TABLE 3.
Crystallographic data for the M5 variant of cathepsin K·E64·C4-S complex
| Crystallographic data | |
| Space group | C2 |
| Unit cell constants | |
| a, b, c (Å) | 140.56, 42.01, 87.51 |
| α, β, γ | 90.0°, 94.19°, 90.0° |
| Data collection | |
| Temperature (K) | 100 |
| Detector | ADSC Q210 (ALS)a |
| Wavelength (Å) | 1.11587 |
| Resolution (Å) | 50-2.25 |
| High resolution shell (Å) | 2.33-2.25 |
| Total observations | 88,259 |
| Unique reflections | 24,692 (2411)b |
| Redundancy | 3.6 (3.4)b |
| I/σ(I) | 10 (2.5)b |
| Completeness (%) | 99.6 (98.3)b |
| Rsym (%) | 13.3 (53.5)b |
| Structure Refinement | |
| Refinement resolution (Å) | 40-2.25 |
| Unique reflections (all/test) | 24,685/1256 |
| Rwork/Rfreec(%) | 17.5/23.6 |
| No. of atomsd | 3286/50/90/260 |
| r.m.s.d. from idealitye | |
| Bond lengths (Å) | 0.010 |
| Bond angles | 1.295° |
| Ramachandran plot for the M5 variant of cathepsin K | |
| Favored (%) | 96.5 |
| Allowed (%) | 3.5 |
| Outliers (%) | 0.0 |
| Mean B factors (Å2)f | 24.1/30.0/58.3/31.5 |
a ADSC, Area Detector System Corporation; ALS, Advanced Light Source at Lawrence Berkeley Laboratory, the beamline 8.3.1.
b Values within parentheses refer to the highest resolution shell.
c Rfree was calculated using 5% of all unique data.
d Number of non-hydrogen atoms of M5/non-hydrogen of E64 inhibitor atoms/non-hydrogen atoms of C4-S/water molecules.
e r.m.s.d. indicates root mean square deviation.
f Mean B factors for protein, inhibitor, oligosaccharide, and water, respectively.