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 18559

Title: Solution NMR structure of the PHD domain of human MLL5. Northeast structural genomics consortium target HR6512A.   PubMed: 24130829

Deposition date: 2012-06-29 Original release date: 2012-07-31

Authors: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Wu, Hong; Min, Jinrong; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Wu, Hong; Yap, Damian; Zeng, Hong; Dombrovski, Ludmila; Houliston, Scott; Aparicio, Samuel; Arrowsmith, Cheryl. "Solution NMR structure and histone binding of the PHD domain of human MLL5."  PLoS ONE 8, e77020-e77020 (2013).

Assembly members:
MLL5, polymer, 98 residues, 9318.508 Da.
ZINC ION, non-polymer, 65.409 Da.

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

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

Entity Sequences (FASTA):
MLL5: MHHHHHHSSGRENLYFQGSE DGSYGTDVTRCICGFTHDDG YMICCDKCSVWQHIDCMGID RQHIPDTYLCERCQPRNLDK ERAVLLQRRKRENMSDGD

Data sets:
Data typeCount
13C chemical shifts298
15N chemical shifts74
1H chemical shifts472

Additional metadata:

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

PDB 2LV9 4L58
DBJ BAE28389 BAE35839 BAE43262 BAE88379
EMBL CAH93210
GB AAD04721 AAF75564 AAH01296 AAH36286 AAH62583
REF NP_001075920 NP_001094321 NP_061152 NP_081260 NP_891847
SP Q3UG20 Q8IZD2
TPG DAA30676

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