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Open data
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Basic information
Entry | Database: PDB / ID: 1yab | ||||||
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Title | Structure of T. maritima FliN flagellar rotor protein | ||||||
![]() | chemotaxis protein | ||||||
![]() | STRUCTURAL PROTEIN / Thermotoga maritima / flagellar motor / rotor / FliN / FliY | ||||||
Function / homology | ![]() bacterial-type flagellum basal body / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hill, C.P. / Blair, D.F. / Brown, P.N. / Mathews, M.A.A. / Joss, L.A. | ||||||
![]() | ![]() Title: Crystal Structure of the Flagellar Rotor Protein FliN from Thermotoga maritima Authors: Brown, P.N. / Mathews, M.A.A. / Joss, L.A. / Hill, C.P. / Blair, D.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 44.8 KB | Display | ![]() |
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PDB format | ![]() | 32.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.9 KB | Display | ![]() |
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Full document | ![]() | 437.6 KB | Display | |
Data in XML | ![]() | 9.1 KB | Display | |
Data in CIF | ![]() | 11.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1o6aS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 4 / Auth seq-ID: 68 - 152 / Label seq-ID: 1 - 85
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Details | Two molecules of FliN constructu containing residues 68 to 154 form the asymmetric unit. The two monomers interact over a large surface, with intertwined elements, each forming a saddle shape that interlocks with the other. |
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Components
#1: Protein | Mass: 9800.546 Da / Num. of mol.: 2 / Fragment: residues 68-154 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.7 Å3/Da / Density % sol: 70 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.9 Details: 18% MPD, 100mM MES buffer, pH 5.9, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 1, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979277 Å / Relative weight: 1 |
Reflection | Resolution: 3.4→87.7 Å / Num. all: 7246 / Num. obs: 7246 / % possible obs: 95.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 11 % / Rsym value: 0.07 / Net I/σ(I): 7.3 |
Reflection shell | Resolution: 3.4→3.52 Å / Redundancy: 11 % / Mean I/σ(I) obs: 1.8 / Num. unique all: 996 / Rsym value: 0.289 / % possible all: 93.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1O6A.pdb Resolution: 3.4→19.9 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.904 / SU B: 24.248 / SU ML: 0.373 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.738 / ESU R Free: 0.439 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 112.247 Å2
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Refinement step | Cycle: LAST / Resolution: 3.4→19.9 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Number: 668 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 3.397→3.581 Å / Total num. of bins used: 10
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