+Open data
-Basic information
Entry | Database: PDB / ID: 1ab6 | ||||||
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Title | STRUCTURE OF CHEY MUTANT F14N, V86T | ||||||
Components | CHEMOTAXIS PROTEIN CHEY | ||||||
Keywords | CHEMOTAXIS / SENSORY TRANSDUCTION / PHOSPHORYLATION / FLAGELLAR ROT | ||||||
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 / MOLECULAR / Resolution: 2.2 Å | ||||||
Authors | Wilcock, D. / Pisabarro, M.T. / Lopez-Hernandez, E. / Serranno, L. / Coll, M. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1998 Title: Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability. Authors: Wilcock, D. / Pisabarro, M.T. / Lopez-Hernandez, E. / Serrano, L. / Coll, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ab6.cif.gz | 59.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ab6.ent.gz | 44 KB | Display | PDB format |
PDBx/mmJSON format | 1ab6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ab6_validation.pdf.gz | 414 KB | Display | wwPDB validaton report |
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Full document | 1ab6_full_validation.pdf.gz | 415.6 KB | Display | |
Data in XML | 1ab6_validation.xml.gz | 11.2 KB | Display | |
Data in CIF | 1ab6_validation.cif.gz | 14.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/1ab6 ftp://data.pdbj.org/pub/pdb/validation_reports/ab/1ab6 | HTTPS FTP |
-Related structure data
Related structure data | 1ab5C 3chyS S: Starting model for refinement C: citing same article (ref.) |
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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: 13634.692 Da / Num. of mol.: 2 / Mutation: F14N, V86T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PTZ18U (PHARMACIA) / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P06143, UniProt: P0AE67*PLUS #2: Water | ChemComp-HOH / | Compound details | THE CIS PROLINE AT 110 NECESSARY FOR ACTIVITY OF THE PROTEIN. | |
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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: 3.15 Å3/Da / Density % sol: 61 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / pH: 7.2 Details: THE PROTEIN WAS CRYSTALLIZED WITH 3.0M AMMONIUM SULFATE, PH7.2 AT 20C., temperature 293K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 1, 1995 / Details: SLITS |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→15 Å / Num. obs: 13544 / % possible obs: 86 % / Observed criterion σ(I): 2 / Redundancy: 1.8 % / Biso Wilson estimate: 40.4 Å2 / Rmerge(I) obs: 0.048 |
Reflection shell | Resolution: 2.2→2.34 Å / Rmerge(I) obs: 0.29 / % possible all: 55.6 |
Reflection | *PLUS Num. measured all: 25441 |
Reflection shell | *PLUS % possible obs: 55.6 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR Starting model: 3CHY Resolution: 2.2→10 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: A POSTERIORI / σ(F): 2 / Details: RESOLUTION-DEPENDENT WEIGHTING
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Displacement parameters | Biso mean: 35.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.029 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.843 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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