| Val3→Phe |
β1 |
Larger residue inserted into hydrophobic core |
| Leu4→Phe |
β1 |
Larger residue inserted into hydrophobic core |
| Tyr19→Cys |
α1 |
Loss of buried packing interaction |
| Pro53→Leu |
α2 |
Expected to disrupt packing |
| Thr62→Ala |
β4–α3 |
Solvent exposed to active site cleft |
| Ala66→Val |
α3 |
Larger residue is expected to disrupt packing |
| Cys73→Arg |
α3 |
Charged residue inserted into hydrophobic core |
| Val82→Phe |
α4 |
Large hydrophobic exposed to solvent |
| Val99→Ala |
β5–α6 |
Loss of packing interactions |
| Ala104→Val |
α6 |
Larger residue is expected to disrupt packing |
| Ile129→Thr |
α7 |
Hydrophilic residue inserted into hydrophobic core |
| Ser212→Pro |
α10 |
Disruption of helix, packing constraints |
| Gly225→Ser |
β10–α11 |
Disruption of tight turn |
| Thr228→Met |
α11 |
Larger residue could disrupt packing |
| Pro248→Gln |
α12 |
Tight turn, hydrophilic residue into hydrophobic packing environment |
| Glu249→stop |
α12 |
Truncated protein, loss of helix 12 |
