Ascl1 human bHLH transcription factor.
Ascl1 was studied by generating different overlapping fragments (A,B,C and D)
that represent different functional motifs on the Ascl1 polypeptide chain.
Fragment D is composed of a 44 aa tag at the N-terminus followed by residues
118-236 of the full length sequence.

The reported chemical shift assignment is numbered according to "Baronti_et_al.".
All assigned chemical shifts of Ascl1 fragments deposited start from the first
biologically relevant aminoacid and do not take into account the artificial tag
at the N-terminus (see "Baronti_et_al.").

Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1.

Basic Helix-Loop-Helix (bHLH) DNA binding domain and disordered C-terminal domain of Ascl1.
Fragment 118-236 of the full length sequence.

Residues 1-44 represent the artificial affinity and solubility tag.
Ascl1 fragment D chemical shift assignment start from residue 45
(residue 1 in the assignment file).

Basic Helix-Loop-Helix (bHLH) DNA binding domain and disordered C-terminal domain of Ascl1. Fragment 118-236 of the full length sequence.

Magnetic Resonance Center - University of Florence Italy

A set of 3D BEST-TROSY HCN and HNN spectra were recorded for sequential
resonance assignment, complemented by a sequential HADAMAC experiment for
amino-acid type identification.

Equipped with cryogenically cooled triple-resonance probeheads (TCI)