. 2022 Feb 11;2(3):247–259. doi: 10.1021/acsphyschemau.1c00052

Table 3. Results Obtained from the GCMC Titration Analysis of the Both apo- and holo-Ferritin, with and without Constraints on the Protein and Ligand^a.

structure	sampling	ΔG_bind^°	optimal N	N(B_equil)
apo	constrained	–90.0 ± 0.8	9	8.7 ± 0.1
apo	unconstrained	–109.2 ± 0.8	10	10.2 ± 0.2
holo	constrained	–63.2 ± 0.4	4	3.8 ± 0.1
holo	unconstrained	–77.4 ± 0.8	6	6.0 ± 0.2

The table shows the value of the binding free energy minimum (ΔG_bind^° in kJ/mol), along with the corresponding optimal value of N. For comparison, the mean number of waters observed at B_equil is also given (with standard error).

Table 3. Results Obtained from the GCMC Titration Analysis of the Both apo- and holo-Ferritin, with and without Constraints on the Protein and Liganda.

Table 3. Results Obtained from the GCMC Titration Analysis of the Both apo- and holo-Ferritin, with and without Constraints on the Protein and Ligand^a.