+Open data
-Basic information
Entry | Database: PDB / ID: 2jpj | ||||||
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Title | Lactococcin G-a in DPC | ||||||
Components | Bacteriocin lactococcin-G subunit alpha | ||||||
Keywords | ANTIMICROBIAL PROTEIN / Anti-microbial / Membrane bound | ||||||
Function / homology | Alpha enterocin/lactococcin / Alpha/beta enterocin family / killing of cells of another organism / defense response to bacterium / Bacteriocin lactococcin-G subunit alpha Function and homology information | ||||||
Biological species | Lactococcus lactis (lactic acid bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | LactococcinG, alpha-peptide M21L/M24L double mutant in DPC micelles | ||||||
Authors | Rogne, P. / Fimland, G. / Nissen-Meyer, J. / Kristiansen, P.E. | ||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2008 Title: Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G Authors: 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 | 2jpj.cif.gz | 276.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jpj.ent.gz | 233.4 KB | Display | PDB format |
PDBx/mmJSON format | 2jpj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jpj_validation.pdf.gz | 484.5 KB | Display | wwPDB validaton report |
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Full document | 2jpj_full_validation.pdf.gz | 647.4 KB | Display | |
Data in XML | 2jpj_validation.xml.gz | 20.6 KB | Display | |
Data in CIF | 2jpj_validation.cif.gz | 29.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jp/2jpj ftp://data.pdbj.org/pub/pdb/validation_reports/jp/2jpj | HTTPS FTP |
-Related structure data
Related structure data | 2jpkC 2jplC 2jpmC C: citing same article (ref.) |
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Similar structure data | |
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: 4317.870 Da / Num. of mol.: 1 / Mutation: M21L, M24L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lactococcus lactis (lactic acid bacteria) Strain: LMGT 2081 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): RIL (DE3) pLysS / References: UniProt: P36961 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: LactococcinG, alpha-peptide M21L/M24L double mutant in DPC micelles | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1 mM [U-15N] lcnGa, 200 mM [U-2H] DPC, 0.1 % TFA, 10 % D2O, 0.2 mM DSS, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | pH: 2.8 / 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: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 662 / NOE intraresidue total count: 268 / NOE long range total count: 0 / NOE medium range total count: 197 / NOE sequential total count: 197 / Hydrogen bond constraints total count: 40 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 21 / Protein psi angle constraints total count: 21 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 102 / Conformers submitted total number: 20 |