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Yorodumi- PDB-2jvj: NMR Solution Structure of the Hyper-Sporulation Response Regulato... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2jvj | ||||||
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Title | NMR Solution Structure of the Hyper-Sporulation Response Regulator Spo0F Mutant I90A from Bacillus subtilis | ||||||
Components | Sporulation initiation phosphotransferase F | ||||||
Keywords | TRANSFERASE / RESPONSE REGULATOR / TWO-COMPONENT SYSTEMS / BACTERIAL SIGNAL TRANSDUCTION / PHOSPHO-RELAY / (BETA/ALPHA)5 PROTEIN / Cytoplasm / Kinase / Magnesium / Metal-binding / Phosphorylation / Sporulation / Two-component regulatory system | ||||||
Function / homology | Function and homology information Transferases; Transferring phosphorus-containing groups / sporulation resulting in formation of a cellular spore / phosphorelay signal transduction system / kinase activity / phosphorylation / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Bobay, B.G. / McLaughlin, P.D. / Thompson, R.J. / Hoch, J.A. / Cavanagh, J. | ||||||
Citation | Journal: To be Published Title: Covariance identifies dynamic residues at the interfaces in protein/protein complexes Authors: Bobay, B.G. / White, R.A. / Szurmant, H. / Sullivan, D.M. / McLaughlin, P.D. / Hwa, T. / Hoch, J.A. / Cavanagh, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jvj.cif.gz | 469.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jvj.ent.gz | 409.6 KB | Display | PDB format |
PDBx/mmJSON format | 2jvj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jv/2jvj ftp://data.pdbj.org/pub/pdb/validation_reports/jv/2jvj | HTTPS FTP |
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-Related structure data
Related structure data | 2jviC 2jvkC C: citing same article (ref.) |
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Similar structure data | |
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: 15273.733 Da / Num. of mol.: 1 / Mutation: I90A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: spo0F / Plasmid: pET-20b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE)3 References: UniProt: P06628, Transferases; Transferring phosphorus-containing groups |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 25 / pH: 6.9 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR constraints | NOE constraints total: 3238 / NOE intraresidue total count: 740 / NOE medium range total count: 1908 / NOE sequential total count: 2498 | ||||||||||||||||||||
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 / Maximum lower distance constraint violation: 1.8 Å / Maximum upper distance constraint violation: 6 Å | ||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.036 Å / Distance rms dev error: 0.002 Å |