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Yorodumi- PDB-5tn2: Solution Structure of the C-terminal multimerization domain of th... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5tn2 | ||||||
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Title | Solution Structure of the C-terminal multimerization domain of the master biofilm-regulator SinR from Bacillus subtilis | ||||||
Components | HTH-type transcriptional regulator SinR | ||||||
Keywords | TRANSCRIPTION / biofilm formation / multimerization domain | ||||||
Function / homology | Function and homology information sporulation resulting in formation of a cellular spore / protein dimerization activity / DNA-binding transcription factor activity / negative regulation of gene expression / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / DNA binding Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Draughn, G.L. / Bobay, B.G. / Stowe, S.D. / Thompson, R.J. / Cavanagh, J. | ||||||
Funding support | United States, 1items
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Citation | Journal: J.Mol.Biol. / Year: 2019 Title: The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis. Authors: Milton, M.E. / Draughn, G.L. / Bobay, B.G. / Stowe, S.D. / Olson, A.L. / Feldmann, E.A. / Thompson, R.J. / Myers, K.H. / Santoro, M.T. / Kearns, D.B. / Cavanagh, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5tn2.cif.gz | 610.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5tn2.ent.gz | 531.8 KB | Display | PDB format |
PDBx/mmJSON format | 5tn2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tn/5tn2 ftp://data.pdbj.org/pub/pdb/validation_reports/tn/5tn2 | HTTPS FTP |
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-Related structure data
Related structure data | 5tmxC 5tn0C 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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NMR ensembles |
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Details | Monomer as determined by gel filtration |
-Components
#1: Protein/peptide | Mass: 5722.338 Da / Num. of mol.: 4 / Fragment: residues 69-111 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (strain 168) (bacteria) Strain: 168 / Gene: sinR, flaD, sin, BSU24610 / Production host: Escherichia coli (E. coli) / References: UniProt: P06533 |
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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: 200 mM / Label: conditions_1 / pH: 6 / Pressure: 1 atm / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 4 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |