BMRB Entry 50388

Title:
1H, 13C, and 15N backbone chemical shift assignments of the macrodomain of SARS-CoV-2 non-structural protein 3b bound to ADPr   PubMed: 32803496
Deposition date:
2020-07-13
Original release date:
2020-08-19
Authors:
Schwalbe, Harald; Sreeramulu, Sridhar; Banci, Lucia; Cantini, Fancesca; Richter, Christian; Lohr, Frank
Citation:

Citation: Cantini, Francesca; Banco, Lucia; Altincekic, Nadide; Bains, Jasleen; Dhamotharan, Karthikeyan; Fuks, Christin; Gande, Santosh; Hargittay, Bruno; Hutchison, Marie; Korn, Sophie; Kubatova, Nina; Kutz, Felicitas; Meiser, Nathalie; Linhardt, Verena; Pyper, Dennis; Furtig, Boris; Hengesbach, Martin; Lohr, Frank; Qureshi, Nusrat; Richter, Christian; Saxena, Krishna; Schlundt, Andreas; Schwalbe, Harald; Sreeramulu, Sridhar; Tants, Jan-Niklas; Wacker, Anna; Weigand, Julia; Wohnert, Jens; Tsika, Aikaterini; Fourkiotis, Nikolaos; Spyroulias, Georgios. "1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b"  Biomol. NMR Assignments 14, 339-346 (2020).

Assembly members:

Assembly members:
entity_1, polymer, 173 residues, Formula weight is not available
ADENOSINE-5-DIPHOSPHORIBOSE, non-polymer, 559.316 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:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a(+)

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a(+)

Data sets:
Data typeCount
13C chemical shifts437
15N chemical shifts145
1H chemical shifts145

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nsp3b1
2APRr2

Entities:

Entity 1, Nsp3b 173 residues - Formula weight is not available

1   GLYHISMETVALASNSERPHESERGLYTYR
2   LEULYSLEUTHRASPASNVALTYRILELYS
3   ASNALAASPILEVALGLUGLUALALYSLYS
4   VALLYSPROTHRVALVALVALASNALAALA
5   ASNVALTYRLEULYSHISGLYGLYGLYVAL
6   ALAGLYALALEUASNLYSALATHRASNASN
7   ALAMETGLNVALGLUSERASPASPTYRILE
8   ALATHRASNGLYPROLEULYSVALGLYGLY
9   SERCYSVALLEUSERGLYHISASNLEUALA
10   LYSHISCYSLEUHISVALVALGLYPROASN
11   VALASNLYSGLYGLUASPILEGLNLEULEU
12   LYSSERALATYRGLUASNPHEASNGLNHIS
13   GLUVALLEULEUALAPROLEULEUSERALA
14   GLYILEPHEGLYALAASPPROILEHISSER
15   LEUARGVALCYSVALASPTHRVALARGTHR
16   ASNVALTYRLEUALAVALPHEASPLYSASN
17   LEUTYRASPLYSLEUVALSERSERPHELEU
18   GLUMETLYS

Entity 2, APRr - C15 H23 N5 O14 P2 - 559.316 Da.

1   APR

Samples:

sample_1: Nsp3b, [U-13C; U-15N], 650 uM; Bis-Tris 25 mM; NaCl 150 mM; TCEP 3 mM; ADPr 6.5 mM

sample_conditions_1: ionic strength: 184 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D best-TROSY HSQCsample_1isotropicsample_conditions_1
2D HSQC HNsample_1isotropicsample_conditions_1
3D best-TROSYHNCACBsample_1isotropicsample_conditions_1
3D best-TROSY HN(CO)CACBsample_1isotropicsample_conditions_1
3D best-TROSY HNCOsample_1isotropicsample_conditions_1

Software:

LOGS v2.2 - collection

TOPSPIN v4.0.6 - acquisition and processing

CARA - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Bruker Avance neo 1200 MHz 1200 MHz

Related Database Links:

GB MN908947.3

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