Table 1.

NMR ensemble statistics of FUS: U1 SL3 complex.

	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.