The assembly contains metal coordination bonds within the Zinc-finger motifs

Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 21 03:50:37 2007

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

NMR assignment of the N-terminal TRAF-like RING zinc finger domain of human FLN29.

This construct contains the first 140 residues in N-terminal of the full 582 residues protein.
The glycine residue in position 1 results from the TEV protease cleavage of the Histidine tag and is not part of the native N-terminal FLN29 sequence

unnamed protein product [Macaca fascicularis]

TRAF-type zinc finger domain containing 1 [synthetic construct]

TRAF-type zinc finger domain containing 1 [Homo sapiens]

TRAF-type zinc finger domain containing 1, isoform CRA_a [Homo sapiens]

TRAF-type zinc finger domain-containing protein 1 [Homo sapiens]

TRAF-type zinc finger domain-containing protein 1 [Macaca mulatta]

TRAF-type zinc finger domain-containing protein 1 [Macaca fascicularis]

PREDICTED: TRAF-type zinc finger domain-containing protein 1 isoform X1 [Callithrix jacchus]

RecName: Full=TRAF-type zinc finger domain-containing protein 1; AltName: Full=Protein FLN29

RecName: Full=TRAF-type zinc finger domain-containing protein 1

gene of unknown function located at hCh12q24.1

N-terminal TRAF-like RING zinc finger domain of human FLN29
1H 13C and 15N chemical shift for the human FLN29

Aubin Group, Centre for Biologics Research, Health Canada

Health Canada
triple resonance cryoprobe

IRIC Montreal
triple resonance cryoprobe

200 uM FLN29
20 mM NaPi
50 uM ZnCl2
1 mM DTT pH 7.4

400 uM FLN29
20 mM NaPi
50 uM ZnCl2
1 mM DTT pH 7.4

Buffer
20 mM NaPi
50 uM ZnCl2
1 mM DTT pH 7.4

NMR spectra processing and displaying software

assisted protein sequential NMR assignments

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax