BMRB Entry 50557

Title:
SARS-CoV-2 nucleoprotein 175-263   PubMed: 33730325
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).

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

Experimental source:

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

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

Data sets:
Data typeCount
13C chemical shifts136
15N chemical shifts78
1H chemical shifts78

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N175-2631

Entities:

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

1   GLYARGARGMETGLYSERARGGLYGLYSER
2   GLNALASERSERARGSERSERSERARGSER
3   ARGASNSERSERARGASNSERTHRPROGLY
4   SERSERARGGLYTHRSERPROALAARGMET
5   ALAGLYASNGLYGLYASPALAALALEUALA
6   LEULEULEULEUASPARGLEUASNGLNLEU
7   GLUSERLYSMETSERGLYLYSGLYGLNGLN
8   GLNGLNGLYGLNTHRVALTHRLYSLYSSER
9   ALAALAGLUALASERLYSLYSPROARGGLN
10   LYSARGTHR

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_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