TABLE 1.
Crystallographic data
Numbers in parentheses represent values for the highest resolution shell. PDB, Protein Data Bank.
| NtdA-PLP | NtdA-PMP | K6P external aldimine | |
|---|---|---|---|
| Data collection | |||
| Space group | P21 | P21 | P21 |
| Unit cell dimensions | |||
| a, b, c (Å) | 50.2, 106.5, 98.6 | 50.1, 107.0, 99.2 | 49.7, 106.4, 98.2 |
| α, β, γ | 90.0°, 96.2°, 90.0° | 90.0°, 95.8°, 90.0° | 90.0°, 96.4°, 90.0° |
| Resolution range (Å) | 30.0–2.30 (2.38–2.30) | 37.0–2.22 (2.30–2.22) | 46.7–1.71 (1.75–1.71) |
| No. of unique reflections | 45,198 (3874) | 50,732 (4827) | 108,740 (7967) |
| Completeness | 98.5 (85.1) | 99.4 (96.2) | 99.3 (98.5) |
| Redundancy | 7.9 (5.9) | 3.8 (3.1) | 4.0 (3.8) |
| Rmerge (%)a | 8.5 (29.4) | 10.4 (43.8) | 6.6 (75.5) |
| I/σI | 22.6 (4.3) | 11.5 (3.1) | 14.3 (2.2) |
| Refinement statistics | |||
| Resolution (Å) | 28.9–2.30 | 37.0–2.22 | 46.7–1.71 |
| Rwork/Rfree (%)b | 16.1/21.4 | 15.8/21.1 | 15.2/8.6 |
| B-factor (Å2) | |||
| Overall | |||
| Protein | 32.8 | 23.9 | 22.7 |
| Ligand | 24.3 | 21.3 | 22.5 |
| Water | 33.9 | 30.5 | 36.0 |
| No. of ligand or cofactor molecules | 2 LLP | 2 PMP | 2 K6P |
| r.m.s.d. | |||
| Bonds (Å) | 0.007 | 0.007 | 0.007 |
| Angles | 1.049° | 1.052° | 1.130° |
| Ramachandran (%) | |||
| Favored | 96.6 | 97.5 | 97.8 |
| Allowed | 3.4 | 2.5 | 2.2 |
| PDB codes | 4K2B | 4K2I | 4K2M |
a Rmerge = Σ|Io − 〈I〉|/ΣI, where I is the intensity of a reflection and 〈I〉 is the mean intensity of a group of equivalent reflections.
b Rwork = Σ‖Fobs| − |Fcalc‖/Σ|Fobs|. Rfree is 5% of the randomly excluded reflections from refinement.