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. 2011 Nov 2;17(3):331–343. doi: 10.1007/s00775-011-0855-y

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© The Author(s) 2011

This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.

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Fig. 7 — Multiple sequence alignments of HpSlyD and its homologues using the MUSCLE algorithm [56] with default parameters. Secondary structure elements were annotated by Geneious 5.3.4 (http://www.geneious.com) according to the calculated NMR structure as shown in Fig. 2c and other resolved structures of SlyD homologues. The α2 helix (in red) is only present in FKBP from Methanothermococcus thermolithotrophicus (MtFKBP17). Identical and similar residues between the homologues are highlighted in black or gray. The conserved HGHXH sequence previously mentioned is encircled in a red box. Residues of peptidylprolyl isomerase (PPIase) catalytic sites of HpSlyD are highlighted with blue. The UniPort accession numbers are as follows: Q6MQW6 (Bdellovibrio bacteriovorus SlyD), A1VXJ8 (Campylobacter jejuni SlyD), P0A9K9 (EcSlyD), P44830 (Haemophilus influenza SlyD), O25748 (HpSlyD), Q0EWE3 (Mariprofundus ferrooxydans), Q2W0E9 (Magnetospirillum magneticum), A3CV43 (Methanoculleus marisnigri FKBP PPIase), O52980 (MtFKBP17), Q82U07 (Nitrosomonas europaea SlyD), C7N8E0 (Slackia heliotrinireducens PPIase), O83369 (Treponema pallidum SlyD), and Q5SLE7 (TtSlyD)