Table 1.

RMS deviations (Å) between crystal structures and tropomyosin models

PDB IDa	Li et al. model (2011)b	von der Ecken et al. model (2014)c
1C1G	1.91	4.76
1IC2	1.15	1.39
1KQL	1.26	1.71
3U1A	0.89	1.46
3U59	1.51	1.92
2D3E	1.65	2.85
2B9C	1.31	1.56

Root-mean-square deviation (RMSD) for the Cα-backbone atoms between tropomyosin models and crystal structures, after alignment with the rmsd-plugin of the program VMD (Humphrey et al. 1996)

^aThe splayed or non-coiled-coil ends of the crystal structures were truncated prior to RMSD calculation, the employed residues are: 1C1G, Whitby-Phillips model (2000), residues 50–175 (same as segment shown in Fig. 2a). 1IC2, N-terminal 81 residues (striated muscle α-tropomyosin, Brown et al. (2001)). 1KQL, C-terminal 31 residues (rat striated muscle α-tropomyosin, Li et al. (2002)). 3U1A, N-terminal 81 residues (chicken gizzard smooth muscle α-tropomyosin, Rao et al. (2012)). 3U59, N-terminal 98 residues (chicken gizzard smooth muscle α-tropomyosin, Rao et al. (2012)). 2D3E, 134 C-terminal residues (rabbit striated muscle α-tropomyosin, Nitanai et al. (2007)). 2B9C, residues 98–175 (rat striated muscle α-tropomyosin, Brown et al. (2005))

^bLi et al. (2011) model, shown in Fig. 1a, 2b and 3a

^cvon der Ecken et al. (2014) model, shown in Fig. 1b and 2c