Table 3.
Side Chain Distances of Native and Substituted Cysteines in Native Antithrombin Structuresa
| 1E05 | 1T1F | |||
|---|---|---|---|---|
| AT residues | Cα–Cα | Cβ–Cβ | Cα–Cα | Cβ–Cβ |
| V375–S380 | 4.9 | 6.1 | 4.8 | 5.9 |
| L373–S380 | 6.9 | 6.4 | 6.8 | 6.5 |
| E374–E381 | 5.4 | 5.2 | 5.6 | 5.8 |
| K222–E381 | 5.2 | 4.5 | 5.3 | 4.4 |
| K222–K139 | 5.1 | 4.3 | 5.3 | 4.5 |
| C8–C128 | 5.5 | 4.1 | 5.7 | 3.8 |
| C21–C95 | 5.5 | 4.2 | 5.5 | 3.8 |
| C247–C430 | 6.2 | 3.6 | 6.2 | 3.8 |
a
Distances (in angstroms) between α-carbons and β-carbons of paired cysteine residues were measured in dimeric (PDB entry 1E05) and monomeric (PDB entry 1T1F) native antithrombin structures with PyMol version 2.2.3.