Table I.
Data Collection and Structural Refinement Statistics of rHSA-Myr-DAUDA Complex
| Data collection | rHSA-Myr-DAUDA |
|---|---|
| X-ray wavelength (Å) | 1.04 |
| Space group | C2 |
| Cell dimensions (Å) | 176.66, 37.14, 90.20, β = 104.38° |
| Independent reflections | 1177608 |
| Resolution range (Å) | 50.0–2.6 (2.64–2.60)a |
| Completeness (%) | 98.5 (96.1)a |
| Multiplicity (redundancy) | 3.1 (2.3) |
| Rsym(%)b | 8.7 (67.0)a |
| I/σ | 24.9 (2.0)a |
| Refinement statistics | |
| Rwork(%)c | 25.1 (34.2) |
| Rfree(%)d | 26.0 (35.1) |
| Average B values | |
| Protein | 61.82 |
| Myristate | 63.63 |
| DAUDA | 65.65 |
| Root mean square deviation from ideal values | |
| Bond lengths (Å) | 0.011 |
| Bond angles (°) | 1.8 |
| Percent of residues | |
| in favored region | 88.8 |
| in allowed region | 8.5 |
| and in outlier region | 2.6 |
a
Values in parentheses are for the outermost resolution shells.
b
Rsym = Σ| (Ihkl) – (I)|/Σ (Ihkl), where Ihkl is the weighted mean intensity of a given reflection.
c
Rwork = Σ|Fobs − Fcalc|/ΣFobs, where Fobs and Fcalc are the observed and calculated structure factors, respectively.
d
Rfree is the Rwork calculated using a randomly selected 5% reflection data omitted from the refinement.