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- PDB-1o9w: F17-aG lectin domain from Escherichia coli in complex with N-acet... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1o9w | ||||||
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Title | F17-aG lectin domain from Escherichia coli in complex with N-acetyl-glucosamine | ||||||
![]() | F17A-G FIMBRIAL ADHESIN | ||||||
![]() | SUGAR BINDING PROTEIN / ![]() | ||||||
Function / homology | ![]() adhesion of symbiont to host / cell adhesion involved in single-species biofilm formation / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Buts, L. / De Genst, E. / Loris, R. / Oscarson, S. / Lahmann, M. / Messens, J. / Brosens, E. / Wyns, L. / Bouckaert, J. / De Greve, H. | ||||||
![]() | ![]() Title: The Fimbrial Adhesin F17-G of Enterotoxigenic Escherichia Coli Has an Immunoglobulin-Like Lectin Domain that Binds N-Acetylglucosamine Authors: Buts, L. / Bouckaert, J. / De Genst, E. / Loris, R. / Oscarson, S. / Lahmann, M. / Messens, J. / Brosens, E. / Wyns, L. / De Greve, H. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2003 Title: Solving the Phase Problem for Carbohydrate -Binding Proteins Using Selenium Derivatives of Their Ligands: A Case Study Involving the Bacterial F17-G Adhesin Authors: Buts, L. / Loris, R. / De Genst, E. / Oscarson, S. / Lahmann, M. / Messens, J. / Brosens, E. / Wyns, L. / De Greve, H. / Bouckaert, J. #2: Journal: J.Bacteriol. / Year: 1991 Title: Identification, Characterization and Nucleotide Sequence of the F17G Gene, which Determines Receptor Binding of Escherichia Coli F17 Fimbriae Authors: Lintermans, P.F. / Bertels, A. / Schlicker, C. / Deboeck, F. / Charlier, G. / Pohl, P. / Norgren, M. / Normark, S. / Van Montagu, M. / De Greve, H. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.9 KB | Display | ![]() |
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PDB format | ![]() | 33.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1o9vSC ![]() 1o9zC 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: 19048.227 Da / Num. of mol.: 1 / Fragment: CARBOHYDRATE-BINDING DOMAIN, RESIDUES 23-199 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Sugar | ChemComp-NAG / ![]() |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.89 Å3/Da / Density % sol: 33 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 4.6 Details: 30% PEG4000, 0.1M SODIUM ACETATE (PH 4.6), 0.2M AMMONIUM ACETATE | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
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: MARRESEARCH / Detector: CCD / Date: Aug 15, 2002 / Details: MIRRORS |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.65→25 Å / Num. obs: 20396 / % possible obs: 100 % / Redundancy: 48 % / Biso Wilson estimate: 27.8 Å2 / Rsym value: 0.073 / Net I/σ(I): 8.2 |
Reflection shell | Resolution: 1.66→1.81 Å / Rsym value: 0.52 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1O9V Resolution: 1.65→24.77 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1557043.04 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 61.5472 Å2 / ksol: 0.395503 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.65→24.77 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.75 Å / Rfactor Rfree error: 0.024 / Total num. of bins used: 6
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Xplor file |
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Refine LS restraints | *PLUS
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