BMRB Entry 34709
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34709
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NMR-STAR v3 text file.
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Title: Solution structure of homodimeric Capsid protein (residues 17-95) of Tick-borne encephalitis virus (d16-TBEVC) PubMed: 36223838
Deposition date: 2022-02-14 Original release date: 2022-10-14
Authors: Novotny, R.
Citation: Selinger, Martin; Novotny, Radim; Sys, Jakub; Roby, Justin; Tykalova, Hana; Ranjani, Ganji Sri; Vancova, Marie; Jaklova, Katerina; Kaufman, Filip; Bloom, Marshall; Zdrahal, Zbynek; Grubhoffer, Libor; Forwood, Jade; Hrabal, Richard; Rumlova, Michaela; Sterba, Jan. "Tick-borne encephalitis virus capsid protein induces translational shutoff as revealed by its structural-biological analysis" J. Biol. Chem. 298, 102585-102585 (2022).
Assembly members:
entity_1, polymer, 79 residues, 8869.752 Da.
Natural source: Common Name: Tick-borne encephalitis virus Taxonomy ID: 11084 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Tick-borne encephalitis virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET22B
Entity Sequences (FASTA):
entity_1: VSKETATKTRQPRVQMPNGL
VLMRMMGILWHAVAGTARNP
VLKAFWNSVPLKQATAALRK
IKRTVSALMVGLQKRGKRR
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 58 |
| 1H chemical shifts | 394 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 1 |
Entities:
Entity 1, unit_1 79 residues - 8869.752 Da.
| 1 | VAL | SER | LYS | GLU | THR | ALA | THR | LYS | THR | ARG | ||||
| 2 | GLN | PRO | ARG | VAL | GLN | MET | PRO | ASN | GLY | LEU | ||||
| 3 | VAL | LEU | MET | ARG | MET | MET | GLY | ILE | LEU | TRP | ||||
| 4 | HIS | ALA | VAL | ALA | GLY | THR | ALA | ARG | ASN | PRO | ||||
| 5 | VAL | LEU | LYS | ALA | PHE | TRP | ASN | SER | VAL | PRO | ||||
| 6 | LEU | LYS | GLN | ALA | THR | ALA | ALA | LEU | ARG | LYS | ||||
| 7 | ILE | LYS | ARG | THR | VAL | SER | ALA | LEU | MET | VAL | ||||
| 8 | GLY | LEU | GLN | LYS | ARG | GLY | LYS | ARG | ARG |
Samples:
sample_1: d16-TBEVC, [U-99% 13C; U-99% 15N], 0.4 mM; NaCl, none, 50 mM; sodium phosphate, none, 50 mM; glycerol, none, 5%
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.5, Bruker Biospin - collection, processing
CcpNmr Analysis v2.5.2, CCPN - chemical shift assignment, data analysis, peak picking
X-PLOR NIH v3.2, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
HADDOCK v2.2, Bonvin - processing
NMR spectrometers:
- Bruker AVANCE 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts