HEADER MEMBRANE PROTEIN, TRANSFERASE 10-OCT-16 5TL9
TITLE CRYSTAL STRUCTURE OF MPGES-1 BOUND TO INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN E SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MICROSOMAL GLUTATHIONE S-TRANSFERASE 1-LIKE 1,MGST1-L1,
COMPND 5 MICROSOMAL PROSTAGLANDIN E SYNTHASE 1,MPGES-1,P53-INDUCED GENE 12
COMPND 6 PROTEIN;
COMPND 7 EC: 5.3.99.3;
COMPND 8 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: PTGES, MGST1L1, MPGES1, PGES, PIG12;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROSTAGLANDIN, ENZYME, INTEGRAL MEMBRANE PROTEIN, ALPHA HELIX, MPGES1
KEYWDS 2 - LIGAND 0, MEMBRANE PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.G.LUZ,S.ANTONYSAMY,K.PARTRIDGE,M.FISHER
REVDAT 5 29-JUL-20 5TL9 1 COMPND REMARK HETNAM SITE
REVDAT 4 04-DEC-19 5TL9 1 REMARK
REVDAT 3 06-SEP-17 5TL9 1 REMARK
REVDAT 2 15-MAR-17 5TL9 1 JRNL
REVDAT 1 01-MAR-17 5TL9 0
JRNL AUTH K.M.PARTRIDGE,S.ANTONYSAMY,S.N.BHATTACHAR,S.CHANDRASEKHAR,
JRNL AUTH 2 M.J.FISHER,A.FRETLAND,K.GOODING,A.HARVEY,N.E.HUGHES,
JRNL AUTH 3 S.L.KUKLISH,J.G.LUZ,P.R.MANNINEN,J.E.MCGEE,D.R.MUDRA,
JRNL AUTH 4 A.NAVARRO,B.H.NORMAN,S.J.QUIMBY,M.A.SCHIFFLER,A.V.SLOAN,
JRNL AUTH 5 A.M.WARSHAWSKY,J.M.WELLER,J.S.YORK,X.P.YU
JRNL TITL DISCOVERY AND CHARACTERIZATION OF
JRNL TITL 2 [(CYCLOPENTYL)ETHYL]BENZOIC ACID INHIBITORS OF MICROSOMAL
JRNL TITL 3 PROSTAGLANDIN E SYNTHASE-1.
JRNL REF BIOORG. MED. CHEM. LETT. V. 27 1478 2017
JRNL REFN ESSN 1464-3405
JRNL PMID 28190634
JRNL DOI 10.1016/J.BMCL.2016.11.011
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 80353
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4300
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5479
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 268
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1175
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 127
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.34000
REMARK 3 B12 (A**2) : 0.05000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.028
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.028
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.019
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.963
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1431 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1944 ; 1.114 ; 2.051
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 168 ; 3.965 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 51 ;39.793 ;20.980
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 215 ;11.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;12.426 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 217 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1033 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 633 ; 2.128 ;22.656
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 803 ; 2.167 ;35.777
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 797 ; 3.884 ;31.178
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
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): 2282 ; 4.786 ; NULL
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): 1430 ; 0.359 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 45 ;42.895 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1479 ;16.348 ; 5.000
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 : NULL
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: NULL
REMARK 4
REMARK 4 5TL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 78.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80353
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.9 28% PEG 1K, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 294.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.65900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.31978
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.98467
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 38.65900
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.31978
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.98467
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 38.65900
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.31978
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.98467
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.63957
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 81.96933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 44.63957
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 81.96933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 44.63957
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 81.96933
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 429 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 -1
REMARK 465 ALA A 0
REMARK 465 LEU A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 HIS A 4
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 MET A 8 33.05 -94.23
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 437 DISTANCE = 5.91 ANGSTROMS
DBREF 5TL9 A 2 152 UNP O14684 PTGES_HUMAN 2 152
SEQADV 5TL9 MET A -1 UNP O14684 INITIATING METHIONINE
SEQADV 5TL9 ALA A 0 UNP O14684 EXPRESSION TAG
SEQADV 5TL9 LEU A 1 UNP O14684 EXPRESSION TAG
SEQRES 1 A 154 MET ALA LEU PRO ALA HIS SER LEU VAL MET SER SER PRO
SEQRES 2 A 154 ALA LEU PRO ALA PHE LEU LEU CYS SER THR LEU LEU VAL
SEQRES 3 A 154 ILE LYS MET TYR VAL VAL ALA ILE ILE THR GLY GLN VAL
SEQRES 4 A 154 ARG LEU ARG LYS LYS ALA PHE ALA ASN PRO GLU ASP ALA
SEQRES 5 A 154 LEU ARG HIS GLY GLY PRO GLN TYR CSO ARG SER ASP PRO
SEQRES 6 A 154 ASP VAL GLU ARG CYS LEU ARG ALA HIS ARG ASN ASP MET
SEQRES 7 A 154 GLU THR ILE TYR PRO PHE LEU PHE LEU GLY PHE VAL TYR
SEQRES 8 A 154 SER PHE LEU GLY PRO ASN PRO PHE VAL ALA TRP MET HIS
SEQRES 9 A 154 PHE LEU VAL PHE LEU VAL GLY ARG VAL ALA HIS THR VAL
SEQRES 10 A 154 ALA TYR LEU GLY LYS LEU ARG ALA PRO ILE ARG SER VAL
SEQRES 11 A 154 THR TYR THR LEU ALA GLN LEU PRO CYS ALA SER MET ALA
SEQRES 12 A 154 LEU GLN ILE LEU TRP GLU ALA ALA ARG HIS LEU
MODRES 5TL9 CSO A 59 CYS MODIFIED RESIDUE
HET CSO A 59 7
HET 7DN A 201 36
HET GSH A 202 20
HET JZR A 203 18
HET BOG A 204 20
HET PG4 A 205 13
HET PG4 A 206 13
HET PEG A 207 7
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM 7DN 2-{2-[(1S,2S)-2-{[1-(8-METHYLQUINOLIN-2-YL)PIPERIDINE-
HETNAM 2 7DN 4-CARBONYL]AMINO}CYCLOPENTYL]ETHYL}BENZOIC ACID
HETNAM GSH GLUTATHIONE
HETNAM JZR HEXYL BETA-D-GLUCOPYRANOSIDE
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 2 7DN C30 H35 N3 O3
FORMUL 3 GSH C10 H17 N3 O6 S
FORMUL 4 JZR C12 H24 O6
FORMUL 5 BOG C14 H28 O6
FORMUL 6 PG4 2(C8 H18 O5)
FORMUL 8 PEG C4 H10 O3
FORMUL 9 HOH *137(H2 O)
HELIX 1 AA1 SER A 5 SER A 10 5 6
HELIX 2 AA2 ALA A 12 LYS A 42 1 31
HELIX 3 AA3 ASN A 46 HIS A 53 1 8
HELIX 4 AA4 GLY A 55 CSO A 59 5 5
HELIX 5 AA5 ASP A 62 PHE A 91 1 30
HELIX 6 AA6 ASN A 95 GLY A 119 1 25
HELIX 7 AA7 PRO A 124 HIS A 151 1 28
LINK C TYR A 58 N CSO A 59 1555 1555 1.34
LINK C CSO A 59 N ARG A 60 1555 1555 1.33
CISPEP 1 ALA A 123 PRO A 124 0 4.71
CRYST1 77.318 77.318 122.954 90.00 90.00 120.00 H 3 9
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 0.012934 0.007467 0.000000 0.00000
SCALE2 0.000000 0.014934 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
