Table 1 Data collection and refinement statistics (molecular replacement).
From: Identification of an allosteric binding site for RORγt inhibition
PDB ID | 4YPQ | 5C4O | 5C4U | 5C4S | 5C4T |
|---|---|---|---|---|---|
Ligand name | MRL-871 | MRL-871 | MRL-367 | MRL-299 | MRL-673 |
Data collection | |||||
Space group | R32:H | P 61 2 2 | P 61 2 2 | P 61 2 2 | P 61 2 2 |
Cell dimensions | |||||
a, b, c (Å) | 173.8, 173.8, 67.2 | 108.5, 108.5, 104.7 | 108.1, 108.1, 106.5 | 108.4, 108.4, 106.3 | 107.3, 107.3, 100.4 |
α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
Resolution (Å) | 35.47–2.32 (2.40–2.32)* | 69.91–2.24 (2.32–2.24) | 93.6–2.08 (2.154–2.08) | 93.92–2.23 (2.31–2.23) | 92.9–1.77 (1.836–1.77) |
Rsym | 0.121 (0.886) | 0.047 (1.45) | 0.0420 (1.236) | 0.056 (1.402) | 0.0565 (1.239) |
I/σI | 12.1 (2.7) | 35.91 (2.57) | 38.87 (2.62) | 30.03 (2.51) | 29.46 (2.61) |
Completeness (%) | 100.0 (100.0) | 99.94 (99.89) | 99.78 (99.36) | 99.99 (100.0) | 99.99 (100.00) |
Redundancy | 11.7 (11.6) | 16.0 (15.8) | 19.3 (19.9) | 18.8 (19.2) | 19.1 (19.7) |
Refinement | |||||
Resolution (Å) | 35.47–2.32 | 69.91–2.24 | 93.6–2.08 | 93.9–2.23 | 92.9–1.77 |
No. reflections | 16882 | 17932 | 22579 | 18547 | 33582 |
Rwork/Rfree | 0.174/0.227 | 0.227/0.266 | 0.228/0.273 | 0.218/0.261 | 0.192/0.223 |
No. atoms | |||||
Protein | 1987 | 1996 | 1994 | 1987 | 1985 |
Ligand/ion | 32 | 60 | 51 | 45 | 118 |
Water | 130 | 14 | 23 | 18 | 101 |
B-factors | |||||
Protein | 45.70 | 67.90 | 59.80 | 67.9 | 39.6 |
Ligand/ion | 41.50 | 102.5 | 57.70 | 64.1 | 50.50 |
Water | 47.30 | 64.20 | 57.80 | 63.9 | 45.30 |
R.m.s. deviations | |||||
Bond lengths (Å) | 0.008 | 0.014 | 0.014 | 0.014 | 0.015 |
Bond angles (°) | 1.04 | 1.78 | 1.81 | 1.75 | 1.64 |
