Table 4.
Energy difference between the native enzyme and their mutants.
| Method | Mutant | ΔE (kcal/mol) |
|---|---|---|
| PoPMuSiC | D170F | 0.067 |
| D170T | 0.063 | |
| D399M | 0.009 | |
| E487I | 0.040 | |
| E487Y | 0.091 | |
| G142F | 0.066 | |
| P183T | 0.094 | |
| P203C | −0.063 | |
| P203V | −0.025 | |
| Alignment | G431D | 0.013 |
| I217F | 0.020 | |
| N275K | 0.068 | |
| N275R | 0.045 | |
| N372D | −0.003 | |
| N79D | −0.050 | |
| Q65R | 0.007 | |
| Ionic interaction | G234D-N271K-N270R | 0.073 |
| G234E-N271K-N270R | 0.059 | |
| G234k-N271E-N270D | −0.010 | |
| G234R | 0.184 | |
| (3-SB) G234R-N271E-N270D | −0.094 | |
| S264E | 0.038 | |
| T147E | −0.044 | |
| Disulfide bridges | D233C-T310C/H184C-S284C | −0.002 |
| (3-DB) D233C-T310C/H184C-S284C/K396C-D399C | −0.131 | |
| (4-DB) D233C-T310C/H184C-S284C/K396C-D399C/N94C-G465C | −0.177 | |
| D233C-T310C | −0.100 | |
| H184C-S284C | −0.064 | |
| K396C-D399C | −0.037 | |
| N94C-G465C | 0.007 | |
| Disturbance of active site | F468P | −0.091 |
| F481M | −0.022 | |
| G420L | 0.136 | |
| L132T | −0.084 | |
| L416I | 0.029 | |
| L469F | −0.009 | |
| M85V | 0.014 | |
| S130D | −0.017 | |
| W85F | −0.042 |
In the first column are represented the search method for the proposed mutants; second column, the proposed residue shift for the mutants design and the last column presents the mutant energy after the minimization, taking as a baseline the Lacc 6 energy.