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- PDB-1qun: X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM U... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qun | ||||||
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Title | X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI | ||||||
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![]() | CHAPERONE/STRUCTURAL PROTEIN / CHAPERONE ADHESIN DONOR STRAND COMPLEMENTATION / CHAPERONE-STRUCTURAL PROTEIN COMPLEX | ||||||
Function / homology | ![]() pilus tip / mechanosensory behavior / cell adhesion involved in single-species biofilm formation / pilus / cell-substrate adhesion / D-mannose binding / host cell membrane / chaperone-mediated protein folding / protein folding chaperone / cell wall organization ...pilus tip / mechanosensory behavior / cell adhesion involved in single-species biofilm formation / pilus / cell-substrate adhesion / D-mannose binding / host cell membrane / chaperone-mediated protein folding / protein folding chaperone / cell wall organization / outer membrane-bounded periplasmic space / cell adhesion Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Choudhury, D. / Thompson, A. / Stojanoff, V. / Langerman, S. / Pinkner, J. / Hultgren, S.J. / Knight, S. | ||||||
![]() | ![]() Title: X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Authors: Choudhury, D. / Thompson, A. / Stojanoff, V. / Langermann, S. / Pinkner, J. / Hultgren, S.J. / Knight, S.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 708.5 KB | Display | ![]() |
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PDB format | ![]() | 593.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 487.9 KB | Display | ![]() |
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Full document | ![]() | 781.3 KB | Display | |
Data in XML | ![]() | 108.4 KB | Display | |
Data in CIF | ![]() | 152.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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8 | ![]()
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11 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 22694.023 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 29081.314 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.42 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8.4 Details: Ammonium Sulphate, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.2 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. all: 182983 / Num. obs: 142580 / Observed criterion σ(F): 2 |
Reflection | *PLUS % possible obs: 98 % / Rmerge(I) obs: 0.076 |
Reflection shell | *PLUS Rmerge(I) obs: 0.253 |
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Processing
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Refinement | Resolution: 2.8→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.24 / Rfactor Rwork: 0.24 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |