Movie S1.

Conformational rearrangements upon binding ADP•BeF3 in the TerLP74-26 ATPase. An interpolation between TerL apo and ADP•BeF3-bound structures using the UCSF Chimera “Morph Conformations” tool (default parameters) (59) was performed. The movie demonstrates the effects of substrate binding and release on the lid subdomain (pink). A closer view reveals how residues in the P-loop move to engage ADP•BeF3 (Fig. 3C). Finally, a wide view reveals the large-scale movement of the Rossmann fold upon ADP•BeF3 binding and release if the lid is held stationary (Fig. 3D).

Structure and mechanism of the ATPase that powers viral genome packaging

Brendan J. Hilbert, Janelle A. Hayes, Nicholas P. Stone, Caroline M. Duffy, Banumathi Sankaran, and Brian A. Kelch

PNAS. 2015. DOI: 10.1073/pnas.1506951112