Table 1 NMR and refinement statistics for SCPs-A6 and G6 structures.

From: Development of chimeric peptides to facilitate the neutralisation of lipopolysaccharides during bactericidal targeting of multidrug-resistant Escherichia coli

 

A6

G6

NMR distance and dihedral constraints

Distance constraints

Total NOE

392

336

 Unambiguous

317

274

  Intra-residue

170

169

  Inter-residue

147

105

   Sequential (|i – j| = 1)

88

75

   Medium-range (1 < |i – j| < 5)

13

10

   Long-range (|i – j| > = 5)

46

20

 Ambiguous

75

62

Total dihedral angle restraints

 ϕ

37

25

 ψ

37

25

Structure statistics

Violations (mean and s.d.)

 Distance constraints (Å)

0.0317 ± 0.00339

0.0163 ± 0.00270

 Dihedral angle constraints (º)

0.524 ± 0.174

0.311 ± 0.163

Deviations from idealized geometry

  

 Bond lengths (Å)

0.00341 ± 0.000202

0.00317 ± 0.000131

 Bond angles (º)

0.450 ± 0.0194

0.407 ± 0.0251

 Impropers (º)

1.07 ± 0.173

0.852 ± 0.134

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

 Heavy

1.96b

1.95c

 Backbone

0.61b

0.68c

  1. aCalculated using the ordered residues in the killing domain of A6 (residue 29–43) and G6 (residue 24–38).
  2. bPairwise r.m.s. deviation was calculated among 20 refined structures.
  3. cPairwise r.m.s. deviation was calculated among 10 refined structures.
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