Table 1.
Aux-C20/ATPase domain docking energies, buried surface areas, and convergence statistics
| Good set | Nonconverged set | |
| Interaction energies (kcal/mole): | ||
| A. Direct electrostatic | −159 ± 6 | −93 ± 35 |
| B. van der Waals | −42 ± 7 | −31 ± 6 |
| C. Desolvation enthalpy | +183 ± 12 | +115 ± 38 |
| D. Desolvation free energy | +124 ± 15 | +93 ± 17 |
| A + B + D | −76 ± 5 | −31 ± 27 |
| Buried interface surface (Å2): | ||
| Buried hydrophobic | 606 ± 162 | 362 ± 115 |
| Buried hydrophilic | 582 ± 100 | 428 ± 145 |
| Buried conserved Aux-C20 | 239 ± 67 | 177 ± 53 |
| Buried conserved ATPase | 569 ± 55 | 455 ± 85 |
| Backbone RMSD (Å)a | ||
| All initial Aux-C20 combined | 9.4 | |
| Initial Aux-C20 by set | 5.3 | 11.2 |
| Final Aux-C20 by set | 2.1 | 10.0 |
a For residues 814–905 of auxilin, found by aligning the ATPase domain. Combined and “nonconverged” set RMSD calculations did not include control structures with purposely “incorrect” initial structures (see Materials and Methods).