BMRB Entry 52378
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52378
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Title: BELL2 1H 13C 15N_assignment PubMed: 38907837
Deposition date: 2024-03-29 Original release date: 2024-07-22
Authors: Delcourte, Loic; Sanchez, Corinne; Morvan, Estelle; Berbon, Melanie; Grelard, Axelle; Saragaglia, Claire; Dakhli, Thiery; Bardiaux, Benjamin; Habenstein, Birgit; Kauffmann, Brice; Saupe, Sven; Loquet, Antoine
Citation: Delcourte, Loic; Sanchez, Corinne; Morvan, Estelle; Berbon, Melanie; Grelard, Axelle; Saragaglia, Claire; Dakhli, Thierry; Thore, Stephane; Bardiaux, Benjamin; Habenstein, Birgit; Kauffmann, Brice; Saupe, Sven; Loquet, Antoine. "NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes" Biomol. NMR Assign. ., .-. (2024).
Assembly members:
entity_1, polymer, 102 residues, Formula weight is not available
Natural source: Common Name: Streptomyces olivochromogenes Taxonomy ID: 1963 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces olivochromogenes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24
Entity Sequences (FASTA):
entity_1: DPISVALLAALAGGAGGELG
RQAWVNLTALARRPFGRGHG
ESAQAPAVSSGEAELVRLQE
TPGDAARAQALSTALAVRAA
FDAEFSSGLQQWHEQAKVVR
TG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 376 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 576 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BELL2 | 1 |
Entities:
Entity 1, BELL2 102 residues - Formula weight is not available
| 1 | ASP | PRO | ILE | SER | VAL | ALA | LEU | LEU | ALA | ALA | ||||
| 2 | LEU | ALA | GLY | GLY | ALA | GLY | GLY | GLU | LEU | GLY | ||||
| 3 | ARG | GLN | ALA | TRP | VAL | ASN | LEU | THR | ALA | LEU | ||||
| 4 | ALA | ARG | ARG | PRO | PHE | GLY | ARG | GLY | HIS | GLY | ||||
| 5 | GLU | SER | ALA | GLN | ALA | PRO | ALA | VAL | SER | SER | ||||
| 6 | GLY | GLU | ALA | GLU | LEU | VAL | ARG | LEU | GLN | GLU | ||||
| 7 | THR | PRO | GLY | ASP | ALA | ALA | ARG | ALA | GLN | ALA | ||||
| 8 | LEU | SER | THR | ALA | LEU | ALA | VAL | ARG | ALA | ALA | ||||
| 9 | PHE | ASP | ALA | GLU | PHE | SER | SER | GLY | LEU | GLN | ||||
| 10 | GLN | TRP | HIS | GLU | GLN | ALA | LYS | VAL | VAL | ARG | ||||
| 11 | THR | GLY |
Samples:
sample_1: HEPES 20 mM; sodium chloride 80 mM; BELL2 domain, [U-100% 13C; U-100% 15N], 1 mM
sample_conditions_1: ionic strength: 0.08 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment
NMR spectrometers:
- Bruker Bruker Avance NEO 700 MHz MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts