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Pac. 13, 100197 (2021). support was evaluated with the aBayes parameter. Accession numbers and bat species are speci ed in the name of the sequences. Sequences are colored according to Fig. 1C. (C) Similarity plot analysis of Laotian and representative bat and pangolin sarbecoviruses based on the full-length genome sequence of SARS-CoV-2 human prototype strain (NC_045512, Wuhan-Hu-1) used as reference. The analysis was performed with the Kimura-2 parameter model, a window size of 1,000 base pairs, and a step size of 100 base pairs with SimPlot program, version 3.5.157. (D) Heatmap of identities at the protein level of representative human, bat, and pangolin sarbecoviruses compared to human SARS-CoV-2 lineage B (NC_045512, Wuhan-Hu-1). Spike protein has been divided into functional domains, and the sequences are ordered according to percentage of identity of the RBD domain. \"*\": absence of a functional ORF10 in Thai bat RacCS203 (accession number MW251308). Heatmap was created using the gplots package in R (version 3.6.3).","title":"Accession numbers and bat species are speci ed in the name of the sequences. Sequences are colored according to Fig. 1C. (C) Similarity plot analysis of Laotian and representative bat and pangolin sarbecoviruses based on the full-length genome sequence of SARS-CoV-2 human prototype strain (NC_045512, Wuhan-Hu-1) used as reference. The analysis was performed with the Kimura-2 parameter model, a window size of 1,000 base pairs, and a step size of 100 base pairs with SimPlot program, version 3.5.157. (D) Heatmap of identities at the protein level of representative human, bat, and pangolin sarbecoviruses compared to human SARS-CoV-2 lineage B (NC_045512, Wuhan-Hu-1). Spike protein has been divided into functional domains, and the sequences are ordered according to percentage of identity of the RBD domain","venue":"Lancet Reg. Health -West. Pac.","year":2020},{"raw":"A) Biolayer interferometry binding analysis of the hACE2 peptidase domain to immobilized BANAL52/103 or BANAL-236 RBDs. Black lines correspond to global t of the data using a 1:1 binding model. (B) Frequency of formation of salt bridges at the interface of RBD and hACE2 during the course of the MD simulations. The analysis is performed for 9 different MD simulations (3 replicates for each complex) of hACE2 in complex with SARS-CoV-2 (shades of green), BANAL-236 (shades of red) and BANAL-52/103 RBDs (shades of blue). (C) Ribbon representations of the crystal structures of hACE2 peptidase domain (cyan) in complex with SARS-CoV-2 (PDB 6M0J) or BANAL-236 (this study, PDB 7PKI)","title":"Biolayer interferometry binding analysis of the hACE2 peptidase domain to immobilized BANAL52/103 or BANAL-236 RBDs. Black lines correspond to global t of the data using a 1:1 binding model. (B) Frequency of formation of salt bridges at the interface of RBD and hACE2 during the course of the MD simulations. The analysis is performed for 9 different MD simulations (3 replicates for each complex) of hACE2 in complex with SARS-CoV-2 (shades of green), BANAL-236 (shades of red) and BANAL-52/103 RBDs (shades of blue). (C) Ribbon representations of the crystal structures of hACE2 peptidase domain (cyan) in complex with SARS-CoV-2"},{"authors":["Rbds"],"raw":"RBDs (pink). Black arrows in the overall structures indicate the structural difference between the two complexes at the level of helix H4. The insets show the main interactions in the ACE2-RBD interfaces. Residues in the RBM mutated between SARS-CoV-2 and BANAL-236 are indicated with colored boxes.","title":"Black arrows in the overall structures indicate the structural difference between the two complexes at the level of helix H4. The insets show the main interactions in the ACE2-RBD interfaces","venue":"Residues in the RBM mutated between SARS-CoV-2 and BANAL-236 are indicated with colored boxes"}]}