BMRB Entry 52549
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52549
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Title: Backbone NMR Resonance Assignment for the Wild Type E. coli b-clamp
Deposition date: 2024-07-14 Original release date: 2024-07-18
Authors: Mahdi, Sam; Lim, Socheata; Beuning, Penny; Korzhnev, Dmitry
Citation: Mahdi, Sam; Lim, Socheata; Beuning, Penny; Korzhnev, Dmitry. "Backbone NMR Resonance Assignment for the Wild type and Stabilized E. coli b-clamp" Biomol. NMR Assignments ., .-..
Assembly members:
entity_1, polymer, 367 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: pET28B+
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 260 |
15N chemical shifts | 195 |
1H chemical shifts | 195 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Wild Type E. coli b-clamp | 1 |
Entities:
Entity 1, Wild Type E. coli b-clamp 367 residues - Formula weight is not available
1 | GLY | MET | LYS | PHE | THR | VAL | GLU | ARG | GLU | HIS | ||||
2 | LEU | LEU | LYS | PRO | LEU | GLN | GLN | VAL | SER | GLY | ||||
3 | PRO | LEU | GLY | GLY | ARG | PRO | THR | LEU | PRO | ILE | ||||
4 | LEU | GLY | ASN | LEU | LEU | LEU | GLN | VAL | ALA | ASP | ||||
5 | GLY | THR | LEU | SER | LEU | THR | GLY | THR | ASP | LEU | ||||
6 | GLU | MET | GLU | MET | VAL | ALA | ARG | VAL | ALA | LEU | ||||
7 | VAL | GLN | PRO | HIS | GLU | PRO | GLY | ALA | THR | THR | ||||
8 | VAL | PRO | ALA | ARG | LYS | PHE | PHE | ASP | ILE | CYS | ||||
9 | ARG | GLY | LEU | PRO | GLU | GLY | ALA | GLU | ILE | ALA | ||||
10 | VAL | GLN | LEU | GLU | GLY | GLU | ARG | MET | LEU | VAL | ||||
11 | ARG | SER | GLY | ARG | SER | ARG | PHE | SER | LEU | SER | ||||
12 | THR | LEU | PRO | ALA | ALA | ASP | PHE | PRO | ASN | LEU | ||||
13 | ASP | ASP | TRP | GLN | SER | GLU | VAL | GLU | PHE | THR | ||||
14 | LEU | PRO | GLN | ALA | THR | MET | LYS | ARG | LEU | ILE | ||||
15 | GLU | ALA | THR | GLN | PHE | SER | MET | ALA | HIS | GLN | ||||
16 | ASP | VAL | ARG | TYR | TYR | LEU | ASN | GLY | MET | LEU | ||||
17 | PHE | GLU | THR | GLU | GLY | GLU | GLU | LEU | ARG | THR | ||||
18 | VAL | ALA | THR | ASP | GLY | HIS | ARG | LEU | ALA | VAL | ||||
19 | CYS | SER | MET | PRO | ILE | GLY | GLN | SER | LEU | PRO | ||||
20 | SER | HIS | SER | VAL | ILE | VAL | PRO | ARG | LYS | GLY | ||||
21 | VAL | ILE | GLU | LEU | MET | ARG | MET | LEU | ASP | GLY | ||||
22 | GLY | ASP | ASN | PRO | LEU | ARG | VAL | GLN | ILE | GLY | ||||
23 | SER | ASN | ASN | ILE | ARG | ALA | HIS | VAL | GLY | ASP | ||||
24 | PHE | ILE | PHE | THR | SER | LYS | LEU | VAL | ASP | GLY | ||||
25 | ARG | PHE | PRO | ASP | TYR | ARG | ARG | VAL | LEU | PRO | ||||
26 | LYS | ASN | PRO | ASP | LYS | HIS | LEU | GLU | ALA | GLY | ||||
27 | CYS | ASP | LEU | LEU | LYS | GLN | ALA | PHE | ALA | ARG | ||||
28 | ALA | ALA | ILE | LEU | SER | ASN | GLU | LYS | PHE | ARG | ||||
29 | GLY | VAL | ARG | LEU | TYR | VAL | SER | GLU | ASN | GLN | ||||
30 | LEU | LYS | ILE | THR | ALA | ASN | ASN | PRO | GLU | GLN | ||||
31 | GLU | GLU | ALA | GLU | GLU | ILE | LEU | ASP | VAL | THR | ||||
32 | TYR | SER | GLY | ALA | GLU | MET | GLU | ILE | GLY | PHE | ||||
33 | ASN | VAL | SER | TYR | VAL | LEU | ASP | VAL | LEU | ASN | ||||
34 | ALA | LEU | LYS | CYS | GLU | ASN | VAL | ARG | MET | MET | ||||
35 | LEU | THR | ASP | SER | VAL | SER | SER | VAL | GLN | ILE | ||||
36 | GLU | ASP | ALA | ALA | SER | GLN | SER | ALA | ALA | TYR | ||||
37 | VAL | VAL | MET | PRO | MET | ARG | LEU |
Samples:
sample_1: Wild Type E. coli b-clamp, [U-13C; U-15N; U-2H; 99% 1HD-Ile,Leu; 99% 1HG-Val], 1 mM; Na2HPO4 100 mM; NaCl 150 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO TROSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCA TROSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY TROSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY v1.47 - chemical shift assignment
NMR spectrometers:
- Agilent VNMRS 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts