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PDBsum entry 1vhr

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Hydrolase PDB id
1vhr
Jmol
Contents
Protein chains
178 a.a. *
Ligands
EPE
SO4
Waters ×141
* Residue conservation analysis
HEADER    HYDROLASE                               20-FEB-96   1VHR
TITLE     HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE
COMPND   3 VHR;
COMPND   4 CHAIN: A, B;
COMPND   5 SYNONYM: VHR;
COMPND   6 EC: 3.1.3.48;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PT7-7-VHR;
SOURCE   9 OTHER_DETAILS: ORIGINAL GENE GDB\:DUSP3; VHR, CHROMOSOME
SOURCE  10 MAP POSITION 17Q21
KEYWDS    HYDROLASE, PROTEIN DUAL-SPECIFICITY PHOSPHATASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.YUVANIYAMA,J.M.DENU,J.E.DIXON,M.A.SAPER
REVDAT   2   24-FEB-09 1VHR    1       VERSN
REVDAT   1   20-JUN-96 1VHR    0
JRNL        AUTH   J.YUVANIYAMA,J.M.DENU,J.E.DIXON,M.A.SAPER
JRNL        TITL   CRYSTAL STRUCTURE OF THE DUAL SPECIFICITY PROTEIN
JRNL        TITL 2 PHOSPHATASE VHR.
JRNL        REF    SCIENCE                       V. 272  1328 1996
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   8650541
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.M.DENU,G.ZHOU,L.WU,R.ZHAO,J.YUVANIYAMA,M.A.SAPER,
REMARK   1  AUTH 2 J.E.DIXON
REMARK   1  TITL   THE PURIFICATION AND CHARACTERIZATION OF A HUMAN
REMARK   1  TITL 2 DUAL-SPECIFIC PROTEIN TYROSINE PHOSPHATASE
REMARK   1  REF    J.BIOL.CHEM.                  V. 270  3796 1995
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 2
REMARK   1  AUTH   G.ZHOU,J.M.DENU,L.WU,J.E.DIXON
REMARK   1  TITL   THE CATALYTIC ROLE OF CYS124 IN THE DUAL
REMARK   1  TITL 2 SPECIFICITY PHOSPHATASE VHR
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 28084 1994
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 3
REMARK   1  AUTH   T.ISHIBASHI,D.P.BOTTARO,A.CHAN,T.MIKI,S.A.AARONSON
REMARK   1  TITL   EXPRESSION CLONING OF A HUMAN DUAL-SPECIFICITY
REMARK   1  TITL 2 PHOSPHATASE
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  89 12170 1992
REMARK   1  REFN                   ISSN 0027-8424
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
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)   (%) : 86.4
REMARK   3   NUMBER OF REFLECTIONS             : 18746
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.254
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.960
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 2768
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 141
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.70
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) : 0.016
REMARK   3   BOND ANGLES            (DEGREES) : 1.65
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.72
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.87
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 1VHR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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        : 27-NOV-94
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
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                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : XUONG-HAMLIN MULTIWIRE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES, XDS
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18952
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.4
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : 0.05500
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR SOFTWARE USED :
REMARK 200  PHASES STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE FULL-LENGTH VHR (RESIDUES 2 -
REMARK 280  185) WAS CRYSTALLIZED AT A CONCENTRATION OF 5-6 MG/ML WITH 14%
REMARK 280  POLYETHYLENE GLYCOL 4000, 22.5 MM LITHIUM SULFATE, 50 MM HEPES
REMARK 280  PH 7.0, AND 0.05% BETA-MERCAPTOETHANOL IN A HANGING DROP OF 20
REMARK 280  MICROLITERS. THE DROP WAS EQUILIBRATED AGAINST 1 ML OF TWICE
REMARK 280  THE CONCENTRATION OF PRECIPITANT SOLUTION AT 23 DEGREE
REMARK 280  CELSIUS., VAPOR DIFFUSION - HANGING DROP, TEMPERATURE 296K
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       30.02000
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
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 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     SER A     2
REMARK 465     GLY A     3
REMARK 465     SER A     4
REMARK 465     PHE A     5
REMARK 465     GLU A     6
REMARK 465     LEU A     7
REMARK 465     SER B     2
REMARK 465     GLY B     3
REMARK 465     SER B     4
REMARK 465     PHE B     5
REMARK 465     GLU B     6
REMARK 465     LEU B     7
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  20      144.76    179.84
REMARK 500    ASP A  47       78.50   -104.38
REMARK 500    ASP A  80       -8.86     84.29
REMARK 500    CYS A 124     -148.12   -146.66
REMARK 500    ASP B  18     -174.02    -68.37
REMARK 500    ALA B  63       44.04   -146.14
REMARK 500    CYS B 124     -143.64   -141.64
REMARK 500    SER B 129      -61.06   -122.54
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 602        DISTANCE =  6.65 ANGSTROMS
REMARK 525    HOH A 603        DISTANCE =  7.51 ANGSTROMS
REMARK 525    HOH B 667        DISTANCE =  7.50 ANGSTROMS
REMARK 525    HOH B 668        DISTANCE =  6.13 ANGSTROMS
REMARK 525    HOH B 669        DISTANCE =  8.49 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RCA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: DESIGNATED RECOGNITION REGION IN PRIMARY
REMARK 800  REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
REMARK 800 SITE_IDENTIFIER: RCB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: DESIGNATED RECOGNITION REGION IN PRIMARY
REMARK 800  REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
REMARK 800 SITE_IDENTIFIER: VRA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE REGION CONTAINING HIGH VARIATION AMONG
REMARK 800  THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE
REMARK 800  PHOSPHATASES.
REMARK 800 SITE_IDENTIFIER: VRB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE REGION CONTAINING HIGH VARIATION AMONG
REMARK 800  THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE
REMARK 800  PHOSPHATASES.
REMARK 800 SITE_IDENTIFIER: GAA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE LOOP CONTAINING THE PUTATIVE GENERAL ACID
REMARK 800  ASP 92.
REMARK 800 SITE_IDENTIFIER: GAB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE LOOP CONTAINING THE PUTATIVE GENERAL ACID
REMARK 800  ASP 92.
REMARK 800 SITE_IDENTIFIER: PLA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHATE BINDING LOOP INCLUDING CATALYTIC
REMARK 800  NUCLEOPHILE CYS 130
REMARK 800 SITE_IDENTIFIER: PLB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHATE BINDING LOOP INCLUDING CATALYTIC
REMARK 800  NUCLEOPHILE CYS 130
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 401
DBREF  1VHR A    2   185  UNP    P51452   DUS3_HUMAN       2    185
DBREF  1VHR B    2   185  UNP    P51452   DUS3_HUMAN       2    185
SEQRES   1 A  184  SER GLY SER PHE GLU LEU SER VAL GLN ASP LEU ASN ASP
SEQRES   2 A  184  LEU LEU SER ASP GLY SER GLY CYS TYR SER LEU PRO SER
SEQRES   3 A  184  GLN PRO CYS ASN GLU VAL THR PRO ARG ILE TYR VAL GLY
SEQRES   4 A  184  ASN ALA SER VAL ALA GLN ASP ILE PRO LYS LEU GLN LYS
SEQRES   5 A  184  LEU GLY ILE THR HIS VAL LEU ASN ALA ALA GLU GLY ARG
SEQRES   6 A  184  SER PHE MET HIS VAL ASN THR ASN ALA ASN PHE TYR LYS
SEQRES   7 A  184  ASP SER GLY ILE THR TYR LEU GLY ILE LYS ALA ASN ASP
SEQRES   8 A  184  THR GLN GLU PHE ASN LEU SER ALA TYR PHE GLU ARG ALA
SEQRES   9 A  184  ALA ASP PHE ILE ASP GLN ALA LEU ALA GLN LYS ASN GLY
SEQRES  10 A  184  ARG VAL LEU VAL HIS CYS ARG GLU GLY TYR SER ARG SER
SEQRES  11 A  184  PRO THR LEU VAL ILE ALA TYR LEU MET MET ARG GLN LYS
SEQRES  12 A  184  MET ASP VAL LYS SER ALA LEU SER ILE VAL ARG GLN ASN
SEQRES  13 A  184  ARG GLU ILE GLY PRO ASN ASP GLY PHE LEU ALA GLN LEU
SEQRES  14 A  184  CYS GLN LEU ASN ASP ARG LEU ALA LYS GLU GLY LYS LEU
SEQRES  15 A  184  LYS PRO
SEQRES   1 B  184  SER GLY SER PHE GLU LEU SER VAL GLN ASP LEU ASN ASP
SEQRES   2 B  184  LEU LEU SER ASP GLY SER GLY CYS TYR SER LEU PRO SER
SEQRES   3 B  184  GLN PRO CYS ASN GLU VAL THR PRO ARG ILE TYR VAL GLY
SEQRES   4 B  184  ASN ALA SER VAL ALA GLN ASP ILE PRO LYS LEU GLN LYS
SEQRES   5 B  184  LEU GLY ILE THR HIS VAL LEU ASN ALA ALA GLU GLY ARG
SEQRES   6 B  184  SER PHE MET HIS VAL ASN THR ASN ALA ASN PHE TYR LYS
SEQRES   7 B  184  ASP SER GLY ILE THR TYR LEU GLY ILE LYS ALA ASN ASP
SEQRES   8 B  184  THR GLN GLU PHE ASN LEU SER ALA TYR PHE GLU ARG ALA
SEQRES   9 B  184  ALA ASP PHE ILE ASP GLN ALA LEU ALA GLN LYS ASN GLY
SEQRES  10 B  184  ARG VAL LEU VAL HIS CYS ARG GLU GLY TYR SER ARG SER
SEQRES  11 B  184  PRO THR LEU VAL ILE ALA TYR LEU MET MET ARG GLN LYS
SEQRES  12 B  184  MET ASP VAL LYS SER ALA LEU SER ILE VAL ARG GLN ASN
SEQRES  13 B  184  ARG GLU ILE GLY PRO ASN ASP GLY PHE LEU ALA GLN LEU
SEQRES  14 B  184  CYS GLN LEU ASN ASP ARG LEU ALA LYS GLU GLY LYS LEU
SEQRES  15 B  184  LYS PRO
HET    SO4  B 502       5
HET    EPE  A 401      15
HETNAM     SO4 SULFATE ION
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN     EPE HEPES
FORMUL   3  SO4    O4 S 2-
FORMUL   4  EPE    C8 H18 N2 O4 S
FORMUL   5  HOH   *141(H2 O)
HELIX    1   1 VAL A    9  LEU A   16  1                                   8
HELIX    2   2 ALA A   42  ALA A   45  1                                   4
HELIX    3   3 ILE A   48  LEU A   54  1                                   7
HELIX    4   4 ALA A   75  TYR A   78  1                                   4
HELIX    5   5 LEU A   98  LEU A  113  5                                  16
HELIX    6   6 ARG A  130  ARG A  142  1                                  13
HELIX    7   7 VAL A  147  ASN A  157  1                                  11
HELIX    8   8 ASP A  164  LYS A  179  1                                  16
HELIX    9   9 VAL B    9  LEU B   16  1                                   8
HELIX   10  10 ALA B   42  ALA B   45  1                                   4
HELIX   11  11 ILE B   48  LYS B   53  1                                   6
HELIX   12  12 LEU B   98  ALA B  114  5                                  17
HELIX   13  13 ARG B  130  GLN B  143  1                                  14
HELIX   14  14 VAL B  147  ASN B  157  1                                  11
HELIX   15  15 ASP B  164  LYS B  179  1                                  16
SHEET    1   A 5 THR A  84  GLY A  87  0
SHEET    2   A 5 HIS A  58  ASN A  61  1  N  VAL A  59   O  THR A  84
SHEET    3   A 5 VAL A 120  HIS A 123  1  N  LEU A 121   O  HIS A  58
SHEET    4   A 5 ILE A  37  GLY A  40  1  N  TYR A  38   O  VAL A 120
SHEET    5   A 5 CYS A  30  THR A  34 -1  N  THR A  34   O  ILE A  37
SHEET    1   B 5 THR B  84  GLY B  87  0
SHEET    2   B 5 HIS B  58  ASN B  61  1  N  VAL B  59   O  THR B  84
SHEET    3   B 5 VAL B 120  HIS B 123  1  N  LEU B 121   O  HIS B  58
SHEET    4   B 5 ILE B  37  GLY B  40  1  N  TYR B  38   O  VAL B 120
SHEET    5   B 5 CYS B  30  THR B  34 -1  N  THR B  34   O  ILE B  37
SITE     1 RCA 11 GLY A  19  SER A  20  GLY A  21  CYS A  22
SITE     2 RCA 11 TYR A  23  SER A  24  LEU A  25  PRO A  26
SITE     3 RCA 11 SER A  27  GLN A  28  PRO A  29
SITE     1 RCB 11 GLY B  19  SER B  20  GLY B  21  CYS B  22
SITE     2 RCB 11 TYR B  23  SER B  24  LEU B  25  PRO B  26
SITE     3 RCB 11 SER B  27  GLN B  28  PRO B  29
SITE     1 VRA 21 ALA A  62  ALA A  63  GLU A  64  GLY A  65
SITE     2 VRA 21 ARG A  66  SER A  67  PHE A  68  MET A  69
SITE     3 VRA 21 HIS A  70  VAL A  71  ASN A  72  THR A  73
SITE     4 VRA 21 ASN A  74  ALA A  75  ASN A  76  PHE A  77
SITE     5 VRA 21 TYR A  78  LYS A  79  ASP A  80  SER A  81
SITE     6 VRA 21 GLY A  82
SITE     1 VRB 21 ALA B  62  ALA B  63  GLU B  64  GLY B  65
SITE     2 VRB 21 ARG B  66  SER B  67  PHE B  68  MET B  69
SITE     3 VRB 21 HIS B  70  VAL B  71  ASN B  72  THR B  73
SITE     4 VRB 21 ASN B  74  ALA B  75  ASN B  76  PHE B  77
SITE     5 VRB 21 TYR B  78  LYS B  79  ASP B  80  SER B  81
SITE     6 VRB 21 GLY B  82
SITE     1 GAA 11 ILE A  88  LYS A  89  ALA A  90  ASN A  91
SITE     2 GAA 11 ASP A  92  THR A  93  GLN A  94  GLU A  95
SITE     3 GAA 11 PHE A  96  ASN A  97  LEU A  98
SITE     1 GAB 11 ILE B  88  LYS B  89  ALA B  90  ASN B  91
SITE     2 GAB 11 ASP B  92  THR B  93  GLN B  94  GLU B  95
SITE     3 GAB 11 PHE B  96  ASN B  97  LEU B  98
SITE     1 PLA  9 HIS A 123  CYS A 124  ARG A 125  GLU A 126
SITE     2 PLA  9 GLY A 127  TYR A 128  SER A 129  ARG A 130
SITE     3 PLA  9 SER A 131
SITE     1 PLB  9 HIS B 123  CYS B 124  ARG B 125  GLU B 126
SITE     2 PLB  9 GLY B 127  TYR B 128  SER B 129  ARG B 130
SITE     3 PLB  9 SER B 131
SITE     1 AC1  9 ASP B  92  CYS B 124  ARG B 125  GLU B 126
SITE     2 AC1  9 GLY B 127  TYR B 128  SER B 129  ARG B 130
SITE     3 AC1  9 HOH B 657
SITE     1 AC2  8 ASP A  92  CYS A 124  ARG A 125  GLU A 126
SITE     2 AC2  8 GLY A 127  TYR A 128  SER A 129  ARG A 130
CRYST1   61.148   60.040   52.016  90.00  98.35  90.00 P 1 21 1      4
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      0.016354  0.000000  0.002400        0.00000
SCALE2      0.000000  0.016656  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019431        0.00000
MTRIX1   1 -0.962481 -0.060958 -0.264412       28.16632    1
MTRIX2   1 -0.050633  0.997671 -0.045694       29.73183    1
MTRIX3   1  0.266582 -0.030591 -0.963327       25.95833    1
      
PROCHECK
Go to PROCHECK summary
 References