BMRB Entry 50469
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50469
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Title: A28 PubMed: 33398629
Deposition date: 2020-09-14 Original release date: 2021-04-13
Authors: Wu, Danni
Citation: Wu, Danni; Lou, Yuan-Chao; Chang, Wen; Tzou, Der-Lii. "NMR assignments of vaccinia virus protein A28: an entry-fusion complex component" Biomol. NMR Assignments 15, 117-120 (2021).
Assembly members:
entity_1, polymer, 109 residues, Formula weight is not available
Natural source: Common Name: Vaccinia virus Taxonomy ID: 10245 Superkingdom: Viruses Kingdom: not available Genus/species: Orthopoxvirus Vaccinia virus
Experimental source: Production method: purified from the natural source
Entity Sequences (FASTA):
entity_1: ATHAAFEYSKSIGGTPALDR
RVQDVNDTISDVKQKWRCVV
YPGNGFVSASIFGFQAEVGP
NNTRSIRKFNTMQQCIDFTF
SDVININIYNPCVVPNINNA
ECQFLKSVL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 471 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 732 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | A28 | 1 |
Entities:
Entity 1, A28 109 residues - Formula weight is not available
| 1 | ALA | THR | HIS | ALA | ALA | PHE | GLU | TYR | SER | LYS | ||||
| 2 | SER | ILE | GLY | GLY | THR | PRO | ALA | LEU | ASP | ARG | ||||
| 3 | ARG | VAL | GLN | ASP | VAL | ASN | ASP | THR | ILE | SER | ||||
| 4 | ASP | VAL | LYS | GLN | LYS | TRP | ARG | CYS | VAL | VAL | ||||
| 5 | TYR | PRO | GLY | ASN | GLY | PHE | VAL | SER | ALA | SER | ||||
| 6 | ILE | PHE | GLY | PHE | GLN | ALA | GLU | VAL | GLY | PRO | ||||
| 7 | ASN | ASN | THR | ARG | SER | ILE | ARG | LYS | PHE | ASN | ||||
| 8 | THR | MET | GLN | GLN | CYS | ILE | ASP | PHE | THR | PHE | ||||
| 9 | SER | ASP | VAL | ILE | ASN | ILE | ASN | ILE | TYR | ASN | ||||
| 10 | PRO | CYS | VAL | VAL | PRO | ASN | ILE | ASN | ASN | ALA | ||||
| 11 | GLU | CYS | GLN | PHE | LEU | LYS | SER | VAL | LEU |
Samples:
sample_1: A28, [U-100% 13C; U-100% 15N], 1 mM
sample_conditions_1: pH: 6.5; 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 CBCANH | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts