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PDBsum entry 1u3i

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Transferase PDB id
1u3i
Jmol
Contents
Protein chain
208 a.a.
Ligands
GSH
Waters ×164
HEADER    TRANSFERASE                             22-JUL-04   1U3I
TITLE     CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANFERASE FROM SCHISTOSOMA MANSONI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE 28 KDA;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: GST 28, SM28 ANTIGEN, PROTECTIVE 28 KDA ANTIGEN, GST CLASS-
COMPND   5 ALPHA;
COMPND   6 EC: 2.5.1.18;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA MANSONI;
SOURCE   3 ORGANISM_TAXID: 6183;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: TGE901;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PTG54
KEYWDS    GST FOLD, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.CHOMILIER,M.-C.VANEY,G.LABESSE,F.TROTTEIN,A.CAPRON,J.-P.MORMON
REVDAT   4   21-MAR-12 1U3I    1       HET
REVDAT   3   13-JUL-11 1U3I    1       VERSN
REVDAT   2   24-FEB-09 1U3I    1       VERSN
REVDAT   1   26-JUL-05 1U3I    0
JRNL        AUTH   J.CHOMILIER,M.-C.VANEY,G.LABESSE,F.TROTTEIN,A.CAPRON,
JRNL        AUTH 2 J.-P.MORMON
JRNL        TITL   CRYSTAL STRUCTURE OF SCHISTOSOMA MANSONI GLUTATHIONE
JRNL        TITL 2 S-TRANSFERASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   F.M.TROTTEIN,M.-C.VANEY,B.BACHET,R.-J.PIERCE,N.COLLOC'H,
REMARK   1  AUTH 2 J.-P.LECOCQ,A.CAPRON,J.-P.MORMON
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK   1  TITL 2 A PROTECTIVE CLONED 28 KDA GLUTATHIONE S-TRANSFERASE FROM
REMARK   1  TITL 3 SCHISTOSOMA MANSONI
REMARK   1  REF    J.MOL.BIOL.                   V. 224   515 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0003
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.28
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1
REMARK   3   NUMBER OF REFLECTIONS             : 23127
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) : 0.175
REMARK   3   R VALUE            (WORKING SET) : 0.174
REMARK   3   FREE R VALUE                     : 0.192
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1246
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) : 1.89
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1571
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.28
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1750
REMARK   3   BIN FREE R VALUE SET COUNT          : 73
REMARK   3   BIN FREE R VALUE                    : 0.2570
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1660
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 164
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : 19.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.70
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.117
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.106
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.063
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.147
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1730 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2331 ; 1.439 ; 1.972
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   207 ; 5.117 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    74 ;33.987 ;23.919
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   329 ;14.267 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;28.969 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   258 ; 0.152 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1273 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   771 ; 0.209 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1179 ; 0.314 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   154 ; 0.200 ; 0.200
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):    40 ; 0.179 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.242 ; 0.200
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):  1070 ; 0.966 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1684 ; 1.386 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   740 ; 2.513 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   647 ; 3.940 ; 4.500
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  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     4        A    82
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7500  60.7670  26.7480
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0508 T22:  -0.1340
REMARK   3      T33:   0.0133 T12:   0.0298
REMARK   3      T13:   0.0413 T23:   0.0060
REMARK   3    L TENSOR
REMARK   3      L11:   4.2768 L22:   2.5810
REMARK   3      L33:   2.9525 L12:   1.8719
REMARK   3      L13:  -0.3853 L23:   1.2832
REMARK   3    S TENSOR
REMARK   3      S11:   0.1655 S12:   0.0746 S13:   0.7059
REMARK   3      S21:  -0.1317 S22:  -0.0161 S23:   0.1642
REMARK   3      S31:  -0.4755 S32:  -0.0371 S33:  -0.1494
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    83        A   101
REMARK   3    RESIDUE RANGE :   A   132        A   211
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2820  40.1060  22.8230
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1067 T22:  -0.1123
REMARK   3      T33:  -0.1168 T12:   0.0117
REMARK   3      T13:   0.0155 T23:  -0.0297
REMARK   3    L TENSOR
REMARK   3      L11:   2.2882 L22:   1.1800
REMARK   3      L33:   1.6969 L12:  -0.0706
REMARK   3      L13:  -0.2223 L23:   0.1078
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0586 S12:   0.1449 S13:  -0.0917
REMARK   3      S21:  -0.0628 S22:   0.0453 S23:  -0.1629
REMARK   3      S31:   0.0671 S32:   0.1009 S33:   0.0133
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   102        A   131
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0430  43.4650  40.3940
REMARK   3    T TENSOR
REMARK   3      T11:   0.0248 T22:   0.2549
REMARK   3      T33:   0.0184 T12:  -0.0048
REMARK   3      T13:  -0.1071 T23:  -0.0415
REMARK   3    L TENSOR
REMARK   3      L11:  14.2773 L22:   9.4094
REMARK   3      L33:   5.8746 L12:   0.7443
REMARK   3      L13:  -0.6782 L23:  -0.7633
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1299 S12:  -1.9203 S13:   0.4833
REMARK   3      S21:   0.9965 S22:  -0.1028 S23:  -1.1385
REMARK   3      S31:  -0.3494 S32:   0.8525 S33:   0.2326
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   301        A   301
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6050  57.3510  37.2900
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0478 T22:   0.0220
REMARK   3      T33:  -0.0113 T12:  -0.0749
REMARK   3      T13:  -0.0062 T23:  -0.1164
REMARK   3    L TENSOR
REMARK   3      L11:  34.1769 L22:  23.9216
REMARK   3      L33:   6.1508 L12:  24.1322
REMARK   3      L13:   0.8974 L23:  -5.8600
REMARK   3    S TENSOR
REMARK   3      S11:   0.7613 S12:  -1.7634 S13:  -0.3260
REMARK   3      S21:   0.2389 S22:  -0.9567 S23:  -0.6905
REMARK   3      S31:  -0.5061 S32:  -0.1075 S33:   0.1954
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1U3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB023198.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-92
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : LURE
REMARK 200  BEAMLINE                       : DW32
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9750
REMARK 200  MONOCHROMATOR                  : CURVED SI (111) - MULTILAYERS
REMARK 200                                   MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24391
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.780
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06700
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.40700
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1OE8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM PHOSPHATE,
REMARK 280  PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
REMARK 290      13555   Y+1/4,X+3/4,-Z+3/4
REMARK 290      14555   -Y+1/4,-X+1/4,-Z+1/4
REMARK 290      15555   Y+3/4,-X+3/4,Z+1/4
REMARK 290      16555   -Y+3/4,X+1/4,Z+3/4
REMARK 290      17555   X+1/4,Z+3/4,-Y+3/4
REMARK 290      18555   -X+3/4,Z+1/4,Y+3/4
REMARK 290      19555   -X+1/4,-Z+1/4,-Y+1/4
REMARK 290      20555   X+3/4,-Z+3/4,Y+1/4
REMARK 290      21555   Z+1/4,Y+3/4,-X+3/4
REMARK 290      22555   Z+3/4,-Y+3/4,X+1/4
REMARK 290      23555   -Z+3/4,Y+1/4,X+3/4
REMARK 290      24555   -Z+1/4,-Y+1/4,-X+1/4
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       60.97500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.97500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.97500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.97500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.97500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.97500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       60.97500
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       60.97500
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       60.97500
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       60.97500
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       60.97500
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       60.97500
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       60.97500
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       60.97500
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       60.97500
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       60.97500
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       60.97500
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       60.97500
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       30.48750
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       91.46250
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       91.46250
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       30.48750
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       30.48750
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       30.48750
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       91.46250
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       91.46250
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       30.48750
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       91.46250
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       30.48750
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       91.46250
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       30.48750
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       91.46250
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       91.46250
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       91.46250
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       30.48750
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       91.46250
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       30.48750
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       30.48750
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       30.48750
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       91.46250
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       91.46250
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       30.48750
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       30.48750
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       91.46250
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       91.46250
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       91.46250
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       91.46250
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       30.48750
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       91.46250
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       30.48750
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       91.46250
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       30.48750
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       30.48750
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       30.48750
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS: Z-1/4,3/4-Y,1/4+X
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 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  0.000000  0.000000  1.000000      -30.48750
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       91.46250
REMARK 350   BIOMT3   2  1.000000  0.000000  0.000000       30.48750
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 437  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 456  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 454  LIES ON A SPECIAL POSITION.
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 465     ALA A     2
REMARK 465     GLY A     3
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    ASP A  61   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A 168   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP A 174   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    ASP A  60     -134.00    -86.58
REMARK 500    ASP A  61      -13.06   -146.64
REMARK 500    HIS A  62      -72.94    -85.73
REMARK 500    HIS A  64      -85.33    172.71
REMARK 500    GLU A  70       99.33     83.50
REMARK 500    GLU A 118      -50.76   -170.05
REMARK 500    LEU A 150     -167.81   -107.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLY A   63     HIS A   64                  149.72
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 GSH A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OE7   RELATED DB: PDB
REMARK 900 GST FROM SCHISTOSOMA HEMATOBIUM
REMARK 900 RELATED ID: 1OE8   RELATED DB: PDB
REMARK 900 GST FROM SCHISTOSOMA HEMATOBIUM
DBREF  1U3I A    1   211  UNP    P09792   GST28_SCHMA      1    211
SEQADV 1U3I PHE A  136  UNP  P09792    LEU   136 CONFLICT
SEQRES   1 A  211  MET ALA GLY GLU HIS ILE LYS VAL ILE TYR PHE ASP GLY
SEQRES   2 A  211  ARG GLY ARG ALA GLU SER ILE ARG MET THR LEU VAL ALA
SEQRES   3 A  211  ALA GLY VAL ASP TYR GLU ASP GLU ARG ILE SER PHE GLN
SEQRES   4 A  211  ASP TRP PRO LYS ILE LYS PRO THR ILE PRO GLY GLY ARG
SEQRES   5 A  211  LEU PRO ALA VAL LYS VAL THR ASP ASP HIS GLY HIS VAL
SEQRES   6 A  211  LYS TRP MET LEU GLU SER LEU ALA ILE ALA ARG TYR MET
SEQRES   7 A  211  ALA LYS LYS HIS HIS MET MET GLY GLU THR ASP GLU GLU
SEQRES   8 A  211  TYR TYR SER VAL GLU LYS LEU ILE GLY GLN ALA GLU ASP
SEQRES   9 A  211  VAL GLU HIS GLU TYR HIS LYS THR LEU MET LYS PRO GLN
SEQRES  10 A  211  GLU GLU LYS GLU LYS ILE THR LYS GLU ILE LEU ASN GLY
SEQRES  11 A  211  LYS VAL PRO VAL LEU PHE ASN MET ILE CYS GLU SER LEU
SEQRES  12 A  211  LYS GLY SER THR GLY LYS LEU ALA VAL GLY ASP LYS VAL
SEQRES  13 A  211  THR LEU ALA ASP LEU VAL LEU ILE ALA VAL ILE ASP HIS
SEQRES  14 A  211  VAL THR ASP LEU ASP LYS GLY PHE LEU THR GLY LYS TYR
SEQRES  15 A  211  PRO GLU ILE HIS LYS HIS ARG GLU ASN LEU LEU ALA SER
SEQRES  16 A  211  SER PRO ARG LEU ALA LYS TYR LEU SER ASN ARG PRO ALA
SEQRES  17 A  211  THR PRO PHE
HET    GSH  A 301      20
HETNAM     GSH GLUTATHIONE
FORMUL   2  GSH    C10 H17 N3 O6 S
FORMUL   3  HOH   *164(H2 O)
HELIX    1   1 ARG A   14  ARG A   16  5                                   3
HELIX    2   2 ALA A   17  GLY A   28  1                                  12
HELIX    3   3 ASP A   40  LYS A   45  1                                   6
HELIX    4   4 PRO A   46  ILE A   48  5                                   3
HELIX    5   5 GLU A   70  HIS A   82  1                                  13
HELIX    6   6 THR A   88  LYS A  111  1                                  24
HELIX    7   7 GLU A  118  GLY A  130  1                                  13
HELIX    8   8 GLY A  130  GLY A  145  1                                  16
HELIX    9   9 THR A  157  ASP A  174  1                                  18
HELIX   10  10 TYR A  182  SER A  196  1                                  15
HELIX   11  11 SER A  196  ARG A  206  1                                  11
SHEET    1   A 4 GLU A  32  ILE A  36  0
SHEET    2   A 4 HIS A   5  PHE A  11  1  N  ILE A   6   O  GLU A  32
SHEET    3   A 4 ALA A  55  THR A  59 -1  O  THR A  59   N  HIS A   5
SHEET    4   A 4 VAL A  65  LEU A  69 -1  O  LYS A  66   N  VAL A  58
CISPEP   1 LEU A   53    PRO A   54          0         3.19
SITE     1 AC1 14 TYR A  10  ARG A  16  TRP A  41  LYS A  45
SITE     2 AC1 14 ARG A  52  LEU A  53  PRO A  54  GLU A  70
SITE     3 AC1 14 SER A  71  ASP A 104  HOH A 313  HOH A 395
SITE     4 AC1 14 HOH A 409  HOH A 434
CRYST1  121.950  121.950  121.950  90.00  90.00  90.00 P 43 3 2     24
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      0.008200  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008200  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008200        0.00000
      
PROCHECK
Go to PROCHECK summary
 References