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PDBsum entry 1pmt

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Transferase PDB id
1pmt
Jmol
Contents
Protein chain
201 a.a.
Ligands
GSH
Waters ×52
HEADER    TRANSFERASE                             23-MAR-98   1PMT
TITLE     GLUTATHIONE TRANSFERASE FROM PROTEUS MIRABILIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE TRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PMGST, GST B1-1;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: DISULFIDE LINK BETWEEN THE CYS 10 AND THE THIOL MOIETY
COMPND   8 OF GLUTATHIONE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE   3 ORGANISM_TAXID: 584;
SOURCE   4 CELLULAR_LOCATION: PERIPLASM;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL
KEYWDS    TRANSFERASE, GLUTATHIONE-CONJUGATING, A PUTATIVE OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.ROSSJOHN,G.POLEKHINA,S.C.FEIL,N.ALLOCATI,M.MASULLI,C.DIILIO,
AUTHOR   2 M.W.PARKER
REVDAT   5   21-DEC-11 1PMT    1       HETATM HETNAM
REVDAT   4   16-NOV-11 1PMT    1       HETATM
REVDAT   3   13-JUL-11 1PMT    1       VERSN
REVDAT   2   24-FEB-09 1PMT    1       VERSN
REVDAT   1   20-APR-99 1PMT    0
JRNL        AUTH   J.ROSSJOHN,G.POLEKHINA,S.C.FEIL,N.ALLOCATI,M.MASULLI,
JRNL        AUTH 2 C.DE ILLIO,M.W.PARKER
JRNL        TITL   A MIXED DISULFIDE BOND IN BACTERIAL GLUTATHIONE TRANSFERASE:
JRNL        TITL 2 FUNCTIONAL AND EVOLUTIONARY IMPLICATIONS.
JRNL        REF    STRUCTURE                     V.   6   721 1998
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9655824
JRNL        DOI    10.1016/S0969-2126(98)00074-4
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.8
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0
REMARK   3   NUMBER OF REFLECTIONS             : 7618
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) : 0.202
REMARK   3   FREE R VALUE                     : 0.301
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 810
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            : 1595
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 52
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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: NULL
REMARK   4
REMARK   4 1PMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : AUG-97
REMARK 200  TEMPERATURE           (KELVIN) : 290
REMARK 200  PH                             : 4.6
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7618
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08000
REMARK 200   FOR THE DATA SET  : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.32900
REMARK 200   FOR SHELL         : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: LUCILIA CUPRINA GST (POLYALANINE, ALL LOOPS
REMARK 200  REMOVED)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y,X,Z+1/4
REMARK 290       4555   Y,-X,Z+3/4
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z+1/2
REMARK 290       7555   Y,X,-Z+3/4
REMARK 290       8555   -Y,-X,-Z+1/4
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       64.70000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       32.35000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       97.05000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       64.70000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       97.05000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       32.35000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       64.70000
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 206  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     LYS A   202
REMARK 465     GLU A   203
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    SER A   9     -161.79    -75.53
REMARK 500    GLU A  65      112.79     77.94
REMARK 500    ASP A  79      -35.37    -36.47
REMARK 500    ILE A  83     -149.80   -134.49
REMARK 500    LYS A  87      -15.91     55.88
REMARK 500    SER A 110      -55.78    -25.28
REMARK 500    GLU A 119      -19.46    -48.89
REMARK 500    SER A 141        7.46    -66.52
REMARK 500    LEU A 175       78.19    -67.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 225        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH A 229        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH A 235        DISTANCE =  6.73 ANGSTROMS
REMARK 525    HOH A 243        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH A 252        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH A 254        DISTANCE =  5.31 ANGSTROMS
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 204
DBREF  1PMT A    1   203  UNP    P15214   GST_PROMI        1    203
SEQRES   1 A  203  MET LYS LEU TYR TYR THR PRO GLY SER CYS SER LEU SER
SEQRES   2 A  203  PRO HIS ILE VAL LEU ARG GLU THR GLY LEU ASP PHE SER
SEQRES   3 A  203  ILE GLU ARG ILE ASP LEU ARG THR LYS LYS THR GLU SER
SEQRES   4 A  203  GLY LYS ASP PHE LEU ALA ILE ASN PRO LYS GLY GLN VAL
SEQRES   5 A  203  PRO VAL LEU GLN LEU ASP ASN GLY ASP ILE LEU THR GLU
SEQRES   6 A  203  GLY VAL ALA ILE VAL GLN TYR LEU ALA ASP LEU LYS PRO
SEQRES   7 A  203  ASP ARG ASN LEU ILE ALA PRO PRO LYS ALA LEU GLU ARG
SEQRES   8 A  203  TYR HIS GLN ILE GLU TRP LEU ASN PHE LEU ALA SER GLU
SEQRES   9 A  203  VAL HIS LYS GLY TYR SER PRO LEU PHE SER SER ASP THR
SEQRES  10 A  203  PRO GLU SER TYR LEU PRO VAL VAL LYS ASN LYS LEU LYS
SEQRES  11 A  203  SER LYS PHE VAL TYR ILE ASN ASP VAL LEU SER LYS GLN
SEQRES  12 A  203  LYS CYS VAL CYS GLY ASP HIS PHE THR VAL ALA ASP ALA
SEQRES  13 A  203  TYR LEU PHE THR LEU SER GLN TRP ALA PRO HIS VAL ALA
SEQRES  14 A  203  LEU ASP LEU THR ASP LEU SER HIS LEU GLN ASP TYR LEU
SEQRES  15 A  203  ALA ARG ILE ALA GLN ARG PRO ASN VAL HIS SER ALA LEU
SEQRES  16 A  203  VAL THR GLU GLY LEU ILE LYS GLU
HET    GSH  A 204      20
HETNAM     GSH GLUTATHIONE
FORMUL   2  GSH    C10 H17 N3 O6 S
FORMUL   3  HOH   *52(H2 O)
HELIX    1   1 CYS A   10  GLU A   20  5                                  11
HELIX    2   2 PHE A   43  ALA A   45  5                                   3
HELIX    3   3 GLY A   66  ALA A   74  1                                   9
HELIX    4   4 PRO A   78  ARG A   80  5                                   3
HELIX    5   5 LEU A   89  SER A  103  1                                  15
HELIX    6   6 HIS A  106  PHE A  113  1                                   8
HELIX    7   7 LEU A  122  LEU A  140  1                                  19
HELIX    8   8 VAL A  153  GLN A  163  1                                  11
HELIX    9   9 PRO A  166  VAL A  168  5                                   3
HELIX   10  10 SER A  176  ALA A  186  1                                  11
HELIX   11  11 PRO A  189  THR A  197  1                                   9
SHEET    1   A 4 SER A  26  ARG A  29  0
SHEET    2   A 4 LYS A   2  TYR A   5  1  N  LEU A   3   O  SER A  26
SHEET    3   A 4 VAL A  54  GLN A  56 -1  N  GLN A  56   O  LYS A   2
SHEET    4   A 4 ILE A  62  THR A  64 -1  N  LEU A  63   O  LEU A  55
LINK         SG  CYS A  10                 SG2 GSH A 204     1555   1555  2.04
CISPEP   1 VAL A   52    PRO A   53          0         0.02
SITE     1 AC1 15 SER A   9  CYS A  10  LYS A  35  GLN A  51
SITE     2 AC1 15 VAL A  52  GLU A  65  GLY A  66  ASN A  99
SITE     3 AC1 15 SER A 103  GLU A 104  HIS A 106  LYS A 107
SITE     4 AC1 15 TRP A 164  HOH A 219  HOH A 253
CRYST1   57.200   57.200  129.400  90.00  90.00  90.00 P 41 2 2      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      0.017483  0.000000  0.000000        0.00000
SCALE2      0.000000  0.017483  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007728        0.00000
      
PROCHECK
Go to PROCHECK summary
 References