH 5.85, VAPOR DIFFUSION, HANGING DROP              
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       28.27100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.32850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.07800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.32850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.27100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.07800            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     ARG A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     LEU A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     ALA A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     SER A   252                                                      
REMARK 465     HIS A   253                                                      
REMARK 465     ALA A   254                                                      
REMARK 465     PRO A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     VAL A   257                                                      
REMARK 465     ILE A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     SER A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     LEU A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     GLU B   -82                                                      
REMARK 465     GLU B   -81                                                      
REMARK 465     MET B   -80                                                      
REMARK 465     LYS B   -79                                                      
REMARK 465     LYS B   -78                                                      
REMARK 465     GLY B   -77                                                      
REMARK 465     HIS B   -76                                                      
REMARK 465     LEU B   -75                                                      
REMARK 465     GLU B   -74                                                      
REMARK 465     ARG B   -73                                                      
REMARK 465     GLU B   -72                                                      
REMARK 465     CYS B   -71                                                      
REMARK 465     MET B   -70                                                      
REMARK 465     GLU B   -69                                                      
REMARK 465     GLU B   -68                                                      
REMARK 465     THR B   -67                                                      
REMARK 465     CYS B   -66                                                      
REMARK 465     SER B   -65                                                      
REMARK 465     TYR B   -64                                                      
REMARK 465     GLU B   -63                                                      
REMARK 465     GLU B   -62                                                      
REMARK 465     ALA B   -61                                                      
REMARK 465     ARG B   -60                                                      
REMARK 465     GLU B   -59                                                      
REMARK 465     VAL B   -58                                                      
REMARK 465     PHE B   -57                                                      
REMARK 465     GLU B   -56                                                      
REMARK 465     ASP B   -55                                                      
REMARK 465     SER B   -54                                                      
REMARK 465     ASP B   -53                                                      
REMARK 465     LYS B   -52                                                      
REMARK 465     THR B   -51                                                      
REMARK 465     ASN B   -50                                                      
REMARK 465     GLU B   -49                                                      
REMARK 465     PHE B   -48                                                      
REMARK 465     TRP B   -47                                                      
REMARK 465     ASN B   -46                                                      
REMARK 465     LYS B   -45                                                      
REMARK 465     TYR B   -44                                                      
REMARK 465     LYS B   -43                                                      
REMARK 465     ASP B   -42                                                      
REMARK 465     GLY B   -41                                                      
REMARK 465     ASP B   -40                                                      
REMARK 465     GLN B   -39                                                      
REMARK 465     CYS B   -38                                                      
REMARK 465     GLU B   -37                                                      
REMARK 465     THR B   -36                                                      
REMARK 465     SER B   -35                                                      
REMARK 465     PRO B   -34                                                      
REMARK 465     CYS B   -33                                                      
REMARK 465     GLN B   -32                                                      
REMARK 465     ASN B   -31                                                      
REMARK 465     GLN B   -30                                                      
REMARK 465     GLY B   -29                                                      
REMARK 465     LYS B   -28                                                      
REMARK 465     CYS B   -27                                                      
REMARK 465     LYS B   -26                                                      
REMARK 465     ASP B   -25                                                      
REMARK 465     GLY B   -24                                                      
REMARK 465     LEU B   -23                                                      
REMARK 465     GLY B   -22                                                      
REMARK 465     GLU B   -21                                                      
REMARK 465     TYR B   -20                                                      
REMARK 465     THR B   -19                                                      
REMARK 465     CYS B   -18                                                      
REMARK 465     THR B   -17                                                      
REMARK 465     CYS B   -16                                                      
REMARK 465     LEU B   -15                                                      
REMARK 465     GLU B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     PHE B   -12                                                      
REMARK 465     GLU B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     LYS B    -9                                                      
REMARK 465     ASN B    -8                                                      
REMARK 465     CYS B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     PHE B    -4                                                      
REMARK 465     THR B    -3                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     ARG B    51                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A 244    OG1  CG2                                            
REMARK 470     ARG B  -2    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  -1    CG   CD   CE   NZ                                   
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    ARG A 115     -175.09   -175.78                                   
REMARK 500    LEU B   0     -128.14     46.49                                   
REMARK 500    GLN B  10     -111.84   -127.08                                   
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 A1245  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  72   O                                                      
REMARK 620 2 HOH A2033   O    85.2                                              
REMARK 620 3 GLN A  75   O    87.2  84.0                                        
REMARK 620 4 ASP A  70   OD1  85.4  70.8 154.2                                  
REMARK 620 5 HOH A2034   O    87.7 150.9 123.8  80.5                            
REMARK 620 6 GLU A  80   OE2 172.8 101.9  92.7  97.6  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1246  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 224   O                                                      
REMARK 620 2 TYR A 185   O    86.8                                              
REMARK 620 3 ASP A 185A  O   113.9  81.6                                        
REMARK 620 4 HOH A2162   O    68.7  89.0 170.0                                  
REMARK 620 5 HOH A2160   O   162.6  95.1  83.5  94.1                            
REMARK 620 6 ARG A 222   O    95.3 168.7  87.4 102.1  86.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1245                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1246                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSI A1247                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2J34   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 1WU1   RELATED DB: PDB                                   
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 4 -[(5-CHLOROINDOL-2-YL)     
REMARK 900 SULFONYL]-2-(2- METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN -2-YL]   
REMARK 900 CARBONYL]PIPERAZINE                                                  
REMARK 900 RELATED ID: 2BQ7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 43                    
REMARK 900 RELATED ID: 1IOE   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55532                    
REMARK 900 RELATED ID: 1F0S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH      
REMARK 900 RPR208707                                                            
REMARK 900 RELATED ID: 1NFW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH       
REMARK 900 RPR209685                                                            
REMARK 900 RELATED ID: 1XKA   RELATED DB: PDB                                   
REMARK 900 FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S) -(3'-   
REMARK 900 AMIDINO-3- BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID              
REMARK 900 RELATED ID: 2GD4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANTITHROMBIN-S195A FACTOR XA-               
REMARK 900 PENTASACCHARIDE COMPLEX                                              
REMARK 900 RELATED ID: 1F0R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH      
REMARK 900 RPR208815                                                            
REMARK 900 RELATED ID: 1MSX   RELATED DB: PDB                                   
REMARK 900 HUMAN FACTOR XA COMPLEXED WITH 2-[3-(15N- AMINO-15N-IMINO-13C-       
REMARK 900 METHYL)PHENOXY]-6-[3 -(15N-AMINO-13C-METHYL)PHENOXY]-3,5- DIFLUORO-  
REMARK 900 4-METHYLPYRIDINE (ZK-806299), BINDING MODELFROM DOUBLE REDOR NMR     
REMARK 900 AND MD SIMULATIONS.                                                  
REMARK 900 RELATED ID: 1LPG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 79.                         
REMARK 900 RELATED ID: 1P0S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BLOOD COAGULATION FACTOR XA IN COMPLEXWITH      
REMARK 900 ECOTIN M84R                                                          
REMARK 900 RELATED ID: 2G00   RELATED DB: PDB                                   
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 3 -(6-(2'-((DIMETHYLAMINO)   
REMARK 900 METHYL)-4-BIPHENYLYL )-7-OXO-3-(TRIFLUOROMETHYL)-4,5,6,7-            
REMARK 900 TETRAHYDRO-1H-PYRAZOLO[3,4-C]PYRIDIN-1- YL)BENZAMIDE                 
REMARK 900 RELATED ID: 2BMG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 50                    
REMARK 900 RELATED ID: 1MQ5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF 3-CHLORO-N-[4-CHLORO -2-[[(4-CHLOROPHENYL)      
REMARK 900 AMINO]CARBONYL]PHENYL]- 4-[(4-METHYL-1-PIPERAZINYL)METHYL]-2-        
REMARK 900 THIOPHENECARBOXAMIDE COMPLEXED WITHHUMAN FACTOR XA                   
REMARK 900 RELATED ID: 1IQN   RELATED DB: PDB                                   
REMARK 900 HUMAN COAGULATION FACTOR XA COMPLEXD WITH M55192                     
REMARK 900 RELATED ID: 1MQ6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF 3-CHLORO-N-[4-CHLORO -2-[[(5-CHLORO-2-          
REMARK 900 PYRIDINYL)AMINO]CARBONYL ]-6-METHOXYPHENYL]-4-[[(4,5-DIHYDRO-2-      
REMARK 900 OXAZOLYL)METHYLAMINO]METHYL]-2- THIOPHENECARBOXAMIDE COMPLEXED WITH  
REMARK 900 HUMAN FACTOR XA                                                      
REMARK 900 RELATED ID: 1XKB   RELATED DB: PDB                                   
REMARK 900 FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S) -(3'-   
REMARK 900 AMIDINO-3- BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID              
REMARK 900 RELATED ID: 2BQW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH COMPOUND 45           
REMARK 900 RELATED ID: 1IQM   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M54471                    
REMARK 900 RELATED ID: 1EZQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH      
REMARK 900 RPR128515                                                            
REMARK 900 RELATED ID: 1IQE   RELATED DB: PDB                                   
REMARK 900 HUMAN COAGULATION FACTOR XA COMPLEXD WITH M55590                     
REMARK 900 RELATED ID: 1G2M   RELATED DB: PDB                                   
REMARK 900 FACTOR XA INHIBITOR COMPLEX                                          
REMARK 900 RELATED ID: 1FJS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE INHIBITOR ZK-807834 (CI-1031)COMPLEXED      
REMARK 900 WITH FACTOR XA                                                       
REMARK 900 RELATED ID: 1LPK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 125.                        
REMARK 900 RELATED ID: 2J4I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 1NFY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH       
REMARK 900 RPR200095                                                            
REMARK 900 RELATED ID: 2UWL   RELATED DB: PDB                                   
REMARK 900 SELECTIVE AND DUAL ACTION ORALLY ACTIVE INHIBITORS OF THROMBIN AND   
REMARK 900 FACTOR XA                                                            
REMARK 900 RELATED ID: 2BOK   RELATED DB: PDB                                   
REMARK 900 FACTOR XA - CATION                                                   
REMARK 900 RELATED ID: 1NFX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH       
REMARK 900 RPR208944                                                            
REMARK 900 RELATED ID: 1LPZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 41.                         
REMARK 900 RELATED ID: 1HCG   RELATED DB: PDB                                   
REMARK 900 BLOOD COAGULATION FACTOR XA                                          
REMARK 900 RELATED ID: 2J94   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 1IQJ   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55124                    
REMARK 900 RELATED ID: 1Z6E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA COMPLEXED TO RAZAXABAN                
REMARK 900 RELATED ID: 2UWP   RELATED DB: PDB                                   
REMARK 900 FACTOR XA INHIBITOR COMPLEX                                          
REMARK 900 RELATED ID: 2J95   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 2CJI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 2J38   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 2BOH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 1                     
REMARK 900 RELATED ID: 1G2L   RELATED DB: PDB                                   
REMARK 900 FACTOR XA INHIBITOR COMPLEX                                          
REMARK 900 RELATED ID: 1NFU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH       
REMARK 900 RPR132747                                                            
REMARK 900 RELATED ID: 1IQI   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55125                    
REMARK 900 RELATED ID: 2BQ6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 21                    
REMARK 900 RELATED ID: 1FAX   RELATED DB: PDB                                   
REMARK 900 COAGULATION FACTOR XA INHIBITOR COMPLEX                              
REMARK 900 RELATED ID: 1IQF   RELATED DB: PDB                                   
REMARK 900 HUMAN COAGULATION FACTOR XA COMPLEXD WITH M55165                     
REMARK 900 RELATED ID: 1NL8   RELATED DB: PDB                                   
REMARK 900 THEORETICAL MODEL OF THE TISSUE FACTOR/ FACTOR VIIA/FACTORXA COMPLEX 
REMARK 900 RELATED ID: 1KYE   RELATED DB: PDB                                   
REMARK 900 FACTOR XA IN COMPLEX WITH (R)-2-(3- ADAMANTAN-1-YL-UREIDO)-3-(3-     
REMARK 900 CARBAMIMIDOYL- PHENYL)-N-PHENETHYL-PROPIONAMIDE                      
REMARK 900 RELATED ID: 1IQG   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55159                    
REMARK 900 RELATED ID: 1IQK   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55113                    
REMARK 900 RELATED ID: 1IQH   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55143                    
REMARK 900 RELATED ID: 1V3X   RELATED DB: PDB                                   
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 1 -[6-METHYL-4,5,6,7-        
REMARK 900 TETRAHYDROTHIAZOLO(5, 4-C)PYRIDIN-2-YL] CARBONYL-2-CARBAMOYL-4 -(6-  
REMARK 900 CHLORONAPHTH-2-YLSULPHONYL)PIPERAZINE                                
REMARK 900 RELATED ID: 1LQD   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.                         
REMARK 900 RELATED ID: 2FZZ   RELATED DB: PDB                                   
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 1 -(3-AMINO-1,2-             
REMARK 900 BENZISOXAZOL-5-YL)-6-(2 '-(((3R)-3-HYDROXY-1-PYRROLIDINYL)METHYL)-4  
REMARK 900 -BIPHENYLYL)-3-(TRIFLUOROMETHYL)-1,4,5,6- TETRAHYDRO-7H-PYRAZOLO[3,  
REMARK 900 4-C]PYRIDIN-7- ONE                                                   
REMARK 900 RELATED ID: 2J2U   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX             
REMARK 900 RELATED ID: 2UWO   RELATED DB: PDB                                   
REMARK 900 SELECTIVE AND DUAL ACTION ORALLY ACTIVE INHIBITORS OF THROMBIN AND   
REMARK 900 FACTOR XA                                                            
REMARK 900 RELATED ID: 1KSN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH       
REMARK 900 FXV673                                                               
REMARK 900 RELATED ID: 1C5M   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING,    
REMARK 900 SUB- MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR    
REMARK 900 RELATED ID: 1IQL   RELATED DB: PDB                                   
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M54476                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SOME RESIDUES IN CHAIN ARE NOT SEEN IN THE ELECTRON                  
REMARK 999 DENSITY. SEQUENCE DATABASE RESIDUES 1-45 (THE GLA DOMAIN)            
REMARK 999 WERE BIOCHEMICALLY REMOVED IN CHAIN B                                
DBREF  2VH0 A   16   264  UNP    P00742   FA10_HUMAN     235    488             
DBREF  2VH0 B  -82    51  UNP    P00742   FA10_HUMAN      46    179             
SEQRES   1 A  254  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 A  254  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 A  254  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 A  254  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 A  254  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 A  254  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 A  254  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 A  254  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 A  254  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 A  254  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 A  254  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 A  254  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 A  254  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 A  254  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 A  254  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 A  254  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 A  254  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 A  254  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 A  254  ARG GLY LEU PRO LYS ALA LYS SER HIS ALA PRO GLU VAL          
SEQRES  20 A  254  ILE THR SER SER PRO LEU LYS                                  
SEQRES   1 B  134  GLU GLU MET LYS LYS GLY HIS LEU GLU ARG GLU CYS MET          
SEQRES   2 B  134  GLU GLU THR CYS SER TYR GLU GLU ALA ARG GLU VAL PHE          
SEQRES   3 B  134  GLU ASP SER ASP LYS THR ASN GLU PHE TRP ASN LYS TYR          
SEQRES   4 B  134  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   5 B  134  GLN GLY LYS CYS LYS ASP GLY LEU GLY GLU TYR THR CYS          
SEQRES   6 B  134  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   7 B  134  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   8 B  134  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   9 B  134  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES  10 B  134  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES  11 B  134  THR LEU GLU ARG                                              
HET     CA  A1245       1                                                       
HET     MG  A1246       1                                                       
HET    GSI  A1247      34                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GSI 2-(5-CHLOROTHIOPHEN-2-YL)-N-[(3S)-1-(4-{2-                       
HETNAM   2 GSI  [(DIMETHYLAMINO)METHYL]-1H-IMIDAZOL-1-YL}-2-                    
HETNAM   3 GSI  FLUOROPHENYL)-2-OXOPYRROLIDIN-3-YL]ETHANESULFONAMIDE            
FORMUL   3   CA    CA 2+                                                        
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GSI    C22 H25 CL F N5 O3 S2                                        
FORMUL   6  HOH   *232(H2 O)                                                    
HELIX    1   1 ALA A   55  GLN A   61  5                                   7    
HELIX    2   2 ARG A  125  SER A  130  1                                   6    
HELIX    3   3 ASP A  164  SER A  172  1                                   9    
HELIX    4   4 PHE A  234  LYS A  243  1                                  10    
HELIX    5   5 LEU B    3  CYS B    8  5                                   6    
SHEET    1  AA 7 GLN A  20  GLU A  21  0                                        
SHEET    2  AA 7 LYS A 156  PRO A 161 -1  O  MET A 157   N  GLN A  20           
SHEET    3  AA 7 THR A 135  GLY A 140 -1  O  GLY A 136   N  VAL A 160           
SHEET    4  AA 7 PRO A 198  PHE A 203 -1  O  PRO A 198   N  SER A 139           
SHEET    5  AA 7 THR A 206  TRP A 215 -1  O  THR A 206   N  PHE A 203           
SHEET    6  AA 7 GLY A 226  LYS A 230 -1  O  ILE A 227   N  TRP A 215           
SHEET    7  AA 7 MET A 180  ALA A 183 -1  O  PHE A 181   N  TYR A 228           
SHEET    1  AB 7 ALA A  81  HIS A  83  0                                        
SHEET    2  AB 7 LYS A  65  VAL A  68 -1  O  VAL A  66   N  HIS A  83           
SHEET    3  AB 7 GLN A  30  ILE A  34 -1  O  LEU A  32   N  ARG A  67           
SHEET    4  AB 7 GLY A  40  ILE A  46 -1  N  PHE A  41   O  LEU A  33           
SHEET    5  AB 7 TYR A  51  THR A  54 -1  O  LEU A  53   N  THR A  45           
SHEET    6  AB 7 ALA A 104  LEU A 108 -1  O  ALA A 104   N  THR A  54           
SHEET    7  AB 7 VAL A  85  LYS A  90 -1  N  GLU A  86   O  ARG A 107           
SHEET    1  BA 2 PHE B  11  GLU B  15  0                                        
SHEET    2  BA 2 SER B  18  SER B  22 -1  O  SER B  18   N  GLU B  15           
SHEET    1  BB 2 TYR B  27  LEU B  29  0                                        
SHEET    2  BB 2 CYS B  36  PRO B  38 -1  O  ILE B  37   N  THR B  28           
SSBOND   1 CYS A   22    CYS A   27                          1555   1555  2.07  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.06  
SSBOND   3 CYS A  122    CYS B   44                          1555   1555  2.06  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.00  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   6 CYS B    1    CYS B   12                          1555   1555  2.08  
SSBOND   7 CYS B    8    CYS B   21                          1555   1555  1.99  
SSBOND   8 CYS B   23    CYS B   36                          1555   1555  2.11  
LINK        CA    CA A1245                 O   ASN A  72     1555   1555  2.31  
LINK        CA    CA A1245                 O   HOH A2033     1555   1555  2.24  
LINK        CA    CA A1245                 O   GLN A  75     1555   1555  2.30  
LINK        CA    CA A1245                 OD1 ASP A  70     1555   1555  2.32  
LINK        CA    CA A1245                 O   HOH A2034     1555   1555  2.36  
LINK        CA    CA A1245                 OE2 GLU A  80     1555   1555  2.32  
LINK        MG    MG A1246                 O   LYS A 224     1555   1555  2.19  
LINK        MG    MG A1246                 O   TYR A 185     1555   1555  2.21  
LINK        MG    MG A1246                 O   ASP A 185A    1555   1555  2.56  
LINK        MG    MG A1246                 O   HOH A2162     1555   1555  2.75  
LINK        MG    MG A1246                 O   HOH A2160     1555   1555  2.41  
LINK        MG    MG A1246                 O   ARG A 222     1555   1555  2.21  
SITE     1 AC1  6 ASP A  70  ASN A  72  GLN A  75  GLU A  80                    
SITE     2 AC1  6 HOH A2033  HOH A2034                                          
SITE     1 AC2  6 TYR A 185  ASP A 185A ARG A 222  LYS A 224                    
SITE     2 AC2  6 HOH A2160  HOH A2162                                          
SITE     1 AC3 19 LYS A  96  GLU A  97  THR A  98  TYR A  99                    
SITE     2 AC3 19 PHE A 174  ASP A 189  ALA A 190  GLN A 192                    
SITE     3 AC3 19 VAL A 213  TRP A 215  GLY A 216  GLY A 219                    
SITE     4 AC3 19 CYS A 220  GLY A 226  ILE A 227  TYR A 228                    
SITE     5 AC3 19 HOH A2053  HOH A2055  HOH A2156                               
CRYST1   56.542   72.156   78.657  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      0.017686  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013859  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012713        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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