HEADER HYDROLASE INHIBITOR/HYDROLASE 20-OCT-10 3PB1
TITLE CRYSTAL STRUCTURE OF A MICHAELIS COMPLEX BETWEEN PLASMINOGEN ACTIVATOR
TITLE 2 INHIBITOR-1 AND UROKINASE-TYPE PLASMINOGEN ACTIVATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR INHIBITOR 1;
COMPND 3 CHAIN: I;
COMPND 4 SYNONYM: PAI, PAI-1, ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR,
COMPND 5 SERPIN E1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PLASMINOGEN ACTIVATOR, UROKINASE;
COMPND 10 CHAIN: E;
COMPND 11 FRAGMENT: UNP RESIDUES 143-395;
COMPND 12 EC: 3.4.21.73;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SERPINE1, PAI1, PLANH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: PLAU, RP11-417O11.1-002;
SOURCE 13 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS PAI-1, UPA, MICHAELIS COMPLEX, STRUCTURAL GENOMICS, STRUCTURE 2
KEYWDS 2 FUNCTION PROJECT, S2F, HYDROLASE INHIBITOR-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LIN,L.JIANG,M.HUANG,STRUCTURE 2 FUNCTION PROJECT (S2F)
REVDAT 3 01-NOV-23 3PB1 1 REMARK SEQADV
REVDAT 2 09-MAR-11 3PB1 1 JRNL
REVDAT 1 29-DEC-10 3PB1 0
JRNL AUTH Z.LIN,L.JIANG,C.YUAN,J.K.JENSEN,X.ZHANG,Z.LUO,B.C.FURIE,
JRNL AUTH 2 B.FURIE,P.A.ANDREASEN,M.HUANG
JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF UROKINASE-TYPE
JRNL TITL 2 PLASMINOGEN ACTIVATOR BY PLASMINOGEN ACTIVATOR INHIBITOR-1.
JRNL REF J.BIOL.CHEM. V. 286 7027 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21199867
JRNL DOI 10.1074/JBC.M110.204537
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 40338
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2142
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4926
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 314
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.230
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.160
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.525
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5061 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6864 ; 1.260 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 619 ; 6.720 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 225 ;34.977 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 862 ;17.958 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;19.617 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 760 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3804 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3098 ; 0.586 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5025 ; 1.140 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1963 ; 1.562 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1839 ; 2.720 ; 4.500
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3PB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80462
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.16200
REMARK 200 R SYM (I) : 0.18500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.58900
REMARK 200 R SYM FOR SHELL (I) : 0.63300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1DVM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M AMMONIUM SULFATE, 0.1M TRIS-HCL,
REMARK 280 PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.61067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.30533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.30533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 114.61067
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: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL I 1
REMARK 465 HIS I 2
REMARK 465 HIS I 3
REMARK 465 PRO I 4
REMARK 465 GLU E 245
REMARK 465 ASN E 246
REMARK 465 GLY E 247
REMARK 465 LEU E 248
REMARK 465 ALA E 249
REMARK 465 LEU E 250
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO I 379 O
REMARK 470 GLU E 244 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP I 14 NH1 ARG I 18 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU I 169 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN I 206 -162.68 -162.37
REMARK 500 GLU I 313 132.68 -175.19
REMARK 500 THR I 339 -80.28 -26.54
REMARK 500 ALA I 340 135.17 178.34
REMARK 500 SER E 54 -157.16 -153.53
REMARK 500 LEU E 97B -51.41 -143.62
REMARK 500 TYR E 171 -86.74 -89.65
REMARK 500 SER E 214 -75.10 -120.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU I 313 PRO I 314 124.81
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 E 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DVM RELATED DB: PDB
REMARK 900 ACTIVE FORM PLASMINOGEN ACTIVATOR INHIBITOR-1
REMARK 900 RELATED ID: 2O8T RELATED DB: PDB
REMARK 900 UROKINASE PLASMINOGEN ACTIVATOR
DBREF 3PB1 I 1 379 UNP P05121 PAI1_HUMAN 24 402
DBREF 3PB1 E 16 250 UNP Q5SWW8 Q5SWW8_HUMAN 143 395
SEQADV 3PB1 HIS I 150 UNP P05121 ASN 173 ENGINEERED MUTATION
SEQADV 3PB1 THR I 154 UNP P05121 LYS 177 ENGINEERED MUTATION
SEQADV 3PB1 GLN I 158 UNP P05121 ASP 181 CONFLICT
SEQADV 3PB1 LEU I 319 UNP P05121 GLN 342 ENGINEERED MUTATION
SEQADV 3PB1 ILE I 354 UNP P05121 MET 377 ENGINEERED MUTATION
SEQADV 3PB1 ALA E 122 UNP Q5SWW8 CYS 263 CONFLICT
SEQADV 3PB1 GLN E 145 UNP Q5SWW8 ASN 286 CONFLICT
SEQADV 3PB1 ALA E 195 UNP Q5SWW8 SER 340 ENGINEERED MUTATION
SEQRES 1 I 379 VAL HIS HIS PRO PRO SER TYR VAL ALA HIS LEU ALA SER
SEQRES 2 I 379 ASP PHE GLY VAL ARG VAL PHE GLN GLN VAL ALA GLN ALA
SEQRES 3 I 379 SER LYS ASP ARG ASN VAL VAL PHE SER PRO TYR GLY VAL
SEQRES 4 I 379 ALA SER VAL LEU ALA MET LEU GLN LEU THR THR GLY GLY
SEQRES 5 I 379 GLU THR GLN GLN GLN ILE GLN ALA ALA MET GLY PHE LYS
SEQRES 6 I 379 ILE ASP ASP LYS GLY MET ALA PRO ALA LEU ARG HIS LEU
SEQRES 7 I 379 TYR LYS GLU LEU MET GLY PRO TRP ASN LYS ASP GLU ILE
SEQRES 8 I 379 SER THR THR ASP ALA ILE PHE VAL GLN ARG ASP LEU LYS
SEQRES 9 I 379 LEU VAL GLN GLY PHE MET PRO HIS PHE PHE ARG LEU PHE
SEQRES 10 I 379 ARG SER THR VAL LYS GLN VAL ASP PHE SER GLU VAL GLU
SEQRES 11 I 379 ARG ALA ARG PHE ILE ILE ASN ASP TRP VAL LYS THR HIS
SEQRES 12 I 379 THR LYS GLY MET ILE SER HIS LEU LEU GLY THR GLY ALA
SEQRES 13 I 379 VAL GLN GLN LEU THR ARG LEU VAL LEU VAL ASN ALA LEU
SEQRES 14 I 379 TYR PHE ASN GLY GLN TRP LYS THR PRO PHE PRO ASP SER
SEQRES 15 I 379 SER THR HIS ARG ARG LEU PHE HIS LYS SER ASP GLY SER
SEQRES 16 I 379 THR VAL SER VAL PRO MET MET ALA GLN THR ASN LYS PHE
SEQRES 17 I 379 ASN TYR THR GLU PHE THR THR PRO ASP GLY HIS TYR TYR
SEQRES 18 I 379 ASP ILE LEU GLU LEU PRO TYR HIS GLY ASP THR LEU SER
SEQRES 19 I 379 MET PHE ILE ALA ALA PRO TYR GLU LYS GLU VAL PRO LEU
SEQRES 20 I 379 SER ALA LEU THR ASN ILE LEU SER ALA GLN LEU ILE SER
SEQRES 21 I 379 HIS TRP LYS GLY ASN MET THR ARG LEU PRO ARG LEU LEU
SEQRES 22 I 379 VAL LEU PRO LYS PHE SER LEU GLU THR GLU VAL ASP LEU
SEQRES 23 I 379 ARG LYS PRO LEU GLU ASN LEU GLY MET THR ASP MET PHE
SEQRES 24 I 379 ARG GLN PHE GLN ALA ASP PHE THR SER LEU SER ASP GLN
SEQRES 25 I 379 GLU PRO LEU HIS VAL ALA LEU ALA LEU GLN LYS VAL LYS
SEQRES 26 I 379 ILE GLU VAL ASN GLU SER GLY THR VAL ALA SER SER SER
SEQRES 27 I 379 THR ALA VAL ILE VAL SER ALA ARG MET ALA PRO GLU GLU
SEQRES 28 I 379 ILE ILE ILE ASP ARG PRO PHE LEU PHE VAL VAL ARG HIS
SEQRES 29 I 379 ASN PRO THR GLY THR VAL LEU PHE MET GLY GLN VAL MET
SEQRES 30 I 379 GLU PRO
SEQRES 1 E 253 ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO
SEQRES 2 E 253 TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER
SEQRES 3 E 253 VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS
SEQRES 4 E 253 TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO
SEQRES 5 E 253 LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG
SEQRES 6 E 253 LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL
SEQRES 7 E 253 GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR
SEQRES 8 E 253 LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG
SEQRES 9 E 253 SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE
SEQRES 10 E 253 GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN
SEQRES 11 E 253 PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU
SEQRES 12 E 253 GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET
SEQRES 13 E 253 THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN
SEQRES 14 E 253 PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU
SEQRES 15 E 253 CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN
SEQRES 16 E 253 GLY ASP ALA GLY GLY PRO LEU VAL CYS SER LEU GLN GLY
SEQRES 17 E 253 ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY
SEQRES 18 E 253 CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL
SEQRES 19 E 253 SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU
SEQRES 20 E 253 GLU ASN GLY LEU ALA LEU
HET SO4 E 1 5
HET SO4 E 2 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *314(H2 O)
HELIX 1 1 PRO I 5 ALA I 26 1 22
HELIX 2 2 SER I 35 LEU I 48 1 14
HELIX 3 3 GLY I 51 GLY I 63 1 13
HELIX 4 4 GLY I 70 MET I 83 1 14
HELIX 5 5 GLY I 108 ARG I 118 1 11
HELIX 6 6 GLU I 128 THR I 144 1 17
HELIX 7 7 LEU I 152 VAL I 157 5 6
HELIX 8 8 PRO I 180 THR I 184 5 5
HELIX 9 9 HIS I 229 ASP I 231 5 3
HELIX 10 10 LEU I 247 ASN I 252 1 6
HELIX 11 11 SER I 255 ASN I 265 1 11
HELIX 12 12 LEU I 286 LEU I 293 1 8
HELIX 13 13 THR I 296 ARG I 300 5 5
HELIX 14 14 THR E 23 GLN E 27 5 5
HELIX 15 15 ALA E 55 PHE E 59 5 5
HELIX 16 16 LYS E 61 GLU E 62A 5 3
HELIX 17 17 SER E 164 GLN E 169 1 6
HELIX 18 18 TYR E 172 VAL E 176 5 5
HELIX 19 19 PHE E 234 THR E 242 1 9
SHEET 1 A 7 VAL I 32 PHE I 34 0
SHEET 2 A 7 THR I 369 VAL I 376 -1 O MET I 373 N PHE I 34
SHEET 3 A 7 PHE I 358 HIS I 364 -1 N PHE I 358 O VAL I 376
SHEET 4 A 7 LEU I 233 PRO I 240 -1 N PHE I 236 O VAL I 361
SHEET 5 A 7 TYR I 220 PRO I 227 -1 N LEU I 226 O MET I 235
SHEET 6 A 7 THR I 196 THR I 214 -1 N ASN I 209 O GLU I 225
SHEET 7 A 7 HIS I 185 HIS I 190 -1 N HIS I 185 O MET I 201
SHEET 1 B 8 VAL I 32 PHE I 34 0
SHEET 2 B 8 THR I 369 VAL I 376 -1 O MET I 373 N PHE I 34
SHEET 3 B 8 PHE I 358 HIS I 364 -1 N PHE I 358 O VAL I 376
SHEET 4 B 8 LEU I 233 PRO I 240 -1 N PHE I 236 O VAL I 361
SHEET 5 B 8 TYR I 220 PRO I 227 -1 N LEU I 226 O MET I 235
SHEET 6 B 8 THR I 196 THR I 214 -1 N ASN I 209 O GLU I 225
SHEET 7 B 8 THR I 267 PRO I 276 -1 O LEU I 275 N MET I 202
SHEET 8 B 8 GLU I 351 ILE I 353 1 O ILE I 352 N LEU I 272
SHEET 1 C 5 LYS I 122 VAL I 124 0
SHEET 2 C 5 ILE I 91 GLN I 100 1 N VAL I 99 O LYS I 122
SHEET 3 C 5 LEU I 163 ASN I 172 -1 O VAL I 164 N PHE I 98
SHEET 4 C 5 LEU I 319 VAL I 328 1 O LYS I 323 N ASN I 167
SHEET 5 C 5 PHE I 278 ASP I 285 -1 N VAL I 284 O GLN I 322
SHEET 1 D 8 GLU E 20 PHE E 21 0
SHEET 2 D 8 LYS E 156 ILE E 163 -1 O MET E 157 N GLU E 20
SHEET 3 D 8 MET E 180 ALA E 184 -1 O ALA E 184 N LYS E 161
SHEET 4 D 8 GLY E 226 ARG E 230 -1 O TYR E 228 N LEU E 181
SHEET 5 D 8 ARG E 206 TRP E 215 -1 N TRP E 215 O VAL E 227
SHEET 6 D 8 PRO E 198 LEU E 203 -1 N CYS E 201 O THR E 208
SHEET 7 D 8 SER E 135 GLY E 140 -1 N GLU E 137 O VAL E 200
SHEET 8 D 8 LYS E 156 ILE E 163 -1 O VAL E 160 N CYS E 136
SHEET 1 E 7 PHE E 30 ARG E 36 0
SHEET 2 E 7 VAL E 38 SER E 48 -1 O THR E 39 N ARG E 35
SHEET 3 E 7 TRP E 51 SER E 54 -1 O ILE E 53 N SER E 45
SHEET 4 E 7 ALA E 104 ARG E 109 -1 O LEU E 106 N VAL E 52
SHEET 5 E 7 MET E 81 LEU E 90 -1 N ILE E 89 O LEU E 105
SHEET 6 E 7 TYR E 64 LEU E 68 -1 N VAL E 66 O PHE E 83
SHEET 7 E 7 PHE E 30 ARG E 36 -1 N TYR E 34 O ILE E 65
SHEET 1 F 2 SER E 95 ALA E 96 0
SHEET 2 F 2 HIS E 99 HIS E 100 -1 O HIS E 100 N SER E 95
SSBOND 1 CYS E 42 CYS E 58 1555 1555 2.03
SSBOND 2 CYS E 50 CYS E 111 1555 1555 2.05
SSBOND 3 CYS E 136 CYS E 201 1555 1555 2.05
SSBOND 4 CYS E 168 CYS E 182 1555 1555 2.05
SSBOND 5 CYS E 191 CYS E 220 1555 1555 2.05
SITE 1 AC1 6 SER E 48 PRO E 49 CYS E 50 TRP E 51
SITE 2 AC1 6 ARG I 30 HOH I 497
SITE 1 AC2 3 SER E 125 MET E 126 ARG E 239
CRYST1 97.711 97.711 171.916 90.00 90.00 120.00 P 32 2 1 6
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 0.010234 0.005909 0.000000 0.00000
SCALE2 0.000000 0.011818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
