BMRB Entry 34040
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PDB ID:
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
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 190 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 322 |
Additional metadata:
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 | LEU | LEU | LEU | LEU | VAL | VAL | ALA | LEU | GLY | ||||
| 4 | ILE | GLY | LEU | PHE | MET | ARG | ARG | 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 HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts