HEADER TRANSFERASE 01-JUN-00 1F3A
TITLE CRYSTAL STRUCTURE OF MGSTA1-1 IN COMPLEX WITH GSH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE YA CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-11D
KEYWDS GLUTATHIONE S-TRANSFERASE, GLUTATHIONE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GU,S.V.SINGH,X.JI
REVDAT 5 30-AUG-23 1F3A 1 AUTHOR JRNL REMARK
REVDAT 4 04-OCT-17 1F3A 1 REMARK
REVDAT 3 24-FEB-09 1F3A 1 VERSN
REVDAT 2 01-APR-03 1F3A 1 JRNL
REVDAT 1 18-OCT-00 1F3A 0
JRNL AUTH Y.GU,S.V.SINGH,X.JI
JRNL TITL RESIDUE R216 AND CATALYTIC EFFICIENCY OF A MURINE CLASS
JRNL TITL 2 ALPHA GLUTATHIONE S-TRANSFERASE TOWARD BENZO[A]PYRENE
JRNL TITL 3 7(R),8(S)-DIOL 9(S), 10(R)-EPOXIDE.
JRNL REF BIOCHEMISTRY V. 39 12552 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11027134
JRNL DOI 10.1021/BI001396U
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.XIAO,S.P.SINGH,B.NANDURI,Y.C.AWASTHI,P.ZIMNIAK,X.JI
REMARK 1 TITL CRYSTAL STRUCTURE OF A MURINE GLUTATHIONE S-TRANSFERASE IN
REMARK 1 TITL 2 COMPLEX WITH A GLUTATHIONE CONJUGATE OF 4-HYDROXYNON-2-ENAL
REMARK 1 TITL 3 IN ONE SUBUNIT AND GLUTATHIONE IN THE OTHER: EVIDENCE OF
REMARK 1 TITL 4 SIGNALING ACROSS THE DIMER INTERFACE
REMARK 1 REF BIOCHEMISTRY V. 38 11887 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI990468I
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 34998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1863
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 : 3559
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.62
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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.750
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1F3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37317
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.710
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.35
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
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: NULL
REMARK 200 SOFTWARE USED: DIFFERENCE FOURIER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, ISOPROPANOL, HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 49.65150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.81850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.65150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.81850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 4440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 732 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 367 LIES ON A SPECIAL POSITION.
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 GLN A 222
REMARK 465 GLN B 222
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE B 221 CG1 CG2 CD1
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 LYS B 220
REMARK 475 ILE B 221
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 12 -71.16 -64.08
REMARK 500 GLN A 66 105.22 76.30
REMARK 500 ASP A 170 96.92 -167.83
REMARK 500 ALA A 218 -46.60 -169.35
REMARK 500 PHE A 219 -162.49 -122.14
REMARK 500 ARG B 12 -73.57 -65.57
REMARK 500 GLN B 66 109.69 79.53
REMARK 500 VAL B 109 26.93 -70.85
REMARK 500 PRO B 113 -22.97 -33.64
REMARK 500 ALA B 209 -66.66 -3.34
REMARK 500 LYS B 210 -81.18 -52.34
REMARK 500 GLN B 211 -47.77 -12.00
REMARK 500 ALA B 218 -34.57 -152.77
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 224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 226
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B48 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MGSTA4-4 IN COMPLEX WITH GSH CONJUGATE OF 4-
REMARK 900 HYDROXYNONENAL IN ONE SUBUNIT AND GSH IN THE OTHER
REMARK 900 RELATED ID: 1F3B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MGSTA1-1 IN COMPLEX WITH GSH CONJUGATE OF
REMARK 900 BENZO[A]PYRENE EPOXIDE
DBREF 1F3A A 1 222 UNP P13745 GSTA1_MOUSE 1 222
DBREF 1F3A B 1 222 UNP P13745 GSTA1_MOUSE 1 222
SEQRES 1 A 222 ALA GLY LYS PRO VAL LEU HIS TYR PHE ASN ALA ARG GLY
SEQRES 2 A 222 ARG MET GLU CYS ILE ARG TRP LEU LEU ALA ALA ALA GLY
SEQRES 3 A 222 VAL GLU PHE GLU GLU LYS PHE ILE GLN SER PRO GLU ASP
SEQRES 4 A 222 LEU GLU LYS LEU LYS LYS ASP GLY ASN LEU MET PHE ASP
SEQRES 5 A 222 GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU ALA
SEQRES 6 A 222 GLN THR ARG ALA ILE LEU ASN TYR ILE ALA THR LYS TYR
SEQRES 7 A 222 ASP LEU TYR GLY LYS ASP MET LYS GLU ARG ALA LEU ILE
SEQRES 8 A 222 ASP MET TYR SER GLU GLY ILE LEU ASP LEU THR GLU MET
SEQRES 9 A 222 ILE GLY GLN LEU VAL LEU CYS PRO PRO ASP GLN ARG GLU
SEQRES 10 A 222 ALA LYS THR ALA LEU ALA LYS ASP ARG THR LYS ASN ARG
SEQRES 11 A 222 TYR LEU PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY
SEQRES 12 A 222 GLN ASP TYR LEU VAL GLY ASN ARG LEU THR ARG VAL ASP
SEQRES 13 A 222 ILE HIS LEU LEU GLU VAL LEU LEU TYR VAL GLU GLU PHE
SEQRES 14 A 222 ASP ALA SER LEU LEU THR PRO PHE PRO LEU LEU LYS ALA
SEQRES 15 A 222 PHE LYS SER ARG ILE SER SER LEU PRO ASN VAL LYS LYS
SEQRES 16 A 222 PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO MET ASP
SEQRES 17 A 222 ALA LYS GLN ILE GLN GLU ALA ARG LYS ALA PHE LYS ILE
SEQRES 18 A 222 GLN
SEQRES 1 B 222 ALA GLY LYS PRO VAL LEU HIS TYR PHE ASN ALA ARG GLY
SEQRES 2 B 222 ARG MET GLU CYS ILE ARG TRP LEU LEU ALA ALA ALA GLY
SEQRES 3 B 222 VAL GLU PHE GLU GLU LYS PHE ILE GLN SER PRO GLU ASP
SEQRES 4 B 222 LEU GLU LYS LEU LYS LYS ASP GLY ASN LEU MET PHE ASP
SEQRES 5 B 222 GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU ALA
SEQRES 6 B 222 GLN THR ARG ALA ILE LEU ASN TYR ILE ALA THR LYS TYR
SEQRES 7 B 222 ASP LEU TYR GLY LYS ASP MET LYS GLU ARG ALA LEU ILE
SEQRES 8 B 222 ASP MET TYR SER GLU GLY ILE LEU ASP LEU THR GLU MET
SEQRES 9 B 222 ILE GLY GLN LEU VAL LEU CYS PRO PRO ASP GLN ARG GLU
SEQRES 10 B 222 ALA LYS THR ALA LEU ALA LYS ASP ARG THR LYS ASN ARG
SEQRES 11 B 222 TYR LEU PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY
SEQRES 12 B 222 GLN ASP TYR LEU VAL GLY ASN ARG LEU THR ARG VAL ASP
SEQRES 13 B 222 ILE HIS LEU LEU GLU VAL LEU LEU TYR VAL GLU GLU PHE
SEQRES 14 B 222 ASP ALA SER LEU LEU THR PRO PHE PRO LEU LEU LYS ALA
SEQRES 15 B 222 PHE LYS SER ARG ILE SER SER LEU PRO ASN VAL LYS LYS
SEQRES 16 B 222 PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO MET ASP
SEQRES 17 B 222 ALA LYS GLN ILE GLN GLU ALA ARG LYS ALA PHE LYS ILE
SEQRES 18 B 222 GLN
HET GSH A 224 20
HET GSH B 226 20
HETNAM GSH GLUTATHIONE
FORMUL 3 GSH 2(C10 H17 N3 O6 S)
FORMUL 5 HOH *450(H2 O)
HELIX 1 1 MET A 15 ALA A 25 1 11
HELIX 2 2 SER A 36 ASP A 46 1 11
HELIX 3 3 GLN A 66 TYR A 78 1 13
HELIX 4 4 ASP A 84 LEU A 108 1 25
HELIX 5 5 VAL A 109 CYS A 111 5 3
HELIX 6 6 GLN A 115 ARG A 130 1 16
HELIX 7 7 ARG A 130 GLY A 143 1 14
HELIX 8 8 THR A 153 ALA A 171 1 19
HELIX 9 9 SER A 172 THR A 175 5 4
HELIX 10 10 PHE A 177 SER A 189 1 13
HELIX 11 11 LEU A 190 GLN A 198 1 9
HELIX 12 12 ASP A 208 LYS A 217 1 10
HELIX 13 13 MET B 15 GLY B 26 1 12
HELIX 14 14 SER B 36 ASP B 46 1 11
HELIX 15 15 GLN B 66 TYR B 78 1 13
HELIX 16 16 ASP B 84 GLN B 107 1 24
HELIX 17 17 LEU B 108 CYS B 111 5 4
HELIX 18 18 GLN B 115 ARG B 130 1 16
HELIX 19 19 ARG B 130 GLY B 143 1 14
HELIX 20 20 THR B 153 ASP B 170 1 18
HELIX 21 21 ALA B 171 THR B 175 5 5
HELIX 22 22 PHE B 177 SER B 189 1 13
HELIX 23 23 LEU B 190 GLN B 198 1 9
HELIX 24 24 ASP B 208 LYS B 217 1 10
SHEET 1 A 4 GLU A 30 ILE A 34 0
SHEET 2 A 4 VAL A 5 PHE A 9 1 N LEU A 6 O GLU A 30
SHEET 3 A 4 MET A 56 ILE A 59 -1 O MET A 56 N HIS A 7
SHEET 4 A 4 MET A 62 ALA A 65 -1 N MET A 62 O ILE A 59
SHEET 1 B 4 GLU B 30 PHE B 33 0
SHEET 2 B 4 VAL B 5 TYR B 8 1 O LEU B 6 N LYS B 32
SHEET 3 B 4 MET B 56 ILE B 59 -1 O MET B 56 N HIS B 7
SHEET 4 B 4 MET B 62 ALA B 65 -1 N MET B 62 O ILE B 59
CISPEP 1 VAL A 54 PRO A 55 0 0.52
CISPEP 2 VAL B 54 PRO B 55 0 0.93
SITE 1 AC1 17 TYR A 8 ARG A 14 LYS A 44 GLN A 53
SITE 2 AC1 17 VAL A 54 PRO A 55 GLN A 66 THR A 67
SITE 3 AC1 17 HOH A 382 HOH A 498 HOH A 503 HOH A 611
SITE 4 AC1 17 HOH A 686 HOH A 754 ASP B 100 ARG B 130
SITE 5 AC1 17 HOH B 422
SITE 1 AC2 14 ASP A 100 ARG A 130 ARG B 14 LYS B 44
SITE 2 AC2 14 ASP B 52 GLN B 53 VAL B 54 PRO B 55
SITE 3 AC2 14 GLN B 66 THR B 67 HOH B 345 HOH B 464
SITE 4 AC2 14 HOH B 598 HOH B 636
CRYST1 99.303 93.637 52.217 90.00 91.80 90.00 C 1 2 1 8
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 0.010070 0.000000 0.000316 0.00000
SCALE2 0.000000 0.010680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019160 0.00000
(ATOM LINES ARE NOT SHOWN.)
END