TABLE 1.
Summary of crystallographic information
| CCM3 | CCM3 | |
|---|---|---|
| Protein | ||
| Space group | P212121 | P4122 |
| Cell dimensions, a, b, c (Å) | 63.1, 116.0, 123.0 | 77.4, 77.4, 108.6 |
| Resolution range (Å)a | 25–2.50 (2.59–2.50) | 25–3.05 (3.16–3.05) |
| Unique reflectionsa | 31805 | 6699 |
| Completeness (%)a | 99.1 (97.4) | 99.3 (98.0) |
| Rsym (%)a | 6.1 (66.2) | 8.4 (49.1) |
| Mn (I/σI)a | 16.3 (2.0) | 19.3 (2.7) |
| Rfactor (%)a | 22.9 (30.2) | 27.8 (34.9) |
| Free Rfactor (%)a | 28.8 (40.1) | 29.3 (41.5) |
| Residue range built | A:15–212 | 14–210 |
| B: 1–210 | ||
| C:10–210 | ||
| D: 8–210 | ||
| Free R reflections (%) | 5.1 | 4.9 |
| Free R reflections, no.a | 1600 (101) | 316 (30) |
| No. non-hydrogen protein atoms | 6655 | 1630 |
| No. water molecules | 70 | 0 |
| Model quality | ||
| RMSD bond lengths (Å) | 0.008 | 0.006 |
| RMSD bond angles (°) | 1.106 | 0.881 |
| Mean B-factors | ||
| Overall (Å2) | 79.3 | 146.5 |
| Protein atoms (Å2) | 79.5 | 146.5 |
| Protein atoms NTD (N-69) (Å2) | 58.7 | 132.9 |
| Protein atoms αE-EF linker (70–97) (A2) | 80.0 | 148.5 |
| Protein atoms FAT,(98-C) (Å2) | 90.1 | 152.5 |
| Water (Å2) | 63.2 | – |
| Ramachandran plot (%) favored/allowed/disallowed | 92.5/7.5/0 | 90.4/9.5/0 |
a Parentheses indicate the highest resolution shell.