PMC:7643666 / 14521-15148 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7643666","sourcedb":"PMC","sourceid":"7643666","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7643666","text":"Analysis of molecular dynamics considering the variation of RMSD during the time indicated each complex reaching a conformational steady-state, as observed from the presence of RMSD plateau (see Supplementary Figure S1) [35]. In Figure 2A the structural coordinates of Myotis daubentonii and Rhinolophus ferrumequinum ACE2 derived from the last step of molecular dynamics are superimposed to the crystal structure of hACE2. The poses are very similar (RMSD on backbone heavy atoms: 5.83 Å) and the residues defining the protein-protein interaction framework are almost conserved (see Supplementary Tables S3–S7, Figures S2–S6).","tracks":[]}