BMRB Entry 28135
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28135
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Intrinsically Disordered Domain of human ANP32A PubMed: 32694517
Deposition date: 2020-06-27 Original release date: 2021-12-20
Authors: Camacho Zarco, Aldo; Kalayil, Sissy; Maurin, Damien; Salvi, Nicola; Delaforge, Elise; Milles, Sigrid; Ringkj bing Jensen, Malene; Hart, Darren; Cusack, Stephen; Blackledge, Martin
Citation: Camacho-Zarco, Aldo; Kalayil, Sissy; Maurin, Damien; Salvi, Nicola; Delaforge, Elise; Milles, Sigrid; Ringkj bing 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).
Assembly members:
Instrinsically_disordered_domain_of_human_ANP32A, polymer, 110 residues, 12828.23 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: phIDD
Entity Sequences (FASTA):
Instrinsically_disordered_domain_of_human_ANP32A: GRQYLDGYDRDDKEAPDSDA
EGYVEGLDDEEEDEDEEEYD
EDAQVVEDEEDEDEEEEGEE
EDVSGEEEEDEEGYNDGEVD
DEEDEEEFGEEERGQKRKRE
PEDEGEDDDD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 152 |
| 15N chemical shifts | 76 |
| 1H chemical shifts | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hIDD | 1 |
Entities:
Entity 1, hIDD 110 residues - 12828.23 Da.
The peptide includes in the N-terminal (before residue 151) some residues that correspond to the folded domain of ANP32A.
| 1 | GLY | ARG | GLN | TYR | LEU | ASP | GLY | TYR | ASP | ARG | |
| 2 | ASP | ASP | LYS | GLU | ALA | PRO | ASP | SER | ASP | ALA | |
| 3 | GLU | GLY | TYR | VAL | GLU | GLY | LEU | ASP | ASP | GLU | |
| 4 | GLU | GLU | ASP | GLU | ASP | GLU | GLU | GLU | TYR | ASP | |
| 5 | GLU | ASP | ALA | GLN | VAL | VAL | GLU | ASP | GLU | GLU | |
| 6 | ASP | GLU | ASP | GLU | GLU | GLU | GLU | GLY | GLU | GLU | |
| 7 | GLU | ASP | VAL | SER | GLY | GLU | GLU | GLU | GLU | ASP | |
| 8 | GLU | GLU | GLY | TYR | ASN | ASP | GLY | GLU | VAL | ASP | |
| 9 | ASP | GLU | GLU | ASP | GLU | GLU | GLU | PHE | GLY | GLU | |
| 10 | GLU | GLU | ARG | GLY | GLN | LYS | ARG | LYS | ARG | GLU | |
| 11 | PRO | GLU | ASP | GLU | GLY | GLU | ASP | ASP | ASP | ASP |
Samples:
sample_1: Instrinsically disordered domain of human ANP32A, [U-99% 13C; U-99% 15N], 0.7 mM; D2O, [U-99% 2H], 10%; sodium chloride 200 mM; TRIS 50 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 293.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D iHNCA | 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 shifts
SPARKY: Backbone
or all simulated shifts