. Author manuscript; available in PMC: 2010 Jul 15.

Published in final edited form as: J Am Chem Soc. 2009 Jul 15;131(27):9522–9531. doi: 10.1021/ja902336c

Table 3.

Clustering statistics and Cα atomic rms differences to the reference structure for the EIN-HPr docking calculations.

Relaxation Data	% structures in cluster containing lowest energy structure	C α rms difference to reference structure (Å)^a
		Overall	HPr with EIN superimposed
Experimental data	76	1.20±0.03	2.79±0.12
Synthetic data
0% noise^b	83	0.51±0.27	1.32±0.76
0% noise	83	0.48±0.19	1.35±0.39
1% noise	80	0.59±0.15	1.65±0.32
2% noise	89	0.79±0.17	2.04±0.37
5% noise	82	0.48±0.15	1.27±0.43
10% noise	72	1.82±0.35	4.08±1.02

The reference structure of the complex was generated by best-fitting the X-ray structures of free EIN (1ZYM)⁴⁵ and HPr (1POH)⁵⁴ on to the NMR structure of the EIN-HPr complex (3EZA).⁵² This ensures that the reported rms differences do not reflect internal coordinate differences between the NMR and X-ray coordinates of EIN and HPr.⁴⁰

The hydrophobic contact potential was not included in these calculations.