Table 4. Data collection parameters and refinement statistics.
Data collection | C5685•mAChE |
PDB entry code | 4A23 |
Space group | P212121 |
Unit cell dimensions (Å) | 78.9×111.8×227.0 |
Resolution range (Å) | 19.64–2.40 (2.4–2.53) |
Total number of reflections | 585242 (85350) |
Unique reflections | 79036 (11407) |
Completeness (%) | 99.6 (99.8) |
Multiplicity | 7.4 (7.5) |
R merge 1 | 0.053 (0.358) |
Mean(I)/sd(I) | 25.8 (7.5) |
Refinement | |
R-factor2/R free 3 (%) | 17.5/20.9 |
B-factor4 (Å2) | 48.24 |
Number of water molecules | 871 |
RMSD from ideal values | |
Bond lengths (Å) | 0.008 |
Bond angle (°) | 1.135 |
Ramachandran plot %/no. of residues | |
Most favoured regions | 1030 (97.2%) |
Allowed regions | 26 (2.5%) |
Residues in disallowed regions | 4 (0.4%)5 |
Rmerge = (∑|I−<I>|)/∑I, where I is the observed intensity and <I> is the average intensity obtained after multiple observations of symmetry related reflections.
R-factor = (∑∥Fo|−|Fc∥)/∑Fo, where Fo are observed and Fc calculated structure factors.
Rfree uses 2% randomly chosen reflections defined in Brunger [77].
B-factor is the mean factor for protein main chain A/B.
Corresponds to Ala 342, Ala542, Lys496 and Ser497of the B monomer.