Table II. Data reduction, phasing and refinement statistics.
| |
Peak |
Inflection |
Remote |
|---|---|---|---|
| Data collection | |||
| Resolution (Å)a | 1.69 (1.75–1.69) | ||
| Space group | P21 | ||
| Cell dimensions(Å) | a = 28.69, b = 72.07, c = 34.17 | ||
| Cell angles (°) | α = β =90, γ = 97.70 | ||
| Wavelength (Å) | 0.9786 | 0.9788 | 0.8731 |
| f′, f″ | –8.2, 7.2 | –10.1, 3.7 | –2.3, 4.0 |
| Total data | 99 470 | 104 025 | 80 439 |
| Unique data | 15 317 | 15 352 | 15 506 |
| Redundancy | 6.5 | 6.8 | 5.2 |
| Completeness (%) | 98.2 (81.4) | 98.1 (80.4) | 99.9 (99.9) |
| I/σ(I) | 28.2 (4.0) | 25.9 (3.3) | 22.2 (2.3) |
|
Rmerge (%)b |
5.5 (40.4) |
5.0 (50.6) |
4.7 (44.5) |
| Phasing |
|
|
|
| Rano (%)c | 5.7 | 4.5 | 4.9 |
| Rdisp (%)d | – | 3.4 | 4.8 |
| FOM (solve/resolve) |
0.4/0.45 |
|
|
| Refinement |
|
|
|
| Resolution range | 36.04–1.70 | ||
| No. of unique reflections | 13 807 | ||
| Rworke (Rfreef) | 17.86 (21.94) | ||
| R.m.s.d. bonds (Å) | 0.012 (0.021)g | ||
| R.m.s.d. angles (deg) | 1.375 (1.955)g | ||
| R.m.s.d. chiral (Å3) | 4.827 (5.000)g | ||
| R.m.s.d. main-chain bond B (Å2) | 0.770 (1.500)g | ||
| R.m.s.d. side-chain bond B (Å2) |
2.440 (3.000)g |
|
|
| Model quality (Ramachandran plot)h |
|
|
|
| Residues in most favoured regions (%) | 94.5 | ||
| Residues in additional allowed regions (%) |
5.5 |
|
|
| No. of atoms per asymmetric unit (average B values) (Å2) |
|
|
|
| Protein | 919 (21.3) | ||
| Peptide | 179 (23.0) | ||
| Water | 239 (37.8) | ||
| Ions (Cd) | 1 (17.8) |
FOM, figure of merit (the cosine of the mean phase error); R.m.s.d., root mean square deviation.
aValues in parentheses correspond to the highest resolution shell.
bRmerge = ΣjΣh (|Ij,h – <Ih>|)/ΣjΣh(<Ih>), where h is the unique reflection index, Ij,h is the intensity of the symmetry-related reflection and <Ih> is the mean intensity.
cRano = Σ|I(+) – I(–)|/Σ|<I>| for anomalous differences, where <I> is the average of Friedel amplitudes.
dRdisp = Σ|Iλ1 – Iλ2|/Σ|<I>| for dispersive differences, where <I> is the average amplitude at two wavelengths λ1 and λ2.
eR = Σh||Fo|h – |Fc|h|/ Σh|Fo|h, where h defines the unique reflections.
fCalculated on a random 5% of the data.
gTarget values in parentheses.
hValues from PROCHECK (Laskowski et al., 1993).