Supplementary Figure 3: Details of intermolecular contacts of ASF1–H3–H4 dimer complex and structural comparisons of different chaperone–H3–H4 complexes.

(a, b) Views of details of the intermolecular interactions between ASF1 and H3–H4 dimer from PDB 2IO5 (Natsume, R. et al., Nature 446, 338-341, 2007). Panel a highlighting the interactions of ASF1 with the helices α2 and α3 of H3, and panel b highlighting the interactions of ASF1 with the βc strand and C-terminus of H4. (c) Structural comparison of the ASF1–H3–H4 dimer complex (colored in silver) and our MCM2 HBD–H3–H4 dimer–ASF1 complex (in color). (d, e) Following the comparison shown in panel c, the RMSDs of residues in H3 (panel d) and H4 (panel e) were plotted respectively. The conformational differences on H3–H4 dimer caused upon binding of MCM2 HBD are spread out and include the L1 loop, the α2 helix and the L2 loop of H3 (panel d), as well as the α1 helix, the tip of α2 helix, the L2 loop and especially the α3 helix of H4 (panel e). (f) Structural comparison of one half of the MCM2 HBD–H3–H4 tetramer complex (colored in silver) with the MCM2 HBD–H3–H4 dimer–ASF1 complex (in color). (g, h) Following the comparison shown in panel f, the RMSDs of residues in H3 (panel g) and H4 (panel h) were plotted respectively.