Extended Data Fig. 9: EV-D68 residues interacting with Fc-MFSD6(L3).

(a) Interactions within 4 Å distance from the Fc-MFSD6(L3) (chain E). The model for EV-D68 in complex with Fc-MFSD6(L3) is coloured, with VP1 (purple) and VP3 (red). The model for apo EV-D68 is grey. Residues between L1208 and T1216 are part of the VP1 GH loop. Fc-MFSD6(L3) is yellow, with start and end residues labelled. (b) Hydrogen bonding and salt bridge interactions and distances from PISA. *Indicates interaction not found by PISA but measured in Chimera. The atom ID starts with the atom (H (hydrogen), O (oxygen), N (nitrogen)). Protein atom IDs with one letter belong to the main chain; others belong to the side chain. Glycan atom IDs are relative to carbon numbering. NAG represents GlcNAc. (c-d) Selected interactions (also shown in Supplementary Video 1) show residues interacting with (c) R205 with H-bonds and (d) two GlcNAcs with H-bonds. The model is in atomic colouring (carbon (grey), hydrogen (white), oxygen (red), nitrogen (blue)). The map is transparent grey. Hydrogen bonds are shown with dashed lines. (e) EV-D68 RIVEM roadmap plot showing interacting residues. The large triangle marks the boundary of the projected asymmetric unit. The icosahedral symmetry axes are indicated by an oval, triangle, and pentagon. Residues interacting with Fc-MFSD6(L3) (chains E-F) within 4 Å distance are coloured by capsid protein with VP1 (purple), VP2 (green), and VP3 (red). A bright red outline marks capsid residues with H-bonds or a salt bridge with Fc-MFSD6(L3) (also in (b)). (f) EV-D68 RIVEM roadmap coloured by radial distance from 135 Å (blue) to 160 Å (red). A bright yellow outline marks capsid residues interacting with Fc-MFSD6(L3) within 4 Å distance and encloses part of the canyon, a depressed region (blue).