Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50469
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 33398629
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
Data type | Count |
13C chemical shifts | 471 |
15N chemical shifts | 116 |
1H chemical shifts | 732 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | A28 | 1 |
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 |
sample_1: A28, [U-100% 13C; U-100% 15N], 1 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
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 |
NMRView - chemical shift assignment, data analysis
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks