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PDBsum entry 3qag

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Transferase PDB id
3qag
Jmol
Contents
Protein chain
238 a.a.
Ligands
GSH
PEG ×2
EDO
Waters ×97
HEADER    TRANSFERASE                             11-JAN-11   3QAG
TITLE     HUMAN GLUTATHIONE TRANSFERASE O2 WITH GLUTATHIONE -NEW CRYSTAL FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE OMEGA-2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: GSTO-2;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: GSTO2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15/REP4;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS    GLUTATHIONE TRANSFERASE, GST, DEHYDROASCORBATE REDUCTASE,
KEYWDS   2 TRANSFERASE, REDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.ZHOU,P.G.BOARD,A.J.OAKLEY
REVDAT   4   26-JUN-13 3QAG    1       JRNL
REVDAT   3   16-MAY-12 3QAG    1       JRNL
REVDAT   2   08-FEB-12 3QAG    1       LINK
REVDAT   1   11-JAN-12 3QAG    0
JRNL        AUTH   H.ZHOU,J.BROCK,D.LIU,P.G.BOARD,A.J.OAKLEY
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE DEHYDROASCORBATE REDUCTASE
JRNL        TITL 2 ACTIVITY OF HUMAN OMEGA-CLASS GLUTATHIONE TRANSFERASES.
JRNL        REF    J.MOL.BIOL.                   V. 420   190 2012
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   22522127
JRNL        DOI    10.1016/J.JMB.2012.04.014
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6
REMARK   3   NUMBER OF REFLECTIONS             : 19842
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.265
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 1081
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1428
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.54
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1990
REMARK   3   BIN FREE R VALUE SET COUNT          : 77
REMARK   3   BIN FREE R VALUE                    : 0.2380
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1950
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 38
REMARK   3   SOLVENT ATOMS            : 97
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.02000
REMARK   3    B22 (A**2) : 0.02000
REMARK   3    B33 (A**2) : -0.03000
REMARK   3    B12 (A**2) : 0.01000
REMARK   3    B13 (A**2) : -0.00000
REMARK   3    B23 (A**2) : -0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.005
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2062 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2795 ; 1.180 ; 1.977
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   243 ; 5.542 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    97 ;35.552 ;23.093
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   343 ;14.517 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;18.638 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   297 ; 0.083 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1579 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1203 ; 0.448 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1958 ; 0.833 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   859 ; 1.437 ; 3.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   834 ; 2.375 ; 4.500
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     2        A   239
REMARK   3    RESIDUE RANGE :   A  1001        A  1004
REMARK   3    RESIDUE RANGE :   A   240        A   336
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3950  21.7460  14.2163
REMARK   3    T TENSOR
REMARK   3      T11:   0.0556 T22:   0.0029
REMARK   3      T33:   0.0560 T12:   0.0107
REMARK   3      T13:   0.0247 T23:   0.0090
REMARK   3    L TENSOR
REMARK   3      L11:   1.8964 L22:   1.8344
REMARK   3      L33:   2.5807 L12:   0.8428
REMARK   3      L13:   0.3937 L23:   0.0427
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0490 S12:   0.0013 S13:   0.0246
REMARK   3      S21:  -0.1011 S22:  -0.0163 S23:   0.0821
REMARK   3      S31:   0.0265 S32:   0.0384 S33:   0.0653
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3QAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON
REMARK 200  BEAMLINE                       : MX1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954448
REMARK 200  MONOCHROMATOR                  : DOUBLE SI WITH SAGITTALY BENT
REMARK 200                                   SECOND CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19843
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.08400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.9000
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) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.34600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3Q18
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 2% V/V POLYETHYLENE
REMARK 280  GLYCOL 400, 2M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
REMARK 290       7555   Y,X,-Z+2/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+1/3
REMARK 290      10555   -Y,-X,-Z+1/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      234.93333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      117.46667
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      176.20000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.73333
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      293.66667
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      234.93333
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      117.46667
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       58.73333
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      176.20000
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      293.66667
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: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.500000 -0.866025  0.000000       26.56900
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       46.01886
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       58.73333
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 A     1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A  85      120.05     78.59
REMARK 500    SER A 140       49.78    -69.47
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    TRP A 179        24.3      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 283        DISTANCE =  5.72 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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q18   RELATED DB: PDB
REMARK 900 GSTO2
REMARK 900 RELATED ID: 3Q19   RELATED DB: PDB
REMARK 900 GSTO2 WITH GSH
REMARK 900 RELATED ID: 1EEM   RELATED DB: PDB
REMARK 900 GSTO1
DBREF  3QAG A    1   239  UNP    Q9H4Y5   GSTO2_HUMAN      1    243
SEQADV 3QAG SER A   80  UNP  Q9H4Y5    CYS    80 ENGINEERED MUTATION
SEQADV 3QAG SER A  121  UNP  Q9H4Y5    CYS   121 ENGINEERED MUTATION
SEQADV 3QAG SER A  136  UNP  Q9H4Y5    CYS   136 ENGINEERED MUTATION
SEQADV 3QAG SER A  140  UNP  Q9H4Y5    CYS   140 ENGINEERED MUTATION
SEQADV 3QAG SER A  170  UNP  Q9H4Y5    CYS   170 ENGINEERED MUTATION
SEQADV 3QAG SER A  214  UNP  Q9H4Y5    CYS   214 ENGINEERED MUTATION
SEQADV 3QAG     A       UNP  Q9H4Y5    PHE   240 DELETION
SEQADV 3QAG     A       UNP  Q9H4Y5    GLY   241 DELETION
SEQADV 3QAG     A       UNP  Q9H4Y5    LEU   242 DELETION
SEQADV 3QAG     A       UNP  Q9H4Y5    CYS   243 DELETION
SEQRES   1 A  239  MET SER GLY ASP ALA THR ARG THR LEU GLY LYS GLY SER
SEQRES   2 A  239  GLN PRO PRO GLY PRO VAL PRO GLU GLY LEU ILE ARG ILE
SEQRES   3 A  239  TYR SER MET ARG PHE CYS PRO TYR SER HIS ARG THR ARG
SEQRES   4 A  239  LEU VAL LEU LYS ALA LYS ASP ILE ARG HIS GLU VAL VAL
SEQRES   5 A  239  ASN ILE ASN LEU ARG ASN LYS PRO GLU TRP TYR TYR THR
SEQRES   6 A  239  LYS HIS PRO PHE GLY HIS ILE PRO VAL LEU GLU THR SER
SEQRES   7 A  239  GLN SER GLN LEU ILE TYR GLU SER VAL ILE ALA CYS GLU
SEQRES   8 A  239  TYR LEU ASP ASP ALA TYR PRO GLY ARG LYS LEU PHE PRO
SEQRES   9 A  239  TYR ASP PRO TYR GLU ARG ALA ARG GLN LYS MET LEU LEU
SEQRES  10 A  239  GLU LEU PHE SER LYS VAL PRO HIS LEU THR LYS GLU CYS
SEQRES  11 A  239  LEU VAL ALA LEU ARG SER GLY ARG GLU SER THR ASN LEU
SEQRES  12 A  239  LYS ALA ALA LEU ARG GLN GLU PHE SER ASN LEU GLU GLU
SEQRES  13 A  239  ILE LEU GLU TYR GLN ASN THR THR PHE PHE GLY GLY THR
SEQRES  14 A  239  SER ILE SER MET ILE ASP TYR LEU LEU TRP PRO TRP PHE
SEQRES  15 A  239  GLU ARG LEU ASP VAL TYR GLY ILE LEU ASP CYS VAL SER
SEQRES  16 A  239  HIS THR PRO ALA LEU ARG LEU TRP ILE SER ALA MET LYS
SEQRES  17 A  239  TRP ASP PRO THR VAL SER ALA LEU LEU MET ASP LYS SER
SEQRES  18 A  239  ILE PHE GLN GLY PHE LEU ASN LEU TYR PHE GLN ASN ASN
SEQRES  19 A  239  PRO ASN ALA PHE ASP
HET    GSH  A1001      20
HET    PEG  A1002       7
HET    PEG  A1003       7
HET    EDO  A1004       4
HETNAM     GSH GLUTATHIONE
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   2  GSH    C10 H17 N3 O6 S
FORMUL   3  PEG    2(C4 H10 O3)
FORMUL   5  EDO    C2 H6 O2
FORMUL   6  HOH   *97(H2 O)
HELIX    1   1 CYS A   32  LYS A   45  1                                  14
HELIX    2   2 PRO A   60  LYS A   66  5                                   7
HELIX    3   3 GLU A   85  TYR A   97  1                                  13
HELIX    4   4 ASP A  106  PHE A  120  1                                  15
HELIX    5   5 LYS A  122  ARG A  135  1                                  14
HELIX    6   6 SER A  140  ASN A  162  1                                  23
HELIX    7   7 SER A  172  GLY A  189  1                                  18
HELIX    8   8 ILE A  190  SER A  195  5                                   6
HELIX    9   9 THR A  197  TRP A  209  1                                  13
HELIX   10  10 ASP A  210  LEU A  217  1                                   8
HELIX   11  11 ASP A  219  GLN A  232  1                                  14
HELIX   12  12 ASN A  233  ASP A  239  5                                   7
SHEET    1   A 4 HIS A  49  ASN A  53  0
SHEET    2   A 4 ILE A  24  SER A  28  1  N  ILE A  26   O  VAL A  52
SHEET    3   A 4 VAL A  74  GLU A  76 -1  O  GLU A  76   N  ARG A  25
SHEET    4   A 4 LEU A  82  TYR A  84 -1  O  ILE A  83   N  LEU A  75
LINK         SG  CYS A  32                 SG2 GSH A1001     1555   1555  2.06
CISPEP   1 ILE A   72    PRO A   73          0         1.59
SITE     1 AC1 11 CYS A  32  TYR A  34  LYS A  59  HIS A  71
SITE     2 AC1 11 ILE A  72  PRO A  73  GLU A  85  SER A  86
SITE     3 AC1 11 HOH A 249  HOH A 308  HOH A 327
SITE     1 AC2  5 LYS A 101  LEU A 102  PHE A 103  GLY A 167
SITE     2 AC2  5 SER A 172
SITE     1 AC3  1 TRP A 209
CRYST1   53.138   53.138  352.400  90.00  90.00 120.00 P 65 2 2     12
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      0.018819  0.010865  0.000000        0.00000
SCALE2      0.000000  0.021730  0.000000        0.00000
SCALE3      0.000000  0.000000  0.002838        0.00000
      
PROCHECK
Go to PROCHECK summary
 References