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Database: PDB
Entry: 3QN7
LinkDB: 3QN7
Original site: 3QN7 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           08-FEB-11   3QN7              
TITLE     POTENT AND SELECTIVE BICYCLIC PEPTIDE INHIBITOR (UK18) OF HUMAN       
TITLE    2 UROKINASE-TYPE PLASMINOGEN ACTIVATOR(UPA)                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UROKINASE-TYPE PLASMINOGEN ACTIVATOR     
COMPND   5 CHAIN B;                                                             
COMPND   6 SYNONYM: U-PLASMINOGEN ACTIVATOR, UPA;                               
COMPND   7 EC: 3.4.21.73;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: BICYCLIC PEPTIDE INHIBITOR;                                
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: UK18;                                                       
COMPND  14 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: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY CELLS (HEK-293); 
SOURCE  10 EXPRESSION_SYSTEM_CELL: MAMMALIAN CELLS;                             
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PSECTAGA;                                 
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    BICYCLIC PEPTIDE INHIBITOR, CHYMOTRYPSIN FOLD, SERINE PROTEASE,       
KEYWDS   2 UROKINASE RECEPTOR (UPAR), EXTRACELLULAR, HYDROLASE-HYDROLASE        
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ANGELINI,L.CENDRON,J.TOUATI,G.WINTER,G.ZANOTTI,C.HEINIS             
REVDAT   2   10-APR-13 3QN7    1       JRNL                                     
REVDAT   1   15-FEB-12 3QN7    0                                                
JRNL        AUTH   A.ANGELINI,L.CENDRON,S.CHEN,J.TOUATI,G.WINTER,G.ZANOTTI,     
JRNL        AUTH 2 C.HEINIS                                                     
JRNL        TITL   BICYCLIC PEPTIDE INHIBITOR REVEALS LARGE CONTACT INTERFACE   
JRNL        TITL 2 WITH A PROTEASE TARGET                                       
JRNL        REF    ACS CHEM.BIOL.                V.   7   817 2012              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   22304751                                                     
JRNL        DOI    10.1021/CB200478T                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.ZHAO,C.YUAN,T.WIND,Z.HUANG,P.A.ANDREASEN,M.HUANG           
REMARK   1  TITL   STRUCTURAL BASIS OF SPECIFICITY OF A PEPTIDYL UROKINASE      
REMARK   1  TITL 2 INHIBITOR, UPAIN-1                                           
REMARK   1  REF    J.STRUCT.BIOL.                V. 160     1 2007              
REMARK   1  REFN                   ISSN 1047-8477                               
REMARK   1  PMID   17692534                                                     
REMARK   1  DOI    10.1016/J.JSB.2007.06.003                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.SPRAGGON,C.PHILLIPS,U.K.NOWAK,C.P.PONTING,D.SAUNDERS,      
REMARK   1  AUTH 2 C.M.DOBSON,D.I.STUART,E.Y.JONES                              
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN       
REMARK   1  TITL 2 UROKINASE-TYPE PLASMINOGEN ACTIVATOR                         
REMARK   1  REF    STRUCTURE                     V.   3   681 1995              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   8591045                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17487                          
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) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 946                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1313                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2050                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 132                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.96000                                             
REMARK   3    B22 (A**2) : -0.96000                                             
REMARK   3    B33 (A**2) : 1.44000                                              
REMARK   3    B12 (A**2) : -0.48000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.495         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2113 ; 0.021 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2862 ; 1.900 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   259 ; 7.462 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;27.911 ;22.903       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   354 ;16.772 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;19.594 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   305 ; 0.154 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1602 ; 0.009 ; 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):  1292 ; 1.329 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2085 ; 2.344 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   821 ; 3.220 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   777 ; 4.940 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063856.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.939                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : TOROIDAL FOCUSING MIRRORS          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18155                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: 2NWN.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.05M SODIUM        
REMARK 280  CITRATE, 5%(V/V) PEG 400, PH 4.3, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.62500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.00186            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       14.24000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.62500            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       35.00186            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       14.24000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.62500            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       35.00186            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       14.24000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       70.00372            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       28.48000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       70.00372            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       28.48000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       70.00372            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       28.48000            
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: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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   246                                                      
REMARK 465     GLU A   247                                                      
REMARK 465     GLU A   248                                                      
REMARK 465     ASN A   249                                                      
REMARK 465     GLY A   250                                                      
REMARK 465     LEU A   251                                                      
REMARK 465     ALA A   252                                                      
REMARK 465     LEU A   253                                                      
REMARK 465     GLY B    17                                                      
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   O    HOH A   347     O    HOH A   351              1.93            
REMARK 500   OE1  GLU A    77     O    HOH A   361              2.11            
REMARK 500   O    HOH A   270     O    HOH A   337              2.12            
REMARK 500   O    GLN A   130     OG1  THR A   133              2.18            
REMARK 500   O    HOH A    52     O    HOH A   299              2.18            
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    HOH A   326     O    HOH A   318     8555     2.05            
REMARK 500   O    HOH A   358     O    HOH A   312     8554     2.09            
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    MET A  74   CA  -  CB  -  CG  ANGL. DEV. =  10.7 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    ARG A  23A     -54.78    114.34                                   
REMARK 500    SER A  26D    -117.74     43.61                                   
REMARK 500    SER A  43     -155.01   -153.21                                   
REMARK 500    PRO A  52C      28.36    -79.89                                   
REMARK 500    ASP A  90     -141.74    -82.00                                   
REMARK 500    THR A  91A     -71.40    -54.30                                   
REMARK 500    TYR A 172     -102.50   -100.49                                   
REMARK 500    SER A 217      -61.11   -125.23                                   
REMARK 500    ASP A 226A      16.15     59.56                                   
REMARK 500    CYS B   2     -137.64     52.37                                   
REMARK 500    SER B  14      118.51    120.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER B    3     ARG B    4                 -144.90                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A  23A       24.3      L          L   OUTSIDE RANGE           
REMARK 500    SER A  26D       25.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 107B       21.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG B   4        24.7      L          L   OUTSIDE RANGE           
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 ZBR B 18                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF BICYCLIC PEPTIDE       
REMARK 800  INHIBITOR                                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LMW   RELATED DB: PDB                                   
REMARK 900 HUMAN UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)                     
REMARK 900 RELATED ID: 2NWN   RELATED DB: PDB                                   
REMARK 900 HUMAN UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA) IN COMPLEX          
REMARK 900 WITH A BICYCLIC PEPTIDE INHIBITOR (UK18)                             
DBREF  3QN7 A    1   253  UNP    P00749   UROK_HUMAN     179    431             
DBREF  3QN7 B    1    17  PDB    3QN7     3QN7             1     17             
SEQADV 3QN7 ALA A  121  UNP  P00749    CYS   299 ENGINEERED MUTATION            
SEQADV 3QN7 GLN A  144  UNP  P00749    ASN   322 ENGINEERED MUTATION            
SEQRES   1 A  253  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 A  253  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 A  253  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 A  253  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 A  253  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 A  253  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 A  253  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 A  253  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 A  253  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 A  253  GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 A  253  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 A  253  GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 A  253  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 A  253  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 A  253  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 A  253  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 A  253  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 A  253  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 A  253  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU          
SEQRES  20 A  253  GLU ASN GLY LEU ALA LEU                                      
SEQRES   1 B   17  ALA CYS SER ARG TYR GLU VAL ASP CYS ARG GLY ARG GLY          
SEQRES   2 B   17  SER ALA CYS GLY                                              
HET    ZBR  B  18       9                                                       
HETNAM     ZBR 1,3,5-TRIS(BROMOMETHYL)BENZENE                                   
FORMUL   3  ZBR    C9 H9 BR3                                                    
FORMUL   4  HOH   *132(H2 O)                                                    
HELIX    1   1 THR A    8  GLN A   12  5                                   5    
HELIX    2   2 ALA A   44  PHE A   48  5                                   5    
HELIX    3   3 LYS A   53  GLU A   55A 5                                   3    
HELIX    4   4 SER A  163  GLN A  168  1                                   6    
HELIX    5   5 PHE A  237  HIS A  244  1                                   8    
SHEET    1   A 8 GLU A   5  PHE A   6  0                                        
SHEET    2   A 8 LYS A 155  ILE A 162 -1  O  MET A 156   N  GLU A   5           
SHEET    3   A 8 MET A 181  ALA A 185 -1  O  ALA A 185   N  LYS A 160           
SHEET    4   A 8 GLY A 229  ARG A 233 -1  O  TYR A 231   N  LEU A 182           
SHEET    5   A 8 ARG A 209  TRP A 218 -1  N  TRP A 218   O  VAL A 230           
SHEET    6   A 8 PRO A 201  LEU A 206 -1  N  CYS A 204   O  THR A 211           
SHEET    7   A 8 SER A 134  GLY A 139 -1  N  GLU A 136   O  VAL A 203           
SHEET    8   A 8 LYS A 155  ILE A 162 -1  O  VAL A 159   N  CYS A 135           
SHEET    1   B 7 PHE A  15  ARG A  21  0                                        
SHEET    2   B 7 VAL A  27  SER A  37 -1  O  VAL A  30   N  ILE A  18           
SHEET    3   B 7 TRP A  40  SER A  43 -1  O  ILE A  42   N  SER A  34           
SHEET    4   B 7 ALA A  99  ARG A 104 -1  O  LEU A 101   N  VAL A  41           
SHEET    5   B 7 MET A  74  LEU A  83 -1  N  ILE A  82   O  LEU A 100           
SHEET    6   B 7 TYR A  57  LEU A  61 -1  N  LEU A  61   O  MET A  74           
SHEET    7   B 7 PHE A  15  ARG A  21 -1  N  TYR A  19   O  ILE A  58           
SHEET    1   C 2 SER A  88  ALA A  89  0                                        
SHEET    2   C 2 HIS A  94  HIS A  95 -1  O  HIS A  95   N  SER A  88           
SSBOND   1 CYS A   31    CYS A   47                          1555   1555  2.06  
SSBOND   2 CYS A   39    CYS A  110                          1555   1555  2.03  
SSBOND   3 CYS A  135    CYS A  204                          1555   1555  2.06  
SSBOND   4 CYS A  167    CYS A  183                          1555   1555  2.06  
SSBOND   5 CYS A  194    CYS A  222                          1555   1555  2.09  
LINK         SG  CYS B   2                 C9  ZBR B  18     1555   1555  1.80  
LINK         SG  CYS B   9                 C7  ZBR B  18     1555   1555  1.81  
LINK         SG  CYS B  16                 C8  ZBR B  18     1555   1555  1.73  
CISPEP   1 HIS A   22    ARG A   23A         0         0.84                     
CISPEP   2 ARG A   23A   GLY A   24B         0        16.86                     
CISPEP   3 GLY A   24B   GLY A   25C         0         8.24                     
CISPEP   4 GLU A  107B   GLY A  108C         0        15.97                     
CISPEP   5 GLY B   13    SER B   14          0        15.14                     
SITE     1 AC1  6 ASP A  50A CYS B   2  ARG B   4  CYS B   9                    
SITE     2 AC1  6 ARG B  10  CYS B  16                                          
SITE     1 AC2 33 ARG A  20  HIS A  22  ARG A  23A GLY A  24B                   
SITE     2 AC2 33 GLY A  25C TYR A  29  VAL A  30  CYS A  31                    
SITE     3 AC2 33 HIS A  46  ILE A  49  ASP A  50A TYR A  51B                   
SITE     4 AC2 33 HIS A  94  TYR A 150  ASP A 192  SER A 193                    
SITE     5 AC2 33 GLN A 195  GLY A 196  SER A 198  GLY A 219                    
SITE     6 AC2 33 GLY A 221  CYS A 222  LYS A 227  GLY A 229                    
SITE     7 AC2 33 HOH A 269  HOH A 304  HOH A 356  ZBR B  18                    
SITE     8 AC2 33 HOH B  19  HOH B  72  HOH B  85  HOH B 103                    
SITE     9 AC2 33 HOH B 108                                                     
CRYST1  121.250  121.250   42.720  90.00  90.00 120.00 H 3           9          
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      0.008247  0.004762  0.000000        0.00000                         
SCALE2      0.000000  0.009523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023408        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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