HEADER TRANSFERASE 24-JUN-06 2DSA
TITLE TERNARY COMPLEX OF BPHK, A BACTERIAL GST
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: BURKHOLDERIA XENOVORANS;
SOURCE 3 ORGANISM_TAXID: 266265;
SOURCE 4 STRAIN: LB400;
SOURCE 5 GENE: BPHK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GJ1158
KEYWDS GLUTATHIONE S-TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.I.TOCHEVA,M.E.P.MURPHY
REVDAT 5 25-OCT-23 2DSA 1 REMARK
REVDAT 4 07-DEC-11 2DSA 1 HET HETATM HETNAM
REVDAT 3 13-JUL-11 2DSA 1 VERSN
REVDAT 2 09-DEC-08 2DSA 1 JRNL VERSN
REVDAT 1 22-AUG-06 2DSA 0
JRNL AUTH E.I.TOCHEVA,P.D.FORTIN,L.D.ELTIS,M.E.P.MURPHY
JRNL TITL STRUCTURES OF TERNARY COMPLEXES OF BPHK, A BACTERIAL
JRNL TITL 2 GLUTATHIONE S-TRANSFERASE THAT REDUCTIVELY DECHLORINATES
JRNL TITL 3 POLYCHLORINATED BIPHENYL METABOLITES
JRNL REF J.BIOL.CHEM. V. 281 30933 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16920719
JRNL DOI 10.1074/JBC.M603125200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 54562
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2918
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3778
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6224
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 144
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 0.62000
REMARK 3 B12 (A**2) : -0.21000
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): 0.213
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.356
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6520 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8868 ; 1.259 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 796 ; 5.111 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 300 ;42.091 ;24.400
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 992 ;16.539 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;20.331 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 952 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5128 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3037 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4481 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 292 ; 0.141 ; 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): 51 ; 0.247 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.062 ; 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): 4077 ; 0.665 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6368 ; 1.180 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2793 ; 1.495 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2500 ; 2.376 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2DSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000025783.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54562
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05800
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1F2E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M K/NA TARTRATE, 0.1M MES, PH 6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.10000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.38935
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.96667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 56.10000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 32.38935
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 73.96667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 56.10000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 32.38935
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 73.96667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.77870
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 147.93333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 64.77870
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 147.93333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 64.77870
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 147.93333
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: 5640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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: 5670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 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 ILE A 201
REMARK 465 LYS A 202
REMARK 465 GLU A 203
REMARK 465 ILE B 201
REMARK 465 LYS B 202
REMARK 465 GLU B 203
REMARK 465 ILE C 201
REMARK 465 LYS C 202
REMARK 465 GLU C 203
REMARK 465 ILE D 201
REMARK 465 LYS D 202
REMARK 465 GLU D 203
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LYS C 80 O HOH C 3261 2.08
REMARK 500 O LYS A 80 O HOH A 1255 2.11
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 65 113.38 74.86
REMARK 500 LEU B 32 1.88 -68.58
REMARK 500 GLU B 65 115.95 69.64
REMARK 500 LEU B 105 -74.62 -111.46
REMARK 500 GLU C 65 112.66 74.44
REMARK 500 VAL D 46 -67.44 -91.73
REMARK 500 GLU D 65 119.17 66.42
REMARK 500 LEU D 105 -74.54 -111.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 2224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C 3224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH D 4224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPX A 1225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPX B 2225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPX C 3225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPX D 4225
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GDR RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF BPHK, A BACTERIAL GST.
REMARK 900 RELATED ID: 1PMT RELATED DB: PDB
REMARK 900 GST FROM P. MIRABILIS
REMARK 900 RELATED ID: 1F2E RELATED DB: PDB
REMARK 900 GST FROM S. PAUCIMOBILIS
REMARK 900 RELATED ID: 1A0F RELATED DB: PDB
REMARK 900 GST FROM E.COLI
DBREF 2DSA A 1 203 UNP Q9RAF0 Q9RAF0_9RALS 1 187
DBREF 2DSA B 1 203 UNP Q9RAF0 Q9RAF0_9RALS 1 187
DBREF 2DSA C 1 203 UNP Q9RAF0 Q9RAF0_9RALS 1 187
DBREF 2DSA D 1 203 UNP Q9RAF0 Q9RAF0_9RALS 1 187
SEQRES 1 A 203 MET LYS LEU TYR TYR SER PRO GLY ALA CYS SER LEU SER
SEQRES 2 A 203 PRO HIS ILE ALA LEU ARG GLU ALA GLY LEU ASN PHE GLU
SEQRES 3 A 203 LEU VAL GLN VAL ASP LEU ALA SER LYS LYS THR ALA SER
SEQRES 4 A 203 GLY GLN ASP TYR LEU GLU VAL ASN PRO ALA GLY TYR VAL
SEQRES 5 A 203 PRO CYS LEU GLN LEU ASP ASP GLY ARG THR LEU THR GLU
SEQRES 6 A 203 GLY PRO ALA ILE VAL GLN TYR VAL ALA ASP GLN VAL PRO
SEQRES 7 A 203 GLY LYS GLN LEU ALA PRO ALA ASN GLY SER PHE GLU ARG
SEQRES 8 A 203 TYR HIS LEU GLN GLN TRP LEU ASN PHE ILE SER SER GLU
SEQRES 9 A 203 LEU HIS LYS SER PHE SER PRO LEU PHE ASN PRO ALA SER
SEQRES 10 A 203 SER ASP GLU TRP LYS ASN ALA VAL ARG GLN SER LEU ASN
SEQRES 11 A 203 THR ARG LEU GLY GLN VAL ALA ARG GLN LEU GLU HIS ALA
SEQRES 12 A 203 PRO TYR LEU LEU GLY ASP GLN LEU SER VAL ALA ASP ILE
SEQRES 13 A 203 TYR LEU PHE VAL VAL LEU GLY TRP SER ALA TYR VAL ASN
SEQRES 14 A 203 ILE ASP LEU SER PRO TRP PRO SER LEU GLN ALA PHE GLN
SEQRES 15 A 203 GLY ARG VAL GLY GLY ARG GLU ALA VAL GLN SER ALA LEU
SEQRES 16 A 203 ARG ALA GLU GLY LEU ILE LYS GLU
SEQRES 1 B 203 MET LYS LEU TYR TYR SER PRO GLY ALA CYS SER LEU SER
SEQRES 2 B 203 PRO HIS ILE ALA LEU ARG GLU ALA GLY LEU ASN PHE GLU
SEQRES 3 B 203 LEU VAL GLN VAL ASP LEU ALA SER LYS LYS THR ALA SER
SEQRES 4 B 203 GLY GLN ASP TYR LEU GLU VAL ASN PRO ALA GLY TYR VAL
SEQRES 5 B 203 PRO CYS LEU GLN LEU ASP ASP GLY ARG THR LEU THR GLU
SEQRES 6 B 203 GLY PRO ALA ILE VAL GLN TYR VAL ALA ASP GLN VAL PRO
SEQRES 7 B 203 GLY LYS GLN LEU ALA PRO ALA ASN GLY SER PHE GLU ARG
SEQRES 8 B 203 TYR HIS LEU GLN GLN TRP LEU ASN PHE ILE SER SER GLU
SEQRES 9 B 203 LEU HIS LYS SER PHE SER PRO LEU PHE ASN PRO ALA SER
SEQRES 10 B 203 SER ASP GLU TRP LYS ASN ALA VAL ARG GLN SER LEU ASN
SEQRES 11 B 203 THR ARG LEU GLY GLN VAL ALA ARG GLN LEU GLU HIS ALA
SEQRES 12 B 203 PRO TYR LEU LEU GLY ASP GLN LEU SER VAL ALA ASP ILE
SEQRES 13 B 203 TYR LEU PHE VAL VAL LEU GLY TRP SER ALA TYR VAL ASN
SEQRES 14 B 203 ILE ASP LEU SER PRO TRP PRO SER LEU GLN ALA PHE GLN
SEQRES 15 B 203 GLY ARG VAL GLY GLY ARG GLU ALA VAL GLN SER ALA LEU
SEQRES 16 B 203 ARG ALA GLU GLY LEU ILE LYS GLU
SEQRES 1 C 203 MET LYS LEU TYR TYR SER PRO GLY ALA CYS SER LEU SER
SEQRES 2 C 203 PRO HIS ILE ALA LEU ARG GLU ALA GLY LEU ASN PHE GLU
SEQRES 3 C 203 LEU VAL GLN VAL ASP LEU ALA SER LYS LYS THR ALA SER
SEQRES 4 C 203 GLY GLN ASP TYR LEU GLU VAL ASN PRO ALA GLY TYR VAL
SEQRES 5 C 203 PRO CYS LEU GLN LEU ASP ASP GLY ARG THR LEU THR GLU
SEQRES 6 C 203 GLY PRO ALA ILE VAL GLN TYR VAL ALA ASP GLN VAL PRO
SEQRES 7 C 203 GLY LYS GLN LEU ALA PRO ALA ASN GLY SER PHE GLU ARG
SEQRES 8 C 203 TYR HIS LEU GLN GLN TRP LEU ASN PHE ILE SER SER GLU
SEQRES 9 C 203 LEU HIS LYS SER PHE SER PRO LEU PHE ASN PRO ALA SER
SEQRES 10 C 203 SER ASP GLU TRP LYS ASN ALA VAL ARG GLN SER LEU ASN
SEQRES 11 C 203 THR ARG LEU GLY GLN VAL ALA ARG GLN LEU GLU HIS ALA
SEQRES 12 C 203 PRO TYR LEU LEU GLY ASP GLN LEU SER VAL ALA ASP ILE
SEQRES 13 C 203 TYR LEU PHE VAL VAL LEU GLY TRP SER ALA TYR VAL ASN
SEQRES 14 C 203 ILE ASP LEU SER PRO TRP PRO SER LEU GLN ALA PHE GLN
SEQRES 15 C 203 GLY ARG VAL GLY GLY ARG GLU ALA VAL GLN SER ALA LEU
SEQRES 16 C 203 ARG ALA GLU GLY LEU ILE LYS GLU
SEQRES 1 D 203 MET LYS LEU TYR TYR SER PRO GLY ALA CYS SER LEU SER
SEQRES 2 D 203 PRO HIS ILE ALA LEU ARG GLU ALA GLY LEU ASN PHE GLU
SEQRES 3 D 203 LEU VAL GLN VAL ASP LEU ALA SER LYS LYS THR ALA SER
SEQRES 4 D 203 GLY GLN ASP TYR LEU GLU VAL ASN PRO ALA GLY TYR VAL
SEQRES 5 D 203 PRO CYS LEU GLN LEU ASP ASP GLY ARG THR LEU THR GLU
SEQRES 6 D 203 GLY PRO ALA ILE VAL GLN TYR VAL ALA ASP GLN VAL PRO
SEQRES 7 D 203 GLY LYS GLN LEU ALA PRO ALA ASN GLY SER PHE GLU ARG
SEQRES 8 D 203 TYR HIS LEU GLN GLN TRP LEU ASN PHE ILE SER SER GLU
SEQRES 9 D 203 LEU HIS LYS SER PHE SER PRO LEU PHE ASN PRO ALA SER
SEQRES 10 D 203 SER ASP GLU TRP LYS ASN ALA VAL ARG GLN SER LEU ASN
SEQRES 11 D 203 THR ARG LEU GLY GLN VAL ALA ARG GLN LEU GLU HIS ALA
SEQRES 12 D 203 PRO TYR LEU LEU GLY ASP GLN LEU SER VAL ALA ASP ILE
SEQRES 13 D 203 TYR LEU PHE VAL VAL LEU GLY TRP SER ALA TYR VAL ASN
SEQRES 14 D 203 ILE ASP LEU SER PRO TRP PRO SER LEU GLN ALA PHE GLN
SEQRES 15 D 203 GLY ARG VAL GLY GLY ARG GLU ALA VAL GLN SER ALA LEU
SEQRES 16 D 203 ARG ALA GLU GLY LEU ILE LYS GLU
HET GSH A1224 20
HET HPX A1225 16
HET GSH B2224 20
HET HPX B2225 16
HET GSH C3224 20
HET HPX C3225 16
HET GSH D4224 20
HET HPX D4225 16
HETNAM GSH GLUTATHIONE
HETNAM HPX (2Z,4E)-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC ACID
FORMUL 5 GSH 4(C10 H17 N3 O6 S)
FORMUL 6 HPX 4(C12 H10 O4)
FORMUL 13 HOH *205(H2 O)
HELIX 1 1 SER A 11 GLY A 22 1 12
HELIX 2 2 ASP A 42 VAL A 46 5 5
HELIX 3 3 GLU A 65 VAL A 77 1 13
HELIX 4 4 PRO A 78 GLN A 81 5 4
HELIX 5 5 SER A 88 LEU A 105 1 18
HELIX 6 6 LEU A 105 SER A 110 1 6
HELIX 7 7 PRO A 111 ASN A 114 5 4
HELIX 8 8 SER A 118 LEU A 140 1 23
HELIX 9 9 SER A 152 TRP A 164 1 13
HELIX 10 10 SER A 165 TYR A 167 5 3
HELIX 11 11 TRP A 175 GLY A 187 1 13
HELIX 12 12 ARG A 188 GLU A 198 1 11
HELIX 13 13 SER B 11 GLY B 22 1 12
HELIX 14 14 ASP B 42 VAL B 46 5 5
HELIX 15 15 GLU B 65 VAL B 77 1 13
HELIX 16 16 PRO B 78 GLN B 81 5 4
HELIX 17 17 SER B 88 LEU B 105 1 18
HELIX 18 18 LEU B 105 SER B 110 1 6
HELIX 19 19 PRO B 111 PHE B 113 5 3
HELIX 20 20 SER B 118 ALA B 143 1 26
HELIX 21 21 SER B 152 GLY B 163 1 12
HELIX 22 22 TRP B 164 VAL B 168 5 5
HELIX 23 23 TRP B 175 GLY B 187 1 13
HELIX 24 24 ARG B 188 GLU B 198 1 11
HELIX 25 25 SER C 11 GLY C 22 1 12
HELIX 26 26 ASP C 42 VAL C 46 5 5
HELIX 27 27 GLU C 65 GLN C 76 1 12
HELIX 28 28 VAL C 77 GLN C 81 5 5
HELIX 29 29 SER C 88 LEU C 105 1 18
HELIX 30 30 LEU C 105 SER C 110 1 6
HELIX 31 31 PRO C 111 ASN C 114 5 4
HELIX 32 32 SER C 118 LEU C 140 1 23
HELIX 33 33 SER C 152 GLY C 163 1 12
HELIX 34 34 TRP C 175 GLY C 187 1 13
HELIX 35 35 ARG C 188 GLU C 198 1 11
HELIX 36 36 SER D 11 GLY D 22 1 12
HELIX 37 37 ASP D 42 VAL D 46 5 5
HELIX 38 38 GLU D 65 VAL D 77 1 13
HELIX 39 39 PRO D 78 GLN D 81 5 4
HELIX 40 40 SER D 88 LEU D 105 1 18
HELIX 41 41 LEU D 105 ASN D 114 1 10
HELIX 42 42 SER D 118 ALA D 143 1 26
HELIX 43 43 SER D 152 GLY D 163 1 12
HELIX 44 44 TRP D 164 ASN D 169 5 6
HELIX 45 45 TRP D 175 GLY D 187 1 13
HELIX 46 46 ARG D 188 GLY D 199 1 12
SHEET 1 A 5 LYS A 36 THR A 37 0
SHEET 2 A 5 GLU A 26 ASP A 31 -1 N ASP A 31 O LYS A 36
SHEET 3 A 5 LYS A 2 TYR A 5 1 N LEU A 3 O VAL A 28
SHEET 4 A 5 CYS A 54 GLN A 56 -1 O GLN A 56 N LYS A 2
SHEET 5 A 5 THR A 62 THR A 64 -1 O LEU A 63 N LEU A 55
SHEET 1 B 5 LYS B 36 THR B 37 0
SHEET 2 B 5 GLU B 26 ASP B 31 -1 N ASP B 31 O LYS B 36
SHEET 3 B 5 LYS B 2 TYR B 5 1 N TYR B 5 O VAL B 28
SHEET 4 B 5 CYS B 54 GLN B 56 -1 O GLN B 56 N LYS B 2
SHEET 5 B 5 THR B 62 THR B 64 -1 O LEU B 63 N LEU B 55
SHEET 1 C 5 LYS C 36 THR C 37 0
SHEET 2 C 5 GLU C 26 ASP C 31 -1 N ASP C 31 O LYS C 36
SHEET 3 C 5 LYS C 2 TYR C 5 1 N LEU C 3 O VAL C 28
SHEET 4 C 5 CYS C 54 GLN C 56 -1 O GLN C 56 N LYS C 2
SHEET 5 C 5 THR C 62 THR C 64 -1 O LEU C 63 N LEU C 55
SHEET 1 D 5 LYS D 36 THR D 37 0
SHEET 2 D 5 GLU D 26 ASP D 31 -1 N ASP D 31 O LYS D 36
SHEET 3 D 5 LYS D 2 TYR D 5 1 N LEU D 3 O VAL D 28
SHEET 4 D 5 CYS D 54 GLN D 56 -1 O GLN D 56 N LYS D 2
SHEET 5 D 5 THR D 62 THR D 64 -1 O LEU D 63 N LEU D 55
CISPEP 1 VAL A 52 PRO A 53 0 -3.07
CISPEP 2 VAL B 52 PRO B 53 0 3.19
CISPEP 3 VAL C 52 PRO C 53 0 -2.20
CISPEP 4 VAL D 52 PRO D 53 0 2.52
SITE 1 AC1 16 CYS A 10 LEU A 32 LYS A 35 TYR A 51
SITE 2 AC1 16 VAL A 52 GLU A 65 GLY A 66 HIS A 106
SITE 3 AC1 16 LYS A 107 HPX A1225 HOH A1226 HOH A1232
SITE 4 AC1 16 HOH A1239 ASN B 99 SER B 103 GLU B 104
SITE 1 AC2 15 ASN A 99 SER A 103 GLU A 104 ALA B 9
SITE 2 AC2 15 CYS B 10 LEU B 32 TYR B 51 VAL B 52
SITE 3 AC2 15 GLU B 65 GLY B 66 HIS B 106 HPX B2225
SITE 4 AC2 15 HOH B2228 HOH B2243 HOH B2244
SITE 1 AC3 15 CYS C 10 LYS C 35 TYR C 51 VAL C 52
SITE 2 AC3 15 GLU C 65 GLY C 66 HIS C 106 HPX C3225
SITE 3 AC3 15 HOH C3226 HOH C3233 HOH C3241 HOH C3274
SITE 4 AC3 15 ASN D 99 SER D 103 GLU D 104
SITE 1 AC4 14 ASN C 99 SER C 103 GLU C 104 CYS D 10
SITE 2 AC4 14 LEU D 32 LYS D 35 TYR D 51 VAL D 52
SITE 3 AC4 14 GLU D 65 GLY D 66 HIS D 106 HPX D4225
SITE 4 AC4 14 HOH D4229 HOH D4239
SITE 1 AC5 8 PRO A 7 GLY A 8 HIS A 106 SER A 110
SITE 2 AC5 8 PHE A 113 TRP A 164 TYR A 167 GSH A1224
SITE 1 AC6 8 PRO B 7 GLY B 8 ALA B 9 SER B 39
SITE 2 AC6 8 HIS B 106 SER B 110 TYR B 167 GSH B2224
SITE 1 AC7 9 PRO C 7 GLY C 8 ALA C 9 HIS C 106
SITE 2 AC7 9 SER C 110 PHE C 113 TRP C 164 TYR C 167
SITE 3 AC7 9 GSH C3224
SITE 1 AC8 9 PRO D 7 GLY D 8 ALA D 9 SER D 39
SITE 2 AC8 9 HIS D 106 SER D 110 TRP D 164 TYR D 167
SITE 3 AC8 9 GSH D4224
CRYST1 112.200 112.200 221.900 90.00 90.00 120.00 H 3 36
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 0.008912 0.005145 0.000000 0.00000
SCALE2 0.000000 0.010291 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004506 0.00000
(ATOM LINES ARE NOT SHOWN.)
END