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Database: PDB
Entry: 3IG6
LinkDB: 3IG6
Original site: 3IG6 
HEADER    HYDROLASE                               27-JUL-09   3IG6              
TITLE     LOW MOLECULAR WEIGTH HUMAN UROKINASE TYPE PLASMINOGEN ACTIVATOR 2-[6- 
TITLE    2 (3'-AMINOMETHYL-BIPHENYL-3-YLOXY)-4-(3-DIMETHYLAMINO-PYRROLIDIN-1-   
TITLE    3 YL)-3,5-DIFLUORO-PYRIDIN-2-YLOXY]-4-DIMETHYLAMINO-BENZOIC ACID       
TITLE    4 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: FRAGMENT OF LIGHT CHAIN;                                   
COMPND   5 SYNONYM: U-PLASMINOGEN ACTIVATOR, UPA, UROKINASE-TYPE PLASMINOGEN    
COMPND   6 ACTIVATOR LONG CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR SHORT   
COMPND   7 CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR CHAIN B;               
COMPND   8 EC: 3.4.21.73;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND  14 SYNONYM: U-PLASMINOGEN ACTIVATOR, UPA, UROKINASE-TYPE PLASMINOGEN    
COMPND  15 ACTIVATOR LONG CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR SHORT   
COMPND  16 CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR CHAIN B;               
COMPND  17 EC: 3.4.21.73;                                                       
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLAU;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PLAU;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SELECTIVE, S1 SITE INHIBITOR, STRUCTURE-BASED DRUG DESIGN, UROKINASE, 
KEYWDS   2 BLOOD COAGULATION, DISULFIDE BOND, EGF-LIKE DOMAIN, FIBRINOLYSIS,    
KEYWDS   3 GLYCOPROTEIN, HYDROLASE, KRINGLE, PHOSPHOPROTEIN, PLASMINOGEN        
KEYWDS   4 ACTIVATION, PROTEASE, SECRETED, SERINE PROTEASE, ZYMOGEN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ADLER,M.WHITLOW                                                     
REVDAT   2   16-NOV-11 3IG6    1       VERSN  HETATM                            
REVDAT   1   13-OCT-09 3IG6    0                                                
JRNL        AUTH   C.W.WEST,M.ADLER,D.ARNAIZ,D.CHEN,K.CHU,G.GUALTIERI,E.HO,     
JRNL        AUTH 2 C.HUWE,D.LIGHT,G.PHILLIPS,R.PULK,D.SUKOVICH,M.WHITLOW,       
JRNL        AUTH 3 S.YUAN,J.BRYANT                                              
JRNL        TITL   IDENTIFICATION OF ORALLY BIOAVAILABLE, NON-AMIDINE           
JRNL        TITL 2 INHIBITORS OF UROKINASE PLASMINOGEN ACTIVATOR (UPA)          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  5712 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19703768                                                     
JRNL        DOI    10.1016/J.BMCL.2009.08.008                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2005                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 132827.960                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42641                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1684                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2250               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2240               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.252                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 4.000                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 1849                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0060               
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 46597                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.83                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5887                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 232                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3939                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 93                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.50000                                              
REMARK   3    B22 (A**2) : 1.59000                                              
REMARK   3    B33 (A**2) : -3.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.94000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.66                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.430 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.170 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.620 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.060 ; 3.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 50.94                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.P                                  
REMARK   3  PARAMETER FILE  2  : WATER_REP.PAR                                  
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : 438.PAR                                        
REMARK   3  PARAMETER FILE  5  : &_1_PARAMETER_INFILE_5                         
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : 438.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054369.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL, CYLINDRICALLY      
REMARK 200                                   BENT, SI(220)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : X-GEN                              
REMARK 200  DATA SCALING SOFTWARE          : X-GEN                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47497                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 2.450                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05350                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.26                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.24400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX, XTALVIEW                                         
REMARK 200 STARTING MODEL: PDB ENTRY 1LMW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.4 G/L, 1 MM LIGAND IN 50 MM TRIS PH   
REMARK 280  7.4, 5 MM NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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                                                                      
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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 839  LIES ON A SPECIAL POSITION.                          
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     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     THR A    17                                                      
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 465     LYS B   243                                                      
REMARK 465     GLU B   244                                                      
REMARK 465     GLU B   245                                                      
REMARK 465     ASN B   246                                                      
REMARK 465     GLY B   247                                                      
REMARK 465     LEU B   248                                                      
REMARK 465     ALA B   249                                                      
REMARK 465     LEU B   250                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     LEU C     9                                                      
REMARK 465     ARG C    19                                                      
REMARK 465     PRO C    20                                                      
REMARK 465     ARG C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     LYS C    23                                                      
REMARK 465     ARG D    36T                                                     
REMARK 465     GLY D    36U                                                     
REMARK 465     GLY D    36V                                                     
REMARK 465     GLU D   244                                                      
REMARK 465     GLU D   245                                                      
REMARK 465     ASN D   246                                                      
REMARK 465     GLY D   247                                                      
REMARK 465     LEU D   248                                                      
REMARK 465     ALA D   249                                                      
REMARK 465     LEU D   250                                                      
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     GLN C  15    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 243    CG   CD   CE   NZ                                   
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    HOH D   859     O    HOH D   859     2556     1.08            
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    VAL B  41      -66.86   -108.12                                   
REMARK 500    SER B  54     -154.86   -149.67                                   
REMARK 500    ASP B  97     -145.92    -96.92                                   
REMARK 500    TYR B 171     -104.14    -98.83                                   
REMARK 500    SER B 214      -59.30   -124.77                                   
REMARK 500    VAL D  41      -62.38   -106.89                                   
REMARK 500    SER D  54     -154.85   -147.59                                   
REMARK 500    PRO D  60C      37.20    -80.65                                   
REMARK 500    ASP D  97     -148.62   -105.10                                   
REMARK 500    LEU D  97B     -61.40   -130.00                                   
REMARK 500    TYR D 171     -102.59    -91.77                                   
REMARK 500    SER D 214      -58.17   -123.38                                   
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 438 B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 438 D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 450                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SQA   RELATED DB: PDB                                   
REMARK 900 UPA WITH INHIBITOR                                                   
REMARK 900 RELATED ID: 1W14   RELATED DB: PDB                                   
REMARK 900 UPA WITH INHIBITOR                                                   
REMARK 900 RELATED ID: 1VJA   RELATED DB: PDB                                   
REMARK 900 UPA WITH INHIBITOR                                                   
REMARK 900 RELATED ID: 1OWJ   RELATED DB: PDB                                   
REMARK 900 UPA WITH INHIBITOR                                                   
REMARK 900 RELATED ID: 1F92   RELATED DB: PDB                                   
REMARK 900 UPA WITH INHIBITOR                                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS STATE THAT THE ACTIVE FORM OF UROKINASE IS CREATED BY A      
REMARK 999 PROTEOLYTIC CLIP, THUS IT HAS TWO CHAINS                             
DBREF  3IG6 A    1    23  UNP    Q5SWW9   UROK_HUMAN     156    178             
DBREF  3IG6 B   16   250  UNP    Q5SWW9   UROK_HUMAN     179    431             
DBREF  3IG6 C    1    23  UNP    Q5SWW9   UROK_HUMAN     156    178             
DBREF  3IG6 D   16   250  UNP    Q5SWW9   UROK_HUMAN     179    431             
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  253  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 B  253  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 B  253  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 B  253  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 B  253  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 B  253  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 B  253  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 B  253  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 B  253  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 B  253  GLN THR ILE CYS LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 B  253  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 B  253  ASN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 B  253  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 B  253  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 B  253  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 B  253  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 B  253  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 B  253  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 B  253  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU          
SEQRES  20 B  253  GLU ASN GLY LEU ALA LEU                                      
SEQRES   1 C   23  LYS PRO SER SER PRO PRO GLU GLU LEU LYS PHE GLN CYS          
SEQRES   2 C   23  GLY GLN LYS THR LEU ARG PRO ARG PHE LYS                      
SEQRES   1 D  253  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 D  253  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 D  253  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 D  253  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 D  253  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 D  253  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 D  253  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 D  253  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 D  253  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 D  253  GLN THR ILE CYS LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 D  253  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 D  253  ASN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 D  253  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 D  253  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 D  253  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 D  253  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 D  253  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 D  253  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 D  253  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU          
SEQRES  20 D  253  GLU ASN GLY LEU ALA LEU                                      
HET    438  B 400      44                                                       
HET    438  D 401      44                                                       
HET    PO4  D 450       5                                                       
HETNAM     438 2-[(6-{[3'-(AMINOMETHYL)BIPHENYL-3-YL]OXY}-4-[(3R)-3-            
HETNAM   2 438  (DIMETHYLAMINO)PYRROLIDIN-1-YL]-3,5-DIFLUOROPYRIDIN-2-          
HETNAM   3 438  YL)OXY]-4-(DIMETHYLAMINO)BENZOIC ACID                           
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5  438    2(C33 H35 F2 N5 O4)                                          
FORMUL   7  PO4    O4 P 3-                                                      
FORMUL   8  HOH   *227(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  THR B  242  1                                   9    
HELIX    7   7 THR D   23  GLN D   27  5                                   5    
HELIX    8   8 ALA D   55  PHE D   59  5                                   5    
HELIX    9   9 LYS D   61  GLU D   62A 5                                   3    
HELIX   10  10 SER D  164  GLN D  169  1                                   6    
HELIX   11  11 TYR D  172  VAL D  176  5                                   5    
HELIX   12  12 PHE D  234  LYS D  243  1                                  10    
SHEET    1   A 8 GLU B  20  PHE B  21  0                                        
SHEET    2   A 8 LYS B 156  ILE B 163 -1  O  MET B 157   N  GLU B  20           
SHEET    3   A 8 MET B 180  ALA B 184 -1  O  CYS B 182   N  ILE B 163           
SHEET    4   A 8 GLY B 226  ARG B 230 -1  O  TYR B 228   N  LEU B 181           
SHEET    5   A 8 ARG B 206  TRP B 215 -1  N  TRP B 215   O  VAL B 227           
SHEET    6   A 8 PRO B 198  LEU B 203 -1  N  LEU B 203   O  ARG B 206           
SHEET    7   A 8 SER B 135  GLY B 140 -1  N  GLU B 137   O  VAL B 200           
SHEET    8   A 8 LYS B 156  ILE B 163 -1  O  VAL B 160   N  CYS B 136           
SHEET    1   B 7 PHE B  30  ARG B  36  0                                        
SHEET    2   B 7 VAL B  38  SER B  48 -1  O  VAL B  41   N  ILE B  33           
SHEET    3   B 7 TRP B  51  SER B  54 -1  O  ILE B  53   N  SER B  45           
SHEET    4   B 7 ALA B 104  ARG B 109 -1  O  LEU B 106   N  VAL B  52           
SHEET    5   B 7 MET B  81  LEU B  90 -1  N  GLU B  84   O  ARG B 109           
SHEET    6   B 7 TYR B  64  LEU B  68 -1  N  VAL B  66   O  PHE B  83           
SHEET    7   B 7 PHE B  30  ARG B  36 -1  N  TYR B  34   O  ILE B  65           
SHEET    1   C 2 SER B  95  ALA B  96  0                                        
SHEET    2   C 2 HIS B  99  HIS B 100 -1  O  HIS B 100   N  SER B  95           
SHEET    1   D 8 GLU D  20  PHE D  21  0                                        
SHEET    2   D 8 LYS D 156  ILE D 163 -1  O  MET D 157   N  GLU D  20           
SHEET    3   D 8 MET D 180  ALA D 184 -1  O  CYS D 182   N  ILE D 163           
SHEET    4   D 8 GLY D 226  ARG D 230 -1  O  TYR D 228   N  LEU D 181           
SHEET    5   D 8 ARG D 206  TRP D 215 -1  N  TRP D 215   O  VAL D 227           
SHEET    6   D 8 PRO D 198  LEU D 203 -1  N  LEU D 203   O  ARG D 206           
SHEET    7   D 8 SER D 135  GLY D 140 -1  N  GLU D 137   O  VAL D 200           
SHEET    8   D 8 LYS D 156  ILE D 163 -1  O  VAL D 160   N  CYS D 136           
SHEET    1   E 7 PHE D  30  ARG D  35  0                                        
SHEET    2   E 7 THR D  39  SER D  48 -1  O  THR D  39   N  ARG D  35           
SHEET    3   E 7 TRP D  51  SER D  54 -1  O  ILE D  53   N  SER D  45           
SHEET    4   E 7 ALA D 104  ARG D 109 -1  O  LEU D 106   N  VAL D  52           
SHEET    5   E 7 MET D  81  LEU D  90 -1  N  ILE D  89   O  LEU D 105           
SHEET    6   E 7 TYR D  64  LEU D  68 -1  N  VAL D  66   O  PHE D  83           
SHEET    7   E 7 PHE D  30  ARG D  35 -1  N  TYR D  34   O  ILE D  65           
SHEET    1   F 2 SER D  95  ALA D  96  0                                        
SHEET    2   F 2 HIS D  99  HIS D 100 -1  O  HIS D 100   N  SER D  95           
SSBOND   1 CYS A   13    CYS B  122                          1555   1555  2.03  
SSBOND   2 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   3 CYS B   50    CYS B  111                          1555   1555  2.04  
SSBOND   4 CYS B  136    CYS B  201                          1555   1555  2.04  
SSBOND   5 CYS B  168    CYS B  182                          1555   1555  2.04  
SSBOND   6 CYS B  191    CYS B  220                          1555   1555  2.04  
SSBOND   7 CYS C   13    CYS D  122                          1555   1555  2.04  
SSBOND   8 CYS D   42    CYS D   58                          1555   1555  2.03  
SSBOND   9 CYS D   50    CYS D  111                          1555   1555  2.03  
SSBOND  10 CYS D  136    CYS D  201                          1555   1555  2.03  
SSBOND  11 CYS D  168    CYS D  182                          1555   1555  2.04  
SSBOND  12 CYS D  191    CYS D  220                          1555   1555  2.04  
SITE     1 AC1 26 VAL B  41  HIS B  57  ALA B  96  LEU B  97B                   
SITE     2 AC1 26 ALA B  98  HIS B  99  ASP B 189  SER B 190                    
SITE     3 AC1 26 CYS B 191  GLN B 192  GLY B 193  SER B 195                    
SITE     4 AC1 26 GLY B 216  GLY B 218  CYS B 220  HOH B 717                    
SITE     5 AC1 26 HOH B 720  ILE D  60  ASP D  60A LYS D  92                    
SITE     6 AC1 26 TYR D  94  SER D  95  ALA D  96  HOH D 675                    
SITE     7 AC1 26 HOH D 764  HOH D 851                                          
SITE     1 AC2 16 TYR B 149  LEU B 150  SER D 146  ASP D 189                    
SITE     2 AC2 16 SER D 190  CYS D 191  GLN D 192  SER D 195                    
SITE     3 AC2 16 TRP D 215  GLY D 216  ARG D 217  GLY D 218                    
SITE     4 AC2 16 CYS D 220  PO4 D 450  HOH D 619  HOH D 718                    
SITE     1 AC3  6 HIS D  57  GLN D 192  GLY D 193  SER D 195                    
SITE     2 AC3  6 438 D 401  HOH D 739                                          
CRYST1   70.855   52.294   72.580  90.00  90.23  90.00 P 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      0.014113  0.000000  0.000058        0.00000                         
SCALE2      0.000000  0.019123  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013778        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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