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- PDB-1cey: ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CH... -

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Basic information

Entry
Database: PDB / ID: 1cey
TitleASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY
ComponentsCHEY
KeywordsSIGNAL TRANSDUCTION
Function / homology
Function and homology information


bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity ...bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / protein acetylation / acetyltransferase activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm
Similarity search - Function
Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Response regulator / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chemotaxis protein CheY / Chemotaxis protein CheY
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsMoy, F.J. / Lowry, D.F. / Matsumura, P. / Dahlquist, F.W. / Krywko, J.E. / Domaille, P.J.
CitationJournal: Biochemistry / Year: 1994
Title: Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
Authors: Moy, F.J. / Lowry, D.F. / Matsumura, P. / Dahlquist, F.W. / Krywko, J.E. / Domaille, P.J.
History
DepositionNov 23, 1994Processing site: BNL
Revision 1.0Feb 7, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CHEY


Theoretical massNumber of molelcules
Total (without water)13,9811
Polymers13,9811
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: CIS PROLINE - PRO 110 MODEL 1 / 2: CIS PROLINE - PRO 110 MODEL 2 / 3: CIS PROLINE - PRO 110 MODEL 3 / 4: CIS PROLINE - PRO 110 MODEL 4 / 5: CIS PROLINE - PRO 110 MODEL 5 / 6: CIS PROLINE - PRO 110 MODEL 6 / 7: CIS PROLINE - PRO 110 MODEL 7 / 8: CIS PROLINE - PRO 110 MODEL 8 / 9: CIS PROLINE - PRO 110 MODEL 9 / 10: CIS PROLINE - PRO 110 MODEL 10 / 11: CIS PROLINE - PRO 110 MODEL 11 / 12: CIS PROLINE - PRO 110 MODEL 12 / 13: CIS PROLINE - PRO 110 MODEL 13 / 14: CIS PROLINE - PRO 110 MODEL 14 / 15: CIS PROLINE - PRO 110 MODEL 15 / 16: CIS PROLINE - PRO 110 MODEL 16 / 17: CIS PROLINE - PRO 110 MODEL 17 / 18: CIS PROLINE - PRO 110 MODEL 18 / 19: CIS PROLINE - PRO 110 MODEL 19 / 20: CIS PROLINE - PRO 110 MODEL 20 / 21: CIS PROLINE - PRO 110 MODEL 21 / 22: CIS PROLINE - PRO 110 MODEL 22 / 23: CIS PROLINE - PRO 110 MODEL 23 / 24: CIS PROLINE - PRO 110 MODEL 24 / 25: CIS PROLINE - PRO 110 MODEL 25 / 26: CIS PROLINE - PRO 110 MODEL 26 / 27: CIS PROLINE - PRO 110 MODEL 27 / 28: CIS PROLINE - PRO 110 MODEL 28 / 29: CIS PROLINE - PRO 110 MODEL 29 / 30: CIS PROLINE - PRO 110 MODEL 30 / 31: CIS PROLINE - PRO 110 MODEL 31 / 32: CIS PROLINE - PRO 110 MODEL 32 / 33: CIS PROLINE - PRO 110 MODEL 33 / 34: CIS PROLINE - PRO 110 MODEL 34 / 35: CIS PROLINE - PRO 110 MODEL 35 / 36: CIS PROLINE - PRO 110 MODEL 36 / 37: CIS PROLINE - PRO 110 MODEL 37 / 38: CIS PROLINE - PRO 110 MODEL 38 / 39: CIS PROLINE - PRO 110 MODEL 39 / 40: CIS PROLINE - PRO 110 MODEL 40 / 41: CIS PROLINE - PRO 110 MODEL 41 / 42: CIS PROLINE - PRO 110 MODEL 42 / 43: CIS PROLINE - PRO 110 MODEL 43 / 44: CIS PROLINE - PRO 110 MODEL 44 / 45: CIS PROLINE - PRO 110 MODEL 45 / 46: CIS PROLINE - PRO 110 MODEL 46
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)46 / -
Representative

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Components

#1: Protein CHEY


Mass: 13981.136 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: CHEY / References: UniProt: P06143, UniProt: P0AE67*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 46

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