+Open data
-Basic information
Entry | Database: PDB / ID: 2kv5 | ||||||
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Title | Solution structure of the par toxin Fst in DPC micelles | ||||||
Components | Putative uncharacterized protein RNAI | ||||||
Keywords | TOXIN / toxin-antitoxin / bacterial | ||||||
Function / homology | Uncharacterized protein Function and homology information | ||||||
Biological species | Enterococcus faecalis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model 1 | ||||||
Authors | Zangger, K. / Gobl, C. / Kosol, S. / Ruckert, H.M. | ||||||
Citation | Journal: Biochemistry / Year: 2010 Title: Solution structure and membrane binding of the toxin fst of the par addiction module Authors: Gobl, C. / Kosol, S. / Stockner, T. / Ruckert, H.M. / Zangger, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kv5.cif.gz | 212.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kv5.ent.gz | 178.6 KB | Display | PDB format |
PDBx/mmJSON format | 2kv5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kv/2kv5 ftp://data.pdbj.org/pub/pdb/validation_reports/kv/2kv5 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3767.479 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: synthesized by FMOC-based solid-phase peptide synthesis Source: (synth.) Enterococcus faecalis (bacteria) / References: UniProt: Q9RLG7 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 50mM potassium phosphate; 100mM [U-99% 2H] DPC; 0.02% sodium azide; 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 5.0 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |