Table 1.
Data collection and refinement statisticsa
| Hs PCDH1 EC1-4bc | Hs PCDH1 EC1-4mc | Hs PCDH1 EC3-4bc | |
|---|---|---|---|
| Data collection | |||
| Space group | P6122 | P6122 | P42212 |
| Cell dimensions | |||
| a, b, c (Å) | 146.98, 146.98, 147.69 | 147.23, 147.23, 149.37 | 125.57, 125.57, 45.29 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 90 |
| Molecules per asymmetric unit | 1 | 1 | 1 |
| Resolution (Å) | 2.85 | 3.15 | 3.05 |
| I/ σ(I) | 18.3 (1.923) | 58 (2.5) | 12 (1.67) |
| Rmerge | 0.156 (1.627) | 0.078 (1.762) | 0.166 (1.027) |
| Rmeas | 0.164 (1.710) | 0.079 (1.792) | 0.175 (1.110) |
| Rpim | 0.050 (0.521) | 0.013 (0.321) | 0.054 (0.401) |
| CC1/2 | 0.998 (0.716) | 1.004 (0.794) | 0.938 (0.551) |
| CC* | 0.999 (0.913) | 1.001 (0.941) | 0.981 (0.843) |
| Completeness (%) | 100.0 (100.0) | 100.0 (99.9) | 99.3 (90.6) |
| Redundancy | 10.7 (10.6) | 36.4 (28.2) | 9.9 (6.5) |
| Refinement | |||
| Resolution (Å) | 48.26–2.85 (2.93–2.85) | 48.53–3.15 (3.22–3.15) | 44.43–3.05 (3.13–3.05) |
| No. of reflections | 22,567 | 17,231 | 7363 |
| Rwork/Rfree | 22.1/24.3 | 21.5/26.3 | 21.9/26.6 |
| No. of atoms | |||
| Protein | 3288 | 3284 | 1533 |
| Ligand/ion | 26 | 34 | 4 |
| Water | 25 | 0 | 6 |
| B-factors | |||
| Protein | 78.75 | 152.67 | 64.93 |
| Ligand/ion | 87.18 | 127.24 | 60.20 |
| Water | 47.34 | 0 | 37.05 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.010 | 0.0095 | 0.0093 |
| Bond angles (°) | 1.484 | 1.503 | 1.536 |
| Ramachandran plot (%) | |||
| Most favored | 87.8 | 83.2 | 86.0 |
| Additionally allowed | 11.7 | 16.8 | 14.0 |
| Generously allowed | 0.5 | 0.0 | 0.0 |
| Disallowed | 0.0 | 0.0 | 0.0 |
| PDB ID code | 6BX7 | 6MGA | 6PIM |
aOne crystal was used for each structure. Values in parentheses are for highest-resolution shell