BMRB Entry 27925
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27925
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Sterbova, Petra; Wu, Danny; Lou, Yuan-Chao; Wang, Chun-Hsiung; Chang, Wei-Hau; Tzou, Der-Lii. "1H, 13C, and 15N resonance assignments of the capsid protrusion domain of dragon grouper nervous necrosis virus" Biomol. NMR Assignments 14, 63-66 (2020).
PubMed: 31848940
Assembly members:
Protrusion_domain, polymer, 125 residues, 13809.3 Da.
Natural source: Common Name: Dragon grouper nervous necrosis virus Taxonomy ID: 292633 Superkingdom: virus Kingdom: not available Genus/species: betanodavirus not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETDuet
Entity Sequences (FASTA):
Protrusion_domain: TPEETTAPIMTQGSLYNDSL
STNDFKSILLGSTPLDIAPD
GAVFQLDRPLSIDYSLGTGD
VDRAVYWHLKKFAGNAGTPA
GWFRWGIWDNFNKTFTDGVA
YYSDEQPRQILLPVGTVCTR
VDSEN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 552 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 843 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Protrusio domain monomer | 1 |
Entities:
Entity 1, Protrusio domain monomer 125 residues - 13809.3 Da.
This is the protrusion domain of Dragon grouper nervous necrosis virus coat protein
| 1 | THR | PRO | GLU | GLU | THR | THR | ALA | PRO | ILE | MET | ||||
| 2 | THR | GLN | GLY | SER | LEU | TYR | ASN | ASP | SER | LEU | ||||
| 3 | SER | THR | ASN | ASP | PHE | LYS | SER | ILE | LEU | LEU | ||||
| 4 | GLY | SER | THR | PRO | LEU | ASP | ILE | ALA | PRO | ASP | ||||
| 5 | GLY | ALA | VAL | PHE | GLN | LEU | ASP | ARG | PRO | LEU | ||||
| 6 | SER | ILE | ASP | TYR | SER | LEU | GLY | THR | GLY | ASP | ||||
| 7 | VAL | ASP | ARG | ALA | VAL | TYR | TRP | HIS | LEU | LYS | ||||
| 8 | LYS | PHE | ALA | GLY | ASN | ALA | GLY | THR | PRO | ALA | ||||
| 9 | GLY | TRP | PHE | ARG | TRP | GLY | ILE | TRP | ASP | ASN | ||||
| 10 | PHE | ASN | LYS | THR | PHE | THR | ASP | GLY | VAL | ALA | ||||
| 11 | TYR | TYR | SER | ASP | GLU | GLN | PRO | ARG | GLN | ILE | ||||
| 12 | LEU | LEU | PRO | VAL | GLY | THR | VAL | CYS | THR | ARG | ||||
| 13 | VAL | ASP | SER | GLU | ASN |
Samples:
sample_1: Protrusion Domain, [U15N; U13C], 1.2 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(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 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks