Table 2.

Statistics of the NMR structure and sterochemical quality by PROCHECK and MOLMOL

	Value for ensemble of 20 structures	Value for average structure	Reference value for x-ray structures (2.0 Å)
Ramachandran plot statistics
Residues in most favored regions [A,B,L], %	43.1	62.5	75 ± 10
Residues in additional allowed regions [a,b,l,p], %	50	37.5
Residues in generously allowed regions [∼a,∼b,∼l,∼p], %	6.9	0
Residues in disallowed regions, %	0%	0%
Main-chain statistics
SD of ω angle, degrees	6.3	7.4	6.0 ± 3.0
Bad contacts per 100 residues	N/A*	0	4.2 ± 10
Cα chirality, SD of ζ angle, degrees	2.4	1.5	3.1 ± 1.6
H bond energy, kcal/mol	0.9	0.8	0.6 ± 0.2
Side-chain statistics
χ-1 gauche minus, degrees	11.7	10.7	18.1 ± 6.5
χ-1 trans, degrees	9.0	8.1	19.0 ± 5.3
χ-1 gauche plus, degrees	9.4	6.9	17.5 ± 4.9
χ-1 pooled, degrees	16.3	14.8	18.2 ± 4.8
χ-2 trans, degrees	33.6	32.5	20.4 ± 5.0
Distance constraint violations (>0.3 Å)	0	N/A	N/A
Intrapeptide CHARMM energy, kcal/mol	−186.7 ± 1.2	N/A	N/A
Rmsd to the mean (20 structures) for backbone atoms, Å	0.30 ± 0.12	N/A	N/A
Rmsd to the mean (20 structures) for all heavy atoms, Å	0.63 ± 0.21	N/A	N/A

PROCHECK estimated equivalent resolution for the R*-bound Gtα(340–350) is 2.9 Å. *, Single structures only; N/A, not applicable.