TABLE 1.
Predictions of distances at the hSERT Cys double mutants
The homology model of SERT based on the LeuTAa was used to measure the approximate S–S distances between residues. Each residue was computationally mutated to cysteine, and the distance between the Cys pair (S–S) was determined (PyMOL; DeLano Scientific, LLC, San Carlos, CA). Approximate distances were based on an orientation of the -SH side chains, which were positioned by the default setting in PyMOL with no steric clashes observed.
| Mutant pair | Predicted distance (Cys–Cys) |
|---|---|
| Å | |
| TMH XI-X | |
| F556C-T497C | 12.1 |
| F556C-G498C | 8.0 |
| TMH XI-VI | |
| F556C-A330C | 7.7 |
| F556C-A331C | 5.5 |
| F556C-Q332C | 12.9 |
| TMH I-VI | |
| I108C-A330C | Inaccessible |
| I108C-A331C | 5.0 |
| I108C-Q332C | 3.5 |
| I108C-E396C | Inaccessible |