Table 2. Intrahelical angles and distances for Ca2+-S100A1 and other Ca2+-S100 structures.
Intrahelical angles and distances were calculated using UCSF Chimera and previously established methods (Drohat et al., 1998 ▸).
Intrahelical angles (°) | Intrahelical distances (Å) | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
R.m.s.d. (Å) | I to II | I to III | I to IV | II to III | II to IV | III to IV | I to II | I to III | I to IV | II to III | II to IV | III to IV | |
S100A1 (X-ray)† | 0.5 | 140.0 | −116.5 | 127.4 | 103.4 | −28.8 | 110.2 | 8.1 | 16.8 | 11.3 | 9.9 | 13.9 | 9.1 |
S100A1 (NMR)‡ | 2.6 | 133.3 | −106.5 | 129.4 | 117.5 | −33.0 | 119.7 | 9.8 | 19.5 | 13.4 | 10.2 | 12.4 | 8.5 |
S100A1–RyRP (NMR)§ | 2.5 | 137.8 | −94.4 | 123.5 | 121.5 | −40.6 | 137.2 | 9.7 | 19.3 | 12.4 | 10.4 | 12.6 | 9.9 |
S100A4 (X-ray)¶ | 1.5 | 140.2 | −112.6 | 131.3 | 106.2 | −34.9 | 108.5 | 8.1 | 17.2 | 11.1 | 10.0 | 13.6 | 8.8 |
S100B (X-ray)†† | 1.0 | 138.7 | −126.6 | 126.7 | 93.8 | −36.6 | 100.1 | 8.7 | 17.3 | 11.0 | 9.5 | 13.9 | 9.0 |
S100B (NMR)‡‡ | 2.9 | 131.9 | −124.0 | 124.3 | 103.4 | −38.7 | 103.1 | 10.4 | 20.1 | 12.1 | 10.2 | 13.2 | 9.9 |
S100Z (X-ray)§§ | 0.7 | 136.2 | −107.6 | 131.8 | 116.2 | −25.6 | 112.7 | 7.6 | 17.0 | 11.2 | 9.7 | 12.7 | 8.9 |
The r.m.s.d. for the S100A1 crystal structure corresponds to the average alignment of each monomer in the asymmetric unit.