HEADER TRANSFERASE(GLUTATHIONE) 15-OCT-93 1HNC
TITLE CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2:
TITLE 2 EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TRANSFERASE(GLUTATHIONE)
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RAGHUNATHAN,R.J.CHANDROSS,R.H.KRETSINGER,T.J.ALLISON,C.J.PENINGTON,
AUTHOR 2 G.S.RULE
REVDAT 5 07-FEB-24 1HNC 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1HNC 1 VERSN
REVDAT 3 01-APR-03 1HNC 1 JRNL
REVDAT 2 15-JAN-95 1HNC 1 JRNL
REVDAT 1 31-JAN-94 1HNC 0
JRNL AUTH S.RAGHUNATHAN,R.J.CHANDROSS,R.H.KRETSINGER,T.J.ALLISON,
JRNL AUTH 2 C.J.PENINGTON,G.S.RULE
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE
JRNL TITL 2 GSTM2-2. EFFECTS OF LATTICE PACKING ON CONFORMATIONAL
JRNL TITL 3 HETEROGENEITY.
JRNL REF J.MOL.BIOL. V. 238 815 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8182750
JRNL DOI 10.1006/JMBI.1994.1336
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.R.PENINGTON,G.S.RULE
REMARK 1 TITL MAPPING OF THE SUBSTRATE-BINDING SITE OF A HUMAN CLASS MU
REMARK 1 TITL 2 GLUTATHIONE TRANSFERASE USING NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 31 2912 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.R.VORACHEK,W.R.PEARSON,G.S.RULE
REMARK 1 TITL CLONING, EXPRESSION, AND CHARACTERIZATION OF A CLASS MU
REMARK 1 TITL 2 GLUTATHIONE TRANSFERASE FROM HUMAN MUSCLE, THE PRODUCT OF
REMARK 1 TITL 3 THE GST4 LOCUS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 88 443 1991
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 18827
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.110
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE ELECTRON DENSITY FOR RESIDUES 203 - 217 IS POORLY
REMARK 3 DEFINED.
REMARK 3
REMARK 3 THE TEMPERATURE FACTORS WERE NOT REFINED TO CONVERGENCE.
REMARK 4
REMARK 4 1HNC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 28.46800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.03550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.03550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.46800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.83500
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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 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 PRO A 1 CA - N - CD ANGL. DEV. = -10.4 DEGREES
REMARK 500 PRO B 1 CA - N - CD ANGL. DEV. = -10.8 DEGREES
REMARK 500 PRO C 1 CA - N - CD ANGL. DEV. = -11.0 DEGREES
REMARK 500 PRO D 1 CA - N - CD ANGL. DEV. = -10.9 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 ARG A 10 -74.25 -54.35
REMARK 500 ASP A 24 13.97 57.45
REMARK 500 TYR A 40 71.08 48.17
REMARK 500 ASP A 41 89.81 -69.56
REMARK 500 GLN A 71 120.68 70.82
REMARK 500 SER A 72 -69.88 -28.93
REMARK 500 ASN A 84 19.92 59.24
REMARK 500 LEU A 85 38.59 -90.60
REMARK 500 GLU A 88 -74.10 -87.00
REMARK 500 ASP A 118 43.58 -88.13
REMARK 500 GLN A 128 28.43 -79.86
REMARK 500 ALA A 129 -23.38 -147.41
REMARK 500 GLU A 170 83.10 -157.16
REMARK 500 PRO A 206 2.89 -59.57
REMARK 500 MET A 211 -34.15 -148.03
REMARK 500 ALA A 212 -53.73 -166.49
REMARK 500 ARG B 10 -70.72 -61.55
REMARK 500 TYR B 40 75.61 -67.30
REMARK 500 SER B 43 -92.37 -138.43
REMARK 500 GLU B 48 -60.74 -95.78
REMARK 500 LYS B 49 -75.64 10.85
REMARK 500 GLN B 71 112.46 73.43
REMARK 500 LEU B 85 49.23 -98.49
REMARK 500 ASP B 118 3.23 -67.30
REMARK 500 GLU B 170 97.07 -161.73
REMARK 500 GLU B 191 -61.80 -29.50
REMARK 500 ARG B 201 9.32 174.47
REMARK 500 PHE B 202 -72.73 -82.84
REMARK 500 VAL B 207 -74.24 -68.66
REMARK 500 LYS B 210 -48.32 73.84
REMARK 500 ASN C 8 48.49 -78.56
REMARK 500 ARG C 42 40.65 -89.58
REMARK 500 GLU C 48 14.96 -145.89
REMARK 500 GLN C 71 124.64 75.93
REMARK 500 LEU C 85 48.02 -84.38
REMARK 500 GLU C 88 -74.08 -94.82
REMARK 500 LEU C 148 2.87 90.29
REMARK 500 GLU C 170 92.59 -167.19
REMARK 500 SER C 172 -17.76 -49.39
REMARK 500 PRO C 178 -74.79 -55.96
REMARK 500 SER C 199 -166.42 -77.12
REMARK 500 THR C 209 103.84 -37.23
REMARK 500 LYS C 210 -47.60 72.21
REMARK 500 ALA C 212 55.00 -165.75
REMARK 500 MET D 34 -70.96 -151.45
REMARK 500 PRO D 38 11.65 -56.39
REMARK 500 TYR D 40 99.56 -63.81
REMARK 500 ARG D 42 -45.54 48.83
REMARK 500 SER D 43 -42.73 -16.54
REMARK 500 ASN D 47 23.71 -69.80
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ALTHOUGH CRYSTALS WERE GROWN IN THE PRESENCE OF
REMARK 600 GLUTATHIONE S-(2,4 DINITROBENZENE), ONLY THE GLUTATHIONE
REMARK 600 PORTION HAS OBSERVABLE DENSITY. COORDINATES ARE REPORTED
REMARK 600 FOR THE GLUTATHIONE PORTION ONLY (RESIDUE GDN).
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GDN A 218
REMARK 610 GDN B 218
REMARK 610 GDN C 218
REMARK 610 GDN D 218
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDN A 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDN B 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDN C 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDN D 218
DBREF 1HNC A 1 217 UNP P28161 GSTM2_HUMAN 1 217
DBREF 1HNC B 1 217 UNP P28161 GSTM2_HUMAN 1 217
DBREF 1HNC C 1 217 UNP P28161 GSTM2_HUMAN 1 217
DBREF 1HNC D 1 217 UNP P28161 GSTM2_HUMAN 1 217
SEQADV 1HNC PHE A 214 UNP P28161 TRP 214 CONFLICT
SEQADV 1HNC PHE B 214 UNP P28161 TRP 214 CONFLICT
SEQADV 1HNC PHE C 214 UNP P28161 TRP 214 CONFLICT
SEQADV 1HNC PHE D 214 UNP P28161 TRP 214 CONFLICT
SEQRES 1 A 217 PRO MET THR LEU GLY TYR TRP ASN ILE ARG GLY LEU ALA
SEQRES 2 A 217 HIS SER ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES 3 A 217 TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO ASP
SEQRES 4 A 217 TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 A 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES 6 A 217 THR HIS LYS ILE THR GLN SER ASN ALA ILE LEU ARG TYR
SEQRES 7 A 217 ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU SER GLU LYS
SEQRES 8 A 217 GLU GLN ILE ARG GLU ASP ILE LEU GLU ASN GLN PHE MET
SEQRES 9 A 217 ASP SER ARG MET GLN LEU ALA LYS LEU CYS TYR ASP PRO
SEQRES 10 A 217 ASP PHE GLU LYS LEU LYS PRO GLU TYR LEU GLN ALA LEU
SEQRES 11 A 217 PRO GLU MET LEU LYS LEU TYR SER GLN PHE LEU GLY LYS
SEQRES 12 A 217 GLN PRO TRP PHE LEU GLY ASP LYS ILE THR PHE VAL ASP
SEQRES 13 A 217 PHE ILE ALA TYR ASP VAL LEU GLU ARG ASN GLN VAL PHE
SEQRES 14 A 217 GLU PRO SER CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES 15 A 217 PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER ALA
SEQRES 16 A 217 TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL PHE
SEQRES 17 A 217 THR LYS MET ALA VAL PHE GLY ASN LYS
SEQRES 1 B 217 PRO MET THR LEU GLY TYR TRP ASN ILE ARG GLY LEU ALA
SEQRES 2 B 217 HIS SER ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES 3 B 217 TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO ASP
SEQRES 4 B 217 TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 B 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES 6 B 217 THR HIS LYS ILE THR GLN SER ASN ALA ILE LEU ARG TYR
SEQRES 7 B 217 ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU SER GLU LYS
SEQRES 8 B 217 GLU GLN ILE ARG GLU ASP ILE LEU GLU ASN GLN PHE MET
SEQRES 9 B 217 ASP SER ARG MET GLN LEU ALA LYS LEU CYS TYR ASP PRO
SEQRES 10 B 217 ASP PHE GLU LYS LEU LYS PRO GLU TYR LEU GLN ALA LEU
SEQRES 11 B 217 PRO GLU MET LEU LYS LEU TYR SER GLN PHE LEU GLY LYS
SEQRES 12 B 217 GLN PRO TRP PHE LEU GLY ASP LYS ILE THR PHE VAL ASP
SEQRES 13 B 217 PHE ILE ALA TYR ASP VAL LEU GLU ARG ASN GLN VAL PHE
SEQRES 14 B 217 GLU PRO SER CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES 15 B 217 PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER ALA
SEQRES 16 B 217 TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL PHE
SEQRES 17 B 217 THR LYS MET ALA VAL PHE GLY ASN LYS
SEQRES 1 C 217 PRO MET THR LEU GLY TYR TRP ASN ILE ARG GLY LEU ALA
SEQRES 2 C 217 HIS SER ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES 3 C 217 TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO ASP
SEQRES 4 C 217 TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 C 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES 6 C 217 THR HIS LYS ILE THR GLN SER ASN ALA ILE LEU ARG TYR
SEQRES 7 C 217 ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU SER GLU LYS
SEQRES 8 C 217 GLU GLN ILE ARG GLU ASP ILE LEU GLU ASN GLN PHE MET
SEQRES 9 C 217 ASP SER ARG MET GLN LEU ALA LYS LEU CYS TYR ASP PRO
SEQRES 10 C 217 ASP PHE GLU LYS LEU LYS PRO GLU TYR LEU GLN ALA LEU
SEQRES 11 C 217 PRO GLU MET LEU LYS LEU TYR SER GLN PHE LEU GLY LYS
SEQRES 12 C 217 GLN PRO TRP PHE LEU GLY ASP LYS ILE THR PHE VAL ASP
SEQRES 13 C 217 PHE ILE ALA TYR ASP VAL LEU GLU ARG ASN GLN VAL PHE
SEQRES 14 C 217 GLU PRO SER CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES 15 C 217 PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER ALA
SEQRES 16 C 217 TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL PHE
SEQRES 17 C 217 THR LYS MET ALA VAL PHE GLY ASN LYS
SEQRES 1 D 217 PRO MET THR LEU GLY TYR TRP ASN ILE ARG GLY LEU ALA
SEQRES 2 D 217 HIS SER ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES 3 D 217 TYR GLU GLU LYS LYS TYR THR MET GLY ASP ALA PRO ASP
SEQRES 4 D 217 TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES 5 D 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES 6 D 217 THR HIS LYS ILE THR GLN SER ASN ALA ILE LEU ARG TYR
SEQRES 7 D 217 ILE ALA ARG LYS HIS ASN LEU CYS GLY GLU SER GLU LYS
SEQRES 8 D 217 GLU GLN ILE ARG GLU ASP ILE LEU GLU ASN GLN PHE MET
SEQRES 9 D 217 ASP SER ARG MET GLN LEU ALA LYS LEU CYS TYR ASP PRO
SEQRES 10 D 217 ASP PHE GLU LYS LEU LYS PRO GLU TYR LEU GLN ALA LEU
SEQRES 11 D 217 PRO GLU MET LEU LYS LEU TYR SER GLN PHE LEU GLY LYS
SEQRES 12 D 217 GLN PRO TRP PHE LEU GLY ASP LYS ILE THR PHE VAL ASP
SEQRES 13 D 217 PHE ILE ALA TYR ASP VAL LEU GLU ARG ASN GLN VAL PHE
SEQRES 14 D 217 GLU PRO SER CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES 15 D 217 PHE ILE SER ARG PHE GLU GLY LEU GLU LYS ILE SER ALA
SEQRES 16 D 217 TYR MET LYS SER SER ARG PHE LEU PRO ARG PRO VAL PHE
SEQRES 17 D 217 THR LYS MET ALA VAL PHE GLY ASN LYS
HET GDN A 218 20
HET GDN B 218 20
HET GDN C 218 20
HET GDN D 218 20
HETNAM GDN GLUTATHIONE S-(2,4 DINITROBENZENE)
FORMUL 5 GDN 4(C16 H19 N5 O10 S)
HELIX 1 1 LEU A 12 THR A 23 1 12
HELIX 2 2 ARG A 42 PHE A 50 1 9
HELIX 3 3 GLN A 71 LYS A 82 1 12
HELIX 4 4 SER A 89 CYS A 114 1 26
HELIX 5 5 ASP A 118 GLN A 128 1 11
HELIX 6 6 ALA A 129 GLY A 142 1 14
HELIX 7 7 THR A 153 GLU A 170 1 18
HELIX 8 8 PRO A 171 ALA A 176 5 6
HELIX 9 9 PHE A 177 LEU A 190 1 14
HELIX 10 10 LEU A 190 LYS A 198 1 9
HELIX 11 11 LEU B 12 THR B 23 1 12
HELIX 12 12 SER B 43 LYS B 49 1 7
HELIX 13 13 PHE B 50 GLY B 53 5 4
HELIX 14 14 GLN B 71 HIS B 83 1 13
HELIX 15 15 SER B 89 TYR B 115 1 27
HELIX 16 16 ASP B 118 GLY B 142 1 25
HELIX 17 17 THR B 153 GLU B 170 1 18
HELIX 18 18 PRO B 171 ALA B 176 5 6
HELIX 19 19 PHE B 177 GLY B 189 1 13
HELIX 20 20 LEU B 190 SER B 199 1 10
HELIX 21 21 VAL B 207 ALA B 212 1 6
HELIX 22 22 ARG C 10 LEU C 12 5 3
HELIX 23 23 ALA C 13 THR C 23 1 11
HELIX 24 24 ARG C 42 ASN C 47 1 6
HELIX 25 25 GLN C 71 HIS C 83 1 13
HELIX 26 26 SER C 89 ASP C 116 1 28
HELIX 27 27 ASP C 118 GLU C 120 5 3
HELIX 28 28 LYS C 121 GLY C 142 1 22
HELIX 29 29 THR C 153 GLU C 170 1 18
HELIX 30 30 GLU C 170 ASP C 175 1 6
HELIX 31 31 PHE C 177 GLY C 189 1 13
HELIX 32 32 LEU C 190 SER C 199 1 10
HELIX 33 33 LEU D 12 THR D 23 1 12
HELIX 34 34 TRP D 45 LYS D 49 5 5
HELIX 35 35 GLN D 71 HIS D 83 1 13
HELIX 36 36 SER D 89 TYR D 115 1 27
HELIX 37 37 ASP D 118 GLN D 128 1 11
HELIX 38 38 ALA D 129 GLY D 142 1 14
HELIX 39 39 VAL D 155 GLU D 170 1 16
HELIX 40 40 SER D 172 ALA D 176 5 5
HELIX 41 41 PHE D 177 LEU D 190 1 14
HELIX 42 42 LEU D 190 LYS D 198 1 9
SHEET 1 A 4 TYR A 27 GLU A 29 0
SHEET 2 A 4 MET A 2 GLY A 5 1 O MET A 2 N GLU A 28
SHEET 3 A 4 TYR A 61 ASP A 64 -1 O TYR A 61 N GLY A 5
SHEET 4 A 4 HIS A 67 THR A 70 -1 N HIS A 67 O ASP A 64
SHEET 1 B 4 TYR B 27 TYR B 32 0
SHEET 2 B 4 MET B 2 TRP B 7 1 O MET B 2 N GLU B 28
SHEET 3 B 4 TYR B 61 ASP B 64 -1 O TYR B 61 N GLY B 5
SHEET 4 B 4 HIS B 67 THR B 70 -1 N HIS B 67 O ASP B 64
SHEET 1 C 4 TYR C 27 TYR C 32 0
SHEET 2 C 4 MET C 2 TRP C 7 1 O MET C 2 N GLU C 28
SHEET 3 C 4 TYR C 61 ASP C 64 -1 O TYR C 61 N GLY C 5
SHEET 4 C 4 HIS C 67 THR C 70 -1 O HIS C 67 N ASP C 64
SHEET 1 D 4 TYR D 27 TYR D 32 0
SHEET 2 D 4 MET D 2 TRP D 7 1 O MET D 2 N GLU D 28
SHEET 3 D 4 TYR D 61 ASP D 64 -1 O TYR D 61 N GLY D 5
SHEET 4 D 4 HIS D 67 THR D 70 -1 O HIS D 67 N ASP D 64
CISPEP 1 LEU A 59 PRO A 60 0 0.34
CISPEP 2 LEU B 59 PRO B 60 0 0.15
CISPEP 3 LEU C 59 PRO C 60 0 2.35
CISPEP 4 LEU D 59 PRO D 60 0 0.91
SITE 1 AC1 11 TYR A 6 TRP A 7 LEU A 12 TRP A 45
SITE 2 AC1 11 ASN A 58 LEU A 59 PRO A 60 GLN A 71
SITE 3 AC1 11 SER A 72 MET A 211 ASP B 105
SITE 1 AC2 11 ASP A 105 TYR B 6 TRP B 7 LEU B 12
SITE 2 AC2 11 TRP B 45 ASN B 58 LEU B 59 GLN B 71
SITE 3 AC2 11 SER B 72 MET B 104 TYR B 115
SITE 1 AC3 11 TRP C 7 LEU C 12 ARG C 42 TRP C 45
SITE 2 AC3 11 LYS C 49 ASN C 58 LEU C 59 GLN C 71
SITE 3 AC3 11 SER C 72 MET C 211 ASP D 105
SITE 1 AC4 10 ASP C 105 TYR D 6 TRP D 7 LEU D 12
SITE 2 AC4 10 TRP D 45 LYS D 49 ASN D 58 LEU D 59
SITE 3 AC4 10 GLN D 71 SER D 72
CRYST1 56.936 79.670 220.071 90.00 90.00 90.00 P 21 21 21 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 0.017564 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004544 0.00000
(ATOM LINES ARE NOT SHOWN.)
END