BMRB Entry 17552

Title:
Backbone resonance chemical shift assignments of Ph SAM linker
Deposition date:
2011-03-28
Original release date:
2012-05-10
Authors:
Ilangovan, Udayar; Kim, Chongwoo
Citation:

Citation: Robinson, Angela; Leal, Belinda; Chadwell, Linda; Wang, Renjing; Ilangovan, Udayar; Kaur, Yogeet; Junco, Sarah; Schirf, Virgil; Osmulski, Pawel; Gaczynska, Maria; Hinck, Andrew; Demeler, Borries; McEwen, Donald; Kim, Chongwoo. "The growth-suppressive function of the polycomb group protein polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain."  J. Biol. Chem. 287, 8702-8713 (2012).
PubMed: 22275371

Assembly members:

Assembly members:
Ph_SAM_Linker, polymer, 108 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-3c

Data sets:
Data typeCount
13C chemical shifts203
15N chemical shifts98
1H chemical shifts98

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ph SAM linker1

Entities:

Entity 1, Ph SAM linker 108 residues - Formula weight is not available

1   GLYTHRARGGLYVALGLYSERGLYGLUTHR
2   ASNGLYLEUGLYTHRGLYGLYILEVALGLY
3   VALASPALAMETALALEUVALASPARGLEU
4   ASPGLUALAMETALAGLUGLULYSMETGLN
5   THRGLUALATHRPROLYSLEUSERGLUSER
6   PHEILELEUGLYALASERTHRGLUVALPRO
7   METSERLEUPROVALGLNALAALAILESER
8   ALALEUALAALAPROLEUGLYSERLEUSER
9   VALALALEUPROTHRLEUALAPROLEUSER
10   VALVALTHRSERGLYALAALAPROLYSSER
11   SERGLUVALASNGLYTHRASPARG

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks