spacer
spacer

PDBsum entry 2gwo

Go to PDB code: 
Top Page protein Protein-protein interface(s) links
Hydrolase PDB id
2gwo
Jmol
Contents
Protein chain
169 a.a.
Waters ×260
HEADER    HYDROLASE                               05-MAY-06   2GWO
TITLE     CRYSTAL STRUCTURE OF TMDP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DUAL SPECIFICITY PROTEIN PHOSPHATASE 13;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: TESTIS- AND SKELETAL-MUSCLE-SPECIFIC DSP, DUAL
COMPND   5 SPECIFICITY PHOSPHATASE SKRP4, TMDP;
COMPND   6 EC: 3.1.3.48, 3.1.3.16;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: DUSP13, TMDP;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ALPHA/BETA, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.J.KIM,S.E.RYU,J.H.KIM
REVDAT   2   24-FEB-09 2GWO    1       VERSN
REVDAT   1   20-MAR-07 2GWO    0
JRNL        AUTH   S.J.KIM,D.G.JEONG,T.S.YOON,J.H.SON,S.K.CHO,S.E.RYU,
JRNL        AUTH 2 J.H.KIM
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TMDP, A TESTIS-SPECIFIC
JRNL        TITL 2 DUAL SPECIFICITY PROTEIN PHOSPHATASE: IMPLICATIONS
JRNL        TITL 3 FOR SUBSTRATE SPECIFICITY
JRNL        REF    PROTEINS                      V.  66   239 2007
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   17044055
JRNL        DOI    10.1002/PROT.21197
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.9
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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 29446
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) : 0.198
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1443
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            : 5382
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 260
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) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74
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 2GWO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037640.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-02
REMARK 200  TEMPERATURE           (KELVIN) : 93
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29452
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M NACL, 10% ETOH, 10MM DTT, PH
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       36.12000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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     MET A     1
REMARK 465     ASP A     2
REMARK 465     SER A     3
REMARK 465     LEU A     4
REMARK 465     GLN A     5
REMARK 465     LYS A     6
REMARK 465     GLN A     7
REMARK 465     ASP A     8
REMARK 465     LEU A     9
REMARK 465     ARG A    10
REMARK 465     ARG A    11
REMARK 465     PRO A    12
REMARK 465     LYS A    13
REMARK 465     ILE A    14
REMARK 465     HIS A    15
REMARK 465     GLY A    16
REMARK 465     ALA A    17
REMARK 465     VAL A    18
REMARK 465     GLN A    19
REMARK 465     ALA A    20
REMARK 465     SER A    21
REMARK 465     PRO A    22
REMARK 465     TYR A    23
REMARK 465     GLN A    24
REMARK 465     GLU A   194
REMARK 465     THR A   195
REMARK 465     GLY A   196
REMARK 465     ARG A   197
REMARK 465     PHE A   198
REMARK 465     MET B     1
REMARK 465     ASP B     2
REMARK 465     SER B     3
REMARK 465     LEU B     4
REMARK 465     GLN B     5
REMARK 465     LYS B     6
REMARK 465     GLN B     7
REMARK 465     ASP B     8
REMARK 465     LEU B     9
REMARK 465     ARG B    10
REMARK 465     ARG B    11
REMARK 465     PRO B    12
REMARK 465     LYS B    13
REMARK 465     ILE B    14
REMARK 465     HIS B    15
REMARK 465     GLY B    16
REMARK 465     ALA B    17
REMARK 465     VAL B    18
REMARK 465     GLN B    19
REMARK 465     ALA B    20
REMARK 465     SER B    21
REMARK 465     PRO B    22
REMARK 465     TYR B    23
REMARK 465     GLN B    24
REMARK 465     GLU B   194
REMARK 465     THR B   195
REMARK 465     GLY B   196
REMARK 465     ARG B   197
REMARK 465     PHE B   198
REMARK 465     MET C     1
REMARK 465     ASP C     2
REMARK 465     SER C     3
REMARK 465     LEU C     4
REMARK 465     GLN C     5
REMARK 465     LYS C     6
REMARK 465     GLN C     7
REMARK 465     ASP C     8
REMARK 465     LEU C     9
REMARK 465     ARG C    10
REMARK 465     ARG C    11
REMARK 465     PRO C    12
REMARK 465     LYS C    13
REMARK 465     ILE C    14
REMARK 465     HIS C    15
REMARK 465     GLY C    16
REMARK 465     ALA C    17
REMARK 465     VAL C    18
REMARK 465     GLN C    19
REMARK 465     ALA C    20
REMARK 465     SER C    21
REMARK 465     PRO C    22
REMARK 465     TYR C    23
REMARK 465     GLN C    24
REMARK 465     MET D     1
REMARK 465     ASP D     2
REMARK 465     SER D     3
REMARK 465     LEU D     4
REMARK 465     GLN D     5
REMARK 465     LYS D     6
REMARK 465     GLN D     7
REMARK 465     ASP D     8
REMARK 465     LEU D     9
REMARK 465     ARG D    10
REMARK 465     ARG D    11
REMARK 465     PRO D    12
REMARK 465     LYS D    13
REMARK 465     ILE D    14
REMARK 465     HIS D    15
REMARK 465     GLY D    16
REMARK 465     ALA D    17
REMARK 465     VAL D    18
REMARK 465     GLN D    19
REMARK 465     ALA D    20
REMARK 465     SER D    21
REMARK 465     PRO D    22
REMARK 465     TYR D    23
REMARK 465     GLN D    24
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS C 138   CB    CYS C 138   SG     -0.126
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    CYS A 138   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES
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    ARG A  38       51.75   -102.79
REMARK 500    GLN A  84     -134.03   -117.64
REMARK 500    THR A  87      -75.49    -87.75
REMARK 500    SER A  96       61.04   -103.73
REMARK 500    ASP A 106       57.31   -101.60
REMARK 500    CYS A 138     -155.70   -119.12
REMARK 500    SER A 143      -74.78   -121.58
REMARK 500    CYS A 175       78.00   -157.42
REMARK 500    GLN B  84     -124.96   -110.27
REMARK 500    THR B  87      -72.81   -103.65
REMARK 500    CYS B 138     -159.90   -132.05
REMARK 500    SER B 143      -72.01   -119.40
REMARK 500    ASN B 158       51.02     39.66
REMARK 500    CYS B 175       73.82   -158.83
REMARK 500    GLN C  84     -123.18   -120.00
REMARK 500    THR C  87      -72.74   -105.50
REMARK 500    CYS C 138     -151.32   -126.58
REMARK 500    SER C 143      -76.44   -120.51
REMARK 500    CYS C 175       85.67   -161.88
REMARK 500    GLN D  84     -137.79   -117.23
REMARK 500    THR D  87      -77.87    -87.67
REMARK 500    CYS D 138     -147.37   -123.00
REMARK 500    CYS D 175       76.22   -170.94
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2GWO A    1   198  UNP    Q9UII6   DUS13_HUMAN      1    198
DBREF  2GWO B    1   198  UNP    Q9UII6   DUS13_HUMAN      1    198
DBREF  2GWO C    1   198  UNP    Q9UII6   DUS13_HUMAN      1    198
DBREF  2GWO D    1   198  UNP    Q9UII6   DUS13_HUMAN      1    198
SEQADV 2GWO CYS A  156  UNP  Q9UII6    TYR   156 SEE REMARK 999
SEQADV 2GWO CYS B  156  UNP  Q9UII6    TYR   156 SEE REMARK 999
SEQADV 2GWO CYS C  156  UNP  Q9UII6    TYR   156 SEE REMARK 999
SEQADV 2GWO CYS D  156  UNP  Q9UII6    TYR   156 SEE REMARK 999
SEQRES   1 A  198  MET ASP SER LEU GLN LYS GLN ASP LEU ARG ARG PRO LYS
SEQRES   2 A  198  ILE HIS GLY ALA VAL GLN ALA SER PRO TYR GLN PRO PRO
SEQRES   3 A  198  THR LEU ALA SER LEU GLN ARG LEU LEU TRP VAL ARG GLN
SEQRES   4 A  198  ALA ALA THR LEU ASN HIS ILE ASP GLU VAL TRP PRO SER
SEQRES   5 A  198  LEU PHE LEU GLY ASP ALA TYR ALA ALA ARG ASP LYS SER
SEQRES   6 A  198  LYS LEU ILE GLN LEU GLY ILE THR HIS VAL VAL ASN ALA
SEQRES   7 A  198  ALA ALA GLY LYS PHE GLN VAL ASP THR GLY ALA LYS PHE
SEQRES   8 A  198  TYR ARG GLY MET SER LEU GLU TYR TYR GLY ILE GLU ALA
SEQRES   9 A  198  ASP ASP ASN PRO PHE PHE ASP LEU SER VAL TYR PHE LEU
SEQRES  10 A  198  PRO VAL ALA ARG TYR ILE ARG ALA ALA LEU SER VAL PRO
SEQRES  11 A  198  GLN GLY ARG VAL LEU VAL HIS CYS ALA MET GLY VAL SER
SEQRES  12 A  198  ARG SER ALA THR LEU VAL LEU ALA PHE LEU MET ILE CYS
SEQRES  13 A  198  GLU ASN MET THR LEU VAL GLU ALA ILE GLN THR VAL GLN
SEQRES  14 A  198  ALA HIS ARG ASN ILE CYS PRO ASN SER GLY PHE LEU ARG
SEQRES  15 A  198  GLN LEU GLN VAL LEU ASP ASN ARG LEU GLY ARG GLU THR
SEQRES  16 A  198  GLY ARG PHE
SEQRES   1 B  198  MET ASP SER LEU GLN LYS GLN ASP LEU ARG ARG PRO LYS
SEQRES   2 B  198  ILE HIS GLY ALA VAL GLN ALA SER PRO TYR GLN PRO PRO
SEQRES   3 B  198  THR LEU ALA SER LEU GLN ARG LEU LEU TRP VAL ARG GLN
SEQRES   4 B  198  ALA ALA THR LEU ASN HIS ILE ASP GLU VAL TRP PRO SER
SEQRES   5 B  198  LEU PHE LEU GLY ASP ALA TYR ALA ALA ARG ASP LYS SER
SEQRES   6 B  198  LYS LEU ILE GLN LEU GLY ILE THR HIS VAL VAL ASN ALA
SEQRES   7 B  198  ALA ALA GLY LYS PHE GLN VAL ASP THR GLY ALA LYS PHE
SEQRES   8 B  198  TYR ARG GLY MET SER LEU GLU TYR TYR GLY ILE GLU ALA
SEQRES   9 B  198  ASP ASP ASN PRO PHE PHE ASP LEU SER VAL TYR PHE LEU
SEQRES  10 B  198  PRO VAL ALA ARG TYR ILE ARG ALA ALA LEU SER VAL PRO
SEQRES  11 B  198  GLN GLY ARG VAL LEU VAL HIS CYS ALA MET GLY VAL SER
SEQRES  12 B  198  ARG SER ALA THR LEU VAL LEU ALA PHE LEU MET ILE CYS
SEQRES  13 B  198  GLU ASN MET THR LEU VAL GLU ALA ILE GLN THR VAL GLN
SEQRES  14 B  198  ALA HIS ARG ASN ILE CYS PRO ASN SER GLY PHE LEU ARG
SEQRES  15 B  198  GLN LEU GLN VAL LEU ASP ASN ARG LEU GLY ARG GLU THR
SEQRES  16 B  198  GLY ARG PHE
SEQRES   1 C  198  MET ASP SER LEU GLN LYS GLN ASP LEU ARG ARG PRO LYS
SEQRES   2 C  198  ILE HIS GLY ALA VAL GLN ALA SER PRO TYR GLN PRO PRO
SEQRES   3 C  198  THR LEU ALA SER LEU GLN ARG LEU LEU TRP VAL ARG GLN
SEQRES   4 C  198  ALA ALA THR LEU ASN HIS ILE ASP GLU VAL TRP PRO SER
SEQRES   5 C  198  LEU PHE LEU GLY ASP ALA TYR ALA ALA ARG ASP LYS SER
SEQRES   6 C  198  LYS LEU ILE GLN LEU GLY ILE THR HIS VAL VAL ASN ALA
SEQRES   7 C  198  ALA ALA GLY LYS PHE GLN VAL ASP THR GLY ALA LYS PHE
SEQRES   8 C  198  TYR ARG GLY MET SER LEU GLU TYR TYR GLY ILE GLU ALA
SEQRES   9 C  198  ASP ASP ASN PRO PHE PHE ASP LEU SER VAL TYR PHE LEU
SEQRES  10 C  198  PRO VAL ALA ARG TYR ILE ARG ALA ALA LEU SER VAL PRO
SEQRES  11 C  198  GLN GLY ARG VAL LEU VAL HIS CYS ALA MET GLY VAL SER
SEQRES  12 C  198  ARG SER ALA THR LEU VAL LEU ALA PHE LEU MET ILE CYS
SEQRES  13 C  198  GLU ASN MET THR LEU VAL GLU ALA ILE GLN THR VAL GLN
SEQRES  14 C  198  ALA HIS ARG ASN ILE CYS PRO ASN SER GLY PHE LEU ARG
SEQRES  15 C  198  GLN LEU GLN VAL LEU ASP ASN ARG LEU GLY ARG GLU THR
SEQRES  16 C  198  GLY ARG PHE
SEQRES   1 D  198  MET ASP SER LEU GLN LYS GLN ASP LEU ARG ARG PRO LYS
SEQRES   2 D  198  ILE HIS GLY ALA VAL GLN ALA SER PRO TYR GLN PRO PRO
SEQRES   3 D  198  THR LEU ALA SER LEU GLN ARG LEU LEU TRP VAL ARG GLN
SEQRES   4 D  198  ALA ALA THR LEU ASN HIS ILE ASP GLU VAL TRP PRO SER
SEQRES   5 D  198  LEU PHE LEU GLY ASP ALA TYR ALA ALA ARG ASP LYS SER
SEQRES   6 D  198  LYS LEU ILE GLN LEU GLY ILE THR HIS VAL VAL ASN ALA
SEQRES   7 D  198  ALA ALA GLY LYS PHE GLN VAL ASP THR GLY ALA LYS PHE
SEQRES   8 D  198  TYR ARG GLY MET SER LEU GLU TYR TYR GLY ILE GLU ALA
SEQRES   9 D  198  ASP ASP ASN PRO PHE PHE ASP LEU SER VAL TYR PHE LEU
SEQRES  10 D  198  PRO VAL ALA ARG TYR ILE ARG ALA ALA LEU SER VAL PRO
SEQRES  11 D  198  GLN GLY ARG VAL LEU VAL HIS CYS ALA MET GLY VAL SER
SEQRES  12 D  198  ARG SER ALA THR LEU VAL LEU ALA PHE LEU MET ILE CYS
SEQRES  13 D  198  GLU ASN MET THR LEU VAL GLU ALA ILE GLN THR VAL GLN
SEQRES  14 D  198  ALA HIS ARG ASN ILE CYS PRO ASN SER GLY PHE LEU ARG
SEQRES  15 D  198  GLN LEU GLN VAL LEU ASP ASN ARG LEU GLY ARG GLU THR
SEQRES  16 D  198  GLY ARG PHE
FORMUL   5  HOH   *260(H2 O)
HELIX    1   1 THR A   27  ARG A   38  1                                  12
HELIX    2   2 ASP A   57  ASP A   63  1                                   7
HELIX    3   3 ASP A   63  LEU A   70  1                                   8
HELIX    4   4 THR A   87  TYR A   92  1                                   6
HELIX    5   5 LEU A  112  VAL A  114  5                                   3
HELIX    6   6 TYR A  115  SER A  128  1                                  14
HELIX    7   7 SER A  143  GLU A  157  1                                  15
HELIX    8   8 THR A  160  ALA A  170  1                                  11
HELIX    9   9 ASN A  177  ARG A  193  1                                  17
HELIX   10  10 THR B   27  VAL B   37  1                                  11
HELIX   11  11 ASP B   57  ARG B   62  1                                   6
HELIX   12  12 ASP B   63  GLY B   71  1                                   9
HELIX   13  13 THR B   87  TYR B   92  1                                   6
HELIX   14  14 ASP B  111  VAL B  114  5                                   4
HELIX   15  15 TYR B  115  SER B  128  1                                  14
HELIX   16  16 SER B  143  GLU B  157  1                                  15
HELIX   17  17 THR B  160  ALA B  170  1                                  11
HELIX   18  18 ASN B  177  GLY B  192  1                                  16
HELIX   19  19 THR C   27  ARG C   38  1                                  12
HELIX   20  20 ASP C   57  ASP C   63  1                                   7
HELIX   21  21 ASP C   63  GLY C   71  1                                   9
HELIX   22  22 THR C   87  TYR C   92  1                                   6
HELIX   23  23 LEU C  112  LEU C  127  1                                  16
HELIX   24  24 SER C  143  ASN C  158  1                                  16
HELIX   25  25 THR C  160  ALA C  170  1                                  11
HELIX   26  26 ASN C  177  THR C  195  1                                  19
HELIX   27  27 THR D   27  ARG D   38  1                                  12
HELIX   28  28 ASP D   57  ASP D   63  1                                   7
HELIX   29  29 ASP D   63  GLY D   71  1                                   9
HELIX   30  30 THR D   87  TYR D   92  1                                   6
HELIX   31  31 LEU D  112  SER D  128  1                                  17
HELIX   32  32 SER D  143  GLU D  157  1                                  15
HELIX   33  33 THR D  160  ALA D  170  1                                  11
HELIX   34  34 ASN D  177  THR D  195  1                                  19
SHEET    1   A 2 THR A  42  ASN A  44  0
SHEET    2   A 2 THR B  42  ASN B  44 -1  O  LEU B  43   N  LEU A  43
SHEET    1   B 5 ILE A  46  TRP A  50  0
SHEET    2   B 5 LEU A  53  GLY A  56 -1  O  LEU A  53   N  TRP A  50
SHEET    3   B 5 VAL A 134  HIS A 137  1  O  VAL A 134   N  PHE A  54
SHEET    4   B 5 HIS A  74  ASN A  77  1  N  VAL A  76   O  LEU A 135
SHEET    5   B 5 GLU A  98  GLY A 101  1  O  GLU A  98   N  VAL A  75
SHEET    1   C 5 ILE B  46  TRP B  50  0
SHEET    2   C 5 LEU B  53  GLY B  56 -1  O  LEU B  53   N  TRP B  50
SHEET    3   C 5 VAL B 134  HIS B 137  1  O  VAL B 134   N  PHE B  54
SHEET    4   C 5 HIS B  74  ASN B  77  1  N  VAL B  76   O  LEU B 135
SHEET    5   C 5 GLU B  98  GLY B 101  1  O  GLU B  98   N  VAL B  75
SHEET    1   D 2 THR C  42  ASN C  44  0
SHEET    2   D 2 THR D  42  ASN D  44 -1  O  LEU D  43   N  LEU C  43
SHEET    1   E 5 ILE C  46  TRP C  50  0
SHEET    2   E 5 LEU C  53  GLY C  56 -1  O  LEU C  53   N  TRP C  50
SHEET    3   E 5 VAL C 134  HIS C 137  1  O  VAL C 134   N  PHE C  54
SHEET    4   E 5 HIS C  74  ASN C  77  1  N  VAL C  76   O  LEU C 135
SHEET    5   E 5 GLU C  98  GLY C 101  1  O  TYR C 100   N  ASN C  77
SHEET    1   F 5 ILE D  46  TRP D  50  0
SHEET    2   F 5 LEU D  53  GLY D  56 -1  O  LEU D  53   N  TRP D  50
SHEET    3   F 5 VAL D 134  HIS D 137  1  O  VAL D 134   N  PHE D  54
SHEET    4   F 5 HIS D  74  ASN D  77  1  N  VAL D  76   O  LEU D 135
SHEET    5   F 5 GLU D  98  GLY D 101  1  O  GLU D  98   N  VAL D  75
CRYST1   61.586   72.240   89.896  90.00  99.66  90.00 P 1 21 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      0.016237  0.000000  0.002764        0.00000
SCALE2      0.000000  0.013843  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011284        0.00000
      
PROCHECK
Go to PROCHECK summary
 References