(a) The C10 epitopes (circled by green dots) in an E protein raft identified by using a distance cutoff of 5 Å between the side chains of Fab and the E protein. The Fab molecules bind to both ends of each E protein dimer. The DI, DII and DIII of the E proteins in one raft are coloured in red, yellow and blue, respectively, those in neighbouring rafts are in grey. The three individual E proteins in an asymmetric unit are labelled as A, B and C molecules and those in the neighbouring asymmetric unit within the raft as A′, B′ and C′. The epitope residues within the intra-dimer interface are shown as light blue spheres, those at the inter-dimer and inter-raft interfaces as red and dark blue spheres, respectively. (b) The epitope within the intra-dimer interface on B-B′ dimer. The ZIKV c10 epitope residues that are conserved (similar charges or hydrophobicity) and non-conserved when compared to DENV are shown as green and magenta spheres, respectively. (c) Charge complementarity of the C10 intra-dimer epitope with the Fab paratope. Positive, negative and neutral charges are coloured in blue, red and white, respectively. Possible interacting residues are labelled.