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Open data
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Basic information
Entry | Database: PDB / ID: 1klf | ||||||
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Title | FIMH ADHESIN-FIMC CHAPERONE COMPLEX WITH D-MANNOSE | ||||||
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![]() | CHAPERONE/ADHESIN COMPLEX / ADHESIN-CHAPERONE COMPLEX / MANNOSE-BOUND / CHAPERONE-ADHESIN COMPLEX 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 | ![]() ![]() ![]() | ||||||
![]() | Hung, C.S. / Bouckaert, J. | ||||||
![]() | ![]() Title: Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection. Authors: Hung, C.S. / Bouckaert, J. / Hung, D. / Pinkner, J. / Widberg, C. / DeFusco, A. / Auguste, C.G. / Strouse, R. / Langermann, S. / Waksman, G. / Hultgren, S.J. | ||||||
History |
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Remark 300 | BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH ...BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 16CHAIN(S). SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). THE BIOMOLECULES ARE 1, 2, 3, 4, 5, 6, 7 AND 8 RESPECTIVELY, EACH CONSISTING OF A COMPLEX OF CHAPERONE FIMC WITH ADHESIN FIMH. THERE IS NO BIOLOGICALLY SIGNIFICANT HIGHER OLIGOMERIZATION STATE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 723.3 KB | Display | ![]() |
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PDB format | ![]() | 598.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 617.7 KB | Display | ![]() |
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Full document | ![]() | 920.9 KB | Display | |
Data in XML | ![]() | 165.7 KB | Display | |
Data in CIF | ![]() | 223.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kiuC ![]() 1qunS 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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8 | ![]()
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Unit cell |
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Details | 1 chaperone - 1 adhesin - 1 mannose is one biological assembly |
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Components
#1: Protein | Mass: 22724.049 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: Sugar | ChemComp-MAN / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.2 Details: ammonium suplhate, pH 8.20, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: CUSTOM-MADE / Detector: CCD / Date: Mar 18, 2001 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.79→43.68 Å / Num. all: 100438 / Num. obs: 99135 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 66.3 Å2 / Rmerge(I) obs: 0.069 / Rsym value: 0.069 / Net I/σ(I): 13 |
Reflection shell | Resolution: 2.79→2.9 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.478 / Mean I/σ(I) obs: 2.7 / Rsym value: 0.478 / % possible all: 99.9 |
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 50 Å / Num. measured all: 370427 |
Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.9 Å / % possible obs: 99.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1QUN Resolution: 2.79→43.68 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 1364705.86 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: FLAT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 96.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.79→43.68 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINED / Weight Biso : 8 / Weight position: 250 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.79→2.96 Å / Rfactor Rfree error: 0.01 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 50 Å / Rfactor Rfree: 0.279 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.42 / Rfactor Rwork: 0.35 / Rfactor obs: 0.35 |