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PDBsum entry 6gst

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
6gst
Jmol
Contents
Protein chains
217 a.a. *
Ligands
GSH ×2
Waters ×420
* Residue conservation analysis
HEADER    TRANSFERASE                             26-JAN-96   6GST
TITLE     FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE
TITLE    2 SITE OF A CLASS MU GLUTATHIONE TRANSFERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MU CLASS GLUTATHIONE S-TRANSFERASE OF ISOENZYME 3-3;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: RAT GST;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE   3 ORGANISM_COMMON: BLACK RAT;
SOURCE   4 ORGANISM_TAXID: 10117;
SOURCE   5 ORGAN: LIVER;
SOURCE   6 GENE: CDNA INSERT OF CLONE PGT33MX;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: M5219;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGT33MX;
SOURCE  11 EXPRESSION_SYSTEM_GENE: CDNA INSERT OF CLONE PGT33MX
KEYWDS    GLUTATHIONE TRANSFERASE, ISOENZYME 3-3, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.XIAO,X.JI,R.N.ARMSTRONG,G.L.GILLILAND
REVDAT   3   07-DEC-11 6GST    1       FORMUL HETATM VERSN
REVDAT   2   24-FEB-09 6GST    1       VERSN
REVDAT   1   08-NOV-96 6GST    0
SPRSDE     08-NOV-96 6GST      1GST
JRNL        AUTH   G.XIAO,S.LIU,X.JI,W.W.JOHNSON,J.CHEN,J.F.PARSONS,
JRNL        AUTH 2 W.J.STEVENS,G.L.GILLILAND,R.N.ARMSTRONG
JRNL        TITL   FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE
JRNL        TITL 2 ACTIVE SITE OF A CLASS MU GLUTHATHIONE TRANSFERASE.
JRNL        REF    BIOCHEMISTRY                  V.  35  4753 1996
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   8664265
JRNL        DOI    10.1021/BI960189K
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   X.JI,W.W.JOHNSON,M.A.SESAY,L.DICKERT,S.M.PRASAD,H.L.AMMON,
REMARK   1  AUTH 2 R.N.ARMSTRONG,G.L.GILLILAND
REMARK   1  TITL   STRUCTURE AND FUNCTION OF THE XENOBIOTIC SUBSTRATE BINDING
REMARK   1  TITL 2 SITE OF A GLUTATHIONE S-TRANSFERASE AS REVEALED BY X-RAY
REMARK   1  TITL 3 CRYSTALLOGRAPHIC ANALYSIS OF PRODUCT COMPLEXES WITH THE
REMARK   1  TITL 4 DIASTEREOMERS OF
REMARK   1  TITL 5 9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE
REMARK   1  REF    BIOCHEMISTRY                  V.  33  1043 1994
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
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 SITE OF
REMARK   1  TITL 2 GLUTATHIONE S-TRANSFERASE. OBSERVATION OF AN ON-FACET
REMARK   1  TITL 3 HYDROGEN BOND BETWEEN THE SIDE CHAIN OF THREONINE 13 AND THE
REMARK   1  TITL 4 PI-CLOUD OF TYROSINE 6 AND ITS INFLUENCE ON CATALYSIS
REMARK   1  REF    J.AM.CHEM.SOC.                V. 115  7910 1993
REMARK   1  REFN                   ISSN 0002-7863
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 REACTION
REMARK   1  TITL 2 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,P.ZHANG,X.JI,W.W.JOHNSON,G.L.GILLILAND,R.N.ARMSTRONG
REMARK   1  TITL   CONTRIBUTION OF TYROSINE 6 TO THE CATALYTIC MECHANISM OF
REMARK   1  TITL 2 ISOENZYME 3-3 OF GLUTATHIONE S-TRANSFERASE
REMARK   1  REF    J.BIOL.CHEM.                  V. 267  4296 1992
REMARK   1  REFN                   ISSN 0021-9258
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 ANALYSIS OF
REMARK   1  TITL 3 THE BINARY COMPLEX OF ISOENZYME 3-3 AND GLUTATHIONE AT 2.2-A
REMARK   1  TITL 4 RESOLUTION
REMARK   1  REF    BIOCHEMISTRY                  V.  31 10169 1992
REMARK   1  REFN                   ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : GPRLSA
REMARK   3   AUTHORS     : FUREY
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.0
REMARK   3   NUMBER OF REFLECTIONS             : 19298
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.149
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  FIT/AGREEMENT OF MODEL WITH ALL DATA.
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            : 3636
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 40
REMARK   3   SOLVENT ATOMS            : 420
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.68
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.012 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.033 ; 0.036
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.032 ; 0.040
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.019 ; 0.030
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.189 ; 0.200
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.192 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.209 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.215 ; 0.300
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 3.700 ; 5.000
REMARK   3    STAGGERED                 (DEGREES) : 18.300; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : 18.200; 15.000
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.704 ; 1.000
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.229 ; 1.500
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.210 ; 1.500
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 1.926 ; 2.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 6GST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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        : 07-MAY-91
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : XENGEN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40404
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6
REMARK 200  DATA REDUNDANCY                : 3.550
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
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): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       44.12000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.72000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.12000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.72000
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: 3980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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    PHE A   140     NH2  ARG A   144              2.06
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   NH1  ARG B    67     NH1  ARG B    67     2555     2.04
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 B 100   CD    GLU B 100   OE1    -0.070
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  17   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ALA A  33   N   -  CA  -  CB  ANGL. DEV. =  -9.4 DEGREES
REMARK 500    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A  77   CD  -  NE  -  CZ  ANGL. DEV. =  13.8 DEGREES
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES
REMARK 500    GLU A  91   OE1 -  CD  -  OE2 ANGL. DEV. =   7.6 DEGREES
REMARK 500    GLU A  91   CG  -  CD  -  OE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500    ARG A  93   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG A  95   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    VAL A  99   CG1 -  CB  -  CG2 ANGL. DEV. = -10.5 DEGREES
REMARK 500    ARG A 107   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP A 118   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =  12.2 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ASP A 156   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP A 161   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD2 ANGL. DEV. =  -9.3 DEGREES
REMARK 500    ASP A 182   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ASP A 182   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ARG A 186   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ARG A 186   NE  -  CZ  -  NH1 ANGL. DEV. =  10.0 DEGREES
REMARK 500    ARG A 186   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    LEU A 211   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES
REMARK 500    MET B   2   CG  -  SD  -  CE  ANGL. DEV. =  -9.7 DEGREES
REMARK 500    VAL B   9   CA  -  CB  -  CG1 ANGL. DEV. =  12.6 DEGREES
REMARK 500    ARG B  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG B  17   CD  -  NE  -  CZ  ANGL. DEV. =  -8.6 DEGREES
REMARK 500    ARG B  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    TYR B  40   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    TYR B  40   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG B  42   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG B  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ASP B  55   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG B  67   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES
REMARK 500    ARG B  67   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES
REMARK 500    ARG B  67   NE  -  CZ  -  NH1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ARG B  77   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG B  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG B  81   NE  -  CZ  -  NH1 ANGL. DEV. =  13.7 DEGREES
REMARK 500    ARG B  81   NE  -  CZ  -  NH2 ANGL. DEV. = -10.0 DEGREES
REMARK 500    GLU B  90   CG  -  CD  -  OE1 ANGL. DEV. =  12.1 DEGREES
REMARK 500    ARG B  93   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG B  93   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG B  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG B  95   CG  -  CD  -  NE  ANGL. DEV. =  12.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      62 ANGLE DEVIATIONS.
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    TYR A  40       81.14     31.80
REMARK 500    GLN A  71      110.31     80.98
REMARK 500    ALA B  37      151.19    -46.43
REMARK 500    GLN B  71      110.78     76.42
REMARK 500    PRO B 124      -64.92    -27.27
REMARK 500    GLU B 170       81.73   -153.48
REMARK 500    ALA B 212     -178.95    -51.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  42         0.16    SIDE CHAIN
REMARK 500    ARG A 144         0.09    SIDE CHAIN
REMARK 500    ARG A 186         0.15    SIDE CHAIN
REMARK 500    ARG B  17         0.10    SIDE CHAIN
REMARK 500    ARG B 144         0.20    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    GLN A 165         10.71
REMARK 500    PRO A 178         12.14
REMARK 500    ASP B 161         11.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER A  72        24.9      L          L   OUTSIDE RANGE
REMARK 500    PHE A 177        23.9      L          L   OUTSIDE RANGE
REMARK 500    ASP B  39        24.3      L          L   OUTSIDE RANGE
REMARK 500    PHE B 147        21.8      L          L   OUTSIDE RANGE
REMARK 500    TRP B 214        24.9      L          L   OUTSIDE RANGE
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 334        DISTANCE =  8.86 ANGSTROMS
REMARK 525    HOH A 347        DISTANCE =  8.44 ANGSTROMS
REMARK 525    HOH A 393        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A 427        DISTANCE =  7.58 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 218
DBREF  6GST A    1   217  UNP    P04905   GSTM1_RAT        1    217
DBREF  6GST B    1   217  UNP    P04905   GSTM1_RAT        1    217
SEQRES   1 A  217  PRO MET ILE LEU GLY TYR TRP 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 TRP 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 TRP 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 TRP SER ASN LYS
SEQRES   1 B  217  PRO MET ILE LEU GLY TYR TRP 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 TRP 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 TRP 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 TRP SER ASN LYS
HET    GSH  A 218      20
HET    GSH  B 218      20
HETNAM     GSH GLUTATHIONE
FORMUL   3  GSH    2(C10 H17 N3 O6 S)
FORMUL   5  HOH   *420(H2 O)
HELIX    1   1 HIS A   14  TYR A   22  1                                   9
HELIX    2   2 SER A   43  LYS A   49  1                                   7
HELIX    3   3 SER A   72  LYS A   82  1                                  11
HELIX    4   4 GLU A   90  TYR A  115  1                                  26
HELIX    5   5 PHE A  119  PHE A  126  1                                   8
HELIX    6   6 ILE A  130  LEU A  141  1                                  12
HELIX    7   7 TYR A  154  PHE A  169  5                                  16
HELIX    8   8 PRO A  171  LEU A  174  5                                   4
HELIX    9   9 PRO A  178  GLU A  188  1                                  11
HELIX   10  10 LYS A  191  LYS A  198  1                                   8
HELIX   11  11 HIS B   14  TYR B   22  1                                   9
HELIX   12  12 SER B   43  LYS B   51  1                                   9
HELIX   13  13 SER B   72  LYS B   82  1                                  11
HELIX   14  14 GLU B   90  CYS B  114  1                                  25
HELIX   15  15 PHE B  119  LEU B  127  1                                   9
HELIX   16  16 ILE B  130  LEU B  141  1                                  12
HELIX   17  17 TYR B  154  PHE B  169  1                                  16
HELIX   18  18 PRO B  178  GLU B  188  1                                  11
HELIX   19  19 LYS B  191  LYS B  198  1                                   8
SHEET    1   A 4 TYR A  27  TYR A  32  0
SHEET    2   A 4 MET A   2  TRP A   7  1  N  MET A   2   O  GLU A  28
SHEET    3   A 4 TYR A  61  ASP A  64 -1  N  ILE A  63   O  ILE A   3
SHEET    4   A 4 ARG A  67  THR A  70 -1  N  ILE A  69   O  LEU A  62
SHEET    1   B 4 TYR B  27  TYR B  32  0
SHEET    2   B 4 MET B   2  TRP B   7  1  N  MET B   2   O  GLU B  28
SHEET    3   B 4 TYR B  61  ASP B  64 -1  N  ILE B  63   O  ILE B   3
SHEET    4   B 4 ARG B  67  THR B  70 -1  N  ILE B  69   O  LEU B  62
CISPEP   1 ALA A   37    PRO A   38          0         2.47
CISPEP   2 LEU A   59    PRO A   60          0         3.49
CISPEP   3 THR A  205    PRO A  206          0        -3.94
CISPEP   4 ALA B   37    PRO B   38          0         3.53
CISPEP   5 LEU B   59    PRO B   60          0        -3.38
CISPEP   6 THR B  205    PRO B  206          0         0.41
SITE     1 AC1 16 TYR A   6  TRP A   7  TRP A  45  LYS A  49
SITE     2 AC1 16 ASN A  58  LEU A  59  GLN A  71  SER A  72
SITE     3 AC1 16 ASP B 105  HOH A 221  HOH A 223  HOH A 239
SITE     4 AC1 16 HOH A 277  HOH A 351  HOH A 413  HOH A 414
SITE     1 AC2 18 ASP A 105  TYR B   6  TRP B   7  TRP B  45
SITE     2 AC2 18 LYS B  49  ASN B  58  LEU B  59  GLN B  71
SITE     3 AC2 18 SER B  72  HOH B 221  HOH B 222  HOH B 261
SITE     4 AC2 18 HOH B 266  HOH B 278  HOH B 307  HOH B 321
SITE     5 AC2 18 HOH B 353  HOH B 386
CRYST1   88.240   69.440   81.280  90.00 106.01  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      0.011333  0.000000  0.003252        0.00000
SCALE2      0.000000  0.014401  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012800        0.00000
MTRIX1   1  0.819290 -0.091670  0.566010       -6.58350    1
MTRIX2   1 -0.093400 -0.995290 -0.025990       31.56297    1
MTRIX3   1  0.565730 -0.031570 -0.823990       26.49589    1
      
PROCHECK
Go to PROCHECK summary
 References