TABLE 2.
Comparison of fractional secondary structure composition in inhibitor-free and inhibitor-bound crystal structures of Eg5
Secondary structure assignments in crystallographic data are obtained from DSSP analysis. Fractional compositions were calculated for each protein within the asymmetric unit cell and averaged, when appropriate. Subtraction values of inhibitor-bound from inhibitor-free Eg5 (1II6) structures are shown.
| Compared structures | Percentage change in secondary structure |
|||||
|---|---|---|---|---|---|---|
| β-Sheet | α helix | 310 helix | Turn | Bend | β bridge | |
| % | % | % | % | % | % | |
| (STC) 3KEN versus 1II6 | −0.7 | 1.5 | 0.0 | −1.5 | 0.8 | 0.0 |
| (monastrol) 1Q0B versus 1II6 | 3.0 | −1.4 | 1.6 | 0.3 | −0.7 | 0.0 |
| (monastrol) 1X88 versus 1II6 | 2.3 | −1.5 | 1.6 | 0.9 | −1.6 | 0.0 |
| 1YRS versus 1II6 | 0.0 | −2.4 | 1.2 | 1.2 | 0.9 | −0.3 |
| 2IEH versus 1II6 | 2.7 | −2.6 | 0.0 | 2.4 | 0.7 | −0.3 |