Table 3. Residue-specific interactions.
| % access*
|
Neighboring residues in van der Waals contacts
|
% Identity
|
||
|---|---|---|---|---|
| Residue | WT | K24nL | ||
| F6 | 2.5 | 1.9 | F10, R14, F17 | 100 |
| F10 | 7.6 | 3.8 | F6, V9, F17, K29, K32, L34 | 91 |
| F17 | 2.1 | 4.9 | F6, F10, M12, L20, Q25, L28, K29 | 87 |
| L20 | 16.9 | 17.5 | M12, F17, P21, K24, L28 | 74 |
| L28 | 17.3 | 5.9 | F10, F17, L20, K24, H27 | 70 |
| L34 | 17.7 | 22.4 | F10 | 96 |
| F35 | 66.7 | 53.3 | L1, F6, F10, K29, L34 | 100 |
| D3 | 38.7 | 37.9 | R14 | 61(D/E) |
| R14 | 28.7 | 31.1 | F6, L1, D3 | 70(R/K) |
| Q25 | 12.0 | 10.7 | F17, L22, A18, L20 | 57(39 K/R) |
| K24 | 23.7 | 17.1 | L20, P21, W23, H27, L28 | 87(9 R) |
| K29 | 16.7 | 13.1 | F10, F17, Q25, Q26, F35 | 91(9 R) |
Van der Waals interactions <4 Å, with those between the core Phes and residues residing in a different helix are given in italics. Interactions that are observed in the x-ray structures but not in the NMR structure 1VII are shown in bold. The sequence identity is based on a comparison of villin from 23 species (8).
*
Values are given for WT (pH 6.7) and K24nL (pH 7.0); values for the other two structures are similar.