The authors note that Fig. 4 and Fig. S4 appeared incorrectly. The corrected figures and their legends appear below. The SI has been corrected online.The authors also note that on page 1 of the supporting information, right column, second full paragraph, lines 5-13, "The starting structure was solvated in a 62 × 129 × 69-Å TIP3 water box (6) with 54 chloride ions to neutralize the system, resulting in 53,872 atoms. The system was minimized for three consecutive 500-conjugate gradient steps, during which the protein was first held fixed; next, only the heavy atoms of the protein were held fixed, and finally, all atoms were allowed to move. After the energy minimizations, the system was heated gradually from 0 K to 310 K over 52 ps, and the temperature was maintained using Langevin dynamics" should instead appear as "The starting structure was solvated in a 68 × 116 × 79-Å TIP3 water box (6) with 53 chloride ions to neutralize the system, resulting in 59,606 atoms. The system was minimized for two consecutive 500-conjugate gradient steps, during which the protein was first held fixed; next, only the heavy atoms of the protein were held fixed. After the energy minimizations, the system was heated gradually from 0 K to 310 K over 9.3 ps, and the temperature was maintained using Langevin dynamics. Subsequently, the system was equilibrated by 4 rounds, first the heavy atoms were held fixed, then only backbone atoms, then only Cα atoms, and finally all atoms were allowed to move." These errors do not affect the conclusions of the article.A B C Fig. 4. Steered molecular dynamics (SMD) simulation of CD44 HABD by pulling force. (A) Snapshots of the HABD-HA8 complex at 0 ns (Left) and 3.5 ns (Right) during the SMD simulation. In the SMD simulation, the Cα carbon of the C-terminal residue Ile173 (gray sphere) was pulled at 10 Å/ns in the indicated direction (arrow), whereas the C2 atom of the N-acetylglucosamine residue (green sphere) was kept fixed. In the snapshot after 3.5 ns in the SMD simulation, the C-terminal mechanosensitive latch was completely separated from the α1 helix. (B) The time course of the hydrogen bond donor-acceptor distances between HA NAG1177 and I100 (red) and E52 and Y166 (blue). (C) Schematic depiction of the mechanosensitive latch in the force-induced conformational change of CD44 HABD.