BMRB Entry 28135

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Intrinsically Disordered Domain of human ANP32A
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:

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).
PubMed: 32694517

Assembly members:

Assembly members:
Instrinsically_disordered_domain_of_human_ANP32A, polymer, 110 residues, 12828.23 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: phIDD

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts76
1H chemical shifts76

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1hIDD1

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   GLYARGGLNTYRLEUASPGLYTYRASPARG
2   ASPASPLYSGLUALAPROASPSERASPALA
3   GLUGLYTYRVALGLUGLYLEUASPASPGLU
4   GLUGLUASPGLUASPGLUGLUGLUTYRASP
5   GLUASPALAGLNVALVALGLUASPGLUGLU
6   ASPGLUASPGLUGLUGLUGLUGLYGLUGLU
7   GLUASPVALSERGLYGLUGLUGLUGLUASP
8   GLUGLUGLYTYRASNASPGLYGLUVALASP
9   ASPGLUGLUASPGLUGLUGLUPHEGLYGLU
10   GLUGLUARGGLYGLNLYSARGLYSARGGLU
11   PROGLUASPGLUGLYGLUASPASPASPASP

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D iHNCAsample_1isotropicsample_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