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PDBsum entry 2dc5

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Top Page protein Protein-protein interface(s) links
Transferase PDB id
2dc5
Jmol
Contents
Protein chains
218 a.a.
Waters ×563
HEADER    TRANSFERASE                             28-DEC-05   2DC5
TITLE     CRYSTAL STRUCTURE OF MOUSE GLUTATHIONE S-TRANSFERASE, MU7
TITLE    2 (GSTM7) AT 1.6 A RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE, MU 7;
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_VECTOR_TYPE: PLASMID;
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PX050309-01;
SOURCE   7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS    STRUCTURAL GENOMICS, GLUTATHIONE S-TRANSFERASE, RIKEN
KEYWDS   2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA,
KEYWDS   3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS   4 ANALYSES
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KAMO,S.KISHISHITA,K.MURAYAMA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR   2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT   2   24-FEB-09 2DC5    1       VERSN
REVDAT   1   28-JUN-06 2DC5    0
JRNL        AUTH   S.KAMO,S.KISHISHITA,K.MURAYAMA,M.SHIROUZU,
JRNL        AUTH 2 S.YOKOYAMA
JRNL        TITL   CRYSTAL STRUCTURE OF MOUSE GLUTATHIONE
JRNL        TITL 2 S-TRANSFERASE, MU7 (GSTM7) AT 1.6 A RESOLUTION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.60 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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 245598.630
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.4
REMARK   3   NUMBER OF REFLECTIONS             : 113517
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) : 0.188
REMARK   3   FREE R VALUE                     : 0.202
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 5559
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
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) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 17342
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190
REMARK   3   BIN FREE R VALUE                    : 0.2500
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 915
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3618
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 563
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.75000
REMARK   3    B22 (A**2) : -0.45000
REMARK   3    B33 (A**2) : -1.30000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17
REMARK   3   ESD FROM SIGMAA              (A) : 0.09
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) : 0.19
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.10
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80
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) : 1.960 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.710 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.080 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.140 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 45.39
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK   4
REMARK   4 2DC5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JAN-06.
REMARK 100 THE RCSB ID CODE IS RCSB025239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-05
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               : SPRING-8
REMARK 200  BEAMLINE                       : BL26B2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790
REMARK 200  MONOCHROMATOR                  : SILICON
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113517
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 4.626
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05200
REMARK 200   FOR THE DATA SET  : 22.0419
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.15300
REMARK 200   FOR SHELL         : 7.902
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2GTU
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M NA HEPES
REMARK 280  PH 7.5, 28% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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       43.19250
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.30500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.19250
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.30500
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: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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     GLY A     1
REMARK 465     SER A     2
REMARK 465     SER A     3
REMARK 465     GLY A     4
REMARK 465     SER A     5
REMARK 465     SER A     6
REMARK 465     GLY A     7
REMARK 465     SER A   226
REMARK 465     GLY A   227
REMARK 465     PRO A   228
REMARK 465     SER A   229
REMARK 465     SER A   230
REMARK 465     GLY A   231
REMARK 465     GLY B     1
REMARK 465     SER B     2
REMARK 465     SER B     3
REMARK 465     GLY B     4
REMARK 465     SER B     5
REMARK 465     SER B     6
REMARK 465     GLY B     7
REMARK 465     SER B   226
REMARK 465     GLY B   227
REMARK 465     PRO B   228
REMARK 465     SER B   229
REMARK 465     SER B   230
REMARK 465     GLY B   231
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    ALA A  45      167.63    -47.63
REMARK 500    PRO A  46       -3.38    -56.35
REMARK 500    PRO A  65      118.14    -39.02
REMARK 500    GLN A  79      114.48     78.08
REMARK 500    GLU B  56      -17.80   -140.87
REMARK 500    PRO B  65      124.33    -38.96
REMARK 500    GLN B  79      113.24     78.15
REMARK 500    LYS B 180       -1.03     73.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007000002.1   RELATED DB: TARGETDB
DBREF  2DC5 A    8   225  GB     30354091 AAH51924         1    218
DBREF  2DC5 B    8   225  GB     30354091 AAH51924         1    218
SEQADV 2DC5 GLY A    1  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER A    2  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER A    3  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY A    4  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER A    5  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER A    6  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY A    7  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 MSE A    8  GB   30354091  MET     1 MODIFIED RESIDUE
SEQADV 2DC5 MSE A   10  GB   30354091  MET     3 MODIFIED RESIDUE
SEQADV 2DC5 MSE A   42  GB   30354091  MET    35 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  112  GB   30354091  MET   105 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  116  GB   30354091  MET   109 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  141  GB   30354091  MET   134 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  142  GB   30354091  MET   135 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  205  GB   30354091  MET   198 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  215  GB   30354091  MET   208 MODIFIED RESIDUE
SEQADV 2DC5 MSE A  219  GB   30354091  MET   212 MODIFIED RESIDUE
SEQADV 2DC5 SER A  226  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY A  227  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 PRO A  228  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER A  229  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER A  230  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY A  231  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY B    1  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER B    2  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER B    3  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY B    4  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER B    5  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER B    6  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY B    7  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 MSE B    8  GB   30354091  MET     1 MODIFIED RESIDUE
SEQADV 2DC5 MSE B   10  GB   30354091  MET     3 MODIFIED RESIDUE
SEQADV 2DC5 MSE B   42  GB   30354091  MET    35 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  112  GB   30354091  MET   105 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  116  GB   30354091  MET   109 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  141  GB   30354091  MET   134 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  142  GB   30354091  MET   135 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  205  GB   30354091  MET   198 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  215  GB   30354091  MET   208 MODIFIED RESIDUE
SEQADV 2DC5 MSE B  219  GB   30354091  MET   212 MODIFIED RESIDUE
SEQADV 2DC5 SER B  226  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY B  227  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 PRO B  228  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER B  229  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 SER B  230  GB   30354091            CLONING ARTIFACT
SEQADV 2DC5 GLY B  231  GB   30354091            CLONING ARTIFACT
SEQRES   1 A  231  GLY SER SER GLY SER SER GLY MSE PRO MSE THR LEU GLY
SEQRES   2 A  231  TYR TRP ASP ILE ARG GLY LEU ALA HIS ALA ILE ARG LEU
SEQRES   3 A  231  PHE LEU GLU TYR THR ASP SER SER TYR GLU GLU LYS ARG
SEQRES   4 A  231  TYR THR MSE GLY ASP ALA PRO ASP TYR ASP GLN SER GLN
SEQRES   5 A  231  TRP LEU ASN GLU LYS PHE LYS LEU GLY LEU ASP PHE PRO
SEQRES   6 A  231  ASN LEU PRO TYR LEU ILE ASP GLY SER HIS LYS ILE THR
SEQRES   7 A  231  GLN SER ASN ALA ILE LEU ARG TYR LEU GLY ARG LYS HIS
SEQRES   8 A  231  ASN LEU CYS GLY GLU THR GLU GLU GLU ARG ILE ARG VAL
SEQRES   9 A  231  ASP ILE LEU GLU ASN GLN LEU MSE ASP ASN ARG MSE VAL
SEQRES  10 A  231  LEU ALA ARG LEU CYS TYR ASN ALA ASP PHE GLU LYS LEU
SEQRES  11 A  231  LYS PRO GLY TYR LEU GLU GLN LEU PRO GLY MSE MSE ARG
SEQRES  12 A  231  LEU TYR SER GLU PHE LEU GLY LYS ARG PRO TRP PHE ALA
SEQRES  13 A  231  GLY ASP LYS ILE THR PHE VAL ASP PHE ILE ALA TYR ASP
SEQRES  14 A  231  VAL LEU GLU ARG ASN GLN VAL PHE GLU ALA LYS CYS LEU
SEQRES  15 A  231  ASP ALA PHE PRO ASN LEU LYS ASP PHE ILE ALA ARG PHE
SEQRES  16 A  231  GLU GLY LEU LYS LYS ILE SER ASP TYR MSE LYS THR SER
SEQRES  17 A  231  ARG PHE LEU PRO ARG PRO MSE PHE THR LYS MSE ALA THR
SEQRES  18 A  231  TRP GLY SER ASN SER GLY PRO SER SER GLY
SEQRES   1 B  231  GLY SER SER GLY SER SER GLY MSE PRO MSE THR LEU GLY
SEQRES   2 B  231  TYR TRP ASP ILE ARG GLY LEU ALA HIS ALA ILE ARG LEU
SEQRES   3 B  231  PHE LEU GLU TYR THR ASP SER SER TYR GLU GLU LYS ARG
SEQRES   4 B  231  TYR THR MSE GLY ASP ALA PRO ASP TYR ASP GLN SER GLN
SEQRES   5 B  231  TRP LEU ASN GLU LYS PHE LYS LEU GLY LEU ASP PHE PRO
SEQRES   6 B  231  ASN LEU PRO TYR LEU ILE ASP GLY SER HIS LYS ILE THR
SEQRES   7 B  231  GLN SER ASN ALA ILE LEU ARG TYR LEU GLY ARG LYS HIS
SEQRES   8 B  231  ASN LEU CYS GLY GLU THR GLU GLU GLU ARG ILE ARG VAL
SEQRES   9 B  231  ASP ILE LEU GLU ASN GLN LEU MSE ASP ASN ARG MSE VAL
SEQRES  10 B  231  LEU ALA ARG LEU CYS TYR ASN ALA ASP PHE GLU LYS LEU
SEQRES  11 B  231  LYS PRO GLY TYR LEU GLU GLN LEU PRO GLY MSE MSE ARG
SEQRES  12 B  231  LEU TYR SER GLU PHE LEU GLY LYS ARG PRO TRP PHE ALA
SEQRES  13 B  231  GLY ASP LYS ILE THR PHE VAL ASP PHE ILE ALA TYR ASP
SEQRES  14 B  231  VAL LEU GLU ARG ASN GLN VAL PHE GLU ALA LYS CYS LEU
SEQRES  15 B  231  ASP ALA PHE PRO ASN LEU LYS ASP PHE ILE ALA ARG PHE
SEQRES  16 B  231  GLU GLY LEU LYS LYS ILE SER ASP TYR MSE LYS THR SER
SEQRES  17 B  231  ARG PHE LEU PRO ARG PRO MSE PHE THR LYS MSE ALA THR
SEQRES  18 B  231  TRP GLY SER ASN SER GLY PRO SER SER GLY
MODRES 2DC5 MSE A    8  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A   10  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A   42  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  112  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  116  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  141  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  142  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  205  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  215  MET  SELENOMETHIONINE
MODRES 2DC5 MSE A  219  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B    8  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B   10  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B   42  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  112  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  116  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  141  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  142  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  205  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  215  MET  SELENOMETHIONINE
MODRES 2DC5 MSE B  219  MET  SELENOMETHIONINE
HET    MSE  A   8       8
HET    MSE  A  10       8
HET    MSE  A  42       8
HET    MSE  A 112       8
HET    MSE  A 116       8
HET    MSE  A 141       8
HET    MSE  A 142       8
HET    MSE  A 205       8
HET    MSE  A 215       8
HET    MSE  A 219       8
HET    MSE  B   8       8
HET    MSE  B  10       8
HET    MSE  B  42       8
HET    MSE  B 112       8
HET    MSE  B 116       8
HET    MSE  B 141       8
HET    MSE  B 142       8
HET    MSE  B 205       8
HET    MSE  B 215       8
HET    MSE  B 219       8
HETNAM     MSE SELENOMETHIONINE
FORMUL   1  MSE    20(C5 H11 N O2 SE)
FORMUL   3  HOH   *563(H2 O)
HELIX    1   1 ARG A   18  LEU A   20  5                                   3
HELIX    2   2 ALA A   21  THR A   31  1                                  11
HELIX    3   3 GLN A   50  ASN A   55  1                                   6
HELIX    4   4 GLN A   79  HIS A   91  1                                  13
HELIX    5   5 THR A   97  TYR A  123  1                                  27
HELIX    6   6 ASP A  126  GLY A  150  1                                  25
HELIX    7   7 THR A  161  GLU A  178  1                                  18
HELIX    8   8 PHE A  185  LEU A  198  1                                  14
HELIX    9   9 LEU A  198  LYS A  206  1                                   9
HELIX   10  10 ALA B   21  THR B   31  1                                  11
HELIX   11  11 GLN B   50  ASN B   55  1                                   6
HELIX   12  12 GLN B   79  HIS B   91  1                                  13
HELIX   13  13 THR B   97  TYR B  123  1                                  27
HELIX   14  14 ASP B  126  GLY B  150  1                                  25
HELIX   15  15 PHE B  162  GLU B  178  1                                  17
HELIX   16  16 PHE B  185  GLY B  197  1                                  13
HELIX   17  17 LEU B  198  MSE B  205  1                                   8
SHEET    1   A 4 TYR A  35  TYR A  40  0
SHEET    2   A 4 MSE A  10  TRP A  15  1  N  LEU A  12   O  LYS A  38
SHEET    3   A 4 TYR A  69  ASP A  72 -1  O  TYR A  69   N  GLY A  13
SHEET    4   A 4 HIS A  75  THR A  78 -1  O  ILE A  77   N  LEU A  70
SHEET    1   B 4 TYR B  35  TYR B  40  0
SHEET    2   B 4 MSE B  10  TRP B  15  1  N  LEU B  12   O  LYS B  38
SHEET    3   B 4 TYR B  69  ASP B  72 -1  O  ILE B  71   N  THR B  11
SHEET    4   B 4 HIS B  75  THR B  78 -1  O  ILE B  77   N  LEU B  70
LINK         C   MSE A   8                 N   PRO A   9     1555   1555  1.34
LINK         C   PRO A   9                 N   MSE A  10     1555   1555  1.33
LINK         C   MSE A  10                 N   THR A  11     1555   1555  1.33
LINK         C   THR A  41                 N   MSE A  42     1555   1555  1.33
LINK         C   MSE A  42                 N   GLY A  43     1555   1555  1.33
LINK         C   LEU A 111                 N   MSE A 112     1555   1555  1.33
LINK         C   MSE A 112                 N   ASP A 113     1555   1555  1.33
LINK         C   ARG A 115                 N   MSE A 116     1555   1555  1.33
LINK         C   MSE A 116                 N   VAL A 117     1555   1555  1.33
LINK         C   GLY A 140                 N   MSE A 141     1555   1555  1.33
LINK         C   MSE A 141                 N   MSE A 142     1555   1555  1.33
LINK         C   MSE A 142                 N   ARG A 143     1555   1555  1.33
LINK         C   TYR A 204                 N   MSE A 205     1555   1555  1.33
LINK         C   MSE A 205                 N   LYS A 206     1555   1555  1.33
LINK         C   PRO A 214                 N   MSE A 215     1555   1555  1.33
LINK         C   MSE A 215                 N   PHE A 216     1555   1555  1.33
LINK         C   LYS A 218                 N   MSE A 219     1555   1555  1.33
LINK         C   MSE A 219                 N   ALA A 220     1555   1555  1.33
LINK         C   MSE B   8                 N   PRO B   9     1555   1555  1.34
LINK         C   PRO B   9                 N   MSE B  10     1555   1555  1.33
LINK         C   MSE B  10                 N   THR B  11     1555   1555  1.33
LINK         C   THR B  41                 N   MSE B  42     1555   1555  1.33
LINK         C   MSE B  42                 N   GLY B  43     1555   1555  1.33
LINK         C   LEU B 111                 N   MSE B 112     1555   1555  1.33
LINK         C   MSE B 112                 N   ASP B 113     1555   1555  1.33
LINK         C   ARG B 115                 N   MSE B 116     1555   1555  1.33
LINK         C   MSE B 116                 N   VAL B 117     1555   1555  1.33
LINK         C   GLY B 140                 N   MSE B 141     1555   1555  1.33
LINK         C   MSE B 141                 N   MSE B 142     1555   1555  1.33
LINK         C   MSE B 142                 N   ARG B 143     1555   1555  1.33
LINK         C   TYR B 204                 N   MSE B 205     1555   1555  1.33
LINK         C   MSE B 205                 N   LYS B 206     1555   1555  1.33
LINK         C   PRO B 214                 N   MSE B 215     1555   1555  1.33
LINK         C   MSE B 215                 N   PHE B 216     1555   1555  1.33
LINK         C   LYS B 218                 N   MSE B 219     1555   1555  1.33
LINK         C   MSE B 219                 N   ALA B 220     1555   1555  1.33
CISPEP   1 MSE A    8    PRO A    9          0         0.01
CISPEP   2 LEU A   67    PRO A   68          0         0.35
CISPEP   3 ARG A  213    PRO A  214          0        -0.21
CISPEP   4 ALA B   45    PRO B   46          0        -0.06
CISPEP   5 LEU B   67    PRO B   68          0         0.29
CISPEP   6 ARG B  213    PRO B  214          0        -0.20
CRYST1   86.385   94.610   57.761  90.00  90.00  90.00 P 21 21 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      0.011576  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010570  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017313        0.00000
      
PROCHECK
Go to PROCHECK summary
 References