TABLE 2.
TrkA-d5/N-term@NGF interactions
| NGF Residues | CS (nm2)
|
 f.c. |
ΔΔ
|
||||||
|---|---|---|---|---|---|---|---|---|---|
| 1WWW | f.c. | c1 | c2 | 1WWW | f.c. | c1 | c2 | ||
| His-4 | 1.03 | 1.06 | 1.00 | 1.19 | 2.99 | 5.40 | 4.60 | 5.18 | 3.44 |
| Pro-5 | 0.47 | 0.51 | 0.57 | 0.36 | 1.47 | – | – | – | – |
| Ile-6 | 0.79 | 0.83 | 0.95 | 0.72 | −0.55 | 2.10 | 2.06 | 2.95 | 2.47 |
| Phe-7 | 0.39 | 0.49 | 0.54 | 0.25 | −0.84 | 1.27 | – | 1.44 | 1.39 |
| His-8(Gly) | 0 | 0 | 0 | 0 | 0 | – | 0.49 | – | – |
| Arg-9 | 0.44 | 0.57 | 0.53 | 1.06 | 2.52 | 0.29 | 2.11 | 2.06 | 2.99 |
| Gly-10 | 0.02 | 0.08 | 0.04 | 0.07 | – | – | – | – | – |
| Glu-11 | 0.65 | 0.68 | 0.90 | 0.83 | 6.33 | 0.69 | 2.50 | 1.83 | 2.82 |
| Phe-12 | 0.30 | 0.29 | 0.45 | 0.38 | −0.22 | 0.70 | 4.18 | 0.70 | 1.93 |
| Ser-13 | 0.34 | 0.39 | 0.10 | * | −2.13 | 0.35 | 0.35 | −0.22 | * |
Contact surface (CS) (61), electrostatic alanine scanning calculations (
(65), and binding energy hot-spot predictions 
(48,49) are reported for NGF residues from His-4 to Ser-13. The NGF/trkA-d5 full-complex (f.c.) is the last MD snapshot of the previously performed simulation (47) and the c1 and c2 conformations are those after 5.7 ns of MD.
*
In c2, Ser-13 is absent.