BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34040

Title: N-terminal motif dimerization of EGFR transmembrane domain in bicellar environment   PubMed: 28291355

Deposition date: 2016-09-12 Original release date: 2017-03-30

Authors: Bragin, P.; Bocharov, E.; Mineev, K.; Bocharova, O.; Arseniev, A.

Citation: Bocharov, E.; Bragin, P.; Pavlov, K.; Bocharova, O.; Mineev, K.; Polyansky, A.; Volynsky, P.; Efremov, R.; Arseniev, A.. "The Conformation of the Epidermal Growth Factor Receptor Transmembrane Domain Dimer Dynamically Adapts to the Local Membrane Environment."  Biochemistry 56, 1697-1705 (2017).

Assembly members:
entity_1, polymer, 44 residues, 4733.849 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: EGCPTNGPKIPSIATGMVGA LLLLLVVALGIGLFMRRRHI VRKR

Data sets:
Data typeCount
13C chemical shifts190
15N chemical shifts42
1H chemical shifts322

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 44 residues - 4733.849 Da.

1   GLUGLYCYSPROTHRASNGLYPROLYSILE
2   PROSERILEALATHRGLYMETVALGLYALA
3   LEULEULEULEULEUVALVALALALEUGLY
4   ILEGLYLEUPHEMETARGARGARGHISILE
5   VALARGLYSARG

Samples:

sample_1: entity_1 mM; DHPC, [U-2H], 30 mM; DMPC, [U-2H], 10 mM; TCEP 5 mM; phosphate buffer pH 5.8 50 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 5.8; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY with heteronuclear filtrationsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz

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