HEADER TRANSFERASE 30-NOV-05 2C80
TITLE STRUCTURE OF SH28GST IN COMPLEX WITH S-HEXYL GLUTATHIONE
CAVEAT 2C80 MET B 114 C-ALPHA IS PLANAR
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
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_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-23D
KEYWDS SIGMA CLASS GST, DETOXIFICATION, GLUTATHIONE, PROSTAGLANDIN D2
KEYWDS 2 SYNTHASE, INHIBITOR, TRANSFERASE, ANTIGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BAIOCCO,L.J.GOURLAY,F.ANGELUCCI,A.BELLELLI,M.BRUNORI,A.E.MIELE
REVDAT 5 13-DEC-23 2C80 1 REMARK
REVDAT 4 08-MAY-13 2C80 1 TITLE CAVEAT SOURCE REMARK
REVDAT 4 2 1 VERSN HETNAM HETSYN FORMUL
REVDAT 3 24-FEB-09 2C80 1 VERSN
REVDAT 2 12-JUL-06 2C80 1 JRNL
REVDAT 1 21-JUN-06 2C80 0
JRNL AUTH P.BAIOCCO,L.J.GOURLAY,F.ANGELUCCI,J.FONTAINE,M.HERVE,
JRNL AUTH 2 A.E.MIELE,F.TROTTEIN,M.BRUNORI,A.BELLELLI
JRNL TITL PROBING THE MECHANISM OF GSH ACTIVATION IN SCHISTOSOMA
JRNL TITL 2 HAEMATOBIUM GLUTATHIONE-S-TRANSFERASE BY SITE-DIRECTED
JRNL TITL 3 MUTAGENESIS AND X-RAY 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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 18295
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 985
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) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1281
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.03000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.439
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.258
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.178
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.140
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3483 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4689 ; 1.186 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 414 ; 5.317 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;30.170 ;24.172
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 655 ;14.402 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;23.352 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 520 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2540 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1695 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2356 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 237 ; 0.148 ; 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): 47 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.177 ; 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): 2144 ; 0.452 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3367 ; 0.786 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1509 ; 1.138 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1322 ; 1.813 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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: NULL
REMARK 4
REMARK 4 2C80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1290026605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2
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 : 18295
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
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 (%): 44.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG3350, 0.2M MES PH 6.0, 5MM BETA
REMARK 280 -MERCAPTOETHANOL, PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290
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 94.30067
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 47.15033
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: 4830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.2 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 400
REMARK 400 COMPOUND
REMARK 400 CENTRAL ROLE IN THE PARASITE DETOXIFICATION SYSTEM
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 465 GLY B 3
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 MET B 114 CA MET B 114 CB -0.320
REMARK 500 GLU B 117 CA GLU B 117 CB 0.713
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 MET B 114 CB - CA - C ANGL. DEV. = 14.9 DEGREES
REMARK 500 MET B 114 N - CA - CB ANGL. DEV. = 12.1 DEGREES
REMARK 500 MET B 114 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 GLU B 118 N - CA - C ANGL. DEV. = 17.3 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 70 95.99 72.20
REMARK 500 GLU A 118 -76.13 -22.00
REMARK 500 ASP A 174 106.20 -160.78
REMARK 500 ALA A 207 66.96 96.98
REMARK 500 ARG B 14 -71.12 -74.96
REMARK 500 GLU B 70 96.26 70.06
REMARK 500 GLU B 117 30.36 -63.24
REMARK 500 GLU B 118 10.12 174.61
REMARK 500 GLU B 119 -81.82 36.34
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 GLU B 118 GLU B 119 42.85
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 GTX A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 1213
REMARK 900
REMARK 900 RELATED ENTRIES
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 PH 6.0
REMARK 900 RELATED ID: 2CAI RELATED DB: PDB
REMARK 900 STRUCTURE OF GLUTATHIONE-S-TRANSFERASE MUTANT, R21L, FROM
REMARK 900 SCHISTOSOMA HAEMATOBIUM
REMARK 900 RELATED ID: 2CAQ RELATED DB: PDB
REMARK 900 STRUCTURE OF R21L MUTANT OF SH28GST IN COMPLEX WITH GSH
DBREF 2C80 A 1 211 UNP P30113 GST28_SCHBO 1 211
DBREF 2C80 B 1 211 UNP P30113 GST28_SCHBO 1 211
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 ARG 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 ARG 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 GTX A1212 26
HET PG4 B1212 13
HET GTX B1213 26
HETNAM GTX S-HEXYLGLUTATHIONE
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 GTX 2(C16 H30 N3 O6 S 1+)
FORMUL 4 PG4 C8 H18 O5
FORMUL 6 HOH *228(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 PRO A 116 GLY A 130 1 15
HELIX 8 8 GLY A 130 ALA 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
HELIX 12 12 ALA B 17 GLY B 28 1 12
HELIX 13 13 ASP B 40 LYS B 45 1 6
HELIX 14 14 PRO B 46 ILE B 48 5 3
HELIX 15 15 GLU B 70 HIS B 82 1 13
HELIX 16 16 THR B 88 LYS B 111 1 24
HELIX 17 17 GLU B 119 GLY B 130 1 12
HELIX 18 18 GLY B 130 ALA B 145 1 16
HELIX 19 19 THR B 157 ASP B 174 1 18
HELIX 20 20 TYR B 182 SER B 196 1 15
HELIX 21 21 SER B 196 ASP B 205 1 10
SHEET 1 AA 4 GLU A 32 ILE A 36 0
SHEET 2 AA 4 HIS A 5 PHE A 11 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 ILE B 36 0
SHEET 2 BA 4 HIS B 5 PHE B 11 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 VAL B 69 -1 O LYS B 66 N ILE B 58
CISPEP 1 LEU A 53 PRO A 54 0 2.99
CISPEP 2 ARG A 206 ALA A 207 0 27.63
CISPEP 3 LEU B 53 PRO B 54 0 0.85
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 TYR A 110 HOH A2106 HOH A2107
SITE 4 AC1 14 ASP B 104 HOH B2059
SITE 1 AC2 7 LYS A 80 GLY A 86 TYR A 92 LYS B 80
SITE 2 AC2 7 GLY B 86 THR B 88 TYR B 92
SITE 1 AC3 18 ASP A 104 TYR B 10 GLY B 15 ARG B 16
SITE 2 AC3 18 TRP B 41 LYS B 45 ARG B 52 LEU B 53
SITE 3 AC3 18 PRO B 54 GLU B 70 SER B 71 TYR B 110
SITE 4 AC3 18 LEU B 113 PHE B 211 HOH B2118 HOH B2119
SITE 5 AC3 18 HOH B2120 HOH B2121
CRYST1 52.832 52.832 141.451 90.00 90.00 120.00 P 32 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 0.018928 0.010928 0.000000 0.00000
SCALE2 0.000000 0.021856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
