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Table 3 Rosetta multi-objective reduction technique.

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

Rosetta Energy Function

 

Native PDB Id

Ω PF reduction

Minimum lRMSD (Ã…)

  

( r = | Ω PF |/| Ω | )

Ω

Ω TE ( r )

Ω PF

Ω TE (5%)

Ω TE (10%)

Ω PC (5%)

Ω PC (10%)

1

1dtdB

1%

6.7

10.8

9.1

10.6

10.2

10.2

8.6

2

1isuA

2%

6.5

8.9

8.6

8.9

8.6

8.0

7.5

3

1c8cA

2%

5.6

7.9

7.1

7.8

7.0

7.1

6.8

4

1sap

3%

6.1

7.4

7.1

7.4

6.8

6.8

6.6

5

1hz6A

3%

2.5

2.8

2.8

2.8

2.6

2.7

2.6

6

1wapA

1%

7.4

8.8

8.8

8.5

8.5

8.8

8.1

7

1fwp

3%

6.1

7.2

7.0

7.1

7.1

7.2

6.9

8

1ail

> 1%

4.8

8.2

6.2

7.6

7.5

7.5

6.9

9

1aoy

2%

6.2

10.1

9.1

9.2

9.2

9.3

9.2

10

1cc5

1%

5.0

6.3

6.3

5.7

5.7

5.5

5.4

11

2ezk

1%

3.9

9.1

6.2

5.2

5.1

5.1

4.9

12

1hhp

3%

10.8

13.9

12.6

13.9

13.6

13.0

12.9

13

2hg6

2%

10.6

12.2

11.5

12.0

12.0

12.0

11.7

14

3gwl

1%

7.1

8.9

8.5

8.7

8.4

8.0

7.8

15

2h5nD

1%

8.9

13.0

10.4

12.3

12.1

12.2

11.4

  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 Rosetta 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%.