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PDBsum entry 2cai

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
2cai
Jmol
Contents
Protein chains
208 a.a.
Ligands
SO4 ×10
PG4 ×3
BME ×3
Waters ×183
HEADER    TRANSFERASE                             21-DEC-05   2CAI
TITLE     STRUCTURE OF GLUTATHIONE-S-TRANSFERASE MUTANT, R21L, FROM
TITLE    2 SCHISTOSOMA HAEMATOBIUM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE 28 KDA;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: GST 28, GST CLASS-SIGMA;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA HAEMATOBIUM;
SOURCE   3 ORGANISM_COMMON: BLOOD FLUKE;
SOURCE   4 ORGANISM_TAXID: 6185;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-23D
KEYWDS    TRANSFERASE, GLUTATHIONE S-TRANSFERASE, HOMODIMER,
KEYWDS   2 THIOREDOXIN-LIKE FOLD, DETOXIFICATION, ANTIGEN, MULTIGENE
KEYWDS   3 FAMILY
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.BAIOCCO,L.J.GOURLAY,F.ANGELUCCI,A.BELLELLI,M.BRUNORI,
AUTHOR   2 A.E.MIELE
REVDAT   3   24-FEB-09 2CAI    1       VERSN
REVDAT   2   12-JUL-06 2CAI    1       JRNL
REVDAT   1   21-JUN-06 2CAI    0
JRNL        AUTH   P.BAIOCCO,L.J.GOURLAY,F.ANGELUCCI,J.FONTAINE,
JRNL        AUTH 2 M.HERVE,A.E.MIELE,F.TROTTEIN,M.BRUNORI,A.BELLELLI
JRNL        TITL   PROBING THE MECHANISM OF GSH ACTIVATION IN
JRNL        TITL 2 SCHISTOSOMA HAEMATOBIUM GLUTATHIONE-S-TRANSFERASE
JRNL        TITL 3 BY SITE-DIRECTED MUTAGENESIS AND X-RAY
JRNL        TITL 4 CRYSTALLOGRAPHY.
JRNL        REF    J.MOL.BIOL.                   V. 360   678 2006
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16777141
JRNL        DOI    10.1016/J.JMB.2006.05.040
REMARK   2
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.26
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 105.41
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 24373
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) : 0.218
REMARK   3   R VALUE            (WORKING SET) : 0.215
REMARK   3   FREE R VALUE                     : 0.272
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1309
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) : 2.26
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1769
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230
REMARK   3   BIN FREE R VALUE SET COUNT          : 97
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3362
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 101
REMARK   3   SOLVENT ATOMS            : 183
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.25
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): 0.300
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.241
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.172
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.793
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3496 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4707 ; 1.508 ; 1.992
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   415 ; 6.311 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;35.823 ;24.459
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   647 ;16.348 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;17.181 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   522 ; 0.106 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2495 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1878 ; 0.224 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2350 ; 0.310 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   239 ; 0.156 ; 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):   132 ; 0.239 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.208 ; 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):  2139 ; 0.818 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3371 ; 1.375 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1506 ; 1.960 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1336 ; 3.059 ; 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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : 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
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2CAI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-05.
REMARK 100 THE PDBE ID CODE IS EBI-26574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-05
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.40
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25780
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 22.000
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 20.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 9.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1OE7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG200, PBS PH7.4, 5MM
REMARK 280  MERCAPTOETHANOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z,-X,-Y
REMARK 290       7555   -Z,-X,Y
REMARK 290       8555   -Z,X,-Y
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z,-X
REMARK 290      11555   Y,-Z,-X
REMARK 290      12555   -Y,-Z,X
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2
REMARK 290      24555   -Y+1/2,-Z+1/2,X+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 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  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        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        0.00000
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000
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        0.00000
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.35800
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       74.35800
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.35800
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       74.35800
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       74.35800
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       74.35800
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       74.35800
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       74.35800
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       74.35800
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       74.35800
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       74.35800
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       74.35800
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       74.35800
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       74.35800
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       74.35800
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       74.35800
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       74.35800
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       74.35800
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       74.35800
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       74.35800
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       74.35800
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       74.35800
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       74.35800
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       74.35800
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       74.35800
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       74.35800
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 GENERATING THE BIOMOLECULE
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400  IMPORTANT ROLE IN THE PARASITE DETOXIFICATION SYSTEM
REMARK 400  ENGINEERED RESIDUE IN CHAIN A, ARG 21 TO LEU
REMARK 400  ENGINEERED RESIDUE IN CHAIN B, ARG 21 TO LEU
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     THR A     2
REMARK 465     GLY A     3
REMARK 465     MET B     1
REMARK 465     THR B     2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PRO A  46    CG   CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 118   CG    GLU A 118   CD      0.653
REMARK 500    GLY B   3   N     GLY B   3   CA      0.178
REMARK 500    LYS B  43   CG    LYS B  43   CD      0.409
REMARK 500
REMARK 500 REMARK: NULL
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    GLY A  50   N   -  CA  -  C   ANGL. DEV. = -15.6 DEGREES
REMARK 500    GLU A 118   CB  -  CG  -  CD  ANGL. DEV. = -16.4 DEGREES
REMARK 500    GLU A 118   CG  -  CD  -  OE1 ANGL. DEV. = -25.7 DEGREES
REMARK 500    ARG B  14   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG B  14   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES
REMARK 500    LYS B  43   CB  -  CG  -  CD  ANGL. DEV. = -19.2 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 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    LYS A  43      -65.82   -162.00
REMARK 500    ILE A  44      -88.20     78.08
REMARK 500    GLU A  70       90.70     73.46
REMARK 500    ALA A 207     -146.82     60.23
REMARK 500    ALA A 208      109.52     73.76
REMARK 500    THR A 209       90.55     51.97
REMARK 500    PRO A 210      105.26    -21.63
REMARK 500    ASP B  60      -72.48   -169.20
REMARK 500    ASN B  61      -74.60     -5.95
REMARK 500    HIS B  64     -155.17   -125.31
REMARK 500    GLU B  70       88.45     69.25
REMARK 500    ALA B 207      -74.54     79.02
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 PRO A   49     GLY A   50                  -32.19
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    GLU A 118         0.18    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 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    LYS A  43        22.8      L          L   OUTSIDE RANGE
REMARK 500    ILE A  44        21.0      L          L   OUTSIDE RANGE
REMARK 500    ASN B  61        23.5      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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1218
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A1219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B1218
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C80   RELATED DB: PDB
REMARK 900  STRUCTURE OF SH28GST IN COMPLEX WITH
REMARK 900  S-HEXYL GLUTATHIONE
REMARK 900 RELATED ID: 2C8U   RELATED DB: PDB
REMARK 900  STRUCTURE OF R21Q MUTANT OF SH28GST
REMARK 900 RELATED ID: 2CA8   RELATED DB: PDB
REMARK 900  STRUCTURE OF SH28GST IN COMPLEX WITH GSH AT
REMARK 900   PH 6.0
DBREF  2CAI A    1   211  UNP    P30113   GST28_SCHBO      1    211
DBREF  2CAI B    1   211  UNP    P30113   GST28_SCHBO      1    211
SEQADV 2CAI LEU A   21  UNP  P30113    ARG    21 ENGINEERED MUTATION
SEQADV 2CAI LEU B   21  UNP  P30113    ARG    21 ENGINEERED MUTATION
SEQRES   1 A  211  MET THR GLY ASP HIS ILE LYS VAL ILE TYR PHE ASN GLY
SEQRES   2 A  211  ARG GLY ARG ALA GLU SER ILE LEU MET THR LEU VAL ALA
SEQRES   3 A  211  ALA GLY VAL ASN 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 ILE THR ASP ASN HIS GLY HIS VAL
SEQRES   6 A  211  LYS TRP MET VAL GLU SER LEU ALA ILE ALA ARG TYR MET
SEQRES   7 A  211  ALA LYS LYS HIS HIS MET MET GLY GLY THR GLU GLU GLU
SEQRES   8 A  211  TYR TYR ASN VAL GLU LYS LEU ILE GLY GLN ALA GLU ASP
SEQRES   9 A  211  LEU GLU HIS GLU TYR TYR LYS THR LEU MET LYS PRO GLU
SEQRES  10 A  211  GLU GLU LYS GLN LYS ILE ILE LYS GLU ILE LEU ASN GLY
SEQRES  11 A  211  LYS VAL PRO VAL LEU LEU ASP ILE ILE CYS GLU SER LEU
SEQRES  12 A  211  LYS ALA 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 GLU 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 ASP ARG ALA ALA
SEQRES  17 A  211  THR PRO PHE
SEQRES   1 B  211  MET THR GLY ASP HIS ILE LYS VAL ILE TYR PHE ASN GLY
SEQRES   2 B  211  ARG GLY ARG ALA GLU SER ILE LEU MET THR LEU VAL ALA
SEQRES   3 B  211  ALA GLY VAL ASN TYR GLU ASP GLU ARG ILE SER PHE GLN
SEQRES   4 B  211  ASP TRP PRO LYS ILE LYS PRO THR ILE PRO GLY GLY ARG
SEQRES   5 B  211  LEU PRO ALA VAL LYS ILE THR ASP ASN HIS GLY HIS VAL
SEQRES   6 B  211  LYS TRP MET VAL GLU SER LEU ALA ILE ALA ARG TYR MET
SEQRES   7 B  211  ALA LYS LYS HIS HIS MET MET GLY GLY THR GLU GLU GLU
SEQRES   8 B  211  TYR TYR ASN VAL GLU LYS LEU ILE GLY GLN ALA GLU ASP
SEQRES   9 B  211  LEU GLU HIS GLU TYR TYR LYS THR LEU MET LYS PRO GLU
SEQRES  10 B  211  GLU GLU LYS GLN LYS ILE ILE LYS GLU ILE LEU ASN GLY
SEQRES  11 B  211  LYS VAL PRO VAL LEU LEU ASP ILE ILE CYS GLU SER LEU
SEQRES  12 B  211  LYS ALA SER THR GLY LYS LEU ALA VAL GLY ASP LYS VAL
SEQRES  13 B  211  THR LEU ALA ASP LEU VAL LEU ILE ALA VAL ILE ASP HIS
SEQRES  14 B  211  VAL THR ASP LEU ASP LYS GLU PHE LEU THR GLY LYS TYR
SEQRES  15 B  211  PRO GLU ILE HIS LYS HIS ARG GLU ASN LEU LEU ALA SER
SEQRES  16 B  211  SER PRO ARG LEU ALA LYS TYR LEU SER ASP ARG ALA ALA
SEQRES  17 B  211  THR PRO PHE
HET    SO4  A1212       5
HET    SO4  A1213       5
HET    SO4  A1214       5
HET    SO4  A1215       5
HET    SO4  B1212       5
HET    SO4  B1213       5
HET    SO4  B1214       5
HET    SO4  B1215       5
HET    SO4  B1216       5
HET    SO4  B1217       5
HET    PG4  A1216      13
HET    PG4  A1217      13
HET    PG4  A1218      13
HET    BME  A1219       4
HET    BME  A1220       4
HET    BME  B1218       4
HETNAM     SO4 SULFATE ION
HETNAM     PG4 TETRAETHYLENE GLYCOL
HETNAM     BME BETA-MERCAPTOETHANOL
HETSYN     PG4 POLYETHYLENE GLYCOL PEG400
HETSYN     BME 2-SULFHYDRYL-ETHANOL
FORMUL   3  SO4    10(O4 S 2-)
FORMUL  13  PG4    3(C8 H18 O5)
FORMUL  16  BME    3(C2 H6 O S)
FORMUL  19  HOH   *183(H2 O1)
HELIX    1   1 ALA A   17  GLY A   28  1                                  12
HELIX    2   2 ILE A   44  ILE A   48  5                                   5
HELIX    3   3 GLU A   70  HIS A   82  1                                  13
HELIX    4   4 THR A   88  LYS A  111  1                                  24
HELIX    5   5 PRO A  116  GLY A  130  1                                  15
HELIX    6   6 GLY A  130  ALA A  145  1                                  16
HELIX    7   7 THR A  157  ASP A  174  1                                  18
HELIX    8   8 TYR A  182  SER A  196  1                                  15
HELIX    9   9 SER A  196  SER A  204  1                                   9
HELIX   10  10 ALA B   17  GLY B   28  1                                  12
HELIX   11  11 ASP B   40  LYS B   45  1                                   6
HELIX   12  12 PRO B   46  ILE B   48  5                                   3
HELIX   13  13 GLU B   70  HIS B   82  1                                  13
HELIX   14  14 THR B   88  LYS B  111  1                                  24
HELIX   15  15 PRO B  116  ASN B  129  1                                  14
HELIX   16  16 GLY B  130  ALA B  145  1                                  16
HELIX   17  17 THR B  157  ASP B  174  1                                  18
HELIX   18  18 TYR B  182  SER B  196  1                                  15
HELIX   19  19 SER B  196  SER B  204  1                                   9
SHEET    1  AA 4 GLU A  32  ARG A  35  0
SHEET    2  AA 4 HIS A   5  TYR A  10  1  O  ILE A   6   N  GLU A  32
SHEET    3  AA 4 ALA A  55  THR A  59 -1  O  ALA A  55   N  ILE A   9
SHEET    4  AA 4 VAL A  65  VAL A  69 -1  O  LYS A  66   N  ILE A  58
SHEET    1  BA 4 GLU B  32  ARG B  35  0
SHEET    2  BA 4 HIS B   5  TYR B  10  1  O  ILE B   6   N  GLU B  32
SHEET    3  BA 4 ALA B  55  THR B  59 -1  O  ALA B  55   N  ILE B   9
SHEET    4  BA 4 VAL B  65  MET B  68 -1  O  LYS B  66   N  ILE B  58
CISPEP   1 LYS A   43    ILE A   44          0        29.67
CISPEP   2 GLY A   50    GLY A   51          0       -10.20
CISPEP   3 LEU A   53    PRO A   54          0        -7.49
CISPEP   4 ALA A  208    THR A  209          0         9.72
CISPEP   5 THR A  209    PRO A  210          0         7.84
CISPEP   6 PRO A  210    PHE A  211          0       -12.42
CISPEP   7 ILE B   48    PRO B   49          0        -5.23
CISPEP   8 PRO B   49    GLY B   50          0         6.84
CISPEP   9 LEU B   53    PRO B   54          0        -5.47
CISPEP  10 ASN B   61    HIS B   62          0         9.74
CISPEP  11 GLY B   63    HIS B   64          0        10.35
SITE     1 AC1  6 ARG A 189  HOH A2087  HOH A2088  LEU B 178
SITE     2 AC1  6 THR B 179  HIS B 186
SITE     1 AC2  6 PHE A  11  ASN A  12  GLY A  15  ARG A  16
SITE     2 AC2  6 HOH A2090  HOH A2091
SITE     1 AC3  7 ARG A  16  GLU A  70  SER A  71  HOH A2092
SITE     2 AC3  7 HOH A2093  HOH A2094  HOH A2095
SITE     1 AC4  4 ASP A   4  ASP A  60  ASN A  61  HIS A  62
SITE     1 AC5  3 THR B  88  GLU B  89  HOH B2078
SITE     1 AC6  9 LEU A 178  THR A 179  HIS A 186  HOH A2067
SITE     2 AC6  9 HOH A2087  HIS B 186  ARG B 189  HOH B2079
SITE     3 AC6  9 HOH B2080
SITE     1 AC7  6 ARG B  16  PRO B  54  GLU B  70  SER B  71
SITE     2 AC7  6 HOH B2081  HOH B2082
SITE     1 AC8  5 PHE B  11  ASN B  12  GLY B  15  ARG B  16
SITE     2 AC8  5 HOH B2083
SITE     1 AC9  6 HIS A  64  VAL A  65  LYS A 125  LYS B 201
SITE     2 AC9  6 ALA B 207  HOH B2076
SITE     1 BC1  4 GLU A 117  ARG B  35  SER B  37  GLN B  39
SITE     1 BC2  9 GLN A 121  LEU A 173  ASP A 174  HOH A2096
SITE     2 BC2  9 GLY B  13  TYR B 202  LEU B 203  ASP B 205
SITE     3 BC2  9 BME B1218
SITE     1 BC3  9 GLY A  13  TYR A 202  LEU A 203  ASP A 205
SITE     2 BC3  9 HOH A2097  HOH A2099  LEU B 173  ASP B 174
SITE     3 BC3  9 HOH B2049
SITE     1 BC4  6 LYS A  80  GLY A  86  TYR A  92  LYS B  80
SITE     2 BC4  6 GLY B  86  TYR B  92
SITE     1 BC5  3 LEU A  72  ARG A  76  GLU A 103
SITE     1 BC6  4 TYR A  77  MET A  78  LYS A  81  PHE B 211
SITE     1 BC7  4 GLU A 117  PG4 A1216  ASN B  12  GLY B  13
CRYST1  148.716  148.716  148.716  90.00  90.00  90.00 I 2 3        48
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      0.006724  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006724  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006724        0.00000
      
PROCHECK
Go to PROCHECK summary
 References