Table I. NMR structure determination statistics.

Restraint statistics	Tandem Vps27 UIM	Vps27 UIM-1–ubiquitin complex
Distance restraints	858	2138
Unambiguous NOE distance restraints	412	1625
Intraresidue	256	846
Sequential (|i – j| = 1)	124	295
Medium range (1 < |i – j| ≤ 4)	32	231
Intramolecular long range (|i – j| > 4)	0	177
Intermolecular		76
Hydrogen-bonding distance restraints	50	76
Ambiguous NOE distance restraints	396	437
Torsion angle restraints	66 (33 φ, 33 ψ)	112 (51 φ, 51 ψ, 10 χ1)
Structure quality of NMR ensemble
Restraint satisfaction
RMS differences for distance restraints (Å)	0.007 ± 0.000	0.011 ± 0.000
RMS differences for torsion angle restraints (°)	0.012 ± 0.007	0.098 ± 0.012
Deviations from ideal covalent geometry
Bond lengths (Å)	0.001 ± 0.000	0.001 ± 0.000
Bond angles (°)	0.305 ± 0.003	0.327 ± 0.002
Impropers (°)	0.149 ± 0.003	0.214 ± 0.004
Ramachandran plot statistics
Residues in most favored regions (%)	65.4	87.3
Residues in allowed regions (%)	29.4	11.8
Residues in disallowed regions (%)	5.1	0.9
Average atomic RMSDs from the average structure
All atoms (Å)	11.4	1.90
All atoms except disordered regionsa (Å)	10.0	1.32
Backbone atoms (N, Cα, C′)
All residues (Å)	10.8	1.31
All residues excluding disordered regionsa (Å)	9.1	0.57
Secondary structural elements (Å)	0.27 and 0.36b	0.53

^aDisordered regions in the tandem Vps27 UIM include residues 249–258, 273–303 and 324–329, while those in the Vps27 UIM-1–ubiquitin complex include residues 256–257 and 274–278 of Vps27 and 73–76 of ubiquitin.

^bReported values are for the αA and αB helices corresponding to residues 259–272 and 304–323, respectively.