Table 1.
Protein | Best memory
|
Predicted structure EF-15
|
Predicted structure EF
|
|||||
---|---|---|---|---|---|---|---|---|
NRES | Q | %I | rms*† | Q | rms* | Q | rms* | |
1r69 | 63 | 0.89 | 52.4 | 0.85 | 0.73 | 2.17 | 0.68 | 6.08 |
1utg | 70 | 0.90 | 55.7 | 0.78 | 0.31 | 8.30 | 0.53 | 6.58 |
3icb | 75 | 0.52 | 28.0 | 3.28 | 0.57 | 3.51 | 0.60 | 3.38 |
5pal | 109 | 0.89 | 44.4 | 0.85 | 0.62 | 3.69 | 0.77 | 2.33 |
1ccr | 112 | 0.87 | 57.4 | 1.39 | 0.79 | 1.96 | 0.80 | 2.4 |
1res | 43 | 0.48 | 16.3 | 13.02 | 0.33 | 6.84 | 0.42 | 7.77 |
1hyp | 75 | 0.43 | 22.7 | 5.46 | 0.32 | 8.14 | 0.29 | 12.13 |
5cyt(R) | 103 | 0.75 | 34.3 | 1.56 | 0.32 | 9.99 | 0.44 | 5.94 |
The Protein Data Bank designation of the protein is listed in column 1. The next four columns list the number of residues (NRES), the degree of sequence identity of the target with the most homologous structure in the memory set as well as the Q-score and rms deviation. Columns 6 and 7 give the Q-score and rms deviation for predicted structures using the EF-15 (γn=3) values with respect to the correct structure, and the last two columns given the results for using EF (γn=2 values).
Based on Cα atoms.
Based on alignment to homolog.