Table 3. Van der Waals interactions between the propeptide and the mature protein.
As in Table 2 ▶, the majority of interactions seen are near to one of the three conformational changes described. The table shows three ‘peaks’ approximately centred on Val39, Ile67 and Thr76; these peaks correspond to the hydrophobic pocket, the S1 pocket and the S2 pocket, respectively, although part of the second peak can be attributed to residues involved in the formation of the S2 pocket. Residues were considered to be in van der Waals contact if the distance between any of their constituent atoms was less than 4.2.
| Propeptide | Mature protein |
|---|---|
| Lys34 | Thr479, Tyr480 |
| Thr35 | Tyr480 |
| Leu36 | Ile468, Gln470, Ile477, Tyr480, Phe483 |
| Asp37 | Gln470 |
| Gly38 | Ser349 |
| Val39 | Ile347, Met348, Ser349, Ile468, Glu482, Phe483 |
| Glu40 | Ile347, Met348, Glu482, Phe483 |
| Thr41 | Ser345, Lys346, Met348, Tyr447, Phe483 |
| Ala42 | Ser345, Lys346, Met348, |
| Tyr44 | Ile451, Asp452 |
| Tyr48 | Asp452, Tyr454 |
| Tyr51 | Tyr455 |
| Leu52 | Gly453 |
| Ala61 | Pro259 |
| Lys62 | Pro259 |
| Tyr63 | Gly162, Tyr455 |
| Asn64 | Asn114, Met160, Ser161, Gly162, Tyr455 |
| Gly65 | Gly162, Ser163, Leu360 |
| Val66 | Ser163, Leu260, Asn261 |
| Ile67 | Ser163, Ser164, Tyr454, Tyr455, Leu456 |
| Phe69 | Val166, Arg215, Asp320, Tyr322, Leu344 |
| Pro70 | Leu344, Ile451, Tyr455 |
| His71 | Leu344, Ser345, Ile451 |
| Glu72 | Lys346 |
| Met73 | Arg215, Thr319, Gly343, Ser345, Lys346, Asp375 |
| Glu74 | Arg215, Asp375, Ser409, Glu441 |
| Gly75 | Arg215, Asn217, Thr319, Ser409 |
| Thr76 | Val214, Arg215, Leu216, Asn217, Thr222, Tyr408, Ser409 |
| Thr77 | Asn217, Thr222 |
| Leu78 | Leu216, Glu221, Thr222, Asn225, Ala226, Tyr230 |
| Arg79 | Asp219, Glu221, Thr222, Asn225 |