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- PDB-1ybj: Structural and Dynamics studies of both apo and holo forms of the... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ybj | ||||||
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Title | Structural and Dynamics studies of both apo and holo forms of the hemophore HasA | ||||||
![]() | Hemophore HasA | ||||||
![]() | METAL BINDING PROTEIN / alpha+beta structure / curved anti-parallel beta-sheet | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wolff, N. / Izadi-Pruneyre, N. / Couprie, J. / Habeck, M. / Linge, J. / Rieping, W. / Wandersman, C. / Nilges, M. / Delepierre, M. / Lecroisey, A. | ||||||
![]() | ![]() Title: Comparative analysis of structural and dynamic properties of the loaded and unloaded hemophore HasA: functional implications. Authors: Wolff, N. / Izadi-Pruneyre, N. / Couprie, J. / Habeck, M. / Linge, J. / Rieping, W. / Wandersman, C. / Nilges, M. / Delepierre, M. / Lecroisey, 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 | ![]() | 486.4 KB | Display | ![]() |
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PDB format | ![]() | 403.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 18289.494 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||
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NMR experiment |
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NMR details | Text: H-bond constraints according to the amide proton-deuterium exchange measurements (15N HSQC experiments) |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 20mM sodium phosphate buffer / pH: 5.6 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: ![]() Details: Structures are based on a total of 3537 distance restraints (where 3145 were unambiguous and 392 ambiguous),111 phi torsion angles and 34 hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 10 |