| content |
HEADER HYDROLASE 16-MAY-08 3D59
TITLE CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING
TITLE 2 FACTOR ACETYLHYDROLASE
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, PAF 2-ACYLHYDROLASE, LDL-
COMPND 6 ASSOCIATED PHOSPHOLIPASE A2, LDL-PLA(2), 2-ACETYL-1-
COMPND 7 ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE, 1-ALKYL-2-
COMPND 8 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE;
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 GENE: PLA2G7, PAFAH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PLASMA PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, SECRETED
KEYWDS 2 PROTEIN, ALPHA/BETA-HYDROLASE-FOLD, LDL-BOUND; LIPOPROTEIN
KEYWDS 3 ASSOCIATED PHOSPHOLIPASE A2, LP-PLA2, GROUP VIIA PLA2,
KEYWDS 4 GLYCOPROTEIN, HYDROLASE, LIPID DEGRADATION, POLYMORPHISM,
KEYWDS 5 SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR U.SAMANTA,B.J.BAHNSON
REVDAT 1 09-SEP-08 3D59 0
JRNL AUTH U.SAMANTA,B.J.BAHNSON
JRNL TITL CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET
JRNL TITL 2 ACTIVATING FACTOR ACETYLHYDROLASE: STRUCTURAL
JRNL TITL 3 IMPLICATION TO LIPOPROTEIN BINDING AND CATALYSIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.142
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.131
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 6384
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.131
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 5314
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 100893
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6055
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 511
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 6556.52
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 38
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 57242
REMARK 3 NUMBER OF RESTRAINTS : 72220
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.053
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.068
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.031
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.061
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3D59 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB047608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-2006; 12-AUG-2006
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; APS
REMARK 200 BEAMLINE : X29A; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100; 1.006, 1.009
REMARK 200 MONOCHROMATOR : SI(111); SI(111)
REMARK 200 OPTICS : ROSENBAUM-ROCK; ROSENBAUM-ROCK
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC
REMARK 200 QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127359
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.920
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL2MAP, SOLVE, RESOLVE, CCP4I, ARP/WARP, SHELXL
REMARK 200 -97
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293.0K, PH 6.60
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 -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 58.09200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.53050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.09200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.53050
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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 596 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 652 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 670 LIES ON A SPECIAL POSITION.
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
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 ASN A 426
REMARK 465 GLN A 427
REMARK 465 HIS A 428
REMARK 465 ILE A 429
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 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 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 LYS B 55 CG CD CE NZ
REMARK 470 GLN B 88 CG CD OE1 NE2
REMARK 470 ASP B 89 CG OD1 OD2
REMARK 470 ASN B 90 CG OD1 ND2
REMARK 470 ASP B 91 CG OD1 OD2
REMARK 470 ARG B 92 CG CD NE CZ NH1 NH2
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 GLN B 427 CG CD OE1 NE2
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 -175.77 -68.57
REMARK 500 LYS A 266 75.85 -117.61
REMARK 500 SER A 273 -117.17 64.88
REMARK 500 HIS A 399 57.46 -102.67
REMARK 500 LYS A 400 -167.29 -118.77
REMARK 500 ASP B 73 -169.63 -69.25
REMARK 500 TRP B 115 -36.24 -38.25
REMARK 500 LYS B 266 77.51 -118.13
REMARK 500 SER B 273 -115.78 66.79
REMARK 500 HIS B 399 65.50 -109.68
REMARK 500 ASN B 426 41.17 -106.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 2
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 11
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 12
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 13
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 14
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 15
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 16
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 17
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 18
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 19
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 20
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 21
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 22
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 23
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 24
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 25
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 26
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 27
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 28
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 29
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 32
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 33
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 35
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 36
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 37
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE B 38
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 39
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D5E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING
REMARK 900 FACTOR ACETYLHYDROLASE COVALENTLY INHIBITED BY PARAOXON
DBREF 3D59 A 47 429 UNP Q13093 PAFA_HUMAN 47 429
DBREF 3D59 B 47 429 UNP Q13093 PAFA_HUMAN 47 429
SEQRES 1 A 383 ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY
SEQRES 2 A 383 ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE
SEQRES 3 A 383 ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR
SEQRES 4 A 383 PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE
SEQRES 5 A 383 PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU
SEQRES 6 A 383 GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU
SEQRES 7 A 383 PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO
SEQRES 8 A 383 LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER
SEQRES 9 A 383 HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE
SEQRES 10 A 383 GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA
SEQRES 11 A 383 VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR
SEQRES 12 A 383 PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER
SEQRES 13 A 383 TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR
SEQRES 14 A 383 HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU
SEQRES 15 A 383 CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS
SEQRES 16 A 383 GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP
SEQRES 17 A 383 MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE
SEQRES 18 A 383 ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE
SEQRES 19 A 383 GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE
SEQRES 20 A 383 ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL
SEQRES 21 A 383 TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER
SEQRES 22 A 383 GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS
SEQRES 23 A 383 LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR
SEQRES 24 A 383 ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR
SEQRES 25 A 383 PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU
SEQRES 26 A 383 LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER
SEQRES 27 A 383 ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY
SEQRES 28 A 383 LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU
SEQRES 29 A 383 GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN
SEQRES 30 A 383 THR THR ASN GLN HIS ILE
SEQRES 1 B 383 ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY
SEQRES 2 B 383 ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE
SEQRES 3 B 383 ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR
SEQRES 4 B 383 PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE
SEQRES 5 B 383 PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU
SEQRES 6 B 383 GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU
SEQRES 7 B 383 PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO
SEQRES 8 B 383 LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER
SEQRES 9 B 383 HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE
SEQRES 10 B 383 GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA
SEQRES 11 B 383 VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR
SEQRES 12 B 383 PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER
SEQRES 13 B 383 TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR
SEQRES 14 B 383 HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU
SEQRES 15 B 383 CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS
SEQRES 16 B 383 GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP
SEQRES 17 B 383 MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE
SEQRES 18 B 383 ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE
SEQRES 19 B 383 GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE
SEQRES 20 B 383 ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL
SEQRES 21 B 383 TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER
SEQRES 22 B 383 GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS
SEQRES 23 B 383 LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR
SEQRES 24 B 383 ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR
SEQRES 25 B 383 PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU
SEQRES 26 B 383 LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER
SEQRES 27 B 383 ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY
SEQRES 28 B 383 LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU
SEQRES 29 B 383 GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN
SEQRES 30 B 383 THR THR ASN GLN HIS ILE
HET ACT A 11 4
HET ACT A 12 4
HET ACT A 15 4
HET ACT A 16 4
HET ACT A 19 4
HET ACT A 20 4
HET ACT A 22 4
HET ACT A 24 4
HET ACT A 25 4
HET ACT A 28 4
HET ACT A 29 4
HET ACT A 30 4
HET ACT A 32 4
HET ACT A 33 4
HET ACT A 35 4
HET ACT A 36 4
HET ACT A 39 4
HET SO4 B 1 5
HET SO4 B 2 5
HET ACT B 13 4
HET ACT B 14 4
HET ACT B 17 4
HET ACT B 18 4
HET ACT B 21 4
HET ACT B 23 4
HET ACT B 26 4
HET ACT B 27 4
HET ACT B 31 4
HET ACT B 34 4
HET ACT B 37 4
HET ACT B 38 4
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
FORMUL 3 ACT 29(C2 H3 O2 1-)
FORMUL 20 SO4 2(O4 S 2-)
FORMUL 34 HOH *511(H2 O)
HELIX 1 1 ASN A 100 GLY A 112 1 13
HELIX 2 2 HIS A 114 GLY A 126 1 13
HELIX 3 3 TYR A 160 HIS A 170 1 11
HELIX 4 4 ASP A 192 GLY A 199 1 8
HELIX 5 5 LYS A 210 GLU A 212 5 3
HELIX 6 6 GLU A 213 HIS A 241 1 29
HELIX 7 7 ASP A 254 LYS A 259 5 6
HELIX 8 8 SER A 273 ASP A 286 1 14
HELIX 9 9 GLY A 303 ARG A 309 5 7
HELIX 10 10 TYR A 324 LYS A 333 1 10
HELIX 11 11 VAL A 350 ALA A 360 5 11
HELIX 12 12 GLY A 362 LEU A 369 1 8
HELIX 13 13 ASP A 376 GLY A 397 1 22
HELIX 14 14 ASP A 401 GLN A 404 5 4
HELIX 15 15 TRP A 405 GLU A 410 1 6
HELIX 16 16 ASN B 100 GLY B 112 1 13
HELIX 17 17 TRP B 115 GLY B 126 1 12
HELIX 18 18 TYR B 160 HIS B 170 1 11
HELIX 19 19 ASP B 192 ILE B 198 1 7
HELIX 20 20 LYS B 210 GLU B 212 5 3
HELIX 21 21 GLU B 213 HIS B 241 1 29
HELIX 22 22 ASP B 254 LYS B 259 5 6
HELIX 23 23 SER B 273 ASP B 286 1 14
HELIX 24 24 GLU B 305 ARG B 309 5 5
HELIX 25 25 TYR B 324 CYS B 334 1 11
HELIX 26 26 VAL B 350 ALA B 360 5 11
HELIX 27 27 GLY B 362 LEU B 369 1 8
HELIX 28 28 ASP B 376 GLY B 397 1 22
HELIX 29 29 ASP B 401 GLN B 404 5 4
HELIX 30 30 TRP B 405 GLU B 410 1 6
SHEET 1 A10 ASN A 133 TRP A 134 0
SHEET 2 A10 SER A 64 PHE A 72 1 N VAL A 65 O ASN A 133
SHEET 3 A10 THR A 79 SER A 87 -1 O LEU A 83 N THR A 68
SHEET 4 A10 ILE A 173 VAL A 177 -1 O ALA A 176 N ARG A 82
SHEET 5 A10 TYR A 144 SER A 150 1 N VAL A 147 O ALA A 175
SHEET 6 A10 ILE A 262 HIS A 272 1 O ASP A 263 N TYR A 144
SHEET 7 A10 CYS A 291 LEU A 295 1 O LEU A 295 N GLY A 271
SHEET 8 A10 LEU A 314 SER A 319 1 O PHE A 315 N ALA A 294
SHEET 9 A10 ARG A 341 ILE A 346 1 O LYS A 342 N PHE A 316
SHEET 10 A10 LEU A 416 PRO A 418 -1 O ILE A 417 N THR A 345
SHEET 1 B 2 THR A 95 LEU A 96 0
SHEET 2 B 2 THR A 129 THR A 130 -1 O THR A 130 N THR A 95
SHEET 1 C 2 ALA A 186 TYR A 189 0
SHEET 2 C 2 SER A 202 TYR A 205 -1 O LEU A 204 N THR A 187
SHEET 1 D10 ASN B 133 TRP B 134 0
SHEET 2 D10 VAL B 65 PHE B 72 1 N VAL B 65 O ASN B 133
SHEET 3 D10 THR B 79 PRO B 86 -1 O LEU B 83 N THR B 68
SHEET 4 D10 ILE B 173 VAL B 177 -1 O ALA B 176 N ARG B 82
SHEET 5 D10 TYR B 144 SER B 150 1 N VAL B 147 O ALA B 175
SHEET 6 D10 ILE B 262 HIS B 272 1 O ASP B 263 N TYR B 144
SHEET 7 D10 CYS B 291 LEU B 295 1 O LEU B 295 N GLY B 271
SHEET 8 D10 LEU B 314 SER B 319 1 O PHE B 315 N ALA B 294
SHEET 9 D10 ARG B 341 ILE B 346 1 O ILE B 344 N ASN B 318
SHEET 10 D10 LEU B 416 PRO B 418 -1 O ILE B 417 N THR B 345
SHEET 1 E 2 THR B 95 LEU B 96 0
SHEET 2 E 2 THR B 129 THR B 130 -1 O THR B 130 N THR B 95
SHEET 1 F 2 ALA B 186 TYR B 189 0
SHEET 2 F 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 -10.74
CISPEP 2 PHE B 72 ASP B 73 0 -12.19
SITE 1 AC1 8 LYS A 143 HIS A 241 ARG A 264 HOH A 476
SITE 2 AC1 8 SER B 308 ARG B 309 PRO B 311 LYS B 339
SITE 1 AC2 4 SER A 230 GLN A 231 SER A 234 HOH A 494
SITE 1 AC3 4 LYS A 143 ILE A 262 ASP A 263 ARG A 264
SITE 1 AC4 4 SER A 202 TRP A 203 TYR B 189 LYS B 191
SITE 1 AC5 5 HIS A 74 ASP A 192 GLN A 193 HOH A 662
SITE 2 AC5 5 HOH A 713
SITE 1 AC6 6 LYS A 246 ASN A 247 PHE A 253 MET A 255
SITE 2 AC6 6 HOH A 490 HOH A 495
SITE 1 AC7 2 PHE A 72 HOH A 481
SITE 1 AC8 2 LEU A 124 THR A 361
SITE 1 AC9 3 TRP A 298 TYR A 324 HOH A 446
SITE 1 BC1 5 LYS A 191 HOH A 534 TYR B 189 LYS B 191
SITE 2 BC1 5 HOH B 548
SITE 1 BC2 4 GLU A 305 SER A 308 ARG A 309 ASP B 260
SITE 1 BC3 2 LYS A 394 HIS A 395
SITE 1 BC4 6 PRO A 57 ARG A 58 ASN A 378 HOH A 548
SITE 2 BC4 6 HOH A 566 HOH A 711
SITE 1 BC5 3 ASN A 378 ASP A 382 HOH A 510
SITE 1 BC6 3 ARG A 182 HOH A 555 HOH A 700
SITE 1 BC7 7 ASP A 338 GLU A 410 ASP A 412 PRO A 418
SITE 2 BC7 7 HOH A 542 HOH A 635 HOH A 710
SITE 1 BC8 8 LYS A 101 LYS A 201 ARG B 182 ARG B 207
SITE 2 BC8 8 HOH B 471 HOH B 482 HOH B 490 HOH B 496
SITE 1 BC9 6 ASP A 89 ASN A 90 ASN B 100 LYS B 101
SITE 2 BC9 6 HOH B 521 HOH B 634
SITE 1 CC1 3 TRP B 134 LEU B 251 HOH B 518
SITE 1 CC2 4 TYR B 321 PHE B 322 HIS B 351 HOH B 449
SITE 1 CC3 3 SER B 230 GLN B 231 SER B 234
SITE 1 CC4 3 LYS B 266 LEU B 398 HIS B 399
SITE 1 CC5 4 TRP B 298 PHE B 300 TYR B 324 HOH B 441
SITE 1 CC6 2 LEU B 107 PHE B 357
SITE 1 CC7 3 LYS A 259 HOH A 679 ARG B 309
SITE 1 CC8 3 HIS B 74 ASP B 192 GLN B 193
SITE 1 CC9 4 LYS A 370 HOH A 620 ILE B 329 HOH B 639
SITE 1 DC1 3 PRO B 140 ASP B 412 HOH B 594
CRYST1 116.184 83.061 96.705 90.00 115.09 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 0.008607 0.000000 0.004030 0.00000
SCALE2 0.000000 0.012039 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011418 0.00000
END |