HEADER HYDROLASE/HYDROLASE INHIBITOR 12-FEB-14 4OS1
TITLE CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)
TITLE 2 COMPLEXED WITH BICYCLIC PEPTIDE UK601 (BICYCLIC 1)
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 UK601 (BICYCLIC 1);
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_CELL_LINE: 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 4 02-JUN-21 4OS1 1 SOURCE REMARK SEQADV LINK
REVDAT 3 22-NOV-17 4OS1 1 REMARK
REVDAT 2 05-NOV-14 4OS1 1 JRNL
REVDAT 1 24-SEP-14 4OS1 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 12091
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 623
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 882
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.2850
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 : 14
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.47000
REMARK 3 B22 (A**2) : -0.74000
REMARK 3 B33 (A**2) : 2.21000
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): 0.316
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.064
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2105 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1957 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2853 ; 1.185 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4497 ; 0.731 ; 3.005
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 6.241 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 92 ;29.833 ;23.043
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 351 ;14.934 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.164 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 306 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2363 ; 0.004 ; 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 4OS1 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_1000084878.
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 : 12754
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 45.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.08600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.40
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 (%): 40.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
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 26.20100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.49750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.86400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.49750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.20100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.86400
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: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 UK601 (BICYCLIC 1) IS CYCLIC PEPTIDE, A MEMBER
REMARK 400 OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: BICYCLIC PEPTIDE UK601 (BICYCLIC 1)
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 GLN A 27 53.00 -143.50
REMARK 500 VAL A 41 -63.39 -104.58
REMARK 500 SER A 54 -155.72 -149.68
REMARK 500 ASP A 97 -167.58 -102.57
REMARK 500 TYR A 171 -109.09 -88.29
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 ACT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF BICYCLIC PEPTIDE
REMARK 800 UK601 (BICYCLIC 1)
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: 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: 4OS5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA)
REMARK 900 COMPLEXED WITH BICYCLIC PEPTIDE UK603 (BICYCLIC 2)
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 4OS1 A 16 242 UNP P00749 UROK_HUMAN 179 423
DBREF 4OS1 B 1 15 PDB 4OS1 4OS1 1 15
SEQADV 4OS1 ALA A 122 UNP P00749 CYS 299 ENGINEERED MUTATION
SEQADV 4OS1 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 81S ALA LEU GLY ARG GLY CYS GLU ASN HIS ARG CYS
SEQRES 2 B 15 LEU NH2
HET 81S B 2 9
HET NH2 B 15 1
HET SO4 A 301 5
HET SO4 A 302 5
HET ACT A 303 4
HETNAM 81S (4S)-4,5-DISULFANYL-L-NORVALINE
HETNAM NH2 AMINO GROUP
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
FORMUL 2 81S C5 H11 N O2 S2
FORMUL 2 NH2 H2 N
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 ACT C2 H3 O2 1-
FORMUL 6 HOH *130(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 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 GLY A 44 N ALA A 31
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 LEU A 68 O MET A 81
SHEET 7 B 7 PHE A 30 ARG A 36 -1 N ALA A 32 O TYR A 67
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 2.05
SSBOND 2 CYS A 50 CYS A 111 1555 1555 2.02
SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.04
LINK C GLY B 1 N 81S B 2 1555 1555 1.33
LINK C 81S B 2 N ALA B 3 1555 1555 1.33
LINK SE 81S B 2 SG CYS B 8 1555 1555 2.05
LINK SD2 81S B 2 SG CYS B 13 1555 1555 2.05
LINK C LEU B 14 N NH2 B 15 1555 1555 1.37
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 417
SITE 1 AC2 4 ARG A 35 HIS A 37 ARG A 37A LYS A 187
SITE 1 AC3 3 LYS A 110A LYS A 223 HOH A 490
SITE 1 AC4 29 GLU A 20 PHE A 21 THR A 23 ARG A 35
SITE 2 AC4 29 HIS A 57 CYS A 58 ASP A 60A TYR A 60B
SITE 3 AC4 29 TYR A 64 HIS A 99 SER A 174 ASP A 189
SITE 4 AC4 29 SER A 190 CYS A 191 GLN A 192 GLY A 193
SITE 5 AC4 29 SER A 195 SER A 214 TRP A 215 GLY A 218
SITE 6 AC4 29 GLY A 226 HOH A 444 HOH A 469 HOH A 471
SITE 7 AC4 29 HOH B 101 HOH B 102 HOH B 103 HOH B 104
SITE 8 AC4 29 HOH B 105
CRYST1 52.402 53.728 84.995 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 0.019083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018612 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011765 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
