TABLE 1.
Crystal structure data collection and refinement statistics
| Data collection | Chimera B1 | Chimera B3 |
|---|---|---|
| Space group | P61 | P61 |
| Cell dimensions | ||
| a, b, c | 299.3, 299.3, 47.9 Å | 173.2, 173.2, 47.9 Å |
| α, β, γ | 90, 90, 120° | 90, 90, 120° |
| Wavelength | 0.98 | 0.98 |
| Resolutiona | 25 to 2.0 Å (2.03 to 2.0 Å) | 25 to 2.0 Å (2.03 to 2.0 Å) |
| Rmergea | 6.3 (38.5) | 5.8 (30.1) |
| I/σIa | 11.9 (3.8) | 15.8 (6.1) |
| Completenessa | 99.8% (99.7%) | 99.9% (100%) |
| Redundancya | 5.1 (4.3) | 6.2 (6.1) |
| Refinement | ||
| Resolutiona | 25 to 2.0 Å (2.03 to 2.0 Å) | 25 to 2.0 Å (2.03 to 2.0 Å) |
| No. reflectionsb | 158,213 (8364) | 52,933 (2833) |
| Rwork / Rfreec | 0.219/0.254 | 0.148/0.178 |
| No. of atoms | ||
| Protein | 11,832 | 3958 |
| Water | 1586 | 535 |
| Ligand | 139 | 63 |
| Wilson B-factor | 23.0 | 25.3 |
| Average B-factor | ||
| Protein | 14.6 Å2 | 21.2 Å2 |
| Water | 40.8 Å2 | 41.4 Å2 |
| Ligand | 26.9 Å2 | 43.5 Å2 |
| Ramachandran | ||
| Most favored | 99.02% | 98.95% |
| Allowed | 1.95% | 1.87% |
| Disallowed | 0.14% | 0.0% |
| r.m.s.d. | ||
| Bond lengths | 0.008 Å | 0.005 Å |
| Bond angles | 1.325° | 1.169° |
| PDB accession no. | 4GXQ | 4GXR |
a Data in parentheses represent highest resolution shell.
b Data in parentheses represent the number of reflections used during refinement.
c Rfactor = Σ|Fobs − Fcalc|/Σ|Fobs|, where Rwork refers to the Rfactor for the data utilized in the refinement and Rfree refers to the Rfactor for 5% of the data that were excluded from the refinement.