Table 4.
β-Trypsin – BPTI interaction: thermodynamic data and ZD scores for X-ray determined and in silico modeled BPTI-Lys 15 mutants
| Mutationa | ΔG° (kcal/mol)b | Nsolxr,c | Best Rankxr | ZDbest | ZD-sxr | ZDscxr | ZDelxr | ZDdesxr | ZD-sxr2,d | Nsolxr2 | Best Rankxr2 | ZD-smod,e | Nsolmod | Best Rankmod |
| GLY | -5.73 | 63 | 9 | 51.7 | 43.2 | 34.8 | -0.9 | 9.3 | 42.3 | 62 | 13 | 42.5 | 62 | 1 |
| THR | -7.50 | 80 | 1 | 54.3 | 45.0 | 35.8 | -1.2 | 10.4 | 44.4 | 79 | 1 | 45.5 | 70 | 1 |
| ASP | -6.54 | 76 | 1 | 54.9 | 44.7 | 37.6 | -2.2 | 9.3 | 44.8 | 71 | 1 | 44.2 | 78 | 1 |
| MET | -10.36 | 79 | 1 | 56.8 | 47.1 | 36.7 | -1.1 | 11.5 | 46.1 | 78 | 1 | 45.4 | 74 | 1 |
| GLU | -8.59 | 73 | 1 | 58.7 | 47.7 | 38.8 | -1.2 | 10.1 | 47.3 | 74 | 1 | 44.8 | 76 | 1 |
| GLN | -8.73 | 89 | 1 | 55.5 | 44.8 | 36.4 | -0.8 | 9.2 | 45.1 | 84 | 1 | 43.9 | 74 | 1 |
| HIS | -9.27 | 88 | 1 | 62.5 | 48.7 | 38.6 | 0.2 | 9.9 | 49.4 | 87 | 1 | 47.0 | 77 | 1 |
| PHE | -11.04 | 85 | 1 | 67.1 | 51.8 | 40.1 | -0.1 | 11.8 | 51.6 | 85 | 1 | 49.0 | 71 | 1 |
aResidue in which BPTI-Lys 15 was mutated. The PDB entries corresponding to these variants are 3BTG, 3BTT, 3BTD, 3BTM, 3BTE, 3BTQ, 3BTH and 3BTF [28]
bStandard free energy of association as obtained from the relationship ΔG° = RT ln KD. Experimental data from Ref [10]
cHere, and in the following columns, xr refers to the results of docking runs from the experimentally resolved X-ray structures
dHere, and in the following columns, xr2 refers to the results of docking runs from the experimentally resolved X-ray structures in the absence of interface water molecules
eHere, and in the following columns, mod refers to the results of docking runs from the in silico modelled structures of the same complexes