BMRB Entry 28134
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28134
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Camacho-Zarco, Aldo; Kalayil, Sissy; Maurin, Damien; Salvi, Nicola; Delaforge, Elise; Milles, Sigrid; Ringkjobing Jensen, Malene; Hart, Darren; Cusack, Stephen; Blackledge, Martin. "Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A" Nat. Commun. 11, 3656-3656 (2020).
PubMed: 32694517
Assembly members:
Instrinsically_disordered_domain_of_chicken_ANP32A, polymer, 8 residues, 32227.14 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pAvIDD
Entity Sequences (FASTA):
Instrinsically_disordered_domain_of_chicken_ANP32A: GMDMKKRIHLELRNRTPSDV
KELVLDNCRSYEGKIEGLTD
EFEELEFLSTINVGLASVAN
LPKLNKLKKLELSDNRVSGG
LEVLAEKCPNLTHLNLSGNK
IKDLGTIEPLKKLENLKSLD
LFNCEVTNLNDYRENVFKLL
PQLTYLDGYDRDDKEAPDSD
AEGYVEGLDDEEEDEDVLSL
VKDRDDKEAPDSDAEGYVEG
LDDEEEDEDEEEYDDDAQVV
EDEEDEEEEEEGEEEDVSGE
EEEDEEGYNDGDVDDDEDEE
EPDEERGQKRKREPEDEGDE
DD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 124 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 66 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | avIDD | 1 |
Entities:
Entity 1, avIDD 8 residues - 32227.14 Da.
The backbone of the intrinsically disordered domain of chicken ANP32A (avIDD), starting at residue 157, was assigned. However the construct used for assignment includes also the folded domain. The construct starts with a Gly, which is derived from the TEV cleavage site. Numbering starts with the second residue (residue 1), a Met already found in chicken (Gallus gallus) ANP32A.
| 1 | GLY | MET | ASP | MET | LYS | LYS | ARG | ILE | HIS | LEU | ||||
| 2 | GLU | LEU | ARG | ASN | ARG | THR | PRO | SER | ASP | VAL | ||||
| 3 | LYS | GLU | LEU | VAL | LEU | ASP | ASN | CYS | ARG | SER | ||||
| 4 | TYR | GLU | GLY | LYS | ILE | GLU | GLY | LEU | THR | ASP | ||||
| 5 | GLU | PHE | GLU | GLU | LEU | GLU | PHE | LEU | SER | THR | ||||
| 6 | ILE | ASN | VAL | GLY | LEU | ALA | SER | VAL | ALA | ASN | ||||
| 7 | LEU | PRO | LYS | LEU | ASN | LYS | LEU | LYS | LYS | LEU | ||||
| 8 | GLU | LEU | SER | ASP | ASN | ARG | VAL | SER | GLY | GLY | ||||
| 9 | LEU | GLU | VAL | LEU | ALA | GLU | LYS | CYS | PRO | ASN | ||||
| 10 | LEU | THR | HIS | LEU | ASN | LEU | SER | GLY | ASN | LYS | ||||
| 11 | ILE | LYS | ASP | LEU | GLY | THR | ILE | GLU | PRO | LEU | ||||
| 12 | LYS | LYS | LEU | GLU | ASN | LEU | LYS | SER | LEU | ASP | ||||
| 13 | LEU | PHE | ASN | CYS | GLU | VAL | THR | ASN | LEU | ASN | ||||
| 14 | ASP | TYR | ARG | GLU | ASN | VAL | PHE | LYS | LEU | LEU | ||||
| 15 | PRO | GLN | LEU | THR | TYR | LEU | ASP | GLY | TYR | ASP | ||||
| 16 | ARG | ASP | ASP | LYS | GLU | ALA | PRO | ASP | SER | ASP | ||||
| 17 | ALA | GLU | GLY | TYR | VAL | GLU | GLY | LEU | ASP | ASP | ||||
| 18 | GLU | GLU | GLU | ASP | GLU | ASP | VAL | LEU | SER | LEU | ||||
| 19 | VAL | LYS | ASP | ARG | ASP | ASP | LYS | GLU | ALA | PRO | ||||
| 20 | ASP | SER | ASP | ALA | GLU | GLY | TYR | VAL | GLU | GLY | ||||
| 21 | LEU | ASP | ASP | GLU | GLU | GLU | ASP | GLU | ASP | GLU | ||||
| 22 | GLU | GLU | TYR | ASP | ASP | ASP | ALA | GLN | VAL | VAL | ||||
| 23 | GLU | ASP | GLU | GLU | ASP | GLU | GLU | GLU | GLU | GLU | ||||
| 24 | GLU | GLY | GLU | GLU | GLU | ASP | VAL | SER | GLY | GLU | ||||
| 25 | GLU | GLU | GLU | ASP | GLU | GLU | GLY | TYR | ASN | ASP | ||||
| 26 | GLY | ASP | VAL | ASP | ASP | ASP | GLU | ASP | GLU | GLU | ||||
| 27 | GLU | PRO | ASP | GLU | GLU | ARG | GLY | GLN | LYS | ARG | ||||
| 28 | LYS | ARG | GLU | PRO | GLU | ASP | GLU | GLY | ASP | GLU | ||||
| 29 | ASP | ASP |
Samples:
sample_1: ANP32A, [U-99% 13C; U-99% 15N], 0.7 mM; Tris-HCl 50 mM; NaCl 200 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D iHNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D iHNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks