Figure 4

Contact map representing the monomer-dimer equilibrium of E7. Inter- and intra-molecular contacts in the RAM ensemble are depicted by orange and blue colours, respectively. Residues 1–98 (monomer one) and residues 99–196 (monomer two) are depicted along x and y axes. The E7N domain in the RAM ensemble is predominantly extended and involved in transient intra-molecular contacts between: (1) residues in the N-terminal end (lower left), and (2) Tyr23/Tyr25 and His51/His73 (lower right). Inter-molecular contacts are present at the dimer interface and these contacts superimpose well with the contacts present in the structures of low-risk HPV-1a and HPV-45 variants (Figure S3). Interestingly, residue H51 is placed at the exit of the folded part of E7C and makes both inter- and intra-molecular contacts (Fig. 5). Intermolecular contacts are made with the small helix α2 (Val90, Cys94) and β1-β2 loop Lys60) of E7C (top). This same residue makes intramolecular contacts with Tyr23 (lower right).