1. Volume 16, Issue 6, Pages 965-975 (June 2008)
Solution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine Transferase 
Xu Wang, Thomas Weldeghiorghis, Guofeng Zhang, Barbara Imperiali, James H. Prestegard 
Structure 
Volume 16, Issue 6, Pages (June 2008)
DOI: /j.str
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2. Figure 1
Predicted Secondary Structural Elements and Experimentally Determined Secondary Structural Elements
Prediction is done using secondary prediction function of mGenthreader (Jones, 1999). Experimental secondary structure is determined using back bone dihedral angles predicted using TALOS and chemical shifts.
Structure  , DOI: ( /j.str )
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3. Figure 2 Annotated HSQC Spectrum of Deuterated Alg13
Each assigned peak is labeled with the residue number and one letter residue name.
Structure  , DOI: ( /j.str )
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4. Figure 3 Structural Representations of Alg13
(A) Backbone ensemble of 10 lowest energy Alg13 structures from 50 structures calculated using XPLOR-NIH. Residues 30–220 are shown. The backbone is colored on the basis of secondary structure.
(B) Schematic ribbon diagram of the Alg13 structure.
Structure  , DOI: ( /j.str )
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5. Figure 4 Topology Representations of Alg 13
(A) Schematic illustration of the predicted topology of Alg13. The numbering of the element is according to the scheme from Figure 1. Note that the predicted helix after β2 gave rise to both α3 and β3.
(B) Schematic illustration of the experimentally determined topology of Alg13.
Structure  , DOI: ( /j.str )
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6. Figure 5 Rotational Correlation Time Measurements of Alg13
The error range in the rotational correlation time is calculated specifically for each residue as follows: the upper error range is the difference between the maximum rotational correlation time found in the Monte Carlo search (confidence level 90%) and the best-fitting time found in the search. The lower error range is the difference between the minimum rotational correlation time found in the search (confidence level 90%) and the best fitting time found in the search. The C terminus is considerably more dynamic than the rest of the protein.
Structure  , DOI: ( /j.str )
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7. Figure 6 Ligand-Binding Sites in Alg13
(A) Chemical shift changes produced by 2.6 mM UDP-GlcNAc. The two horizontal lines on the graph represent standard deviations in chemical shift changes.
(B) Mapping of UDP-GlcNAc-generated chemical shift changes on Alg13 structure. Residues with perturbation bigger than two standard deviations are colored red. This includes residues 35, 39, 123, 126, 143, 144, 145, 147, 148, 150, 155, 158, 159, 160, 166, 168, and 169. Side chains of possible carbohydrate-interacting residues (residues 165–158) are shown in green.
(C) Mapping of UDP-TEMPO-generated signal dispersion on Alg13 structure. Residues 41, 124–126, 139, 146, 150, 161–169, 171, 174, 175, and 213–220 are peaks that have disappeared in the presence of TEMPO and reappeared after reduction and are colored in blue. Residues 35–39, 141, 143, 144, 145, 147, 148, and 160 are peaks that have disappeared in the presence of TEMPO but failed to reappear after reduction of TEMPO and are colored in red. Side chains of possible carbohydrate-interacting residues (residues 165–158) are shown in green.
Structure  , DOI: ( /j.str )
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