Skip to main content
. 2016 Dec 22;17(Suppl 19):500. doi: 10.1186/s12859-016-1372-3

Table 2.

Structural characterized features used in the graph constructions for the PI-resistance mutants to IDV and LPV

Vpocketa3) AllosCommb ΔΔG score / ΔSc (kcal/mol) RMSd (Å)
Indinavir (IDV) — molecular weight = ~614 g/mol
IDV_0 (major/minor) 1929.67 (1863.57) 0.989 (0.745) −1.37 / −1.18 1.14
IDV_1 (major/minor) 1884.57 0.770 (0.825) 4.32 / −0.45 1.09
IDV_2 (major/minor) 1769.62 0.518 (0.468) 2.14 / 0.72 1.04
Lopinavir (LPV) — molecular weight = ~629 g/mol
LPV_0 (wt) 1659.68 (2201.32) 0.696 (0.257) 0.13 / 0.34 0.88
LPV_1 (major/minor) 1872.66 0.590 (0.547) 4.53 / 0.58 1.0
LPV_2 (major/minor) 1867.24 0.665 (0.452) 1.51 / −0.15 0.98
LPV_3 (major/minor) 1781.42 0.8 (0.646) 4.28 / 1.47 1.06
LPV_4 (major/minor) 2029.70 0.769 (0.646) 1.51 / 0.48 1.08
LPV_5 (minor) 2051.45 0.167 (0.944) 1.28 / 0.62 1.08
LPV_6 (minor) 2034.89 0.385 (0.944) 2.27 / 0.78 1.08

aPocket volume of the native protease [PDB: 1ODW], which contains no mutations in the presence of corresponding PIs, is shown in parentheses for comparison purpose. In the cases of wild type proteases LPV_0, there is a single mutation found (i.e. L63P) in the structures when compared to the native protease sequence. The complexes that contain the quadruple mutants and show increased pocket volume are in bold

bFor comparison purposes of allosteric effect, communication estimated values of the native protease were shown in parentheses

cΔΔG and ΔS scores represent free energy and vibrational energy respectively, demonstrating thermo-stability of the protease when mutated from the native protease