Correction: The Translocation Domain of Botulinum Neurotoxin A Moderates the Propensity of the Catalytic Domain to Interact with Membranes at Acidic pH.

[This corrects the article DOI: 10.1371/journal.pone.0153401.].

A reference was incorrectly omitted in Table 1. The authors have provided the reference and a corrected table here.

46. Micsonai A, Wien F, Kernya L, Lee YH, Goto Y, Réfrégiers M, Kardos J. Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy. Proc Natl Acad Sci U S A. 2015; 112: E3095–E3103. doi 10.1073/pnas.1500851112. PMID:26038575.

Table 1

Comparison of the secondary structure of the three proteins based on the far-UV CD spectra at pH 7 (BeStSel [46]) with the secondary structure observed in the crystal structure of BoNT/A (3BTA) (STRIDE PDB).

	BeStSel				STRIDE PDB
	LC	HN	LC-HN	LC + HN isolated	LC	HN	LC-HN	LC + HN isolated
alpha	28.3	51.8	39.6	40.05	30.2	50.2	40.7	40.2
beta	17.3	7	14.2	12.15	14	1.4	9.7	7.7
Others1	54.4	41.2	46.2	47.8	55.8	48.4	49.6	52.1

1Others: turns and random coils