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Table 3 Final Results of HopDock presented in this work.

From: HopDock: a probabilistic search algorithm for decoy sampling in protein-protein docking

PDB ID (Chains)

Size

Budda [9] (Ã…)

Prev. [16] (Ã…)

pyDock [4] (Ã…)

ClusPro [6] (Ã…)

HopDock (Ã…)

1C1Y (A,B)

2034

1.2

1.3

10.4

7.2

1.9

1DS6 (A,B)

2839

1.2

1.8

0.8

1.7

3.4

1TX4 (A,B)

2957

1.4

2.4

18.5

4.7

1.0

1WWW (W,Y)

1644

11.4

2.2

18.2

17.2

2.2

1FLT (V,Y)

1528

1.5

1.1

2.8

4.7

1.5

1IKN (A,C)

3178

1.2

2.0

20.1

19.7

2.2

1IKN (C,D)

2505

2.0

2.0

16.7

20.9

4.6

1VCB (A,B)

1447

0.7

2.1

1.4

1.9

3.6

1VCB (B,C)

1846

1.3

1.3

22.7

1.9

1.7

1OHZ (A,B)

1443

1.8

1.7

7.5

3.3

2.2

1T6G (A,C)

4022

1.6

2.5

0.1

14.8

2.5

1ZHI (A,B)

2633

25.3

1.7

23.8

24.1

3.3

2HQS (A,C)

3983

29.1

2.2

15.2

16.6

2.6

1QAV (A,B)

1503

1.4

1.0

9.6

1.7

2.6

1G4Y (B,R)

1838

0.8

2.3

26.2

1.9

4.1

1CSE (E,I)

2442

0.7

1.5

13.2

1.1

2.7

1G4U (R,S)

4188

1.0

2.2

27.6

16.1

5.6

  1. A comparative analysis has been performed on all seventeen dimers. For the comparison, two geometry-based (Budda [9] and work in [16]) and two energy-based methods (pyDock [4] and ClusPro [6]) have been chosen. Lowest lRMSD to native structure is reported for Budda in column 3, work in [16] in column 4, pyDock in column 5, ClusPro in column 6, and HopDock in column 7.