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Table 2 Dependence of performance of perturbation-based scores on various properties of protein structures and conformational changes evaluated by the average (⟨Z⟩) and standard deviation (σ Z ) of the Z scores (statistics of the long list).

From: Large-scale evaluation of dynamically important residues in proteins predicted by the perturbation analysis of a coarse-grained elastic model

Property

Range

⟨Z⟩(σ Z ) of

  

δf i

δλ m, i

Size

100–153

-1.14(1.34)

-1.30(1.24)

-1.08(1.44)

 

153–263

-1.72(1.55)

-1.90(1.41)

-1.32(1.59)

 

263–804

-2.48(1.91)

-2.22(1.69)

-2.36(1.81)

RMSD

1.00–1.40

-1.71(1.96)

-1.71(1.58)

-1.58(1.76)

 

1.40–2.28

-1.65(1.53)

-1.95(1.48)

-1.62(1.79)

 

2.28–20.85

-2.09(1.62)

-1.78(1.48)

-1.66(1.64)

Max overlap

0.05–0.27

-1.61(1.55)

-1.75(1.48)

-1.25(1.58)

 

0.27–0.37

-1.85(1.66)

-1.80(1.50)

-1.57(1.79)

 

0.37–0.82

-1.93(1.91)

-1.88(1.58)

-1.97(1.71)

Collectivity

0.01–0.13

-1.81(1.68)

-1.97(1.43)

-1.49(1.59)

 

0.13–0.33

-1.84(1.66)

-1.85(1.58)

-1.69(1.70)

 

0.33–0.79

-1.76(1.82)

-1.61(1.52)

-1.64(1.86)

DynDom domain partition

success

-1.68(1.63)

-1.77(1.45)

-1.47(1.61)

 

fail

-2.11(1.88)

-1.92(1.67)

-1.93(1.94)