Skip to main content
. Author manuscript; available in PMC: 2013 Mar 1.
Published in final edited form as: Nat Struct Mol Biol. 2012 Aug 5;19(9):916–924. doi: 10.1038/nsmb.2353

Table 2.

NMR and refinement statistics

PHF20 Tudor2–p53KC370me2
NMR distance and dihedral constraints
Distance constraints
Total NOE 3,022
 Intra-residue 479
 Sequential (|ij| = 1) 476
 Medium-range (|ij| < 5) 260
 Long-range (|ij| ≥5) 666
 Ambiguous 1,141
Hydrogen bonds 27
Total dihedral angle restraints 105
φ 32
ψ 33
χ1 40
Structure statistics
Violations (mean and s.d.)
 Distance constraints (Å) 0.10 ± 0.02
 Dihedral angle constraints (°) 2.66 ± 0.94
 Max. dihedral angle violation (°) 3.98 ± 0.37
 Max. distance constraint violation (Å) 0.21 ± 0.01
Deviations from idealized geometry
 Bond lengths (Å) 0.0085 ± 0.0001
 Bond angles (°) 2.15 ± 0.02
 Impropers (°) 0.22 ± 0.02
Average pairwise r.m.s. deviationa (Å)
 Heavy 0.72 ± 0.11
Ramachandran plot
 Favored region (%) 88.9
 Allowed region (%) 9.7
a

Pairwise r.m.s. deviation was calculated for residues 91–138 from an ensemble of 20 structures.