Table 3.
Rotamers changes in the ecRBP (1URP molecule A/2DRI) and tmRBP (apoprotein molecule A/ribose-bound form) binding pocket residues.
| ecRBP | tmRBP | |||||||||
| Δχ1 (°) | Δχ2 (°) | Δχ3 (°) | Δχ4 (°) | (Σ|Δχ|)/Nχ(°) | Δχ1 (°) | Δχ2 (°) | Δχ3 (°) | Δχ4 (°) | (Σ|Δχ|)/Nχ(°) | |
| ASN13 | 12 | -13 | 13 | 13 | -1 | 7 | ||||
| PHE15 | -1 | 16 | 8 | 26 | -173 | 100 | ||||
| PHE16 | -7 | 10 | 8 | -17 | 26 | 22 | ||||
| ASP89 | -18 | 17 | 18 | -1 | 19 | 10 | ||||
| ARG90 | 26 | -17 | -27 | 70 | 35 | -1 | -5 | 5 | 0 | 3 |
| ARG141/148 | -1 | -12 | -7 | -6 | 6 | 0 | -12 | 4 | -19 | 9 |
| PHE164/172 | 0 | 0 | 0 | 1 | 4 | 3 | ||||
| ASN190/198 | -7 | -4 | 5 | 4 | -8 | 6 | ||||
| ASP215/223 | 14 | 4 | 9 | -1 | 6 | 3 | ||||
| ↑GLN235/244 | -20 | -7 | 45 | 24 | -3 | 9 | -29 | 14 | ||
C-terminal amino acids are in bold face type; the hinge amino acid that interacts with ribose is indicated by an arrow. Where amino acid numbering differs, ecRBP residues are listed first.