BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 50558

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50558

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Title: 1H, 13C and 15N Backbone Chemical Shift Assignments of the N-terminal and Central Intrinsically Disordered Domains of SARS-CoV-2 Nucleoprotein   PubMed: 33730325

Deposition date: 2020-11-10 Original release date: 2021-04-07

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

Citation: Guseva, Serafima; Marino Perez, Laura; Camacho-Zarco, Aldo; Mamigonian-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:
entity_1, polymer, 263 residues, Formula weight is not available

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

Entity Sequences (FASTA):
entity_1: MSDNGPQNQRNAPRITFGGP SDSTGSNQNGERSGARSKQR RPQGLPNNTASWFTALTQHG KEDLKFPRGQGVPINTNSSP DDQIGYYRRATRRIRGGDGK MKDLSPRWYFYYLGTGPEAG LPYGANKDGIIWVATEGALN TPKDHIGTRNPANNAAIVLQ LPQGTTLPKGFYAEGSRGGS QASSRSSSRSRNSSRNSTPG SSRGTSPARMAGNGGDAALA LLLLDRLNQLESKMSGKGQQ QQGQTVTKKSAAEASKKPRQ KRT

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts94
1H chemical shifts94

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SARS-CoV-2 N123 Nucleoprotein1

Entities:

Entity 1, SARS-CoV-2 N123 Nucleoprotein 263 residues - Formula weight is not available

1   METSERASPASNGLYPROGLNASNGLNARG
2   ASNALAPROARGILETHRPHEGLYGLYPRO
3   SERASPSERTHRGLYSERASNGLNASNGLY
4   GLUARGSERGLYALAARGSERLYSGLNARG
5   ARGPROGLNGLYLEUPROASNASNTHRALA
6   SERTRPPHETHRALALEUTHRGLNHISGLY
7   LYSGLUASPLEULYSPHEPROARGGLYGLN
8   GLYVALPROILEASNTHRASNSERSERPRO
9   ASPASPGLNILEGLYTYRTYRARGARGALA
10   THRARGARGILEARGGLYGLYASPGLYLYS
11   METLYSASPLEUSERPROARGTRPTYRPHE
12   TYRTYRLEUGLYTHRGLYPROGLUALAGLY
13   LEUPROTYRGLYALAASNLYSASPGLYILE
14   ILETRPVALALATHRGLUGLYALALEUASN
15   THRPROLYSASPHISILEGLYTHRARGASN
16   PROALAASNASNALAALAILEVALLEUGLN
17   LEUPROGLNGLYTHRTHRLEUPROLYSGLY
18   PHETYRALAGLUGLYSERARGGLYGLYSER
19   GLNALASERSERARGSERSERSERARGSER
20   ARGASNSERSERARGASNSERTHRPROGLY
21   SERSERARGGLYTHRSERPROALAARGMET
22   ALAGLYASNGLYGLYASPALAALALEUALA
23   LEULEULEULEUASPARGLEUASNGLNLEU
24   GLUSERLYSMETSERGLYLYSGLYGLNGLN
25   GLNGLNGLYGLNTHRVALTHRLYSLYSSER
26   ALAALAGLUALASERLYSLYSPROARGGLN
27   LYSARGTHR

Samples:

sample_1: SARS-CoV-2 Nucleoprotein, [U-98% 13C; U-98% 15N], 0.9 mM; Na-Phosphate 50 mM; NaCl 250 mM; DTT 2 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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