Figure 2.
Conformation of the key asparagine residues in the SF. (A) Cryo-EM structure (PDB: 6NQ0). (B) Super-open state was observed in the simulations. (C and D) Reorientation of the key SF residues (N653 and N274, magenta) from the cryo-EM open (blue) to the super-open state (green) with H-bond formation between the asparagine side chains (distances shown in orange).

Conformation of the key asparagine residues in the SF. (A) Cryo-EM structure (PDB: 6NQ0). (B) Super-open state was observed in the simulations. (C and D) Reorientation of the key SF residues (N653 and N274, magenta) from the cryo-EM open (blue) to the super-open state (green) with H-bond formation between the asparagine side chains (distances shown in orange).

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