BMRB Entry 16148
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16148
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Title: NMR structure of Plantaricin K in DPC-micelles PubMed: 19538999
Deposition date: 2009-01-30 Original release date: 2009-06-25
Authors: Rogne, Per; Haugen, Mads Christofer; Nissen-Meyer, Jon; Kristiansen, Per Eugen
Citation: Rogne, Per; Haugen, Christofer; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per Eugen. "Three-dimensional structure of the two-peptide bacteriocin plantaricin JK" Peptides 30, 1613-1621 (2009).
Assembly members:
PlnK, polymer, 32 residues, 3509.989 Da.
Natural source: Common Name: Lactobacillus plantarum Taxonomy ID: 1590 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactobacillus plantarum
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
PlnK: RRSRKNGIGYAIGYAFGAVE
RAVLGGSRDYNK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 47 |
| 15N chemical shifts | 31 |
| 1H chemical shifts | 186 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PlnK | 1 |
Entities:
Entity 1, PlnK 32 residues - 3509.989 Da.
| 1 | ARG | ARG | SER | ARG | LYS | ASN | GLY | ILE | GLY | TYR | ||||
| 2 | ALA | ILE | GLY | TYR | ALA | PHE | GLY | ALA | VAL | GLU | ||||
| 3 | ARG | ALA | VAL | LEU | GLY | GLY | SER | ARG | ASP | TYR | ||||
| 4 | ASN | LYS |
Samples:
sample_1: PlnK 1 mM; DPC, [U-99% 2H], 170 mM; TFA 0.1%; D2O 10%; H2O 90%; DSS 0.2 mM
sample_conditions_1: ionic strength: 0 M; pH: 2.5; pressure: 1 atm; temperature: 312 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
Molmol v2k2, Koradi, Billeter and Wuthrich - data analysis
ACME v2001.006.11.26, Delaglio, Zhengrong and Bax - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16149 |
| PDB | |
| EMBL | CAA64197 CCC77914 CDN27149 |
| GB | AAS21882 ACO06037 ADE08244 ADN97561 AFJ79559 |
| REF | WP_003641972 WP_011100996 WP_033611279 YP_004888428 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts