GenomeNet

Database: PDB
Entry: 4MNW
LinkDB: 4MNW
Original site: 4MNW 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-SEP-13   4MNW              
TITLE     CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)       
TITLE    2 COMPLEXED WITH BICYCLIC PEPTIDE UK749                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR CHAIN B;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 179-423);                   
COMPND   5 SYNONYM: U-PLASMINOGEN ACTIVATOR, UPA;                               
COMPND   6 EC: 3.4.21.73;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: BICYCLIC PEPTIDE UK749;                                    
COMPND  11 CHAIN: B;                                                            
COMPND  12 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: HEK 293;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PSECTAGA;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 OTHER_DETAILS: MODIFIED WITH 1,3,5-TRIS(BROMOMETHYL)BENZENE (TBMB)   
KEYWDS    COMPETITIVE INHIBITOR, BICYCLIC PEPTIDE, INHIBITOR, PROTEASE, 1, 3,   
KEYWDS   2 5-TRIS(BROMOMETHYL)BENZENE (TBMB) CYCLIZATION, EXTRACELLULAR,        
KEYWDS   3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHEN,F.POJER,C.HEINIS                                               
REVDAT   3   15-NOV-17 4MNW    1       REMARK                                   
REVDAT   2   26-FEB-14 4MNW    1       JRNL                                     
REVDAT   1   05-FEB-14 4MNW    0                                                
JRNL        AUTH   S.CHEN,D.BERTOLDO,A.ANGELINI,F.POJER,C.HEINIS                
JRNL        TITL   PEPTIDE LIGANDS STABILIZED BY SMALL MOLECULES.               
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  53  1602 2014              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   24453110                                                     
JRNL        DOI    10.1002/ANIE.201309459                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 34787                          
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) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.171                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1811                            
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) : 1.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2597                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 126                          
REMARK   3   BIN FREE R VALUE                    : 0.1750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 169                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : 1.71000                                              
REMARK   3    B33 (A**2) : -1.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.094         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.140         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.968                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2153 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1990 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2913 ; 1.164 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4573 ; 1.904 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   258 ; 6.059 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    96 ;35.569 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   357 ;12.115 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;11.187 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   310 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2398 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   504 ; 0.002 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4143 ; 5.010 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    52 ;26.885 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4209 ; 7.761 ; 5.000       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4MNW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082146.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36626                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.13200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG4000, 15% GLYCEROL, 0.17 M        
REMARK 280  AMMONIUM SULFATE, 0.1 M SODIUM ACETATE, PH 4.5, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.28500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.08500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.98000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.08500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.28500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.98000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE BICYCLIC PEPTIDE UK749 IS CYCLIC PEPTIDE, A MEMBER OF INHIBITOR  
REMARK 400 CLASS.                                                               
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: BICYCLIC PEPTIDE UK749                                       
REMARK 400   CHAIN: B                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_2: RESIDUE ZBR                                           
REMARK 400   DESCRIPTION: 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 A  41      -64.49   -106.26                                   
REMARK 500    SER A  54     -156.90   -149.45                                   
REMARK 500    PRO A  60C      44.18    -84.81                                   
REMARK 500    ASP A  93       34.34    -98.16                                   
REMARK 500    TYR A 171     -110.99    -90.97                                   
REMARK 500    SER A 214      -56.94   -124.55                                   
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 SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR BICYCLIC PEPTIDE UK749            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MNV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BICYCLIC PEPTIDE UK729 BOUND AS AN ACYL-ENZYME  
REMARK 900 INTERMEDIATE TO UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)           
REMARK 900 RELATED ID: 4MNX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK811                                
REMARK 900 RELATED ID: 4MNY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK903                                
REMARK 900 RELATED ID: 3QN7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK18                                 
REMARK 900 RELATED ID: 2NWN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH MONO-CYCLIC PEPTIDE UPAIN-1                           
REMARK 900 RELATED ID: 4JK5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK18-D-SER                           
REMARK 900 RELATED ID: 4JK6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK18-D-ABA                           
REMARK 900 RELATED ID: 4GLY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK504                                
DBREF  4MNW A   16   242  UNP    P00749   UROK_HUMAN     179    423             
DBREF  4MNW B    1    14  PDB    4MNW     4MNW             1     14             
SEQADV 4MNW ALA A  122  UNP  P00749    CYS   299 ENGINEERED MUTATION            
SEQADV 4MNW GLN A  145  UNP  P00749    ASN   322 ENGINEERED MUTATION            
SEQRES   1 A  245  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 A  245  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 A  245  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 A  245  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 A  245  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 A  245  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 A  245  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 A  245  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 A  245  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 A  245  GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 A  245  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 A  245  GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 A  245  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 A  245  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 A  245  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 A  245  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 A  245  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 A  245  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 A  245  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR                  
SEQRES   1 B   14  GLN CYS TRP ASP ARG GLY CYS GLU ASN ARG LYS CYS ASN          
SEQRES   2 B   14  NH2                                                          
HET    NH2  B  14       1                                                       
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    GOL  A 303       6                                                       
HET    GOL  A 304       6                                                       
HET    GOL  A 305       6                                                       
HET    GOL  A 306       6                                                       
HET    GOL  A 307       6                                                       
HET    ACT  A 308       4                                                       
HET    ZBR  B 101       9                                                       
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     ZBR 1,3,5-TRIS(BROMOMETHYL)BENZENE                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  GOL    5(C3 H8 O3)                                                  
FORMUL  10  ACT    C2 H3 O2 1-                                                  
FORMUL  11  ZBR    C9 H9 BR3                                                    
FORMUL  12  HOH   *169(H2 O)                                                    
HELIX    1   1 THR A   23  GLN A   27  5                                   5    
HELIX    2   2 ALA A   55  PHE A   59  5                                   5    
HELIX    3   3 LYS A   61  GLU A   62A 5                                   3    
HELIX    4   4 SER A  164  GLN A  169  1                                   6    
HELIX    5   5 TYR A  172  VAL A  176  5                                   5    
HELIX    6   6 PHE A  234  THR A  242  1                                   9    
SHEET    1   A 8 GLU A  20  PHE A  21  0                                        
SHEET    2   A 8 LYS A 156  ILE A 163 -1  O  MET A 157   N  GLU A  20           
SHEET    3   A 8 MET A 180  ALA A 184 -1  O  CYS A 182   N  ILE A 163           
SHEET    4   A 8 GLY A 226  ARG A 230 -1  O  TYR A 228   N  LEU A 181           
SHEET    5   A 8 ARG A 206  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    6   A 8 PRO A 198  LEU A 203 -1  N  LEU A 203   O  ARG A 206           
SHEET    7   A 8 SER A 135  GLY A 140 -1  N  GLU A 137   O  VAL A 200           
SHEET    8   A 8 LYS A 156  ILE A 163 -1  O  VAL A 160   N  CYS A 136           
SHEET    1   B 7 PHE A  30  ARG A  36  0                                        
SHEET    2   B 7 VAL A  38  SER A  48 -1  O  VAL A  41   N  ILE A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  ILE A  53   N  SER A  45           
SHEET    4   B 7 ALA A 104  ARG A 109 -1  O  LEU A 106   N  VAL A  52           
SHEET    5   B 7 MET A  81  LEU A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6   B 7 TYR A  64  LEU A  68 -1  N  VAL A  66   O  PHE A  83           
SHEET    7   B 7 PHE A  30  ARG A  36 -1  N  TYR A  34   O  ILE A  65           
SHEET    1   C 2 SER A  95  ALA A  96  0                                        
SHEET    2   C 2 HIS A  99  HIS A 100 -1  O  HIS A 100   N  SER A  95           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.02  
SSBOND   2 CYS A   50    CYS A  111                          1555   1555  2.03  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.04  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.05  
LINK         C   ASN B  13                 N   NH2 B  14     1555   1555  1.33  
LINK         SG  CYS B  12                 C7  ZBR B 101     1555   1555  1.82  
LINK         SG  CYS B   2                 C8  ZBR B 101     1555   1555  1.82  
LINK         SG  CYS B   7                 C9  ZBR B 101     1555   1555  1.84  
SITE     1 AC1  8 LYS A  61  HIS A 100  THR A 177  LYS A 179                    
SITE     2 AC1  8 MET A 180  GOL A 306  HOH A 518  HOH A 550                    
SITE     1 AC2  5 SER A 164  HIS A 165  ARG A 166  ARG A 206                    
SITE     2 AC2  5 HOH A 549                                                     
SITE     1 AC3  9 THR A  23  SER A  71  ARG A  72  THR A  77                    
SITE     2 AC3  9 GLN A 154  HOH A 523  GLN B   1  CYS B   2                    
SITE     3 AC3  9 TRP B   3                                                     
SITE     1 AC4  6 HIS A 165  GLN A 169  THR A 177  THR A 178                    
SITE     2 AC4  6 HOH A 518  HOH A 550                                          
SITE     1 AC5  4 ARG A  35  HIS A  37  ARG A  37A LYS A 187                    
SITE     1 AC6 10 HIS A  99  HIS A 100  ASN A 101  ASP A 102                    
SITE     2 AC6 10 LYS A 179  MET A 180  SER A 214  TRP A 215                    
SITE     3 AC6 10 THR A 229  SO4 A 301                                          
SITE     1 AC7  4 TRP A 186  LYS A 187  ALA A 221  HOH A 515                    
SITE     1 AC8  3 SER A 125  MET A 126  ARG A 239                               
SITE     1 AC9 44 GLU A  20  PHE A  21  THR A  22  THR A  23                    
SITE     2 AC9 44 ARG A  35  VAL A  41  HIS A  57  CYS A  58                    
SITE     3 AC9 44 ASP A  60A TYR A  60B TYR A  64  ARG A  72                    
SITE     4 AC9 44 LEU A  97B HIS A  99  GLU A 144  GLN A 154                    
SITE     5 AC9 44 GLN A 169  SER A 174  ASP A 189  SER A 190                    
SITE     6 AC9 44 GLN A 192  GLY A 193  SER A 195  TRP A 215                    
SITE     7 AC9 44 GLY A 216  ARG A 217  GLY A 218  LYS A 224                    
SITE     8 AC9 44 GLY A 226  GOL A 303  HOH A 404  HOH A 442                    
SITE     9 AC9 44 HOH A 466  HOH A 526  HOH A 530  HOH B 201                    
SITE    10 AC9 44 HOH B 202  HOH B 203  HOH B 204  HOH B 205                    
SITE    11 AC9 44 HOH B 206  HOH B 207  HOH B 208  HOH B 209                    
CRYST1   52.570   53.960   80.170  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019022  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018532  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012474        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system