Human Glucocorticoid Receptor DNA binding domain (DBD) assigned chemical shifts

We use methanol as an external reference to calibrate the temperature of our
spectrometers, which we then correct for during our experiments, according to
the methods in (1), which is based on the work of (2,3).
1. J. Cavanagh, W.J. Fairbrother, A.G. Palmer, M. Rance, N. J. Skelton. (1995)
Protein NMR Spectroscopy. Elsevier Academic Press.
2. A.J. Hartel, P.P. Lankhorst, C. Altona.
Eur. J. Biochem. 129, 343-357 (1982).
3. L.P.M. Orbons, G.A. van der Marel, J.H. van Boom, C. Altona.
Eur. J. Biochem. 170, 225-239 (1987).

Conserved allosteric ensembles in disordered proteins using TROSY/anti-TROSY R2-filtered spectroscopy.

The initial 5 amino acids remain after thrombin cleavage;
residue 420 is the initial L in the sequence.

first zinc finger spans residues 421-441

second zinc finger spans residues 457-476

Assigned chemical shifts for residues 420-501 from the human glucocorticoid receptor

JHU Biomolecular NMR Facility 600 MHz magnet

assignments for the D3 translational isoform of GR (336-525)

assignments for the D2 translational isoform of GR (331-525)

assignments for the D1 translational isoform of GR (316-525)

165 uM DBD, 10% D2O, 20 mM Na2HPO4, pH 7.0, 100 mM NaCl, 5 mM TCEP;
samples were thoroughly purged of oxygen under nitrogen and argon,
stored in Shigemi tubes to minimize oxidation of zinc fingers.