TABLE 1.
Statistics of diffraction data and structure refinement
| Wild type | I148L | |
|---|---|---|
| Data collection | ||
| Space group | P3221 | P3221 |
| Cell dimensions | ||
| a, b, c (Å) | 90, 90, 120 | 90, 90, 120 |
| α, β, γ (°) | 79.2, 79.2, 134.3 | 79.1, 79.1, 134.8 |
| Resolution (Å) | 20.0-2.30 (2.38-2.30)a | 15.0-2.40 (2.49-2.40) |
| Rsym or Rmergeb | 0.128 (0.390) | 0.140 (0.373) |
| I/σI | 5.1 (1.9) | 4.9 (1.9) |
| Completeness (%) | 97.0 (97.0) | 98.2 (98.2) |
|
Redundancy
|
7.1 (7.2)
|
7.3 (7.5)
|
| Refinement | ||
| Resolution (Å) | 15.0-2.30 | 15.0-2.40 |
| No. of reflections | 21,499 | 19,161 |
| Rwork/Rfreec | 0.206/0.267 | 0.211/0.257 |
| No. of atoms | 3254 | 3254 |
| Protein | 3102 | 3102 |
| Ligand/ion | 31 | 31 |
| Water | 121 | 121 |
| B-factors (Å2) | 27.23 | 24.37 |
| Protein | 27.27 | 24.41 |
| Ligand/ion | 22.97 | 19.13 |
| Water | 27.20 | 24.57 |
| R.m.s.d. | ||
| Bond lengths (Å) | 0.007 | 0.007 |
|
Bond angles (°)
|
1.282
|
1.304
|
| Ramachandran plot (%) | ||
| Most favored regions | 90.8 | 88.2 |
| Allowed regions | 9.2 | 11.8 |
| Generously allowed regions | 0 | 0 |
| Disallowed regions | 0 | 0 |
a
Values in parentheses are for highest resolution shell.
b
Rsym or Rmerge = ∑h∑i|Ihi - 〈Ih〉|/∑h∑iIhi, where Ihi and <Ih> are the i-th and mean measurement of the intensity of reflection h, respectively.
c
Rwork/Rfree = ∑h|Fo.h - Fc.h|/∑hFo.h, where Fo.h and Fc.h are the observed and calculated structure factor amplitudes, respectively.