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Yorodumi- PDB-1xsf: Solution structure of a resuscitation promoting factor domain fro... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xsf | ||||||
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Title | Solution structure of a resuscitation promoting factor domain from Mycobacterium tuberculosis | ||||||
Components | Probable resuscitation-promoting factor rpfB | ||||||
Keywords | CELL CYCLE / HYDROLASE / LYSOZYME-LIKE STRUCTURE | ||||||
Function / homology | Function and homology information dormancy exit of symbiont in host / positive regulation of growth rate / Hydrolases / quorum sensing / regulation of cell population proliferation / hydrolase activity / negative regulation of gene expression / positive regulation of gene expression / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | SOLUTION NMR / molecular dynamics in explicit solvent | ||||||
Authors | Cohen-Gonsaud, M. / Barthe, P. / Henderson, B. / Ward, J. / Roumestand, C. / Keep, N.H. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2005 Title: The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes Authors: Cohen-Gonsaud, M. / Barthe, P. / Bagneris, C. / Henderson, B. / Ward, J. / Roumestand, C. / Keep, N.H. #1: Journal: J.Biomol.Nmr / Year: 2004 Title: Letter to the Editor: (1)H, (15)N, and (13)C chemical shift assignments of the resuscitation promoting factor domain of Rv1009 from Mycobacterium tuberculosis Authors: Cohen-Gonsaud, M. / Barthe, P. / Pommier, F. / Harris, R. / Driscoll, P.C. / Keep, N.H. / Roumestand, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xsf.cif.gz | 900.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xsf.ent.gz | 787.6 KB | Display | PDB format |
PDBx/mmJSON format | 1xsf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xs/1xsf ftp://data.pdbj.org/pub/pdb/validation_reports/xs/1xsf | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11357.573 Da / Num. of mol.: 1 / Fragment: RPFBc DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: Rv1009 / Plasmid: pET15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O05594, UniProt: P9WG29*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 25mM Na-Acetate / pH: 4.6 / Pressure: ambient / Temperature: 293 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: molecular dynamics in explicit solvent / Software ordinal: 1 Details: the structures are based on a total of 1757 restraints, 1613 are NOE-derived distance constraints, 124 dihedral angle restraints, 20 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 30 / Conformers submitted total number: 30 |