Table 1. Crystallographic model refinement and data collection statistics.
| Sample | RNMT 165–476 - RAM 2–45 | RNMT 165–476 limited proteolysis | RNMT 165–476 Δ416-456 |
|---|---|---|---|
| PDB code | 5E8J | 5E9W | 5E9J |
| Data measurement | |||
| Source | DLS ID24 | DLS ID04 | ESRF ID30 |
| Space group | P1 | P212121 | P212121 |
| Unit cell (Å/°) | a = 49.15, b = 50.49, c = 84.58, α = 90.06, β = 92.41, γ = 115.41 | a = 77.46, b = 99.16, c = 167.61, α = β = γ = 90.00 | a = 70.76, b = 114.38, c = 134.81, α = β = γ = 90.00 |
| Resolution (Å) | 29.44–2.35 (2.48–2.35) | 29.58–2.28 (2.41–2.28) | 87.21–3.47 (3.71–3.47) |
| Observations | 45164 (5607) | 160886 (23186) | 67860 (6796) |
| Unique observations | 28355 (3888) | 57298 (8296) | 13618 (1770) |
| Rmerge(%) | 0.11 (0.49) | 0.08 (0.27) | 0.21 (0.97) |
| I/σI | 6.6 (2.0) | 10.3 (3.9) | 6.6 (1.6) |
| Completeness (%) | 92.8 (87.1) | 97.0 (97.6) | 92.2 (67.6) |
| Multiplicity | 1.6 (1.4) | 2.8 (2.8) | 4.9 (3.8) |
| Refinement Statistics | |||
| Resolution range (Å) | 28.16–2.35 | 29.57–2.28 | 48.80–3.47 |
| R-factor Rwork/Rfree | 0.21/0.26 (0.26/0.32) | 0.22/0.25 (0.27/0.32) | 0.23/0.26 (0.33/0.40) |
| Molprobity score | 2.15 | 1.82 | 2.41 |
| Number of atoms* | |||
| Protein | 5807 | 8989 | 4441 |
| Ligand | 96 | 104 | 90 |
| Water | 219 | 307 | 0 |
| Mean B-factor (Å2) | 24.55 | 22.42 | 91.00 |
| RMS bond length deviation (Å) | 0.003 | 0.008 | 0.003 |
| RMS angle deviation (°) | 0.790 | 1.342 | 0.784 |
| Residues in favored region of the Ramachandran plot (%) | 95.7 | 95.9 | 94.8 |
| Residues in allowed region of the Ramachandran plot (%) | 3.3 | 3.3 | 4.9 |
*Hydrogen atoms are not taken into account.
Values in parentheses are for the outer shell.