Table 1.
Summary of Diffraction Data and Structure Refinement Statistics of H3(1–10) and H3(1–15)T3ph Peptide Complexes with wild-type Survivin and Survivin(K62Y/H80W) Double Mutant.
| Summary of diffraction data | |||
|---|---|---|---|
| Crystal | H3(1–15)T3ph- Survivin |
H3(1–10)- Survivin |
H3(1–10) Survivin(K62Y/H80W) |
| PDB code | 3UIG | 3UII | 3UIK |
| Beamline | APS-24ID-C | APS-24ID-E | APS-24ID-E |
| Wavelength (Å) | 0.9795 | 0.9792 | 0.9792 |
| Space group | C2 | C2 | C2 |
| Cell parameters | |||
| a (Å) | 115.8 | 115.3 | 114.8 |
| b (Å) | 71.0 | 71.3 | 71.0 |
| c (Å) | 82.3 | 81.6 | 81.6 |
| β (°) | 128.8 | 128.5 | 129.3 |
| Resolution (Å) | 50.0-2.4 (2.49-2.40)a | 50.0-2.6 (2.69-2.60) | 30.0-2.7 (2.80-2.70) |
| Rmerge (%) | 5.2 (52.7) | 8.6 (52.9) | 7.4 (64.0) |
| Observed reflections | 82,484 | 66,350 | 50,310 |
| Unique reflections | 20,244 | 16,412 | 13,470 |
| Redundancy | 4.1 (3.9) | 4.0 (3.9) | 3.7 (3.5) |
| Average I/σ(I) | 17.2 (2.0) | 10.1 (2.0) | 31.4 (1.8) |
| Completeness (%) | 97.9 (86.9) | 98.9 (96.4) | 96.6 (83.6) |
| Refinement and structure model | |||
| R / R free | 21.3 / 25.0 | 22.2 / 27.3 | 21.9 / 28.1 |
| Number of atoms | 2,329 | 2,293 | 2290 |
| Protein / Peptide | 2,215 / 90 | 2,210 / 64 | 2224 / 64 |
| Water | 22 | 17 | - |
| Zn2+ ion | 2 | 2 | 2 |
| Average B factor (Å2) | 96.3 | 89.1 | 119.6 |
| Protien / Peptide | 95.9 / 110.0 | 88.4 / 115.1 | 118.2 / 169.1 |
| Water | 85.5 | 82.3 | - |
| Zn2+ ion | 73.0 | 76.5 | 98.6 |
| RMS deviations | |||
| Bond lengths (Å) | 0.010 | 0.013 | 0.010 |
| Bond angles (°) | 1.224 | 1.430 | 1.408 |
a
Values in parentheses are for highest-resolution shell.