Figures
Figs 1, 3, and 4 are incorrect; the publisher apologizes for the errors. The authors have provided corrected versions here.
(A) Sequence alignment of receptor binding domains (RBD) of SARS-CoV and SARS-CoV-2. The residues underlined are mutations found in the RBDs. Any residue numbers referred in the text are positions in this sequence alignment. (B) X-ray structures of RBD1 of SARS-CoV (PDB: 2AJF) and RBD2 of SARS-CoV-2 (PDB: 6M0J), respectively, bound to human receptor angiotensin-converting enzyme 2 (ACE2). (C) MD simulation setup for RBD1-ACE2 and RBD2-ACE2 complexes.
(A) Free-energy profiles computed as a function of the distance between the centers of mass of the RBDs and ACE2 using AMBER and C36 FFs. (B) Snapshots showing an initial configuration of RBD1-ACE complex and its configuration at 500 ns from the simulations using C36 FF. This 500 ns configuration was reproducible and showed in 3 out of 8 replicates (C) Distribution of the distance d between the Cαs of L486 of RBD1 and L79 of ACE2 and compared with d of F486-L79 in RBD2-ACE2.
(A) Free-energy profiles computed from US simulations as function of RRBD-ACE2 using C36-FF. (B) Three-dimension distributions of the stable pairs (refer Fig 2) as function of the biasing distance between the centers of mass of RBD2 and ACE2. (C) A snapshot during the Umbrella simulations using RRBD-ACE2 = 70 Å. Residue A475 in RBD2 is located right behind F486.
Reference
- 1. Ngo VA, Jha RK (2021) Identifying key determinants and dynamics of SARS-CoV-2/ACE2 tight interaction. PLoS ONE 16(9): e0257905. https://doi.org/10.1371/journal.pone.0257905 pmid:34582502
Citation: Ngo VA, Jha RK (2021) Correction: Identifying key determinants and dynamics of SARS-CoV-2/ACE2 tight interaction. PLoS ONE 16(11): e0259705. https://doi.org/10.1371/journal.pone.0259705
Published: November 3, 2021
Copyright: © 2021 Ngo, Jha. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.