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- PDB-4wem: Co-complex structure of the F4 fimbrial adhesin FaeG variant ac w... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4wem | |||||||||
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Title | Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain antibody V1 | |||||||||
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![]() | STRUCTURAL PROTEIN / Complex / llama single domain antibody / adhesin / nanobody | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Moonens, K. / Van den Broeck, I. / Pardon, E. / De Kerpel, M. / Remaut, H. / De Greve, H. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies. Authors: Moonens, K. / Van den Broeck, I. / Okello, E. / Pardon, E. / De Kerpel, M. / Remaut, H. / De Greve, H. #1: Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2013 Title: Orally fed seeds producing designer IgAs protect weaned piglets against enterotoxigenic Escherichia coli infection. Authors: Virdi, V. / Coddens, A. / De Buck, S. / Millet, S. / Goddeeris, B.M. / Cox, E. / De Greve, H. / Depicker, A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 163.6 KB | Display | ![]() |
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PDB format | ![]() | 128 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4wenC ![]() 4weuC ![]() 3hlrS 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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Unit cell |
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Components
#1: Protein | Mass: 28703.873 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Antibody | Mass: 13978.585 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
#3: Chemical | ChemComp-PO4 / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.76 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.2 M Potassium bromide, 0.1 M Sodium acetate pH 5.5, 15 % w/v PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 10, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→47.62 Å / Num. obs: 68481 / % possible obs: 99.9 % / Redundancy: 11.2 % / Net I/σ(I): 24.8 |
Reflection shell | Resolution: 1.55→1.63 Å / Redundancy: 10.9 % / Mean I/σ(I) obs: 4.2 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3HLR Resolution: 1.55→47.62 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.966 / SU B: 2.666 / SU ML: 0.049 / Cross valid method: FREE R-VALUE / ESU R: 0.065 / ESU R Free: 0.067 / 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: 34.314 Å2
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Refinement step | Cycle: 1 / Resolution: 1.55→47.62 Å
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Refine LS restraints |
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