Fig. 2

Measures of sequence diversity for PvAMA1 and relationship to key binding interfaces. a Spatially-derived nucleotide diversity (π) for PvAMA1 displayed over the modelled PvAMA1 structure. A radius of 15 Å was used for each 3D sliding window. b Normalized Shannon entropy for PvAMA1 residues on a per-site basis, with no spatial averaging performed. Higher entropy values are indicative of greater sequence diversity across all strains at that residue position. c Residues involved in the binding of PvAMA1 to its PvRON2 ligand. Residues within 4 Å of the RON2 peptide are shown in blue on the modelled PvAMA1 structure (as defined by the PDB structure 5NQG). Note that some binding residues are not visible due to the presence of the flexible Domain II loop near the RON2 binding groove