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PDBsum entry 1md4

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
1md4
Jmol
Contents
Protein chain
208 a.a. *
Ligands
MES ×2
GSH ×2
Waters ×312
* Residue conservation analysis
HEADER    TRANSFERASE                             06-AUG-02   1MD4
TITLE     A FOLDING MUTANT OF HUMAN CLASS PI GLUTATHIONE TRANSFERASE,
TITLE    2 CREATED BY MUTATING GLYCINE 146 OF THE WILD-TYPE PROTEIN
TITLE    3 TO VALINE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PI GLUTATHIONE TRANSFERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: HGSTP1-1, GLUTATHIONE S-TRANSFERASE P;
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: XL_1 BLUE;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKHP1
KEYWDS    GST, NUCLEATION MECHANISM, CONSERVED FOLDING MODULE,
KEYWDS   2 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.K.-W.KONG,B.DRAGANI,A.ACETO,R.COCCO,B.MANNERVIK,
AUTHOR   2 G.STENBERG,W.J.MCKINSTRY,G.POLEKHINA,M.W.PARKER
REVDAT   3   24-FEB-09 1MD4    1       VERSN
REVDAT   2   22-JUL-03 1MD4    1       JRNL
REVDAT   1   21-AUG-02 1MD4    0
JRNL        AUTH   G.K.-W.KONG,G.POLEKHINA,W.J.MCKINSTRY,M.W.PARKER,
JRNL        AUTH 2 B.DRAGANI,A.ACETO,D.PALUDI,D.R.PRINCIPE,
JRNL        AUTH 3 B.MANNERVIK,G.STENBERG
JRNL        TITL   CONTRIBUTION OF GLYCINE 146 TO A CONSERVED FOLDING
JRNL        TITL 2 MODULE AFFECTING STABILITY AND REFOLDING OF HUMAN
JRNL        TITL 3 GLUTATHIONE TRANSFERASE P1-1
JRNL        REF    J.BIOL.CHEM.                  V. 278  1291 2003
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12414796
JRNL        DOI    10.1074/JBC.M209581200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1689082.100
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.7
REMARK   3   NUMBER OF REFLECTIONS             : 25365
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 SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1280
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3524
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3063
REMARK   3   BIN FREE R VALUE                    : 0.3411
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 98
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            : 3268
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 64
REMARK   3   SOLVENT ATOMS            : 312
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 17.36000
REMARK   3    B22 (A**2) : -9.23000
REMARK   3    B33 (A**2) : -8.13000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -1.39000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26
REMARK   3   ESD FROM SIGMAA              (A) : 0.30
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.110 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.740 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.770 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.480 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 49.54
REMARK   3
REMARK   3  NCS MODEL : CONSTR
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : MES.PARAM
REMARK   3  PARAMETER FILE  4  : GSH.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : MES.TOP
REMARK   3  TOPOLOGY FILE  4   : GSH.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1MD4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-AUG-02.
REMARK 100 THE RCSB ID CODE IS RCSB016827.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54179
REMARK 200  MONOCHROMATOR                  : NICKEL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25365
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7
REMARK 200  DATA REDUNDANCY                : 3.100
REMARK 200  R MERGE                    (I) : 0.11700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.7000
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) : 2.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.51800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 10GS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, PEG 8000, CALCIUM CHLORIDE,
REMARK 280  DTT(DITHIOTHREITOL), GLUTATHIONE(REDUCED), PH 5.4, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K
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       38.63500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.72000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.63500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.72000
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: 3980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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     PRO A     1
REMARK 465     PRO B     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   NE2  GLN B    84     NE2  GLN B    84     2656     1.88
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    GLN A  64      111.46     85.35
REMARK 500    ASN A 110       69.38   -166.35
REMARK 500    THR A 141     -100.65   -109.18
REMARK 500    VAL A 144      -24.93   -144.18
REMARK 500    PRO A 187      -70.59    -30.28
REMARK 500    GLN B  64      111.42     85.43
REMARK 500    ASN B 110       69.76   -166.19
REMARK 500    THR B 141     -100.45   -108.86
REMARK 500    VAL B 144      -24.47   -143.58
REMARK 500    PRO B 187      -71.31    -29.75
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 MES A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 2001
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 3001
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 4001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MD3   RELATED DB: PDB
REMARK 900 1MD3 CONTAINS THE SAME PROTEIN, G146A MUTANT.
DBREF  1MD4 A    1   209  UNP    P09211   GSTP1_HUMAN      1    209
DBREF  1MD4 B    1   209  UNP    P09211   GSTP1_HUMAN      1    209
SEQADV 1MD4 VAL A  145  UNP  P09211    GLY   145 ENGINEERED
SEQADV 1MD4 VAL B  145  UNP  P09211    GLY   145 ENGINEERED
SEQRES   1 A  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES   2 A  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES   3 A  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES   4 A  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES   5 A  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES   6 A  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES   7 A  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES   8 A  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES   9 A  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES  10 A  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES  11 A  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES  12 A  209  VAL VAL ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES  13 A  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES  14 A  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES  15 A  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES  16 A  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES  17 A  209  GLN
SEQRES   1 B  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES   2 B  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES   3 B  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES   4 B  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES   5 B  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES   6 B  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES   7 B  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES   8 B  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES   9 B  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES  10 B  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES  11 B  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES  12 B  209  VAL VAL ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES  13 B  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES  14 B  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES  15 B  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES  16 B  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES  17 B  209  GLN
HET    MES  A1001      12
HET    MES  B2001      12
HET    GSH  A3001      20
HET    GSH  B4001      20
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM     GSH GLUTATHIONE
FORMUL   3  MES    2(C6 H13 N O4 S)
FORMUL   5  GSH    2(C10 H17 N3 O6 S)
FORMUL   7  HOH   *312(H2 O)
HELIX    1   1 ARG A   11  ARG A   13  5                                   3
HELIX    2   2 CYS A   14  GLN A   24  1                                  11
HELIX    3   3 THR A   34  GLU A   40  1                                   7
HELIX    4   4 GLY A   41  CYS A   47  1                                   7
HELIX    5   5 GLN A   64  LEU A   76  1                                  13
HELIX    6   6 ASP A   82  ASN A  110  1                                  29
HELIX    7   7 ASN A  110  GLN A  135  1                                  26
HELIX    8   8 ASN A  136  LYS A  140  5                                   5
HELIX    9   9 SER A  149  ALA A  166  1                                  18
HELIX   10  10 PHE A  173  ARG A  186  1                                  14
HELIX   11  11 ARG A  186  SER A  195  1                                  10
HELIX   12  12 SER A  195  ASN A  200  1                                   6
HELIX   13  13 ARG B   11  ARG B   13  5                                   3
HELIX   14  14 CYS B   14  GLN B   24  1                                  11
HELIX   15  15 THR B   34  GLU B   40  1                                   7
HELIX   16  16 GLY B   41  CYS B   47  1                                   7
HELIX   17  17 GLN B   64  LEU B   76  1                                  13
HELIX   18  18 ASP B   82  ASN B  110  1                                  29
HELIX   19  19 ASN B  110  GLN B  135  1                                  26
HELIX   20  20 ASN B  136  LYS B  140  5                                   5
HELIX   21  21 SER B  149  ALA B  166  1                                  18
HELIX   22  22 PHE B  173  ARG B  186  1                                  14
HELIX   23  23 ARG B  186  SER B  195  1                                  10
HELIX   24  24 SER B  195  ASN B  200  1                                   6
SHEET    1   A 4 TRP A  28  VAL A  32  0
SHEET    2   A 4 TYR A   3  TYR A   7  1  N  VAL A   5   O  GLU A  31
SHEET    3   A 4 LYS A  54  ASP A  57 -1  O  LYS A  54   N  VAL A   6
SHEET    4   A 4 LEU A  60  TYR A  63 -1  O  LEU A  62   N  PHE A  55
SHEET    1   B 4 TRP B  28  VAL B  32  0
SHEET    2   B 4 TYR B   3  TYR B   7  1  N  VAL B   5   O  GLU B  31
SHEET    3   B 4 LYS B  54  ASP B  57 -1  O  LYS B  54   N  VAL B   6
SHEET    4   B 4 LEU B  60  TYR B  63 -1  O  LEU B  62   N  PHE B  55
CISPEP   1 LEU A   52    PRO A   53          0         0.46
CISPEP   2 LEU B   52    PRO B   53          0         0.38
SITE     1 AC1  5 TRP A  28  GLU A  30  GLU A 197  HOH A3068
SITE     2 AC1  5 ASP B 171
SITE     1 AC2  3 TRP B  28  PHE B 192  GLU B 197
SITE     1 AC3 14 TYR A   7  PHE A   8  ARG A  13  TRP A  38
SITE     2 AC3 14 LYS A  44  GLN A  51  LEU A  52  PRO A  53
SITE     3 AC3 14 GLN A  64  SER A  65  HOH A3014  HOH A3060
SITE     4 AC3 14 HOH A3089  ASP B  98
SITE     1 AC4 15 ASP A  98  TYR B   7  PHE B   8  ARG B  13
SITE     2 AC4 15 TRP B  38  LYS B  44  GLN B  51  LEU B  52
SITE     3 AC4 15 PRO B  53  GLN B  64  SER B  65  HOH B4021
SITE     4 AC4 15 HOH B4024  HOH B4054  HOH B4069
CRYST1   77.270   89.440   68.920  90.00  98.07  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      0.012942  0.000000  0.001835        0.00000
SCALE2      0.000000  0.011181  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014655        0.00000
      
PROCHECK
Go to PROCHECK summary
 References