BMRB Entry 50513

Title:
Backbone chemical shift assignments for the Betacoronavirus SARS-CoV-2 non-structural protein Nsp9   PubMed: 33392924
Deposition date:
2020-10-15
Original release date:
2020-11-10
Authors:
Buchko, Garry
Citation:

Citation: Buchko, Garry; Zhou, Mowei; Craig, Justin; Van Voorhis, Wesley; Myler, Peter. "Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms - us) dynamics in the C-terminal helix at the dimer interface."  Biomol. NMR Assign. 15, 107-116 (2021).

Assembly members:

Assembly members:
entity_1, polymer, 135 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 SARS-CoV-2

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a-TEV

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a-TEV

Data sets:
Data typeCount
13C chemical shifts327
15N chemical shifts92
1H chemical shifts346

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 1 135 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYGLUASNLEUTYRPHEGLNGLY
3   HISMETASNASNGLULEUSERPROVALALA
4   LEUARGGLNMETSERCYSALAALAGLYTHR
5   THRGLNTHRALACYSTHRASPASPASNALA
6   LEUALATYRTYRASNTHRTHRLYSGLYGLY
7   ARGPHEVALLEUALALEULEUSERASPLEU
8   GLNASPLEULYSTRPALAARGPHEPROLYS
9   SERASPGLYTHRGLYTHRILETYRTHRGLU
10   LEUGLUPROPROCYSARGPHEVALTHRASP
11   THRPROLYSGLYPROLYSVALLYSTYRLEU
12   TYRPHEILELYSGLYLEUASNASNLEUASN
13   ARGGLYMETVALLEUGLYSERLEUALAALA
14   THRVALARGLEUGLN

Samples:

sample_1: Nsp9, [U-98% 13C; U-98% 15N; U-70% 2H], 0.5 mM; sodium chloride 100 mM; TRIS 20 mM; DTT 1 mM

sample_2: Nsp9, [U-98% % 15N], 0.5 mM; sodium chloride 100 mM; TRIS 20 mM; DTT 1 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 15N edited NOESYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D 13C-edited NOESY aliphsample_1isotropicsample_conditions_1
3D 15N-edited TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACB B-optimizedsample_1isotropicsample_conditions_1

Software:

SPARKY1.414 - data analysis

FELIX v2007 - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

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