Extended Data Fig. 5: Analysis of the sequence composition of 320 human SH3 domains.
From: Visualizing protein breathing motions associated with aromatic ring flipping
a, Distribution of amino acid types at the position of Y526 of JIP1-SH3 following a sequence alignment of all 320 SH3 domains. b, Sequence alignment of all identified SH3 domains carrying either a phenylalanine (F) or tyrosine (Y) at the position of Y526 in JIP1-SH3. For each sequence the PCA group is indicated along with the PDB code and resolution of available crystal structures. c, Pie charts showing the distribution of amino acid types in the different SH3 domains at positions corresponding to residue 493, 517, 520 and 541 in JIP1-SH3. The pie charts are colour-coded according to the size score assigned to each amino acid type corresponding to the number of heavy atoms in their side chains (see online Methods). d, Illustration of the backbone conformation of the β-sheet formed between the 516–521 and 524–529 regions in SH3 domains with tyrosine or phenylalanine at position 526. The β-bulge conformation observed in WT JIP1-SH3 is observed in all SH3 domains for which high-resolution crystal structures are available.
