Proteus: An algorithm for proposing stabilizing mutation pairs based on interactions observed in known protein 3D structures

Table 2 The overall accuracy of mutants that present a higher number of contacts or at least keep the number of contacts when compared to the wild type (details were included in the supplementary material: Tables S7, S8, S9, S10)

Proteus ID	PDB ID	HB	Weak HB	Ionic	Aromatic	Polar	Weak polar	Hydrophobic¹
UM6SQD	2YWY	0.84	0.66	0.96²	0.84²	0.94	0.98	0.28
N7Q9RZ	1LVB	0.97	0.79	1.0	0.9	0.95	1.0	0.26
YTP3YC	1LGY	0.77	0.66²	0.98²	0.9	0.96	1.0	0.31
4L8HLU	1BGA	0.79	0.42	0.84	0.77²	0.87	0.98	0.22

¹For hydrophobic interactions, we also calculated the accuracy considering mutant structures that reduced or kept the number of contacts. For this case, UM6SQD presented an accuracy of 0.84; N7Q9RZ of 0.82; YTP3YC of 0.86; and 4L8HLU of 0.88. ² Not statistically relevant (check supplementary material for details). HB: hydrogen bonds. The projects are available at http://proteus.dcc.ufmg.br/result/id/[Proteus ID]

ISSN: 1471-2105