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. 2021 Mar 9;13(3):439. doi: 10.3390/v13030439

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Binding interactions and energy of spike proteins with the CR3022 antibody. (A) The hydrogen interaction of wildtype was better than mutant spike proteins. (B) The binding interaction of wildtype spike protein with the heavy chain of CR3022 antibody, N501 (circled) making hydrophobic contact (hydrogen bonds are shown with green dots and non-polar interactions with magenta and brick semicircle). (C) The binding interaction of N501Y mutant spike protein with heavy chain of CR30222 antibody. (D) The binding interaction of N440K mutant spike protein with heavy chain of CR3022 antibody.