HEADER    COMPLEX (OPERON REPRESSOR/PEPTIDE)      12-MAY-95   1WRS
TITLE     NMR STUDY OF HOLO TRP REPRESSOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HOLO TRP REPRESSOR;
COMPND   3 CHAIN: R, S;
COMPND   4 MOL_ID: 2;
COMPND   5 MOLECULE: TRP;
COMPND   6 CHAIN: V, W;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 STRAIN: CY15070 AND CY17071;
SOURCE   4 MOL_ID: 2;
SOURCE   5 SYNTHETIC: YES
KEYWDS    OPERON REPRESSOR, TRANSCRIPTION REGULATION, DNA-BINDING,
KEYWDS   2 PEPTIDE
EXPDTA    NMR, 15 STRUCTURES
AUTHOR    D.ZHAO,Z.ZHENG
REVDAT   1   20-JUN-96 1WRS    0
JRNL        AUTH   D.ZHAO,C.H.ARROWSMITH,X.JIA,O.JARDETZKY
JRNL        TITL   REFINED SOLUTION STRUCTURES OF THE ESCHERICHIA COLI
JRNL        TITL 2 TRP HOLO- AND APOREPRESSOR
JRNL        REF    J.MOL.BIOL.                   V. 229   735 1993
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                 0070
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   H.ZHANG,D.ZHAO,M.REVINGTON,W.LEE,X.JIA,
REMARK   1  AUTH 2 C.ARROWSMITH,O.JARDETZKY
REMARK   1  TITL   THE SOLUTION STRUCTURES OF THE TRP
REMARK   1  TITL 2 REPRESSOR-OPERATOR DNA COMPLEX
REMARK   1  REF    J.MOL.BIOL.                   V. 238   592 1994
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                 0070
REMARK   1 REFERENCE 2
REMARK   1  AUTH   D.ZHAO,O.JARDETZKY
REMARK   1  TITL   SEQUENTIAL SIMULATED ANNEALING: AN EFFICIENT
REMARK   1  TITL 2 PROCEDURE FOR STRUCTURAL REFINEMENT BASED ON NMR
REMARK   1  TITL 3 CONSTRAINTS
REMARK   1  REF    J.PHYS.CHEM.                  V.  97  3007 1993
REMARK   1  REFN   ASTM JPCHAX  US ISSN 0022-3654                 0037
REMARK   1 REFERENCE 3
REMARK   1  AUTH   C.ARROWSMITH,R.PACHTER,R.ALTMAN,O.JARDETZKY
REMARK   1  TITL   THE SOLUTION STRUCTURES OF ESCHERICHIA COLI TRP
REMARK   1  TITL 2 REPRESSOR AND TRP APOREPRESSOR AT AN INTERMEDIATE
REMARK   1  TITL 3 RESOLUTION
REMARK   1  REF    EUR.J.BIOCHEM.                V. 202    53 1991
REMARK   1  REFN   ASTM EJBCAI  IX ISSN 0014-2956                 0262
REMARK   1 REFERENCE 4
REMARK   1  AUTH   C.H.ARROWSMITH,R.PACHTER,R.B.ALTMAN,S.B.IYER,
REMARK   1  AUTH 2 O.JARDETZKY
REMARK   1  TITL   SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SECONDARY
REMARK   1  TITL 2 STRUCTURE IN SOLUTION OF ESCHERICHIA COLI TRP
REMARK   1  TITL 3 REPRESSOR
REMARK   1  REF    BIOCHEMISTRY                  V.  29  6332 1990
REMARK   1  REFN   ASTM BICHAW  US ISSN 0006-2960                 0033
REMARK   1 REFERENCE 5
REMARK   1  AUTH   C.H.ARROWSMITH,J.CAREY,L.TREAT-CLEMONS,O.JARDETZKY
REMARK   1  TITL   NMR ASSIGNMENTS FOR THE AMINO-TERMINAL RESIDUES OF
REMARK   1  TITL 2 TRP REPRESSOR AND THEIR ROLE IN DNA BINDING
REMARK   1  REF    BIOCHEMISTRY                  V.  28  3875 1989
REMARK   1  REFN   ASTM BICHAW  US ISSN 0006-2960                 0033
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.01
REMARK   3   BOND ANGLES            (DEGREES) : 2.1
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3   DISTANCE RESTRAINTS        1510
REMARK   3   DIHEDRAL ANGLE RESTRAINTS  292
REMARK   3   RMSD VERSUS MEAN (BACKBONE ATOMS OF THE ABC CORE)
REMARK   3                              0.7+/-0.2 ANGSTROMS
REMARK   3   RMSD NOE RESTRAINT VIOLATIONS
REMARK   3                              0.066  ANGSTROMS
REMARK   3   RMSD DIHEDRAL RESTRAINT VIOLATIONS
REMARK   3                              1.     DEGREES
REMARK   4
REMARK   4 1WRS COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996
REMARK   6
REMARK   6 TRP REPRESSOR IS A STABLE DIMERIC PROTEIN WITH TWO
REMARK   6 L-TRYPTOPHAN LIGANDS.  ANY ANALYSIS OF THIS STRUCTURE
REMARK   6 REQUIRES THAT A FULL DIMER BE OBSERVED AT ONE TIME.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : NULL
REMARK 210  PH                             : NULL
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL
REMARK 210  SPECTROMETER MODEL             : NULL
REMARK 210  SPECTROMETER MANUFACTURER      : NULL
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : NULL
REMARK 210   METHOD USED                   : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1WRS  R    SWS     P03032       1 -     2 NOT IN ATOMS LIST
REMARK 999 1WRS  R    SWS     P03032     107 -   107 NOT IN ATOMS LIST
REMARK 999 1WRS  S    SWS     P03032       1 -     2 NOT IN ATOMS LIST
REMARK 999 1WRS  S    SWS     P03032     107 -   107 NOT IN ATOMS LIST
DBREF  1WRS R    4   107  SWS    P03032   TRPR_ECOLI       3    106
DBREF  1WRS S    4   107  SWS    P03032   TRPR_ECOLI       3    106
DBREF  1WRS V    1     1  PDB    1WRS     1WRS             1      1
DBREF  1WRS W    1     1  PDB    1WRS     1WRS             1      1
SEQRES   1 R  105  GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN ARG HIS
SEQRES   2 R  105  GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS ASN ALA
SEQRES   3 R  105  TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN LEU MET
SEQRES   4 R  105  LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR ARG VAL
SEQRES   5 R  105  ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET SER GLN
SEQRES   6 R  105  ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE ALA THR
SEQRES   7 R  105  ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA PRO VAL
SEQRES   8 R  105  GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU LYS SER
SEQRES   9 R  105  ASP
SEQRES   1 S  105  GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN ARG HIS
SEQRES   2 S  105  GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS ASN ALA
SEQRES   3 S  105  TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN LEU MET
SEQRES   4 S  105  LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR ARG VAL
SEQRES   5 S  105  ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET SER GLN
SEQRES   6 S  105  ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE ALA THR
SEQRES   7 S  105  ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA PRO VAL
SEQRES   8 S  105  GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU LYS SER
SEQRES   9 S  105  ASP
SEQRES   1 V    1  TRP
SEQRES   1 W    1  TRP
HELIX    1   1 GLN R   17  TYR R   30  1                                  14
HELIX    2   2 HIS R   35  LEU R   39  1                                   5
HELIX    3   3 PRO R   45  LEU R   61  1                                  17
HELIX    4   4 THR R   81  ALA R   91  5                                  11
HELIX    5   5 ARG R   97  LEU R  105  1                                   9
HELIX    6   6 GLU S   18  ASN S   32  1                                  15
HELIX    7   7 HIS S   35  MET S   42  1                                   8
HELIX    8   8 ASP S   46  ARG S   63  1                                  18
HELIX    9   9 THR S   81  ASN S   87  1                                   7
HELIX   10  10 GLU S   95  LEU S  104  5                                  10
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
MODEL        1


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