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- PDB-4b4p: Crystal Structure of the lectin domain of F18 fimbrial adhesin FedF. -
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Open data
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Basic information
Entry | Database: PDB / ID: 4b4p | ||||||
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Title | Crystal Structure of the lectin domain of F18 fimbrial adhesin FedF. | ||||||
![]() | F18 FIMBRIAL ADHESIN AC | ||||||
![]() | CELL ADHESION / FIMBRIAE / BACTERIAL ADHESINS / PROTEIN-CARBOHYDRATE INTERACTIONS / ABH BLOOD GROUP BINDING / STEC / ETEC / SPR / MST / BSI | ||||||
Function / homology | Jelly Rolls - #1210 / Jelly Rolls / Sandwich / Mainly Beta / BROMIDE ION / F18 fimbrial adhesin AC![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Moonens, K. / Bouckaert, J. / Coddens, A. / Tran, T. / Panjikar, S. / De Kerpel, M. / Cox, E. / Remaut, H. / De Greve, H. | ||||||
![]() | ![]() Title: Structural Insight in Histo-Blood Group Binding by the F18 Fimbrial Adhesin Fedf. Authors: Moonens, K. / Bouckaert, J. / Coddens, A. / Tran, T. / Panjikar, S. / De Kerpel, M. / Cox, E. / Remaut, H. / De Greve, H. #1: Journal: Microb.Pathog. / Year: 1996 Title: Characterization of F18 Fimbrial Genes Fede and Fedf Involved in Adhesion and Length of Enterotoxemic Escherichia Coli Strain 107/86. Authors: Imberechts, H. / Wild, P. / Charlier, G. / De Greve, H. / Lintermans, P. / Pohl, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 68.7 KB | Display | ![]() |
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PDB format | ![]() | 55.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.5 KB | Display | ![]() |
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Full document | ![]() | 451.1 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 20.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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Components
#1: Protein | Mass: 16311.161 Da / Num. of mol.: 2 / Fragment: LECTIN DOMAIN, RESIDUES 35-185 Source method: isolated from a genetically manipulated source Details: FRAGMENT ENCOMPASSES RESIDUES 15-165 OF MATURE FEDF PROTEIN Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-BR / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45 % / Description: NONE |
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Crystal grow | Method: vapor diffusion, sitting drop Details: 0.17 M AMMONIUM SULFATE, 25.5% (W/V) PEG 4000 AND 15% (V/V) GLYCEROL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.77 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→19.81 Å / Num. obs: 24427 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Rrim(I) all: 0.07 / Net I/σ(I): 28.83 |
Reflection shell | Highest resolution: 1.8 Å / Mean I/σ(I) obs: 12.94 / Rrim(I) all: 0.185 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.8→19.81 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.928 / SU B: 2.601 / SU ML: 0.082 / Cross valid method: THROUGHOUT / ESU R: 0.129 / ESU R Free: 0.126 / 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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.696 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→19.81 Å
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Refine LS restraints |
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