The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle

BMC Structural Biology

Table 1 Statistics for the ensemble of structures of the murine DLC2 SAM domain^a

Distance restraints
Intraresidue	377
Sequential (\|i-j\| = 1)	172
Medium range (2 ≤ \|i-j\| ≤ 4	76
Long range (4 < \|i-j\|)	95
Hydrogen bond pairs (HN-O, N-O)	42
Residual Dipolar Couplings
H-NH	23
NOE violations
> 0.5 Å	0.0 ± 0.0
> 0.3 Å	18.0 ± 3.2
Dihedral angle restraints^b
φ/ψ angles for each amino acid	57
Deviations from standard geometry (XPLOR-NIH)
Bonds	0.0125 ± 0.0004
Angles	1.4838 ± 0.0399
Impropers	1.9898 ± 0.2513
Pairwise RMSD (Secondary structure^c)
Backbone	0.64 ± 0.11 Å
All heavy atoms	1.47 ± 0.16 Å
Ramachandran Statistics^d
Most favored regions	86.6 %
Additional allowed regions	12.0 %
Generously allowed regions	1.4 %
Disallowed regions	0.0 %

^aEnsemble of the top 20 structures with lowest overall energy and number of restraint violations.
^bPredicted from chemical shifts using the PREDITOR web server.
^cRMSD values for residues 58–69, 73–81, 88–94, 103–117.
^dDetermined with PROCHECK-NMR for 10 lowest-energy structures.

ISSN: 1472-6807