HEADER BLOOD CLOTTING 17-MAR-11 3R4L
TITLE HUMAN VERY LONG HALF LIFE PLASMINOGEN ACTIVATOR INHIBITOR TYPE-1
CAVEAT 3R4L NAG B 1 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR INHIBITOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 24-402;
COMPND 5 SYNONYM: PAI, PAI-1, ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR,
COMPND 6 SERPIN E1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: ACTIVE FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PAI1, PLANH1, SERPINE1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS SERINE PROTEASE INHIBITOR, PAI-1, VERY LONG HALF LIFE, PLASMINOGEN
KEYWDS 2 ACTIVATOR INHIBITOR TYPE 1, CARBOHYDRATE, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YANG,H.ZHENG,Q.HAN,E.SKRZYPCZAK-JANKUN,J.JANKUN
REVDAT 4 13-SEP-23 3R4L 1 HETSYN
REVDAT 3 29-JUL-20 3R4L 1 CAVEAT COMPND REMARK SEQADV
REVDAT 3 2 1 HET HETNAM FORMUL LINK
REVDAT 3 3 1 SITE ATOM
REVDAT 2 08-NOV-17 3R4L 1 REMARK
REVDAT 1 02-NOV-11 3R4L 0
JRNL AUTH J.JANKUN,J.YANG,H.ZHENG,F.Q.HAN,A.AL-SENAIDY,
JRNL AUTH 2 E.SKRZYPCZAK-JANKUN
JRNL TITL REMARKABLE EXTENSION OF PAI-1 HALF-LIFE SURPRISINGLY BRINGS
JRNL TITL 2 NO CHANGES TO ITS STRUCTURE.
JRNL REF INT.J.MOL.MED. V. 29 61 2012
JRNL REFN ISSN 1107-3756
JRNL PMID 21947232
JRNL DOI 10.3892/IJMM.2011.798
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.CHOROSTOWSKA-WYNIMKO,R.SWIERCZ,E.SKRZYPCZAK-JANKUN,
REMARK 1 AUTH 2 A.WOJTOWICZ,S.H.SELMAN,J.JANKUN
REMARK 1 TITL A NOVEL FORM OF THE PLASMINOGEN ACTIVATOR INHIBITOR CREATED
REMARK 1 TITL 2 BY CYSTEINE MUTATIONS EXTENDS ITS HALF-LIFE: RELEVANCE TO
REMARK 1 TITL 3 CANCER AND ANGIOGENESIS.
REMARK 1 REF MOL.CANCER THER. V. 2 19 2003
REMARK 1 REFN ISSN 1535-7163
REMARK 1 PMID 12533669
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.JANKUN,A.M.ALEEM,S.H.SELMAN,V.BASRUR,E.SKRZYPCZAK-JANKUN
REMARK 1 TITL VLHL PLASMINOGEN ACTIVATOR INHIBITOR SPONTANEOUSLY
REMARK 1 TITL 2 REACTIVATES FROM THE LATENT TO ACTIVE FORM.
REMARK 1 REF INT.J.MOL.MED. V. 23 57 2009
REMARK 1 REFN ISSN 1107-3756
REMARK 1 PMID 19082507
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0093
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.8
REMARK 3 NUMBER OF REFLECTIONS : 13038
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 709
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1014
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2995
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.73000
REMARK 3 B22 (A**2) : 3.73000
REMARK 3 B33 (A**2) : -5.60000
REMARK 3 B12 (A**2) : 1.87000
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): 1.367
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.408
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.310
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.309
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3149 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4281 ; 1.860 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 376 ; 8.148 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;36.098 ;23.841
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 526 ;21.882 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;23.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 496 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2343 ; 0.008 ; 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): 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: NULL
REMARK 4
REMARK 4 3R4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : ASYMMETRIC CURVED CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13852
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.699
REMARK 200 RESOLUTION RANGE LOW (A) : 33.003
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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 (%): 64.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.025M NACL, 27% TERT-BUTANOL, 0.050M
REMARK 280 TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 64.82700
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 129.65400
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 129.65400
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 64.82700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A 24
REMARK 465 HIS A 25
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 LYS A 51 126.87 -28.25
REMARK 500 ASP A 91 170.30 -58.60
REMARK 500 LYS A 127 109.89 -56.07
REMARK 500 MET A 133 -70.92 -39.83
REMARK 500 ARG A 141 -179.81 51.43
REMARK 500 SER A 142 171.71 54.50
REMARK 500 VAL A 152 -125.17 30.10
REMARK 500 SER A 172 -94.23 -88.18
REMARK 500 ASN A 173 40.18 -85.61
REMARK 500 LYS A 177 -35.20 -32.42
REMARK 500 VAL A 180 120.41 121.21
REMARK 500 GLN A 182 -31.12 -37.69
REMARK 500 SER A 206 32.25 -97.75
REMARK 500 LYS A 214 171.16 -55.08
REMARK 500 ASP A 216 12.57 -67.94
REMARK 500 SER A 218 -176.25 -58.43
REMARK 500 GLN A 326 -39.84 -154.09
REMARK 500 GLU A 336 -84.54 -15.79
REMARK 500 ASN A 352 82.32 -170.27
REMARK 500 GLU A 353 -55.58 80.06
REMARK 500 VAL A 357 70.33 -57.58
REMARK 500 ALA A 358 -8.79 48.18
REMARK 500 VAL A 364 138.67 -37.51
REMARK 500 VAL A 366 50.43 -101.79
REMARK 500 ALA A 368 -125.57 -79.58
REMARK 500 ALA A 371 105.86 -1.55
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 A 336 PRO A 337 -142.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q02 RELATED DB: PDB
REMARK 900 PLASMINOGEN ACTIVATOR INHIBITOR-1 IN A METASTABLE ACTIVE
REMARK 900 CONFORMATION, MUTANT W175F
REMARK 900 RELATED ID: 1DVM RELATED DB: PDB
REMARK 900 PLASMINOGEN ACTIVATOR INHIBITOR-1, ACTIVE, MUTANT N150H, K154T,
REMARK 900 Q319L, M354I
REMARK 900 RELATED ID: 1B3K RELATED DB: PDB
REMARK 900 PLASMINOGEN ACTIVATOR INHIBITOR-1, ACTIVE, MUTANT N150H, K154T,
REMARK 900 Q319L, M354I
DBREF 3R4L A 24 402 UNP P05121 PAI1_HUMAN 24 402
SEQADV 3R4L CYS A 197 UNP P05121 GLN 197 ENGINEERED MUTATION
SEQADV 3R4L CYS A 355 UNP P05121 GLY 355 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 ASN LEU LEU GLY LYS 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 CYS 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 GLN PHE GLN ALA ASP PHE THR SER LEU SER ASP GLN
SEQRES 25 A 379 GLU PRO LEU HIS VAL ALA GLN ALA LEU GLN LYS VAL LYS
SEQRES 26 A 379 ILE GLU VAL ASN GLU SER CYS 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 MET 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
MODRES 3R4L ASN A 232 ASN GLYCOSYLATION SITE
MODRES 3R4L ASN A 288 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET BMA B 4 11
HET FUC B 5 10
HET NAG A 408 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 BMA 2(C6 H12 O6)
FORMUL 2 FUC C6 H12 O5
FORMUL 4 HOH *17(H2 O)
HELIX 1 1 SER A 29 ALA A 49 1 21
HELIX 2 2 SER A 58 GLN A 70 1 13
HELIX 3 3 LEU A 71 THR A 73 5 3
HELIX 4 4 GLY A 74 GLY A 86 1 13
HELIX 5 5 GLY A 93 MET A 106 1 14
HELIX 6 6 GLY A 131 ARG A 141 1 11
HELIX 7 7 GLU A 151 THR A 167 1 17
HELIX 8 8 HIS A 252 ASP A 254 5 3
HELIX 9 9 LEU A 270 ASN A 275 1 6
HELIX 10 10 SER A 278 ASN A 288 1 11
HELIX 11 11 LEU A 309 LEU A 316 1 8
HELIX 12 12 THR A 319 ARG A 323 5 5
SHEET 1 A 7 VAL A 55 PHE A 57 0
SHEET 2 A 7 THR A 392 VAL A 399 -1 O MET A 396 N PHE A 57
SHEET 3 A 7 PHE A 381 HIS A 387 -1 N PHE A 381 O VAL A 399
SHEET 4 A 7 LEU A 256 PRO A 263 -1 N PHE A 259 O VAL A 384
SHEET 5 A 7 TYR A 243 PRO A 250 -1 N LEU A 247 O ILE A 260
SHEET 6 A 7 THR A 219 THR A 237 -1 N THR A 234 O ILE A 246
SHEET 7 A 7 HIS A 208 HIS A 213 -1 N PHE A 212 O VAL A 220
SHEET 1 B 8 VAL A 55 PHE A 57 0
SHEET 2 B 8 THR A 392 VAL A 399 -1 O MET A 396 N PHE A 57
SHEET 3 B 8 PHE A 381 HIS A 387 -1 N PHE A 381 O VAL A 399
SHEET 4 B 8 LEU A 256 PRO A 263 -1 N PHE A 259 O VAL A 384
SHEET 5 B 8 TYR A 243 PRO A 250 -1 N LEU A 247 O ILE A 260
SHEET 6 B 8 THR A 219 THR A 237 -1 N THR A 234 O ILE A 246
SHEET 7 B 8 THR A 290 PRO A 299 -1 O LEU A 298 N MET A 225
SHEET 8 B 8 GLU A 374 ILE A 376 1 O ILE A 375 N LEU A 295
SHEET 1 C 5 LYS A 145 VAL A 147 0
SHEET 2 C 5 ILE A 114 GLN A 123 1 N VAL A 122 O LYS A 145
SHEET 3 C 5 LEU A 186 PHE A 194 -1 O VAL A 187 N PHE A 121
SHEET 4 C 5 GLN A 342 VAL A 351 1 O LEU A 344 N LEU A 188
SHEET 5 C 5 PHE A 301 ASP A 308 -1 N VAL A 307 O GLN A 345
SSBOND 1 CYS A 197 CYS A 355 1555 1555 2.02
LINK ND2 ASN A 232 C1 NAG A 408 1555 1555 1.44
LINK ND2 ASN A 288 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 5 1555 1555 1.45
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.44
LINK O6 BMA B 3 C1 BMA B 4 1555 1555 1.47
CISPEP 1 THR A 362 ALA A 363 0 -22.62
CRYST1 72.007 72.007 194.481 90.00 90.00 120.00 P 31 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 0.013888 0.008018 0.000000 0.00000
SCALE2 0.000000 0.016036 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005142 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
