BMRB Entry 50334

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50334

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Title:
1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of coronavirus-2 non-structural protein 3e
Deposition date:
2020-06-21
Original release date:
2020-06-27
Authors:
Korn, Sophie; Dhamotharan, Karthikeyan; Furtig, Boris; Hengesbach, Martin; Lohr, Frank; Qureshi, Nusrat; Richter, Christian; Saxena, Krishna; Schwalbe, Harald; Tants, Jan-Niklas; Weigand, Julia; Wohnert, Jens; Schlundt, Andreas
Citation:

Citation: Korn, Sophie; Dhamotharan, Karthikeyan; Furtig, Boris; Hengesbach, Martin; Lohr, Frank; Qureshi, Nusrat; Richter, Christian; Saxena, Krishna; Schwalbe, Harald; Tants, Jan-Niklas; Weigand, Julia; Wohnert, Jens; Schlundt, Andreas. "1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e"  Biomol. NMR Assign. 14, 329-333 (2020).
PubMed: 32770392

Assembly members:

Assembly members:
entity_1, polymer, 120 residues, 13745 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGYFTEQPIDLVPNQPYP NASFDNFKFVCDNIKFADDL NQLTGYKKPASRELKVTFFP DLNGDVVAIDYKHYTPSFKK GAKLLHKPIVWHVNNATNKA TYKPNTWCIRCLWSTKPVET

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts115
1H chemical shifts122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nsp3e1

Entities:

Entity 1, Nsp3e 120 residues - 13745 Da.

GAMG is an artificial overhang from TEV cleavage.

1   GLYALAMETGLYTYRPHETHRGLUGLNPRO
2   ILEASPLEUVALPROASNGLNPROTYRPRO
3   ASNALASERPHEASPASNPHELYSPHEVAL
4   CYSASPASNILELYSPHEALAASPASPLEU
5   ASNGLNLEUTHRGLYTYRLYSLYSPROALA
6   SERARGGLULEULYSVALTHRPHEPHEPRO
7   ASPLEUASNGLYASPVALVALALAILEASP
8   TYRLYSHISTYRTHRPROSERPHELYSLYS
9   GLYALALYSLEULEUHISLYSPROILEVAL
10   TRPHISVALASNASNALATHRASNLYSALA
11   THRTYRLYSPROASNTHRTRPCYSILEARG
12   CYSLEUTRPSERTHRLYSPROVALGLUTHR

Samples:

sample_1: Nsp3e(1088-1203), [U-100% 15N], 1120 uM; D2O, [U-100% 2H], 10%; DSS 300 uM; sodium azide 0.02%; sodium chloride 150 mM; sodium phosphate, pH 7.0 25 mM; TCEP 2 mM

sample_2: Nsp3e(1088-1203), [U-100% 13C; U-100% 15N], 577 uM; D2O 10%; DSS 300 uM; sodium azide 0.02%; sodium chloride 150 mM; sodium phosphate, pH 7.0 25 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N heteronoesample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D BEST-TROSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.4.2 - chemical shift assignment, data analysis

TOPSPIN v3.2 - 4.0 - collection, processing

NMR spectrometers:

  • Bruker AVANCE III 950 MHz
  • Bruker Avance II 600 MHz

Related Database Links:

NCBI YP_009725299.1

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