BMRB Entry 34040

Name: N-terminal motif dimerization of EGFR transmembrane domain in bicellar environment
Published: 2017-03-30

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PDB ID: 5lv6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34040
MolProbity Validation Chart

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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: 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:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	190
15N chemical shifts	42
1H chemical shifts	322

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

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

1

GLU

GLY

CYS

PRO

THR

ASN

GLY

PRO

LYS

ILE

2

PRO

SER

ILE

ALA

THR

GLY

MET

VAL

GLY

ALA

3

LEU

VAL

ALA

LEU

GLY

4

ILE

GLY

LEU

PHE

MET

ARG

HIS

ILE

5

VAL

ARG

LYS

ARG

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:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY with heteronuclear filtration	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_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