Table 1. X-Ray Data and Structure Refinement Statistics.
| PTC-PAPU | PTC-PALO | Truncated PTC-PALO | |
| Data collection | |||
| ESRF Beamline | BM16 | ID23-2 | ID14-4 |
| Wavelength (Å) | 0.980 | 0.873 | 0.979 |
| Space group | P6322 | P1 | P6322 |
| Unit cell a, b, c (Å) | 117.2, 117.2, 225.3 | 81.5, 81.7, 82.3 | 90.0, 90.0, 184.3 |
| α, β, γ (°) | 90, 90, 120 | 105, 103, 101 | 90, 90, 120 |
| Resolution range (Å)a | 30–2.50 | 30–2.00 | 40-1.59 |
| (2.59–2.50) | (2.10–2.00) | (1.67–1.59) | |
| Reflections, total/unique | 692,675/32,509 | 194,037/114,553 | 611,850/60,518 |
| Completeness (%)a | 100 (100) | 87.5 (79.5) | 100 (99.8) |
| I/σa | 35.1 (9.5) | 10.9 (1.8) | 5.7 (2.1) |
| R sym b (%)a | 11.5 (42.8) | 5.5 (42.5) | 8.2 (36.6) |
| Refinement Statistics | |||
| Resolution range | 23–2.50 | 30–2.00 | 30-1.59 |
| R-factor/R free c | 18.7/21.6 | 19.6/23.7 | 16.2/18.0 |
| Molecules and atoms refined | |||
| Polypeptide chains | 2 | 6 | 1 |
| Protein atoms | 5,422 | 15,480 | 2,446 |
| PAPU or PALO | 2 | 6 | 1 |
| RMSDd bonds (Å)/angles (°) | 0.011/1.16 | 0.008/1.01 | 0.007/1.13 |
| Average B-factor (Å2) | |||
| Protein | 19.8 | 33.8 | 12.7 |
| PAPU or PALO | 11.1 | 30.2 | 8.5 |
| Ramachandran Plote (%) | |||
| Favored | 93.3 | 92.2 | 92.6 |
| Allowed | 6.1 | 7.1 | 6.4 |
| Generously allowed | 0 | 0 | 0 |
| Disallowed | 0.7 | 0.7 | 0.7 |
a
Values in parenthesis are data for the highest resolution shell.
b
R sym = ΣI−<I>/ΣI, where I is the observed intensity and <I> the average intensity.
c
R-factor = Σh ∥F obs|−|F calc∥/Σh |F obs|, where |F obs| and |F calc| are observed and calculated structure factors amplitudes for all reflections (R-factor). R free, R based on 5% of the data, withheld for the cross-validation test.
d
RMSD: root mean square deviation.
e
Using PROCHECK.