BMRB Entry 36080

Title:
NMR Structure and Localization of a Large Fragment of the SARS-CoV Fusion Protein: Implications in Viral Cell Fusion   PubMed: 28988778
Deposition date:
2017-05-02
Original release date:
2018-02-06
Authors:
Bhattacharjya, S.; Chatterjee, D.
Citation:

Citation: Mahajan, Mukesh; Chatterjee, Deepak; Bhuvaneswari, Kannaian; Pillay, Shubhadra; Bhattacharjya, Surajit. "NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion"  Biochim. Biophys. Acta 1860, 407-415 (2018).

Assembly members:

Assembly members:
Spike protein S2, polymer, 65 residues, 7544.744 Da.

Natural source:

Natural source:   Common Name: HCoV-SARS   Taxonomy ID: 227859   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betacoronavirus SARS-related coronavirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Experimental source:

Natural source:   Common Name: HCoV-SARS   Taxonomy ID: 227859   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betacoronavirus SARS-related coronavirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts56
15N chemical shifts56
1H chemical shifts141

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 65 residues - 7544.744 Da.

1   PROARGASNTHRARGGLUVALPHEALAGLN
2   VALLYSGLNMETTYRLYSTHRPROTHRLEU
3   LYSTYRPHEGLYGLYPHEASNPHESERGLN
4   ILELEUPROSERPROLEULYSPROTHRLYS
5   ARGSERPHEILEGLUASPLEULEUPHEASN
6   LYSVALTHRLEUALAASPALAGLYPHEMET
7   LYSGLNTYRGLYGLU

Samples:

sample_1: Large Fragment of the SARS-CoV Fusion Protein, [U-13C; U-15N], 0.2 M; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
Hetronuclear NOEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

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