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PDBsum entry 1pgt

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
1pgt
Jmol
Contents
Protein chain
210 a.a. *
Ligands
GTX ×2
EPE ×2
Waters ×326
* Residue conservation analysis
HEADER    TRANSFERASE                             17-FEB-97   1PGT
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-
TITLE    2 1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: GST, HGSTP1-1[V104];
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES;
COMPND   8 OTHER_DETAILS: HGSTP1-1[V104] AND HGSTP1-1[I104] ARE
COMPND   9 NATURALLY OCCURRING VARIANTS OF HGSTP1-1 OBTAINED BY SITE-
COMPND  10 DIRECTED MUTAGENESIS
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL_LINE: 293;
SOURCE   6 ORGAN: PLACENTA;
SOURCE   7 CELLULAR_LOCATION: CYTOPLASM;
SOURCE   8 GENE: GTP_HUMAN;
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS    TRANSFERASE, PI CLASS, HGSTP1-1[V104], DETOXIFICATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.JI
REVDAT   3   24-FEB-09 1PGT    1       VERSN
REVDAT   2   01-APR-03 1PGT    1       JRNL
REVDAT   1   04-SEP-97 1PGT    0
JRNL        AUTH   X.JI,M.TORDOVA,R.O'DONNELL,J.F.PARSONS,J.B.HAYDEN,
JRNL        AUTH 2 G.L.GILLILAND,P.ZIMNIAK
JRNL        TITL   STRUCTURE AND FUNCTION OF THE XENOBIOTIC
JRNL        TITL 2 SUBSTRATE-BINDING SITE AND LOCATION OF A POTENTIAL
JRNL        TITL 3 NON-SUBSTRATE-BINDING SITE IN A CLASS PI
JRNL        TITL 4 GLUTATHIONE S-TRANSFERASE.
JRNL        REF    BIOCHEMISTRY                  V.  36  9690 1997
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   9245401
JRNL        DOI    10.1021/BI970805S
REMARK   1
REMARK   1 REFERENCE 1
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 2
REMARK   1  AUTH   P.ZIMNIAK,B.NANDURI,S.PIKULA,J.BANDOROWICZ-PIKULA,
REMARK   1  AUTH 2 S.S.SINGHAL,S.K.SRIVASTAVA,S.AWASTHI,Y.C.AWASTHI
REMARK   1  TITL   NATURALLY OCCURRING HUMAN GLUTATHIONE
REMARK   1  TITL 2 S-TRANSFERASE GSTP1-1 ISOFORMS WITH ISOLEUCINE AND
REMARK   1  TITL 3 VALINE IN POSITION 104 DIFFER IN ENZYMIC PROPERTIES
REMARK   1  REF    EUR.J.BIOCHEM.                V. 224   893 1994
REMARK   1  REFN                   ISSN 0014-2956
REMARK   1 REFERENCE 3
REMARK   1  AUTH   P.REINEMER,H.W.DIRR,R.LADENSTEIN,R.HUBER,
REMARK   1  AUTH 2 M.LO BELLO,G.FEDERICI,M.W.PARKER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF CLASS PI
REMARK   1  TITL 2 GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN
REMARK   1  TITL 3 COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 A RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 227   214 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    1.80 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) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.0
REMARK   3   NUMBER OF REFLECTIONS             : 38224
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.182
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) : 0.2270
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) : 43132
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3282
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 82
REMARK   3   SOLVENT ATOMS            : 326
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.48
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.94
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) : 0.015 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.033 ; 0.036
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.071 ; 0.040
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.020 ; 0.030
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.199 ; 0.200
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.220 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.163 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.167 ; 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) : 6.300 ; 5.000
REMARK   3    STAGGERED                 (DEGREES) : 17.000; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : 19.000; 15.000
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.723 ; 1.000
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.169 ; 1.500
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.389 ; 1.500
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 2.034 ; 2.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: X-PLOR IS USED AT EARLY STAGE OF
REMARK   3  REFINEMENT. GPRLSA IS A MODIFIED VERSION OF PROLSQ BY FUREY,
REMARK   3  WANG AND SAX (J. APPL. CRYSTALLOGR.,1982,15,160-166). CROSS-
REMARK   3  VALIDATION INCLUDES GEOMETRY CHECK AND R FACTOR CALCULATION
REMARK   3  FOR ALL DATA.
REMARK   4
REMARK   4 1PGT 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        : MAR-96
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR571
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43132
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0
REMARK 200  DATA REDUNDANCY                : 4.200
REMARK 200  R MERGE                    (I) : 0.05700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.41
REMARK 200  R MERGE FOR SHELL          (I) : 0.30300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.810
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: PDB ENTRY 1GSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN IN HANGING
REMARK 280  DROPS WHICH INITIALLY CONSISTED OF 5.9 MG/ML PROTEIN IN 0.1 M
REMARK 280  HEPES BUFFER (PH 6.5) CONTAINING 8.3 MM S-HEXYLGLUTATHIONE AND
REMARK 280  1.0 M BUFFERED (PH 6.5) AMMONIUM SULFATE. THE DROPS WERE
REMARK 280  EQUILIBRATED AT 293 K AGAINST WELL SOLUTION CONTAINING BETWEEN
REMARK 280  1.9 - 2.0 M AMMONIUM SULFATE IN 0.1 M HEPES BUFFER (PH 6.5).,
REMARK 280  VAPOR DIFFUSION - HANGING DROP
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       39.69500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.40000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       39.69500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.40000
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: 4570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET B     0
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  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ASP A  59   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ARG A  74   CD  -  NE  -  CZ  ANGL. DEV. =  21.0 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   8.1 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    ASP A  94   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A 100   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    PHE A 150   CB  -  CG  -  CD1 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG A 186   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG B  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG B  70   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ARG B  70   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG B  74   CD  -  NE  -  CZ  ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG B  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ASP B  90   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG B 100   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B 186   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG B 186   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 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    GLN A  64      106.26     88.62
REMARK 500    ASN A 110       40.87   -158.55
REMARK 500    THR A 141     -114.96   -118.10
REMARK 500    GLU B  40      -72.43    -57.59
REMARK 500    GLN B  64      109.52     81.41
REMARK 500    ASN B 110       42.13   -155.74
REMARK 500    THR B 141     -118.24   -123.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX A 210
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 211
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 210
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 211
DBREF  1PGT A    0   209  UNP    P09211   GSTP1_HUMAN      1    210
DBREF  1PGT B    0   209  UNP    P09211   GSTP1_HUMAN      1    210
SEQRES   1 A  210  MET PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY
SEQRES   2 A  210  ARG CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY
SEQRES   3 A  210  GLN SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP
SEQRES   4 A  210  GLN GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN
SEQRES   5 A  210  LEU PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN
SEQRES   6 A  210  SER ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY
SEQRES   7 A  210  LEU TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP
SEQRES   8 A  210  MET VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR
SEQRES   9 A  210  VAL SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP
SEQRES  10 A  210  ASP TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE
SEQRES  11 A  210  GLU THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE
SEQRES  12 A  210  ILE VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU
SEQRES  13 A  210  LEU ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY
SEQRES  14 A  210  CYS LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY
SEQRES  15 A  210  ARG LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA
SEQRES  16 A  210  SER PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY
SEQRES  17 A  210  LYS GLN
SEQRES   1 B  210  MET PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY
SEQRES   2 B  210  ARG CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY
SEQRES   3 B  210  GLN SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP
SEQRES   4 B  210  GLN GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN
SEQRES   5 B  210  LEU PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN
SEQRES   6 B  210  SER ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY
SEQRES   7 B  210  LEU TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP
SEQRES   8 B  210  MET VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR
SEQRES   9 B  210  VAL SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP
SEQRES  10 B  210  ASP TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE
SEQRES  11 B  210  GLU THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE
SEQRES  12 B  210  ILE VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU
SEQRES  13 B  210  LEU ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY
SEQRES  14 B  210  CYS LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY
SEQRES  15 B  210  ARG LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA
SEQRES  16 B  210  SER PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY
SEQRES  17 B  210  LYS GLN
HET    GTX  A 210      26
HET    EPE  A 211      15
HET    GTX  B 210      26
HET    EPE  B 211      15
HETNAM     GTX S-HEXYLGLUTATHIONE
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN     EPE HEPES
FORMUL   3  GTX    2(C16 H30 N3 O6 S 1+)
FORMUL   4  EPE    2(C8 H18 N2 O4 S)
FORMUL   7  HOH   *326(H2 O)
HELIX    1   1 GLY A   12  ASP A   23  5                                  12
HELIX    2   2 VAL A   35  GLU A   40  1                                   6
HELIX    3   3 SER A   42  SER A   46  1                                   5
HELIX    4   4 SER A   65  LEU A   76  1                                  12
HELIX    5   5 GLN A   83  THR A  109  1                                  27
HELIX    6   6 TYR A  111  GLN A  135  1                                  25
HELIX    7   7 GLN A  137  GLY A  139  5                                   3
HELIX    8   8 PHE A  150  LEU A  165  1                                  16
HELIX    9   9 CYS A  169  ALA A  172  5                                   4
HELIX   10  10 PRO A  174  SER A  184  1                                  11
HELIX   11  11 PRO A  187  LEU A  193  1                                   7
HELIX   12  12 PRO A  196  VAL A  199  1                                   4
HELIX   13  13 GLY B   12  ASP B   23  5                                  12
HELIX   14  14 VAL B   35  GLU B   40  1                                   6
HELIX   15  15 SER B   42  SER B   46  1                                   5
HELIX   16  16 SER B   65  LEU B   76  1                                  12
HELIX   17  17 GLN B   83  THR B  109  1                                  27
HELIX   18  18 TYR B  111  SER B  134  1                                  24
HELIX   19  19 GLN B  137  GLY B  139  5                                   3
HELIX   20  20 PHE B  150  LEU B  165  1                                  16
HELIX   21  21 PRO B  174  SER B  184  1                                  11
HELIX   22  22 PRO B  187  ALA B  194  1                                   8
HELIX   23  23 PRO B  196  VAL B  199  1                                   4
SHEET    1   A 4 LYS A  29  VAL A  32  0
SHEET    2   A 4 TYR A   3  TYR A   7  1  N  VAL A   5   O  LYS A  29
SHEET    3   A 4 LYS A  54  ASP A  57 -1  N  GLN A  56   O  THR A   4
SHEET    4   A 4 LEU A  60  TYR A  63 -1  N  LEU A  62   O  PHE A  55
SHEET    1   B 4 TRP B  28  VAL B  32  0
SHEET    2   B 4 TYR B   3  TYR B   7  1  N  TYR B   3   O  LYS B  29
SHEET    3   B 4 LYS B  54  ASP B  57 -1  N  GLN B  56   O  THR B   4
SHEET    4   B 4 LEU B  60  TYR B  63 -1  N  LEU B  62   O  PHE B  55
CISPEP   1 LEU A   52    PRO A   53          0         6.91
CISPEP   2 LEU B   52    PRO B   53          0         2.89
SITE     1 AC1 19 TYR A   7  PHE A   8  ARG A  13  VAL A  35
SITE     2 AC1 19 TRP A  38  LYS A  44  GLN A  51  LEU A  52
SITE     3 AC1 19 PRO A  53  GLN A  64  SER A  65  TYR A 108
SITE     4 AC1 19 HOH A 602  HOH A 612  HOH A 697  HOH A 729
SITE     5 AC1 19 HOH A 819  HOH A 829  ASP B  98
SITE     1 AC2  7 ALA A  22  TRP A  28  LYS A  29  GLU A  30
SITE     2 AC2  7 GLU A 197  HOH A 680  ASP B 171
SITE     1 AC3 17 ASP A  98  TYR B   7  PHE B   8  ARG B  13
SITE     2 AC3 17 VAL B  35  TRP B  38  LYS B  44  GLY B  50
SITE     3 AC3 17 GLN B  51  LEU B  52  PRO B  53  GLN B  64
SITE     4 AC3 17 SER B  65  TYR B 108  HOH B 622  HOH B 698
SITE     5 AC3 17 HOH B 815
SITE     1 AC4  8 ASP A 171  ALA B  22  TRP B  28  LYS B  29
SITE     2 AC4  8 GLU B  30  GLU B 197  HOH B 717  HOH B 765
CRYST1   79.390   90.800   69.150  90.00  98.08  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      0.012596  0.000000  0.001788        0.00000
SCALE2      0.000000  0.011013  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014606        0.00000
MTRIX1   1  0.946070 -0.108441  0.305274       -4.44801    1
MTRIX2   1 -0.108718 -0.993941 -0.016148        1.30476    1
MTRIX3   1  0.305175 -0.017912 -0.952128       28.25868    1
      
PROCHECK
Go to PROCHECK summary
 References