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. Author manuscript; available in PMC: 2013 Mar 1.
Published in final edited form as: Proteins. 2011 Nov 24;80(3):807–817. doi: 10.1002/prot.23238

Table I.

Structural Statistics for KAP25 peptide: a) bound to SPase I Δ2-75 and b) in presence of DPC micelles

Parameter Ensemble
Distance restraints Bound a DPCb
All 207 246
Short range (|i-j|<=1) 185 162
Medium-range (1<|i-j|<5) 22 74
Long-range (|i-j|>=5) 0 10
Average CYANA target function value 0.16 0.15
Violations
NOE (> 0.2 Å) 0 0
RMSDc
Average backbone RMSD to mean 1.48 Å 0.64 Å
Average heavy atom RMSD to mean 1.96 Å 0.96 Å
RMS Z score
Bond length 1.065+/- 0.000 1.065+/- 0.000
Bond angles 0.175+/- 0.001 0.174+/- 0.001
Omega angle restraints 0.019+/- 0.005 0.017+/- 0.007
Side chain planarity 0.029+/- 0.007 0.028+/- 0.006
Improper dihedral distribution 0.304+/- 0.002 0.304+/- 0.001
Ramchandran statisticsd
Residues in most favored regions 64.0% 62.9%
Residues in additional allowed regions 35.4% 37.1%
Residues in generously allowed regions 0.6% 0%
Residues in disallowed regions 0% 0%
a

20 mM Sodium phosphate buffer, 22 °C

b

20 mM Sodium phosphate buffer, 40 °C, 75mM DPC (1:1.4 peptide:micelles molar ratio)

c

Residues -11 to -1

d

All residues