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. Author manuscript; available in PMC: 2019 Mar 14.
Published in final edited form as: FEBS J. 2018 Oct 1;285(22):4165–4180. doi: 10.1111/febs.14660

Table 1. Summary of conformational constraints and statistics for the 20 accepted NMR structures of the human INI1/SNF5 RPT1 domain.


Structural constraints
   Intraresidue 663
   Sequential 393
   Medium-range (2 < |ij| < 4) 421
   Long-range (|ij| > 4) 539
   Dihedral angle constraints 21
   TALOS constraintsa 124
   Distance constraints for 38 hydrogen bonds 76
   Total 2237
Statistics for accepted structures
   Statistical parameters (±SD)
      RMS deviation for distance constraints 0.0070 ± 0.0004 Å
      RMS deviation for dihedral constraints  0.342 ± 0.024°
    Mean CNS energy term (kcal·mol−1 ± SD)
      E (overall) 80.61 ± 4.31
      E (van der Waals) 19.87 ± 1.35
      E (distance constraints) 7.69 ± 0.91
      E (dihedral and TALOS constraints) 2.07 ± 0.28
   RMS deviations from the ideal geometry (SD)
      Bond lengths 0.0015 ± 0.0001 Å
      Bond angles 0.356 ± 0.0078°
      Improper angles   0.250 ± 0.009°
   Average atomic RMSD from the mean structure (SD)
      Residues 184–249 (backbone)b 0.237 ± 0.053 Å
      Residues 184–249 (all heavy atoms)c 0.720 ± 0.062 Å
Structural qualityd
   Residues in most favored region of Ramachanran Plot 88.4%
   Residues in additional allowed region of Ramachandran Plot 10.4%
   Residues in generously allowed region of Ramachandran Plot 1.2%
   Residues in disallowed region of Ramachandran Plot 0.0%
PDB code 5L7B

a

Dihedral angles are estimated using TALOS+-based chemical shifts of backbone atoms of each amino acid.

b

Backbone heavy atoms include backbone N, Ca, CO.

c

Heavy atoms include both backbone and side chain non-hydrogen atoms.

d

Statistics are for residues 184–259.