Table 2. Average Root Mean Squared Fluctuation (RMSF) Values in Angstroms of the Backbone Atoms for Different Regions of the Protein from the MD Simulations.

region of protein	residue range	Myr apo (Å)a	Myr ternary (Å)a	apo (Å)b	ternary (Å)b
entire protein	2–350	1.07	1.16	1.18	1.17
N-terminus/A-helix	2–40	1.97	2.41	2.89	3.40
core (N/C-lobes)	41–300	0.89	0.95	0.92	0.83
N-lobe	41–126	0.89	0.94	0.95	0.79
C-lobe	127–300	0.89	0.95	0.90	0.86
C-tail	301–350	1.31	1.33	1.22	1.15
myristate pocket	13–18; 95–105; 150–160; 300–308	0.80	1.04	0.96	1.11
catalytic loop	164–172	0.68	0.54	0.68	0.54
DFG motif	184–186	0.97	0.60	0.86	0.55
ATP site residues	49–55, 70, 120–127, 327–331	1.19	0.95	1.04	0.84
Activation Loop	192–200	1.15	1.23	1.11	0.97
B-helix	76–81	1.18	1.16	1.39	0.98
C-helix	84–96	0.77	0.92	0.86	0.75
β-strand 2	56–61	0.78	0.89	0.75	0.63
β-strand 3	68–75	0.76	0.78	0.78	0.64
β-strand 4	106–111	0.66	0.78	0.80	0.68
β-strand 5	115–121	0.67	0.76	0.74	0.60

^aThese simulations are of the protein when it is myristylated at its N-terminal glycine residue.

^bThese simulations correspond to the protein that is not myristylated. Apo simulations are of the protein in the absence of ligands, and ternary state corresponds to simulations where the protein was bound to ATP and an inhibitory peptide, SP20.