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Open data
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Basic information
Entry | Database: PDB / ID: 1djm | ||||||
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Title | SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI | ||||||
![]() | CHEMOTAXIS PROTEIN Y![]() | ||||||
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Function / homology | ![]() 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 / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Cho, H.S. / Lee, S.Y. / Yan, D. / Pan, X. / Parkinson, J.S. / Kustu, S. / Wemmer, D.E. / Pelton, J.G. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 901 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 356 KB | Display | ![]() |
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Full document | ![]() | 523.5 KB | Display | |
Data in XML | ![]() | 47.3 KB | Display | |
Data in CIF | ![]() | 84 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. |
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Sample preparation
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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![]() |
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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 |