Table 1.
FUS RRM | U1 SL3 | |
---|---|---|
NMR distance and dihedral constraints | ||
Distance restraints | ||
Total NOE | 3569 | 344 |
Intra-residue | 631 | 132 |
Inter-residue | 2910 | 192 |
Sequential (|i – j | = 1) | 915 | 138 |
Nonsequential (|i – j | > 1) | 1995 | 54 |
Hydrogen bondsa | 28 | 20 |
Protein–nucleic acid intermolecular | 92 | |
Total dihedral angle restraintsb | ||
Protein | 66 | |
ϕ | 33 | |
ψ | 33 | |
Nucleic acid | 125 | |
Base pair | ||
Sugar pucker | 25 | |
Backbone | 100 | |
Based on A-form geometry | 125 | |
Structure statistics | ||
Violations (mean and s.d.) | ||
Distance constraints > 0.3 Å | 3.0 ± 1.2 | |
Dihedral angle constraints > 5° | 1.1 ± 0.9 | |
Max. dihedral angle violation (°) | 6.95 ± 3.96 | |
Max. distance constraint violation (Å) | 0.38 ± 0.03 | |
Deviations from idealised geometry | ||
Bond lengths (Å) | 0.0041 ± 0.0001 | |
Bond angles (°) | 1.404 ± 0.008 | |
Average pairwise r.m.s. deviationc (Å) | ||
Protein | ||
Heavy | 0.45 ± 0.06 | |
Backbone | 0.20 ± 0.04 | |
RNA | ||
All RNA heavy | 0.72 ± 0.16 | |
RNA backbone | 0.71 ± 0.15 | |
Complex | ||
Protein and nucleic acid backbone | 0.71 ± 0.16 | |
Protein and nucleic acid heavy | 0.79 ± 0.15 |
aHydrogen bond constraints were identified from slow-exchanging amide protons in D2O and imino protons in H2O.
bDihedral angle based TALOS+, sugar puckers based on homonuclear TOCSY, RNA backbone constraints in A form stem based on standard A-form geometry.
cRoot-mean-squared deviation was calculated using the protein residue range 284–370 (chain ID: A) and the RNA residue range 4–24 (chain ID: B) calculated on the ensemble of 18 NMR structures.