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PDBsum entry 1gnw

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
1gnw
Jmol
Contents
Protein chains
210 a.a. *
Ligands
GTX ×4
Waters ×660
* Residue conservation analysis
HEADER    TRANSFERASE                             15-SEP-96   1GNW
TITLE     STRUCTURE OF GLUTATHIONE S-TRANSFERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 2.5.1.18;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE   3 ORGANISM_COMMON: THALE CRESS;
SOURCE   4 ORGANISM_TAXID: 3702;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS    TRANSFERASE, HERBICIDE DETOXIFICATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.REINEMER,L.PRADE,P.HOF,T.NEUEFEIND,R.HUBER,K.PALME,
AUTHOR   2 H.D.BARTUNIK,B.BIESELER
REVDAT   2   24-FEB-09 1GNW    1       VERSN
REVDAT   1   17-SEP-97 1GNW    0
JRNL        AUTH   P.REINEMER,L.PRADE,P.HOF,T.NEUEFEIND,R.HUBER,
JRNL        AUTH 2 R.ZETTL,K.PALME,J.SCHELL,I.KOELLN,H.D.BARTUNIK,
JRNL        AUTH 3 B.BIESELER
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF GLUTATHIONE
JRNL        TITL 2 S-TRANSFERASE FROM ARABIDOPSIS THALIANA AT 2.2 A
JRNL        TITL 3 RESOLUTION: STRUCTURAL CHARACTERIZATION OF
JRNL        TITL 4 HERBICIDE-CONJUGATING PLANT GLUTATHIONE
JRNL        TITL 5 S-TRANSFERASES AND A NOVEL ACTIVE SITE
JRNL        TITL 6 ARCHITECTURE.
JRNL        REF    J.MOL.BIOL.                   V. 255   289 1996
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   8551521
JRNL        DOI    10.1006/JMBI.1996.0024
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 21738
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 SET) : 0.175
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   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3490
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 26
REMARK   3   SOLVENT ATOMS            : 220
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.50
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) : 0.19
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.77
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.700 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1GNW 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        : 1994
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          : ENRAF-NONIUS FAST
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23438
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : 0.09400
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/2
REMARK 290       6555   X-Y,X,Z+1/2
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        0.00000
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        0.00000
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       34.98000
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       34.98000
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       34.98000
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: 5860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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     ALA A     1
REMARK 465     ALA B     1
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    LEU B  64   CA  -  CB  -  CG  ANGL. DEV. =  14.8 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    GLU A  66      103.80     80.69
REMARK 500    ASP A  89       79.80   -108.34
REMARK 500    GLU B  66      103.57     77.59
REMARK 500    GLN B  81      144.82   -173.27
REMARK 500    PRO B 183        0.37    -68.58
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 227        DISTANCE =  6.18 ANGSTROMS
REMARK 525    HOH A 258        DISTANCE =  6.40 ANGSTROMS
REMARK 525    HOH A 284        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A 291        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A 312        DISTANCE =  5.92 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C SSEQI
REMARK 615     HOH B  310
REMARK 615     HOH B  311
REMARK 615     HOH B  312
REMARK 615     HOH B  313
REMARK 615     HOH B  314
REMARK 615     HOH B  315
REMARK 615     HOH B  316
REMARK 615     HOH B  317
REMARK 615     HOH B  318
REMARK 615     HOH B  319
REMARK 615     HOH B  320
REMARK 615     HOH B  321
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 212
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX A 213
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 212
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 213
DBREF  1GNW A    1   211  UNP    P46422   GSTF4_ARATH      1    211
DBREF  1GNW B    1   211  UNP    P46422   GSTF4_ARATH      1    211
SEQRES   1 A  211  ALA GLY ILE LYS VAL PHE GLY HIS PRO ALA SER ILE ALA
SEQRES   2 A  211  THR ARG ARG VAL LEU ILE ALA LEU HIS GLU LYS ASN LEU
SEQRES   3 A  211  ASP PHE GLU LEU VAL HIS VAL GLU LEU LYS ASP GLY GLU
SEQRES   4 A  211  HIS LYS LYS GLU PRO PHE LEU SER ARG ASN PRO PHE GLY
SEQRES   5 A  211  GLN VAL PRO ALA PHE GLU ASP GLY ASP LEU LYS LEU PHE
SEQRES   6 A  211  GLU SER ARG ALA ILE THR GLN TYR ILE ALA HIS ARG TYR
SEQRES   7 A  211  GLU ASN GLN GLY THR ASN LEU LEU GLN THR ASP SER LYS
SEQRES   8 A  211  ASN ILE SER GLN TYR ALA ILE MET ALA ILE GLY MET GLN
SEQRES   9 A  211  VAL GLU ASP HIS GLN PHE ASP PRO VAL ALA SER LYS LEU
SEQRES  10 A  211  ALA PHE GLU GLN ILE PHE LYS SER ILE TYR GLY LEU THR
SEQRES  11 A  211  THR ASP GLU ALA VAL VAL ALA GLU GLU GLU ALA LYS LEU
SEQRES  12 A  211  ALA LYS VAL LEU ASP VAL TYR GLU ALA ARG LEU LYS GLU
SEQRES  13 A  211  PHE LYS TYR LEU ALA GLY GLU THR PHE THR LEU THR ASP
SEQRES  14 A  211  LEU HIS HIS ILE PRO ALA ILE GLN TYR LEU LEU GLY THR
SEQRES  15 A  211  PRO THR LYS LYS LEU PHE THR GLU ARG PRO ARG VAL ASN
SEQRES  16 A  211  GLU TRP VAL ALA GLU ILE THR LYS ARG PRO ALA SER GLU
SEQRES  17 A  211  LYS VAL GLN
SEQRES   1 B  211  ALA GLY ILE LYS VAL PHE GLY HIS PRO ALA SER ILE ALA
SEQRES   2 B  211  THR ARG ARG VAL LEU ILE ALA LEU HIS GLU LYS ASN LEU
SEQRES   3 B  211  ASP PHE GLU LEU VAL HIS VAL GLU LEU LYS ASP GLY GLU
SEQRES   4 B  211  HIS LYS LYS GLU PRO PHE LEU SER ARG ASN PRO PHE GLY
SEQRES   5 B  211  GLN VAL PRO ALA PHE GLU ASP GLY ASP LEU LYS LEU PHE
SEQRES   6 B  211  GLU SER ARG ALA ILE THR GLN TYR ILE ALA HIS ARG TYR
SEQRES   7 B  211  GLU ASN GLN GLY THR ASN LEU LEU GLN THR ASP SER LYS
SEQRES   8 B  211  ASN ILE SER GLN TYR ALA ILE MET ALA ILE GLY MET GLN
SEQRES   9 B  211  VAL GLU ASP HIS GLN PHE ASP PRO VAL ALA SER LYS LEU
SEQRES  10 B  211  ALA PHE GLU GLN ILE PHE LYS SER ILE TYR GLY LEU THR
SEQRES  11 B  211  THR ASP GLU ALA VAL VAL ALA GLU GLU GLU ALA LYS LEU
SEQRES  12 B  211  ALA LYS VAL LEU ASP VAL TYR GLU ALA ARG LEU LYS GLU
SEQRES  13 B  211  PHE LYS TYR LEU ALA GLY GLU THR PHE THR LEU THR ASP
SEQRES  14 B  211  LEU HIS HIS ILE PRO ALA ILE GLN TYR LEU LEU GLY THR
SEQRES  15 B  211  PRO THR LYS LYS LEU PHE THR GLU ARG PRO ARG VAL ASN
SEQRES  16 B  211  GLU TRP VAL ALA GLU ILE THR LYS ARG PRO ALA SER GLU
SEQRES  17 B  211  LYS VAL GLN
HET    GTX  A 212      31
HET    GTX  A 213      31
HET    GTX  B 212      31
HET    GTX  B 213      31
HETNAM     GTX S-HEXYLGLUTATHIONE
FORMUL   3  GTX    4(C16 H30 N3 O6 S 1+)
FORMUL   7  HOH   *220(H2 O)
HELIX    1   1 ILE A   12  GLU A   23  1                                  12
HELIX    2   2 LEU A   35  ASP A   37  5                                   3
HELIX    3   3 GLU A   39  LYS A   41  5                                   3
HELIX    4   4 PHE A   45  ARG A   48  1                                   4
HELIX    5   5 SER A   67  ARG A   77  1                                  11
HELIX    6   6 ILE A   93  HIS A  108  1                                  16
HELIX    7   7 ASP A  111  GLN A  121  1                                  11
HELIX    8   8 PHE A  123  TYR A  127  1                                   5
HELIX    9   9 GLU A  133  LEU A  154  1                                  22
HELIX   10  10 LEU A  167  GLY A  181  1                                  15
HELIX   11  11 PRO A  183  THR A  189  5                                   7
HELIX   12  12 PRO A  192  THR A  202  1                                  11
HELIX   13  13 PRO A  205  VAL A  210  1                                   6
HELIX   14  14 ILE B   12  LYS B   24  1                                  13
HELIX   15  15 LEU B   35  ASP B   37  5                                   3
HELIX   16  16 GLU B   39  LYS B   41  5                                   3
HELIX   17  17 PHE B   45  SER B   47  5                                   3
HELIX   18  18 SER B   67  ARG B   77  1                                  11
HELIX   19  19 ILE B   93  HIS B  108  1                                  16
HELIX   20  20 ASP B  111  GLN B  121  1                                  11
HELIX   21  21 PHE B  123  TYR B  127  1                                   5
HELIX   22  22 GLU B  133  GLU B  156  1                                  24
HELIX   23  23 LEU B  167  GLY B  181  1                                  15
HELIX   24  24 PRO B  183  THR B  189  5                                   7
HELIX   25  25 PRO B  192  THR B  202  1                                  11
HELIX   26  26 PRO B  205  GLU B  208  1                                   4
SHEET    1   A 4 GLU A  29  HIS A  32  0
SHEET    2   A 4 ILE A   3  GLY A   7  1  N  VAL A   5   O  GLU A  29
SHEET    3   A 4 ALA A  56  ASP A  59 -1  N  GLU A  58   O  LYS A   4
SHEET    4   A 4 LEU A  62  PHE A  65 -1  N  LEU A  64   O  PHE A  57
SHEET    1   B 4 GLU B  29  HIS B  32  0
SHEET    2   B 4 ILE B   3  GLY B   7  1  N  VAL B   5   O  GLU B  29
SHEET    3   B 4 ALA B  56  ASP B  59 -1  N  GLU B  58   O  LYS B   4
SHEET    4   B 4 LEU B  62  PHE B  65 -1  N  LEU B  64   O  PHE B  57
CISPEP   1 GLU A   43    PRO A   44          0        -0.02
CISPEP   2 VAL A   54    PRO A   55          0         0.20
CISPEP   3 GLU B   43    PRO B   44          0         0.24
CISPEP   4 VAL B   54    PRO B   55          0         0.47
SITE     1 AC1 15 LEU A  35  HIS A  40  LYS A  41  GLN A  53
SITE     2 AC1 15 VAL A  54  PRO A  55  GLU A  66  SER A  67
SITE     3 AC1 15 ARG A  68  GTX A 213  HOH A 219  HOH A 229
SITE     4 AC1 15 HOH A 235  HOH A 288  HIS B 108
SITE     1 AC2  8 SER A  11  ILE A  12  ALA A  13  GLN A  53
SITE     2 AC2  8 GTX A 212  HOH A 288  HOH A 304  HOH A 305
SITE     1 AC3 14 HIS A 108  HOH A 259  ALA B  13  LEU B  35
SITE     2 AC3 14 LYS B  41  GLN B  53  VAL B  54  GLU B  66
SITE     3 AC3 14 SER B  67  ARG B  68  GTX B 213  HOH B 217
SITE     4 AC3 14 HOH B 224  HOH B 238
SITE     1 AC4  5 SER B  11  ILE B  12  ALA B  13  ILE B 122
SITE     2 AC4  5 GTX B 212
CRYST1  113.300  113.300   69.960  90.00  90.00 120.00 P 63         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      0.008826  0.005096  0.000000        0.00000
SCALE2      0.000000  0.010192  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014294        0.00000
      
PROCHECK
Go to PROCHECK summary
 References