Thesis Title: Subtitle - NMR Spectroscopy Research Group

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Figure S2.3 Assigned constant-time 13 C-HSQC spectrum of the cz- 186/ /La 3+ complex, where cz-
186 was biosynthetically fractionally 13 C-labeled using 20% uniformly 13 C-labeled
glucose ................................................................................................................................. 58
Figure S2.4 Assigned constant-time 13 C-HSQC spectrum of the cz- 186/ /La 3+ complex
containing 13 C/ 15 N-Leu labeled cz- 186 (blue) superimposed onto a 2D (H)C(C)H-
TOCSY spectrum of the same sample (red) ........................................................................ 59
Figure S2.5 Comparisons of calculated and experimental PCS in the cz- 186/ /Dy 3+ complex for
methyl groups of (a) Met, (b) Ala, (c) Thr, (d) Val, (e) Leu, and (f) Ile ............................. 60
Figure S2.6 Comparisons of calculated and experimental 13 C and 1 H PCS as in Figure S2.5 but for
the cz- 186/ /Yb 3+ complex. ............................................................................................... 62
Figure 3.1 Screenshots of Numbat main windows ........................................................................... 80
Figure 3.2 Euler angle definitions used by Numbat ......................................................................... 84
Figure 3.3 Visualisation of the Δχ-tensor in MOLMOL and PyMOL, and display of its
orientational uncertainty in a Sanson-Flamsteed projection plot ........................................ 85
Figure 3.4 The four degenerate solutions arising from the symmetry of the Δχ-tensor around the x,
y and z axes ......................................................................................................................... 92
Figure 3.5 The complex between ε186 and θ determined by superimposition of Δχ-tensors .......... 92
Figure 4.1 Fold identification by pseudocontact shifts ................................................................... 106
Figure 4.2 Improved conformational sampling by PCS-ROSETTA .............................................. 108
Figure 4.3 Energy landscapes generated by PCS-ROSETTA ........................................................ 108
Figure 4.4 Superimpositions of ribbon representations of the backbones of the lowest energy
structures calculated with PCS-ROSETTA (blue) onto the corresponding target structures
(red) ................................................................................................................................... 110
Figure S4.1 Fold identification by pseudocontact shift score and ROSETTA energy ................... 119
Figure S4.2 Improved fragment assembly by PCS-ROSETTA ..................................................... 120
Figure S4.3 Energy landscape generated by CS-ROSETTA and PCS-ROSETTA, with full atom
ROSETTA energies and C α rmsd values being calculated using only the core residues as
defined in Table S4.1 ......................................................................................................... 121
Figure S4.4 Identification of successful calculations with PCS-ROSETTA .................................. 122
Figure S4.5 Flow diagram of PCS-ROSETTA ............................................................................... 123
Figure S4.6 Expected C α rmsd of the lowest energy structure calculated with PCS-ROSETTA .. 124
Figure 5.1 Capacity of the PCS score, as the only energy term, to fold the protein ....................... 131
Figure 5.2 The intersection of isosurfaces defines the position and orientation of peptide fragments
in the protein structure ....................................................................................................... 131