Table I.
Data Collection and Refinement Statistics for the HA2-Del Crystal Structure
| PDB | 4P67 |
|---|---|
| Data Collection | |
| Wavelength (Å) | 0.979 |
| Space group | P31 |
| Unit cell dimensions (Å) | a = b = 58.44 c = 66.99 a = b = 90°, g = 120° |
| Resolution range (Å) | 20-1.9 |
| Observed reflections | 142,034 |
| Unique reflections | 20,121 |
| Completeness (%) a | 99.5 (100.0)a |
| I/sI | 14.6 (3.0) |
| R-merge (I) b | 0.074 (0.654) |
| Structure Refinement | |
| Rcryst (%) c | 0.185 (0.209) a |
| Rfree (%) c | 0.242 (0.281) a |
| Protein nonhydrogen atoms | 1949 |
| Water molecules | 130 |
| Average B-factor (Å2) | 44.47 |
| RMS Deviations from Ideal Value | |
| Bonds (Å) | 0.013 |
| Angles (°) | 1.47 |
| Torsion angles (°) | 16.8 |
| Overall coordinate error based on R-factor | 0.038 |
|
Ramachandran statistics (%) (for non-Gly/Pro residues) |
|
| most favorable | 99.52 |
| additional allowed | 0.48 |
a
Values in parentheses indicate statistics for the high resolution bin.
b
Rmerge = ΣΣ j|Ij(hkl) – <I(hkl)>|/ ΣΣ j|<I(hkl)>|, where Ij is the intensity measurement for reflection j and <I> is the mean intensity over j reflections.
c
Rcryst/(Rfree) = Σ ||Fo(hkl)| – |Fc(hkl)||/ Σ |Fo(hkl)|, where Fo and Fc are observed and calculated structure factors, respectively. No s-cutoff was applied. 5% of the reflections were excluded from refinement and used to calculate Rfree.