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Database: PDB
Entry: 4OS5
LinkDB: 4OS5
Original site: 4OS5 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           12-FEB-14   4OS5              
TITLE     CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)       
TITLE    2 COMPLEXED WITH BICYCLIC PEPTIDE UK603 (BICYCLIC 2)                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 179-423);                   
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 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: BICYCLIC PEPTIDE UK603 (BICYCLIC 2);                       
COMPND  13 CHAIN: B;                                                            
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_STRAIN: HEK293;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PSECTAGA;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES                                                       
KEYWDS    BICYCLIC PEPTIDE, INHIBITOR, PROTEASE, DISULFIDE BRIDGES,             
KEYWDS   2 CYCLIZATION, EXTRACELLULAR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHEN,F.POJER,C.HEINIS                                               
REVDAT   3   22-NOV-17 4OS5    1       REMARK                                   
REVDAT   2   05-NOV-14 4OS5    1       JRNL                                     
REVDAT   1   24-SEP-14 4OS5    0                                                
JRNL        AUTH   S.CHEN,R.GOPALAKRISHNAN,T.SCHAER,F.MARGER,R.HOVIUS,          
JRNL        AUTH 2 D.BERTRAND,F.POJER,C.HEINIS                                  
JRNL        TITL   DITHIOL AMINO ACIDS CAN STRUCTURALLY SHAPE AND ENHANCE THE   
JRNL        TITL 2 LIGAND-BINDING PROPERTIES OF POLYPEPTIDES.                   
JRNL        REF    NAT CHEM                      V.   6  1009 2014              
JRNL        REFN                   ESSN 1755-4349                               
JRNL        PMID   25343607                                                     
JRNL        DOI    10.1038/NCHEM.2043                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 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) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 10703                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 563                             
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) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 737                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 44                           
REMARK   3   BIN FREE R VALUE                    : 0.2000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2038                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.37000                                             
REMARK   3    B22 (A**2) : -2.03000                                             
REMARK   3    B33 (A**2) : 3.39000                                              
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): 0.402         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.233         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2102 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1954 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2850 ; 1.421 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4491 ; 0.790 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   257 ; 6.269 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    92 ;32.904 ;23.043       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   351 ;15.194 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;16.255 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   306 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2359 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   496 ; 0.001 ; 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):  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 : 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 4OS5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084882.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-13                          
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                       : X06DA                              
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                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11300                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.900                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% 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       26.19650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.08850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.96700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.08850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.19650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.96700            
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: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 UK603 (BICYCLIC 2) IS CYCLIC PEPTIDE, A MEMBER  
REMARK 400 OF INHIBITOR CLASS.                                                  
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: BICYCLIC PEPTIDE UK603 (BICYCLIC 2)                          
REMARK 400   CHAIN: B                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
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      -60.28   -108.00                                   
REMARK 500    SER A  54     -156.33   -151.52                                   
REMARK 500    PRO A  60C      34.00    -83.87                                   
REMARK 500    ASP A  97     -164.98   -100.98                                   
REMARK 500    TYR A 127       46.83     38.18                                   
REMARK 500    TYR A 171     -108.18    -89.80                                   
REMARK 500    SER A 214      -58.62   -128.20                                   
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 CHAIN B OF BICYCLIC PEPTIDE       
REMARK 800  UK603 (BICYCLIC 2)                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GLY   RELATED DB: PDB                                   
REMARK 900 HUMAN UROKINASE-TYPE PLASMINOGEN ACTIVATOR UPA IN COMPLEX WITH THE   
REMARK 900 TWO-DISULFIDE BRIDGE PEPTIDE UK504                                   
REMARK 900 RELATED ID: 4OS1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK601 (BICYCLIC 1)                   
REMARK 900 RELATED ID: 4OS2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK602 (BICYCLIC 1)                   
REMARK 900 RELATED ID: 4OS4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK603 (BICYCLIC 1)                   
REMARK 900 RELATED ID: 4OS6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK604 (BICYCLIC 2)                   
REMARK 900 RELATED ID: 4OS7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)      
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK607 (BICYCLIC)                     
DBREF  4OS5 A   16   242  UNP    P00749   UROK_HUMAN     179    423             
DBREF  4OS5 B    1    15  PDB    4OS5     4OS5             1     15             
SEQADV 4OS5 ALA A  122  UNP  P00749    CYS   299 ENGINEERED MUTATION            
SEQADV 4OS5 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   15  GLY 81R ALA LEU GLY ARG GLY CYS GLU ASN HIS ARG CYS          
SEQRES   2 B   15  LEU NH2                                                      
HET    81R  B   2       9                                                       
HET    NH2  B  15       1                                                       
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HETNAM     81R (4R)-4,5-DISULFANYL-L-NORVALINE                                  
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  81R    C5 H11 N O2 S2                                               
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *105(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  ALA A 184   N  LYS A 161           
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  CYS A 201   O  THR A 208           
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  GLU A  84   O  ARG A 109           
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  2.06  
SSBOND   2 CYS A   50    CYS A  111                          1555   1555  2.01  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  1.99  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.05  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.04  
LINK         C   GLY B   1                 N   81R B   2     1555   1555  1.34  
LINK         C   81R B   2                 N   ALA B   3     1555   1555  1.34  
LINK         C   LEU B  14                 N   NH2 B  15     1555   1555  1.36  
LINK         SD2 81R B   2                 SG  CYS B   8     1555   1555  2.03  
LINK         SE  81R B   2                 SG  CYS B  13     1555   1555  2.04  
SITE     1 AC1  6 LYS A  61  HIS A 100  THR A 177  LYS A 179                    
SITE     2 AC1  6 MET A 180  HOH A 401                                          
SITE     1 AC2  3 ARG A  35  HIS A  37  ARG A  37A                              
SITE     1 AC3 34 GLY A  19  GLU A  20  PHE A  21  THR A  22                    
SITE     2 AC3 34 ASN A  26  ARG A  35  VAL A  41  HIS A  57                    
SITE     3 AC3 34 CYS A  58  ASP A  60A TYR A  60B TYR A  64                    
SITE     4 AC3 34 HIS A  99  GLU A 144  SER A 174  ASP A 189                    
SITE     5 AC3 34 SER A 190  CYS A 191  GLN A 192  GLY A 193                    
SITE     6 AC3 34 SER A 195  SER A 214  TRP A 215  GLY A 218                    
SITE     7 AC3 34 GLY A 226  HOH A 402  HOH A 419  HOH A 463                    
SITE     8 AC3 34 HOH A 483  HOH A 491  HOH B 101  HOH B 102                    
SITE     9 AC3 34 HOH B 103  HOH B 104                                          
CRYST1   52.393   53.934   82.177  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      0.019087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018541  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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