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 17552

Title: Backbone resonance chemical shift assignments of Ph SAM linker   PubMed: 22275371

Deposition date: 2011-03-28 Original release date: 2012-05-10

Authors: Ilangovan, Udayar; Kim, Chongwoo

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).

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

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

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

Entity Sequences (FASTA):
Ph_SAM_Linker: GTRGVGSGETNGLGTGGIVG VDAMALVDRLDEAMAEEKMQ TEATPKLSESFILGASTEVP MSLPVQAAISALAAPLGSLS VALPTLAPLSVVTSGAAPKS SEVNGTDR

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

Samples:

sample_1: Ph SAM Linker, [U-100% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_2: Ph SAM Linker, [U-100% 13C; U-100% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectral Visualization

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker DRX 600 MHz

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