Table 1.
Data collection and refinement statistics
| PepTSt apo | PepTSt AAAc | PepTSt AF | |
|---|---|---|---|
| Data collection | |||
| Space group | C2221 | C2221 | C2221 |
| Cell dimensions | |||
| a, b, c (Å) | 102.2, 110.2, 111.0 | 103.4, 110.7, 110.6 | 102.1, 110.3, 110.7 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Wavelength (Å) | 0.9686 | 1.0332 | 0.9686 |
| Resolution (Å)a | 39.1–2.35 (2.48–2.35) | 75.56–2.52 (2.59–2.52) | 51.03–2.47 (2.53–2.47) |
| CC1/2(%)b | 98.6 (63.4) | 99.6 (74.6) | 99.8 (53.0) |
| Rmerge | 15.8 (71.0) | 8.0 (56.8) | 7.3 (64.0) |
| Rpim | 6.1 (37.7) | 5.2 (37.0) | 4.6 (40.8) |
| I/σI | 8.3 (2.2) | 10.4 (2.2) | 10.9 (2.0) |
| Completeness (%) | 99.3 (98.0) | 98.7 (99.3) | 97.9 (99.4) |
| Redundancy | 6.0 (4.1) | 3.2 (3.2) | 4.1 (4.2) |
| Number of crystals | 7 | 1 | 1 |
| Refinement | |||
| Resolution (Å) | 39.1–2.35 | 75.56–2.52 | 51.04–2.47 |
| Number of reflections | 26,224 | 21,332 | 22,139 |
| Rwork/Rfree | 21.3/24.2 | 19.8/24.2 | 22.2/26.6 |
| Number of atoms | |||
| Protein | 3,440 | 3,582 | 3,321 |
| Ligand | N/A | 16 | 17 |
| Lipid | 198 | 132 | 132 |
| Ions | 5 | 5 | 5 |
| Water | 54 | 45 | 38 |
| B-factors (Å2) | |||
| Protein | 38.4 | 49.8 | 39.7 |
| Ligand | N/A | 75.9c | 62.8 |
| Lipid | 54.8 | 61.4 | 54.0 |
| Ions | 56.4 | 69.6 | 61.7 |
| Water | 34.2 | 44.1 | 36.9 |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.006 | 0.006 | 0.006 |
| Bond angles (°) | 0.913 | 0.915 | 0.879 |
| Ramachandran statistics favoured/outliers (%) | 99.0/0 | 98.3/0.2 | 99.0/0/0 |
a
Highest resolution shell is shown in parenthesis.
b
Percentage of correlation between intensities from random half-datasets, as given by XDS.
c
PepTSt tri-Ala complex was deposited with the carboxy terminus of the tripeptide oriented towards the extracellular side of the membrane.