+Open data
-Basic information
Entry | Database: PDB / ID: 1fqw | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF ACTIVATED CHEY | ||||||
Components | CHEMOTAXIS CHEY PROTEIN | ||||||
Keywords | SIGNALING PROTEIN / response regulator / Activated CheY / Chemotaxis / two-component signal transduction / BeF3 / receiver domain | ||||||
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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.37 Å | ||||||
Authors | Lee, S.Y. / Cho, H.S. / Pelton, J.G. / Yan, D. / Berry, E.A. / Wemmer, D.E. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: Crystal structure of activated CheY. Comparison with other activated receiver domains. Authors: Lee, S.Y. / Cho, H.S. / Pelton, J.G. / Yan, D. / Berry, E.A. / Wemmer, D.E. #1: 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. #2: Journal: J.Mol.Biol. / Year: 1999 Title: Phosphorylated Aspartate in the Structure of a Response Regulator Protein Authors: Lewis, R.J. / Brannigan, J.A. / Muchova, K. / Barak, I. / Wilkinson, A.J. #3: Journal: Structure / Year: 1999 Title: Conformational changes induced by phosphorylation of the FixJ receiver domain Authors: Birck, C. / Mourey, L. / Gouet, P. / Fabry, B. / Schumacher, J. / Rousseau, P. / Kahn, D. / Samama, J.P. #4: Journal: Biochemistry / Year: 2000 Title: The 1.9A resolution Crystal structure of Phosphono-CheY, an Analogue of the Active Form of the Response Regulator, CheY Authors: Halkides, C.J. / McEvoy, M.M. / Casper, E. / Matsumura, P. / Volz, K. / Dahlquist, F.W. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1fqw.cif.gz | 65.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1fqw.ent.gz | 48.8 KB | Display | PDB format |
PDBx/mmJSON format | 1fqw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fqw_validation.pdf.gz | 423.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1fqw_full_validation.pdf.gz | 427.5 KB | Display | |
Data in XML | 1fqw_validation.xml.gz | 13.7 KB | Display | |
Data in CIF | 1fqw_validation.cif.gz | 19 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fq/1fqw ftp://data.pdbj.org/pub/pdb/validation_reports/fq/1fqw | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is a monomer from each chain. |
-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) / Plasmid details: PET21 / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.18 Å3/Da / Density % sol: 70.57 % | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Ammonium sulfate, Tris buffer, MnCl2, glycerol, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.4 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 17, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2.37→25 Å / Num. all: 89177 / Num. obs: 17703 / % possible obs: 89.1 % / Observed criterion σ(I): -3 / Redundancy: 5 % / Biso Wilson estimate: 39.4 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 13.2 |
Reflection shell | Resolution: 2.37→2.41 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.23 / Num. unique all: 500 / % possible all: 52.2 |
Reflection | *PLUS Num. measured all: 89177 |
Reflection shell | *PLUS % possible obs: 52.2 % / Rmerge(I) obs: 0.23 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.37→15 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 643531.15 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44.8 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.37→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS | NCS model details: CONSTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.37→2.52 Å / Rfactor Rfree error: 0.029 / Total num. of bins used: 6
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 0.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 4.8 % / Rfactor obs: 0.21 / Rfactor Rfree: 0.24 / Rfactor Rwork: 0.21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 44.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.317 / % reflection Rfree: 4.5 % / Rfactor Rwork: 0.282 |