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HEADER HYDROLASE 12-APR-16 5JAN
TITLE EXPLOITATION OF A NOVEL BINDING POCKET IN HUMAN LIPOPROTEIN-ASSOCIATED
TITLE 2 PHOSPHOLIPASE A2 (LP-PLA2) DISCOVERED THROUGH X-RAY
TITLE 3 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: 562
KEYWDS PHOSPHOLIPASE, LIPID METABOLISM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.DAY
REVDAT 1 25-MAY-16 5JAN 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. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 21778
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1172
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1567
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2978
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.67000
REMARK 3 B22 (A**2) : -2.14000
REMARK 3 B33 (A**2) : 3.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.78000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.280
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.474
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3071 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2904 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4154 ; 1.425 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6684 ; 0.932 ; 2.988
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 372 ; 6.805 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;38.836 ;23.865
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 532 ;14.233 ;15.028
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;13.984 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3472 ; 0.000 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 738 ; 0.000 ; 0.020
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): 1485 ; 1.057 ; 3.139
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1484 ; 1.036 ; 3.135
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): 1584 ; 1.347 ; 3.546
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1585 ; 1.347 ; 3.549
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): 1071 ; 3.396 ; 7.298
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 55 A 425
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7183 14.6937 1.0399
REMARK 3 T TENSOR
REMARK 3 T11: 0.1260 T22: 0.1333
REMARK 3 T33: 0.0270 T12: 0.0013
REMARK 3 T13: 0.0471 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 2.4734 L22: 2.2689
REMARK 3 L33: 1.6822 L12: -0.3773
REMARK 3 L13: 0.3040 L23: -0.3996
REMARK 3 S TENSOR
REMARK 3 S11: 0.0407 S12: -0.0469 S13: 0.0695
REMARK 3 S21: 0.0124 S22: -0.0338 S23: 0.0995
REMARK 3 S31: -0.0350 S32: -0.1306 S33: -0.0070
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5JAN 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_1000220262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 93
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-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21778
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 46.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5000
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M 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 50.18650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.04000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.18650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.04000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 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 -174.77 -69.23
REMARK 500 SER A 273 -118.10 71.25
REMARK 500 HIS A 399 66.86 -111.50
REMARK 500 LYS A 400 -168.30 -124.05
REMARK 500
REMARK 500 REMARK: NULL
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 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 285 O
REMARK 620 2 HOH A 719 O 108.7
REMARK 620 3 GLU A 285 O 0.0 108.7
REMARK 620 4 HOH A 719 O 122.5 13.9 122.5
REMARK 620 5 HOH A 678 O 87.2 125.2 87.2 120.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL 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 CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6HP A 504
DBREF 5JAN A 46 428 UNP Q13093 PAFA_HUMAN 46 428
SEQADV 5JAN HIS A 429 UNP Q13093 EXPRESSION TAG
SEQADV 5JAN HIS A 430 UNP Q13093 EXPRESSION TAG
SEQADV 5JAN HIS A 431 UNP Q13093 EXPRESSION TAG
SEQADV 5JAN HIS A 432 UNP Q13093 EXPRESSION TAG
SEQADV 5JAN 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 CL A 501 1
HET CL A 502 1
HET CA A 503 1
HET 6HP A 504 31
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETNAM 6HP 1,3-DIMETHYL-6-(2-METHYLPROPOXY)PYRIMIDINE-2,4(1H,3H)-
HETNAM 2 6HP DIONE
FORMUL 2 CL 2(CL 1-)
FORMUL 4 CA CA 2+
FORMUL 5 6HP C10 H16 N2 O3
FORMUL 6 HOH *131(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 HIS A 170 1 11
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 GLY A 242 1 30
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 GLY A 303 TYR A 307 5 5
HELIX 10 AB1 TYR A 324 CYS A 334 1 11
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
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 SER A 64 PHE A 72 1 N VAL A 65 O ASN A 133
SHEET 4 AA111 THR A 79 SER A 87 -1 O LEU A 83 N THR A 68
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 ILE A 270 N SER A 150
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 PHE A 315 N ALA A 294
SHEET 10 AA111 ARG A 341 ILE A 346 1 O LYS A 342 N PHE A 316
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 LEU A 204 N THR A 187
LINK O GLU A 285 CA CA A 503 1555 1555 2.41
LINK CA CA A 503 O HOH A 719 1555 1555 2.74
LINK O GLU A 285 CA CA A 503 1555 2655 2.61
LINK CA CA A 503 O HOH A 719 1555 2655 2.60
LINK CA CA A 503 O HOH A 678 1555 2655 2.26
CISPEP 1 PHE A 72 ASP A 73 0 -8.29
SITE 1 AC1 1 HIS A 351
SITE 1 AC2 4 ARG A 92 LEU A 93 PRO A 325 ALA A 326
SITE 1 AC3 3 GLU A 285 HOH A 678 HOH A 719
SITE 1 AC4 7 ASP A 89 LEU A 153 GLU A 214 SER A 273
SITE 2 AC4 7 TRP A 298 PHE A 322 HOH A 626
CRYST1 100.373 92.080 48.273 90.00 112.60 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 0.009963 0.000000 0.004147 0.00000
SCALE2 0.000000 0.010860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022438 0.00000
TER 2982 THR A 425
MASTER 333 0 4 15 13 0 5 6 3127 1 34 30
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