BMRB Entry 15001

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Title: Structures and chemical shift assignments for the ADD domain of the ATRX protein   PubMed: 17609377

Deposition date: 2006-09-13 Original release date: 2007-06-18

Authors: Yang, Ji-Chun; Neuhaus, David

Citation: Argentaro, Anthony; Yang, Ji-Chun; Chapman, Lynda; Kowalczyk, Monika; Gibbons, Richard; Higgs, Douglas; Neuhaus, David; Rhodes, Daniela. "Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX"  Proc. Natl. Acad. Sci. U. S. A. 104, 11939-11944 (2007).

Assembly members:
ADD_domain_156-296, polymer, 142 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ADD_domain_156-296: GAMADKRGDGLHGIVSCTAC GQQVNHFQKDSIYRHPSLQV LICKNCFKYYMSDDISRDSD GMDEQCRWCAEGGNLICCDF CHNAFCKKCILRNLGRKELS TIMDENNQWYCYICHPEPLL DLVTACNSVFENLEQLLQQN KK

Additional metadata:

• Assembly
• Samples and Experiments
• Software
• Spectrometers
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Related Database Links:

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts