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 50772

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50772

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: The 1H, 15N, and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the Middle East Respiratory Syndrome Coronavirus   PubMed: 33914244

Deposition date: 2021-02-17 Original release date: 2021-05-18

Authors: de Araujo, Talita; Barbosa, Glauce; Sanches, Karoline; Azevedo, Jessica; Cabral, Katia; Almeida, Marcius; Almeida, Fabio

Citation: de Araujo, Talita; Barbosa, Glauce; Sanches, Karoline; Azevedo, Jessica; Cabral, Katia; Almeida, Marcius; Almeida, Fabio. "The 1H, 15N, and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the Middle East Respiratory Syndrome Coronavirus"  Biomol. NMR Assignments 15, 341-345 (2021).

Assembly members:
entity_1, polymer, 136 residues, Formula weight is not available

Natural source:   Common Name: MERS-CoV   Taxonomy ID: 1335626   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betacoronavirus MERS-CoV

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b(+)

Entity Sequences (FASTA):
entity_1: GAAPNNTVSWYTGLTQHGKV PLTFPPGQGVPLNANSTPAQ NAGYWRRQDRKINTGNGIKQ LAPRWYFYYTGTGPEAALPF RAVKDGIVWVHEDGATDAPS TFGTRNPNNDSAIVTQFAPG TKLPKNFHIEGTGGNS

Data sets:
Data typeCount
13C chemical shifts520
15N chemical shifts131
1H chemical shifts800

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MERS N-NTD1

Entities:

Entity 1, MERS N-NTD 136 residues - Formula weight is not available

1   GLYALAALAPROASNASNTHRVALSERTRP
2   TYRTHRGLYLEUTHRGLNHISGLYLYSVAL
3   PROLEUTHRPHEPROPROGLYGLNGLYVAL
4   PROLEUASNALAASNSERTHRPROALAGLN
5   ASNALAGLYTYRTRPARGARGGLNASPARG
6   LYSILEASNTHRGLYASNGLYILELYSGLN
7   LEUALAPROARGTRPTYRPHETYRTYRTHR
8   GLYTHRGLYPROGLUALAALALEUPROPHE
9   ARGALAVALLYSASPGLYILEVALTRPVAL
10   HISGLUASPGLYALATHRASPALAPROSER
11   THRPHEGLYTHRARGASNPROASNASNASP
12   SERALAILEVALTHRGLNPHEALAPROGLY
13   THRLYSLEUPROLYSASNPHEHISILEGLU
14   GLYTHRGLYGLYASNSER

Samples:

sample_1: N-terminal domain of MERS N Protein, [U-100% 13C; U-100% 15N], 200 uM; sodium phosphate 20 mM; sodium chloride 50 mM; PMSF 0.5 mM; EDTA 3 mM; sodium azide 3 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

NMRbox - data analysis

TOPSPIN - collection

NMRPipe - processing

CcpNMR - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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