BMRB Entry 28134

Title:
Backbone 1H, 13C, 15N chemical shift assignment for the intrinsically disordered domain of chicken 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; 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:

Assembly members:
Instrinsically_disordered_domain_of_chicken_ANP32A, polymer, 8 residues, 32227.14 Da.

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts124
15N chemical shifts66
1H chemical shifts66

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1avIDD1

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   GLYMETASPMETLYSLYSARGILEHISLEU
2   GLULEUARGASNARGTHRPROSERASPVAL
3   LYSGLULEUVALLEUASPASNCYSARGSER
4   TYRGLUGLYLYSILEGLUGLYLEUTHRASP
5   GLUPHEGLUGLULEUGLUPHELEUSERTHR
6   ILEASNVALGLYLEUALASERVALALAASN
7   LEUPROLYSLEUASNLYSLEULYSLYSLEU
8   GLULEUSERASPASNARGVALSERGLYGLY
9   LEUGLUVALLEUALAGLULYSCYSPROASN
10   LEUTHRHISLEUASNLEUSERGLYASNLYS
11   ILELYSASPLEUGLYTHRILEGLUPROLEU
12   LYSLYSLEUGLUASNLEULYSSERLEUASP
13   LEUPHEASNCYSGLUVALTHRASNLEUASN
14   ASPTYRARGGLUASNVALPHELYSLEULEU
15   PROGLNLEUTHRTYRLEUASPGLYTYRASP
16   ARGASPASPLYSGLUALAPROASPSERASP
17   ALAGLUGLYTYRVALGLUGLYLEUASPASP
18   GLUGLUGLUASPGLUASPVALLEUSERLEU
19   VALLYSASPARGASPASPLYSGLUALAPRO
20   ASPSERASPALAGLUGLYTYRVALGLUGLY
21   LEUASPASPGLUGLUGLUASPGLUASPGLU
22   GLUGLUTYRASPASPASPALAGLNVALVAL
23   GLUASPGLUGLUASPGLUGLUGLUGLUGLU
24   GLUGLYGLUGLUGLUASPVALSERGLYGLU
25   GLUGLUGLUASPGLUGLUGLYTYRASNASP
26   GLYASPVALASPASPASPGLUASPGLUGLU
27   GLUPROASPGLUGLUARGGLYGLNLYSARG
28   LYSARGGLUPROGLUASPGLUGLYASPGLU
29   ASPASP

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D iHNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D iHNCACBsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1

Software:

SPARKY v3, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

UNP A0A1D5P3M1
AlphaFold A0A1D5P3M1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks