BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50620

Title: 1H, 13C and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)   PubMed: 33770349

Deposition date: 2020-12-07 Original release date: 2021-06-01

Authors: Wang, Ying; Kirkpatrick, John; Carlomagno, Teresa

Citation: Wang, Ying; Kirkpatrick, John; Zur Lage, Susanne; Korn, Sophie; Neissner, Konstantin; Schwalbe, Harald; Schlundt, Andreas; Carlomagno, Teresa. "1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)"  Biomol. NMR Assignments ., .-. (2021).

Assembly members:
entity_1, polymer, 182 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: pETM11

Entity Sequences (FASTA):
entity_1: GAMESLVPGFNEKTHVQLSL PVLQVRDVLVRGFGDSVEEV LSEARQHLKDGTCGLVEVEK GVLPQLEQPYVFIKRSDART APHGHVMVELVAELEGIQYG RSGETLGVLVPHVGEIPVAY RKVLLRKNGNKGAGGHSYGA DLKSFDLGDELGTDPYEDFQ ENWNTKHSSGVTRELMRELN GG

Data sets:
Data typeCount
13C chemical shifts505
15N chemical shifts165
1H chemical shifts165

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nsp11

Entities:

Entity 1, Nsp1 182 residues - Formula weight is not available

The first two residues (GA) in the protein construct used are cloning artifacts. Therefore, the appropriate residue numbering has the first residue (G) designated as residue-number '-1', so that the third residue has residue-number '1'.

1   GLYALAMETGLUSERLEUVALPROGLYPHE
2   ASNGLULYSTHRHISVALGLNLEUSERLEU
3   PROVALLEUGLNVALARGASPVALLEUVAL
4   ARGGLYPHEGLYASPSERVALGLUGLUVAL
5   LEUSERGLUALAARGGLNHISLEULYSASP
6   GLYTHRCYSGLYLEUVALGLUVALGLULYS
7   GLYVALLEUPROGLNLEUGLUGLNPROTYR
8   VALPHEILELYSARGSERASPALAARGTHR
9   ALAPROHISGLYHISVALMETVALGLULEU
10   VALALAGLULEUGLUGLYILEGLNTYRGLY
11   ARGSERGLYGLUTHRLEUGLYVALLEUVAL
12   PROHISVALGLYGLUILEPROVALALATYR
13   ARGLYSVALLEULEUARGLYSASNGLYASN
14   LYSGLYALAGLYGLYHISSERTYRGLYALA
15   ASPLEULYSSERPHEASPLEUGLYASPGLU
16   LEUGLYTHRASPPROTYRGLUASPPHEGLN
17   GLUASNTRPASNTHRLYSHISSERSERGLY
18   VALTHRARGGLULEUMETARGGLULEUASN
19   GLYGLY

Samples:

sample_1: Nsp1, [U-13C; U-15N], 350 uM; sodium phosphate 50 mM; sodium chloride 200 mM; DTT 2 mM; EDTA 2 mM; sodium azide 0.01%; DSS 0.001%; D2O, [U-2H], 10%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2 - collection

NMRPipe v10.1 - processing

CcpNMR v2.4 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz
  • Bruker AVANCE III HD 850 MHz

Related Database Links:

NCBI YP_009725297.1

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