Table 1.

Determination of the NMR Structure of Flavodoxin-4 in Aqueous Solution Containing 20 mM Sodium Phosphate and 50 mM NaCl at pH 6.0: Input for the Structure Calculations of the Apo-protein (Apo) and the FMN Complex (Holo) and Characterization of the Bundles of 20 Energy-minimized CYANA Conformers Representing These Structures

Quantity	Valuea
	Holo (298K)	Apo (308K)
NOE upper distance limit	2471	2392
Intraresidual	646	630
Short range	709	646
Medium range	455	399
Long range	661	717
Dihedral angle constraints	798	795
Residual target function value (Å2)	2.04±0.26	1.95±0.21
Residual NOE violations
Number≥0.1 Å	22±4	16±4
Maximum (Å)	0.14±0.4	0.13±0.01
Residual dihedral angle violations
Number≥2.5°	1±1	2±1
Maximum (°)	3.0±1.1	3.5±1.0
RMSD from ideal geometry
Bond lengths (Å)	0.012	0.012
Bond angles (°)	2.2	2.2
AMBER energies [kcal mol−1]
Total	−5351± 155	−4737±134
van der Waals	−397±27	−328±17
Electrostatic	−6071±174	−5723±132
RMSD to the mean coordinates (Å)b
Backbone (5−150)	0.66±0.09	1.67±0.48
Heavy atoms (5−150)	1.18±0.10	2.43±0.64
Backbone (5−10,16−37,68−150)	0.56±0.10	0.58±0.09
Heavy atoms (5−10,16−37,68−150)	1.11±0.17	1.05±0.14
Ramachandran plot statistics (%)c
Most favored regions	78.8	72.6
Additional allowed regions	20.8	26.3
Generously allowed regions	0.5	1.0
Disallowed regions	0.0	0.1

^aExcept for the top six entries, which represent the input generated for the final cycle of structure calculation with UNIO-ATNOS/CANDID and CYANA 3.0, average values and standard deviations for the 20 energy-minimized conformers are given.

^bThe numbers in parentheses indicate the residues for which the RMSD was calculated.

^cAs determined by PROCHECK.¹⁸