Skip to main content
. 2016 Sep 20;113(40):11294–11299. doi: 10.1073/pnas.1613286113

Table 1.

Distances across binding pocket in monomers of βI-tubulin and variants

Distance definition Distance in complex Average distance [Å] (% of snapshots with distance ≥ distance in complex)
βI-Tubulin T218A T218A.S275A
23–215 18.39 20.1 ± 0.9 (97.3) 18.9 ± 1.4 (63.5) 19.3 ± 1.4 (76.0)
23–279 23.34 26.5 ± 1.3 (99.2) 23.1 ± 2.6 (51.5) 23.8 ± 3.4 (73.3)
23–360 11.34 12.4 ± 1.6 (73.3) 12.0 ± 1.4 (67.2) 13.2 ± 1.4 (91.2)
215–279 9.8 11.3 ± 1.0 (95.2) 12.8 ± 2.5 (85.3) 12.6 ± 1.5 (97.6)
215–360 16.43 17.6 ± 1.4 (80.3) 17.5 ± 1.3 (78.7) 17.8 ± 1.8 (79.5)
279–360 16.06 18.5 ± 1.7 (90.7) 14.7 ± 2.7 (36.3) 14.9 ± 3.4 (38.9)

Distance is measured between the Cα atoms of the two residues in the definition.