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- PDB-2bs8: Crystal structure of F17b-G in complex with N-acetyl-D-glucosamine -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bs8 | ||||||
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Title | Crystal structure of F17b-G in complex with N-acetyl-D-glucosamine | ||||||
![]() | ADHESIN | ||||||
![]() | SUGAR BINDING PROTEIN / LECTIN / FIMBRIAE / PROTEIN-SUGAR COMPLEX / SUGAR-BINDING PROTEIN | ||||||
Function / homology | ![]() adhesion of symbiont to host / cell adhesion involved in single-species biofilm formation / pilus / carbohydrate binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Buts, L. / Wellens, A. / VanMolle, I. / Wyns, L. / Loris, R. / Lahmann, M. / Oscarson, S. / DeGreve, H. / Bouckaert, J. | ||||||
![]() | ![]() Title: Impact of Natural Variation in Bacterial F17G Adhesins on Crystallization Behaviour. Authors: Buts, L. / Wellens, A. / Van Molle, I. / Wyns, L. / Loris, R. / Lahmann, M. / Oscarson, S. / De Greve, H. / Bouckaert, J. | ||||||
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 | ![]() | 53.8 KB | Display | ![]() |
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PDB format | ![]() | 36.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.4 KB | Display | ![]() |
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Full document | ![]() | 456.8 KB | Display | |
Data in XML | ![]() | 13 KB | Display | |
Data in CIF | ![]() | 18 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zk5C ![]() 1zplC ![]() 2bs7C ![]() 2bsbC ![]() 2bscC ![]() 1o9wS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 18896.871 Da / Num. of mol.: 1 / Fragment: LECTIN DOMAIN, RESIDUES 23-198 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Sugar | ChemComp-NAG / |
#3: Water | ChemComp-HOH / |
Sequence details | ELECTRON DENSITY AND NUCLEOTIDE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 60 % |
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Crystal grow | Method: vapor diffusion, hanging drop Details: HANGING DROP: 1 MICROLITER OF 10% ETHANOL WITH 1.5 M NACL PLUS 1 MICROLITER OF 16 MG/ML F17BG |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 20, 2002 / Details: BENT MIRROR |
Radiation | Monochromator: TRIANGULAR MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.81 Å / Relative weight: 1 |
Reflection | Resolution: 2.24→23 Å / Num. obs: 11000 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Biso Wilson estimate: 43.9 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2.24→2.32 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.21 / Mean I/σ(I) obs: 5 / % possible all: 91.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1O9W Resolution: 2.25→22.91 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 2439377.41 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Solvent model: CNS BULK SOLVENT MODEL USED / Bsol: 216.269 Å2 / ksol: 0.466888 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.35 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.25→22.91 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.25→2.32 Å / Total num. of bins used: 10 / % reflection obs: 91.1 % |