Table 1 NMR and refinement statistics for Heimdallarchaeota profilin.

From: Heimdallarchaea encodes profilin with eukaryotic-like actin regulation and polyproline binding

 

Heimdallarchaeota profilin

NMR distance and dihedral constraints

1980

Distance constraints

   Total NOE

1135

   Intra-residue

161

Inter-residue

   Sequential (|ij | = 1)

322

   Medium-range (|ij | < 4)

252

   Long-range (|ij | > 5)

400

Intermolecular

   Hydrogen bonds

43

Total dihedral angle restraints

   ϕ

98

   ψ

98

   3JHNαscalar couplings

83

Structure statistics

   Violations (mean and s.d.)

0

   Distance constraints (Å)

0.3

   Dihedral angle constraints (°)

0

   Max. dihedral angle violation (°)

0

   Max. distance constraint violation (Å)

0.3

Deviations from idealized geometry

   Bond lengths (Å)

3

   Bond angles (°)

0

   Impropers (°)

0

Average pairwise r.m.s. deviation (residues 21–145 (Å)

   Heavy

1.05 ± 0.27

   Backbone

0.50 ± 0.22

  1. “Pairwise r.m.s. the deviation was calculated among 20 refined structures.”
  2. Ramachandran statistics are in the Methods section at end of the Refinement subsection.