BMRB Entry 25593

Name: Spatial structure of HER2/ErbB2 dimeric transmembrane domain in the presence of cytoplasmic juxtamembrane domains
Published: 2016-02-22

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PDB ID: 2n2a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25593
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
entity: AEQRASPLTSIISAVVGILL VVVLGVVFGILIKRRQQKIR KYTMRRLLQETELVEPLG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	54
1H chemical shifts	420

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 58 residues - 6509.924 Da.

1

ALA

GLU

GLN

ARG

ALA

SER

PRO

LEU

THR

SER

2

ILE

SER

ALA

VAL

GLY

ILE

LEU

3

VAL

LEU

GLY

VAL

PHE

GLY

ILE

4

LEU

ILE

LYS

ARG

GLN

LYS

ILE

ARG

5

LYS

TYR

THR

MET

ARG

LEU

GLN

GLU

6

THR

GLU

LEU

VAL

GLU

PRO

LEU

GLY

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:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HCACO	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_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