Skip to main content
. Author manuscript; available in PMC: 2020 Sep 1.
Published in final edited form as: Hum Mutat. 2019 Jun 18;40(9):1400–1413. doi: 10.1002/humu.23789

Table 3 –

Average r.m.s.d. values computed in the last 50 ns (100 ns) of the simulations at 300 K (355 K).

System ar.m.s.d. 300K ar.m.s.d. 355K bRgyr 300K bRgyr 355K
Wild type 0.16(1) nm 0.21(4) nm 1.35(1) nm 1.39(1) nm
p.D104G 0.13(1) nm 0.18(2) nm 1.36(1) nm 1.39(1) nm
p.A107V 0.14(2) nm 0.23(3) nm 1.36(1) nm 1.40(1) nm
p.F109L 0.17(2) nm 0.15(3) nm 1.36(1) nm 1.40(1) nm
p.Y123S 0.18(1) nm 0.18(2) nm 1.35(1) nm 1.39(1) nm
p.S161I 0.13(1) nm 0.21(2) nm 1.36(1) nm 1.40(1) nm
p.S181F 0.19(2) nm 0.19(2) nm 1.35(1) nm 1.39(1) nm
p.S202F 0.15(2) nm 0.13(2) nm 1.36(1) nm 1.39(1) nm
a

The r.m.s.d. is calculated on the backbone of the protein and taking as reference structure the one at the end of the equilibration procedure of the wild type simulation.

b

The average values of the radius of gyration (Rgyr) are computed in the last 50 ns (100 ns) of the simulations at 300 K (355 K) considering the backbone of the protein.