Table 2. Statistics of distance and dihedral angle restraints used for 3D structure calculations and quality ensemble of 200 NMR-derived structures of the peptides on the last steps of MD simulations with the time-averaged distance and dihedral angle restraints.

		Peptide
		Tat1_4-5TO	Tat1_8-9TO	Tat1_8-9TOD	Tat1_4-5TO,8-9TOD	Tat1_A4-5,8–9
Interproton distances:	total number	57	36	48	48	71
	intra-residue	46	27	39	37	59
	i, i+1	11	9	9	11	11
	i, i+2	0	0	0	0	1
Dihedral angle restraints a		18	22	23	17	25
Structure b		8,9 β I or IV (38%)	-	-	6 γ(63%)	5,6 β I or IV (81%)
Hydrogen bonds c		s.c.6-CO5	-	Hε10-CO8	HN7-CO5	s.c10-CO12
RMSD 1-9bb [Å]		1.008	1.357	1.187	0.865	1.140
Rg heavy [Å]		8.4	9.7	7.7	8.3	9.5

^aThe distance constraints and the ³J_HNHα vicinal coupling constants were used in the HABAS algorithm of the DYANA package to generate φ, ψ and χ¹ dihedral angle restraints.

^b The content of the conformers with indicated turn structure is given in parentheses.

^c Hydrogen bonds appearing in more than 50% of the structures in the final ensemble.