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Database: PDB
Entry: 1GI7
LinkDB: 1GI7
Original site: 1GI7 
HEADER    BLOOD CLOTTING, HYDROLASE               22-JAN-01   1GI7              
TITLE     A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED   
TITLE    2 SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SHORT CHAIN;                                               
COMPND   5 SYNONYM: UPA, U-PLASMINOGEN ACTIVATOR, UROKINASE-PLASMINOGEN         
COMPND   6 ACTIVATOR;                                                           
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND  12 SYNONYM: UPA, U-PLASMINOGEN ACTIVATOR, UROKINASE-PLASMINOGEN         
COMPND  13 ACTIVATOR;                                                           
COMPND  14 EC: 3.4.21.73;                                                       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PPIC9LMWUPA;                              
SOURCE   9 OTHER_DETAILS: CHEM.BIOL. 7, 299-312, 2000;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PPIC9LMWUPA;                              
SOURCE  18 OTHER_DETAILS: CHEM.BIOL. 7, 299-312, 2000                           
KEYWDS    THREE-CENTERED, VERY SHORT HYDROGEN BOND, OXYANION HOLE WATER, SHIFT  
KEYWDS   2 OF PKA OF HIS57, STRUCTURE-BASED DRUG DESIGN, SPECIFICITY,           
KEYWDS   3 UROKINASE, TRYPSIN, THROMBIN, ZN+2-MEDIATED INHIBITION, BLOOD        
KEYWDS   4 CLOTTING, HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.A.KATZ,K.ELROD,C.LUONG,M.RICE,R.L.MACKMAN,P.A.SPRENGELER,J.SPENCER, 
AUTHOR   2 J.HATAYTE,J.JANC,J.LINK,J.LITVAK,R.RAI,K.RICE,S.SIDERIS,E.VERNER,    
AUTHOR   3 W.YOUNG                                                              
REVDAT   6   04-OCT-17 1GI7    1       REMARK                                   
REVDAT   5   13-JUL-11 1GI7    1       VERSN                                    
REVDAT   4   03-NOV-09 1GI7    1       MASTER REMARK SEQADV                     
REVDAT   3   24-FEB-09 1GI7    1       VERSN                                    
REVDAT   2   01-APR-03 1GI7    1       JRNL                                     
REVDAT   1   22-JAN-02 1GI7    0                                                
JRNL        AUTH   B.A.KATZ,K.ELROD,C.LUONG,M.J.RICE,R.L.MACKMAN,               
JRNL        AUTH 2 P.A.SPRENGELER,J.SPENCER,J.HATAYE,J.JANC,J.LINK,J.LITVAK,    
JRNL        AUTH 3 R.RAI,K.RICE,S.SIDERIS,E.VERNER,W.YOUNG                      
JRNL        TITL   A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A         
JRNL        TITL 2 MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE  
JRNL        TITL 3 SITE.                                                        
JRNL        REF    J.MOL.BIOL.                   V. 307  1451 2001              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11292354                                                     
JRNL        DOI    10.1006/JMBI.2001.4516                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.50                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.500                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 67.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 15438                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1523                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2003                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 256                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 4.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  ONLY LEU_A9 TO THR A17 ARE INCLUDED FOR THE A-CHAIN.                
REMARK   3  RESIDUES PRIOR AND AFTER THESE RESIDUES ARE NOT VISIBLE             
REMARK   3  (DISORDERED).                                                       
REMARK   3  RESIDUES AFTER THR B242 ARE NOT VISIBLE (DISORDERED).               
REMARK   3                                                                      
REMARK   3  RESIDUES SIMULTANEOUSLY REFINED IN TWO OR MORE CONFORMATIONS ARE:   
REMARK   3  MET B47, THR B139, ARG B166, GLN B192, SER B202                     
REMARK   3                                                                      
REMARK   3  DISORDERED WATERS ARE:                                              
REMARK   3                                                                      
REMARK   3  HOH510 WHICH IS CLOSE TO A SYMMETRY-RELATED EQUIVALENT OF HOH511;   
REMARK   3                                                                      
REMARK   3  NO ENERGY TERMS BETWEEN CITRATE 1 AND 2 ARE INCLUDED BECAUSE THEY   
REMARK   3  ARE                                                                 
REMARK   3  HYDROGEN-BONDED TO ONE ANOTHER VIA AN UNUSUALLY SHORT HYDROGEN BOND 
REMARK   3  BETWEEN CARBOXYLATE/HYDROXYL GROUPS.                                
REMARK   4                                                                      
REMARK   4 1GI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000001539.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.970                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21259                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY                : 1.700                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-PROPANOL PEG 4000, PH 6.5, VAPOR       
REMARK 280  DIFFUSION AT 298 K, PH 6.50                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       41.17500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.89500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       41.17500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.89500            
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: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     LYS A    23                                                      
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   HZ1  LYS B    92     HE1  TRP B   237              1.33            
REMARK 500   H1   HOH B   247     O    HOH B   365              1.37            
REMARK 500   O    HOH B   328     H2   HOH B   410              1.37            
REMARK 500   O    HOH B   268     H2   HOH B   271              1.43            
REMARK 500   O    SER B    75     H1   HOH B   491              1.48            
REMARK 500   OG1  THR B   177     H1   HOH B   256              1.51            
REMARK 500   HG   SER B   195     O    HOH B   385              1.51            
REMARK 500   HO7  CIT B     1     O7   CIT B     2              1.52            
REMARK 500   O    ALA B   183     H2   HOH B   325              1.53            
REMARK 500   O    HOH B   247     H1   HOH B   364              1.54            
REMARK 500   OG   SER B   135     H1   HOH B   436              1.57            
REMARK 500   O    VAL B    85     H1   HOH B   257              1.57            
REMARK 500   OG1  THR B   229     H2   HOH B   400              1.57            
REMARK 500   O    GLY B   196     H1   HOH B   401              1.57            
REMARK 500   OE1  GLN A    15     H2   HOH A   475              1.59            
REMARK 500   O    ILE B   108     H1   HOH B   375              1.59            
REMARK 500   OH   TYR B    64     H1   HOH B   443              1.60            
REMARK 500   O    HOH B   448     O    HOH B   475              2.09            
REMARK 500   O    HOH B   328     O    HOH B   410              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLN B   204     H2   HOH B   302     1545     1.34            
REMARK 500   O    HOH B   462     H2   HOH B   492     4555     1.46            
REMARK 500   H2   HOH B   363     O    HOH B   368     2555     1.54            
REMARK 500   O    PRO B   185A    H2   HOH B   269     4546     1.56            
REMARK 500   H2   HOH B   275     O    HOH B   458     4556     1.57            
REMARK 500   O    GLN B   204     O    HOH B   302     1545     2.14            
REMARK 500   O    HOH B   462     O    HOH B   492     4555     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS B  57   NE2   HIS B  57   CD2    -0.072                       
REMARK 500    HIS B  91   NE2   HIS B  91   CD2    -0.069                       
REMARK 500    HIS B 165   NE2   HIS B 165   CD2    -0.070                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A  13   CA  -  CB  -  SG  ANGL. DEV. =   7.3 DEGREES          
REMARK 500    HIS B  37   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES          
REMARK 500    CYS B  42   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B 109   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    LEU B 199   N   -  CA  -  C   ANGL. DEV. = -17.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN B  27       56.51   -144.60                                   
REMARK 500    ARG B  37A     -26.94    -29.45                                   
REMARK 500    SER B  54     -154.20   -149.66                                   
REMARK 500    ASP B  93       38.09     78.33                                   
REMARK 500    ASP B  97     -162.42   -127.02                                   
REMARK 500    LEU B  97B     -58.65    111.42                                   
REMARK 500    CYS B 111     -168.75   -102.82                                   
REMARK 500    TYR B 127       36.59     39.55                                   
REMARK 500    LYS B 143      152.13    -49.42                                   
REMARK 500    TYR B 171     -100.14   -117.76                                   
REMARK 500    SER B 174       30.93    -86.98                                   
REMARK 500    TRP B 186       49.09     31.47                                   
REMARK 500    ASP B 189      177.34    178.11                                   
REMARK 500    SER B 240       -8.37    -58.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 120 B 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C5X   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR                
DBREF  1GI7 A    1    23  UNP    P00749   UROK_HUMAN     156    178             
DBREF  1GI7 B   16   242  UNP    P00749   UROK_HUMAN     179    423             
SEQADV 1GI7 ALA B  145  UNP  P00749    ASN   322 ENGINEERED                     
SEQRES   1 A   23  LYS PRO SER SER PRO PRO GLU GLU LEU LYS PHE GLN CYS          
SEQRES   2 A   23  GLY GLN LYS THR LEU ARG PRO ARG PHE LYS                      
SEQRES   1 B  245  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 B  245  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 B  245  VAL THR TYR VAL CYS GLY GLY SER LEU MET SER PRO CYS          
SEQRES   4 B  245  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 B  245  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 B  245  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 B  245  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 B  245  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 B  245  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 B  245  GLN THR ILE CYS LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 B  245  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 B  245  ALA SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 B  245  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 B  245  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 B  245  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 B  245  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 B  245  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 B  245  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 B  245  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR                  
HET    120  B 246      31                                                       
HET    CIT  B   1      18                                                       
HET    CIT  B   2      18                                                       
HETNAM     120 2-(2-OXO-1,2-DIHYDRO-PYRIDIN-3-YL)-1H-BENZOIMIDAZOLE-5-          
HETNAM   2 120  CARBOXAMIDINE                                                   
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3  120    C13 H12 N5 O 1+                                              
FORMUL   4  CIT    2(C6 H8 O7)                                                  
FORMUL   6  HOH   *256(H2 O)                                                    
HELIX    1   1 THR B   23  GLN B   27  5                                   5    
HELIX    2   2 ALA B   55  PHE B   59  5                                   5    
HELIX    3   3 LYS B   61  GLU B   62A 5                                   3    
HELIX    4   4 SER B  164  GLN B  169  1                                   6    
HELIX    5   5 TYR B  172  VAL B  176  5                                   5    
HELIX    6   6 PHE B  234  SER B  240  1                                   7    
SHEET    1   A 7 PHE B  30  HIS B  37  0                                        
SHEET    2   A 7 TRP B  51  SER B  54 -1  O  TRP B  51   N  MET B  47           
SHEET    3   A 7 ALA B 104  ARG B 109 -1  O  ALA B 104   N  SER B  54           
SHEET    4   A 7 MET B  81  LEU B  90 -1  N  GLU B  84   O  ARG B 109           
SHEET    5   A 7 TYR B  64  LEU B  68 -1  O  VAL B  66   N  PHE B  83           
SHEET    6   A 7 PHE B  30  HIS B  37 -1  O  ALA B  32   N  TYR B  67           
SHEET    1   B 2 SER B  95  ALA B  96  0                                        
SHEET    2   B 2 HIS B  99  HIS B 100 -1  N  HIS B 100   O  SER B  95           
SSBOND   1 CYS A   13    CYS B  122                          1555   1555  2.02  
SSBOND   2 CYS B   42    CYS B   58                          1555   1555  2.02  
SSBOND   3 CYS B   50    CYS B  111                          1555   1555  2.02  
SSBOND   4 CYS B  136    CYS B  201                          1555   1555  2.02  
SSBOND   5 CYS B  168    CYS B  182                          1555   1555  2.01  
SSBOND   6 CYS B  191    CYS B  220                          1555   1555  2.03  
SITE     1 AC1 15 PRO B 185A GLN B 185B ASP B 189  SER B 190                    
SITE     2 AC1 15 CYS B 191  GLN B 192  SER B 195  GLY B 216                    
SITE     3 AC1 15 GLY B 219  GLY B 226  HOH B 385  HOH B 387                    
SITE     4 AC1 15 HOH B 388  HOH B 390  HOH B 478                               
SITE     1 AC2  9 CIT B   2  TYR B  67  LYS B  82  SER B 164                    
SITE     2 AC2  9 HIS B 165  ARG B 166  HOH B 334  HOH B 380                    
SITE     3 AC2  9 HOH B 428                                                     
SITE     1 AC3 10 CIT B   1  ARG B  36  LYS B  82  LYS B 110A                   
SITE     2 AC3 10 HIS B 165  ARG B 166  THR B 178  ARG B 230                    
SITE     3 AC3 10 HOH B 331  HOH B 334                                          
CRYST1   82.350   49.790   66.120  90.00 113.23  90.00 C 1 2 1       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      0.012143  0.000000  0.005212        0.00000                         
SCALE2      0.000000  0.020084  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016458        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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