Figure 1. c.3700 A>G mutation (ΔI1234_R1239) is predicted to induce local conformational defect in NBD2 of CFTR in molecular dynamic simulations.

1. Representative snapshots of NBD2 in WT‐CFTR (left panel) and ΔI1234_R1239‐CFTR (right panel) systems following 30 ns of simulation. Each secondary structure element of the labeled β‐strands is represented by a unique color as follows: isolated‐bridge, brown; coil, gray; β‐strand, yellow; 3–10 helix, dark blue; α‐helix, cyan; turn, green; Walker A is in magenta, while the rest of NBD2 is in transparent representation. The amide N and carbonyl C atoms of residues 1,233 and 1,240, respectively, are shown as red spheres, and the backbone atoms between the same residue pair are shown in red cartoon representation.
2. Replica‐averaged root‐mean‐square deviation (RMSD) of backbone atoms of NBD2 from the starting conformation of WT‐CFTR and ΔI1234_R1239‐CFTR as a function of the residue number is represented in red and blue thick lines, respectively. The six‐residue deletion (ΔI1234_R1239) is labeled “del”. The thick black and magenta lines denote β‐strands and the Walker A motif, respectively.