BMRB Entry 50557

Name: SARS-CoV-2 nucleoprotein 175-263
Published: 2021-04-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50557

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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:

SARS-CoV-2 nucleoprotein 175-263

Deposition date:

2020-11-10

Original release date:

2021-04-07

Authors:

Guseva, Serafima; Marino, Laura; Camacho-Zarco, Aldo; Bessa, Luiza; Salvi, Nicola; Malki, Anas; Maurin, Damien; Blackledge, Martin

Citation:

Citation: Guseva, Serafima; Marino, Laura; Camacho-Zarco, Aldo; Bessa, Luiza; Salvi, Nicola; Malki, Anas; Maurin, Damien; Blackledge, Martin. "1H, 13C and 15N Backbone Chemical Shift Assignments of the N-terminal and Central Intrinsically Disordered Domains of SARS-CoV-2 Nucleoprotein" Biomol. NMR Assign. 15, 255-260 (2021).
PubMed: 33730325

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, Formula weight is not available

Natural source:

Natural source: Common Name: SARS-CoV-2 Taxonomy ID: 2697049 Superkingdom: Viruses Kingdom: not available Genus/species: Betacoronavirus HCoV-SARS

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GRRMGSRGGSQASSRSSSRS RNSSRNSTPGSSRGTSPARM AGNGGDAALALLLLDRLNQL ESKMSGKGQQQQGQTVTKKS AAEASKKPRQKRT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	136
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N175-263	1

Entities:

Entity 1, N175-263 93 residues - Formula weight is not available

1

GLY

ARG

MET

GLY

SER

ARG

GLY

SER

2

GLN

ALA

SER

ARG

SER

ARG

SER

3

ARG

ASN

SER

ARG

ASN

SER

THR

PRO

GLY

4

SER

ARG

GLY

THR

SER

PRO

ALA

ARG

MET

5

ALA

GLY

ASN

GLY

ASP

ALA

LEU

ALA

6

LEU

ASP

ARG

LEU

ASN

GLN

LEU

7

GLU

SER

LYS

MET

SER

GLY

LYS

GLY

GLN

8

GLN

GLY

GLN

THR

VAL

THR

LYS

SER

9

ALA

GLU

ALA

SER

LYS

PRO

ARG

GLN

10

LYS

ARG

THR

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 600 uM; Na-Phosphate 50 mM; NaCl 250 mM; DTT 2 mM

sample_2: protein, [U-100% 13C; U-100% 15N; U-80% 2H], 300 uM; Na-Phosphate 50 mM; NaCl 250 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 6; pressure: 1 atm; temperature: 298.2 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.7 - collection

NMRPipe - processing

SPARKY v3.19 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz

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