BMRB Entry 27189
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27189
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Title: N,H,Ca,Cb chemical shifts and methionine sidechain chemical shifts of the isolated P1 domain of CheA from Escherichia Coli PubMed: 29184123
Deposition date: 2017-07-21 Original release date: 2017-12-14
Authors: Minato, Yuichi; Ueda, Takumi; Machiyama, Asako; Iwai, Hideo; Shimada, Ichio
Citation: Minato, Yuichi; Ueda, Takumi; Machiyama, Asako; Iwai, Hideo; Shimada, Ichio. "Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR" Sci. Rep. 7, 16462-16462 (2017).
Assembly members:
P1_domain_of_CheA, polymer, 132 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 Vector: pET43a
Entity Sequences (FASTA):
P1_domain_of_CheA: MDISDFYQTFFDEADELLAD
MEQHLLVLQPEAPDAEQLNA
IFRAAHSIKGGAGTFGFSVL
QETTHLMENLLDEARRGEMQ
LNTDIINLFLETKDIMQEQL
DAYKQSQEPDAASFDYICQA
LRQLALEAKGET
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 254 |
15N chemical shifts | 128 |
1H chemical shifts | 168 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | P1 domain of CheA | 1 |
Entities:
Entity 1, P1 domain of CheA 132 residues - Formula weight is not available
1 | MET | ASP | ILE | SER | ASP | PHE | TYR | GLN | THR | PHE | ||||
2 | PHE | ASP | GLU | ALA | ASP | GLU | LEU | LEU | ALA | ASP | ||||
3 | MET | GLU | GLN | HIS | LEU | LEU | VAL | LEU | GLN | PRO | ||||
4 | GLU | ALA | PRO | ASP | ALA | GLU | GLN | LEU | ASN | ALA | ||||
5 | ILE | PHE | ARG | ALA | ALA | HIS | SER | ILE | LYS | GLY | ||||
6 | GLY | ALA | GLY | THR | PHE | GLY | PHE | SER | VAL | LEU | ||||
7 | GLN | GLU | THR | THR | HIS | LEU | MET | GLU | ASN | LEU | ||||
8 | LEU | ASP | GLU | ALA | ARG | ARG | GLY | GLU | MET | GLN | ||||
9 | LEU | ASN | THR | ASP | ILE | ILE | ASN | LEU | PHE | LEU | ||||
10 | GLU | THR | LYS | ASP | ILE | MET | GLN | GLU | GLN | LEU | ||||
11 | ASP | ALA | TYR | LYS | GLN | SER | GLN | GLU | PRO | ASP | ||||
12 | ALA | ALA | SER | PHE | ASP | TYR | ILE | CYS | GLN | ALA | ||||
13 | LEU | ARG | GLN | LEU | ALA | LEU | GLU | ALA | LYS | GLY | ||||
14 | GLU | THR |
Samples:
sample_1: P1 domain of CheA, [U-13C; U-15N], 0.78 mM; sodium phosphate 20 mM; DTT 2 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 7.1; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts