HEADER TRANSFERASE 12-OCT-05 2C3T
TITLE HUMAN GLUTATHIONE-S-TRANSFERASE T1-1, W234R MUTANT, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE THETA 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HUMAN GLUTATHIONE TRANSFERASE T1-1, GST CLASS-THETA 1;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE
KEYWDS TRANSFERASE, GLUTATHIONE, GLUTATHIONE TRANSFERASE, T1-1, POLYMORPHISM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TARS,A.-K.LARSSON,A.SHOKEER,B.OLIN,B.MANNERVIK,G.J.KLEYWEGT
REVDAT 5 13-DEC-23 2C3T 1 REMARK
REVDAT 4 15-MAY-19 2C3T 1 REMARK
REVDAT 3 24-FEB-09 2C3T 1 VERSN
REVDAT 2 14-DEC-05 2C3T 1 JRNL
REVDAT 1 30-NOV-05 2C3T 0
JRNL AUTH K.TARS,A.-K.LARSSON,A.SHOKEER,B.OLIN,B.MANNERVIK,
JRNL AUTH 2 G.J.KLEYWEGT
JRNL TITL STRUCTURAL BASIS OF THE SUPPRESSED CATALYTIC ACTIVITY OF
JRNL TITL 2 WILD-TYPE HUMAN GLUTATHIONE TRANSFERASE T1-1 COMPARED TO ITS
JRNL TITL 3 W234R MUTANT.
JRNL REF J.MOL.BIOL. V. 355 96 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16298388
JRNL DOI 10.1016/J.JMB.2005.10.049
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 33761
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1805
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2519
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7676
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 267
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.16
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): 1.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.332
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.230
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.042
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7864 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10696 ; 1.233 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 952 ; 1.273 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 340 ;19.612 ;23.647
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1376 ; 6.831 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ; 5.676 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1224 ; 0.004 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5880 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3938 ; 0.203 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5379 ; 0.311 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 538 ; 0.187 ; 0.500
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): 63 ; 0.196 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.305 ; 0.500
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): 5028 ; 0.811 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7792 ; 1.370 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3322 ; 1.993 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2904 ; 3.098 ; 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 : 1.20
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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2C3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290025964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 200 DATA REDUNDANCY : 1.500
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 2C3Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING-DROP VAPOR-DIFFUSION
REMARK 280 TECHNIQUE. 5 MICROLITRES OF RESERVOIR SOLUTION [35% (V/V) PEG
REMARK 280 3350, 200 MM MG(NO3)2, AND 2 MM DITHIOTHREITOL] WERE MIXED WITH
REMARK 280 5 MICROLITRES OF PROTEIN SOLUTION (10 MG/ML IN 10 MM TRIS-HCL PH
REMARK 280 7.8, 15 % GLYCEROL) AND 1 MICROLITRE OF 100 MM CACL2, PH 8.00,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 82.26200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.91100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 82.26200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.91100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: C, D
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 ENGINEERED RESIDUE IN CHAIN A, TRP 233 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, TRP 233 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, TRP 233 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, TRP 233 TO ARG
REMARK 400
REMARK 400 THE ENGINEERED RESIDUE IS NUMBERED 234 IN THE COORDINATE
REMARK 400 RECORDS BELOW.
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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 MET C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 MET D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2036 O HOH C 2065 4457 1.79
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 LEU B 41 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 50 -6.80 -57.77
REMARK 500 GLU A 66 104.60 69.24
REMARK 500 LYS A 79 101.10 43.73
REMARK 500 THR A 105 -88.73 -128.27
REMARK 500 VAL A 118 -63.00 -131.33
REMARK 500 VAL A 122 -81.00 -75.87
REMARK 500 PHE A 151 -66.66 -108.99
REMARK 500 GLN A 153 -118.34 64.33
REMARK 500 VAL A 184 -60.36 -128.39
REMARK 500 PRO A 225 -37.37 -27.52
REMARK 500 LEU B 9 3.51 -63.39
REMARK 500 GLU B 66 110.31 66.69
REMARK 500 LYS B 79 63.46 39.27
REMARK 500 TYR B 85 82.18 -151.16
REMARK 500 PRO B 86 153.83 -49.76
REMARK 500 THR B 105 -90.79 -113.01
REMARK 500 VAL B 118 -49.51 -132.52
REMARK 500 PHE B 151 -70.26 -112.82
REMARK 500 GLN B 153 -127.05 48.90
REMARK 500 PRO B 225 -32.93 -29.62
REMARK 500 LEU C 9 4.13 -64.74
REMARK 500 ASN C 49 85.98 142.07
REMARK 500 GLU C 66 112.92 79.80
REMARK 500 LYS C 79 51.88 37.11
REMARK 500 TYR C 85 83.94 -156.71
REMARK 500 THR C 105 -87.83 -120.85
REMARK 500 VAL C 118 -47.33 -139.47
REMARK 500 PHE C 151 -70.59 -108.13
REMARK 500 GLN C 153 -128.50 54.67
REMARK 500 ALA C 217 -66.21 -21.95
REMARK 500 LYS C 218 -5.86 -55.97
REMARK 500 PRO C 225 -2.95 -47.83
REMARK 500 LEU D 9 -3.81 -59.75
REMARK 500 ASP D 34 94.37 -64.27
REMARK 500 GLU D 66 106.20 70.80
REMARK 500 LYS D 79 66.09 23.76
REMARK 500 THR D 105 -89.37 -116.05
REMARK 500 PHE D 151 -71.72 -107.50
REMARK 500 GLN D 153 -130.24 54.95
REMARK 500 PRO D 225 2.22 -51.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C3N RELATED DB: PDB
REMARK 900 HUMAN GLUTATHIONE-S-TRANSFERASE T1-1, APO FORM
REMARK 900 RELATED ID: 2C3Q RELATED DB: PDB
REMARK 900 HUMAN GLUTATHIONE-S-TRANSFERASE T1-1 W234R MUTANT, COMPLEX WITH S-
REMARK 900 HEXYLGLUTATHIONE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 6XHIS TAG ADDED TO THE N-TERMINUS OF PROTEIN. RESIDUE TRP
REMARK 999 234 MUTATED TO ARGININE.
DBREF 2C3T A -6 1 PDB 2C3T 2C3T -6 1
DBREF 2C3T A 2 240 UNP P30711 GSTT1_HUMAN 1 239
DBREF 2C3T B -6 1 PDB 2C3T 2C3T -6 1
DBREF 2C3T B 2 240 UNP P30711 GSTT1_HUMAN 1 239
DBREF 2C3T C -6 1 PDB 2C3T 2C3T -6 1
DBREF 2C3T C 2 240 UNP P30711 GSTT1_HUMAN 1 239
DBREF 2C3T D -6 1 PDB 2C3T 2C3T -6 1
DBREF 2C3T D 2 240 UNP P30711 GSTT1_HUMAN 1 239
SEQADV 2C3T ARG A 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQADV 2C3T ARG B 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQADV 2C3T ARG C 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQADV 2C3T ARG D 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQRES 1 A 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 A 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 A 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 A 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 A 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 A 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 A 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 A 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 A 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 A 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 A 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 A 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 A 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 A 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 A 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 A 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 A 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 A 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 A 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
SEQRES 1 B 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 B 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 B 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 B 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 B 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 B 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 B 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 B 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 B 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 B 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 B 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 B 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 B 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 B 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 B 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 B 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 B 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 B 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 B 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
SEQRES 1 C 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 C 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 C 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 C 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 C 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 C 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 C 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 C 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 C 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 C 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 C 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 C 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 C 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 C 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 C 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 C 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 C 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 C 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 C 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
SEQRES 1 D 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 D 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 D 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 D 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 D 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 D 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 D 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 D 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 D 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 D 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 D 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 D 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 D 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 D 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 D 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 D 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 D 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 D 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 D 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
FORMUL 5 HOH *267(H2 O)
HELIX 1 1 PRO A 13 ASN A 24 1 12
HELIX 2 2 GLY A 38 LEU A 41 5 4
HELIX 3 3 SER A 42 ASN A 49 1 8
HELIX 4 4 GLU A 66 TYR A 78 1 13
HELIX 5 5 GLN A 87 THR A 104 1 18
HELIX 6 6 THR A 105 VAL A 118 1 14
HELIX 7 7 PRO A 121 LEU A 124 5 4
HELIX 8 8 SER A 129 ASP A 149 1 21
HELIX 9 9 ALA A 166 GLY A 181 1 16
HELIX 10 10 LYS A 190 ALA A 201 1 12
HELIX 11 11 GLU A 204 LEU A 215 1 12
HELIX 12 12 ASP A 224 ILE A 239 1 16
HELIX 13 13 PRO B 13 ASN B 24 1 12
HELIX 14 14 GLY B 38 LEU B 41 5 4
HELIX 15 15 SER B 42 ASN B 49 1 8
HELIX 16 16 GLU B 66 TYR B 78 1 13
HELIX 17 17 GLN B 87 THR B 104 1 18
HELIX 18 18 THR B 105 VAL B 118 1 14
HELIX 19 19 PRO B 121 LEU B 124 5 4
HELIX 20 20 SER B 129 ASP B 149 1 21
HELIX 21 21 ALA B 166 GLY B 181 1 16
HELIX 22 22 LYS B 190 ALA B 201 1 12
HELIX 23 23 GLU B 204 LEU B 215 1 12
HELIX 24 24 ASP B 224 ILE B 239 1 16
HELIX 25 25 PRO C 13 ASN C 24 1 12
HELIX 26 26 GLY C 38 LEU C 41 5 4
HELIX 27 27 SER C 42 ASN C 49 1 8
HELIX 28 28 GLU C 66 TYR C 78 1 13
HELIX 29 29 GLN C 87 THR C 104 1 18
HELIX 30 30 THR C 105 VAL C 118 1 14
HELIX 31 31 PRO C 121 LEU C 124 5 4
HELIX 32 32 SER C 129 ASP C 149 1 21
HELIX 33 33 ALA C 166 GLY C 181 1 16
HELIX 34 34 LYS C 190 ALA C 201 1 12
HELIX 35 35 GLU C 204 LEU C 215 1 12
HELIX 36 36 ASP C 224 ILE C 239 1 16
HELIX 37 37 PRO D 13 ASN D 24 1 12
HELIX 38 38 GLY D 38 LEU D 41 5 4
HELIX 39 39 SER D 42 ASN D 49 1 8
HELIX 40 40 GLU D 66 TYR D 78 1 13
HELIX 41 41 GLN D 87 THR D 104 1 18
HELIX 42 42 THR D 105 VAL D 118 1 14
HELIX 43 43 PRO D 121 LEU D 124 5 4
HELIX 44 44 SER D 129 ASP D 149 1 21
HELIX 45 45 ALA D 166 GLY D 181 1 16
HELIX 46 46 LYS D 190 ALA D 201 1 12
HELIX 47 47 GLU D 204 LEU D 215 1 12
HELIX 48 48 ASP D 224 ILE D 239 1 16
SHEET 1 AA 4 GLU A 29 ILE A 32 0
SHEET 2 AA 4 GLY A 2 LEU A 9 1 O LEU A 3 N GLU A 29
SHEET 3 AA 4 VAL A 54 ASP A 59 -1 O ALA A 56 N TYR A 6
SHEET 4 AA 4 ASP A 61 LEU A 64 -1 O PHE A 62 N ASP A 59
SHEET 1 BA 4 GLU B 29 ILE B 32 0
SHEET 2 BA 4 GLY B 2 LEU B 9 1 O LEU B 3 N GLU B 29
SHEET 3 BA 4 VAL B 54 ASP B 59 -1 O ALA B 56 N TYR B 6
SHEET 4 BA 4 ASP B 61 LEU B 64 -1 O PHE B 62 N ASP B 59
SHEET 1 CA 4 GLU C 29 ILE C 32 0
SHEET 2 CA 4 GLY C 2 LEU C 9 1 O LEU C 3 N GLU C 29
SHEET 3 CA 4 VAL C 54 ASP C 59 -1 O ALA C 56 N TYR C 6
SHEET 4 CA 4 ASP C 61 LEU C 64 -1 O PHE C 62 N ASP C 59
SHEET 1 DA 4 GLU D 29 ILE D 32 0
SHEET 2 DA 4 GLY D 2 LEU D 9 1 O LEU D 3 N GLU D 29
SHEET 3 DA 4 VAL D 54 ASP D 59 -1 O ALA D 56 N TYR D 6
SHEET 4 DA 4 ASP D 61 LEU D 64 -1 O PHE D 62 N ASP D 59
CISPEP 1 VAL A 54 PRO A 55 0 0.59
CISPEP 2 VAL B 54 PRO B 55 0 0.48
CISPEP 3 VAL C 54 PRO C 55 0 0.80
CISPEP 4 VAL D 54 PRO D 55 0 0.28
CRYST1 164.524 111.822 55.924 90.00 90.00 90.00 P 21 21 2 16
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 0.006078 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017881 0.00000
MTRIX1 1 0.968587 -0.183150 -0.168211 9.99224 1
MTRIX2 1 -0.183345 -0.982942 0.014507 54.59685 1
MTRIX3 1 -0.167998 0.016790 -0.985644 57.82712 1
MTRIX1 2 -0.979651 0.132596 0.150673 159.11601 1
MTRIX2 2 0.090234 0.961524 -0.259478 7.89670 1
MTRIX3 2 -0.179281 -0.240602 -0.953923 91.50109 1
MTRIX1 3 -0.998501 0.051620 0.018206 165.27914 1
MTRIX2 3 -0.045300 -0.966004 0.254527 46.28961 1
MTRIX3 3 0.030725 0.253321 0.966894 21.41075 1
(ATOM LINES ARE NOT SHOWN.)
END
