Extended Data Fig. 9: Amino acids in proximity of the CIM-834 binding pocket and their conservation in the M protein sequence of different human coronaviruses.
From: A coronavirus assembly inhibitor that targets the viral membrane protein
a-b, M protein chains in grey (dark grey = chain A, light grey= chain B). Bound compound displayed as surface. Green residues are within 5 Å of the bound compound. Blue residues are 5-10 Å from bound compound. c, Amino acid alignment of the M proteins of the seven human coronaviruses. Identical residues are shown as dots. Same colour coding as in a,b. d, Comparison of the overall conservation of the M protein sequence among different human coronaviruses versus conservation of the amino acids in the CIM-834 binding pocket (residues 10 Å and 5 Å from the bound compound). Conservation of the complete sequence of the main protease and its active site is provided for comparison. e, Mapping of the conservation rate (identity) of M residues on cryo-EM model (colour scale: red ≤20%, yellow 50%, grey ≥ 70%), based on an alignment of 100 coronaviral sequences. Sequences used for mapping were retrieved from a BLAST search against the M protein sequence, in the UniProtKB (www.uniprot.org).
