Water Evaporation and Conformational Changes from Partially Solvated Ubiquitin

Table 2

Comparison of structural properties of the protein in various environments, averaged over the last 3 ns of the simulation. Except for the bulk water simulation, averages over 3 simulations are shown. The crystal simulations show almost vanishing fluctuations, except for the RMSD.

	Bulk water	Thick shell	Thin shell	Vacuum	crystal
RMSD [Å]	1.8	2.4±0.3	2.7±0.3	2.4±0.1	2.6±0.4
SASA [nm^2]	49.7	47.2±0.4	45.9±0.02	41.9±0.2	42.8
SESA [nm^2]	28.8	29.2±0.1	30.5±0.2	31.1±0.2	31.6
𝑅gyr [Å]	11.93	11.57±0.06	11.49±0.03	11.36±0.05	11.28
HBpp	229.3	230.7±3.1	227.1±3.2	216.9±5.5	223.4
HBps	254.8	250.5±5.4	194.4±3.7	—	87.5