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Table 2 Correspondence between conserved hydrophobic residues in multiple alignments and packing residues in 3D structure

From: Implication of the cause of differences in 3D structures of proteins with high sequence identity based on analyses of amino acid sequences and 3D structures

3α structure
Conserved hydrophobic residues 9-L, 12-A, 16-A, 20-L, 29-Y, 32-L(+), 33-I, 36-A, 39-V, 42-V, 45-L(+), 49-I
Packing residues in 2LHC 16-A, 20-L, 30-F, 33-I, 42-V, 45-L
Packing residues in 2LHG 16-A, 20-L, 25-I, 33-I, 42-V, 45-L
4β + α structure
Conserved hydrophobic residues 5-L(+), 20-A(+), 21-V, 23-A(+), 26-A, 30-F(+), 34-A(+), 43-W, 45-Y, 52-F(+), 54-V
Packing residues in 2LHD 16-A, 20-L, 26-A, 30-F, 34-A, 43-W
Packing residues in 2LHE 16-A, 20-L, 25-I, 34-A, 43-W
  1. "+" denotes a site in multiple alignment with more than 85% conservation.