TABLE 1.

Summary of experimental constraints and structural statistics for the peptides J1, J1cc, J3, and J7

Parameter	Result for peptide
	J1	J1cc	J3	J7
No. of distance restraints	220	202	125	167
Intraresidue (i = j)	54	95	37	43
Sequential (|i − j| = 1)	104	72	69	105
Medium range (1 < |i − j| < 5)	59	32	19	19
Long range (|i − j| > 4)	3	3	0	0
Hydrogen bond restraints	0	0	0	0
No. of dihedral restraints	16	15	11	17
Energiesa
Mean ENOE (kcal mol−1) ± SD	4.4 ± 1.0	8.0 ± 2.2	0.7 ± 0.6	3.8 ± 0.9
Mean RMS deviations from expt data ± SD
NOEs (Å)	0.020 ± 0.002	0.028 ± 0.004	0.011 ± 0.002	0.021 ± 0.002
Dihedrals (°)	0.605 ± 0.357	0.094 ± 0.137	0.157 ± 0.266	0.018 ± 0.049
Mean deviations from ideal ± SDb
Angles (°)	0.71 ± 0.04	0.72 ± 0.05	0.67 ± 0.04	0.58 ± 0.01
Bonds (Å)	0.0052 ± 0.0003	0.0048 ± 0.0003	0.0045 ± 0.0007	0.0022 ± 0.0001
Impropers (°)	0.45 ± 0.03	0.46 ± 0.05	0.44 ± 0.04	0.40 ± 0.01
RMS deviations (Å)c
Backbone atoms (global)	>2	>2	>2	>2
Backbone atoms [S(φ) and S(ψ) > 0.8]	0.93	1.61
Ramachandran plotd
Most favored (%)	44.7	51.8	46.1	35.6
Allowed (%)	48.7	45.4	48.9	58.1
Additionally allowed (%)	6.7	2.9	5.0	6.2
Disallowed (%)	0	0	0	0

^aThe values for E_NOE are calculated from a square well potential with force constants of 50 kcal mol⁻¹ Ų.

^bThe values for the bonds, angles, and impropers show the deviations from ideal values based on perfect stereochemistry.

^cThe RMSD over the backbone heavy atoms (N, C^α, C) over the indicated residues.

^dAs determined by the program PROCHECK-NMR for all residues.