Table 1. A summary of 11 C-Tpr binding sites on CRM1-RanGTP-Snurportin complex predicted based on our simulations.
| Site # | Residue of CRM1/Snurportin* | Energy (kcal/mol) (Simulation #1) | Energy (kcal/mol) (Simulation #2) | RASAS (Simulation #1) | RASAS (Simulation #2) | Position |
| 1 | K112† T113 S115 T118 E121 † K122 | −51.91±44.01 | −151.79±51.69 | 0.79±0.09 | 0.51±0.09 | Far side away from the Snurportin, on convex side |
| 2 | Y240 E243 † | −131.36±23.60 | −83.90±60.09 | 0.46±0.13 | 0.46±0.13 | Far side away from the Snurportin, on convex side |
| 3 | K253 † N256 T285 L289 M292 Q293 | −69.37±32.53 | −18.90±7.86 | 0.85±0.08 | 0.58±0.09 | Far side away from the Snurportin, on convex side |
| 4 | K446 † D447 K455† | −70.70±72.48 | −8.19±20.41 | 0.83±0.18 | 0.99±0.03 | Next to the RanGTP, concave side |
| 5 | T477 Q481 N485 R515 K522 D523 | −20.77±7.51 | −24.79±42.40 | 0.67±0.06 | 0.73±0.11 | Next to the Snurportin-NES binding site, on convex side |
| 6 | R556 † Q593 K594 R596 † R597† | −223.59±107.39 | −223.17±63.76 | 0.64±0.15 | 0.66±0.08 | Near Snurportin, on the concave side |
| 7 | N675 V676 D677† K680 D681P682 E726† | −79.66±41.98 | −0.27±3.46 | 0.70±0.10 | 1.00±0.01 | Immediately next to Snurportin on convex side |
| 8 | E954 † E955 † K995 E1047 † | −125.01±44.76 | −127.33±67.04 | 0.78±0.09 | 0.87±0.07 | Far side away from Snurportin |
| 9 | D1007† K1012 E1013 | −58.68±42.29 | −60.00±44.12 | 0.80±0.12 | 0.92±0.06 | Next to RanGTP, concave side, away from Snurportin; blocked by helix H20B in absence of RanGTP |
| 10 | R55 * † K92 * † | −180.08±70.77 | −37.86±31.57 | 0.44±0.14 | 0.72±0.14 | Side of Snurportin near convex side |
| 11 | E42 * † R46 * D110 * † V111 * P112 * S113* | −155.62±51.86 | −0.54±5.73 | 0.69±0.06 | 0.98±0.03 | Far edge of Snurportin |
Binding sites are sorted according to their position in the amino acid sequence. There are nine binding sites on CRM1 with the total number of 42 residues and two binding sites on Snurportin with the total number of eight residues. In the second column, functional residues predicted by SPPIDER I, salt bridge-making residues, conserved residues, and residues belonging to Snurportin are distinguished by different notations (see below). Moreover, the average interaction energy and RASAS are shown for two simulations in next columns. Notations:
Bold face: Residues which were predicted by SPPIDER as functional interfacial amino acids (21 AAs).
Residues which form a salt bridge (19 AAs). The cutoff is set to 3.2 Å.
Underlined: Residues which are fully conserved (20 AAs).
*Residues from Snurportin.