Table I.
Statistics of X-ray Data Collection and Atomic Refinement (Numbers in Parentheses Refer to the Outer Shell of Data)
| F-dAdo | F-Ade | |
|---|---|---|
| Space group | P212121 | P212121 |
| Unit cell parameters [Å] | a = 71.2, b = 130.6, c = 149.4 | a = 71.8, b = 130.6, c = 149.2 |
| Resolution range [Å] | 100.0–2.5 (2.59–2.50) | 100.0–2.3 (2.38–2.30) |
| Rsyma [%] | 9.0 (39.0) | 10.5 (33.6) |
| Number of unique data | 47561 (4622) | 51620 (1680) |
| Completeness of data [%] | 99.4 (98.1) | 81.2 (26.8) |
| I/σ(I) | 18.1 (5.1) | 16.9 (5.2) |
| Number of residues/asymmetric unit (3) | 847 | 817 |
| Number of protein atoms | 6604 | 6388 |
| Number of ligand atoms | 57 | 33 |
| Number of sulfate atoms | 145 | 145 |
| Number of water atoms | 55 | 217 |
| Matthews' coefficient [Å3/Da]b | 3.6 | 3.6 |
| R [%]c | 20.9 (34.0) | 18.5 (26.0) |
| Rfree [%]d | 24.8 (41.0) | 23.2 (30.0) |
| Test set size [%], selection | 5.0, random | 5.0, random |
| R.m.s. deviations from target values | ||
| Bond lengths [Å] | 0.009 | 0.013 |
| Bond angles [°] | 1.3 | 1.5 |
| Ramachandran angles | ||
| Most favored [%] | 91.2 | 93.5 |
| Additionally allowed [%] | 7.7 | 5.6 |
| Generously allowed [%] | 0.4 | 0.3 |
| Disallowed [%] | 0.7 | 0.6 |
| Errat Overall Quality Factor[%] | 93.5 | 94.0 |
| Verify3D residues with score >0.2[%] | 95.6 | 100.0 |
| Average B factor for protein atoms [Å2] | 54.3 | 48.3 |
| Average B factor for ligand atoms [Å2] | 73.7 | 46.0 |
| Average R.m.s. B for protein atoms [Å2] | 1.06 | 1.68 |
| Average R.m.s. B for ligand atoms [Å2] | 3.21 | 2.81 |
a
, where Io is the observed intensity. Both summations involve all input reflections for which more than one symmetry equivalent is averaged.
b
Matthews' coefficient as defined by Matthews, BW (1968) J Mol Biol 33:491–497.
c
.
d
Rfree as defined by Brünger, AT (1992) Nature (London) 355:472–474.