. 2017 Oct 11;56(44):5886–5899. doi: 10.1021/acs.biochem.7b00822

Table 2. Comparison of the Predicted and Experimental Numbers of Water Molecules (n_w) Hydrating R67 DHFR from the Crystal Structure, SASSIE Fits, and SANS Data.

protein	source	predicted/experimental	no. of water molecules in the hydration layer (n_w)
truncated R67 DHFR	crystal structure (2RH2)⁸	predicted from ASA	1230^a
truncated R67 DHFR	crystal structure (2GQV)⁹	predicted from ASA	1297^b
truncated R67 DHFR	crystal structure (2GQV)⁹	experimental	340 in pore and first hydration shell
truncated R67 DHFR in the presence of betaine	SANS	experimental	380 ± 105
full-length R67 DHFR	frames from SASSIE analysis (χ² < 10)	predicted from ASA averaged for 7936 frames	1800
full-length R67 DHFR in the presence of betaine	SANS	experimental	1285 ± 214
full-length R67 DHFR in the presence of DMSO	SANS	experimental	1253 ± 199

The 2RH2 structure lacks 20 residues at the N-termini.

The 2GQV structure lacks 19 residues at the N-termini. Serine 20 was removed for comparison with 2RH2.

Table 2. Comparison of the Predicted and Experimental Numbers of Water Molecules (nw) Hydrating R67 DHFR from the Crystal Structure, SASSIE Fits, and SANS Data.