TABLE 1.
Crystallographic data and refinement statistics
Rsym = Σ I − 〈I〉 /ΣI, where I = observed intensity, 〈I〉 = average intensity obtained from multiple observations of symmetry related reflections. r.m.s. bond lengths and r.m.s. bond angles are the respective root mean square deviations from ideal values. Free R factor was calculated with 5% of data omitted from the structure refinement.
| TAT (Se-Met)a |
D117A TATa | ||
|---|---|---|---|
| Inflection | Remote | ||
| Data collection | |||
| Wavelength (Å) | 0.9806 | 0.9637 | 1.0 |
| Resolution (Å) | 2.70 (2.75–2.70) | 2.70 (2.75–2.70) | 2.45 (2.49–2.45) |
| Rsym | 9.8 (78.0) | 9.4 (56.4) | 10.9 (50.4) |
| 〈I〉/〈σ(I)〉 | 22.5 (1.8) | 24.9 (2.6) | 33.6 (3.6) |
| Completeness (%) | 100.0 (100.0) | 100.0 (100.0) | 99.9 (99.9) |
| Redundancy | 6.9 (6.5) | 7.0 (7.1) | 11.4 (10.8) |
| Wilson B-factor | 59.6 | 54.3 | 45.7 |
| Refinement | |||
| Resolution (Å) | 47.7–2.70 | 29.06–2.45 | |
| No. of reflections | 11419 | 15066 | |
| Rwork/Rfree (%) | 22.1/23.8 | 19.6/24.8 | |
| No. of atoms | |||
| Protein/ligand | 2315/102 | 2543/102 | |
| Ion/water | 10/13 | 6/41 | |
| Mean B-factors (Å2) | |||
| Protein/ligand | 45.1/46.3 | 49.0/48.3 | |
| Ion/water | 66.4/38.4 | 59.2/43.3 | |
| r.m.s.d. (bond (Å)/angles (°)) | 0.005/0.853 | 0.015/1.52 | |
| Ramachandran plot | |||
| Most favored | 96.1% | 97.3% | |
| Disallowed | 0.6% | 0.0% | |
a Values in parentheses are for highest resolution shell.