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HEADER HYDROLASE 29-SEP-16 5LZ9
TITLE FRAGMENT-BASED INHIBITORS OF LIPOPROTEIN ASSOCIATED PHOSPHOLIPASE A2
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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET30A
KEYWDS LP-PLA2 PHOSPHOLIPASE, HYDROLASE, LIPID METABOLISM, INHIBITORS, LP-
KEYWDS 2 PLA2#4
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WOOLFORD,P.DAY
REVDAT 1 21-DEC-16 5LZ9 0
JRNL AUTH A.J.WOOLFORD,P.J.DAY,V.BENETON,V.BERDINI,J.E.COYLE,Y.DUDIT,
JRNL AUTH 2 P.GRONDIN,P.HUET,L.Y.LEE,E.S.MANAS,R.L.MCMENAMIN,C.W.MURRAY,
JRNL AUTH 3 L.W.PAGE,V.K.PATEL,F.POTVAIN,S.J.RICH,Y.SANG,D.O.SOMERS,
JRNL AUTH 4 L.TROTTET,Z.WAN,X.ZHANG
JRNL TITL FRAGMENT-BASED APPROACH TO THE DEVELOPMENT OF AN ORALLY
JRNL TITL 2 BIOAVAILABLE LACTAM INHIBITOR OF LIPOPROTEIN-ASSOCIATED
JRNL TITL 3 PHOSPHOLIPASE A2 (LP-PLA2).
JRNL REF J. MED. CHEM. V. 59 10738 2016
JRNL REFN ISSN 1520-4804
JRNL PMID 27933945
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01427
REMARK 2
REMARK 2 RESOLUTION. 2.06 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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 24691
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1324
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) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2971
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 252
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : -1.42000
REMARK 3 B33 (A**2) : 0.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.205
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.547
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3092 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2924 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4189 ; 1.445 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6736 ; 1.257 ; 2.985
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 375 ; 6.170 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;38.746 ;23.705
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 543 ;14.402 ;15.055
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;12.691 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 445 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3493 ; 0.001 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 742 ; 0.001 ; 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): 1488 ; 1.459 ; 5.469
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1487 ; 1.459 ; 5.467
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): 1602 ; 1.773 ; 5.905
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1603 ; 1.772 ; 5.906
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): 1086 ; 3.453 ;12.327
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 424
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5079 14.7304 0.7411
REMARK 3 T TENSOR
REMARK 3 T11: 0.0059 T22: 0.0938
REMARK 3 T33: 0.0262 T12: -0.0009
REMARK 3 T13: 0.0017 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 3.2431 L22: 2.3517
REMARK 3 L33: 2.2713 L12: -0.1365
REMARK 3 L13: 0.0664 L23: -0.5482
REMARK 3 S TENSOR
REMARK 3 S11: 0.1070 S12: -0.0506 S13: 0.0794
REMARK 3 S21: -0.0072 S22: -0.0737 S23: 0.1883
REMARK 3 S31: -0.0688 S32: 0.0343 S33: -0.0333
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 5LZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001629.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-12
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-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 44.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.64700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.8.0135
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES/NAOHPH=7.4, 1.3M NACL,
REMARK 280 32.0%W/V PEG 3350,, PH 7.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 50.02200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.66600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.02200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.66600
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: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 NA NA A 502 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 819 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 THR A 425
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 -174.98 -68.15
REMARK 500 HIS A 241 22.80 -78.91
REMARK 500 LYS A 266 77.09 -103.38
REMARK 500 SER A 273 -105.87 61.07
REMARK 500 HIS A 399 55.68 -110.81
REMARK 500 LYS A 400 -162.01 -109.33
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 850 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 851 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 852 DISTANCE = 6.92 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 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 285 O
REMARK 620 2 HOH A 700 O 89.1
REMARK 620 3 HOH A 819 O 125.3 97.7
REMARK 620 4 GLU A 285 O 0.0 89.1 125.3
REMARK 620 5 HOH A 700 O 78.0 161.9 100.2 78.0
REMARK 620 6 HOH A 819 O 125.3 97.9 0.2 125.3 100.0
REMARK 620 N 1 2 3 4 5
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 NA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BR A 503
DBREF 5LZ9 A 46 428 UNP Q13093 PAFA_HUMAN 46 428
SEQADV 5LZ9 HIS A 429 UNP Q13093 EXPRESSION TAG
SEQADV 5LZ9 HIS A 430 UNP Q13093 EXPRESSION TAG
SEQADV 5LZ9 HIS A 431 UNP Q13093 EXPRESSION TAG
SEQADV 5LZ9 HIS A 432 UNP Q13093 EXPRESSION TAG
SEQADV 5LZ9 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 NA A 502 1
HET 7BR A 503 50
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM 7BR 2-FLUORANYL-5-[2-[(4~{S})-4-[4-METHYL-1,1-
HETNAM 2 7BR BIS(OXIDANYLIDENE)THIAN-4-YL]-2-OXIDANYLIDENE-
HETNAM 3 7BR PYRROLIDIN-1-YL]ETHOXY]BENZENECARBONITRILE
FORMUL 2 CL CL 1-
FORMUL 3 NA NA 1+
FORMUL 4 7BR C19 H23 F N2 O4 S
FORMUL 5 HOH *252(H2 O)
HELIX 1 AA1 ASN A 100 GLY A 112 1 13
HELIX 2 AA2 HIS A 114 GLY A 126 1 13
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 GLU A 213 HIS A 241 1 29
HELIX 6 AA6 ASP A 254 LYS A 259 5 6
HELIX 7 AA7 SER A 273 SER A 284 1 12
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 PHE A 359 5 10
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 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 TYR A 85 N GLY A 66
SHEET 5 AA111 ILE A 173 VAL A 177 -1 O ALA A 176 N ARG A 82
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 VAL A 148
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 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 NA NA A 502 1555 1555 2.42
LINK NA NA A 502 O HOH A 700 1555 1555 2.54
LINK NA NA A 502 O HOH A 819 1555 1555 2.06
LINK O GLU A 285 NA NA A 502 1555 2655 2.34
LINK NA NA A 502 O HOH A 700 1555 2655 2.47
LINK NA NA A 502 O HOH A 819 1555 2655 2.06
CISPEP 1 PHE A 72 ASP A 73 0 -9.18
SITE 1 AC1 4 LEU A 93 PRO A 325 ALA A 326 HOH A 836
SITE 1 AC2 3 GLU A 285 HOH A 700 HOH A 819
SITE 1 AC3 15 ASP A 89 LEU A 107 GLY A 152 LEU A 153
SITE 2 AC3 15 GLY A 154 ALA A 155 LEU A 159 SER A 273
SITE 3 AC3 15 PHE A 274 TRP A 298 HIS A 351 GLN A 352
SITE 4 AC3 15 ALA A 355 ASP A 356 PHE A 357
CRYST1 100.044 91.332 51.357 90.00 111.97 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 0.009996 0.000000 0.004032 0.00000
SCALE2 0.000000 0.010949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020996 0.00000
TER 2987 THR A 424
MASTER 357 0 3 14 13 0 6 6 3252 1 54 30
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