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Table 2 AMW multi-objective reduction technique.

From: Rapid sampling of local minima in protein energy surface and effective reduction through a multi-objective filter

AMW Energy Function
  Native PDB Id Ω PF reduction Minimum lRMSD (Å)
   ( r = | Ω PF |/| Ω | ) Ω Ω TE ( r ) Ω PF Ω TE (5%) Ω TE (10%) Ω PC (5%) Ω PC (10%)
1 1dtdB 4% 7.2 7.9 7.7 7.9 7.7 7.7 7.7
2 1isuA 7% 6.0 6.2 6.5 6.4 6.2 6.2 6.2
3 1c8cA 4% 7.4 7.5 7.5 7.5 7.5 7.5 7.5
4 1sap 2% 6.5 7.6 7.5 7.4 7.2 7.4 7.2
5 1hz6A 2% 5.9 6.7 6.3 6.7 6.7 6.7 6.6
6 1wapA 2% 7.7 8.7 8.7 8.7 8.7 8.7 8.7
7 1fwp 7% 6.4 8.1 7.3 8.1 8.1 8.1 8.1
8 1ail 2% 3.4 6.8 5.9 5.8 4.2 4.7 4.4
9 1aoy 6% 5.7 6.9 6.6 6.9 6.5 6.8 6.5
10 1cc5 7% 5.6 8.6 7.0 8.7 8.6 8.6 8.1
11 2ezk 3% 4.4 8.0 7.3 7.7 7.1 7.2 7.1
12 1hhp 1% 10.7 12.0 12.0 11.6 11.6 11.6 10.8
13 2hg6 6% 8.6 10.8 10.5 11.6 10.8 10.9 10.8
14 3gwl 5% 4.2 4.7 5.2 4.7 4.7 4.7 4.7
15 2h5nD 7% 7.9 10.7 10.0 10.8 10.4 10.4 10.4
  1. The minimum lRMSD to the native structure retained by each of the proposed multi-objective ensemble reduction techniques is given for the Ω generated with the AMW energy function. Column 3 gives the size of the Pareto front as a percentage of the size of Ω. Column 4 gives the minimum lRMSD to the native structure of any conformation in the Ω. Columns 5 and 6 give minimum lRMSD retained by Ω TE (r)and Ω PF , respectively, where r is the corresponding value from Column 3. Columns 7-10 compare the minimum lRMSD retained by Ω TE (n)and Ω PC (n)for thresholds of n = 5% and n = 10%.