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 34511

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34511
MolProbity Validation Chart

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

Title: The N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoprotein   PubMed: 33264373

Deposition date: 2020-03-31 Original release date: 2020-04-06

Authors: Veverka, V.; Boura, E.

Citation: Dinesh, Dhurvas Chandrasekaran; Chalupska, Dominika; Silhan, Jan; Koutna, Eliska; Nencka, Radim; Veverka, Vaclav; Boura, Evzen. "Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein"  PLoS Pathog. 16, e1009100-e1009100 (2020).

Assembly members:
entity_1, polymer, 140 residues, 15129.853 Da.

Natural source:   Common Name: COVID-19 virus   Taxonomy ID: 2697049   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betacoronavirus COVID-19

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

Entity Sequences (FASTA):
entity_1: GAMGLPNNTASWFTALTQHG KEDLKFPRGQGVPINTNSSP DDQIGYYRRATRRIRGGDGK MKDLSPRWYFYYLGTGPEAG LPYGANKDGIIWVATEGALN TPKDHIGTRNPANNAAIVLQ LPQGTTLPKGFYAEGSRGGS

Data sets:
Data typeCount
13C chemical shifts574
15N chemical shifts151
1H chemical shifts940

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 140 residues - 15129.853 Da.

1   GLYALAMETGLYLEUPROASNASNTHRALA
2   SERTRPPHETHRALALEUTHRGLNHISGLY
3   LYSGLUASPLEULYSPHEPROARGGLYGLN
4   GLYVALPROILEASNTHRASNSERSERPRO
5   ASPASPGLNILEGLYTYRTYRARGARGALA
6   THRARGARGILEARGGLYGLYASPGLYLYS
7   METLYSASPLEUSERPROARGTRPTYRPHE
8   TYRTYRLEUGLYTHRGLYPROGLUALAGLY
9   LEUPROTYRGLYALAASNLYSASPGLYILE
10   ILETRPVALALATHRGLUGLYALALEUASN
11   THRPROLYSASPHISILEGLYTHRARGASN
12   PROALAASNASNALAALAILEVALLEUGLN
13   LEUPROGLNGLYTHRTHRLEUPROLYSGLY
14   PHETYRALAGLUGLYSERARGGLYGLYSER

Samples:

sample_1: N-NTD, [U-13C; U-15N], 1 mM; sodium phosphate 25 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 125 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - data analysis

Sparky, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, YASARA - structure calculation

NMR spectrometers:

  • Bruker AVANCE 850 MHz

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