Table 1.
Crystallographic Data Parameters
| Data collection | |
|---|---|
| Space group | C2 |
| Unit-cell parameters | |
| a,b,c (Å) | 113.71, 38.96, 93.13 |
| α,β,γ (°) | 90, 100.13, 90 |
| Resolution limits (Å) | 55.87–1.92 (2.02–1.92) |
| No. of reflections | |
| Total | 118,452 (17,774) |
| Unique | 30,573 (4467) |
| Completeness (%) | 98.8 (99.2) |
| Multiplicity | 3.9 (4.0) |
| Mean I/δI | 9.5 (2.5) |
| Rmerge | 0.062 (0.408) |
| Refinement | |
| Rfactor | 0.2184 |
| Rfree | 0.2400 |
| No. of protein atoms | 2896 |
| rmsd | |
| Bonds (Å) | 0.0127 |
| Angles (°) | 1.587 |
| Average B-factors (Å2) | |
| Main chain | 54.2 |
| Side chain | 56.7 |
| TTAI 1st copy | 37.1 |
| TTAI 2nd copy | 50.9 |
| C. Ramachandran criteria (%, assessed by MolProbity‡) | |
| Ramachandran favored | 93.68 |
| Ramachandran outliers | 1.37 |
Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, et al (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res35:W375–W383.