Extended Data Table 1: X-ray crystallography data collection and refinement statistics.
Values in parentheses are for the outer shell. APS, Advanced Photon Source, Argonne National Lab; A.S.U., asymmetric unit; R.m.s., Root mean square. See Extended Data Figure 1 and Methods for further details on the ellipsoidal resolution limits.
| PcdhγB4EC1–6 | ||
|---|---|---|
| Data collection | ||
| Date | 12/0½016 | |
| Beamline | APS 24ID-C | |
| Wavelength (A) | 0.97919 | |
| Space group | P21 | |
| Cell dimensions | ||
| a, b, c (A) | 127.73, 87.58, 149.33 | |
| a, P, Y (°) | 90, 109.94, 90 | |
| Spherical resolution limits | Ellipsoidal resolution limits | |
| Resolution (A) | 40.00–4.50 (5.03–4.50) | 40–6.0/6.8/4.5 (5.05–4.52) |
| No. of reflections | 49398 (13826) | 24717 (966) |
| Unique reflections | 17427 (4999) | 8694 (317) |
| Rmerge | 0.207 (1.921) | 0.112 (0.173) |
| Rmeas | 0.254 (2.366) | 0.138 (0.211) |
| Rpim | 0.145 (1.359) | 0.078 (0.119) |
| CC(½) | 0.993 (0.741) | 0.995 (0.973) |
| I/σI | 2.7 (0.6) | 5.2 (5.7) |
| Spherical completeness (%) | 93.8 (94.9) | 46.7 (5.6) |
| Ellipsoidal completeness (%) | 93.6 (97.2) | |
| Redundancy | 2.8 (2.8) | 2.8 (3.0) |
| Refinement | ||
| Resolution (A) | 40–6.0/6.8/4.5 | |
| Unique reflections | 8683 | |
| Completeness in diffracting ellipsoid (%) | 93.4 | |
| Rwork / Rfree (%) | 23.1 / 27.7 | |
| Molecules in A.S.U. | 2 | |
| Number of atoms | ||
| Protein | 9489 | |
| Ligand/Ion | 253 | |
| Water | 0 | |
| B-factors | ||
| Protein | 138.19 | |
| Ligand/Ion | 157.81 | |
| Water | 0 | |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.002 | |
| Bond angles (°) | 0.565 | |
| Ramachandran Favored (%) | ||
| Favored (%) | 96.96 | |
| Allowed (%) | 3.04 | |
| Outliers (%) | 0.00 | |
| Rotamer outliers (%) | 0.67 | |
| Wilson B | 66.09 | |
| PDB ID | 6E6B | |