+Open data
-Basic information
Entry | Database: PDB / ID: 1qc7 | ||||||
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Title | T. MARITIMA FLIG C-TERMINAL DOMAIN | ||||||
Components | PROTEIN (FLIG) | ||||||
Keywords | STRUCTURAL PROTEIN / FLAGELLAR MOTOR SWITCH PROTEIN | ||||||
Function / homology | Function and homology information bacterial-type flagellum basal body / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / protein heterodimerization activity / protein homodimerization activity / plasma membrane Similarity search - Function | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.2 Å | ||||||
Authors | Lloyd, S.A. / Whitby, F.G. / Blair, D. / Hill, C.P. | ||||||
Citation | Journal: Nature / Year: 1999 Title: Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor Authors: Lloyd, S.A. / Whitby, F.G. / Blair, D.F. / Hill, C.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qc7.cif.gz | 48.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qc7.ent.gz | 35.9 KB | Display | PDB format |
PDBx/mmJSON format | 1qc7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qc/1qc7 ftp://data.pdbj.org/pub/pdb/validation_reports/qc/1qc7 | 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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Unit cell |
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-Components
#1: Protein | Mass: 11531.468 Da / Num. of mol.: 2 / Fragment: FLIG-C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Cellular location: MEMBRANE-ASSOCIATED / Gene: FLIG / Organelle: FLAGELLUM / Cell (production host): BL21 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9WY63 #2: 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: 3.04 Å3/Da / Density % sol: 59.5 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 286 K / pH: 5.2 / Details: ISOPROPANOL, pH 5.2, temperature 286K | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 45 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 13 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL1-5 / Wavelength: 1.0688 |
Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Apr 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0688 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→100 Å / Num. all: 14383 / Num. obs: 14359 / % possible obs: 99 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4 % / Biso Wilson estimate: 35.2 Å2 / Rmerge(I) obs: 0.101 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.2→2.3 Å / Redundancy: 4 % / Rmerge(I) obs: 0.413 / % possible all: 95.4 |
Reflection | *PLUS % possible obs: 97.1 % / Num. measured all: 56990 |
Reflection shell | *PLUS Lowest resolution: 2.24 Å / % possible obs: 92.4 % / Mean I/σ(I) obs: 1.7 |
-Processing
Software |
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Refinement | Resolution: 2.2→100 Å / σ(F): 0 / σ(I): 0
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Refinement step | Cycle: LAST / Resolution: 2.2→100 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 100 Å / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |