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. 2005 Mar 4;88(5):3310–3320. doi: 10.1529/biophysj.104.052019

FIGURE 6.

FIGURE 6

(A) Interaction of the K185 side chain with the β-phosphate of ATP in model/simulation Kir6.24 + ATP (illustrated using the starting model for the simulation). This interaction is maintained in (B) the Kir6.2 + ATP (monomer) simulation, and in (C) one subunit in the Kir6.24 + ATP (tetramer) simulation. In both B and C, the distance between the P atoms of the β-phosphate of ATP and the Nζ atom of the side chain of K185 is shown as a function of time.