HEADER TRANSFERASE 08-NOV-97 5FWG
TITLE TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE
COMPND 3 TRANSFERASE MU CLASS;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: RAT MU CLASS GST, RAT M1-1 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 3-3 (M1-1) ENZY;
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: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PSW1GST33;
SOURCE 13 EXPRESSION_SYSTEM_GENE: CDNA INSERT OF 3-3 (M1-1) ENZYME
KEYWDS GLUTATHIONE TRANSFERASE, UNNATURAL AMINO ACID, 5-
KEYWDS 2 FLUOROTRYPTOPHAN, THREE-DIMENSIONAL STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.PARSONS,G.XIAO,R.N.ARMSTRONG,G.L.GILLILAND
REVDAT 3 24-FEB-09 5FWG 1 VERSN
REVDAT 2 02-SEP-08 5FWG 1 JRNL
REVDAT 1 27-JAN-99 5FWG 0
JRNL AUTH J.F.PARSONS,G.XIAO,G.L.GILLILAND,R.N.ARMSTRONG
JRNL TITL ENZYMES HARBORING UNNATURAL AMINO ACIDS:
JRNL TITL 2 MECHANISTIC AND STRUCTURAL ANALYSIS OF THE
JRNL TITL 3 ENHANCED CATALYTIC ACTIVITY OF A GLUTATHIONE
JRNL TITL 4 TRANSFERASE CONTAINING 5-FLUOROTRYPTOPHAN.
JRNL REF BIOCHEMISTRY V. 37 6286 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9572843
JRNL DOI 10.1021/BI980219E
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.W.JOHNSON,S.LIU,X.JI,G.L.GILLILAND,R.N.ARMSTRONG
REMARK 1 TITL TYROSINE 115 PARTICIPATES BOTH IN CHEMICAL AND
REMARK 1 TITL 2 PHYSICAL STEPS OF THE CATALYTIC MECHANISM OF A
REMARK 1 TITL 3 GLUTATHIONE S-TRANSFERASE
REMARK 1 REF J.BIOL.CHEM. V. 268 11508 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
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 1 REFERENCE 3
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 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT V. 5-E, X-PLOR
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 28281
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) : 0.180
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 : 3644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 371
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 27.800
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.017 ; 0.800 ; 3856
REMARK 3 BOND ANGLES (DEGREES) : 3.000 ; 1.200 ; 5154
REMARK 3 TORSION ANGLES (DEGREES) : 19.530; 0.000 ; 2296
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.013 ; 1.500 ; 112
REMARK 3 GENERAL PLANES (A) : 0.016 ; 4.000 ; 534
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 7.089 ; 1.000 ; 3702
REMARK 3 NON-BONDED CONTACTS (A) : 0.023 ; 10.000; 154
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 : 71.40
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 5FWG 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 : 08-APR-97
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 7.6
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
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 : 184888
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 65.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 6.240
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.13700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR MODIFICATION
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 3GST
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.6
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 43.46950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.37350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.46950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.37350
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: 4760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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
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 B 828 O HOH B 828 2655 1.95
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 28 CD GLU A 28 OE2 0.068
REMARK 500 GLU A 29 CD GLU A 29 OE2 0.077
REMARK 500 GLU A 48 CD GLU A 48 OE2 0.069
REMARK 500 GLU A 88 CD GLU A 88 OE2 0.072
REMARK 500 GLU A 120 CD GLU A 120 OE2 0.084
REMARK 500 GLU A 125 CD GLU A 125 OE2 0.076
REMARK 500 GLU A 132 CD GLU A 132 OE2 0.079
REMARK 500 GLU A 139 CD GLU A 139 OE2 0.086
REMARK 500 GLU A 170 CD GLU A 170 OE2 0.083
REMARK 500 GLU B 21 CD GLU B 21 OE2 0.125
REMARK 500 GLU B 28 CD GLU B 28 OE2 0.067
REMARK 500 GLU B 48 CD GLU B 48 OE2 0.067
REMARK 500 GLU B 91 CD GLU B 91 OE2 0.069
REMARK 500 GLU B 125 CD GLU B 125 OE2 0.066
REMARK 500 GLU B 132 CD GLU B 132 OE2 0.077
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 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 24 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 36 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 36 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP A 39 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 39 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASN A 47 N - CA - CB ANGL. DEV. = 10.8 DEGREES
REMARK 500 ASP A 55 CB - CG - OD1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASP A 55 CB - CG - OD2 ANGL. DEV. = -15.0 DEGREES
REMARK 500 ARG A 67 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 95 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 97 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 97 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 105 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 105 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP A 150 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 156 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 156 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP A 175 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 182 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 182 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASN B 8 N - CA - CB ANGL. DEV. = -15.5 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 17 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 GLU B 21 CB - CG - CD ANGL. DEV. = 17.0 DEGREES
REMARK 500 ASP B 24 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP B 24 CB - CG - OD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 SER B 25 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO B 38 C - N - CD ANGL. DEV. = -14.3 DEGREES
REMARK 500 ASP B 39 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP B 41 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 THR B 70 N - CA - CB ANGL. DEV. = 12.3 DEGREES
REMARK 500 ASP B 97 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG B 107 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 118 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP B 118 CB - CG - OD2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP B 150 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 CYS B 173 CB - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP B 182 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 182 CB - CG - OD2 ANGL. DEV. = -7.8 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 ASP A 41 133.68 -37.24
REMARK 500 PRO A 57 130.35 -37.61
REMARK 500 ASN A 58 -178.46 -174.74
REMARK 500 GLN A 71 113.36 69.97
REMARK 500 CYS A 173 -8.80 -52.00
REMARK 500 LYS A 191 -53.37 -27.05
REMARK 500 ASP B 36 -146.90 -79.28
REMARK 500 TYR B 40 57.35 74.13
REMARK 500 ASP B 41 145.68 -30.63
REMARK 500 GLN B 71 108.56 82.93
REMARK 500 LYS B 123 -58.07 167.69
REMARK 500 CYS B 173 -34.88 -32.45
REMARK 500 LYS B 191 -80.54 -14.79
REMARK 500 ALA B 212 -140.99 -14.64
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 B 609 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B 716 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B 718 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH A 827 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH A 837 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH B 802 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH B 803 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH B 810 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH B 821 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 854 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH B 857 DISTANCE = 5.66 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: GPS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES.
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 5FWG A 1 217 UNP P04905 GSTM1_RAT 1 217
DBREF 5FWG B 1 217 UNP P04905 GSTM1_RAT 1 217
SEQADV 5FWG FTR A 7 UNP P04905 TRP 7 CONFLICT
SEQADV 5FWG FTR A 45 UNP P04905 TRP 45 CONFLICT
SEQADV 5FWG FTR A 146 UNP P04905 TRP 146 CONFLICT
SEQADV 5FWG FTR A 214 UNP P04905 TRP 214 CONFLICT
SEQADV 5FWG FTR B 7 UNP P04905 TRP 7 CONFLICT
SEQADV 5FWG FTR B 45 UNP P04905 TRP 45 CONFLICT
SEQADV 5FWG FTR B 146 UNP P04905 TRP 146 CONFLICT
SEQADV 5FWG FTR B 214 UNP P04905 TRP 214 CONFLICT
SEQRES 1 A 217 PRO MET ILE LEU GLY TYR FTR ASN VAL ARG GLY LEU THR
SEQRES 2 A 217 HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES 3 A 217 TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP
SEQRES 4 A 217 TYR ASP ARG SER GLN FTR LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 A 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES 6 A 217 SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR
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 TYR SER GLU PHE LEU GLY LYS
SEQRES 12 A 217 ARG PRO FTR PHE ALA GLY ASP LYS VAL THR TYR VAL ASP
SEQRES 13 A 217 PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR 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 TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE
SEQRES 17 A 217 SER LYS LEU ALA GLN FTR SER ASN LYS
SEQRES 1 B 217 PRO MET ILE LEU GLY TYR FTR ASN VAL ARG GLY LEU THR
SEQRES 2 B 217 HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES 3 B 217 TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP
SEQRES 4 B 217 TYR ASP ARG SER GLN FTR LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 B 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES 6 B 217 SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR
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 TYR SER GLU PHE LEU GLY LYS
SEQRES 12 B 217 ARG PRO FTR PHE ALA GLY ASP LYS VAL THR TYR VAL ASP
SEQRES 13 B 217 PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR 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 TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE
SEQRES 17 B 217 SER LYS LEU ALA GLN FTR SER ASN LYS
MODRES 5FWG FTR A 7 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR A 45 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR A 146 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR A 214 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR B 7 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR B 45 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR B 146 TRP FLUOROTRYPTOPHANE
MODRES 5FWG FTR B 214 TRP FLUOROTRYPTOPHANE
HET FTR A 7 15
HET FTR A 45 15
HET FTR A 146 15
HET FTR A 214 15
HET FTR B 7 15
HET FTR B 45 15
HET FTR B 146 15
HET FTR B 214 15
HET GPR A 218 35
HET GPR B 218 35
HETNAM FTR FLUOROTRYPTOPHANE
HETNAM GPR (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-
HETNAM 2 GPR DIHYDROPHENANTHRENE
FORMUL 1 FTR 8(C11 H11 F N2 O2)
FORMUL 3 GPR 2(C24 H27 N3 O7 S)
FORMUL 5 HOH *371(H2 O)
HELIX 1 H1A HIS A 14 TYR A 22 1 9
HELIX 2 H2A SER A 43 LEU A 46 1 4
HELIX 3 H3A SER A 72 LYS A 82 1 11
HELIX 4 H4A GLU A 90 CYS A 114 1 25
HELIX 5 H5A PHE A 119 LYS A 128 1 10
HELIX 6 H6A ILE A 130 LEU A 141 1 12
HELIX 7 H7A VAL A 155 PHE A 169 1 15
HELIX 8 H8A PRO A 178 GLU A 188 1 11
HELIX 9 H9A LYS A 191 TYR A 196 1 6
HELIX 10 H1B HIS B 14 TYR B 22 1 9
HELIX 11 H2B SER B 43 LEU B 46 1 4
HELIX 12 HA LYS B 49 LYS B 51 5 3
HELIX 13 H3B SER B 72 HIS B 83 1 12
HELIX 14 H4B GLU B 90 CYS B 114 1 25
HELIX 15 H5B PHE B 119 LYS B 128 1 10
HELIX 16 H6B ILE B 130 LEU B 141 1 12
HELIX 17 H7B TYR B 154 PHE B 169 1 16
HELIX 18 H8B PRO B 178 GLU B 188 1 11
HELIX 19 H9B LYS B 191 MET B 197 1 7
SHEET 1 S1A 4 TYR A 27 TYR A 32 0
SHEET 2 S1A 4 MET A 2 FTR A 7 1 O MET A 2 N GLU A 28
SHEET 3 S1A 4 TYR A 61 ASP A 64 -1 O ILE A 63 N ILE A 3
SHEET 4 S1A 4 ARG A 67 THR A 70 -1 O ARG A 67 N ASP A 64
SHEET 1 S1B 4 TYR B 27 TYR B 32 0
SHEET 2 S1B 4 MET B 2 FTR B 7 1 O MET B 2 N GLU B 28
SHEET 3 S1B 4 TYR B 61 ASP B 64 -1 O ILE B 63 N ILE B 3
SHEET 4 S1B 4 ARG B 67 THR B 70 -1 O ARG B 67 N ASP B 64
LINK N FTR A 7 C TYR A 6 1555 1555 1.31
LINK C FTR A 7 N ASN A 8 1555 1555 1.30
LINK N FTR A 45 C GLN A 44 1555 1555 1.30
LINK C FTR A 45 N LEU A 46 1555 1555 1.31
LINK N FTR A 146 C PRO A 145 1555 1555 1.36
LINK C FTR A 146 N PHE A 147 1555 1555 1.33
LINK N FTR A 214 C GLN A 213 1555 1555 1.34
LINK C FTR A 214 N SER A 215 1555 1555 1.33
LINK N FTR B 7 C TYR B 6 1555 1555 1.32
LINK C FTR B 7 N ASN B 8 1555 1555 1.32
LINK N FTR B 45 C GLN B 44 1555 1555 1.36
LINK C FTR B 45 N LEU B 46 1555 1555 1.34
LINK N FTR B 146 C PRO B 145 1555 1555 1.32
LINK C FTR B 146 N PHE B 147 1555 1555 1.33
LINK N FTR B 214 C GLN B 213 1555 1555 1.33
LINK C FTR B 214 N SER B 215 1555 1555 1.35
CISPEP 1 ALA A 37 PRO A 38 0 0.59
CISPEP 2 LEU A 59 PRO A 60 0 2.35
CISPEP 3 THR A 205 PRO A 206 0 1.82
CISPEP 4 ALA B 37 PRO B 38 0 -0.24
CISPEP 5 LEU B 59 PRO B 60 0 10.64
CISPEP 6 THR B 205 PRO B 206 0 -2.99
SITE 1 GPS 7 TYR A 6 FTR A 7 VAL A 9 LEU A 12
SITE 2 GPS 7 ILE A 111 TYR A 115 SER A 209
SITE 1 AC1 21 TYR A 6 FTR A 7 GLY A 11 LEU A 12
SITE 2 AC1 21 FTR A 45 LYS A 49 ASN A 58 LEU A 59
SITE 3 AC1 21 PRO A 60 GLN A 71 SER A 72 MET A 104
SITE 4 AC1 21 ILE A 111 SER A 209 HOH A 530 HOH A 627
SITE 5 AC1 21 HOH A 745 HOH A 759 HOH A 777 HOH A 779
SITE 6 AC1 21 ASP B 105
SITE 1 AC2 18 ASP A 105 TYR B 6 FTR B 7 LEU B 12
SITE 2 AC2 18 ARG B 42 FTR B 45 LYS B 49 ASN B 58
SITE 3 AC2 18 LEU B 59 PRO B 60 GLN B 71 SER B 72
SITE 4 AC2 18 ILE B 111 HOH B 526 HOH B 598 HOH B 637
SITE 5 AC2 18 HOH B 682 HOH B 813
CRYST1 86.939 68.747 80.539 90.00 105.08 90.00 C 1 2 1 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 0.011502 0.000000 0.003099 0.00000
SCALE2 0.000000 0.014546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012859 0.00000
MTRIX1 1 0.841869 -0.090312 0.532071 -6.46100 1
MTRIX2 1 -0.089096 -0.995629 -0.028023 31.39400 1
MTRIX3 1 0.532277 -0.023813 -0.846236 27.26000 1
(ATOM LINES ARE NOT SHOWN.)
END
