BMRB Entry 27991

Name: Assignment of 1H, 13C and 15N resonances of Influenza A virus (H1N1) Non structural protein 2 (NS2)
Published: 2021-07-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27991

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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:

Assignment of 1H, 13C and 15N resonances of Influenza A virus (H1N1) Non structural protein 2 (NS2)

Deposition date:

2019-07-30

Original release date:

2021-07-20

Authors:

Jaiswal, Nancy; Kumar, Dinesh

Citation:

Citation: Jaiswal, Nancy; Agarwal, Nipanshu; Poluri, Krishna Mohan; Kumar, Dinesh. "Effect of urea concentration on instant refolding of Nuclear Export Protein (NEP) from Influenza-A virus H1N1: A solution NMR based investigation" Int. J. Biol. Macromol. 165, 2508-2519 (2020).
PubMed: 33470198

Assembly members:

Assembly members:
H1N1-NS2, polymer, 119 residues, 14322 Da.

Natural source:

Natural source: Common Name: Influenza A Taxonomy ID: 11320 Superkingdom: Viruses Kingdom: not available Genus/species: Alphainfluenzavirus Influenza A

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H1N1-NS2: MDSNTMSSFQDILMRMSKMQ LGSSSEDLNGMVTRFESLKI YRDSLGETVMRMGDLHYLQS RNEKWREQLGQKFEEIRWLI EEMRHRLKPTENSFEQITFM QALQLLLEVEQEIRTFSFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	349
15N chemical shifts	118
1H chemical shifts	503

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H1N1-NS2	1

Entities:

Entity 1, H1N1-NS2 119 residues - 14322 Da.

protein has 6XHis tag with TEV cleavage site at N terminus

1

MET

ASP

SER

ASN

THR

MET

SER

PHE

GLN

2

ASP

ILE

LEU

MET

ARG

MET

SER

LYS

MET

GLN

3

LEU

GLY

SER

GLU

ASP

LEU

ASN

GLY

4

MET

VAL

THR

ARG

PHE

GLU

SER

LEU

LYS

ILE

5

TYR

ARG

ASP

SER

LEU

GLY

GLU

THR

VAL

MET

6

ARG

MET

GLY

ASP

LEU

HIS

TYR

LEU

GLN

SER

7

ARG

ASN

GLU

LYS

TRP

ARG

GLU

GLN

LEU

GLY

8

GLN

LYS

PHE

GLU

ILE

ARG

TRP

LEU

ILE

9

GLU

MET

ARG

HIS

ARG

LEU

LYS

PRO

THR

10

GLU

ASN

SER

PHE

GLU

GLN

ILE

THR

PHE

MET

11

GLN

ALA

LEU

GLN

LEU

GLU

VAL

GLU

12

GLN

GLU

ILE

ARG

THR

PHE

SER

PHE

GLN

Samples:

sample_1: H1N1-NS2, [U-99% 13C; U-99% 15N], 0.8 ± 0.2 mM; D2O, [U-100% 2H], 10%; H2O 90%; urea 9.7 M; sodium chloride 300 mM; sodium phosphate 50 mM

condition_1: pH*: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	condition_1
3D HNCA	sample_1	isotropic	condition_1
3D CBCA(CO)NH	sample_1	isotropic	condition_1
3D H(CCO)NH	sample_1	isotropic	condition_1
3D HNCACB	sample_1	isotropic	condition_1
3D HNCACO	sample_1	isotropic	condition_1
3D hNCAnH	sample_1	isotropic	condition_1
3D 1H-15N TOCSY	sample_1	isotropic	condition_1

Software:

CARA v1.9.1, Freely Available - chemical shift assignment, data analysis, structure solution

NMR spectrometers:

Bruker Avance 800 MHz

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