Table 1. Comparison of secondary structure prediction results.
Correctly predicted, %
|
||||
---|---|---|---|---|
Helix | Sheet | Coil | ||
SS1 | Helix | 28.9 | 0.8 | 7.2 |
Sheet | 1.2 | 11.8 | 7.5 | |
Coil | 4.6 | 3.6 | 34.4 | |
SS2 | Helix | 31.2 | 0.4 | 5.2 |
Sheet | 0.5 | 14.6 | 5.5 | |
Coil | 4.5 | 4.4 | 33.7 | |
SS3 | Helix | 30.7 | 0.1 | 6.0 |
Sheet | 0.2 | 15.7 | 4.7 | |
Coil | 4.5 | 2.9 | 35.2 |
Results shown were obtained for 137 proteins with 10,127 aa by using sequence only (SS1; see ref. 13), sequence plus 1,000 rosetta models (SS2), and sequence plus native fold (SS3). SS1 yielded 78%, 58%, and 81% correctly predicted helices, sheets, and coils, respectively, with a correctly predicted average of 75%. SS2 yielded 85%, 71%, and 79% correctly predicted helices, sheets, and coils, respectively, with a correctly predicted average of 80%. SS3 yielded 83%, 76%, and 83% correctly predicted helices, sheets, and coils, respectively, with a correctly predicted average of 82%.