HEADER TRANSFERASE 17-FEB-15 5AIS
TITLE COMPLEX OF HUMAN HEMATOPOIETIC PROSTAGANDIN D2 SYNTHASE (HH-
TITLE 2 PGDS) IN COMPLEX WITH AN ACTIVE SITE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE;
COMPND 3 CHAIN: A, C, B, D;
COMPND 4 SYNONYM: H-PGDS, GST CLASS-SIGMA, GLUTATHIONE S-TRANSFERASE,
COMPND 5 GLUTATH IONE-DEPENDENT PGD SYNTHASE, GLUTATHIONE-REQUIRING
COMPND 6 PROSTAGLANDIN D SYNTHASE, PROSTAGLANDIN-H2 D-ISOMERASE;
COMPND 7 EC: 5.3.99.2, 2.5.1.18;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, PROSTAGLANDIN D2 SYNTHASE, PGDS INHIBITORS, INDOLE,
KEYWDS 2 FOCUSED SCREENING, HIT VALIDATION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.EDFELDT,J.EVENAS,M.LEPISTO,A.WARD,J.PETERSEN,L.WISSLER,M.ROHMAN,
AUTHOR 2 U.SIVARS,K.SVENSSON,M.PERRY,I.FEIERBERG,X.ZHOU,T.HANSSON,F.NARJES
REVDAT 2 10-JUN-15 5AIS 1 JRNL
REVDAT 1 03-JUN-15 5AIS 0
JRNL AUTH F.EDFELDT,J.EVEN,M.LEPISTO,A.WARD,J.PETERSEN,L.WISSLER,
JRNL AUTH 2 M.ROHMAN,U.SIVARS,K.SVENSSON,M.PERRY,I.FEIERBERG,X.H.ZHOU,
JRNL AUTH 3 T.HANSSON,F.NARJES
JRNL TITL IDENTIFICATION OF INDOLE INHIBITORS OF HUMAN HEMATOPOIETIC
JRNL TITL 2 PROSTAGLANDIN D2 SYNTHASE (HH-PGDS).
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 2496 2015
JRNL REFN ISSN 0960-894X
JRNL PMID 25978964
JRNL DOI 10.1016/J.BMCL.2015.04.065
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0027
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON,TURK
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.40
REMARK 3 NUMBER OF REFLECTIONS : 64497
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) : 0.23261
REMARK 3 R VALUE (WORKING SET) : 0.23142
REMARK 3 FREE R VALUE : 0.25453
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 3439
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) : 1.850
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.898
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4514
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.52
REMARK 3 BIN R VALUE (WORKING SET) : 0.299
REMARK 3 BIN FREE R VALUE SET COUNT : 237
REMARK 3 BIN FREE R VALUE : 0.312
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6603
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 178
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.768
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : 0.00
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.194
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.102
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6962 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6483 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9468 ; 0.814 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14910 ; 0.670 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 800 ; 4.090 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 337 ;31.973 ;24.273
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1177 ;12.462 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;10.747 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1018 ; 0.044 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7918 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1624 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 5AIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-15.
REMARK 100 THE PDBE ID CODE IS EBI-63074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69399
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85
REMARK 200 RESOLUTION RANGE LOW (A) : 49.47
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : 0.19
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 1.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 62.40100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 62.40100
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.44200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.40100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.72100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.40100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.16300
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 62.40100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.40100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.44200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 62.40100
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 80.16300
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 62.40100
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 26.72100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 HIS A 1
REMARK 465 HIS B 1
REMARK 465 HIS C 1
REMARK 465 HIS D 1
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 GLN A 63 107.36 69.14
REMARK 500 GLN B 63 108.48 69.43
REMARK 500 ARG C 12 -70.26 -67.68
REMARK 500 GLN C 63 110.48 70.51
REMARK 500 GLN D 63 108.35 70.96
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 MG B1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2049 O
REMARK 620 2 HOH B2052 O 99.0
REMARK 620 3 HOH A2044 O 87.0 87.9
REMARK 620 4 HOH A2045 O 86.4 168.0 81.6
REMARK 620 5 HOH B2048 O 171.0 86.9 100.2 89.2
REMARK 620 6 HOH B2051 O 82.3 91.1 169.0 100.3 90.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2045 O
REMARK 620 2 HOH C2043 O 85.2
REMARK 620 3 HOH C2049 O 85.5 87.8
REMARK 620 4 HOH D2029 O 77.7 87.3 162.8
REMARK 620 5 HOH D2030 O 161.8 88.5 111.4 84.9
REMARK 620 6 HOH D2031 O 91.4 169.8 82.3 101.4 97.5
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 CWC C1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CWC D1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CWC A1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CWC B1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH D1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AIV RELATED DB: PDB
REMARK 900 COMPLEX OF HUMAN HEMATOPOIETIC PROSTAGANDIN D2 SYNTHASE (
REMARK 900 HH-PGDS) IN COMPLEX WITH AN ACTIVE SITE INHIBITOR.
DBREF 5AIS A 2 199 UNP O60760 HPGDS_HUMAN 2 199
DBREF 5AIS B 2 199 UNP O60760 HPGDS_HUMAN 2 199
DBREF 5AIS C 2 199 UNP O60760 HPGDS_HUMAN 2 199
DBREF 5AIS D 2 199 UNP O60760 HPGDS_HUMAN 2 199
SEQADV 5AIS HIS A 1 UNP O60760 EXPRESSION TAG
SEQADV 5AIS HIS B 1 UNP O60760 EXPRESSION TAG
SEQADV 5AIS HIS C 1 UNP O60760 EXPRESSION TAG
SEQADV 5AIS HIS D 1 UNP O60760 EXPRESSION TAG
SEQRES 1 A 199 HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY
SEQRES 2 A 199 ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP
SEQRES 3 A 199 ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP
SEQRES 4 A 199 PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO
SEQRES 5 A 199 ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU
SEQRES 6 A 199 ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA
SEQRES 7 A 199 GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE
SEQRES 8 A 199 VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP
SEQRES 9 A 199 ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN
SEQRES 10 A 199 GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP
SEQRES 11 A 199 LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY
SEQRES 12 A 199 ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS
SEQRES 13 A 199 SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP
SEQRES 14 A 199 ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN
SEQRES 15 A 199 ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO
SEQRES 16 A 199 GLN THR LYS LEU
SEQRES 1 B 199 HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY
SEQRES 2 B 199 ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP
SEQRES 3 B 199 ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP
SEQRES 4 B 199 PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO
SEQRES 5 B 199 ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU
SEQRES 6 B 199 ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA
SEQRES 7 B 199 GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE
SEQRES 8 B 199 VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP
SEQRES 9 B 199 ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN
SEQRES 10 B 199 GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP
SEQRES 11 B 199 LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY
SEQRES 12 B 199 ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS
SEQRES 13 B 199 SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP
SEQRES 14 B 199 ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN
SEQRES 15 B 199 ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO
SEQRES 16 B 199 GLN THR LYS LEU
SEQRES 1 C 199 HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY
SEQRES 2 C 199 ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP
SEQRES 3 C 199 ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP
SEQRES 4 C 199 PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO
SEQRES 5 C 199 ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU
SEQRES 6 C 199 ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA
SEQRES 7 C 199 GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE
SEQRES 8 C 199 VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP
SEQRES 9 C 199 ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN
SEQRES 10 C 199 GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP
SEQRES 11 C 199 LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY
SEQRES 12 C 199 ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS
SEQRES 13 C 199 SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP
SEQRES 14 C 199 ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN
SEQRES 15 C 199 ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO
SEQRES 16 C 199 GLN THR LYS LEU
SEQRES 1 D 199 HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY
SEQRES 2 D 199 ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP
SEQRES 3 D 199 ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP
SEQRES 4 D 199 PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO
SEQRES 5 D 199 ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU
SEQRES 6 D 199 ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA
SEQRES 7 D 199 GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE
SEQRES 8 D 199 VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP
SEQRES 9 D 199 ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN
SEQRES 10 D 199 GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP
SEQRES 11 D 199 LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY
SEQRES 12 D 199 ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS
SEQRES 13 D 199 SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP
SEQRES 14 D 199 ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN
SEQRES 15 D 199 ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO
SEQRES 16 D 199 GLN THR LYS LEU
HET CWC C1200 24
HET CWC D1200 24
HET CWC A1200 24
HET CWC B1200 24
HET MG D1201 1
HET MG B1201 1
HET GSH D1202 20
HET GSH C1201 20
HET GSH B1202 20
HET GSH A1201 20
HETNAM CWC 4-(DIMETHYLAMINO)-N-[5-(1H-INDOL-4-YL)
HETNAM 2 CWC PYRIDIN-3-YL]BUTANAMIDE
HETNAM GSH GLUTATHIONE
HETNAM MG MAGNESIUM ION
FORMUL 5 CWC 4(C19 H22 N4 O)
FORMUL 6 GSH 4(C10 H18 N3 O6 S 1+)
FORMUL 7 MG 2(MG 2+)
FORMUL 8 HOH *288(H2 O)
HELIX 1 1 ARG A 12 ARG A 14 5 3
HELIX 2 2 ALA A 15 LEU A 25 1 11
HELIX 3 3 ASP A 38 LEU A 46 1 9
HELIX 4 4 GLN A 63 THR A 72 1 10
HELIX 5 5 THR A 75 GLY A 79 5 5
HELIX 6 6 THR A 81 SER A 100 1 20
HELIX 7 7 LYS A 108 TYR A 122 1 15
HELIX 8 8 TYR A 122 GLY A 136 1 15
HELIX 9 9 THR A 147 LYS A 164 1 18
HELIX 10 10 HIS A 171 ILE A 184 1 14
HELIX 11 11 ILE A 184 ARG A 194 1 11
HELIX 12 12 ARG B 12 ARG B 14 5 3
HELIX 13 13 ALA B 15 LEU B 25 1 11
HELIX 14 14 GLU B 35 ALA B 37 5 3
HELIX 15 15 ASP B 38 SER B 44 1 7
HELIX 16 16 GLN B 63 LYS B 73 1 11
HELIX 17 17 THR B 81 SER B 100 1 20
HELIX 18 18 LYS B 108 ASN B 123 1 16
HELIX 19 19 ASN B 123 GLY B 136 1 14
HELIX 20 20 THR B 147 LYS B 164 1 18
HELIX 21 21 HIS B 171 ILE B 184 1 14
HELIX 22 22 ILE B 184 ARG B 194 1 11
HELIX 23 23 ALA C 15 LEU C 25 1 11
HELIX 24 24 ASP C 38 LEU C 46 1 9
HELIX 25 25 GLN C 63 LYS C 73 1 11
HELIX 26 26 THR C 81 SER C 100 1 20
HELIX 27 27 LYS C 108 ASN C 123 1 16
HELIX 28 28 ASN C 123 GLY C 136 1 14
HELIX 29 29 THR C 147 LYS C 164 1 18
HELIX 30 30 HIS C 171 ALA C 183 1 13
HELIX 31 31 ILE C 184 ARG C 194 1 11
HELIX 32 32 ARG D 12 ARG D 14 5 3
HELIX 33 33 ALA D 15 ASP D 26 1 12
HELIX 34 34 ASP D 38 LEU D 46 1 9
HELIX 35 35 GLN D 63 LYS D 73 1 11
HELIX 36 36 THR D 81 CYS D 101 1 21
HELIX 37 37 LYS D 108 ASN D 123 1 16
HELIX 38 38 ASN D 123 GLY D 136 1 14
HELIX 39 39 THR D 147 LYS D 164 1 18
HELIX 40 40 HIS D 171 ALA D 183 1 13
HELIX 41 41 ILE D 184 ARG D 194 1 11
SHEET 1 AA 4 GLU A 30 ILE A 34 0
SHEET 2 AA 4 TYR A 4 PHE A 9 1 O TYR A 4 N GLU A 30
SHEET 3 AA 4 ILE A 53 VAL A 56 -1 O ILE A 53 N THR A 7
SHEET 4 AA 4 LEU A 59 HIS A 62 -1 O LEU A 59 N VAL A 56
SHEET 1 BA 4 GLU B 30 ILE B 34 0
SHEET 2 BA 4 TYR B 4 PHE B 9 1 O TYR B 4 N GLU B 30
SHEET 3 BA 4 ILE B 53 VAL B 56 -1 O ILE B 53 N THR B 7
SHEET 4 BA 4 THR B 60 HIS B 62 -1 O LEU B 61 N LEU B 54
SHEET 1 CA 4 TYR C 29 ILE C 34 0
SHEET 2 CA 4 TYR C 4 PHE C 9 1 O TYR C 4 N GLU C 30
SHEET 3 CA 4 ILE C 53 VAL C 56 -1 O ILE C 53 N THR C 7
SHEET 4 CA 4 LEU C 59 HIS C 62 -1 O LEU C 59 N VAL C 56
SHEET 1 DA 4 GLU D 30 ILE D 34 0
SHEET 2 DA 4 TYR D 4 PHE D 9 1 O TYR D 4 N GLU D 30
SHEET 3 DA 4 ILE D 53 VAL D 56 -1 O ILE D 53 N THR D 7
SHEET 4 DA 4 LEU D 59 HIS D 62 -1 O LEU D 59 N VAL D 56
LINK MG MG B1201 O HOH A2049 1555 1555 2.17
LINK MG MG B1201 O HOH B2052 1555 1555 2.00
LINK MG MG B1201 O HOH A2044 1555 1555 2.15
LINK MG MG B1201 O HOH A2045 1555 1555 2.17
LINK MG MG B1201 O HOH B2048 1555 1555 2.15
LINK MG MG B1201 O HOH B2051 1555 1555 2.16
LINK MG MG D1201 O HOH C2043 1555 1555 2.11
LINK MG MG D1201 O HOH C2049 1555 1555 2.23
LINK MG MG D1201 O HOH D2029 1555 1555 2.26
LINK MG MG D1201 O HOH D2030 1555 1555 2.06
LINK MG MG D1201 O HOH D2031 1555 1555 1.96
LINK MG MG D1201 O HOH C2045 1555 1555 2.21
CISPEP 1 ILE A 51 PRO A 52 0 9.63
CISPEP 2 ILE B 51 PRO B 52 0 10.74
CISPEP 3 ILE C 51 PRO C 52 0 9.59
CISPEP 4 ILE D 51 PRO D 52 0 8.43
SITE 1 AC1 9 PHE C 9 MET C 11 GLY C 13 ARG C 14
SITE 2 AC1 9 ASP C 96 MET C 99 TRP C 104 TYR C 152
SITE 3 AC1 9 GSH C1201
SITE 1 AC2 13 PHE D 9 MET D 11 GLY D 13 ARG D 14
SITE 2 AC2 13 GLN D 36 ASP D 96 MET D 99 TRP D 104
SITE 3 AC2 13 TYR D 152 LEU D 199 GSH D1202 HOH D2006
SITE 4 AC2 13 HOH D2032
SITE 1 AC3 8 MET A 11 GLY A 13 ARG A 14 ASP A 96
SITE 2 AC3 8 MET A 99 TRP A 104 TYR A 152 GSH A1201
SITE 1 AC4 11 TYR B 8 MET B 11 GLY B 13 ARG B 14
SITE 2 AC4 11 GLN B 36 ASP B 96 MET B 99 TRP B 104
SITE 3 AC4 11 TYR B 152 GSH B1202 HOH B2012
SITE 1 AC5 6 HOH C2043 HOH C2045 HOH C2049 HOH D2029
SITE 2 AC5 6 HOH D2030 HOH D2031
SITE 1 AC6 6 HOH A2044 HOH A2045 HOH A2049 HOH B2048
SITE 2 AC6 6 HOH B2051 HOH B2052
SITE 1 AC7 10 ASP C 97 TYR D 8 ARG D 14 TRP D 39
SITE 2 AC7 10 LYS D 50 ILE D 51 GLN D 63 SER D 64
SITE 3 AC7 10 CWC D1200 HOH D2022
SITE 1 AC8 14 TYR C 8 ARG C 14 TRP C 39 LYS C 43
SITE 2 AC8 14 LYS C 50 ILE C 51 PRO C 52 GLN C 63
SITE 3 AC8 14 SER C 64 CWC C1200 HOH C2009 HOH C2027
SITE 4 AC8 14 HOH C2048 ASP D 97
SITE 1 AC9 14 ASP A 97 TYR B 8 ARG B 14 TRP B 39
SITE 2 AC9 14 LYS B 43 LYS B 50 ILE B 51 PRO B 52
SITE 3 AC9 14 GLN B 63 SER B 64 CWC B1200 HOH B2015
SITE 4 AC9 14 HOH B2016 HOH B2034
SITE 1 BC1 13 TYR A 8 ARG A 14 TRP A 39 LYS A 43
SITE 2 BC1 13 LYS A 50 ILE A 51 GLN A 63 SER A 64
SITE 3 BC1 13 CWC A1200 HOH A2008 HOH A2024 HOH A2050
SITE 4 BC1 13 ASP B 97
CRYST1 124.802 124.802 106.884 90.00 90.00 90.00 I 41 32
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 0.008013 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009356 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
