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PDBsum entry 2h4g

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Hydrolase PDB id
2h4g
Jmol
Contents
Protein chain
297 a.a.
Ligands
694
Waters ×98
HEADER    HYDROLASE                               24-MAY-06   2H4G
TITLE     CRYSTAL STRUCTURE OF PTP1B WITH MONOCYCLIC THIOPHENE
TITLE    2 INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN OF PTP1B;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B, PTP-1B;
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 GENE: PTPN1, PTP1B;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    PROTEIN-DRUG COMPLEX, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.XU,Z.-K.WAN
REVDAT   2   24-FEB-09 2H4G    1       VERSN
REVDAT   1   29-AUG-06 2H4G    0
JRNL        AUTH   Z.K.WAN,J.LEE,W.XU,D.V.ERBE,D.JOSEPH-MCCARTHY,
JRNL        AUTH 2 B.C.FOLLOWS,Y.L.ZHANG
JRNL        TITL   MONOCYCLIC THIOPHENES AS PROTEIN TYROSINE
JRNL        TITL 2 PHOSPHATASE 1B INHIBITORS: CAPTURING INTERACTIONS
JRNL        TITL 3 WITH ASP48.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  4941 2006
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   16806920
JRNL        DOI    10.1016/J.BMCL.2006.06.051
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  TITL   BICYCLIC AND TRICYCLIC THIOPHENES AS PROTEIN
REMARK   1  TITL 2 TYROSINE PHOSPHATASE 1B INHIBITORS
REMARK   1  REF    BIOORG.MED.CHEM.              V.  14  2162 2006
REMARK   1  REFN                   ISSN 0968-0896
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
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)   (%) : 94.9
REMARK   3   NUMBER OF REFLECTIONS             : 15836
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) : 0.193
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 770
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            : 2426
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 21
REMARK   3   SOLVENT ATOMS            : 98
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.84
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.47400
REMARK   3    B22 (A**2) : 1.47400
REMARK   3    B33 (A**2) : -2.94800
REMARK   3    B12 (A**2) : -3.35900
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) : 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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.178 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.947 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.031 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.046 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 27.36
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  : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : 694.PAR
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : CNS_TOPPAR:PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : CNS_TOPPAR:WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2H4G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB037917.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-02
REMARK 200  TEMPERATURE           (KELVIN) : 113
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15836
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9
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) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 63.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.1M HEPES, 0.2M
REMARK 280  MGCL2, PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.69600
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.39200
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       69.39200
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       34.69600
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 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     LEU A   299
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OE1  GLU A   252     O    HOH A   391              2.15
REMARK 500
REMARK 500 REMARK: NULL
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    LEU A 251   C     GLU A 252   N      -0.288
REMARK 500    GLU A 252   C     MET A 253   N      -0.147
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    ASP A  63      -75.46    -50.37
REMARK 500    GLN A  78       33.84     70.05
REMARK 500    GLN A  85      122.51    -23.36
REMARK 500    CYS A 121      141.48   -170.48
REMARK 500    LYS A 131       78.66   -113.30
REMARK 500    LYS A 150     -167.02   -118.17
REMARK 500    CYS A 215     -123.58    -95.04
REMARK 500    ILE A 219      -33.17   -139.08
REMARK 500    ILE A 261      131.65     70.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR A   84     GLN A   85                  146.05
REMARK 500 GLN A   85     GLY A   86                  135.87
REMARK 500 HIS A  214     CYS A  215                  149.03
REMARK 500 ILE A  261     GLN A  262                 -146.82
REMARK 500 MET A  282     GLY A  283                  149.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 694 A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B07   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTP1B WITH TRICYCLIC THIOPHENE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2AZR   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTP1B WITH BICYCLIC THIOPHENE INHIBITOR
REMARK 900 RELATED ID: 2H4K   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTP1B WITH A MONOCYCLIC THIOPHENE
REMARK 900 INHIBITOR
DBREF  2H4G A    1   299  UNP    P18031   PTN1_HUMAN       1    299
SEQRES   1 A  299  MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES   2 A  299  GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES   3 A  299  ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES   4 A  299  ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES   5 A  299  ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES   6 A  299  TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES   7 A  299  ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES   8 A  299  CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES   9 A  299  ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES  10 A  299  SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES  11 A  299  LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES  12 A  299  LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES  13 A  299  GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES  14 A  299  GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES  15 A  299  GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES  16 A  299  PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES  17 A  299  GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG
SEQRES  18 A  299  SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES  19 A  299  MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES  20 A  299  LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES  21 A  299  ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES  22 A  299  VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES  23 A  299  VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP LEU
HET    694  A 300      21
HETNAM     694 4-BROMO-3-(CARBOXYMETHOXY)-5-(4-HYDROXYPHENYL)
HETNAM   2 694  THIOPHENE-2-CARBOXYLIC ACID
FORMUL   2  694    C13 H9 BR O6 S
FORMUL   3  HOH   *98(H2 O)
HELIX    1   1 GLU A    2  SER A   13  1                                  12
HELIX    2   2 SER A   15  ALA A   27  1                                  13
HELIX    3   3 LEU A   37  ASN A   44  5                                   8
HELIX    4   4 THR A   91  GLN A  102  1                                  12
HELIX    5   5 SER A  187  SER A  201  1                                  15
HELIX    6   6 GLY A  220  LYS A  239  1                                  20
HELIX    7   7 ASP A  240  VAL A  244  5                                   5
HELIX    8   8 ASP A  245  ARG A  254  1                                  10
HELIX    9   9 THR A  263  MET A  282  1                                  20
HELIX   10  10 SER A  285  HIS A  296  1                                  12
SHEET    1   A 8 ALA A  69  MET A  74  0
SHEET    2   A 8 ARG A  79  THR A  84 -1  O  TYR A  81   N  ILE A  72
SHEET    3   A 8 VAL A 211  HIS A 214  1  O  VAL A 213   N  ILE A  82
SHEET    4   A 8 GLY A 106  MET A 109  1  N  VAL A 108   O  VAL A 212
SHEET    5   A 8 GLU A 167  TYR A 176  1  O  TYR A 176   N  MET A 109
SHEET    6   A 8 TYR A 153  ASN A 162 -1  N  ARG A 156   O  HIS A 173
SHEET    7   A 8 LEU A 140  ILE A 149 -1  N  ILE A 145   O  GLN A 157
SHEET    8   A 8 MET A 133  PHE A 135 -1  N  MET A 133   O  LEU A 142
SHEET    1   B 2 MET A 114  GLU A 115  0
SHEET    2   B 2 SER A 118  LEU A 119 -1  O  SER A 118   N  GLU A 115
SITE     1 AC1 13 TYR A  46  ASP A  48  LYS A 120  PHE A 182
SITE     2 AC1 13 CYS A 215  SER A 216  ILE A 219  GLY A 220
SITE     3 AC1 13 ARG A 221  GLN A 262  GLN A 266  HOH A 304
SITE     4 AC1 13 HOH A 326
CRYST1   88.365   88.365  104.088  90.00  90.00 120.00 P 31 2 1      6
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      0.011317  0.006534  0.000000        0.00000
SCALE2      0.000000  0.013067  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009607        0.00000
      
PROCHECK
Go to PROCHECK summary
 References