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HEADER HYDROLASE 12-APR-16 5JAD
TITLE COMPOUND BINDING TO HUMAN LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 (LP-
TITLE 2 PLA2)DISCOVERED THROUGH FRAGMENT SCREENING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PAF ACETYLHYDROLASE,1-ALKYL-2-ACETYLGLYCEROPHOSPHOCHOLINE
COMPND 5 ESTERASE,2-ACETYL-1-ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA
COMPND 6 PHOSPHOLIPASE A2,GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-
COMPND 7 PLA(2),PAF 2-ACYLHYDROLASE;
COMPND 8 EC: 3.1.1.47;
COMPND 9 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET30A
KEYWDS PHOSPHOLIPASE, LIPID METABOLISM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.DAY,A.J-A.WOOLFORD
REVDAT 1 25-MAY-16 5JAD 0
JRNL AUTH A.J.WOOLFORD,J.E.PERO,S.ARAVAPALLI,V.BERDINI,J.E.COYLE,
JRNL AUTH 2 P.J.DAY,A.M.DODSON,P.GRONDIN,F.P.HOLDING,L.Y.LEE,P.LI,
JRNL AUTH 3 E.S.MANAS,J.P.MARINO,A.C.MARTIN,B.W.MCCLELAND,R.L.MCMENAMIN,
JRNL AUTH 4 C.W.MURRAY,C.E.NEIPP,L.W.PAGE,V.K.PATEL,F.POTVAIN,S.J.RICH,
JRNL AUTH 5 R.A.RIVERO,K.SMITH,D.O.SOMERS,L.TROTTET,R.VELAGALETI,
JRNL AUTH 6 G.WILLIAMS,R.XIE
JRNL TITL EXPLOITATION OF A NOVEL BINDING POCKET IN HUMAN
JRNL TITL 2 LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 (LP-PLA2) DISCOVERED
JRNL TITL 3 THROUGH X-RAY FRAGMENT SCREENING.
JRNL REF J.MED.CHEM. 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27167608
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00212
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 25600
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1303
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.06
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2395
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.04
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 127
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2973
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.30060
REMARK 3 B22 (A**2) : 4.78390
REMARK 3 B33 (A**2) : 0.51670
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.74190
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.330
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.244
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.212
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.248
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.215
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3070 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4155 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1067 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 76 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 457 ; 16.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3070 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 392 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3692 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 7.18
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.45
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|55 - A|425 }
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0021 14.7021 0.8666
REMARK 3 T TENSOR
REMARK 3 T11: -0.2971 T22: 0.0072
REMARK 3 T33: -0.0808 T12: 0.0156
REMARK 3 T13: -0.0338 T23: -0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 3.4132 L22: 1.2369
REMARK 3 L33: 1.2011 L12: 0.3331
REMARK 3 L13: 0.6517 L23: -0.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.0193 S13: 0.1685
REMARK 3 S21: 0.0258 S22: -0.0308 S23: 0.0964
REMARK 3 S31: 0.0065 S32: 0.0518 S33: 0.0444
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BUSTER REFINEMENT WAS INTERSPERSED WITH
REMARK 3 ROUNDS OF REBUILDING WITH COOT
REMARK 4
REMARK 4 5JAD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218015.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-X
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5417
REMARK 200 MONOCHROMATOR : VARIMAX VHF ARC)SEC OPTIC
REMARK 200 OPTICS : VARIMAX VHF ARC)SEC OPTIC
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103331
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 64.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NACL, 0.1M HEPES/NAOHPH=7.4,
REMARK 280 28.8%W/V PEG 3350, PH 7.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 297K
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 49.48500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.51450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.48500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.51450
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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 MG MG A 501 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 718 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 725 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET 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 54
REMARK 465 ASN A 426
REMARK 465 GLN A 427
REMARK 465 HIS A 428
REMARK 465 HIS A 429
REMARK 465 HIS A 430
REMARK 465 HIS A 431
REMARK 465 HIS A 432
REMARK 465 HIS A 433
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 241 CG ND1 CD2 CE1 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 -166.54 -76.49
REMARK 500 LYS A 243 132.54 -38.22
REMARK 500 LYS A 266 77.50 -113.48
REMARK 500 SER A 273 -116.71 72.63
REMARK 500 ASP A 296 59.88 38.99
REMARK 500 LYS A 400 -165.16 -120.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 743 DISTANCE = 5.95 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 285 O
REMARK 620 2 HOH A 613 O 103.2
REMARK 620 3 GLU A 285 O 0.0 103.2
REMARK 620 4 HOH A 613 O 85.6 154.4 85.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FB2 A 504
DBREF 5JAD A 46 428 UNP Q13093 PAFA_HUMAN 46 428
SEQADV 5JAD HIS A 429 UNP Q13093 EXPRESSION TAG
SEQADV 5JAD HIS A 430 UNP Q13093 EXPRESSION TAG
SEQADV 5JAD HIS A 431 UNP Q13093 EXPRESSION TAG
SEQADV 5JAD HIS A 432 UNP Q13093 EXPRESSION TAG
SEQADV 5JAD HIS A 433 UNP Q13093 EXPRESSION TAG
SEQRES 1 A 388 MET ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG
SEQRES 2 A 388 GLY ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET
SEQRES 3 A 388 PHE ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR
SEQRES 4 A 388 TYR PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP
SEQRES 5 A 388 ILE PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE
SEQRES 6 A 388 LEU GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU
SEQRES 7 A 388 LEU PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER
SEQRES 8 A 388 PRO LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE
SEQRES 9 A 388 SER HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA
SEQRES 10 A 388 ILE GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA
SEQRES 11 A 388 ALA VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR
SEQRES 12 A 388 TYR PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS
SEQRES 13 A 388 SER TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU
SEQRES 14 A 388 THR HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS
SEQRES 15 A 388 GLU CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP
SEQRES 16 A 388 HIS GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE
SEQRES 17 A 388 ASP MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS
SEQRES 18 A 388 ILE ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL
SEQRES 19 A 388 ILE GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY
SEQRES 20 A 388 ILE ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU
SEQRES 21 A 388 VAL TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN
SEQRES 22 A 388 SER GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET
SEQRES 23 A 388 LYS LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE
SEQRES 24 A 388 THR ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE
SEQRES 25 A 388 THR PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS
SEQRES 26 A 388 LEU LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU
SEQRES 27 A 388 SER ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU
SEQRES 28 A 388 GLY LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE
SEQRES 29 A 388 GLU GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE
SEQRES 30 A 388 ASN THR THR ASN GLN HIS HIS HIS HIS HIS HIS
HET MG A 501 1
HET CL A 502 1
HET DMS A 503 4
HET FB2 A 504 17
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM FB2 BENZENESULFONAMIDE
FORMUL 2 MG MG 2+
FORMUL 3 CL CL 1-
FORMUL 4 DMS C2 H6 O S
FORMUL 5 FB2 C6 H7 N O2 S
FORMUL 6 HOH *143(H2 O)
HELIX 1 AA1 ASN A 100 LEU A 111 1 12
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 ILE A 198 1 7
HELIX 5 AA5 GLU A 213 GLY A 242 1 30
HELIX 6 AA6 ASP A 254 LYS A 259 5 6
HELIX 7 AA7 SER A 273 ASP A 286 1 14
HELIX 8 AA8 GLU A 305 ARG A 309 5 5
HELIX 9 AA9 TYR A 324 LYS A 333 1 10
HELIX 10 AB1 VAL A 350 ALA A 360 5 11
HELIX 11 AB2 GLY A 362 LEU A 369 1 8
HELIX 12 AB3 ASP A 376 GLY A 397 1 22
HELIX 13 AB4 ASP A 401 GLN A 404 5 4
HELIX 14 AB5 TRP A 405 GLU A 410 1 6
SHEET 1 AA111 ASP A 94 LEU A 96 0
SHEET 2 AA111 THR A 129 TRP A 134 -1 O THR A 130 N THR A 95
SHEET 3 AA111 VAL A 65 PHE A 72 1 N VAL A 65 O ASN A 133
SHEET 4 AA111 THR A 79 PRO A 86 -1 O TYR A 85 N GLY A 66
SHEET 5 AA111 ILE A 173 VAL A 177 -1 O VAL A 174 N TYR A 84
SHEET 6 AA111 TYR A 144 SER A 150 1 N VAL A 147 O ALA A 175
SHEET 7 AA111 ILE A 262 HIS A 272 1 O ASP A 263 N TYR A 144
SHEET 8 AA111 CYS A 291 LEU A 295 1 O LEU A 295 N GLY A 271
SHEET 9 AA111 LEU A 314 SER A 319 1 O ILE A 317 N ALA A 294
SHEET 10 AA111 ARG A 341 ILE A 346 1 O ILE A 344 N ASN A 318
SHEET 11 AA111 LEU A 416 PRO A 418 -1 O ILE A 417 N THR A 345
SHEET 1 AA2 2 ALA A 186 TYR A 189 0
SHEET 2 AA2 2 SER A 202 TYR A 205 -1 O SER A 202 N TYR A 189
LINK O GLU A 285 MG MG A 501 1555 1555 2.04
LINK MG MG A 501 O HOH A 613 1555 1555 2.46
LINK O GLU A 285 MG MG A 501 1555 2655 2.04
LINK MG MG A 501 O HOH A 613 1555 2655 2.46
CISPEP 1 PHE A 72 ASP A 73 0 -9.01
SITE 1 AC1 2 GLU A 285 HOH A 613
SITE 1 AC2 1 HIS A 351
SITE 1 AC3 6 LEU A 153 SER A 273 TRP A 298 PHE A 322
SITE 2 AC3 6 HIS A 351 HOH A 650
SITE 1 AC4 8 GLY A 152 LEU A 153 GLY A 154 ALA A 155
SITE 2 AC4 8 LEU A 159 TYR A 160 HIS A 272 GLN A 352
CRYST1 98.970 91.029 51.191 90.00 112.05 90.00 C 1 2 1 4
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 0.010104 0.000000 0.004093 0.00000
SCALE2 0.000000 0.010986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021076 0.00000
TER 2977 THR A 425
MASTER 340 0 4 14 13 0 6 6 3132 1 24 30
END |