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 50771

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

Deposition date: 2021-02-17 Original release date: 2021-03-21

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

Citation: 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 ., .-..

Assembly members:
entity_1, polymer, 171 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 TKLPKNFHIEGTGGNSQSSS RASSVSRNSSRSSSQGSRSG NSTRGTSPGPS

Data sets:
Data typeCount
13C chemical shifts594
15N chemical shifts150
1H chemical shifts881

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MERS NTD-SR1

Entities:

Entity 1, MERS NTD-SR 171 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   GLYTHRGLYGLYASNSERGLNSERSERSER
15   ARGALASERSERVALSERARGASNSERSER
16   ARGSERSERSERGLNGLYSERARGSERGLY
17   ASNSERTHRARGGLYTHRSERPROGLYPRO
18   SER

Samples:

sample_1: N-terminal domain with SR rich region of MERS N Protein, [U-100% 13C; U-100% 15N], 200 uM; sodium phosphate 20 mM; PMSF 0.5 mM; sodium azide 3 mM; EDTA 3 mM; sodium chloride 50 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_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

Software:

NMRbox - data analysis

TOPSPIN - collection

NMRPipe - processing

CcpNMR - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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