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Database: PDB
Entry: 3IIT
LinkDB: 3IIT
Original site: 3IIT 
HEADER    HYDROLASE                               03-AUG-09   3IIT              
TITLE     FACTOR XA IN COMPLEX WITH A CIS-1,2-DIAMINOCYCLOHEXANE DERIVATIVE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIVATED FACTOR XA HEAVY CHAIN;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: COAGULATION FACTOR X HEAVY CHAIN, FACTOR X HEAVY CHAIN;     
COMPND   5 EC: 3.4.21.6;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FACTOR X LIGHT CHAIN;                                      
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 125-178;                                      
COMPND  10 SYNONYM: COAGULATION FACTOR X LIGHT CHAIN;                           
COMPND  11 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 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 OTHER_DETAILS: PROTEOLYTIC CLEAVAGE PRODUCT                          
KEYWDS    GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION   
KEYWDS   2 FACTOR, PROTEIN INHIBITOR COMPLEX, CALCIUM-BINDING, BLOOD            
KEYWDS   3 COAGULATION, CLEAVAGE ON PAIR OF BASIC RESIDUES, DISULFIDE BOND,     
KEYWDS   4 EGF-LIKE DOMAIN, GAMMA-CARBOXYGLUTAMIC ACID, HYDROXYLATION,          
KEYWDS   5 PROTEASE, SECRETED, ZYMOGEN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SUZUKI                                                              
REVDAT   2   01-NOV-23 3IIT    1       REMARK LINK                              
REVDAT   1   04-AUG-10 3IIT    0                                                
JRNL        AUTH   K.YOSHIKAWA,S.KOBAYASHI,Y.NAKAMOTO,N.HAGINOYA,S.KOMORIYA,    
JRNL        AUTH 2 T.YOSHINO,T.NAGATA,A.MOCHIZUKI,K.WATANABE,M.SUZUKI,H.KANNO,  
JRNL        AUTH 3 T.OHTA                                                       
JRNL        TITL   DESIGN, SYNTHESIS, AND SAR OF CIS-1,2-DIAMINOCYCLOHEXANE     
JRNL        TITL 2 DERIVATIVES AS POTENT FACTOR XA INHIBITORS. PART II:         
JRNL        TITL 3 EXPLORATION OF 6-6 FUSED RINGS AS ALTERNATIVE S1 MOIETIES.   
JRNL        REF    BIOORG.MED.CHEM.              V.  17  8221 2009              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   19900814                                                     
JRNL        DOI    10.1016/J.BMC.2009.10.024                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 26348                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1375                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1918                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2172                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 192                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54000                                              
REMARK   3    B22 (A**2) : -0.83000                                             
REMARK   3    B33 (A**2) : 0.29000                                              
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): 0.141         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.904         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2260 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3068 ; 1.538 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   285 ; 6.308 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;31.192 ;23.936       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   357 ;12.871 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;21.283 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   335 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1714 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1417 ; 1.101 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2268 ; 2.003 ; 2.300       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   843 ; 3.189 ; 4.500       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   800 ; 4.555 ; 4.500       
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 PARAMETERS FOR MASK CACLULATION        
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RIGID BODY REFINEMENT                     
REMARK   4                                                                      
REMARK   4 3IIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054464.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28857                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.240                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 2.660                              
REMARK 200  R MERGE                    (I) : 0.04840                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC 5.5.0066                                       
REMARK 200 STARTING MODEL: 1FAX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.00, VAPOR DIFFUSION, TEMPERATURE    
REMARK 280  293K                                                                
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       28.02750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.61900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.08950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.61900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.02750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.08950            
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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 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     GLU A  37    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  39    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  62    CG   CD   CE   NZ                                   
REMARK 470     GLN A  75    OE1  NE2                                            
REMARK 470     GLU A  76    CD   OE1  OE2                                       
REMARK 470     GLU A  77    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  92    OD1  ND2                                            
REMARK 470     ARG A  93    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  96    CD   CE   NZ                                        
REMARK 470     GLU A  97    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 115    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 134    CD   CE   NZ                                        
REMARK 470     LYS A 148    CD   CE   NZ                                        
REMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 187    OE1  NE2                                            
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     LYS A 236    CD   CE   NZ                                        
REMARK 470     ARG B  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  87    CG   CD   CE   NZ                                   
REMARK 470     GLN B 104    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 138    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A    60     NZ   LYS A    90              2.06            
REMARK 500   O    HOH A   376     O    HOH B   160              2.09            
REMARK 500   OH   TYR A   185     O    HOH A   368              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  48     -177.31   -170.95                                   
REMARK 500    ARG A 115     -176.27   -174.86                                   
REMARK 500    ASP A 164      132.36    -37.57                                   
REMARK 500    ASP A 205       14.02     57.50                                   
REMARK 500    SER A 214      -65.74   -121.08                                   
REMARK 500    LEU B  88     -128.53     52.75                                   
REMARK 500    GLN B  98     -110.58   -130.94                                   
REMARK 500    GLN B 104     -132.62     41.05                                   
REMARK 500    ASN B 105       42.12   -108.06                                   
REMARK 500    LYS B 122      -50.46   -129.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     D14 A  700                                                       
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 A 261  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A  15   O                                                      
REMARK 620 2 ASP A  70   OD1  81.5                                              
REMARK 620 3 ASN A  72   O    90.6  88.7                                        
REMARK 620 4 GLN A  75   O   105.0 170.4  84.2                                  
REMARK 620 5 GLU A  80   OE2  84.7 106.7 163.0  81.3                            
REMARK 620 6 HOH A 321   O   156.7  75.2  88.9  98.2 101.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 262  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 185   O                                                      
REMARK 620 2 ASP A 185A  O    82.2                                              
REMARK 620 3 ARG A 222   O   168.0  86.9                                        
REMARK 620 4 LYS A 224   O    89.3 120.3  92.0                                  
REMARK 620 5 HOH A 267   O    93.1 174.0  98.1  63.1                            
REMARK 620 6 HOH A 283   O    94.2  84.3  89.5 155.4  92.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 261                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D14 A 700                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2EI6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR       
REMARK 900 RELATED ID: 2EI7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR       
REMARK 900 RELATED ID: 2EI8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR       
REMARK 900 RELATED ID: 1V3X   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR       
REMARK 900 RELATED ID: 1WU1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR       
REMARK 900 RELATED ID: 2D1J   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR       
DBREF  3IIT A   16   243  UNP    P00742   FA10_HUMAN     235    467             
DBREF  3IIT B   85   138  UNP    P00742   FA10_HUMAN     125    178             
SEQRES   1 A  233  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 A  233  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 A  233  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 A  233  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 A  233  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 A  233  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 A  233  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 A  233  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 A  233  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 A  233  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 A  233  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 A  233  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 A  233  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 A  233  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 A  233  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 A  233  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 A  233  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 A  233  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS              
SEQRES   1 B   54  THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS ASP          
SEQRES   2 B   54  GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS SER          
SEQRES   3 B   54  CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS ALA          
SEQRES   4 B   54  CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN THR          
SEQRES   5 B   54  LEU GLU                                                      
HET     CA  A 261       1                                                       
HET     CA  A 262       1                                                       
HET    D14  A 700      32                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     D14 7-CHLORO-N-[(1S,2R,4S)-4-(DIMETHYLCARBAMOYL)-2-{[(5-             
HETNAM   2 D14  METHYL-5,6-DIHYDRO-4H-PYRROLO[3,4-D][1,3]THIAZOL-2-             
HETNAM   3 D14  YL)CARBONYL]AMINO}CYCLOHEXYL]ISOQUINOLINE-3-                    
HETNAM   4 D14  CARBOXAMIDE                                                     
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  D14    C26 H29 CL N6 O3 S                                           
FORMUL   6  HOH   *192(H2 O)                                                    
HELIX    1   1 ALA A   55  ALA A   61A 5                                   8    
HELIX    2   2 GLU A  124A THR A  131  1                                   8    
HELIX    3   3 ASP A  164  SER A  172  1                                   9    
HELIX    4   4 PHE A  234  MET A  242  1                                   9    
HELIX    5   5 LYS B   87  CYS B   96  5                                  10    
SHEET    1   A 8 GLN A  20  GLU A  21  0                                        
SHEET    2   A 8 LYS A 156  VAL A 163 -1  O  MET A 157   N  GLN A  20           
SHEET    3   A 8 MET A 180  ALA A 183 -1  O  CYS A 182   N  VAL A 163           
SHEET    4   A 8 GLY A 226  LYS A 230 -1  O  TYR A 228   N  PHE A 181           
SHEET    5   A 8 THR A 206  TRP A 215 -1  N  TRP A 215   O  ILE A 227           
SHEET    6   A 8 PRO A 198  PHE A 203 -1  N  HIS A 199   O  THR A 210           
SHEET    7   A 8 THR A 135  GLY A 140 -1  N  ILE A 137   O  VAL A 200           
SHEET    8   A 8 LYS A 156  VAL A 163 -1  O  VAL A 160   N  GLY A 136           
SHEET    1   B 7 GLN A  30  ILE A  34  0                                        
SHEET    2   B 7 GLY A  40  ILE A  46 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TYR A  51  THR A  54 -1  O  LEU A  53   N  THR A  45           
SHEET    4   B 7 ALA A 104  LEU A 108 -1  O  ALA A 104   N  THR A  54           
SHEET    5   B 7 ALA A  81  LYS A  90 -1  N  GLU A  86   O  ARG A 107           
SHEET    6   B 7 LYS A  65  VAL A  68 -1  N  VAL A  66   O  HIS A  83           
SHEET    7   B 7 GLN A  30  ILE A  34 -1  N  LEU A  32   O  ARG A  67           
SHEET    1   C 2 PHE B  99  GLU B 103  0                                        
SHEET    2   C 2 SER B 106  SER B 110 -1  O  VAL B 108   N  HIS B 101           
SHEET    1   D 2 TYR B 115  LEU B 117  0                                        
SHEET    2   D 2 CYS B 124  PRO B 126 -1  O  ILE B 125   N  THR B 116           
SSBOND   1 CYS A   22    CYS A   27                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.02  
SSBOND   3 CYS A  122    CYS B  132                          1555   1555  2.03  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  1.93  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.00  
SSBOND   6 CYS B   89    CYS B  100                          1555   1555  2.06  
SSBOND   7 CYS B   96    CYS B  109                          1555   1555  1.99  
SSBOND   8 CYS B  111    CYS B  124                          1555   1555  2.03  
LINK         O   HOH A  15                CA    CA A 261     1555   1555  2.49  
LINK         OD1 ASP A  70                CA    CA A 261     1555   1555  2.22  
LINK         O   ASN A  72                CA    CA A 261     1555   1555  2.46  
LINK         O   GLN A  75                CA    CA A 261     1555   1555  2.25  
LINK         OE2 GLU A  80                CA    CA A 261     1555   1555  2.39  
LINK         O   TYR A 185                CA    CA A 262     1555   1555  2.22  
LINK         O   ASP A 185A               CA    CA A 262     1555   1555  2.56  
LINK         O   ARG A 222                CA    CA A 262     1555   1555  2.35  
LINK         O   LYS A 224                CA    CA A 262     1555   1555  2.31  
LINK        CA    CA A 261                 O   HOH A 321     1555   1555  2.57  
LINK        CA    CA A 262                 O   HOH A 267     1555   1555  2.97  
LINK        CA    CA A 262                 O   HOH A 283     1555   1555  2.37  
SITE     1 AC1  6 HOH A  15  ASP A  70  ASN A  72  GLN A  75                    
SITE     2 AC1  6 GLU A  80  HOH A 321                                          
SITE     1 AC2  6 TYR A 185  ASP A 185A ARG A 222  LYS A 224                    
SITE     2 AC2  6 HOH A 267  HOH A 283                                          
SITE     1 AC3 20 THR A  98  PHE A 174  ASP A 189  ALA A 190                    
SITE     2 AC3 20 GLN A 192  SER A 195  VAL A 213  TRP A 215                    
SITE     3 AC3 20 GLY A 216  GLU A 217  GLY A 218  CYS A 220                    
SITE     4 AC3 20 GLY A 226  ILE A 227  TYR A 228  HOH A 287                    
SITE     5 AC3 20 HOH A 306  HOH A 370  HOH A 372  HOH A 379                    
CRYST1   56.055   72.179   79.238  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      0.017840  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013854  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012620        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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