BMRB Entry 50392

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50392

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Title:
1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10
Deposition date:
2020-07-16
Original release date:
2020-09-09
Authors:
Kubatova, Nina; Schwalbe, Harald; Richter, Christian
Citation:

Citation: Kubatova, N.; Qureshi, N.; Altincekic, N.; Abele, R.; Bains, J.; Ceylan, B.; Ferner, J.; Fuks, C.; Hargittay, B.; Hutchison, M.; de Jesus, V.; Kutz, F.; Wirtz Martin, M.; Meiser, N.; Linhard, V.; Pyper, D.; Trucks, S.; Furtig, B.; Hengesbach, M.; Lohr, F.; Richter, C.; Saxena, K.; Schlundt, A.; Schwalbe, H.; Sreeramulu, S.; Wacker, A.; Weigand, J.; Wirmer-Bartoschek, J.; Wohnert, J.. "1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10"  Biomol. NMR Assign. 15, 65-71 (2021).
PubMed: 33159807

Assembly members:

Assembly members:
entity_1, polymer, 151 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: pET21b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSDKIHHHHHHAGNATEVP ANSTVLSFCAFAVDAAKAYK DYLASGGQPITNCVKMLCTH TGTGQAITVTPEANMDQESF GGASCCLYCRCHIDHPNPKG FCDLKGKYVQIPTTCANDPV GFTLKNTVCTVCGMWKGYGC SCDQLREPMLQ

Data sets:
Data typeCount
13C chemical shifts409
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nsp101

Entities:

Entity 1, Nsp10 151 residues - Formula weight is not available

MGSDKIHHHHHH = His-tag for purification

1   METGLYSERASPLYSILEHISHISHISHIS
2   HISHISALAGLYASNALATHRGLUVALPRO
3   ALAASNSERTHRVALLEUSERPHECYSALA
4   PHEALAVALASPALAALALYSALATYRLYS
5   ASPTYRLEUALASERGLYGLYGLNPROILE
6   THRASNCYSVALLYSMETLEUCYSTHRHIS
7   THRGLYTHRGLYGLNALAILETHRVALTHR
8   PROGLUALAASNMETASPGLNGLUSERPHE
9   GLYGLYALASERCYSCYSLEUTYRCYSARG
10   CYSHISILEASPHISPROASNPROLYSGLY
11   PHECYSASPLEULYSGLYLYSTYRVALGLN
12   ILEPROTHRTHRCYSALAASNASPPROVAL
13   GLYPHETHRLEULYSASNTHRVALCYSTHR
14   VALCYSGLYMETTRPLYSGLYTYRGLYCYS
15   SERCYSASPGLNLEUARGGLUPROMETLEU
16   GLN

Samples:

sample_1: Nsp10, [U-13C; U-15N], 0.5 mM; NaPi 25 mM; NaCl 150 mM

sample_2: Nsp10, [U-13C; U-15N], 0.4 mM; NaPi (pH 7.5) 25 mM; NaCl 150 mM; TCEP 2 mM

sample_3: Nsp10, [U-13C; U-15N], 0.5 mM; Tris/Hcl (pH 7.5) 20 mM; NaCl 150 mM

sample_4: Nsp10, [U-13C; U-15N], 570 uM; NaPi 50 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 175 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 177 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 170 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D best-TROSYsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
(H)C(CCO)NH-TOCSYsample_3isotropicsample_conditions_3
2D best-TROSYsample_4isotropicsample_conditions_4

Software:

LOGS v2.2 - collection

SPARKY v3.114 - chemical shift assignment, peak picking

TOPSPIN - processing

NMR spectrometers:

  • Bruker Bruker Avance neo 900 MHz 900 MHz
  • Bruker Bruker Avance neo 600 MHz 600 MHz

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