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- PDB-1zwt: Structure of the globular head domain of the bundlin, BfpA, of th... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zwt | ||||||
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Title | Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli | ||||||
![]() | Major structural subunit of bundle-forming pilus | ||||||
![]() | CELL ADHESION / alpha-beta fold / beta-sandwich / one disulfide bond | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / Simulated annealing with NMR restraints using ARIA | ||||||
![]() | Ramboarina, S. / Fernandes, P.J. / Daniell, S. / Islam, S. / Frankel, G. / Booy, F. / Donnenberg, M.S. / Matthews, S. | ||||||
![]() | ![]() Title: Structure of the Bundle-forming Pilus from Enteropathogenic Escherichia coli Authors: Ramboarina, S. / Fernandes, P.J. / Daniell, S. / Islam, S. / Simpson, P. / Frankel, G. / Booy, F. / Donnenberg, M.S. / Matthews, S. #1: Journal: J.BIOMOL.NMR / Year: 2004 Title: Complete resonance assignments of bundlin (BfpA) from the bundle-forming pilus of enteropathogenic Escherichia coli Authors: Ramboarina, S. / Fernandes, P. / Simpson, P. / Frankel, G. / Donnenberg, M. / Matthews, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 587.4 KB | Display | ![]() |
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PDB format | ![]() | 513.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 345.2 KB | Display | ![]() |
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Full document | ![]() | 447.5 KB | Display | |
Data in XML | ![]() | 42.7 KB | Display | |
Data in CIF | ![]() | 57.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 16486.092 Da / Num. of mol.: 1 / Fragment: BfpA Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Hydrogen-exchange experiments |
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Sample preparation
Details | Contents: 0.5 mM BfpA U-15N,13C, 20 mM sodium phosphate buffer pH 5.2, 90%H20, 10% D2O Solvent system: 90%H20, 10% D2O |
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Sample conditions | Ionic strength: no salt / pH: 5.2 / Pressure: normal / Temperature: 303 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: Simulated annealing with NMR restraints using ARIA / Software ordinal: 1 Details: 577 Ambiguous and 2277 unambiguous NOE restraints, 86 TALOS constraints and 38 hydrogen bonds were imposed during ARIA structure calculations. | ||||||||||||||||
NMR representative | Selection criteria: least number of violations, lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry, structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 12 |