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Table 3 Sites from non-regulatory pairs evolve independently despite their spatial proximity

From: Inferring Methionine Sulfoxidation and serine Phosphorylation crosstalk from Phylogenetic analyses

Group Sites Regulatory Loop Distance ∆∆G LTR p-value
A S51-I55 Yes β3/β4 6.2 −0.6 ± 1.2 27.7 1.5 10−5
A S90-K86 No β5/α1 9.2 2.1 ± 1.3 5.4 0.242
A S157-I161 No α4/α5 9.7 0.0 ± 0.8 3.9 0.420
A Y199-G203 No β6/α6 8.8 9.7 ± 4.8 0.0 1.000
A S218-M222 Yes? α6/β7 6.3 2.2 ± 2.0 15.9 0.003
A M289-E293 No CT 9.5 −0.3 ± 0.8 5.9 0.207
B C217-M222 No α6/β7 9.9 1.2 ± 2.1 2.1 0.712
B S218-M222 Yes? α6/β7 6.3 2.2 ± 2.0 15.9 0.003
B T219-M222 No α6/β7 4.9 0.6 ± 1.6 0.0 1.000
B E220-M222 No α6/β7 6.7 1.4 ± 1.6 6.5 0.164
B N221-M222 No α6/β7 5.3 1.5 ± 1.9 6.6 0.158
B P223-M222 No α6/β7 5.3 2.1 ± 1.5 10.5 0.033
C S218-C217 No α6/β7 4.4 1.6 ± 1.9 8.5 0.075
C S218-T219 ? α6/β7 4.4 0.5 ± 1.4 17.9 0.001
C S218-E220 No α6/β7 8.4 1.7 ± 1.3 12.9 0.012
C S218-N221 No α6/β7 9.7 2.0 ± 1.8 8.1 0.088
C S218-M222 Yes? α6/β7 6.3 2.2 ± 2.0 15.9 0.003
C S218-P223 No α6/β7 7.7 2.6 ± 1.4 10.5 0.033
  1. The LRTs between the models of correlated and uncorrelated evolution were computed for the indicated site pair, as well as their associated p-values. The distances, in ångströms, between residues are also given. The pairs shown in the upper part of the table (Group A) are those whose members are four residues away from each other and they are outside helices and strands. Three of these tested site pairs were found within the N-terminal domain (NTD), while the other three were located in the C-terminal domain (CTD) of the eIF2α protein. In the middle (Group B) and lower (Group C) parts of the table, the relationships between M222 and its neighbors and S218 and its neighbors, respectively, are analyzed. For each pair of sites, the thermodynamic stability change (ΔΔG) for the 400 possible double-mutants was computed and the mean ± standard deviation is shown in kcal/mol