+Open data
-Basic information
Entry | Database: PDB / ID: 6ahq | ||||||||||||||||||
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Title | Structure of the 40-167 fragment of FliL | ||||||||||||||||||
Components | Flagellar protein FliL | ||||||||||||||||||
Keywords | MOTOR PROTEIN / Flagellar motor protein | ||||||||||||||||||
Function / homology | Flagellar basal body-associated protein FliL / Flagellar basal body-associated protein FliL / bacterial-type flagellum basal body / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane / Flagellar protein FliL Function and homology information | ||||||||||||||||||
Biological species | Vibrio alginolyticus (bacteria) | ||||||||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.398 Å | ||||||||||||||||||
Authors | Takekawa, N. / Isumi, M. / Sakuma, M. / Kojima, S. / Homma, M. / Imada, K. | ||||||||||||||||||
Funding support | Japan, 5items
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Citation | Journal: MBio / Year: 2019 Title: Structure ofVibrioFliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function. Authors: Takekawa, N. / Isumi, M. / Terashima, H. / Zhu, S. / Nishino, Y. / Sakuma, M. / Kojima, S. / Homma, M. / Imada, K. | ||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ahq.cif.gz | 407.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ahq.ent.gz | 336.9 KB | Display | PDB format |
PDBx/mmJSON format | 6ahq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6ahq_validation.pdf.gz | 553.9 KB | Display | wwPDB validaton report |
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Full document | 6ahq_full_validation.pdf.gz | 571.7 KB | Display | |
Data in XML | 6ahq_validation.xml.gz | 63.6 KB | Display | |
Data in CIF | 6ahq_validation.cif.gz | 90.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ah/6ahq ftp://data.pdbj.org/pub/pdb/validation_reports/ah/6ahq | HTTPS FTP |
-Related structure data
Related structure data | 6ahpSC 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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Unit cell |
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Details | Author determined biological unit: unknown. |
-Components
#1: Protein | Mass: 14025.714 Da / Num. of mol.: 20 / Fragment: periplasmic fragment, residues 60-167 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio alginolyticus (bacteria) / Plasmid: pColdI / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: A0A0P7ET86*PLUS |
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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: 3.54 Å3/Da / Density % sol: 65.25 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.1M sodium acetate pH 6.0, 25 % (w/v) PEG-200, 0.15M CaCl2, 1.4% (v/v) EtOH |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 23, 2015 |
Radiation | Monochromator: Double-crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.398→91.3 Å / Num. obs: 54933 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Biso Wilson estimate: 51.07 Å2 / Rmerge(I) obs: 0.137 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 3.398→3.5 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.325 / Mean I/σ(I) obs: 5 / Num. unique obs: 4467 / % possible all: 98.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6AHP Resolution: 3.398→85.551 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 23.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 154.82 Å2 / Biso mean: 54.6049 Å2 / Biso min: 11.42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.398→85.551 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 19
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