HEADER TRANSFERASE 07-AUG-97 3FYG
TITLE CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-
TITLE 2 GLUTATHIONE S-TRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MU CLASS TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE
COMPND 3 S-TRANSFERASE OF ISOENZYME;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: RAT GST;
COMPND 6 EC: 2.5.1.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: LIVER;
SOURCE 7 GENE: CDNA INSERT OF CLONE PGT33M;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PSW1GST33;
SOURCE 13 EXPRESSION_SYSTEM_GENE: CDNA INSERT OF CLONE PGT33M
KEYWDS TRANSFERASE, 3-FLUOROTYROSINE, UNNATURAL AMINO ACID, THREE-
KEYWDS 2 DIMENSIONAL STRUCTURE, DETOXIFICATION ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR G.XIAO,J.F.PARSONS,R.N.ARMSTRONG,G.L.GILLILAND
REVDAT 2 24-FEB-09 3FYG 1 VERSN
REVDAT 1 01-JUN-99 3FYG 0
JRNL AUTH G.XIAO,J.F.PARSONS,K.TESH,R.N.ARMSTRONG,
JRNL AUTH 2 G.L.GILLILAND
JRNL TITL CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF
JRNL TITL 2 RAT GLUTATHIONE TRANSFERASE M1-1 WITH GLOBAL
JRNL TITL 3 SUBSTITUTION OF 3-FLUOROTYROSINE FOR TYROSINE.
JRNL REF J.MOL.BIOL. V. 281 323 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9698551
JRNL DOI 10.1006/JMBI.1998.1935
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.F.PARSONS,R.N.ARMSTRONG
REMARK 1 TITL PROTON CONFIGURATION IN THE GROUND STATE AND
REMARK 1 TITL 2 TRANSITION STATE OF A GLUTATHIONE
REMARK 1 TITL 3 TRANSFERASE-CATALYZED REACTION INFERRED FROM THE
REMARK 1 TITL 4 PROPERTIES OF
REMARK 1 TITL 5 TETRADECA(3-FLUOROTYROSYL)GLUTATHIONE TRANSFERASE
REMARK 1 REF J.AM.CHEM.SOC. V. 118 2295 1996
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.JI,W.W.JOHNSON,M.A.SESAY,L.DICKERT,S.M.PRASAD,
REMARK 1 AUTH 2 H.L.AMMON,R.N.ARMSTRONG,G.L.GILLILAND
REMARK 1 TITL STRUCTURE AND FUNCTION OF THE XENOBIOTIC SUBSTRATE
REMARK 1 TITL 2 BINDING SITE OF A GLUTATHIONE S-TRANSFERASE AS
REMARK 1 TITL 3 REVEALED BY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 1 TITL 4 PRODUCT COMPLEXES WITH THE DIASTEREOMERS OF
REMARK 1 TITL 5 9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-
REMARK 1 TITL 6 DIHYDROPHENANTHRENE
REMARK 1 REF BIOCHEMISTRY V. 33 1043 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH X.JI,R.N.ARMSTRONG,G.L.GILLILAND
REMARK 1 TITL SNAPSHOTS ALONG THE REACTION COORDINATE OF AN SNAR
REMARK 1 TITL 2 REACTION CATALYZED BY GLUTATHIONE TRANSFERASE
REMARK 1 REF BIOCHEMISTRY V. 32 12949 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.LIU,X.JI,G.L.GILLILAND,W.J.STEVENS,R.N.ARMSTRONG
REMARK 1 TITL SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE
REMARK 1 TITL 2 SITE OF GLUTATHIONE S-TRANSFERASE. OBSERVATION OF
REMARK 1 TITL 3 AN ON-FACET HYDROGEN BOND BETWEEN THE SIDE CHAIN
REMARK 1 TITL 4 OF THREONINE 13 AND THE PI-CLOUD OF TYROSINE 6 AND
REMARK 1 TITL 5 ITS INFLUENCE ON CATALYSIS
REMARK 1 REF J.AM.CHEM.SOC. V. 115 7910 1993
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 5
REMARK 1 AUTH X.JI,P.ZHANG,R.N.ARMSTRONG,G.L.GILLILAND
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF A GLUTATHIONE
REMARK 1 TITL 2 S-TRANSFERASE FROM THE MU GENE CLASS. STRUCTURAL
REMARK 1 TITL 3 ANALYSIS OF THE BINARY COMPLEX OF ISOENZYME 3-3
REMARK 1 TITL 4 AND GLUTATHIONE AT 2.2-A RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 31 10169 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 6
REMARK 1 AUTH S.LIU,P.ZHANG,X.JI,W.W.JOHNSON,G.L.GILLILAND,
REMARK 1 AUTH 2 R.N.ARMSTRONG
REMARK 1 TITL CONTRIBUTION OF TYROSINE 6 TO THE CATALYTIC
REMARK 1 TITL 2 MECHANISM OF ISOENZYME 3-3 OF GLUTATHIONE
REMARK 1 TITL 3 S-TRANSFERASE
REMARK 1 REF J.BIOL.CHEM. V. 267 4296 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT V. 5-E
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 243942
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3654
REMARK 3 NUCLEIC ACID ATOMS : NULL
REMARK 3 HETEROGEN ATOMS : NULL
REMARK 3 SOLVENT ATOMS : NULL
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 39.800
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; 0.800 ; 3852
REMARK 3 BOND ANGLES (DEGREES) : 2.360 ; 1.300 ; 5172
REMARK 3 TORSION ANGLES (DEGREES) : 20.000; 0.000 ; 2290
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.010 ; 2.000 ; 108
REMARK 3 GENERAL PLANES (A) : 0.011 ; 5.000 ; 532
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 5.810 ; 1.000 ; 3540
REMARK 3 NON-BONDED CONTACTS (A) : 0.090 ; 10.000; 143
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BABINET SCALING
REMARK 3 KSOL : 0.81
REMARK 3 BSOL : 220.00
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT PROTGEO
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL V1.0
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FYG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-96
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 6.8
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 65.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.750
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 3GST: CLASS MU GST
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 42.71500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.21000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.71500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.21000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 815 O HOH A 851 2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 649 O HOH A 649 2655 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 48 CD GLU A 48 OE1 0.070
REMARK 500 GLU A 88 CD GLU A 88 OE2 0.067
REMARK 500 GLU A 125 CD GLU A 125 OE2 0.069
REMARK 500 GLU A 132 CD GLU A 132 OE2 0.104
REMARK 500 GLU A 188 CD GLU A 188 OE2 0.069
REMARK 500 GLU B 28 CD GLU B 28 OE1 0.073
REMARK 500 GLU B 91 CD GLU B 91 OE2 0.076
REMARK 500 GLU B 120 CD GLU B 120 OE2 0.089
REMARK 500 GLU B 132 CD GLU B 132 OE2 0.089
REMARK 500 GLU B 139 CD GLU B 139 OE1 0.073
REMARK 500 LYS B 198 CD LYS B 198 CE 0.235
REMARK 500 LYS B 198 CE LYS B 198 NZ 0.171
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 24 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 36 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 36 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 PRO A 57 N - CA - CB ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 64 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 150 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 182 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP B 24 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP B 24 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP B 36 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP B 39 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG B 42 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP B 64 CB - CG - OD1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP B 64 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 81 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 81 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 93 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 93 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 118 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP B 150 CB - CG - OD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP B 164 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP B 175 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 182 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 182 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG B 201 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 8 -15.46 -29.77
REMARK 500 PRO A 38 -86.08 -75.15
REMARK 500 SER A 43 -82.31 -28.95
REMARK 500 GLN A 44 -69.89 -25.18
REMARK 500 LYS A 49 -34.08 -31.67
REMARK 500 PRO A 57 116.51 -32.60
REMARK 500 GLN A 71 111.19 73.19
REMARK 500 ASP A 118 34.45 -97.50
REMARK 500 LYS A 123 -74.64 -27.81
REMARK 500 PRO A 171 -14.96 -38.58
REMARK 500 LEU A 190 116.54 -17.75
REMARK 500 SER A 199 160.85 -45.60
REMARK 500 SER A 209 -138.18 -102.56
REMARK 500 LYS A 210 -107.02 -29.76
REMARK 500 LEU A 211 -59.59 -11.41
REMARK 500 ALA A 212 125.76 -20.06
REMARK 500 SER A 215 69.12 83.18
REMARK 500 ASN B 8 25.70 -72.77
REMARK 500 ASP B 55 -73.42 -51.36
REMARK 500 PRO B 57 131.48 -35.02
REMARK 500 GLN B 71 99.40 78.52
REMARK 500 ASP B 118 23.58 -74.35
REMARK 500 PHE B 119 -92.39 -36.60
REMARK 500 GLU B 120 -40.44 -18.36
REMARK 500 LYS B 123 -10.67 -48.49
REMARK 500 PRO B 171 -26.86 -38.34
REMARK 500 CYS B 173 -17.36 -42.70
REMARK 500 SER B 209 -145.50 -100.06
REMARK 500 SER B 215 72.82 82.44
REMARK 500 ASN B 216 31.85 -95.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AVA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR BINDING BOTH THE SUBSTRATE
REMARK 800 GLUTATHIONE AND XENOBIOTIC SUBSTRATE.
REMARK 800 SITE_IDENTIFIER: AVB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR BINDING BOTH THE SUBSTRATE
REMARK 800 GLUTATHIONE AND XENOBIOTIC SUBSTRATE.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR A 218
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR B 218
DBREF 3FYG A 1 217 UNP P04905 GSTM1_RAT 1 217
DBREF 3FYG B 1 217 UNP P04905 GSTM1_RAT 1 217
SEQADV 3FYG YOF A 6 UNP P04905 TYR 6 ENGINEERED
SEQADV 3FYG YOF A 22 UNP P04905 TYR 22 ENGINEERED
SEQADV 3FYG YOF A 27 UNP P04905 TYR 27 ENGINEERED
SEQADV 3FYG YOF A 32 UNP P04905 TYR 32 ENGINEERED
SEQADV 3FYG YOF A 40 UNP P04905 TYR 40 ENGINEERED
SEQADV 3FYG YOF A 61 UNP P04905 TYR 61 ENGINEERED
SEQADV 3FYG YOF A 78 UNP P04905 TYR 78 ENGINEERED
SEQADV 3FYG YOF A 137 UNP P04905 TYR 137 ENGINEERED
SEQADV 3FYG YOF A 154 UNP P04905 TYR 154 ENGINEERED
SEQADV 3FYG YOF A 160 UNP P04905 TYR 160 ENGINEERED
SEQADV 3FYG YOF A 166 UNP P04905 TYR 166 ENGINEERED
SEQADV 3FYG YOF A 196 UNP P04905 TYR 196 ENGINEERED
SEQADV 3FYG YOF A 202 UNP P04905 TYR 202 ENGINEERED
SEQADV 3FYG YOF B 6 UNP P04905 TYR 6 ENGINEERED
SEQADV 3FYG YOF B 22 UNP P04905 TYR 22 ENGINEERED
SEQADV 3FYG YOF B 27 UNP P04905 TYR 27 ENGINEERED
SEQADV 3FYG YOF B 32 UNP P04905 TYR 32 ENGINEERED
SEQADV 3FYG YOF B 40 UNP P04905 TYR 40 ENGINEERED
SEQADV 3FYG YOF B 61 UNP P04905 TYR 61 ENGINEERED
SEQADV 3FYG YOF B 78 UNP P04905 TYR 78 ENGINEERED
SEQADV 3FYG YOF B 137 UNP P04905 TYR 137 ENGINEERED
SEQADV 3FYG YOF B 154 UNP P04905 TYR 154 ENGINEERED
SEQADV 3FYG YOF B 160 UNP P04905 TYR 160 ENGINEERED
SEQADV 3FYG YOF B 166 UNP P04905 TYR 166 ENGINEERED
SEQADV 3FYG YOF B 196 UNP P04905 TYR 196 ENGINEERED
SEQADV 3FYG YOF B 202 UNP P04905 TYR 202 ENGINEERED
SEQRES 1 A 217 PRO MET ILE LEU GLY YOF TRP ASN VAL ARG GLY LEU THR
SEQRES 2 A 217 HIS PRO ILE ARG LEU LEU LEU GLU YOF THR ASP SER SER
SEQRES 3 A 217 YOF GLU GLU LYS ARG YOF ALA MET GLY ASP ALA PRO ASP
SEQRES 4 A 217 YOF ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 A 217 GLY LEU ASP PHE PRO ASN LEU PRO YOF LEU ILE ASP GLY
SEQRES 6 A 217 SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG YOF
SEQRES 7 A 217 LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU
SEQRES 8 A 217 GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET
SEQRES 9 A 217 ASP ASN ARG MET GLN LEU ILE MET LEU CYS TYR ASN PRO
SEQRES 10 A 217 ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE
SEQRES 11 A 217 PRO GLU LYS MET LYS LEU YOF SER GLU PHE LEU GLY LYS
SEQRES 12 A 217 ARG PRO TRP PHE ALA GLY ASP LYS VAL THR YOF VAL ASP
SEQRES 13 A 217 PHE LEU ALA YOF ASP ILE LEU ASP GLN YOF HIS ILE PHE
SEQRES 14 A 217 GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES 15 A 217 PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA
SEQRES 16 A 217 YOF MET LYS SER SER ARG YOF LEU SER THR PRO ILE PHE
SEQRES 17 A 217 SER LYS LEU ALA GLN TRP SER ASN LYS
SEQRES 1 B 217 PRO MET ILE LEU GLY YOF TRP ASN VAL ARG GLY LEU THR
SEQRES 2 B 217 HIS PRO ILE ARG LEU LEU LEU GLU YOF THR ASP SER SER
SEQRES 3 B 217 YOF GLU GLU LYS ARG YOF ALA MET GLY ASP ALA PRO ASP
SEQRES 4 B 217 YOF ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 B 217 GLY LEU ASP PHE PRO ASN LEU PRO YOF LEU ILE ASP GLY
SEQRES 6 B 217 SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG YOF
SEQRES 7 B 217 LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU
SEQRES 8 B 217 GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET
SEQRES 9 B 217 ASP ASN ARG MET GLN LEU ILE MET LEU CYS TYR ASN PRO
SEQRES 10 B 217 ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE
SEQRES 11 B 217 PRO GLU LYS MET LYS LEU YOF SER GLU PHE LEU GLY LYS
SEQRES 12 B 217 ARG PRO TRP PHE ALA GLY ASP LYS VAL THR YOF VAL ASP
SEQRES 13 B 217 PHE LEU ALA YOF ASP ILE LEU ASP GLN YOF HIS ILE PHE
SEQRES 14 B 217 GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES 15 B 217 PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA
SEQRES 16 B 217 YOF MET LYS SER SER ARG YOF LEU SER THR PRO ILE PHE
SEQRES 17 B 217 SER LYS LEU ALA GLN TRP SER ASN LYS
MODRES 3FYG YOF A 6 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 22 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 27 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 32 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 40 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 61 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 78 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 137 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 154 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 160 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 166 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 196 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF A 202 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 6 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 22 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 27 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 32 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 40 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 61 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 78 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 137 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 154 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 160 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 166 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 196 TYR 3-FLUOROTYROSINE
MODRES 3FYG YOF B 202 TYR 3-FLUOROTYROSINE
HET YOF A 6 13
HET YOF A 22 13
HET YOF A 27 13
HET YOF A 32 13
HET YOF A 40 13
HET YOF A 61 13
HET YOF A 78 13
HET YOF A 137 13
HET YOF A 154 18
HET YOF A 160 13
HET YOF A 166 13
HET YOF A 196 13
HET YOF A 202 13
HET YOF B 6 13
HET YOF B 22 13
HET YOF B 27 13
HET YOF B 32 13
HET YOF B 40 13
HET YOF B 61 13
HET YOF B 78 13
HET YOF B 137 13
HET YOF B 154 18
HET YOF B 160 13
HET YOF B 166 13
HET YOF B 196 13
HET YOF B 202 13
HET GPR A 218 35
HET GPR B 218 35
HETNAM YOF 3-FLUOROTYROSINE
HETNAM GPR (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-
HETNAM 2 GPR DIHYDROPHENANTHRENE
FORMUL 1 YOF 26(C9 H10 F N O3)
FORMUL 3 GPR 2(C24 H27 N3 O7 S)
FORMUL 5 HOH *431(H2 O)
HELIX 1 1 GLY A 11 LEU A 20 5 10
HELIX 2 2 SER A 43 GLU A 48 1 6
HELIX 3 3 SER A 72 ALA A 80 1 9
HELIX 4 4 GLU A 90 CYS A 114 1 25
HELIX 5 5 PHE A 119 GLU A 139 1 21
HELIX 6 6 LEU A 158 ILE A 162 5 5
HELIX 7 7 ASP A 164 ILE A 168 5 5
HELIX 8 8 PRO A 178 GLY A 189 1 12
HELIX 9 9 LYS A 191 LYS A 198 1 8
HELIX 10 10 GLY B 11 LEU B 20 5 10
HELIX 11 11 SER B 43 LEU B 46 1 4
HELIX 12 12 SER B 72 HIS B 83 1 12
HELIX 13 13 GLU B 90 CYS B 114 1 25
HELIX 14 14 PHE B 119 GLU B 125 1 7
HELIX 15 15 ILE B 130 GLU B 139 1 10
HELIX 16 16 LEU B 158 ILE B 162 5 5
HELIX 17 17 ASP B 164 ILE B 168 5 5
HELIX 18 18 PRO B 178 GLY B 189 1 12
HELIX 19 19 LYS B 191 LYS B 198 1 8
SHEET 1 A 2 ILE A 63 ASP A 64 0
SHEET 2 A 2 ARG A 67 LYS A 68 -1 O ARG A 67 N ASP A 64
SHEET 1 B 2 ILE B 63 ASP B 64 0
SHEET 2 B 2 ARG B 67 LYS B 68 -1 O ARG B 67 N ASP B 64
LINK N YOF A 6 C GLY A 5 1555 1555 1.31
LINK C YOF A 6 N TRP A 7 1555 1555 1.35
LINK N YOF A 22 C GLU A 21 1555 1555 1.31
LINK C YOF A 22 N THR A 23 1555 1555 1.28
LINK N YOF A 27 C SER A 26 1555 1555 1.29
LINK C YOF A 27 N GLU A 28 1555 1555 1.33
LINK N YOF A 32 C ARG A 31 1555 1555 1.34
LINK C YOF A 32 N ALA A 33 1555 1555 1.32
LINK N YOF A 40 C ASP A 39 1555 1555 1.34
LINK C YOF A 40 N ASP A 41 1555 1555 1.37
LINK N YOF A 61 C PRO A 60 1555 1555 1.32
LINK C YOF A 61 N LEU A 62 1555 1555 1.33
LINK N YOF A 78 C ARG A 77 1555 1555 1.31
LINK C YOF A 78 N LEU A 79 1555 1555 1.35
LINK N YOF A 137 C LEU A 136 1555 1555 1.35
LINK C YOF A 137 N SER A 138 1555 1555 1.35
LINK N YOF A 154 C THR A 153 1555 1555 1.34
LINK C YOF A 154 N VAL A 155 1555 1555 1.33
LINK N YOF A 160 C ALA A 159 1555 1555 1.33
LINK C YOF A 160 N ASP A 161 1555 1555 1.31
LINK N YOF A 166 C GLN A 165 1555 1555 1.33
LINK C YOF A 166 N HIS A 167 1555 1555 1.33
LINK N YOF A 196 C ALA A 195 1555 1555 1.31
LINK C YOF A 196 N MET A 197 1555 1555 1.35
LINK N YOF A 202 C ARG A 201 1555 1555 1.35
LINK C YOF A 202 N LEU A 203 1555 1555 1.36
LINK N YOF B 6 C GLY B 5 1555 1555 1.32
LINK C YOF B 6 N TRP B 7 1555 1555 1.30
LINK N YOF B 22 C GLU B 21 1555 1555 1.32
LINK C YOF B 22 N THR B 23 1555 1555 1.32
LINK N YOF B 27 C SER B 26 1555 1555 1.33
LINK C YOF B 27 N GLU B 28 1555 1555 1.31
LINK N YOF B 32 C ARG B 31 1555 1555 1.33
LINK C YOF B 32 N ALA B 33 1555 1555 1.31
LINK N YOF B 40 C ASP B 39 1555 1555 1.32
LINK C YOF B 40 N ASP B 41 1555 1555 1.33
LINK N YOF B 61 C PRO B 60 1555 1555 1.35
LINK C YOF B 61 N LEU B 62 1555 1555 1.30
LINK N YOF B 78 C ARG B 77 1555 1555 1.32
LINK C YOF B 78 N LEU B 79 1555 1555 1.33
LINK N YOF B 137 C LEU B 136 1555 1555 1.33
LINK C YOF B 137 N SER B 138 1555 1555 1.33
LINK N YOF B 154 C THR B 153 1555 1555 1.31
LINK C YOF B 154 N VAL B 155 1555 1555 1.34
LINK N YOF B 160 C ALA B 159 1555 1555 1.33
LINK C YOF B 160 N ASP B 161 1555 1555 1.32
LINK N YOF B 166 C GLN B 165 1555 1555 1.34
LINK C YOF B 166 N HIS B 167 1555 1555 1.30
LINK N YOF B 196 C ALA B 195 1555 1555 1.30
LINK C YOF B 196 N MET B 197 1555 1555 1.31
LINK N YOF B 202 C ARG B 201 1555 1555 1.33
LINK C YOF B 202 N LEU B 203 1555 1555 1.33
CISPEP 1 ALA A 37 PRO A 38 0 -1.34
CISPEP 2 LEU A 59 PRO A 60 0 4.34
CISPEP 3 THR A 205 PRO A 206 0 -2.64
CISPEP 4 ALA B 37 PRO B 38 0 0.64
CISPEP 5 LEU B 59 PRO B 60 0 1.07
CISPEP 6 THR B 205 PRO B 206 0 0.08
SITE 1 AVA 8 YOF A 6 TRP A 7 VAL A 9 LEU A 12
SITE 2 AVA 8 ILE A 111 TYR A 115 PHE A 208 SER A 209
SITE 1 AVB 8 YOF B 6 TRP B 7 VAL B 9 LEU B 12
SITE 2 AVB 8 ILE B 111 TYR B 115 PHE B 208 SER B 209
SITE 1 AC1 18 YOF A 6 TRP A 7 GLY A 11 LEU A 12
SITE 2 AC1 18 ARG A 42 TRP A 45 LYS A 49 ASN A 58
SITE 3 AC1 18 LEU A 59 GLN A 71 SER A 72 MET A 104
SITE 4 AC1 18 ILE A 207 HOH A 540 HOH A 704 HOH A 743
SITE 5 AC1 18 HOH A 945 ASP B 105
SITE 1 AC2 21 ASP A 105 YOF B 6 TRP B 7 GLY B 11
SITE 2 AC2 21 LEU B 12 ARG B 42 TRP B 45 LYS B 49
SITE 3 AC2 21 ASN B 58 LEU B 59 PRO B 60 GLN B 71
SITE 4 AC2 21 SER B 72 ILE B 111 ILE B 207 SER B 209
SITE 5 AC2 21 HOH B 522 HOH B 525 HOH B 694 HOH B 804
SITE 6 AC2 21 HOH B 816
CRYST1 85.430 88.420 57.260 90.00 90.00 90.00 P 21 21 2 8
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 0.011705 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017464 0.00000
MTRIX1 1 -0.282070 -0.747740 -0.601100 49.75153 1
MTRIX2 1 -0.754600 -0.214000 0.620310 29.32965 1
MTRIX3 1 -0.592470 0.628560 -0.503880 22.56671 1
(ATOM LINES ARE NOT SHOWN.)
END
