BMRB Entry 25729
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25729
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Title: Spatial structure of EGFR transmembrane and juxtamembrane domains in DPC micelles PubMed: 26440883
Deposition date: 2015-07-27 Original release date: 2015-10-12
Authors: Mineev, Konstantin; Bocharov, Eduard; Bocharova, Olga; Arseniev, Alexander
Citation: Mineev, Konstantin; Panova, Stanislava; Bocharov, Eduard; Bocharov, Olga; Arseniev, Alexander. "The Membrane Mimetic Affects the Spatial Structure and Mobility of EGFR Transmembrane and Juxtamembrane Domains" Biochemistry 54, 6295-6298 (2015).
Assembly members:
EGFR, polymer, 54 residues, 5979.388 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 Vector: pGEMEX-1
Entity Sequences (FASTA):
EGFR: GSCKIPSIATGMVGALLLLL
VVALGIGLFMRRRHIVRKRT
LRRLLQERELVEGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 246 |
| 15N chemical shifts | 57 |
| 1H chemical shifts | 421 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 54 residues - 5979.388 Da.
| 1 | GLY | SER | CYS | LYS | ILE | PRO | SER | ILE | ALA | THR | ||||
| 2 | GLY | MET | VAL | GLY | ALA | LEU | LEU | LEU | LEU | LEU | ||||
| 3 | VAL | VAL | ALA | LEU | GLY | ILE | GLY | LEU | PHE | MET | ||||
| 4 | ARG | ARG | ARG | HIS | ILE | VAL | ARG | LYS | ARG | THR | ||||
| 5 | LEU | ARG | ARG | LEU | LEU | GLN | GLU | ARG | GLU | LEU | ||||
| 6 | VAL | GLU | GLY | GLY |
Samples:
sample_1: EGFR, [U-100% 13C; U-100% 15N], 0.3 mM; TCEP 2 mM; sodium phosphate 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 25 mM; pH: 5.8; pressure: 1 atm; temperature: 314 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| HSQC-NOESY-HSQC CN | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8, Keller and Wuthrich - chemical shift assignment
TOPSPIN, Bruker Biospin - processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
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