Horne J, d Auvergne EJ, Coles M, Velkov T, Chin Y, Charman WN, et al. Probing the Flexibility of the DsbA Oxidoreductase from Vibrio cholerae a 15N - 1H Heteronuclear NMR Relaxation Analysis of Oxidized and Reduced Forms of DsbA. J Mol Biol. 2007 Aug;371(3):703 16.
Probing the flexibility of the DsbA oxidoreductase from Vibrio cholerae--a 15N - 1H heteronuclear NMR relaxation analysis of oxidized and reduced forms of DsbA.

d'Auvergne, E. J. and Gooley, P. R. (2008).
Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces.
J. Biomol. NMR, 40(2), 107-119.

Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces.

d'Auvergne, E. J. and Gooley, P. R. (2008).
Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor.
J. Biomol. NMR, 40(2), 121-133.

Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor.

Residues 1-15 (-14-0) represent a non-native affinity tag. This is the extracellular domain of a membrane protein.

The first residue (0, M) is the start codon from the bacterial expression system and hence not present in the native protein.

This antigen is derived from vasoactive intestinal peptide type 1 receptor.

Relaxation and model-free data from beta-2-microglobulin and the heavy chain of the MHC class I complex HLA-B*27:05 in complex with the nonamer peptide pVIPR (RRKWRRWHL).
Relaxation and model-free data from beta-2-microglobulin and the heavy chain of HLA-B*27:05 in complex with the peptide pVIPR

Chemical shifts for the beta-2 Microglobulin subunit of HLA-B*27:05/pVIPR

Chemical shifts for the heavy chain of of HLA-B*27:05/pVIPR