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Yorodumi- PDB-2b1j: Crystal Structure of Unphosphorylated CheY Bound to the N-Terminu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2b1j | ||||||
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Title | Crystal Structure of Unphosphorylated CheY Bound to the N-Terminus of FliM | ||||||
Components |
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Keywords | SIGNALING PROTEIN / CHEY / FLIM / (BETA/ALPHA)5 / PHOSPHORYLATION | ||||||
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-dependent swarming motility / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation ...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-dependent swarming motility / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / positive chemotaxis / acetyltransferase activity / cytoskeletal motor activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Dyer, C.M. / Dahlquist, F.W. | ||||||
Citation | Journal: J.Bacteriol. / Year: 2006 Title: Switched or Not?: the Structure of Unphosphorylated CheY Bound to the N Terminus of FliM. Authors: Dyer, C.M. / Dahlquist, F.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2b1j.cif.gz | 72.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2b1j.ent.gz | 54.1 KB | Display | PDB format |
PDBx/mmJSON format | 2b1j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b1/2b1j ftp://data.pdbj.org/pub/pdb/validation_reports/b1/2b1j | HTTPS FTP |
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-Related structure data
Related structure data | 3chyS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 13981.136 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: cheY / Plasmid: pCW / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL-21 / Keywords: CHEY_ECOLI / References: UniProt: P0AE67 #2: Protein/peptide | Mass: 1689.884 Da / Num. of mol.: 2 / Fragment: N-Terminus / Source method: obtained synthetically / Details: Prepared using solid-state synthesis / References: UniProt: P06974 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.62 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 6000, magnesium chloride, MES buffer, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.542 Å |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jan 24, 2005 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.542 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→40.7 Å / Num. all: 10451 / Num. obs: 10174 / % possible obs: 97.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3 % / Biso Wilson estimate: 34.8 Å2 / Net I/σ(I): 18.8 |
Reflection shell | Resolution: 2.4→2.49 Å / % possible all: 96 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB Entry 3CHY Resolution: 2.4→40.7 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 630184.812 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: Sigma cuttoffs used in refinement were set sufficiently wide that no reflections were excluded.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 75.435 Å2 / ksol: 0.355 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 47 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→40.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.49 Å / Rfactor Rfree error: 0.035 / Total num. of bins used: 10
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Xplor file |
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