BMRB Entry 18814
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18814
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Title: 13C and 15N NMR chemical shifts of E. coli full-length H-NS protein PubMed: 23601147
Deposition date: 2012-10-31 Original release date: 2014-02-14
Authors: Renault, Marie; Garcia, Jesus; Cordeiro, Tiago; Baldus, Marc; Pons, Miquel
Citation: Renault, Marie; Garcia, Jesus; Cordeiro, Tiago; Baldus, Marc; Pons, Miquel. "Protein oligomers studied by solid-state NMR--the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein." FEBS J. 280, 2916-2928 (2013).
Assembly members:
H-NS, polymer, 137 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
H-NS: MSEALKILNNIRTLRAQARE
CTLETLEEMLEKLEVVVNER
REEESAAAAEVEERTRKLQQ
YREMLIADGIDPNELLNSLA
AVKSGTKAKRAQRPAKYSYV
DENGETKTWTGQGRTPAVIK
KAMDEQGKSLDDFLIKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 155 |
| 15N chemical shifts | 7 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H-NS 1-137 | 1 |
Entities:
Entity 1, H-NS 1-137 137 residues - Formula weight is not available
| 1 | MET | SER | GLU | ALA | LEU | LYS | ILE | LEU | ASN | ASN | ||||
| 2 | ILE | ARG | THR | LEU | ARG | ALA | GLN | ALA | ARG | GLU | ||||
| 3 | CYS | THR | LEU | GLU | THR | LEU | GLU | GLU | MET | LEU | ||||
| 4 | GLU | LYS | LEU | GLU | VAL | VAL | VAL | ASN | GLU | ARG | ||||
| 5 | ARG | GLU | GLU | GLU | SER | ALA | ALA | ALA | ALA | GLU | ||||
| 6 | VAL | GLU | GLU | ARG | THR | ARG | LYS | LEU | GLN | GLN | ||||
| 7 | TYR | ARG | GLU | MET | LEU | ILE | ALA | ASP | GLY | ILE | ||||
| 8 | ASP | PRO | ASN | GLU | LEU | LEU | ASN | SER | LEU | ALA | ||||
| 9 | ALA | VAL | LYS | SER | GLY | THR | LYS | ALA | LYS | ARG | ||||
| 10 | ALA | GLN | ARG | PRO | ALA | LYS | TYR | SER | TYR | VAL | ||||
| 11 | ASP | GLU | ASN | GLY | GLU | THR | LYS | THR | TRP | THR | ||||
| 12 | GLY | GLN | GLY | ARG | THR | PRO | ALA | VAL | ILE | LYS | ||||
| 13 | LYS | ALA | MET | ASP | GLU | GLN | GLY | LYS | SER | LEU | ||||
| 14 | ASP | ASP | PHE | LEU | ILE | LYS | GLN |
Samples:
H-NS_(1-137): H-NS, [U-100% 13C; U-100% 15N], 10 mg
H-NS_(1-47): H-NS, [U-100% 13C; U-100% 15N], 15 mg
sample_conditions_1: ionic strength: 0.25 M; pH: 7.0; pressure: 1 atm; temperature: 277 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 13C-13C PDSD | H-NS_(1-47) | solid | sample_conditions_1 |
| 2D 15N-13C NCACX | H-NS_(1-47) | solid | sample_conditions_1 |
| 2D 15N-13C NCOCX | H-NS_(1-47) | solid | sample_conditions_1 |
| 2D 13C-13C PDSD | H-NS_(1-137) | solid | sample_conditions_1 |
| 2D 15N-13C NCACX | H-NS_(1-137) | solid | sample_conditions_1 |
| 2D 15N-13C NCOCX | H-NS_(1-137) | solid | sample_conditions_1 |
| 3D 15N-13C-13C NCOCX | H-NS_(1-137) | solid | sample_conditions_1 |
Software:
SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking
TOPSPIN v3.1, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 700 MHz