BMRB Entry 25593

Title:
Spatial structure of HER2/ErbB2 dimeric transmembrane domain in the presence of cytoplasmic juxtamembrane domains
Deposition date:
2015-05-05
Original release date:
2016-02-22
Authors:
Mineev, Konstantin; Bragin, Pavel; Bocharov, Eduard; Bocharova, Olga; Arseniev, Alexander
Citation:

Citation: Bragin, Pavel; Mineev, Konstantin; Bocharova, Olga; Bocharov, Eduard; Arseniev, Alexander. "HER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane Regions"  J. Mol. Biol. 428, 52-61 (2016).
PubMed: 26585403

Assembly members:

Assembly members:
entity, polymer, 58 residues, 6509.924 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEMEX-1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts54
1H chemical shifts420

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 58 residues - 6509.924 Da.

1   ALAGLUGLNARGALASERPROLEUTHRSER
2   ILEILESERALAVALVALGLYILELEULEU
3   VALVALVALLEUGLYVALVALPHEGLYILE
4   LEUILELYSARGARGGLNGLNLYSILEARG
5   LYSTYRTHRMETARGARGLEULEUGLNGLU
6   THRGLULEUVALGLUPROLEUGLY

Samples:

sample_1: DPC, [U-100% 2H], 4 mg; labeled protein, [U-100% 13C; U-100% 15N], 1 mg; unlabeled protein 1 mg; sodium acetate 50 mM; sodium azide 1e-3%; D2O, [U-99% 2H], 100%

sample_2: DPC, [U-100% 2H], 4 mg; labeled protein, [U-100% 13C; U-100% 15N], 1 mg; sodium acetate 50 mM; sodium azide 1e-3%; D2O, [U-99% 2H], 100%

sample_3: DPC, [U-100% 2H], 4 mg; labeled protein, [U-100% 13C; U-100% 15N], 1 mg; sodium acetate 50 mM; sodium azide 1e-3%; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 3.5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HCACOsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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