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 27432

Title: Solution structure of the cross-linked dimer of the SLy1 SAM domain S320C mutant   PubMed: 30631134

Deposition date: 2018-03-21 Original release date: 2019-01-25

Authors: Kukuk, Laura; Dingley, Andrew; Koenig, Bernd

Citation: Kukuk, Laura; Dingley, Andrew; Granzin, Joachim; Nagel-Steger, Luitgard; Thiagarajan-Rosenkranz, Pallavi; Ciupka, Daniel; Hanel, Karen; Batra-Safferling, Renu; Pacheco, Victor; Stoldt, Matthias; Pfeffer, Klaus; Beer-Hammer, Sandra; Willbold, Dieter; Koenig, Bernd. "Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association."  Sci. Rep. 9, 54-54 (2019).

Assembly members:
Sly1_SAM, polymer, 69 residues, 7940.9134 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
Sly1_SAM: GPKTLHELLERIGLEEHTST LLLNGYQTLEDFKELRETHL NELNIMDPQHRAKLLTAAEL LLDYDTGCE

Data sets:
Data typeCount
13C chemical shifts316
15N chemical shifts72
1H chemical shifts504

Additional metadata:

  • Assembly
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Related Database Links:

UNP Q8K352

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