Table 1.

Average S² from NMR spectroscopy and MD

Technique	NMR		MD
Analysis method	MF∗	relax	M1†			M2‡
Simulation			1	2	3
All residues§	0.901	0.886	0.854	0.853	0.866	0.853
α-helices¶	0.921	0.904	0.894	0.899	0.902	0.896
β-strands‖	0.893	0.877	0.875	0.876	0.890	0.876
Loops∗∗	0.883	0.869	0.803	0.796	0.819	0.797
Ω loop††	0.898	0.901	0.705	0.755	0.746	0.748
Converged residues			0.868	0.876	0.874
Unconverged residues‡‡			0.833	0.820	0.844

^∗Original ModelFree analysis (2).

^†Internal autocorrelation, individual simulations.

^‡Internal autocorrelation by randomization of all simulations.

^§Except N-terminus (H26) and 12 prolines for MD: 27, 62, 67, 107, 145, 167, 174, 183, 219, 226, 252, and 257. For NMR spectroscopy, this also excludes residues that could not be analyzed and residues whose model-free model does not involve an S².

^¶There are 12 α-helices in the structure: H1, 26–40; H2A, 69–71; H2B, 72–85; H3, 109–111; H4, 119–128; H5,132–142; H6, 145–154; H7, 168–170; H8, 183–195; H9, 201–212; H10, 221–224; and H11, 272–288.

^‖There are five β-strands (in one sheet) in the structure: S1, 56–60; S2, 43–50; S3, 259–266; S4, 244–251; and S5, 230–237.

^∗∗Including the Ω loop.

^††The Ω loop spans residues 161–179.

^‡‡Fourteen residues are unconverged in all three simulations: E64, S70, V159, T160, L169, N170, N175, D176, E177, R191, L193, L194, L198, and A202.