Table 4.
Component placement scores for individual secondary-structure elements between filled and empty capsids (50)
Protein name | Residue range(s) | Secondary-structure-element type | Translation (Å) | Rotation (°) |
---|---|---|---|---|
VP1 | 64–68 | α-Helix | 4.7 | 1.0 |
101–109 | α-Helix | 4.6 | 1.0 | |
160–163 | α-Helix | 4.6 | 1.0 | |
210–213 | α-Helix | 4.4 | 1.0 | |
72–80, 116–127, 179–183, 232–243 | β-Sheet | 4.8 | 1.0 | |
90–94, 141–147, 169–173, 218–223 | β-Sheet | 4.7 | 1.0 | |
112–114, 246–248 | β-Sheet | 4.5 | 1.0 | |
VP2 | 81–89 | α-Helix | 4.1 | 4.4 |
170–175 | α-Helix | 3.2 | 4.4 | |
60–62, 96–102, 188–193, 230–239 | β-Sheet | 3.0 | 4.4 | |
69–73, 112–119, 178–182, 210–218 | β-Sheet | 3.1 | 4.4 | |
5–9, 12–16 | β-Sheet | 2.7 | 4.4 | |
VP3 | 43–47 | α-Helix | 4.3 | 4.2 |
99–104 | α-Helix | 4.0 | 4.2 | |
145–148 | α-Helix | 1.9 | 4.2 | |
81–86, 129–135, 152–157, 189–194 | β-Sheet | 2.5 | 4.2 | |
70–73, 114–120, 163–168, 207–216 | β-Sheet | 2.9 | 4.2 | |
109–111, 221–223 | β-Sheet | 4.0 | 4.2 |