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 50618

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50618

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Title: 1H 13C 15N assignment of IDR2-domain (176-248) of Nucleocapsid Protein of SARS-CoV 2 in the 1-248 construct   PubMed: 33660218

Deposition date: 2020-12-04 Original release date: 2021-03-11

Authors: Schiavina, Marco; Pontoriero, Letizia; Felli, Isabella Caterina; Pierattelli, Roberta

Citation: Schiavina, Marco; Pontoriero, Letizia; Uversky, Vladimir; Felli, Isabella Caterina; Pierattelli, Roberta. "The highly flexible, disordered regions of the SARS-CoV 2 Nucleocapsid protein within the 1-248 residue construct: sequence specific resonance assignments through NMR"  Biomol. NMR Assignments 15, 219-227 (2021).

Assembly members:
entity_1, polymer, 248 residues, 26500 Da.

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: pET29b(+)

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

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts64
1H chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SR-rich Domain1

Entities:

Entity 1, SR-rich Domain 248 residues - 26500 Da.

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   GLNGLNGLYGLNTHRVALTHRLYS

Samples:

sample_1: Nucleocapsid protein of SARS-CoV 2: 1-248 construct, [U-100% 13C; U-100% 15N], 300 uM; sodium chloride 450 mM; TRIS 25 mM; sodium azide 0.02 % v/v; D2O, [U-100% 2H], 5 % v/v

sample_2: Nucleocapsid protein of SARS-CoV 2: 1-248 construct, [U-100% 13C; U-100% 15N], 300 uM; sodium chloride 450 mM; TRIS 25 mM; sodium azide 0.02 % v/v; D2O, [U-100% 2H], 5 % v/v

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N BEST TROSYsample_1isotropicsample_conditions_1
2D 13C-15N CONsample_2isotropicsample_conditions_1
3D 1H BT-HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H BT-HNCACBsample_1isotropicsample_conditions_1
3D 1H HNCOsample_1isotropicsample_conditions_1
3D 1H HN(CA)COsample_1isotropicsample_conditions_1
3D 13C (H)CBCACONsample_2isotropicsample_conditions_1
3D 13C (H)CBCANCOsample_2isotropicsample_conditions_1
2D 13C (H)CACOsample_2isotropicsample_conditions_1
2D 13C (H)CBCACOsample_2isotropicsample_conditions_1

Software:

XEASY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz
  • Bruker AVANCE NEO 1200 MHz

Related Database Links:

UNP P0DTC9
AlphaFold P0DTC9

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