Table 1.

Structural statistics

Restraints used in the structure calculation*
Number of distance restraints
Intraresidue	408
Interresidue sequential (i, i + 1)	252
Interresidue medium range (1 < |i − j| < 5)	228
Long range [(|i − j|) ≥ 5]	184
Intermolecular	58
Total	1,131
Structural statistics
rms deviations from distance restraints, Å	0.0037 ± 0.0008
Number of torsion angle restraints (φ, ψ)†	136
rms deviations from dihedral restraints, °	0.076 ± 0.021
rms deviations from idealized geometry
Bonds, Å	0.00080 ± 0.00003
Angle, °	0.30530 ± 0.0012
Improper, °	0.1011 ± 0.0033
Coordinate precision
rms deviations from minimized average   structure‡, Å
Backbone atoms	0.69 ± 0.08
All heavy atoms	1.25 ± 0.10
Ramachandran analysis§
Most favored region, %	84.5
Additionally allowed region, %	14.0
Generously allowed region, %	0.6
Disallowed regions, %	0.9

^*None of the 20 structures exhibited distance violations >0.2 Å or dihedral angles >5°. 

^† Backbone dihedral angle restraints were generated with talos (30) based on analysis of ¹H_α, ¹H_N, ¹³C_α, ¹³C_β, ¹³C′, and ¹⁵N chemical shifts. 

^‡ The coordinate precision is defined as average atomic rms deviation between the 20 structures with lowest energy and the minimized average structure for residues 452–476 and 486–514 of cterRAP74 and 945–961 of cterFCP. The backbone value refers to N, C_α, and C′. 

^§ procheck_nmr (32) was used to assess the quality of the structures.