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Yorodumi- PDB-1cye: THREE DIMENSIONAL STRUCTURE OF CHEMOTACTIC CHE Y PROTEIN IN AQUEO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cye | ||||||
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Title | THREE DIMENSIONAL STRUCTURE OF CHEMOTACTIC CHE Y PROTEIN IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE METHODS | ||||||
Components | CHEY | ||||||
Keywords | SIGNAL 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 / internal peptidyl-lysine acetylation / thermotaxis / 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 / internal peptidyl-lysine acetylation / thermotaxis / phosphorelay response regulator activity / protein acetylation / acetyltransferase activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Santoro, J. / Bruix, M. / Pascual, J. / Lopez, E. / Serrano, L. / Rico, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Three-dimensional structure of chemotactic Che Y protein in aqueous solution by nuclear magnetic resonance methods. Authors: Santoro, J. / Bruix, M. / Pascual, J. / Lopez, E. / Serrano, L. / Rico, M. #1: Journal: Eur.J.Biochem. / Year: 1993 Title: 1H and 15N-NMR Assignment and Solution Structure of the Chemotactic Escherichia Coli Che Y Protein Authors: Bruix, M. / Pascual, J. / Santoro, J. / Prieto, J. / Serrano, L. / Rico, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cye.cif.gz | 471.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cye.ent.gz | 394.9 KB | Display | PDB format |
PDBx/mmJSON format | 1cye.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cye_validation.pdf.gz | 351.6 KB | Display | wwPDB validaton report |
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Full document | 1cye_full_validation.pdf.gz | 455.5 KB | Display | |
Data in XML | 1cye_validation.xml.gz | 36.7 KB | Display | |
Data in CIF | 1cye_validation.cif.gz | 65 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cy/1cye ftp://data.pdbj.org/pub/pdb/validation_reports/cy/1cye | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: 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 | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 14154.330 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
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
NMR software |
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NMR ensemble | Conformers submitted total number: 20 |