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Open data
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Basic information
Entry | Database: PDB / ID: 6ai0 | |||||||||||||||||||||
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Title | Structure of the 328-692 fragment of FlhA (orthorhombic form) | |||||||||||||||||||||
![]() | Flagellar biosynthesis protein FlhA | |||||||||||||||||||||
![]() | PROTEIN TRANSPORT / flagellar type III secretion | |||||||||||||||||||||
Function / homology | ![]() | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||||||||
![]() | Ogawa, Y. / Kinoshita, M. / Minamino, T. / Imada, K. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Insights into the Substrate Specificity Switch Mechanism of the Type III Protein Export Apparatus. Authors: Inoue, Y. / Ogawa, Y. / Kinoshita, M. / Terahara, N. / Shimada, M. / Kodera, N. / Ando, T. / Namba, K. / Kitao, A. / Imada, K. / Minamino, T. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 147 KB | Display | ![]() |
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PDB format | ![]() | 112.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.4 KB | Display | ![]() |
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Full document | ![]() | 458.3 KB | Display | |
Data in XML | ![]() | 26.6 KB | Display | |
Data in CIF | ![]() | 36.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ai1C ![]() 6ai2C ![]() 6ai3C ![]() 3a5iS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 40671.645 Da / Num. of mol.: 2 / Fragment: cytoplasmic fragment, residues 328-692 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: LT2 / SGSC1412 / ATCC 700720 / Gene: flhA, STM1913 / Plasmid: pGEX6p1 Production host: ![]() Strain (production host): SJW1368 / References: UniProt: P40729 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.83 Å3/Da / Density % sol: 56.57 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.1M HEPES NaOH pH 7.5, 10% (w/v) PEG-8000, 0.4M Ca(OAc)2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Jul 5, 2012 |
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: 2.4→66 Å / Num. obs: 36660 / % possible obs: 99 % / Redundancy: 7.2 % / Biso Wilson estimate: 37 Å2 / Rmerge(I) obs: 0.119 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2.4→2.49 Å / Redundancy: 7 % / Rmerge(I) obs: 0.421 / Mean I/σ(I) obs: 3.4 / Num. unique obs: 3767 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3A5I Resolution: 2.4→41.281 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 30.47
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 87.71 Å2 / Biso mean: 48.7591 Å2 / Biso min: 18.92 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.4→41.281 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: 13
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