1. Volume 115, Issue 1, Pages 139-146 (July 1998)
Three-dimensional structure of the major autoantigen in primary biliary cirrhosis 
Mark J. Howard*, Christopher Fuller*, R.William Broadhurst*, Richard N. Perham*, Jian–Guo Tang*, Janet Quinn‡, Austin G. Diamond§, Stephen J. Yeaman‡ 
Gastroenterology 
Volume 115, Issue 1, Pages (July 1998)
DOI: /S (98)
Copyright © 1998 American Gastroenterological Association Terms and Conditions

2. Fig. 1
Two-dimensional 15N-1H multiple quantum correlation spectrum of the inner human lipoyl domain. The spectrum was recorded at pH 6.5 and 308 K. The horizontal axis is proton chemical shift (parts per million relative to 2, 2-dimethyl-2-silapentane-5-sulfonic acid), and vertical axis is 15N chemical shift (parts per million relative to external NH3).
Gastroenterology  , DOI: ( /S (98) )
Copyright © 1998 American Gastroenterological Association Terms and Conditions

3. Fig. 2
Summary of the data used in the sequential assignment and secondary structure determination of the inner lipoyl domain of E2p from human PDC. The arrowheads define the direction of the strands with the dotted lines indicating strands that comprise one β sheet and the solid lines the other. The circles indicate the residues that showed slowly exchanging amide protons, stereospecifically assigned β protons, and coupling constants, which were incorporated in the structure calculations.
Gastroenterology  , DOI: ( /S (98) )
Copyright © 1998 American Gastroenterological Association Terms and Conditions

4. Fig. 3
1H, 1H NOE contact map for the inner human lipoyl domain showing the characteristic pattern for antiparallel β-sheet structure.
Gastroenterology  , DOI: ( /S (98) )
Copyright © 1998 American Gastroenterological Association Terms and Conditions

5. Fig. 4
Superposition of 26 conformers of the inner lipoyl domain of E2p from human PDC. The structures were generated by X-PLOR 3.1 from 1136 NOE restraints, 43 torsion angle restraints, and 28 hydrogen bond restraints. The relatively poorly defined lipoyl-lysine β turn (Asp49 to Ala51) and surface loop (Leu14 to Gly24) are at the top and the N- and C-terminal residues of the domain are at the bottom. The orientation is identical to the MOLSCRIPT representation in Figure 5.
Gastroenterology  , DOI: ( /S (98) )
Copyright © 1998 American Gastroenterological Association Terms and Conditions

6. Fig. 5
Stereo representation of the polypeptide fold (residues His9 to Val85) for the inner lipoyl domain of E2p from human PDC. The site of lipoylation (Lys50) is indicated, together with the type I β turn (black). The β sheet containing the immunologically important lipoyl-lysine residue is shown in dark grey; the β sheet containing the N- and C-terminal residues is shown in light grey. The figure was created using the program MOLSCRIPT.
Gastroenterology  , DOI: ( /S (98) )
Copyright © 1998 American Gastroenterological Association Terms and Conditions

7. Fig. 6
Amino acid sequence and secondary structure alignment of lipoyl domains. The position of each β strand is shown in bold and the amino acid sequence motif harboring the lipoyl-lysine residue at the tip of the β turn is italicized. AVE2o, A. vinelandii E2o; AVE2p-1, A. vinelandii; E2p innermost domain; BSE2p, B. stearothermophilus E2p; ECE2o, E. coli E2o; ECE2p-h, E. coli E2p hybrid domain; human E2p-1, human E2p inner domain (this study). For references, see text.
Gastroenterology  , DOI: ( /S (98) )
Copyright © 1998 American Gastroenterological Association Terms and Conditions