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. Author manuscript; available in PMC: 2006 Jul 7.
Published in final edited form as: Structure. 2005 Jun;13(6):893–904. doi: 10.1016/j.str.2005.03.015

Table 2.

Mobility Scores for Catalytic and Ligand Binding Residues

Active Sites Ligand Binding Sites
Enzymes <M1>cat <M2>cat <MB>cat <M1>lig <M2>lig <MB>lig
All (Set 1)
 Average over proteins 6.72 5.94 12.55 12.15 9.72 16.72
 Standard deviation 8.60 9.91 7.44 13.37 10.31 7.24
All (Set 2)
 Average over proteins 9.06 6.75 13.77
Standard deviation 9.40 8.46 9.09
Monomers (Set 1)
 Average over proteins 4.55 3.47 11.49 11.06 8.89 15.25
 Standard deviation 5.22 4.67 7.55 12.82 10.42 6.94
Multimers (Set 1)
 10GS (dimer) 21.30 41.08 24.45 27.31 23.05 25.62
 1A30 (dimer) 10.13 5.13 11.56 5.24 6.94 24.38
 1CP3 (dimer) 35.90 2.73 21.51 39.33 3.71 22.21
 1CR6 (dimer) 12.98 18.11 20.90 12.92 17.60 18.00
1ARZ (tetramer) 0.10 0.13 12.13 2.81 5.46 27.15

The mobility score 0 < Mik < 1 for a given residue, i, is the ratio of its square fluctuation to that of the residue exhibiting the highest fluctuation in the kth mode. <Mk>cat and <Mk>lig are averages taken over catalytic residues (columns 4–6) or ligand binding residues (columns 7–9) for modes k = 1 and 2. <MB>cat is the equivalent ratio based on temperature factors. The results for the reduced set (19 out of 24) of monomeric enzymes are shown separately. The last five rows display the results for selected multimeric enzymes.