Figure 1
Structural features of the Nsp15 monomer in the apo hexamer. (a) A representative monomer structure (N-term domain: blue, Mid domain: red, and C-term domain: grey), the other dimers (transparent white) in the front trimer, and the backside trimers (pale green) are depicted. The residues shown by CPK models are involved in electrostatic bonding (salt bridges and hydrogen bonds) between the pairs of amino acids listed in (b). In (b), broken lines indicate the pattern of the electrostatic bondings. (c, d) The residues that form inter-monomer interfaces. The white area denotes non-interfacial residues, while other colors (yellow, orange, and dark grey) indicate the hexamer interface residues. In (d), the protein is rotated 180° around the y axis. The structure images in this paper were created using VMD60 unless otherwise specified.
