HEADER TRANSFERASE 07-JUN-06 2H8A
TITLE STRUCTURE OF MICROSOMAL GLUTATHIONE TRANSFERASE 1 IN COMPLEX WITH
TITLE 2 GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROSOMAL GLUTATHIONE S-TRANSFERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MICROSOMAL GST- 1, MICROSOMAL GST-I;
COMPND 5 EC: 2.5.1.18
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116
KEYWDS MEMBRANE PROTEIN, TRANSFERASE
EXPDTA ELECTRON CRYSTALLOGRAPHY
AUTHOR H.HEBERT
REVDAT 7 14-FEB-24 2H8A 1 REMARK
REVDAT 6 21-MAR-12 2H8A 1 HET
REVDAT 5 18-JAN-12 2H8A 1 HETATM HETNAM
REVDAT 4 13-JUL-11 2H8A 1 VERSN
REVDAT 3 24-FEB-09 2H8A 1 VERSN
REVDAT 2 31-JUL-07 2H8A 1 REMARK
REVDAT 1 22-MAY-07 2H8A 0
JRNL AUTH P.J.HOLM,P.BHAKAT,C.JEGERSCHOLD,N.GYOBU,K.MITSUOKA,
JRNL AUTH 2 Y.FUJIYOSHI,R.MORGENSTERN,H.HEBERT
JRNL TITL STRUCTURAL BASIS FOR DETOXIFICATION AND OXIDATIVE STRESS
JRNL TITL 2 PROTECTION IN MEMBRANES.
JRNL REF J.MOL.BIOL. V. 360 934 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16806268
JRNL DOI 10.1016/J.JMB.2006.05.056
REMARK 2
REMARK 2 RESOLUTION. 3.20 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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.3
REMARK 3 NUMBER OF REFLECTIONS : 4409
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) : 0.342
REMARK 3 R VALUE (WORKING SET) : 0.339
REMARK 3 FREE R VALUE : 0.376
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 457
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 262
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.52
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 29
REMARK 3 BIN FREE R VALUE : 0.3980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 964
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
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) : 26.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.58000
REMARK 3 B22 (A**2) : -2.58000
REMARK 3 B33 (A**2) : 3.88000
REMARK 3 B12 (A**2) : -1.29000
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): 1.747
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.635
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.540
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.134
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.619
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.356
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1004 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1358 ; 1.863 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 119 ; 9.855 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 41 ;36.936 ;21.220
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 165 ;26.230 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;16.716 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 159 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 742 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 806 ; 0.363 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 672 ; 0.336 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 91 ; 0.267 ; 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): 69 ; 0.414 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.375 ; 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): 610 ; 0.529 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 970 ; 0.981 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 431 ; 1.131 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 388 ; 1.666 ; 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 2H8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038054.
REMARK 240
REMARK 240 EXPERIMENTAL DETAILS
REMARK 240 RECONSTRUCTION METHOD : CRYSTALLOGRAPHY
REMARK 240 SAMPLE TYPE : 2D ARRAY
REMARK 240 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 240 DATA ACQUISITION
REMARK 240 DATE OF DATA COLLECTION : NULL
REMARK 240 TEMPERATURE (KELVIN) : NULL
REMARK 240 PH : NULL
REMARK 240 NUMBER OF CRYSTALS USED : NULL
REMARK 240 MICROSCOPE MODEL : JEOL 3000SFF
REMARK 240 DETECTOR TYPE : NULL
REMARK 240 ACCELERATION VOLTAGE (KV) : 300
REMARK 240 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 240 RESOLUTION RANGE HIGH (A) : NULL
REMARK 240 RESOLUTION RANGE LOW (A) : NULL
REMARK 240 DATA SCALING SOFTWARE : NULL
REMARK 240 COMPLETENESS FOR RANGE (%) : NULL
REMARK 240 DATA REDUNDANCY : NULL
REMARK 240 IN THE HIGHEST RESOLUTION SHELL
REMARK 240 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :NULL
REMARK 240 HIGHEST RESOLUTION SHELL, RANGE LOW (A) :NULL
REMARK 240 COMPLETENESS FOR SHELL (%) : NULL
REMARK 240 DATA REDUNDANCY IN SHELL : NULL
REMARK 240 R MERGE FOR SHELL (I) : NULL
REMARK 240 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 240 SOFTWARE USED : NULL
REMARK 240 STARTING MODEL : NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
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,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,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 -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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -0.500000 -0.866025 0.000000 -40.90000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 70.84088
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -81.80000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 LEU A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 LEU A 6
REMARK 465 MET A 7
REMARK 465 ASP A 8
REMARK 465 ALA A 44
REMARK 465 ASN A 45
REMARK 465 PRO A 46
REMARK 465 GLU A 47
REMARK 465 ASP A 48
REMARK 465 CYS A 49
REMARK 465 ALA A 50
REMARK 465 GLY A 51
REMARK 465 PHE A 52
REMARK 465 GLY A 53
REMARK 465 LYS A 54
REMARK 465 GLY A 55
REMARK 465 GLU A 56
REMARK 465 ASN A 57
REMARK 465 ALA A 58
REMARK 465 LYS A 59
REMARK 465 LYS A 60
REMARK 465 PHE A 61
REMARK 465 LEU A 148
REMARK 465 ARG A 149
REMARK 465 SER A 150
REMARK 465 ARG A 151
REMARK 465 LEU A 152
REMARK 465 TYR A 153
REMARK 465 LEU A 154
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 NH2 ARG A 70 O THR A 122 2.03
REMARK 500 O LEU A 90 N TYR A 92 2.18
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 VAL A 11 -97.27 -49.43
REMARK 500 PHE A 15 -74.11 -69.29
REMARK 500 SER A 17 -83.11 -34.57
REMARK 500 LEU A 23 -78.90 -76.05
REMARK 500 ALA A 24 -73.62 -30.55
REMARK 500 MET A 27 -3.27 -54.51
REMARK 500 ALA A 34 87.10 -51.19
REMARK 500 GLN A 36 134.98 -22.82
REMARK 500 LEU A 38 93.55 -66.05
REMARK 500 ASN A 40 -49.27 -146.35
REMARK 500 LYS A 41 79.68 -68.05
REMARK 500 ARG A 63 -85.95 -69.62
REMARK 500 THR A 64 -88.43 -10.91
REMARK 500 LEU A 79 -89.88 -57.34
REMARK 500 ASN A 81 -7.67 -43.41
REMARK 500 PRO A 84 -70.27 -68.07
REMARK 500 PHE A 85 -56.27 -26.53
REMARK 500 LEU A 91 -17.07 -36.79
REMARK 500 PRO A 97 -167.86 -48.15
REMARK 500 ASP A 98 -106.24 -62.85
REMARK 500 LEU A 99 -30.20 178.50
REMARK 500 ILE A 104 -74.47 -68.95
REMARK 500 PHE A 109 -81.85 -49.39
REMARK 500 ALA A 112 -80.85 -55.61
REMARK 500 ARG A 113 -34.71 -28.43
REMARK 500 ILE A 114 -85.91 -61.91
REMARK 500 TYR A 115 -52.09 -27.91
REMARK 500 PRO A 123 -142.18 -86.09
REMARK 500 LEU A 124 -28.49 -157.12
REMARK 500 PRO A 125 -100.41 -97.16
REMARK 500 PRO A 127 4.29 -65.86
REMARK 500 ASN A 128 -52.04 -125.96
REMARK 500 VAL A 135 -81.80 -93.07
REMARK 500 VAL A 139 -21.12 -28.99
REMARK 500 SER A 142 -74.84 -67.51
REMARK 500 ALA A 144 -70.42 -74.88
REMARK 500 TYR A 145 -70.59 -46.58
REMARK 500 ARG A 146 -38.83 -36.81
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 218
DBREF 2H8A A 1 154 UNP P08011 MGST1_RAT 1 154
SEQRES 1 A 154 ALA ASP LEU LYS GLN LEU MET ASP ASN GLU VAL LEU MET
SEQRES 2 A 154 ALA PHE THR SER TYR ALA THR ILE ILE LEU ALA LYS MET
SEQRES 3 A 154 MET PHE LEU SER SER ALA THR ALA PHE GLN ARG LEU THR
SEQRES 4 A 154 ASN LYS VAL PHE ALA ASN PRO GLU ASP CYS ALA GLY PHE
SEQRES 5 A 154 GLY LYS GLY GLU ASN ALA LYS LYS PHE LEU ARG THR ASP
SEQRES 6 A 154 GLU LYS VAL GLU ARG VAL ARG ARG ALA HIS LEU ASN ASP
SEQRES 7 A 154 LEU GLU ASN ILE VAL PRO PHE LEU GLY ILE GLY LEU LEU
SEQRES 8 A 154 TYR SER LEU SER GLY PRO ASP LEU SER THR ALA LEU ILE
SEQRES 9 A 154 HIS PHE ARG ILE PHE VAL GLY ALA ARG ILE TYR HIS THR
SEQRES 10 A 154 ILE ALA TYR LEU THR PRO LEU PRO GLN PRO ASN ARG GLY
SEQRES 11 A 154 LEU ALA PHE PHE VAL GLY TYR GLY VAL THR LEU SER MET
SEQRES 12 A 154 ALA TYR ARG LEU LEU ARG SER ARG LEU TYR LEU
HET GSH A 218 20
HETNAM GSH GLUTATHIONE
FORMUL 2 GSH C10 H17 N3 O6 S
HELIX 1 1 ASN A 9 ALA A 24 1 16
HELIX 2 2 LYS A 25 SER A 30 1 6
HELIX 3 3 SER A 31 THR A 33 5 3
HELIX 4 4 LEU A 62 ASN A 81 1 20
HELIX 5 5 ILE A 82 TYR A 92 1 11
HELIX 6 6 THR A 101 THR A 122 1 22
HELIX 7 7 PRO A 125 TYR A 137 1 13
HELIX 8 8 TYR A 137 ARG A 146 1 10
SITE 1 AC1 3 ARG A 73 GLU A 80 LEU A 124
CRYST1 81.800 81.800 100.000 90.00 90.00 120.00 P 6 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 0.012225 0.007058 0.000000 0.00000
SCALE2 0.000000 0.014116 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
