Table 3. Common Spatial Occupancy Group One (CASOG-1) tiling atoms.
VP1 + VP2 + VP3 External | |||||||||||
VP1-PRO1 | VP1-PRO2 | VP1-PRO3 | |||||||||
PDB | Protein | Orientation | Res. | Atom | Res. | Atom | Res. | Atom | |||
1AYM | HRV-A16 | CASOG ONE | P | 146 | 1162 | P | 128 | 3305 | P | 135 | 5375 |
1BEV | EV-G5-27 | CASOG ONE | P | 147 | 1024 | P | 128 | 3048 | P | 135 | 5009 |
1D4M | EV-B-CV-A9 | CASOG ONE | P | 148 | 1170 | P | 128 | 3207 | P | 136 | 5266 |
1EAH | EV-C-PV2 | CASOG ONE | P | 161 | 1046 | P | 128 | 3207 | P | 136 | 5266 |
1HXS | EV-C-PV1-M | CASOG ONE | P | 161 | 1141 | P | 128 | 3227 | P | 136 | 5376 |
1OOP | EV-B5-SVDV | CASOG ONE | P | 147 | 1072 | P | 183 | 1343 | P | 249 | 1871 |
1PIV | EV-C-PV3-S | CASOG ONE | P | 161 | 1127 | P | 128 | 3223 | P | 136 | 5378 |
1TME | TMEV-1 | CASOG ONE | P | 147 | 1147 | P | 132 | 2920 | P | 131 | 4997 |
1V9U | HRV-A2 | CASOG ONE | P | 147 | 1047 | P | 128 | 3077 | P | 135 | 5161 |
1Z7S | EV-C-CV-A21 | CASOG ONE | P | 156 | 1107 | P | 128 | 3204 | P | 135 | 5338 |
3VBH | EVA-71-1 | CASOG ONE | P | 157 | 1188 | P | 128 | 3240 | P | 137 | 5243 |
4CEW | EVA-71-2 | CASOG ONE | P | 157 | 1188 | P | 128 | 3238 | P | 137 | 5241 |
4Q4Y | EV-C-CV-A24 | CASOG ONE | P | 163 | 1114 | P | 128 | 3222 | P | 135 | 5372 |
4WM7 | EV-D68-4WM7 | CASOG ONE | P | 149 | 1079 | P | 128 | 3154 | P | 135 | 5123 |
Table 3 lists specific proline main chain oxygens in the VP1, VP2, and VP3 proteins of CASOG-1 VP1234 crystal structures. These atoms were superposed onto consecutive PICORNAVIRUS TILING POINTS having a chain identifier of “1” (i.e., the VP1-PRO1, VP2-PRO1, and VP3-PRO1 atoms were first superposed onto PICORNAVIRUS TILING POINTS 1, 2, 3, then onto 4, 5, 6, and lastly onto 7, 8, 9). The residues containing the Table 3 proline atoms are aligned in Figure 1 Sections F-1 and D-14. Figure 3 illustrates the three separate superpositions of VP1234 required to construct a CASOG-1 picornavirus capsid tiling piece (3xVP1234). The constructed CASOG-1 picornavirus capsid tiling pieces are shown in Figure 4. Proline residues listed are flanked by an “*” in Figure 1.
Table 3
Weininger, A.; Weininger, S. (2016)
“Common Features in Picornaviruses, Alpha-bungarotoxin, Myelin P2, and CRABP Suggest
Structural Bases for Multiple Sclerosis, Guillain-Barré Syndrome, and Paralysis Induction”
http://www.weiningerworks.com/picornavirus_monograph.html#Table3