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Distant residues modulate conformational opening in SARS-CoV-2 spike protein

The novel coronavirus (SARS-CoV-2) pandemic resulted in the largest public health crisis in recent times. Significant drug design effort against SARS-CoV-2 is focused on the receptor-binding domain (RBD) of the spike protein, although this region is highly prone to mutations causing therapeutic resistance. We applied deep data analysis methods on all-atom molecular dynamics simulations to identify key non-RBD residues that play a crucial role in spike−receptor binding and infection. Because the non-RBD residues are typically conserved across multiple coronaviruses, they can be targeted by broad-spectrum antibodies and drugs to treat infections from new strains that might appear during future epidemics. The MD trajectories are available from Zenodo at [doi.org/10.528c1/zenodo.5052691][1]. The codes and the residue correlation data used in this study are available from GitHub at <https://github.com/dhimanray/COVID-19-correlation-work>. All further details about the methods and t

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