Table 2. Interatomic distances between equivalent atoms in different TTR tetramers.
87/110/117 TTR mutant–wild type TTR (1F41) | 87/110/117 TTR mutant—V122I TTR mutant (5A6I) | 87/110/117 TTR mutant—87/110 TTR mutant (1GKO) |
1F41 wild typeTTR—V122I TTR mutant (5A6I) | 87/110/117 TTR mutant—4-hydroxy-chalcone—TTR complex(5EZP) | |
---|---|---|---|---|---|
Thr 96 B | 2.44 | 1.71 | 2.02 | 0.98 | 2.37 |
Thr 96 C (A’) | 1.29 | 1.97 | 2.08 | 1.73 | 1.15 |
Thr 96 D (B’) | 2.38 | 1.42 | 2.58 | 2.69 | 2.36 |
Leu55 B | 1.77 | 2.26 | 2.13 | 0.77 | 1.06 |
Leu55 C (A’) | 1.86 | 1.56 | 1.45 | 0.47 | 0.80 |
Leu55 D (B’) | 2.27 | 1.52 | 2.67 | 2.11 | 1.90 |
Ser85 B | 3.52 | 0.96 | 0.99 | 3.03 | 2.37 |
Ser85 C (A’) | 3.42 | 2.39 | 3.27 | 2.65 | 2.26 |
Ser85 D (B’) | 3.98 | 2.83 | 2.48 | 1.81 | 2.68 |
Distances (in Å) between Cα atoms for pair of proteins in subunits B, C and D, after superimposing subunit A of the models. Residues of monomer A are not indicated, since they are practically coincident. C and D labels correspond to A’ and B’ in the P21212 space group, i.e. the crystallographic two-fold axis superimposes A’ to A and B’ to B.