Both feet showed marked varus alignment of the heel, rather rigid than unstable joints with diffuse ankle joint pain VAS 8-9.
At seven positions in the HEAT alignment and nine positions in the ARM alignment (marked by asterisks in Fig. 2) we found the frequency of hydrophilic residues (D,E,H,K,N,Q,R) to be less than 4%; on average only 1.6% in HEAT and 1.3% in ARM.
Anisotropy of blueschists is also marked because of alignment of anisotropic amphiboles and epidotes (Bezacier, et al. 2010b).
Also we showed other alanine substitutions in the alignment (marked with stars).
Where intron/exon structure is available, intron position was marked on an alignment (as in Figure 1) of predicted protein sequences.
# Through entire manuscript the Authors state, that there is "change in amino acids R- > K", but those residues are marked on sequence alignment to be in different places.
The HLH region is composed of two hydrophobic α-helices linked by a divergent loop and is marked by the alignment of amino acids of subfamilies 2 and 24 in Figure six (A).
G1 domain, binding α-phosphate, was predicted in β1 sheet, G2-G3 domain, binding γ-phosphate, in β2 sheet and G4 domain, binding guanine ring, in β4-β5 loop (marked in the alignment in Additional file 2).
It is known that aspartic proteases undergo a post-translational modification whereby about 60 residues are cleaved from the N-terminus of the proenzyme producing the mature protein and the predicted cleavage points of these proteins are also marked in the alignment.
