. Author manuscript; available in PMC: 2014 Aug 14.

Published in final edited form as: Biochemistry. 2012 Nov 28;51(49):9826–9835. doi: 10.1021/bi301256s

Table 1.

Structural statistics for μ-KIIIA[C1-C15,C2-C9,C4-C16] and μ-KIIIA[C1-C9,C2-C15,C4-C16]

	μ-KIIIA[C1-C15,C2-C9,C4-C16]	μ-KIIIA[C1-C9,C2-C15,C4-C16]^e
Distance restraints	231	225
Intra (i = j)	97	97
Sequential (\| i – j \| =1)	70	70
Short (l < \| i – j \| < 6 )	45	45
Long	19	13
Dihedral restraints	8	8
Energies (kcal mol⁻¹)^a
E_NOE	1.7 ± 0.4	1.6 ± 0.3
Deviations from ideal geometry^b
Bonds (Å)	0.0015 ± 0.0001	0.0017 ± 0.0002
Angles (°)	0.503 ± 0.005	0.503 ± 0.013
Impropers (°)	0.379 ± 0.009	0.371 ± 0.009
Mean global RMSD (Å)^c
Backbone heavy atoms	0.51 ± 0.12	0.58 ± 0.11
All heavy atoms	1.39 ± 0.26	1.42 ± 0.28

Ramachandran plot^d
Most favoured (%)	81.1	78.9
Allowed (%)	18.9	21.1
Additionally allowed (%)	0	0
Disallowed (%)	0	0

The values for E_NOE are calculated from a square well potential with force constants of 50 kcal mol⁻¹ Å².

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

The pairwise RMSD over the indicated residues calculated in MOLMOL.

As determined by the program PROCHECK-NMR for all residues except Gly and Pro.

Structural statistics for μ-KIIIA[C1-C9,C2-C15,C4-C16] from previously published data²² for comparison