13C/15N/1H chemical shift assignments for Human Cytomegalovirus Protease delta221

Truncated monomeric construct (residues 1-221) and containing a non-native N-terminal His6-tag.

Used average and standard deviation of shifts from all spectral assignments.

separate tube (no insert) similar to the experimental sample tube

Referenced against 10mM DSS in pH 7 phosphate buffer/150mM KCl.

Inhibiting a dynamic viral protease by targeting a non-catalytic cysteine.

Enzyme inhibition by allosteric capture of an inactive conformation.

Broad-spectrum allosteric inhibition of herpesvirus proteases.

Fragment-Based Protein-Protein Interaction Antagonists of a Viral Dimeric Protease.

Formula mass does not contain the N-terminal His6-tag.
Human Cytomegalovirus Protease delta 221

Truncation(residues 1-221)
A141V
A143V
P144A
A209V

Contains a non-native N-terminal Met+His6-tag (residues -7 to -1).
Residue numbering begins at Met1.
This is a C-terminal truncated construct that ends with L221.

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Backbone and side-chain chemical shift assignments for human cytomegalovirus protease delta221 (residues 1-221).
Residues 222-256 truncated from wild-type sequence.

Craik Lab; Dept. of Pharmaceutical Chemistry, UC San Francisco

500 MHz Bruker DRX 4-channel spectrometer equipped with Z-gradient, lock-switch for deuterium decoupling, and a 60-slot BACS sample changer.
Triple-resonance QCI-Cryoprobe with cold 1H and 13C preamps for detection/decoupling of 1H, 13C, and 15N.

800 MHz, 4-channel spectrometer with triple-axis gradients, lock-switch for deuterium decoupling and ultra-shielded US2 magnet.
5mm triple-resonance Z-gradient TXI-Cryoprobe.

Default sample conditions: 25mM KPi (pH 7), 150mM KCl, 0.1mM EDTA, 1mM DTT.

Version of Topspin running on the Bruker DRX500.

Version of Topspin running on the Bruker AV800.