+Open data
-Basic information
Entry | Database: PDB / ID: 1djm | ||||||
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Title | SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI | ||||||
Components | CHEMOTAXIS PROTEIN Y | ||||||
Keywords | SIGNALING PROTEIN / BEFX / CHEY / RESPONSE REGULATOR / CHEMOTAXIS / TWO-COMPONENT | ||||||
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 | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Cho, H.S. / Lee, S.Y. / Yan, D. / Pan, X. / Parkinson, J.S. / Kustu, S. / Wemmer, D.E. / Pelton, J.G. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: NMR structure of activated CheY. Authors: Cho, H.S. / Lee, S.Y. / Yan, D. / Pan, X. / Parkinson, J.S. / Kustu, S. / Wemmer, D.E. / Pelton, J.G. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 Title: Beryllofluoride Mimics Phosphorylation of NtrC and Other Bacterial Response Regulators Authors: Yan, D. / Cho, H.S. / Hastings, C.A. / Igo, M.M. / Lee, S.Y. / Pelton, J.G. / Stewart, V. / Wemmer, D.E. / Kustu, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1djm.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1djm.ent.gz | 901 KB | Display | PDB format |
PDBx/mmJSON format | 1djm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dj/1djm ftp://data.pdbj.org/pub/pdb/validation_reports/dj/1djm | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14112.332 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET21 / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 972 NON-TRIVIAL NOE RESTRAINTS (213 INTRA RESIDUE, 271 SEQUENTIAL, 238 MEDIUM-RANGE, AND 250 LONG-RANGE). 78 PHI TORSION ANGLE RESTRAINTS AND 17 CHI1 ...Details: THE STRUCTURES ARE BASED ON A TOTAL OF 972 NON-TRIVIAL NOE RESTRAINTS (213 INTRA RESIDUE, 271 SEQUENTIAL, 238 MEDIUM-RANGE, AND 250 LONG-RANGE). 78 PHI TORSION ANGLE RESTRAINTS AND 17 CHI1 RESTRAINTS WERE USED. 47 HYDROGEN BONDS ( 94 UPPER AND LOWER DISTANCE RESTRAINTS) WERE USED IN LATER STAGES OF REFINEMENT. | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 60 / Conformers submitted total number: 27 |