BMRB Entry 50239
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50239
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Molecular Basis for the Adaptive Evolution of Environment Sensing by H-NS Proteins PubMed: 33410747
Deposition date: 2020-04-19 Original release date: 2021-08-11
Authors: Kharchenko, Vladlena; Jaremko, Lukasz
Citation: Zhao, Xiaochuan; Shahul Hameed, Umar; Kharchenko, Vladlena; Liao, Chenyi; Huser, Franceline; Remington, Jacob; Radhakrishnan, Anand; Jaremko, Mariusz; Jaremko, Lukasz; Arold, Stefan; Li, Jianing. "Molecular basis for the adaptive evolution of environment-sensing by H-NS proteins" eLife 10, e57467-e57467 (2021).
Assembly members:
entity_1, polymer, 60 residues, Formula weight is not available
Natural source: Common Name: Salmonella typhimurium Taxonomy ID: 90371 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella enterica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX6P-1
Entity Sequences (FASTA):
entity_1: GPLGSGTKAKRAARPAKYSY
VDENGETKTWTGQGRTPAVI
KKAMEEQGKQLEDFLIKELE
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 171 |
15N chemical shifts | 53 |
1H chemical shifts | 117 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 60 residues - Formula weight is not available
1 | GLY | PRO | LEU | GLY | SER | GLY | THR | LYS | ALA | LYS | |
2 | ARG | ALA | ALA | ARG | PRO | ALA | LYS | TYR | SER | TYR | |
3 | VAL | ASP | GLU | ASN | GLY | GLU | THR | LYS | THR | TRP | |
4 | THR | GLY | GLN | GLY | ARG | THR | PRO | ALA | VAL | ILE | |
5 | LYS | LYS | ALA | MET | GLU | GLU | GLN | GLY | LYS | GLN | |
6 | LEU | GLU | ASP | PHE | LEU | ILE | LYS | GLU | LEU | GLU |
Samples:
sample_1: H-NS C-terminal domain (84-137), [U-100% 13C; U-100% 15N], 200 uM; sodium chloride 50 mM; Bis-Tris 20 mM; sodium azide 0.002%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
2D (H)CACO | sample_1 | isotropic | sample_conditions_1 |
2D (H)CACBCO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA - chemical shift assignment
NMR spectrometers:
- Bruker Avance NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts