BMRB Entry 15969
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15969
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Heteronuclear NMR assignments for the dimeric human hepatitis B virus core protein under capsid dissociating conditions PubMed: 18952101
Deposition date: 2008-10-01 Original release date: 2009-02-16
Authors: Freund, Stefan; Johnson, Christopher; Jaulent, Agnes; Ferguson, Neil
Citation: Freund, Stefan; Johnson, Christopher; Jaulent, Agnes; Ferguson, Neil. "Moving towards high resolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein" J. Mol. Biol. 384, 1301-1303 (2008).
Assembly members:
Hepatitis_B_virus_coat_protein, polymer, 149 residues, 33540 Da.
Natural source: Common Name: Hepatitis B virus Taxonomy ID: 10407 Superkingdom: Viruses Kingdom: not available Genus/species: Orthohepadnavirus Hepatitis B virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Hepatitis_B_virus_coat_protein: MDIDPYKEFGATVELLSFLP
SDFFPSVRDLLDTAAALYRD
ALESPEHCSPHHTALRQAIL
CWGDLMTLATWVGTNLEDPA
SRDLVVSYVNTNVGLKFRQL
LWFHISCLTFGRETVLEYLV
SFGVWIRTPPAYRPPNAPIL
STLPETTVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 327 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hepatitis B virus coat protein monomer, chain 1 | 1 |
| 2 | Hepatitis B virus coat protein monomer, chain 2 | 1 |
Entities:
Entity 1, Hepatitis B virus coat protein monomer, chain 1 149 residues - 33540 Da.
The dimeric hepatitis core protein assignments deposited here correspond to residues 1-149 of the full length (183 residues) core protein. The C-terminal nucleic acid binding domain (residues 150-183) was truncated to simplify spectral assignment. Residues 1-149 of the core protein contain all structured regions reported to date and can form recombinant capsid like particles essentially identical to nucleocapsids isolated from patients infected with hepatitis B virus.
| 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 | ALA | ALA | LEU | TYR | ARG | ASP | ||||
| 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 | ASP | LEU | MET | THR | LEU | ALA | THR | ||||
| 8 | TRP | VAL | GLY | THR | ASN | LEU | GLU | ASP | PRO | ALA | ||||
| 9 | SER | ARG | ASP | LEU | VAL | VAL | SER | TYR | VAL | ASN | ||||
| 10 | THR | ASN | VAL | GLY | LEU | LYS | PHE | ARG | GLN | LEU | ||||
| 11 | LEU | TRP | PHE | HIS | ILE | SER | CYS | LEU | THR | PHE | ||||
| 12 | GLY | ARG | GLU | THR | VAL | LEU | 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 coat protein monomer, chain 1, [U-13C; U-15N; U-2H], 150 ± 3 uM
sample_conditions_1: ionic strength: < 30 mM; pH: 9.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY_HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CACO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
FELIX v2004, Accelrys - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 900 MHz
Related Database Links:
| UNP | P03147 |
| PDB | |
| DBJ | BAA85372 BAA85376 |
| EMBL | CAA59662 CAM58608 CAM58609 CAM58712 CAM58713 |
| GB | AAA02846 AAA02847 AAA45486 AAL31811 AAL31812 |
| SP | P03147 Q9QMI2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts