Table 2.
Structural Analytics of TTR Steric Zippers
| Peptide sequence | A. Rosetta relax energy (kcal/mol) | B. Distance sheet‐sheet ± S.D. (Å) | C. Distance strand‐strand (Å) | D. Area buried (Å2) | E. Shape Complementarity | F. Solvation Energy |
|---|---|---|---|---|---|---|
| 28VAVHVF33 | −17.6 (–2.93) | 9.7 ± 0.2 | 4.82 | 89 | 0.57 | 1602 |
| 37AADTWE42 | −16.6 (–2.77) | 8.8 ± 0.1 | 4.70 | 150 | 0.75 | 264 |
| 68IYKVEI73 | −23.6 (–3.93) | 8.0 ± 0.1 | 4.80 | 114 | 0.77 | 1839 |
| 80KALGIS85 | −14.3 (–2.38) | 7.7 ± 0.1 | 4.74 | 152 | 0.71 | 1669 |
| 91AEVVFT96 | −21.4 (–3.57) | 9.3 ± 0.5 | 4.77 | 131 | 0.82 | 1651 |
| 105YTIAAL110 | −21.2 (–3.53) | 9.4 ± 1.0 | 4.79 | 131 | 0.74 | 1683 |
| 106TIAALLS112 | −25.8 (–3.69) | 8.7 ± 0.6 | 4.80 | 152 | 0.67 | 2170 |
| 119TAVVTN124 | −17.0 (–2.83) | 8.2 ± 0.8 | 4.75 | 129 | 0.87 | 917 |
A. Rosetta relax energies calculated from the reported structures by each strand. In parenthesis, average Rosetta relax energies by residue. B. Sheet‐to‐sheet distances are calculated as the average distance between third degree polynomial fits to backbone atoms of opposite β‐sheets, which have been projected down the “fibril” axis. The standard deviation is also reported. C. Strand‐to‐strand distance of parallel sheets is given by the corresponding unit cell length. For in‐register antiparallel sheets, it is calculated as this unit cell length divided by two. For out‐of‐register antiparallel sheets, it is taken as an average over stacked backbone atoms of strand n and n + 2. D. Area buried is calculated as the difference between the solvent accessible surface area of one β‐sheet alone and the same β‐sheet when is in contact with the opposite β‐sheet17. The average area buried per β‐strand is reported. E. Shape complementarity values are calculated for interfaces between opposing sheets of ten β‐strands each.18