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. Author manuscript; available in PMC: 2006 Nov 29.
Published in final edited form as: J Biomol NMR. 2006 Feb;34(2):117–127. doi: 10.1007/s10858-005-5735-8

Table 1.

Experimental restraints
long range NOEs (i - j > 10)1 459
short range interresidue NOEs (i - j < 10) 566
restrictive intraresidue NOEs 210
paramagnetic restraints2 27
13C chemical shift restraints 271
Residual dipolar couplings (C12E5, Da=20 Hz, R = 0.283) 102
Residual dipolar couplings (fd, Da=13.1 Hz, R = 0.309) 32
J-coupling restraints (periodic) 64
dihedral angle restraints3 333
total number of experimental restraints 2,054
Modeling restraints
hydrogen bonds in regular secondary structure4 59
harmonic and modeling restraints5 71
total number of modeling restraints 125
Structural statistics over 17 models
 no. of distance violations > 0.5 Å none
Goodness of fit of RDC restraints to structures
 C12E5 R=1.00, Q=0.05
fd R=0.99, Q=0.12
Ramachandran analysis7
 residues in most favored regions 80.9%
 residues in additional allowed regions 16.8%
 residues in generously allowed regions 2.3%
 residues in dissallowed regions 0.0%
Atypical χ1 rotamers8 1.2%
Side-chain steric interactions < 0.8 Å9 <1%
backbone RMSD (Å) for 17 models 0.62
1

i and j refer to residue numbers.

2

Paramagnetically broadened resonances were constrained to be ≤ 10 Å from the nickel.

3

Dihedral angle restraints were obtained by chemical shift analysis using TALOS (2004 edition) (Cornilescu et al., 1999) (see text).

4

Hydrogen bonds within regular secondary structure were determined by repeated occurrence in unrestrained structures.

5

Harmonic restraints and three hydrogen bonds were applied to model the paramagnetic region as described in text.

7

Ramachandran statistics were calculated using PROCHECK_NMR (Laskowski et al., 1996) and excludes prolines, glycines and terminal residues.

8

Sidechain dihedral angles (χ1) noted as low frequency by WHAT_CHECK (Hooft et al., 1996). No “bad” scores (lower than 0.30) were found in any structure. In eight of the 17 structures, residue 38 was identified as a rare conformer. In seven of the structures, residue 37 was identified as a rare conformer. Residues 7, 77 and 133 occur as rare conformers in more than one structure.

9

Steric interactions occurred in ten structures between the side chain atoms Cɛ2 of Trp 16 and Hɛ22 of Gln 27, and between Cζ2 of Trp 16 and Hɛ22 of Gln 27 in seven structures. Interactions between Hɛ21 of Gln 58 and Cγ1 Ile 61 occur in nine structures. Steric interactions were detected using the van der Waals subroutine of MOLMOL (Koradi et al., 1996).