BMRB Entry 15261
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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/BMR15261
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Title: LactococcinGb in DPC and TFE PubMed: 18187052
Deposition date: 2007-05-22 Original release date: 2008-02-21
Authors: Rogne, Per; Kristiansen, Per; Fimland, Gunnar; Nissen-Meyer, Jon
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:
lcnGb, polymer, 35 residues, 4118.848 Da.
Natural source: Common Name: Lactcococcus 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):
lcnGb: KKWGWLAWVDPAYEFIKGFG
KGAIKEGNKDKWKNI
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 485 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lcnGb | 1 |
Entities:
Entity 1, lcnGb 35 residues - 4118.848 Da.
| 1 | LYS | LYS | TRP | GLY | TRP | LEU | ALA | TRP | VAL | ASP | ||||
| 2 | PRO | ALA | TYR | GLU | PHE | ILE | LYS | GLY | PHE | GLY | ||||
| 3 | LYS | GLY | ALA | ILE | LYS | GLU | GLY | ASN | LYS | ASP | ||||
| 4 | LYS | TRP | LYS | ASN | ILE |
Samples:
LcnGb_DPC: lactococcinG beta, [U-15N], 1 mM; DPC, [U-2H], 200 mM; D2O 10%; TFA 0.1%; DSS 0.2 mM
lcnGb_TFE: Lactococcin Gb, [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 | LcnGb_DPC | isotropic | 25C |
| 2D 1H-1H TOCSY | LcnGb_DPC | isotropic | 25C |
| 2D 1H-1H NOESY | LcnGb_DPC | isotropic | 25C |
| 3D 1H-15N TOCSY | LcnGb_DPC | isotropic | 25C |
| 3D 1H-15N NOESY | LcnGb_DPC | isotropic | 25C |
| 2D 1H-15N HSQC | lcnGb_TFE | isotropic | 25C |
| 2D 1H-1H TOCSY | lcnGb_TFE | isotropic | 25C |
| 2D 1H-1H NOESY | lcnGb_TFE | isotropic | 25C |
| 3D 1H-15N TOCSY | lcnGb_TFE | isotropic | 25C |
| 3D 1H-15N NOESY | lcnGb_TFE | isotropic | 25C |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA v1.4.1, Keller and Wuthrich - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol v2k.2, Koradi, Billeter and Wuthrich - RMSD value calculation, Visualization
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts