spacer
spacer

PDBsum entry 2gsq

Go to PDB code: 
Top Page protein ligands links
Transferase PDB id
2gsq
Jmol
Contents
Protein chain
202 a.a.
Ligands
SO4
GBI ×2
Waters ×211
HEADER    TRANSFERASE                             14-APR-95   2GSQ
TITLE     GLUTATHIONE S-TRANSFERASE FROM SQUID DIGESTIVE GLAND COMPLEXED WITH S-
TITLE    2 (3-IODOBENZYL)GLUTATHIONE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: SQUID GST;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OMMASTREPHES SLOANI;
SOURCE   3 ORGANISM_COMMON: SLOANE'S SQUID;
SOURCE   4 ORGANISM_TAXID: 6633;
SOURCE   5 ORGAN: DIGESTIVE GLAND;
SOURCE   6 GENE: CDNA INSERT OF CLONE PGST5;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: GST5/PET;
SOURCE  11 EXPRESSION_SYSTEM_GENE: CDNA INSERT OF CLONE PGST5
KEYWDS    SQUID DIGESTIVE GLAND, SIGMA CLASS, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.JI,R.N.ARMSTRONG,G.L.GILLILAND
REVDAT   3   13-JUL-11 2GSQ    1       VERSN
REVDAT   2   24-FEB-09 2GSQ    1       VERSN
REVDAT   1   12-APR-96 2GSQ    0
JRNL        AUTH   X.JI,E.C.VON ROSENVINGE,W.W.JOHNSON,R.N.ARMSTRONG,
JRNL        AUTH 2 G.L.GILLILAND
JRNL        TITL   LOCATION OF A POTENTIAL TRANSPORT BINDING SITE IN A SIGMA
JRNL        TITL 2 CLASS GLUTATHIONE TRANSFERASE BY X-RAY CRYSTALLOGRAPHY.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  93  8208 1996
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   8710848
JRNL        DOI    10.1073/PNAS.93.16.8208
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   X.JI,E.C.VON ROSENVINGE,W.W.JOHNSON,S.I.TOMAREV,
REMARK   1  AUTH 2 J.PIATIGORSKY,R.N.ARMSTRONG,G.L.GILLILAND
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE, CATALYTIC PROPERTIES AND
REMARK   1  TITL 2 EVOLUTION OF A SIGMA CLASS GLUTATHIONE TRANSFERASE FROM
REMARK   1  TITL 3 SQUID, A PROGENITOR OF THE LENS-CRYSTALLINS OF CEPHALOPODS
REMARK   1  REF    BIOCHEMISTRY                  V.  34  5317 1995
REMARK   1  REFN                   ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
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)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 11649
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) : 0.173
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  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            : 1598
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 61
REMARK   3   SOLVENT ATOMS            : 211
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.12
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) : 0.017 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.037 ; 0.036
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.037 ; 0.040
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.023 ; 0.030
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.214 ; 0.200
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.198 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.210 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : 0.190 ; 0.300
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 4.000 ; 5.000
REMARK   3    STAGGERED                 (DEGREES) : 22.800; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.708 ; 1.000
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.198 ; 1.500
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.294 ; 1.500
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 1.964 ; 2.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2GSQ 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        : 29-MAY-94
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) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : ELECTRONICS COMPUTING
REMARK 200                                   TECHNOLOGIES
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15331
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 3.100
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   (%): 61.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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       31.62667
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       63.25333
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       63.25333
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       31.62667
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
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 A  10   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG A  18   CD  -  NE  -  CZ  ANGL. DEV. =  11.6 DEGREES
REMARK 500    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    MET A  50   CG  -  SD  -  CE  ANGL. DEV. = -11.3 DEGREES
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ASP A  77   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    GLU A  92   OE1 -  CD  -  OE2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    GLU A  92   CG  -  CD  -  OE2 ANGL. DEV. = -12.4 DEGREES
REMARK 500    ASP A  96   CB  -  CG  -  OD1 ANGL. DEV. =  10.7 DEGREES
REMARK 500    ALA A 110   CB  -  CA  -  C   ANGL. DEV. =   9.6 DEGREES
REMARK 500    ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    VAL A 162   CA  -  CB  -  CG1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    LYS A 172   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES
REMARK 500    ARG A 183   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES
REMARK 500    ARG A 183   CD  -  NE  -  CZ  ANGL. DEV. =  10.9 DEGREES
REMARK 500    ARG A 183   NE  -  CZ  -  NH1 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ARG A 197   CD  -  NE  -  CZ  ANGL. DEV. =  29.2 DEGREES
REMARK 500    ARG A 197   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG A 197   NE  -  CZ  -  NH2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ARG A 200   CD  -  NE  -  CZ  ANGL. DEV. =  18.6 DEGREES
REMARK 500    ARG A 200   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 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    SER A  47       -4.81     81.97
REMARK 500    GLN A  62       98.22     81.95
REMARK 500    PRO A 108      157.14    -49.00
REMARK 500    ALA A 110       39.21   -155.66
REMARK 500    ALA A 111       -0.06   -146.75
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  31         0.16    SIDE CHAIN
REMARK 500    ARG A  86         0.12    SIDE CHAIN
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    VAL A 178        24.2      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 355        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH A 375        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH A 421        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH A 458        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A 460        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A 465        DISTANCE =  6.19 ANGSTROMS
REMARK 525    HOH A 466        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH A 474        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A 489        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A 491        DISTANCE =  5.27 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBI A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBI A 204
DBREF  2GSQ A    1   202  UNP    P46088   GST_OMMSL        2    203
SEQRES   1 A  202  PRO LYS TYR THR LEU HIS TYR PHE PRO LEU MET GLY ARG
SEQRES   2 A  202  ALA GLU LEU CYS ARG PHE VAL LEU ALA ALA HIS GLY GLU
SEQRES   3 A  202  GLU PHE THR ASP ARG VAL VAL GLU MET ALA ASP TRP PRO
SEQRES   4 A  202  ASN LEU LYS ALA THR MET TYR SER ASN ALA MET PRO VAL
SEQRES   5 A  202  LEU ASP ILE ASP GLY THR LYS MET SER GLN SER MET CYS
SEQRES   6 A  202  ILE ALA ARG HIS LEU ALA ARG GLU PHE GLY LEU ASP GLY
SEQRES   7 A  202  LYS THR SER LEU GLU LYS TYR ARG VAL ASP GLU ILE THR
SEQRES   8 A  202  GLU THR LEU GLN ASP ILE PHE ASN ASP VAL VAL LYS ILE
SEQRES   9 A  202  LYS PHE ALA PRO GLU ALA ALA LYS GLU ALA VAL GLN GLN
SEQRES  10 A  202  ASN TYR GLU LYS SER CYS LYS ARG LEU ALA PRO PHE LEU
SEQRES  11 A  202  GLU GLY LEU LEU VAL SER ASN GLY GLY GLY ASP GLY PHE
SEQRES  12 A  202  PHE VAL GLY ASN SER MET THR LEU ALA ASP LEU HIS CYS
SEQRES  13 A  202  TYR VAL ALA LEU GLU VAL PRO LEU LYS HIS THR PRO GLU
SEQRES  14 A  202  LEU LEU LYS ASP CYS PRO LYS ILE VAL ALA LEU ARG LYS
SEQRES  15 A  202  ARG VAL ALA GLU CYS PRO LYS ILE ALA ALA TYR LEU LYS
SEQRES  16 A  202  LYS ARG PRO VAL ARG ASP PHE
HET    SO4  A 300       5
HET    GBI  A 203      28
HET    GBI  A 204      28
HETNAM     SO4 SULFATE ION
HETNAM     GBI S-(3-IODOBENZYL)GLUTATHIONE
FORMUL   2  SO4    O4 S 2-
FORMUL   3  GBI    2(C17 H22 I N3 O6 S)
FORMUL   5  HOH   *211(H2 O)
HELIX    1   1 GLY A   12  HIS A   24  5                                  13
HELIX    2   2 TRP A   38  THR A   44  1                                   7
HELIX    3   3 TYR A   46  ASN A   48  5                                   3
HELIX    4   4 SER A   63  GLU A   73  1                                  11
HELIX    5   5 SER A   81  PHE A  106  1                                  26
HELIX    6   6 LYS A  112  VAL A  135  1                                  24
HELIX    7   7 LEU A  151  HIS A  166  1                                  16
HELIX    8   8 PRO A  175  GLU A  186  1                                  12
HELIX    9   9 PRO A  188  LYS A  196  1                                   9
SHEET    1   A 4 THR A  29  VAL A  32  0
SHEET    2   A 4 TYR A   3  TYR A   7  1  N  LEU A   5   O  THR A  29
SHEET    3   A 4 VAL A  52  ILE A  55 -1  N  ASP A  54   O  THR A   4
SHEET    4   A 4 THR A  58  MET A  60 -1  N  MET A  60   O  LEU A  53
CISPEP   1 MET A   50    PRO A   51          0         2.26
SITE     1 AC1  6 VAL A 101  VAL A 102  LYS A 105  VAL A 162
SITE     2 AC1  6 PHE A 202  GBI A 203
SITE     1 AC2 17 TYR A   7  PHE A   8  ARG A  13  TRP A  38
SITE     2 AC2 17 LYS A  42  ALA A  49  MET A  50  PRO A  51
SITE     3 AC2 17 GLN A  62  SER A  63  ASP A  96  VAL A 102
SITE     4 AC2 17 SO4 A 300  HOH A 301  HOH A 304  HOH A 420
SITE     5 AC2 17 HOH A 432
SITE     1 AC3 11 ARG A  13  VAL A 102  LYS A 103  PHE A 106
SITE     2 AC3 11 ALA A 107  ALA A 114  VAL A 115  GLN A 117
SITE     3 AC3 11 ASN A 118  HOH A 391  HOH A 478
CRYST1   73.150   73.150   94.880  90.00  90.00 120.00 P 31 2 1      6
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      0.013671  0.007893  0.000000        0.00000
SCALE2      0.000000  0.015785  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010540        0.00000
      
PROCHECK
Go to PROCHECK summary
 References