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Open data
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Basic information
Entry | Database: PDB / ID: 3jwn | ||||||
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Title | Complex of FimC, FimF, FimG and FimH | ||||||
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![]() | protein binding/cell adhesion / fimbria / cell adhesion / fimh / fimc / fimf / fimg / chaperone / fibrium / immunoglobulin domain / Fimbrium / Periplasm / Disulfide bond / protein binding-cell adhesion COMPLEX | ||||||
Function / homology | ![]() pilus tip / mechanosensory behavior / cell adhesion involved in single-species biofilm formation / pilus / cell-substrate adhesion / chaperone-mediated protein folding / protein folding chaperone / cell wall organization / outer membrane-bounded periplasmic space / cell adhesion / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Le Trong, I. / Aprikian, P. / Stenkamp, R.E. / Sokurenko, E.V. | ||||||
![]() | ![]() Title: Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting. Authors: Le Trong, I. / Aprikian, P. / Kidd, B.A. / Forero-Shelton, M. / Tchesnokova, V. / Rajagopal, P. / Rodriguez, V. / Interlandi, G. / Klevit, R. / Vogel, V. / Stenkamp, R.E. / Sokurenko, E.V. / Thomas, W.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 344.2 KB | Display | ![]() |
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PDB format | ![]() | 280.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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
-Protein , 4 types, 10 molecules CIEFKLGMHN
#1: Protein | Mass: 22754.031 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 16161.095 Da / Num. of mol.: 4 / Fragment: UNP residues 23-176 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Protein | Mass: 14864.227 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Protein | Mass: 29053.260 Da / Num. of mol.: 2 / Fragment: UNP residues 25-303 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 2 types, 30 molecules ![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 6.03 Å3/Da / Density % sol: 79.62 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4.1 Details: 1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 15, 2008 |
Radiation | Monochromator: double-crystal, SI(111), liquid N2 cooled / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.69→176.8 Å / Num. obs: 119926 / % possible obs: 90.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.5 % / Rmerge(I) obs: 0.147 / Rsym value: 0.147 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.69→2.79 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.862 / % possible all: 46.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entries 1KLF, 3BWU and 3BFQ Resolution: 2.69→48.34 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.899 / SU B: 11.362 / SU ML: 0.222 / Cross valid method: THROUGHOUT / ESU R: 0.337 / ESU R Free: 0.269 / 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: 51.028 Å2
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Refinement step | Cycle: LAST / Resolution: 2.69→48.34 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.69→2.758 Å / Total num. of bins used: 20
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