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Yorodumi- PDB-2rlw: Three-Dimensional Structure of the two Peptides that Constitute t... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2rlw | ||||||
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Title | Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide Bacteriocin Plantaracin EF | ||||||
Components | PlnF | ||||||
Keywords | TOXIN / peptide plnF | ||||||
Function / homology | Bacteriocin Function and homology information | ||||||
Biological species | Lactobacillus plantarum (bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Fimland, N. / Rogne, P. / Fimland, G. / Nissen-Meyer, J. / Kristiansen, P. | ||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2008 Title: Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF Authors: Fimland, N. / Rogne, P. / Fimland, G. / Nissen-Meyer, J. / Kristiansen, P.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rlw.cif.gz | 231.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rlw.ent.gz | 198.2 KB | Display | PDB format |
PDBx/mmJSON format | 2rlw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rlw_validation.pdf.gz | 336.9 KB | Display | wwPDB validaton report |
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Full document | 2rlw_full_validation.pdf.gz | 453.8 KB | Display | |
Data in XML | 2rlw_validation.xml.gz | 15.1 KB | Display | |
Data in CIF | 2rlw_validation.cif.gz | 24.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/2rlw ftp://data.pdbj.org/pub/pdb/validation_reports/rl/2rlw | 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: 3709.182 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lactobacillus plantarum (bacteria) / Strain: C11 / Gene: plnF / Production host: Escherichia coli (E. coli) / Strain (production host): bl21 / References: UniProt: P71469 |
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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: 0.2 mM DSS, 0.1 % TFA, 200 mM [U-2H] DPC, 1 mM [U-95% 15N] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 2.5 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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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: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |