Extended Data Fig. 10: Parametrization of proteins for coarse-grained modelling.

(a) Bead sizes for tegument and host proteins other than UL32 were approximated by the gyroscopic radii from their corresponding AF2 predictions, which is exemplarily shown for UL47 and UL48 proteins. (b) Representation of glycoproteins in the coarse-grained model via clustering of ɑ-carbon from cryoEM or AF2 models into beads, exemplarily shown for gB pre-fusion structure. The transmembrane domains are substituted by beads from the membrane model (light blue). (c) The UL32 AF2 prediction was segmented into 11 parts based on a molecular dynamics simulation. Segment dimensions were calculated from the segment-specific radii of gyration. As the radius of gyration overestimates the volume for a disordered protein, the chain of beads was further subdivided to yield a chain of more but smaller beads. The most n-terminal bead was immobilized by replacing it with a bead from the nucleocapsid shell. The chain of beads was allowed to have segment-specific flexibility at hinges (indicated arrows). (d) Cross-sectional view of the HCMV virion model with tegument proteins other than UL32 removed.