BMRB Entry 51294
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51294
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Title: Backbone assignment of Hepatitis B virus core protein Cp149 dimer by solution NMR at pH 7.5 PubMed: 36042894
Deposition date: 2022-01-27 Original release date: 2022-07-13
Authors: Lecoq, Lauriane; Briday, Mathilde; Bockmann, Anja
Citation: Briday, Mathilde; Hallle, Francois; Lecoq, Lauriane; Radix, Sylvie; Martin, Juliette; Montserret, Roland; Dujardin, Marie; Fogeron, Marie-Laure; Nassal, Michael; Meier, Beat; Lomberget, Thierry; Bockmann, Anja. "Pharmacomodulation of a ligand targeting the HBV capsid hydrophobic pocket" Chem. Sci. 13, 8840-8847 (2022).
Assembly members:
entity_1, polymer, 149 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 Vector: pET28a2
Entity Sequences (FASTA):
entity_1: MDIDPYKEFGATVELLSFLP
SDFFPSVRDLLDTASALYRE
ALESPEHCSPHHTALRQAIL
CWGELMTLATWVGVNLEDPA
SRDLVVSYVNTNMGLKFRQL
LWFHISCLTFGRETVIEYLV
SFGVWIRTPPAYRPPNAPIL
STLPETTVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 182 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Cp149, chain 1 | 1 |
| 2 | Cp149, chain 2 | 1 |
Entities:
Entity 1, Cp149, chain 1 149 residues - Formula weight is not available
| 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: Cp149 dimer, [U-98% 13C; U-98% 15N; U-98% 2H], 100 uM; HEPES 50 mM; DTT 5 mM
sample_2: Cp149 dimer, [U-99% 13C; U-99% 15N], 100 uM; HEPES 50 mM; DTT 5 mM
sample_conditions_1: ionic strength: 0 M; pH: 7.5; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4 - collection, processing
CcpNMR v2.5 - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts