BMRB Entry 25384
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25384
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Title: The Beclin 1 N-terminal Domain (BecN-150CSY)
Deposition date: 2014-12-08 Original release date: 2016-06-30
Authors: Yao, Shenggen; Lee, Erinna; Fairlie, Walter; Keizer, David
Citation: Yao, Shenggen; Lee, Erinna; Pettikiriarachchi, Anne; Evangelista, Marco; Keizer, David; Fairlie, Walter. "Characterisation of the conformational preference and dynamics of the intrinsically disordered N-terminal region of Beclin 1 by NMR spectroscopy" Biochim. Biophys. Acta 1864, 1128-1137 (2016).
Assembly members:
BecN-150CSY, polymer, 165 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BecN-150CSY: MGSSHHHHHHSQDPMEGSKT
SNNSTMQVSFVSQRSSQPLK
LDTSFKILDRVTIQELTAPL
LTTAQAKPGETQEEETNSGE
EPFIETPRQDGVSRRFIPPA
RMMSTESANSFTLIGEASDG
GTMENLSRRLKVTGDLFDIM
SGQTDVDHPLSEESTDTLLD
QLDTY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 438 |
| 15N chemical shifts | 142 |
| 1H chemical shifts | 293 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 165 residues - Formula weight is not available
Residues (-14) - (-1) represent a non-native tag Residue 151 is non-native added to facilitate quantitation by UV spectroscopy
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | GLN | ASP | PRO | MET | GLU | GLY | SER | LYS | THR | ||||
| 3 | SER | ASN | ASN | SER | THR | MET | GLN | VAL | SER | PHE | ||||
| 4 | VAL | SER | GLN | ARG | SER | SER | GLN | PRO | LEU | LYS | ||||
| 5 | LEU | ASP | THR | SER | PHE | LYS | ILE | LEU | ASP | ARG | ||||
| 6 | VAL | THR | ILE | GLN | GLU | LEU | THR | ALA | PRO | LEU | ||||
| 7 | LEU | THR | THR | ALA | GLN | ALA | LYS | PRO | GLY | GLU | ||||
| 8 | THR | GLN | GLU | GLU | GLU | THR | ASN | SER | GLY | GLU | ||||
| 9 | GLU | PRO | PHE | ILE | GLU | THR | PRO | ARG | GLN | ASP | ||||
| 10 | GLY | VAL | SER | ARG | ARG | PHE | ILE | PRO | PRO | ALA | ||||
| 11 | ARG | MET | MET | SER | THR | GLU | SER | ALA | ASN | SER | ||||
| 12 | PHE | THR | LEU | ILE | GLY | GLU | ALA | SER | ASP | GLY | ||||
| 13 | GLY | THR | MET | GLU | ASN | LEU | SER | ARG | ARG | LEU | ||||
| 14 | LYS | VAL | THR | GLY | ASP | LEU | PHE | ASP | ILE | MET | ||||
| 15 | SER | GLY | GLN | THR | ASP | VAL | ASP | HIS | PRO | LEU | ||||
| 16 | SER | GLU | GLU | SER | THR | ASP | THR | LEU | LEU | ASP | ||||
| 17 | GLN | LEU | ASP | THR | TYR |
Samples:
sample_1: BecN-150CSY, [U-15N], 0.18 mM; H2O 95%; D2O 5%
sample_2: BecN-150CSY, [U-100% 13C; U-100% 15N], 0.12 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2, Bruker - processing
XEASY v1.3, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts