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 11032

Title: Solution structure of the knotted tudor domain of the yeast histone acetyltransferase protein, Esa1   PubMed: 18407291

Deposition date: 2008-03-01 Original release date: 2008-04-16

Authors: Shimojo, Hideaki; Sano, Norihiko; Moriwaki, Yoshihito; Okuda, Masahiko; Horikoshi, Masami; Nishimura, Yoshifumi

Citation: Shimojo, Hideaki; Sano, Norihiko; Moriwaki, Yoshihito; Okuda, Masahiko; Horikoshi, Masami; Nishimura, Yoshifumi. "Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain"  J. Mol. Biol. 378, 987-1001 (2008).

Assembly members:
Residues 1-89, polymer, 92 residues, 10791.321 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Residues 1-89: GSHMSHDGKEEPGIAKKINS VDDIIIKCQCWVQKNDEERL AEILSINTRKAPPKFYVHYV NYNKRLDEWITTDRINLDKE VLYPKLKATDED

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts96
1H chemical shifts676

Additional metadata:

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

BMRB 11033
PDB 2RNZ 2RO0
DBJ GAA26555
EMBL CAA99465 CAY86525
GB AHY77525 AJP41755 AJT71177 AJT71665 AJT72155
REF NP_014887
SP Q08649
TPG DAA11012

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