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HEADER HYDROLASE/HYDROLASE INHIBITOR 20-FEB-16 5I9I
TITLE CRYSTAL STRUCTURE OF LP_PLA2 IN COMPLEX WITH DARAPLADIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 47-429;
COMPND 5 SYNONYM: PAF ACETYLHYDROLASE,1-ALKYL-2-ACETYLGLYCEROPHOSPHOCHOLINE
COMPND 6 ESTERASE,2-ACETYL-1-ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA
COMPND 7 PHOSPHOLIPASE A2,GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-
COMPND 8 PLA(2),PAF 2-ACYLHYDROLASE;
COMPND 9 EC: 3.1.1.47;
COMPND 10 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: PLA2G7, PAFAH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS LP_PLA2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.F.LIU,Y.C.XU
REVDAT 1 15-JUN-16 5I9I 0
JRNL AUTH Q.F.LIU,X.D.CHEN,W.Y.CHEN,X.J.YUAN,H.X.SU,J.H.SHEN,Y.C.XU
JRNL TITL STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF
JRNL TITL 2 PROTEIN-LIGAND INTERACTIONS FORMED BETWEEN
JRNL TITL 3 LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 AND INHIBITORS
JRNL REF J.MED.CHEM. V. 59 5115 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27078579
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00282
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.930
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 22260
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.970
REMARK 3 FREE R VALUE TEST SET COUNT : 668
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.0703 - 5.6126 0.95 4559 140 0.1925 0.2514
REMARK 3 2 5.6126 - 4.4563 0.94 4438 138 0.1668 0.2395
REMARK 3 3 4.4563 - 3.8934 0.94 4483 140 0.1615 0.1852
REMARK 3 4 3.8934 - 3.5376 0.95 4523 135 0.1682 0.2490
REMARK 3 5 3.5376 - 3.2841 0.96 4564 140 0.1880 0.2851
REMARK 3 6 3.2841 - 3.0905 0.97 4597 144 0.2128 0.2880
REMARK 3 7 3.0905 - 2.9358 0.97 4668 144 0.2268 0.3068
REMARK 3 8 2.9358 - 2.8080 0.97 4654 141 0.2371 0.3835
REMARK 3 9 2.8080 - 2.6999 0.97 4630 138 0.2540 0.3216
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 5789
REMARK 3 ANGLE : 1.208 7884
REMARK 3 CHIRALITY : 0.046 848
REMARK 3 PLANARITY : 0.006 1021
REMARK 3 DIHEDRAL : 15.192 1980
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5I9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
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) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22260
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 44.064
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 1.960
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5900
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) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3D59
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.6, 0.4M LI2SO4, 27%
REMARK 280 (W/V) (NH4)2SO4, 1M NA-AC, 1.4% 1,4-BUTANEDIOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 57.95000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.95000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.20500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 TOTAL BURIED SURFACE AREA: 110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 42
REMARK 465 PRO A 43
REMARK 465 LEU A 44
REMARK 465 GLY A 45
REMARK 465 SER A 46
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 ALA A 49
REMARK 465 SER A 50
REMARK 465 PHE A 51
REMARK 465 GLY A 52
REMARK 465 GLN A 53
REMARK 465 THR A 425
REMARK 465 ASN A 426
REMARK 465 GLN A 427
REMARK 465 HIS A 428
REMARK 465 ILE A 429
REMARK 465 GLY B 42
REMARK 465 PRO B 43
REMARK 465 LEU B 44
REMARK 465 GLY B 45
REMARK 465 SER B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 ALA B 49
REMARK 465 SER B 50
REMARK 465 PHE B 51
REMARK 465 GLY B 52
REMARK 465 GLN B 53
REMARK 465 THR B 54
REMARK 465 ASP B 89
REMARK 465 ASN B 90
REMARK 465 ASP B 91
REMARK 465 ARG B 92
REMARK 465 LEU B 93
REMARK 465 ASP B 338
REMARK 465 THR B 424
REMARK 465 THR B 425
REMARK 465 ASN B 426
REMARK 465 GLN B 427
REMARK 465 HIS B 428
REMARK 465 ILE B 429
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 THR A 54 OG1 CG2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 SER A 64 OG
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 ASP A 89 CG OD1 OD2
REMARK 470 ASP A 91 CG OD1 OD2
REMARK 470 ARG A 92 NE CZ NH1 NH2
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 THR A 113 OG1 CG2
REMARK 470 HIS A 114 CG ND1 CD2 CE1 NE2
REMARK 470 TRP A 115 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 115 CZ3 CH2
REMARK 470 LEU A 116 CG CD1 CD2
REMARK 470 MET A 117 CG SD CE
REMARK 470 ASN A 119 OD1 ND2
REMARK 470 ILE A 120 CG1 CG2 CD1
REMARK 470 LEU A 123 CG CD1 CD2
REMARK 470 LEU A 124 CG CD1 CD2
REMARK 470 SER A 127 OG
REMARK 470 THR A 129 OG1 CG2
REMARK 470 LYS A 143 CE NZ
REMARK 470 VAL A 174 CG1 CG2
REMARK 470 SER A 194 OG
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 GLN A 211 CG CD OE1 NE2
REMARK 470 GLU A 212 OE1 OE2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 LYS A 227 CG CD CE NZ
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 ASP A 250 CG OD1 OD2
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 LYS A 259 CD CE NZ
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 ASP A 304 CG OD1 OD2
REMARK 470 LYS A 330 NZ
REMARK 470 LYS A 333 CE NZ
REMARK 470 ARG A 347 CG CD NE CZ NH1 NH2
REMARK 470 THR A 361 OG1 CG2
REMARK 470 LYS A 363 CG CD CE NZ
REMARK 470 ILE A 364 CG1 CG2 CD1
REMARK 470 ILE A 365 CG1 CG2 CD1
REMARK 470 MET A 368 CG SD CE
REMARK 470 LYS A 370 CG CD CE NZ
REMARK 470 LYS A 394 CG CD CE NZ
REMARK 470 LYS A 400 CE NZ
REMARK 470 GLU A 414 CG CD OE1 OE2
REMARK 470 ILE A 417 CD1
REMARK 470 ASN A 423 CG OD1 ND2
REMARK 470 THR A 424 OG1 CG2
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2
REMARK 470 SER B 64 OG
REMARK 470 SER B 87 OG
REMARK 470 GLN B 88 CG CD OE1 NE2
REMARK 470 LYS B 109 CG CD CE NZ
REMARK 470 HIS B 114 CG ND1 CD2 CE1 NE2
REMARK 470 TRP B 115 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 115 CZ3 CH2
REMARK 470 LEU B 116 CG CD1 CD2
REMARK 470 LEU B 123 CG CD1 CD2
REMARK 470 LEU B 124 CD1 CD2
REMARK 470 SER B 127 OG
REMARK 470 ASN B 133 CG OD1 ND2
REMARK 470 SER B 136 OG
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ASP B 192 OD1 OD2
REMARK 470 GLN B 193 CG CD OE1 NE2
REMARK 470 SER B 194 OG
REMARK 470 ILE B 198 CG1 CG2 CD1
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 GLN B 211 CG CD OE1 NE2
REMARK 470 GLU B 212 CG CD OE1 OE2
REMARK 470 GLU B 214 CG CD OE1 OE2
REMARK 470 THR B 215 OG1 CG2
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 ASP B 250 CG OD1 OD2
REMARK 470 LYS B 252 CG CD CE NZ
REMARK 470 GLU B 256 CG CD OE1 OE2
REMARK 470 ASP B 304 CG OD1 OD2
REMARK 470 GLU B 305 CG CD OE1 OE2
REMARK 470 SER B 308 OG
REMARK 470 ARG B 309 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 329 CG1 CG2 CD1
REMARK 470 LYS B 330 CD CE NZ
REMARK 470 LYS B 332 CG CD CE NZ
REMARK 470 LYS B 333 CE NZ
REMARK 470 SER B 336 OG
REMARK 470 LYS B 339 CG CD CE NZ
REMARK 470 LYS B 342 CG CD CE NZ
REMARK 470 ARG B 347 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 363 CG CD CE NZ
REMARK 470 ILE B 364 CG1 CG2 CD1
REMARK 470 ILE B 365 CD1
REMARK 470 MET B 368 CG SD CE
REMARK 470 LYS B 370 CG CD CE NZ
REMARK 470 ILE B 375 CG1 CG2 CD1
REMARK 470 ASN B 378 CG OD1 ND2
REMARK 470 VAL B 379 CG1 CG2
REMARK 470 LYS B 386 CE NZ
REMARK 470 LYS B 394 CD CE NZ
REMARK 470 LYS B 400 CG CD CE NZ
REMARK 470 ASP B 401 CG OD1 OD2
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 LEU B 416 CG CD1 CD2
REMARK 470 ILE B 417 CD1
REMARK 470 ASN B 421 CG OD1 ND2
REMARK 470 ILE B 422 CG1 CG2 CD1
REMARK 470 ASN B 423 CG OD1 ND2
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 ASP A 73 -167.81 -71.16
REMARK 500 THR A 113 170.49 -49.26
REMARK 500 HIS A 114 -106.87 -100.36
REMARK 500 PRO A 131 68.82 -68.64
REMARK 500 ALA A 155 -169.64 -111.03
REMARK 500 MET A 255 -17.76 -47.64
REMARK 500 SER A 273 -110.58 62.88
REMARK 500 ASP A 296 64.99 36.18
REMARK 500 ILE A 364 -70.45 -66.82
REMARK 500 HIS A 399 67.66 -105.91
REMARK 500 TRP B 115 0.29 -68.40
REMARK 500 PRO B 131 75.88 -65.88
REMARK 500 LYS B 266 77.15 -114.52
REMARK 500 SER B 273 -108.55 55.61
REMARK 500 ARG B 309 37.58 -141.53
REMARK 500 LYS B 370 32.08 70.71
REMARK 500 HIS B 399 77.70 -108.22
REMARK 500 ASP B 413 140.05 -18.43
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 5HV A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HV B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I8P RELATED DB: PDB
DBREF 5I9I A 47 429 UNP Q13093 PAFA_HUMAN 47 429
DBREF 5I9I B 47 429 UNP Q13093 PAFA_HUMAN 47 429
SEQADV 5I9I GLY A 42 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I PRO A 43 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I LEU A 44 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I GLY A 45 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I SER A 46 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I GLY B 42 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I PRO B 43 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I LEU B 44 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I GLY B 45 UNP Q13093 EXPRESSION TAG
SEQADV 5I9I SER B 46 UNP Q13093 EXPRESSION TAG
SEQRES 1 A 388 GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR
SEQRES 2 A 388 LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS
SEQRES 3 A 388 THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE
SEQRES 4 A 388 LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU
SEQRES 5 A 388 ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY
SEQRES 6 A 388 LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN
SEQRES 7 A 388 ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA
SEQRES 8 A 388 ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO
SEQRES 9 A 388 LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR
SEQRES 10 A 388 LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY
SEQRES 11 A 388 PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA
SEQRES 12 A 388 SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU
SEQRES 13 A 388 ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS
SEQRES 14 A 388 GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG
SEQRES 15 A 388 GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE
SEQRES 16 A 388 LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU
SEQRES 17 A 388 ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE
SEQRES 18 A 388 ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY
SEQRES 19 A 388 GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG
SEQRES 20 A 388 PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO
SEQRES 21 A 388 LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU
SEQRES 22 A 388 PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN
SEQRES 23 A 388 ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU
SEQRES 24 A 388 ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN
SEQRES 25 A 388 PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY
SEQRES 26 A 388 HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL
SEQRES 27 A 388 ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU
SEQRES 28 A 388 GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP
SEQRES 29 A 388 ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO
SEQRES 30 A 388 GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE
SEQRES 1 B 388 GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR
SEQRES 2 B 388 LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS
SEQRES 3 B 388 THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE
SEQRES 4 B 388 LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU
SEQRES 5 B 388 ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY
SEQRES 6 B 388 LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN
SEQRES 7 B 388 ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA
SEQRES 8 B 388 ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO
SEQRES 9 B 388 LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR
SEQRES 10 B 388 LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY
SEQRES 11 B 388 PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA
SEQRES 12 B 388 SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU
SEQRES 13 B 388 ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS
SEQRES 14 B 388 GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG
SEQRES 15 B 388 GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE
SEQRES 16 B 388 LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU
SEQRES 17 B 388 ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE
SEQRES 18 B 388 ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY
SEQRES 19 B 388 GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG
SEQRES 20 B 388 PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO
SEQRES 21 B 388 LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU
SEQRES 22 B 388 PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN
SEQRES 23 B 388 ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU
SEQRES 24 B 388 ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN
SEQRES 25 B 388 PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY
SEQRES 26 B 388 HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL
SEQRES 27 B 388 ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU
SEQRES 28 B 388 GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP
SEQRES 29 B 388 ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO
SEQRES 30 B 388 GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE
HET 5HV A 501 47
HET 5HV B 501 47
HET SO4 B 502 5
HET SO4 B 503 5
HETNAM 5HV N-[2-(DIETHYLAMINO)ETHYL]-2-{2-[(4-FLUOROBENZYL)
HETNAM 2 5HV SULFANYL]-4-OXO-4,5,6,7-TETRAHYDRO-1H-
HETNAM 3 5HV CYCLOPENTA[D]PYRIMIDIN-1-YL}-N-{[4'-(TRIFLUOROMETHYL)
HETNAM 4 5HV BIPHENYL-4-YL]METHYL}ACETAMIDE
HETNAM SO4 SULFATE ION
HETSYN 5HV DARAPLADIB
FORMUL 3 5HV 2(C36 H38 F4 N4 O2 S)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *6(H2 O)
HELIX 1 AA1 ASN A 100 GLY A 112 1 13
HELIX 2 AA2 TRP A 115 GLY A 126 1 12
HELIX 3 AA3 TYR A 160 SER A 169 1 10
HELIX 4 AA4 ASP A 192 GLY A 199 1 8
HELIX 5 AA5 LYS A 210 GLU A 212 5 3
HELIX 6 AA6 GLU A 213 HIS A 241 1 29
HELIX 7 AA7 ASP A 254 LYS A 259 5 6
HELIX 8 AA8 SER A 273 ASP A 286 1 14
HELIX 9 AA9 VAL A 306 ILE A 310 5 5
HELIX 10 AB1 TYR A 324 LYS A 333 1 10
HELIX 11 AB2 VAL A 350 ALA A 360 5 11
HELIX 12 AB3 GLY A 362 LEU A 369 1 8
HELIX 13 AB4 ASP A 376 GLY A 397 1 22
HELIX 14 AB5 ASP A 401 GLN A 404 5 4
HELIX 15 AB6 TRP A 405 GLU A 410 1 6
HELIX 16 AB7 ASN B 100 GLY B 112 1 13
HELIX 17 AB8 HIS B 114 GLY B 126 1 13
HELIX 18 AB9 PHE B 156 LEU B 159 5 4
HELIX 19 AC1 TYR B 160 SER B 169 1 10
HELIX 20 AC2 ASP B 192 ILE B 198 1 7
HELIX 21 AC3 LYS B 210 GLU B 212 5 3
HELIX 22 AC4 GLU B 213 HIS B 241 1 29
HELIX 23 AC5 ASP B 254 LYS B 259 5 6
HELIX 24 AC6 SER B 273 ASP B 286 1 14
HELIX 25 AC7 TYR B 324 LYS B 333 1 10
HELIX 26 AC8 VAL B 350 PHE B 354 5 5
HELIX 27 AC9 ALA B 355 PHE B 359 5 5
HELIX 28 AD1 GLY B 362 LEU B 369 1 8
HELIX 29 AD2 ASP B 376 GLY B 397 1 22
HELIX 30 AD3 LYS B 400 GLN B 404 5 5
HELIX 31 AD4 TRP B 405 GLY B 411 1 7
SHEET 1 AA110 ASN A 133 TRP A 134 0
SHEET 2 AA110 SER A 64 PHE A 72 1 N VAL A 65 O ASN A 133
SHEET 3 AA110 THR A 79 SER A 87 -1 O TYR A 85 N GLY A 66
SHEET 4 AA110 ILE A 173 VAL A 177 -1 O ALA A 176 N ARG A 82
SHEET 5 AA110 TYR A 144 SER A 150 1 N VAL A 147 O ALA A 175
SHEET 6 AA110 ILE A 262 HIS A 272 1 O ALA A 268 N VAL A 148
SHEET 7 AA110 CYS A 291 LEU A 295 1 O LEU A 295 N GLY A 271
SHEET 8 AA110 LEU A 314 SER A 319 1 O PHE A 315 N ALA A 294
SHEET 9 AA110 ARG A 341 ILE A 346 1 O LYS A 342 N PHE A 316
SHEET 10 AA110 LEU A 416 PRO A 418 -1 O ILE A 417 N THR A 345
SHEET 1 AA2 2 THR A 95 LEU A 96 0
SHEET 2 AA2 2 THR A 129 THR A 130 -1 O THR A 130 N THR A 95
SHEET 1 AA3 2 ALA A 186 TYR A 189 0
SHEET 2 AA3 2 SER A 202 TYR A 205 -1 O LEU A 204 N THR A 187
SHEET 1 AA410 ASN B 133 TRP B 134 0
SHEET 2 AA410 SER B 64 PHE B 72 1 N VAL B 65 O ASN B 133
SHEET 3 AA410 THR B 79 SER B 87 -1 O SER B 87 N SER B 64
SHEET 4 AA410 ILE B 173 VAL B 177 -1 O ALA B 176 N ARG B 82
SHEET 5 AA410 TYR B 144 SER B 150 1 N VAL B 147 O ALA B 175
SHEET 6 AA410 ILE B 262 HIS B 272 1 O LYS B 266 N LEU B 146
SHEET 7 AA410 CYS B 291 LEU B 295 1 O LEU B 295 N GLY B 271
SHEET 8 AA410 LEU B 314 SER B 319 1 O PHE B 315 N ALA B 294
SHEET 9 AA410 ARG B 341 ILE B 346 1 O LYS B 342 N PHE B 316
SHEET 10 AA410 LEU B 416 PRO B 418 -1 O ILE B 417 N THR B 345
SHEET 1 AA5 2 THR B 95 LEU B 96 0
SHEET 2 AA5 2 THR B 129 THR B 130 -1 O THR B 130 N THR B 95
SHEET 1 AA6 2 ALA B 186 TYR B 189 0
SHEET 2 AA6 2 SER B 202 TYR B 205 -1 O LEU B 204 N THR B 187
CISPEP 1 PHE A 72 ASP A 73 0 -6.36
CISPEP 2 PHE B 72 ASP B 73 0 -7.57
SITE 1 AC1 17 LEU A 107 PHE A 110 LEU A 111 LEU A 121
SITE 2 AC1 17 GLY A 152 LEU A 153 GLY A 154 LEU A 159
SITE 3 AC1 17 TYR A 160 SER A 273 PHE A 274 TRP A 298
SITE 4 AC1 17 HIS A 351 GLN A 352 PHE A 357 LEU A 369
SITE 5 AC1 17 LEU A 371
SITE 1 AC2 16 LEU B 107 PHE B 110 LEU B 111 LEU B 121
SITE 2 AC2 16 GLY B 152 LEU B 153 GLY B 154 ALA B 155
SITE 3 AC2 16 LEU B 159 SER B 273 PHE B 274 TRP B 298
SITE 4 AC2 16 HIS B 351 GLN B 352 PHE B 357 LEU B 369
SITE 1 AC3 6 GLN A 88 ASP A 89 ASN A 90 ASN B 100
SITE 2 AC3 6 LYS B 101 ARG B 122
SITE 1 AC4 1 ARG B 207
CRYST1 115.900 82.410 96.470 90.00 115.50 90.00 C 1 2 1 8
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 0.008628 0.000000 0.004115 0.00000
SCALE2 0.000000 0.012134 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011484 0.00000
TER 2814 THR A 424
TER 5541 ASN B 423
MASTER 435 0 4 31 28 0 12 6 5649 2 104 60
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