BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34101

Title: Solution structure of the Dbl-homology domain of Bcr-Abl   PubMed: 29235475

Deposition date: 2017-02-16 Original release date: 2017-12-21

Authors: Reckel, S.; Lohr, F.; Buchner, L.; Guntert, P.; Dotsch, V.; Hantschel, O.

Citation: Reckel, Sina; Gehin, Charlotte; Tardivon, Delphine; Georgeon, Sandrine; Kukenshoner, Tim; Lohr, Frank; Koide, Akiko; Buchner, Lena; Panjkovich, Alejandro; Reynaud, Aline; Pinho, Sara; Gerig, Barbara; Svergun, Dmitri; Pojer, Florence; Guntert, Peter; Dotsch, Volker; Koide, Shohei; Gavin, Anne-Claude; Hantschel, Oliver. "Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase"  Nat. Commun. 8, 2101-2101 (2017).

Assembly members:
entity_1, polymer, 218 residues, 24844.432 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):
entity_1: AMASELDLEKGLEMRKWVLS GILASEETYLSHLEALLLPM KPLKAAATTSQPVLTSQQIE TIFFKVPELYEIHKEFYDGL FPRVQQWSHQQRVGDLFQKL ASQLGVYRAFVDNYGVAMEM AEKCCQANAQFAEISENLRA RSNKDAKDPTTKNSLETLLY KPVDRVTRSTLVLHDLLKHT PASHPDHPLLQDALRISQNF LSSINEEITPRRQSMTVK

Data sets:
Data typeCount
13C chemical shifts1008
15N chemical shifts210
1H chemical shifts1656

Additional metadata:

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