Table 2.
Coverage values obtained with the full set of SWs and the selected set (58 SWs) from the Protein Network
| Covering | STRIDE | P-SEA | PBs | ||||||||
| Databank | SWs (%) | Protein Network (%) | α-helix (%) | β-sheet (%) | coil (%) | α-helix (%) | β-sheet (%) | coil (%) | α-helix (%) | β-sheet (%) | coil (%) |
| PAPIA | 91.4 | 89.3 | 97.0 | 92.0 | 81.0 | 99.6 | 94.1 | 78.9 | 98.1 | 95.2 | 80.2 |
| culled-Pdb | 93.6 | 90.3 | 97.1 | 92.4 | 81.6 | 99.6 | 94.6 | 79.5 | 98.0 | 95.5 | 82.9 |
| SCOP-ASTRAL | 92.1 | 89.2 | 97.2 | 92.5 | 81.8 | 99.4 | 94.6 | 79.5 | 98.0 | 95.7 | 82.1 |
| Pdb-select B | 92.3 | 88.9 | 97.4 | 93.2 | 81.0 | 99.6 | 95.1 | 80.9 | 98.0 | 95.3 | 82.5 |
| mean | 92.4 | 89.4 | 97.2 | 92.5 | 81.4 | 99.6 | 94.6 | 79.7 | 98.0 | 95.4 | 81.9 |
The following two columns correspond to the repartition of coverage values of the Protein Network according to the classic secondary structures assigned with two different algorithms: STRIDE (Frishman and Argos 1995) and P-SEA (Labesse et al. 1997). The last column corresponds to the same coverage values assigned with PB m as the α-helix, the PB d as the β-sheet, and the rest as the coil state.