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PDBsum entry 1yts

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Hydrolase PDB id
1yts
Jmol
Contents
Protein chain
278 a.a.
Ligands
SO4 ×2
Waters ×60
HEADER    HYDROLASE                               07-APR-95   1YTS
TITLE     A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA
TITLE    2 PROTEIN TYROSINE PHOSPHATASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: YERSINIA PROTEIN TYROSINE PHOSPHATASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.1.3.48;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA ENTEROCOLITICA;
SOURCE   3 ORGANISM_TAXID: 630;
SOURCE   4 STRAIN: W22703;
SOURCE   5 GENE: YOP51;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE  10 EXPRESSION_SYSTEM_GENE: YOP51
KEYWDS    PROTEIN TYROSINE PHOSPHATASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.L.SCHUBERT,J.A.STUCKEY,E.B.FAUMAN,J.E.DIXON,M.A.SAPER
REVDAT   2   24-FEB-09 1YTS    1       VERSN
REVDAT   1   10-JUL-95 1YTS    0
JRNL        AUTH   H.L.SCHUBERT,E.B.FAUMAN,J.A.STUCKEY,J.E.DIXON,
JRNL        AUTH 2 M.A.SAPER
JRNL        TITL   A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE
JRNL        TITL 2 YERSINIA PROTEIN TYROSINE PHOSPHATASE.
JRNL        REF    PROTEIN SCI.                  V.   4  1904 1995
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   8528087
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   Z.-Y.ZHANG,Y.WANG,J.E.DIXON
REMARK   1  TITL   DISSECTING THE CATALYTIC MECHANISM OF
REMARK   1  TITL 2 PROTEIN-TYROSINE PHOSPHATASES
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  91  1624 1994
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 2
REMARK   1  AUTH   J.A.STUCKEY,H.L.SCHUBERT,E.B.FAUMAN,Z.-Y.ZHANG,
REMARK   1  AUTH 2 J.E.DIXON,M.A.SAPER
REMARK   1  TITL   CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE
REMARK   1  TITL 2 PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH
REMARK   1  TITL 3 TUNGSTATE
REMARK   1  REF    NATURE                        V. 370   571 1994
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 3
REMARK   1  AUTH   Z.-Y.ZHANG,J.C.CLEMENS,H.L.SCHUBERT,J.A.STUCKEY,
REMARK   1  AUTH 2 M.W.F.FISCHER,D.M.HUME,M.A.SAPER,J.E.DIXON
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND PHYSICOCHEMICAL
REMARK   1  TITL 2 CHARACTERIZATION OF A RECOMBINANT YERSINIA PROTEIN
REMARK   1  TITL 3 TYROSINE PHOSPHATASE
REMARK   1  REF    J.BIOL.CHEM.                  V. 267 23759 1992
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
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) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
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             : 9156
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) : 0.174
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
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            : 2137
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 60
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.43
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) : 0.020
REMARK   3   BOND ANGLES            (DEGREES) : 3.70
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 1YTS 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        : 30-JUL-92
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9156
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0
REMARK 200  DATA REDUNDANCY                : 2.490
REMARK 200  R MERGE                    (I) : 0.05200
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOLECULE: YERSINIA PROTEIN TYROSINE
REMARK 280  PHOSPHATASE CYS(403)SER COMPLEXED WITH SULFATE. THE CATALYTIC
REMARK 280  DOMAIN (RESIDUES 163 - 468) OF YOP51 WAS CRYSTALLIZED AT 23
REMARK 280  DEGREES CELSIUS, IN A SOLUTION OF 18 - 24% POLYETHYLENE GLYCOL
REMARK 280  (MW 4000), 5% 2-METHYL-2,4-PENTANEDIOL, 0.1% BETA-
REMARK 280  MERCAPTOETHANOL, 200MM LI2SO4, 0.1M TRIS-HCL, PH 8.5,
REMARK 280  TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       28.20000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.20000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.90000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.20000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.20000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.90000
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: 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 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    HIS A 350   NE2   HIS A 350   CD2    -0.085
REMARK 500    HIS A 402   NE2   HIS A 402   CD2    -0.068
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    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A 205   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ASN A 213   CA  -  CB  -  CG  ANGL. DEV. = -15.2 DEGREES
REMARK 500    CYS A 221   CA  -  C   -  N   ANGL. DEV. = -14.2 DEGREES
REMARK 500    ARG A 228   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    GLN A 233   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES
REMARK 500    CYS A 234   CA  -  CB  -  SG  ANGL. DEV. =  10.4 DEGREES
REMARK 500    ARG A 235   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG A 236   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 241   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG A 255   NE  -  CZ  -  NH2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    THR A 256   CA  -  CB  -  CG2 ANGL. DEV. =   8.6 DEGREES
REMARK 500    SER A 265   CA  -  CB  -  OG  ANGL. DEV. =  17.7 DEGREES
REMARK 500    ARG A 272   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 278   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 295   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    MET A 331   CA  -  CB  -  CG  ANGL. DEV. = -16.5 DEGREES
REMARK 500    MET A 331   CG  -  SD  -  CE  ANGL. DEV. = -19.8 DEGREES
REMARK 500    TYR A 332   CB  -  CG  -  CD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 337   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    TRP A 354   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES
REMARK 500    TRP A 354   CG  -  CD2 -  CE3 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ARG A 380   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A 380   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A 383   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    VAL A 391   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.9 DEGREES
REMARK 500    ARG A 423   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ASP A 431   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    VAL A 433   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.9 DEGREES
REMARK 500    ARG A 440   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 463   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 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 235      121.50    -38.09
REMARK 500    THR A 318      -77.46   -111.57
REMARK 500    ASP A 325       18.09     56.86
REMARK 500    ASN A 353       42.83   -140.44
REMARK 500    PRO A 399      125.50    -34.53
REMARK 500    SER A 403     -112.83   -125.01
REMARK 500    MET A 419        3.75    -67.61
REMARK 500    ASN A 424       55.98   -113.02
REMARK 500    GLN A 426       -0.31     68.64
REMARK 500    ARG A 440      -67.94   -136.86
REMARK 500    VAL A 445       78.36     57.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PL
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE PHOSPHATE BINDING LOOP WHICH IS BELIEVED
REMARK 800  TO BE STRUCTURALLY CONSERVED IN ALL PROTEIN TYROSINE
REMARK 800  PHOSPHATASES
REMARK 800 SITE_IDENTIFIER: WPD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE FLEXIBLE LOOP CONTAINING THE PUTATIVE
REMARK 800  GENERAL ACID, ASP 356, THAT FOLDS OVER THE SULFATE ANION IN
REMARK 800  THE SULFATE-BOUND STRUCTURE.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 YERSINIA PROTEIN TYROSINE PHOSPHATASE.
REMARK 999   ONLY THE CATALYTIC DOMAIN (RESIDUES 163 - 468) WAS
REMARK 999   CRYSTALLIZED.  THE 235 CYS TO ARG MUTATION WAS
REMARK 999   UNINTENTIONAL AND MOST LIKELY THE RESULT OF USING PCR TO
REMARK 999   CONSTRUCT THE PLASMID.  THE
REMARK 999   403 CYS TO SER MUTATION ELIMINATES ALL PTPASE CATALYTIC
REMARK 999   ACTIVITY.
DBREF  1YTS A  191   468  UNP    P15273   YOPH_YEREN     191    468
SEQADV 1YTS ARG A  235  UNP  P15273    CYS   235 CONFLICT
SEQADV 1YTS SER A  403  UNP  P15273    CYS   403 CONFLICT
SEQRES   1 A  278  PRO GLU ALA ARG ALA GLU LEU SER SER ARG LEU THR THR
SEQRES   2 A  278  LEU ARG ASN THR LEU ALA PRO ALA THR ASN ASP PRO ARG
SEQRES   3 A  278  TYR LEU GLN ALA CYS GLY GLY GLU LYS LEU ASN ARG PHE
SEQRES   4 A  278  ARG ASP ILE GLN CYS ARG ARG GLN THR ALA VAL ARG ALA
SEQRES   5 A  278  ASP LEU ASN ALA ASN TYR ILE GLN VAL GLY ASN THR ARG
SEQRES   6 A  278  THR ILE ALA CYS GLN TYR PRO LEU GLN SER GLN LEU GLU
SEQRES   7 A  278  SER HIS PHE ARG MET LEU ALA GLU ASN ARG THR PRO VAL
SEQRES   8 A  278  LEU ALA VAL LEU ALA SER SER SER GLU ILE ALA ASN GLN
SEQRES   9 A  278  ARG PHE GLY MET PRO ASP TYR PHE ARG GLN SER GLY THR
SEQRES  10 A  278  TYR GLY SER ILE THR VAL GLU SER LYS MET THR GLN GLN
SEQRES  11 A  278  VAL GLY LEU GLY ASP GLY ILE MET ALA ASP MET TYR THR
SEQRES  12 A  278  LEU THR ILE ARG GLU ALA GLY GLN LYS THR ILE SER VAL
SEQRES  13 A  278  PRO VAL VAL HIS VAL GLY ASN TRP PRO ASP GLN THR ALA
SEQRES  14 A  278  VAL SER SER GLU VAL THR LYS ALA LEU ALA SER LEU VAL
SEQRES  15 A  278  ASP GLN THR ALA GLU THR LYS ARG ASN MET TYR GLU SER
SEQRES  16 A  278  LYS GLY SER SER ALA VAL ALA ASP ASP SER LYS LEU ARG
SEQRES  17 A  278  PRO VAL ILE HIS SER ARG ALA GLY VAL GLY ARG THR ALA
SEQRES  18 A  278  GLN LEU ILE GLY ALA MET CYS MET ASN ASP SER ARG ASN
SEQRES  19 A  278  SER GLN LEU SER VAL GLU ASP MET VAL SER GLN MET ARG
SEQRES  20 A  278  VAL GLN ARG ASN GLY ILE MET VAL GLN LYS ASP GLU GLN
SEQRES  21 A  278  LEU ASP VAL LEU ILE LYS LEU ALA GLU GLY GLN GLY ARG
SEQRES  22 A  278  PRO LEU LEU ASN SER
HET    SO4  A   1       5
HET    SO4  A   2       5
HETNAM     SO4 SULFATE ION
FORMUL   2  SO4    2(O4 S 2-)
FORMUL   4  HOH   *60(H2 O)
HELIX    1   1 GLU A  192  THR A  207  1                                  16
HELIX    2   2 ARG A  236  THR A  238  5                                   3
HELIX    3   3 GLN A  264  GLU A  276  5                                  13
HELIX    4   4 SER A  288  ALA A  292  1                                   5
HELIX    5   5 GLN A  294  PHE A  296  5                                   3
HELIX    6   6 SER A  362  LYS A  386  1                                  25
HELIX    7   7 ALA A  390  ALA A  392  5                                   3
HELIX    8   8 ARG A  409  ASN A  420  1                                  12
HELIX    9   9 VAL A  429  GLN A  439  1                                  11
HELIX   10  10 ASP A  448  GLN A  461  1                                  14
SHEET    1   A 8 ALA A 246  VAL A 251  0
SHEET    2   A 8 THR A 254  CYS A 259 -1  N  ALA A 258   O  ASN A 247
SHEET    3   A 8 PRO A 399  HIS A 402  1  N  PRO A 399   O  ILE A 257
SHEET    4   A 8 LEU A 282  VAL A 284  1  N  ALA A 283   O  VAL A 400
SHEET    5   A 8 ILE A 344  VAL A 351  1  N  VAL A 349   O  LEU A 282
SHEET    6   A 8 ALA A 329  GLU A 338 -1  N  ILE A 336   O  ILE A 344
SHEET    7   A 8 ILE A 311  MET A 317 -1  N  LYS A 316   O  THR A 333
SHEET    8   A 8 GLY A 306  TYR A 308 -1  N  TYR A 308   O  ILE A 311
SHEET    1   B 2 GLN A 320  GLY A 324  0
SHEET    2   B 2 ILE A 327  ASP A 330 -1  N  ALA A 329   O  VAL A 321
SITE     1  PL  9 HIS A 402  SER A 403  ARG A 404  ALA A 405
SITE     2  PL  9 GLY A 406  VAL A 407  GLY A 408  ARG A 409
SITE     3  PL  9 THR A 410
SITE     1 WPD 11 HIS A 350  VAL A 351  GLY A 352  ASN A 353
SITE     2 WPD 11 TRP A 354  PRO A 355  ASP A 356  GLN A 357
SITE     3 WPD 11 THR A 358  ALA A 359  VAL A 360
SITE     1 AC1  9 ASP A 356  SER A 403  ARG A 404  ALA A 405
SITE     2 AC1  9 GLY A 406  VAL A 407  GLY A 408  ARG A 409
SITE     3 AC1  9 HOH A 522
SITE     1 AC2  4 ARG A 278  SER A 388  SER A 389  ALA A 390
CRYST1   56.400   49.800  100.400  90.00  90.00  90.00 P 21 21 21    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      0.017730  0.000000  0.000000        0.00000
SCALE2      0.000000  0.020080  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009960        0.00000
      
PROCHECK
Go to PROCHECK summary
 References