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. 2003 Oct 3;100(21):12105–12110. doi: 10.1073/pnas.1831973100

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%.