A brief synopsis is given here. Most movement is in the small nucleotide binding lobe, which appears to twist in a clockwise direction upon ATP binding. The major changes are in the C terminal 30 residues shown at the top of the figure and in the interaction of the glycine rich loop with the phosphoryaltion site Thr197. The RMS is determined by sequence alignment followed by structure superposition of those residues found to align in the sequence. Structure superposition uses minimization of the Calpha positions by the method of least-squares.
Sequence homology is reported as a percentage.