Table 1.
Data collection and refinement statistics
| NK1R:CP-99,994a (PDB 6HLL) | NK1R:aprepitanta (PDB 6HLO) | NK1R:netupitanta (PDB 6HLP) | |
|---|---|---|---|
| Data collection | |||
| Space group | C2221 | P212121 | P212121 |
| Cell dimensions | |||
| a, b, c (Å) | 62.00, 122.73, 286.49 | 62.19, 76.45, 167.12 | 61.66, 76.57, 166.04 |
| α, β, γ (°) | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 47.88–3.27 (3.53–3.27)b | 48.24–2.40 (2.49–2.40)b | 49.50–2.20 (2.27–2.20)b |
| Rmerge | 0.689 (4.652) | 0.188 (2.879) | 0.161 (3.066) |
| Rpim | 0.173 (1.225) | 0.052 (0.795) | 0.054 (1.035) |
| I/σ(I) | 5.1 (1.1) | 12.8 (1.7) | 11.9 (1.3) |
| CC1/2 | 0.990 (0.311) | 0.999 (0.753) | 0.998 (0.666) |
| Completeness (%) | 99.9 (99.6) | 100.0 (100.0) | 99.9 (99.4) |
| Redundancy | 32.2 (29.6) | 26.2 (26.4) | 18.5 (18.8) |
| Refinement | |||
| Resolution (Å) | 24.92–3.27 | 29.44–2.40 | 29.24–2.20 |
| No. of reflections (test set) | 17,325 (874) | 31,899 (1656) | 40,668 (1997) |
| Rwork/Rfree | 0.225/0.275 | 0.201/0.229 | 0.204/0.227 |
| No. atoms | |||
| Protein | 3754 | 3832 | 3882 |
| Ligand | 22 | 37 | 42 |
| Water/ion/lipid | – | 355 | 475 |
| B-factors | |||
| Protein | 91.30 | 62.96 | 55.97 |
| Ligand | 87.89 | 54.13 | 51.20 |
| Water/ion/lipid | – | 85.90 | 82.10 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.004 | 0.003 | 0.004 |
| Bond angles (°) | 0.911 | 0.578 | 0.699 |
aThe structures of NK1R in complex with CP-99,994, aprepitant and netupitant were solved using X-ray diffraction data from 6, 6, and 5 crystals, respectively
bValues in parentheses are for highest-resolution shell