Table 1 NMR and refinement statistics for VPS37A21–148

From: Identification of membrane curvature sensing motifs essential for VPS37A phagophore recruitment and autophagosome closure

 

Protein

NMR distance and dihedral constraints

Distance constraints

 Total NOE

2385

 Intra-residue

538

 Inter-residue

1847

  Sequential (|i – j | = 1)

666

  Medium-range (1 < |i – j | ≤ 4)

417

  Long-range (|i – j | ≥ 5)

764

  Intermolecular

0

 Hydrogen bonds

0

Total dihedral angle restraints

  ϕ

97

  ψ

97

Total RDC restraints

  Phage

74

Structure statistics

Violations (mean and s.d.)

  Distance constraints (Å)

0.066 ± 0.001

  Dihedral angle constraints (°)

0.667 ± 0.093

  Max. dihedral angle violation (°)

7.7

  Max. distance constraint violation (Å)

0.67

Deviations from idealized geometry

  Bond lengths (Å)

0.004 ± 0.000

  Bond angles (°)

0.611 ± 0.006

  Impropers (°)

0.504 ± 0.010

Q factora

0.12 ± 0.01

Average pairwise r.m.s. deviationb (Å)

  Heavy

0.9

  Backbone

0.3

  1. aDefinition of the RDC Q factor is given in the literature43.
  2. bPairwise r.m.s. deviation was calculated among 10 refined structures. Evaluated for secondary structure elements: 24–39, 44–45, 51–58, 61–68, 79–83, 86–87, 101–104, 112–125, 129–130.