Table 1 Statistics and summary of structure determination and refinement.

	Cor a 1.0401	Cor a 1.0402	Cor a 1.0403	Cor a 1.0404
PDB ID	6Y3H	6Y3I	6Y3K	6Y3L
Experimental restraints
Total no. of NOE-based distance restraints^a	5027	4062	4396	2662
Intraresidue [i = j]	1577	1232	1630	1175
Sequential [\|i − j\|= 1]	1200	1133	1068	669
Medium range [1 <\|i − j\|< 5]	900	771	701	327
Long range [\|i − j\|≥ 5]	1350	926	997	491
Dihedral angle restraints	267	260	257	255
Hydrogen bond restraints	142	148	140	149
Total no. of restraints	5436	4470	4793	3066
Total no. of restraints per residue	34.0	27.9	30.0	19.2
Long range restraints per residue	8.4	5.8	6.2	3.1
Restraint violations^b
Average distance violation	0.032 ± 0.024 Å	0.015 ± 0.014 Å	0.017 ± 0.010 Å	0.020 ± 0.017 Å
Maximal distance violation^c	0.17 Å	0.092 Å	0.045 Å	0.15 Å
Average dihedral angel violation	0.39 ± 0.90°	0.19 ± 0.17°	0.46 ± 1.00°	0.16 ± 0.15°
Maximal dihedral angle violation^c	14.10°	0.77°	15.7°	0.73°
RMSD values^d
Backbone atoms	0.4 Å	0.4 Å	0.4 Å	0.4 Å
Heavy atoms	0.7 Å	0.5 Å	0.5 Å	0.5 Å
Bond lengths	0.013 Å	0.013 Å	0.013 Å	0.013 Å
Bond angles	2.4°	2.0°	2.1°	2.1°
Ramachandran plot statistics^e
Most favored regions	88.3%	96.2%	93.3%	96.2%
Allowed regions	11.7%	3.0%	6.7%	3.3%
Disallowed regions	0.0%	0.7%	0.0%	0.5%
All-atom clashscore^f	3	0	0	0

^aNumbers are given for all residues (Gly1–Cys160). ^bCalculated for all residues as sum over r⁻⁶. ^cLargest violation among the 20 lowest energy structures. ^dPairwise RMSD was calculated among the 20 lowest energy structures. ^eObtained with the protein structure validation software (PSVS) suite⁶¹. ^fAll-atom clashscore, defined as number of overlaps (≥ 0.4 Å) per 1000 atoms.

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