Table 2.
Least-Squares Refinement Statistics.
| Enzyme Complexed with GDP-perosamine | Enzyme Complexed with GDP-3-deoxyperosamine | |
|---|---|---|
| resolution limits (Å) | 30 - 1.6 | 30 - 1.7 |
| R-factora (overall) %/no. reflections | 16.9/186447 | 19.9/161554 |
| R-factor (working) %/no. reflections | 16.6/167517 | 19.7/153306 |
| R-factor (free) %/no. reflections | 23.8/18930 | 26.3/16248 |
| number of protein atomsb | 11299 | 11408 |
| number of heteroatomsc | 1479 | 1195 |
| Average B values | ||
| protein atoms (Å2) | 28.2 | 21.5 |
| ligands (Å2) | 28.7 | 42.8 |
| solvent (Å2) | 39.1 | 26.8 |
| weighted RMS deviations from ideality | ||
| bond lengths (Å) | 0.013 | 0.014 |
| bond angles (°) | 2.01 | 2.10 |
| trigonal planes (Å) | 0.009 | 0.009 |
| general planes (Å) | 0.018 | 0.018 |
| torsional anglesd (°) | 16.4 | 16.7 |
R-factor = (Σ|Fo − Fc|/Σ|Fo|) × 100 where Fo is the observed structure-factor amplitude and Fc is the calculated structure-factor amplitude.
These include multiple conformations for E145, V162, R231, Q236 and E313 in Subunit2, K43 and I188 in Subunit 3 and I188 in Subunit 4 in the enzyme/GDP-perosamine complex; and S32, and V39 in Subunit 1, and S32, V39, V162, I225, R231, and I312 in Subunit 2 of the enzyme/GDP-3-deoxyperosamine complex.
Heteroatoms include 1259 water molecules, four PLP-linked sugar ligands, and three ethylene glycols for the enzyme/GDP-perosamine complex and 1039 water molecules, four PLPs, four GDP-3-deoxyperosamine ligands, and two ethylene glycols.
The torsional angles were not restrained during the refinement.