Table 1. Data collection and refinement statistics.
Values in parenthesis correspond to the highest resolution bin.
| Wild-type | K126E | ||
|---|---|---|---|
| Properties | UDP-6N3-GlcNAc | NADPH | NADPH |
| Data collection | |||
| Space group | P321 | P6322 | H32 |
| Unit cell | |||
| Dimensions (Å) | a=b=123.78, c=104.46 | a=b=125.18, c=101.79 | a=b=160.5, c=80.05 |
| Angles (°) | α=β=90, γ=120 | α=β=90, γ=120 | α=β=90, γ=120 |
| Wavelength (Å) | 1.0000 | 1.0000 | 1.0000 |
| Resolution range (Å) | 34.8−2.10 | 34.05−2.80 | 40.13−2.20 |
| Total observations | 291899 | 103149 | 93553 |
| Unique observations | 54166 | 12071 | 20104 |
| I/σ (I) | 11.0 (4.1) | 12.2 (2.8) | 8.9 (2.5) |
| Completeness (%) | 99.9 (100) | 99.9 (100) | 99.9 (100) |
| Rmerge (%)* | 10.4 (33.8) | 11.9 (79.8) | 8.8 (49.8) |
| Multiplicity | 5.4 (5.2) | 8.5 (8.9) | 4.7 (4.4) |
| Refinement | |||
| Rwork/Rfree (%)† | 16.4/20.7 | 23.8/27.6 | 19.6/26.4 |
| Number of protein chains | 2 | 1 | 1 |
| Number of protein residues | 693 | 262 | 314 |
| Number of protein atoms | 5562 | 2137 | 2504 |
| Number of ligands | 18‡ | 1 | 6 |
| Number of ligand atoms | 168 | 48 | 73 |
| Number of water molecules | 385 | 3 | 82 |
| B-factor, protein (Å2) | 29.0 | 81.9 | 50.1 |
| B-factor, ligands (Å2) | 53.3 | 80.4 | 76.8 |
| B-factor, water (Å2) | 36.0 | 49.2 | 46.5 |
| RMSD bonds (Å) | 0.023 | 0.008 | 0.017 |
| RMSD bonds (°) | 2.19 | 1.363 | 2.01 |
| Co-ordinate error (Å) | 0.14 | 0.62 | 0.24 |
| Ramachandran plot | |||
| Preferred regions (%) | 97.5 | 92.7 | 95.9 |
| Allowed regions (%) | 2.2 | 7.3 | 4.1 |
| Outliers (%) | 0.3 | 0.0 | 0.0 |
| PDB codes | 3W1V | 3VVB | 3VVC |
*Rmerge=Σhkl Σi|I(hkl)i−[I(hkl)]|/Σhkl ΣiI(hkl).
†Rwork=Σhkl |F(hkl)o−[F(hkl)c]|/ΣhklF(hkl)o; Rfree was calculated as Rwork, where F(hkl)o values were taken from 5% of data not included in the refinement.
‡This structure contains 14 sulfate ions from the crystallization solution.