BMRB Entry 28135

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Intrinsically Disordered Domain of human ANP32A
Published: 2021-12-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28135

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
Instrinsically_disordered_domain_of_human_ANP32A: GRQYLDGYDRDDKEAPDSDA EGYVEGLDDEEEDEDEEEYD EDAQVVEDEEDEDEEEEGEE EDVSGEEEEDEEGYNDGEVD DEEDEEEFGEEERGQKRKRE PEDEGEDDDD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	152
15N chemical shifts	76
1H chemical shifts	76

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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 peaks
SPARKY: Backbone or all simulated peaks

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

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

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