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. 1998 Mar 17;95(6):2932–2937. doi: 10.1073/pnas.95.6.2932

Table 1.

Results of simulated annealing for eight targets

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.