. Author manuscript; available in PMC: 2021 Apr 21.

Published in final edited form as: Biochemistry. 2020 Apr 13;59(15):1527–1536. doi: 10.1021/acs.biochem.0c00094

Table 1.

Skp1ΔΔ dimer NMR structure statistics (PDB ID: 6V88, BMRB ID:30696)

Completeness of resonance assignments^a [%]
Backbone/Side-chain	100.0/100.0
Conformation-restricting distance constraints^b
Intra-residue [i = j]	696
Sequential [\|i - j\| = 1]	1256
Medium range [1 < \|i - j\| < 5]	1360
Long range [\| i - j \| ≥ 5]	1470
Total	4782
Intermolecular NOE constraints (included in above)	182
Dihedral angle constraints	406
NOE constraints per restrained residue (of those, long range)	22.6 (6.4)
CYANA target function [Å²]	2.33
Average number of distance constraint violations per conformer
0.1 - 0.2 Å	9.25
0.2 – 0.5 Å	2.2
>0.5 Å	0
Average number of dihedral angle constraint violations per conformer
>10°	0.1
Average RMSD from mean coordinates [Å]
backbone atoms^c (all)	0.8 (1.2)
heavy atoms^c (all)	1.1 (1.4)
Global quality scores^c (raw / Z-score)
PROCHECK² G-factor (phi-psi)	0.16/0.94
PROCHECK² G-factor (all)	0.14/0.83
Molprobity³ clash score	2.55/1.09
ProsaII⁴	0.74/0.37
Molprobity³ Ramachandran summary [%]
Most favored regions	98.7
Additionally allowed regions	1.3
Disallowed regions	0.0

Commonly observed protein NMR resonances. Excludes amino group of N-terminal Ser, side-chain amino groups of Lys, side-chain guanidinium groups of Arg, carboxyl groups of Asp and Glu, thiol and hydroxyl ¹H of Cys, Ser, Thr and Tyr, and non-protonated aromatic ¹³C.

Calculated with Protein Structure Validation Software (PSVS 1.5; http://psvs.nesg.org/)

Ordered residue ranges: 3-34, 38-44, 46-64, 74-115

Ref. 33;

Ref. 34;

Ref. 35;

⁴

Ref. 36