BMRB Entry 11006

Title:
The Glycosylated EGF-Like Repeats 12 From Mouse NOTCH-1, NMR, Minimized Average Structure
Deposition date:
2007-08-24
Original release date:
2010-10-22
Authors:
Hiruma-Shimizu, Kazumi; Shimizu, Hiroki; Nishimura, Shin-Ichiro
Citation:

Citation: Hiruma-Shimizu, Kazumi; Hosoguchi, Kensaku; Liu, Yan; Fujitani, Naoki; Ohta, Takashi; Hinou, Hiroshi; Matsushita, Takahiko; Shimizu, Hiroki; Feizi, Ten; Nishimura, Shin-Ichiro. "Chemical Synthesis, Folding, and Structural Insights into O-Fucosylated Epidermal Growth Factor-like Repeat 12 of Mouse Notch-1 Receptor"  J. Am. Chem. Soc. 132, 14857-14865 (2010).
PubMed: 20883017

Assembly members:

Assembly members:
mouse_NOTCH-1_EGF12, polymer, 38 residues, 4211.66 Da.
disaccharide, polymer, 2 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mouse_NOTCH-1_EGF12: DVNECISNPCQNDATCLDQI GEFQCICMPGYEGVYCEX
disaccharide: XX

Data sets:
Data typeCount
1H chemical shifts262

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EGF12 peptide1
2NAG b1-3 FUC2

Entities:

Entity 1, EGF12 peptide 38 residues - 4211.66 Da.

The carboxylgroup of C terminus I38 is amidated. -COONH2

1   ASPVALASNGLUCYSILESERASNPROCYS
2   GLNASNASPALATHRCYSLEUASPGLNILE
3   GLYGLUPHEGLNCYSILECYSMETPROGLY
4   TYRGLUGLYVALTYRCYSGLUILE_NH2

Entity 2, NAG b1-3 FUC 2 residues - Formula weight is not available

1   FUCNAG

Samples:

sample_1: mouse NOTCH-1 EGF12 0.55 mM; NAG b1-3 FUC 0.55 mM

sample_conditions_1: ionic strength: 0 M; pH: 5.3; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17527 17528
PDB