BMRB Entry 50622

Title:
nsp9 viral protein
Deposition date:
2020-12-08
Original release date:
2021-05-28
Authors:
Dudas, Erika; Puglisi, Rita; Pastore, Annalisa
Citation:

Citation: Dudas, Erika; Puglisi, Rita; Korn, Sophie Marianne; Alfano, Caterina; Bellone, Maria Laura; Piaz, Fabrizio Dal; Kelly, Geoff; Monaca, Elisa; Schlundt, Andreas; Schwalbe, Harald; Pastore, Annalisa. "Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9."  Biomol. NMR Assign. 15, 235-241 (2021).
PubMed: 33755914

Assembly members:

Assembly members:
entity_1, polymer, 117 residues, Formula weight is not available

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

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts80
1H chemical shifts80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nsp9, chain 11
2nsp9, chain 21

Entities:

Entity 1, nsp9, chain 1 117 residues - Formula weight is not available

GAMGNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQ

1   GLYALAMETGLYASNASNGLULEUSERPRO
2   VALALALEUARGGLNMETSERCYSALAALA
3   GLYTHRTHRGLNTHRALACYSTHRASPASP
4   ASNALALEUALATYRTYRASNTHRTHRLYS
5   GLYGLYARGPHEVALLEUALALEULEUSER
6   ASPLEUGLNASPLEULYSTRPALAARGPHE
7   PROLYSSERASPGLYTHRGLYTHRILETYR
8   THRGLULEUGLUPROPROCYSARGPHEVAL
9   THRASPTHRPROLYSGLYPROLYSVALLYS
10   TYRLEUTYRPHEILELYSGLYLEUASNASN
11   LEUASNARGGLYMETVALLEUGLYSERLEU
12   ALAALATHRVALARGLEUGLN

Samples:

sample_1: SARS-CoV-2 nsp9 A, [U-99% 13C; U-99% 15N], 180 uM; sodium phosphate buffer 25 mM; NaCl 150 mM; TCEP 2 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; 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)CAsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

CcpNMR, Topspin (Bruker), NMRPipe, SMILE - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz

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