1. Figure S5: Fig. S5
2. In the cryo-EM map, seven residues (residues 297-303) in the ?7-205 ?10 loop located on the capsid's outer surface and 3 to 10 residues from the N-206 terminus are unclear and disordered. In addition, one residue from the C-terminus 207 is disordered in some subunits. The A-domain has a ?-hinge core structure 208 composed of five ?-strands (?5, ?8, ?9, ?10, and ?14) that are well conserved 209 among all phages with a known structure;P-Domain;197 Like other phage structures, the phage KHP30 MCP consists of four basic 198 structural units: two domains (A-domain, residues 142-183, 200-253
3. P-loop; 184-199 residues) protruding to the 212 neighboring subunit, which is inserted between ?3 (following ?5) and ?8 and 213 contains an anti-parallel ?-sheet (?6 and ?7). The P-loop participates in the 214 interactions with the adjacent subunit in Hexon, as described below. The other is 215 a long loop containing two ?-helixes (?6 and ?7), which is located on the 216 outermost region in the A-domain and designated an outer segment. This outer 217 segment is not involved in interactions with surrounding subunits and exhibits 218;One is a loop
4. The tips of the E-loop 222 and P-domain are displaced by up to about 10 � and 4 � among the eight MCP 223 subunits forming Hexon, respectively (upper panel in Figure 2D). Interestingly, 224 we found that the conformations of the a-subunit and d-subunit of E-Hexon are 225 quite different from those of the other subunits. These a-and d-subunits are 226 located across the edge of the icosahedron (Figures 1A and S8). The E-loops in 227 the two subunits curve more inward than the other subunits, and generate a 228 convex curvature between the halves of the E-Hexon (Figure 1C). The E-loop of 229 the a-subunit;Structural comparisons of nine MCP subunits in an asymmetric unit showed 221 large conformational changes in the E-loop and P-domain