. Author manuscript; available in PMC: 2008 Sep 7.

Published in final edited form as: J Mol Biol. 2007 Jun 26;372(1):205–222. doi: 10.1016/j.jmb.2007.06.049

Table 3.

Distances between hydrophobic interface residues throughout the simulations

Residue Pair	43 – 144		56 – 131		81 – 169
Protein	Mean (SD)	Max / Min	Mean (SD)	Max / Min	Mean (SD)	Max / Min
Human γC WT (L56)	8.7 (2.2)	14.4 / 4.9	6.9 (1.5)	10.7 / 4.2	6.4 (1.1)	10.3 / 4.7
Human γC C79R (L56)	13.6 (4.4)	22.3 / 4.7	13.1 (5.4)	23.6 / 4.3	7.6 (1.4)	11.7 / 5.0
Human γC R36S (L56)	9.4 (6.2)	24.3 / 4.4	8.1 (4.7)	20.6 / 4.5	7.5 (3.9)	17.1 / 4.5
Mouse γC WT (F56)	5.2 (0.3)	6.5 / 4.2	5.2 (0.3)	6.8 / 4.4	5.5 (0.3)	6.6 / 4.5
Human γD WT (F56)	5.4 (0.4)	7.0 / 4.2	5.2 (0.4)	6.6 / 4.2	5.4 (0.4)	6.9 / 4.5
Human γD R36S (F56)	5.1 (0.3)	6.0 / 4.2	6.5 (0.8)	9.0 / 4.5	5.1 (0.3)	6.7 / 4.2

The Cβ – Cβ distances (Å) for residues across the domain – domain interface during the 5 ns long simulations. The stability of the interface in those proteins with Phe 56 (mouse γC and human γD) can be seen when compared to human γC which has Leu 56.