HEADER BLOOD CLOTTING 29-SEP-08 3EOX
TITLE HIGH QUALITY STRUCTURE OF CLEAVED PAI-1-STAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR INHIBITOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAI-1;
COMPND 5 SYNONYM: PAI-1, PAI, ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 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 EXPRESSION_SYSTEM_STRAIN: MC1061;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PIGE20
KEYWDS CLEAVED PLASMINOGEN ACTIVATOR INHIBITOR-1, PAI-1, SERPIN, STABILIZED,
KEYWDS 2 GLYCOPROTEIN, PLASMINOGEN ACTIVATION, PROTEASE INHIBITOR, SECRETED,
KEYWDS 3 SERINE PROTEASE INHIBITOR, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DEWILDE,P.J.DECLERCK,A.RABIJNS,S.V.STRELKOV
REVDAT 5 01-NOV-23 3EOX 1 REMARK
REVDAT 4 10-NOV-21 3EOX 1 REMARK SEQADV
REVDAT 3 25-OCT-17 3EOX 1 REMARK
REVDAT 2 13-JUL-11 3EOX 1 VERSN
REVDAT 1 17-FEB-09 3EOX 0
JRNL AUTH M.DEWILDE,S.V.STRELKOV,A.RABIJNS,P.J.DECLERCK
JRNL TITL HIGH QUALITY STRUCTURE OF CLEAVED PAI-1-STAB.
JRNL REF J.STRUCT.BIOL. V. 165 126 2009
JRNL REFN ISSN 1047-8477
JRNL PMID 19059484
JRNL DOI 10.1016/J.JSB.2008.11.001
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 12280
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 603
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) : 2.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 806
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2942
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 5.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.24000
REMARK 3 B12 (A**2) : 0.08000
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): 0.354
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.253
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3030 ; 0.004 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4116 ; 0.792 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 371 ; 4.691 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;32.363 ;23.796
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 513 ;13.987 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;12.413 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 466 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2289 ; 0.003 ; 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): 1855 ; 0.181 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3020 ; 0.359 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1175 ; 0.544 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1094 ; 0.977 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 379
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0940 -27.4390 22.0820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: 0.1030
REMARK 3 T33: 0.1875 T12: -0.0038
REMARK 3 T13: 0.0146 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.5702 L22: 1.8915
REMARK 3 L33: 1.2076 L12: -0.2298
REMARK 3 L13: -0.0363 L23: -0.6317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: 0.0434 S13: 0.1167
REMARK 3 S21: -0.0131 S22: -0.0130 S23: 0.0056
REMARK 3 S31: -0.0621 S32: -0.0163 S33: -0.0243
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 3EOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8084
REMARK 200 MONOCHROMATOR : SI 111 HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12280
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.610
REMARK 200 RESOLUTION RANGE LOW (A) : 19.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 9PAI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M LITHIUM SULPHATE MONOHYDRATE, 15%
REMARK 280 PEG 8000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -Y,-X,-Z+2/3
REMARK 290 5555 -X+Y,Y,-Z+1/3
REMARK 290 6555 X,X-Y,-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 -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 47.22133
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 94.44267
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 94.44267
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 47.22133
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 ARG A 118
REMARK 465 SER A 119
REMARK 465 SER A 344
REMARK 465 ALA A 345
REMARK 465 ARG A 346
REMARK 465 MET A 347
REMARK 465 ALA A 348
REMARK 465 PRO A 349
REMARK 465 GLU A 350
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 56 CA CB CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 56 N GLN A 56 CA 0.158
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 SER A 27 61.64 -117.75
REMARK 500 LYS A 88 -52.79 63.56
REMARK 500 ASN A 172 113.14 -170.04
REMARK 500 PHE A 302 -35.99 72.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DB2 RELATED DB: PDB
REMARK 900 STABILIZED, INTACT, ACTIVE CONFORMATION OF PAI-1
REMARK 900 RELATED ID: 9PAI RELATED DB: PDB
REMARK 900 CLEAVED SUBSTRATE VARIANT OF PAI-1
DBREF 3EOX A 1 379 UNP P05121 PAI1_HUMAN 24 402
SEQADV 3EOX HIS A 150 UNP P05121 ASN 173 ENGINEERED MUTATION
SEQADV 3EOX THR A 154 UNP P05121 LYS 177 ENGINEERED MUTATION
SEQADV 3EOX PRO A 301 UNP P05121 GLN 324 ENGINEERED MUTATION
SEQADV 3EOX LEU A 319 UNP P05121 GLN 342 ENGINEERED MUTATION
SEQADV 3EOX ILE A 354 UNP P05121 MET 377 ENGINEERED MUTATION
SEQRES 1 A 379 VAL HIS HIS PRO PRO SER TYR VAL ALA HIS LEU ALA SER
SEQRES 2 A 379 ASP PHE GLY VAL ARG VAL PHE GLN GLN VAL ALA GLN ALA
SEQRES 3 A 379 SER LYS ASP ARG ASN VAL VAL PHE SER PRO TYR GLY VAL
SEQRES 4 A 379 ALA SER VAL LEU ALA MET LEU GLN LEU THR THR GLY GLY
SEQRES 5 A 379 GLU THR GLN GLN GLN ILE GLN ALA ALA MET GLY PHE LYS
SEQRES 6 A 379 ILE ASP ASP LYS GLY MET ALA PRO ALA LEU ARG HIS LEU
SEQRES 7 A 379 TYR LYS GLU LEU MET GLY PRO TRP ASN LYS ASP GLU ILE
SEQRES 8 A 379 SER THR THR ASP ALA ILE PHE VAL GLN ARG ASP LEU LYS
SEQRES 9 A 379 LEU VAL GLN GLY PHE MET PRO HIS PHE PHE ARG LEU PHE
SEQRES 10 A 379 ARG SER THR VAL LYS GLN VAL ASP PHE SER GLU VAL GLU
SEQRES 11 A 379 ARG ALA ARG PHE ILE ILE ASN ASP TRP VAL LYS THR HIS
SEQRES 12 A 379 THR LYS GLY MET ILE SER HIS LEU LEU GLY THR GLY ALA
SEQRES 13 A 379 VAL ASP GLN LEU THR ARG LEU VAL LEU VAL ASN ALA LEU
SEQRES 14 A 379 TYR PHE ASN GLY GLN TRP LYS THR PRO PHE PRO ASP SER
SEQRES 15 A 379 SER THR HIS ARG ARG LEU PHE HIS LYS SER ASP GLY SER
SEQRES 16 A 379 THR VAL SER VAL PRO MET MET ALA GLN THR ASN LYS PHE
SEQRES 17 A 379 ASN TYR THR GLU PHE THR THR PRO ASP GLY HIS TYR TYR
SEQRES 18 A 379 ASP ILE LEU GLU LEU PRO TYR HIS GLY ASP THR LEU SER
SEQRES 19 A 379 MET PHE ILE ALA ALA PRO TYR GLU LYS GLU VAL PRO LEU
SEQRES 20 A 379 SER ALA LEU THR ASN ILE LEU SER ALA GLN LEU ILE SER
SEQRES 21 A 379 HIS TRP LYS GLY ASN MET THR ARG LEU PRO ARG LEU LEU
SEQRES 22 A 379 VAL LEU PRO LYS PHE SER LEU GLU THR GLU VAL ASP LEU
SEQRES 23 A 379 ARG LYS PRO LEU GLU ASN LEU GLY MET THR ASP MET PHE
SEQRES 24 A 379 ARG PRO PHE GLN ALA ASP PHE THR SER LEU SER ASP GLN
SEQRES 25 A 379 GLU PRO LEU HIS VAL ALA LEU ALA LEU GLN LYS VAL LYS
SEQRES 26 A 379 ILE GLU VAL ASN GLU SER GLY THR VAL ALA SER SER SER
SEQRES 27 A 379 THR ALA VAL ILE VAL SER ALA ARG MET ALA PRO GLU GLU
SEQRES 28 A 379 ILE ILE ILE ASP ARG PRO PHE LEU PHE VAL VAL ARG HIS
SEQRES 29 A 379 ASN PRO THR GLY THR VAL LEU PHE MET GLY GLN VAL MET
SEQRES 30 A 379 GLU PRO
FORMUL 2 HOH *123(H2 O)
HELIX 1 1 HIS A 2 SER A 27 1 26
HELIX 2 2 SER A 35 THR A 50 1 16
HELIX 3 3 GLY A 51 GLY A 63 1 13
HELIX 4 4 GLY A 70 GLY A 84 1 15
HELIX 5 5 PRO A 85 LYS A 88 5 4
HELIX 6 6 GLY A 108 ARG A 115 1 8
HELIX 7 7 GLU A 128 HIS A 143 1 16
HELIX 8 8 PRO A 180 THR A 184 5 5
HELIX 9 9 LEU A 247 ASN A 252 1 6
HELIX 10 10 SER A 255 ASN A 265 1 11
HELIX 11 11 LEU A 286 LEU A 293 1 8
HELIX 12 12 THR A 296 ARG A 300 5 5
SHEET 1 A 7 VAL A 32 PHE A 34 0
SHEET 2 A 7 THR A 369 VAL A 376 -1 O MET A 373 N PHE A 34
SHEET 3 A 7 PHE A 358 HIS A 364 -1 N VAL A 362 O PHE A 372
SHEET 4 A 7 LEU A 233 PRO A 240 -1 N PHE A 236 O VAL A 361
SHEET 5 A 7 TYR A 220 PRO A 227 -1 N ASP A 222 O ALA A 239
SHEET 6 A 7 THR A 196 THR A 214 -1 N PHE A 213 O TYR A 221
SHEET 7 A 7 HIS A 185 HIS A 190 -1 N PHE A 189 O VAL A 197
SHEET 1 B 8 VAL A 32 PHE A 34 0
SHEET 2 B 8 THR A 369 VAL A 376 -1 O MET A 373 N PHE A 34
SHEET 3 B 8 PHE A 358 HIS A 364 -1 N VAL A 362 O PHE A 372
SHEET 4 B 8 LEU A 233 PRO A 240 -1 N PHE A 236 O VAL A 361
SHEET 5 B 8 TYR A 220 PRO A 227 -1 N ASP A 222 O ALA A 239
SHEET 6 B 8 THR A 196 THR A 214 -1 N PHE A 213 O TYR A 221
SHEET 7 B 8 THR A 267 PRO A 276 -1 O LEU A 275 N MET A 202
SHEET 8 B 8 ILE A 352 ILE A 353 1 O ILE A 352 N LEU A 272
SHEET 1 C 6 LYS A 122 VAL A 124 0
SHEET 2 C 6 GLU A 90 GLN A 100 1 N VAL A 99 O VAL A 124
SHEET 3 C 6 LEU A 163 GLN A 174 -1 O ASN A 172 N GLU A 90
SHEET 4 C 6 GLY A 332 ILE A 342 -1 O SER A 337 N LEU A 169
SHEET 5 C 6 LEU A 319 VAL A 328 -1 N GLU A 327 O VAL A 334
SHEET 6 C 6 PHE A 278 ASP A 285 -1 N PHE A 278 O VAL A 328
CISPEP 1 ASN A 172 GLY A 173 0 3.60
CRYST1 71.174 71.174 141.664 90.00 90.00 120.00 P 31 1 2 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 0.014050 0.008112 0.000000 0.00000
SCALE2 0.000000 0.016224 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END