TABLE 2.
Fitting of E-glycoprotein and Fab structures into cryo-EM reconstructions
| Structure | pH | sumfa | Clashb (%) | −Denc (%) | θ1d | θ2 | θ3 | cxe | cy | cz |
|---|---|---|---|---|---|---|---|---|---|---|
| 8B10 | ||||||||||
| E1E2 | 7.6 | 36.2 | 0.0 | 2.8 | 184.5 | 80.2 | 175.0 | 21.9 | 88.4 | 277.3 |
| Fab | 7.6 | 31.4 | 0.0 | 2.1 | 200.0 | 10.3 | 200.0 | 22.7 | 94.3 | 337.8 |
| 5F10 | ||||||||||
| E1E2 | 7.6 | 37.2 | 0.0 | 1.9 | 185.0 | 80.5 | 178.0 | 23.6 | 88.7 | 275.7 |
| 6.0 | 36.8 | 0.0 | 1.5 | 185.8 | 80.0 | 179.2 | 23.9 | 89.2 | 274.1 | |
| Fab | 7.6 | 29.7 | 0.0 | 9.6 | 98.0 | 359.3 | 260.8 | 14.3 | 103.2 | 294.8 |
| 6.0 | 30.3 | 0.0 | 9.8 | 97.1 | 360.5 | 260.7 | 14.0 | 101.4 | 294.3 | |
a
Average density for all atomic positions normalized to the highest density in the map (set to 100).
b
Percentage of clashes between symmetry-related atoms.
c
Percentage of atoms positioned in negative density.
d
θ1, θ2, and θ3 are the Eulerian angles (°) that rotate the coordinates from their initial to fitted positions.
e
cx, cy, and cz (Å) are the final center positions of the molecules after fitting.