BMRB Entry 50518

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50518

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

Title:
1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein
Deposition date:
2020-10-19
Original release date:
2020-12-01
Authors:
Korn, Sophie; Lambertz, Roderick; Furtig, Boris; Hengesbach, Martin; Lohr, Frank; Richter, Christian; Schwalbe, Harald; Weigand, Julia; Wohnert, Jens; Schlundt, Andreas
Citation:

Citation: Korn, Sophie; Lambertz, Roderick; Furtig, Boris; Hengesbach, Martin; Lohr, Frank; Richter, Christian; Schwalbe, Harald; Weigand, Julia; Wohnert, Jens; Schlundt, Andreas. "1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein"  Biomol. NMR Assignments 15, 129-135 (2021).
PubMed: 33270159

Assembly members:

Assembly members:
entity_1, polymer, 122 residues, 27112.64 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pKM263

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGTKKSAAEASKKPRQKR TATKAYNVTQAFGRRGPEQT QGNFGDQELIRQGTDYKHWP QIAQFAPSASAFFGMSRIGM EVTPSGTWLTYTGAIKLDDK DPNFKDQVILLNKHIDAYKT FP

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts112
1H chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nprot CTD, chain 11
2Nprot CTD, chain 21

Entities:

Entity 1, Nprot CTD, chain 1 122 residues - 27112.64 Da.

The sequence -3 - 118 contains residues GAMG as leftover from TEV cut. Residues Thr1 to Pro118 correspond to the natural sequence 247-364 within the natural Nucleocapsid protein.

1   GLYALAMETGLYTHRLYSLYSSERALAALA
2   GLUALASERLYSLYSPROARGGLNLYSARG
3   THRALATHRLYSALATYRASNVALTHRGLN
4   ALAPHEGLYARGARGGLYPROGLUGLNTHR
5   GLNGLYASNPHEGLYASPGLNGLULEUILE
6   ARGGLNGLYTHRASPTYRLYSHISTRPPRO
7   GLNILEALAGLNPHEALAPROSERALASER
8   ALAPHEPHEGLYMETSERARGILEGLYMET
9   GLUVALTHRPROSERGLYTHRTRPLEUTHR
10   TYRTHRGLYALAILELYSLEUASPASPLYS
11   ASPPROASNPHELYSASPGLNVALILELEU
12   LEUASNLYSHISILEASPALATYRLYSTHR
13   PHEPRO

Samples:

sample_1: N protein C-terminal dimerization domain, [U-100% 15N], 300 uM; sodium phosphate 25 mM; sodium chloride 50 mM; EDTA 0.5 mM; sodium azide 0.02%; DSS 0.3 mM

sample_2: N protein C-terminal dimerization domain, [U-13C; U-100% 15N], 375 uM; sodium phosphate 25 mM; sodium chloride 50 mM; EDTA 0.5 mM; sodium azide 0.02%; DSS 0.3 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3/4 - collection, processing

CcpNMR v2.4 - chemical shift assignment

NMRFAM-SPARKY - chemical shift assignment, data analysis

LOGS - data archiving

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 950 MHz

Related Database Links:

NCBI YP_009725299.1

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