BMRB Entry 15259
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15259
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Title: LactococcinGa in DPC and TFE PubMed: 18187052
Deposition date: 2007-05-22 Original release date: 2008-02-21
Authors: Rogne, Per; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per
Citation: Rogne, Per; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per. "Three-dimensional structure of the two peptides that constitutes the two-peptide bacteriocin Lactococcin G" Biochim. Biophys. Acta. 1784, 543-554 (2008).
Assembly members:
lcnGa, polymer, 39 residues, 4317.912 Da.
Natural source: Common Name: Lactococcus lactis Taxonomy ID: 1358 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactococcus lactis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
lcnGa: GTWDDIGQGIGRVAYWVGKA
LGNLSDVNQASRINRKKKH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 506 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lcnGa | 1 |
Entities:
Entity 1, lcnGa 39 residues - 4317.912 Da.
| 1 | GLY | THR | TRP | ASP | ASP | ILE | GLY | GLN | GLY | ILE | ||||
| 2 | GLY | ARG | VAL | ALA | TYR | TRP | VAL | GLY | LYS | ALA | ||||
| 3 | LEU | GLY | ASN | LEU | SER | ASP | VAL | ASN | GLN | ALA | ||||
| 4 | SER | ARG | ILE | ASN | ARG | LYS | LYS | LYS | HIS |
Samples:
lcnGa_DPC: lcnGa, [U-15N], 1 mM; DPC, [U-2H], 200 mM; TFA 0.1%; D2O 10%; DSS 0.2 mM
lcnGaTFE: lcnG a TFE, [U-15N], 1 mM; TFE, [U-2H], 90%; TFA 0.1%; DSS 0.2 mM
25C: pH: 2.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | lcnGa_DPC | isotropic | 25C |
| 2D 1H-1H NOESY | lcnGa_DPC | isotropic | 25C |
| 2D 1H-1H TOCSY | lcnGa_DPC | isotropic | 25C |
| 3D 1H-15N NOESY | lcnGa_DPC | isotropic | 25C |
| 3D 1H-15N TOCSY | lcnGa_DPC | isotropic | 25C |
| 2D 1H-15N HSQC | lcnGaTFE | isotropic | 25C |
| 2D 1H-1H TOCSY | lcnGaTFE | isotropic | 25C |
| 2D 1H-1H NOESY | lcnGaTFE | isotropic | 25C |
| 3D 1H-15N TOCSY | lcnGaTFE | isotropic | 25C |
| 3D 1H-15N NOESY | lcnGaTFE | isotropic | 25C |
Software:
VNMR, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA v1.4.1, Keller and Wuthrich - chemical shift assignment, data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - torsion angle prediction
Molmol v2k.2, Koradi, Billeter and Wuthrich - RMSD value calculation, Structure visualization
TOPSPIN v1.3, Bruker Biospin - collection, processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
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