BMRB Entry 52014
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52014
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solid-state NMR assignment of side-chain protons of HBV core protein at fast MAS and high field PubMed: 37829013
Deposition date: 2023-07-06 Original release date: 2023-09-19
Authors: Callon, Morgane; Luder, Dominique; Malar, Alexander; Wiegand, Thomas; Rimal, Vaclav; Lecoq, Lauriane; Bockmann, Anja; Samoson, Ago; Meier, Beat
Citation: Callon, Morgane; Luder, Dominique; Malar, Alexander; Wiegand, Thomas; Rimal, Vaclav; Lecoq, Lauriane; Bockmann, Anja; Samoson, Ago; Meier, Beat. "High and fast: NMR protein\u2013proton side-chain assignments at 160 kHz and 1.2 GHz" Chem. Sci. 14, 10824-10834 (2023).
Assembly members:
entity_1, polymer, 149 residues, 17777 Da.
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 Vector: pET-28a2
Entity Sequences (FASTA):
entity_1: MDIDPYKEFGATVELLSFLP
SDFFPSVRDLLDTASALYRE
ALESPEHCSPHHTALRQAIL
CWGELMTLATWVGVNLEDPA
SRDLVVSYVNTNMGLKFRQL
LWFHISCLTFGRETVIEYLV
SFGVWIRTPPAYRPPNAPIL
STLPETTVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 322 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 414 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Cp149 | 1 |
Entities:
Entity 1, Cp149 149 residues - 17777 Da.
Residues 1-149 of the full-length protein Cp183 containing 183 residues.
| 1 | MET | ASP | ILE | ASP | PRO | TYR | LYS | GLU | PHE | GLY | ||||
| 2 | ALA | THR | VAL | GLU | LEU | LEU | SER | PHE | LEU | PRO | ||||
| 3 | SER | ASP | PHE | PHE | PRO | SER | VAL | ARG | ASP | LEU | ||||
| 4 | LEU | ASP | THR | ALA | SER | ALA | LEU | TYR | ARG | GLU | ||||
| 5 | ALA | LEU | GLU | SER | PRO | GLU | HIS | CYS | SER | PRO | ||||
| 6 | HIS | HIS | THR | ALA | LEU | ARG | GLN | ALA | ILE | LEU | ||||
| 7 | CYS | TRP | GLY | GLU | LEU | MET | THR | LEU | ALA | THR | ||||
| 8 | TRP | VAL | GLY | VAL | ASN | LEU | GLU | ASP | PRO | ALA | ||||
| 9 | SER | ARG | ASP | LEU | VAL | VAL | SER | TYR | VAL | ASN | ||||
| 10 | THR | ASN | MET | GLY | LEU | LYS | PHE | ARG | GLN | LEU | ||||
| 11 | LEU | TRP | PHE | HIS | ILE | SER | CYS | LEU | THR | PHE | ||||
| 12 | GLY | ARG | GLU | THR | VAL | ILE | GLU | TYR | LEU | VAL | ||||
| 13 | SER | PHE | GLY | VAL | TRP | ILE | ARG | THR | PRO | PRO | ||||
| 14 | ALA | TYR | ARG | PRO | PRO | ASN | ALA | PRO | ILE | LEU | ||||
| 15 | SER | THR | LEU | PRO | GLU | THR | THR | VAL | VAL |
Samples:
sample_1: Hepatitis B virus capsid core protein Cp149, [U-99% 13C; U-99% 15N], 1 mg/mL
sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C CP | sample_1 | isotropic | sample_conditions_1 |
| 3D hCCH-TOCSY C9 | sample_1 | isotropic | sample_conditions_1 |
| 3D HcCH-TOCSY WALTZ | sample_1 | isotropic | sample_conditions_1 |
| 3D hNCH | sample_1 | isotropic | sample_conditions_1 |
| 3D hCCH-TOCSY WALTZ | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4 - collection, processing
CcpNMR v2.5 - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker AVANCE NEO 1200 MHz