+Open data
-Basic information
Entry | Database: PDB / ID: 2l9x | ||||||
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Title | Trn- peptide of the two-component bacteriocin Thuricin CD | ||||||
Components | Uncharacterized protein | ||||||
Keywords | ANTIMICROBIAL PROTEIN / thioether bridges / helical loops / crosslinked / post-translationally modified | ||||||
Function / homology | Uncharacterized protein Function and homology information | ||||||
Biological species | Bacillus cereus 95/8201 (bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Sit, C.S. / Mckay, R.T. / Hill, C. / Ross, R.P. / Vederas, J.C. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2011 Title: The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links. Authors: Sit, C.S. / McKay, R.T. / Hill, C. / Ross, R.P. / Vederas, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l9x.cif.gz | 169.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l9x.ent.gz | 126.4 KB | Display | PDB format |
PDBx/mmJSON format | 2l9x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2l9x_validation.pdf.gz | 394.1 KB | Display | wwPDB validaton report |
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Full document | 2l9x_full_validation.pdf.gz | 447.7 KB | Display | |
Data in XML | 2l9x_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 2l9x_validation.cif.gz | 17 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l9/2l9x ftp://data.pdbj.org/pub/pdb/validation_reports/l9/2l9x | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2770.210 Da / Num. of mol.: 1 / Fragment: sequence database residues 18-47 / Source method: isolated from a natural source / Source: (natural) Bacillus cereus 95/8201 (bacteria) / Strain: DPC 6431 / References: UniProt: C2TQ80 |
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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: 0.5 mM [U-99% 13C; U-99% 15N] Trna, 100 uM DSS, CD3OH Solvent system: CD3OH | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |