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Yorodumi- PDB-1qun: X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM U... -
+Open data
-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 | ||||||
Components |
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Keywords | CHAPERONE/STRUCTURAL PROTEIN / CHAPERONE ADHESIN DONOR STRAND COMPLEMENTATION / CHAPERONE-STRUCTURAL PROTEIN COMPLEX | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.8 Å | ||||||
Authors | Choudhury, D. / Thompson, A. / Stojanoff, V. / Langerman, S. / Pinkner, J. / Hultgren, S.J. / Knight, S. | ||||||
Citation | Journal: Science / Year: 1999 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qun.cif.gz | 708.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qun.ent.gz | 593.3 KB | Display | PDB format |
PDBx/mmJSON format | 1qun.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qun_validation.pdf.gz | 487.9 KB | Display | wwPDB validaton report |
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Full document | 1qun_full_validation.pdf.gz | 781.3 KB | Display | |
Data in XML | 1qun_validation.xml.gz | 108.4 KB | Display | |
Data in CIF | 1qun_validation.cif.gz | 152.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qu/1qun ftp://data.pdbj.org/pub/pdb/validation_reports/qu/1qun | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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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.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P31697 #2: Protein | Mass: 29081.314 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P08191 #3: 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: 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: SYNCHROTRON / Site: ESRF / Beamline: BM14 |
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 |
-Processing
Software |
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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 |