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

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Title:
Spatial structure of EGFR transmembrane and juxtamembrane domains in DPC micelles
Deposition date:
2015-07-27
Original release date:
2015-10-12
Authors:
Mineev, Konstantin; Bocharov, Eduard; Bocharova, Olga; Arseniev, Alexander
Citation:

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).
PubMed: 26440883

Assembly members:

Assembly members:
EGFR, polymer, 54 residues, 5979.388 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):
EGFR: GSCKIPSIATGMVGALLLLL VVALGIGLFMRRRHIVRKRT LRRLLQERELVEGG

Data sets:
Data typeCount
13C chemical shifts246
15N chemical shifts57
1H chemical shifts421

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 54 residues - 5979.388 Da.

1   GLYSERCYSLYSILEPROSERILEALATHR
2   GLYMETVALGLYALALEULEULEULEULEU
3   VALVALALALEUGLYILEGLYLEUPHEMET
4   ARGARGARGHISILEVALARGLYSARGTHR
5   LEUARGARGLEULEUGLNGLUARGGLULEU
6   VALGLUGLYGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
HSQC-NOESY-HSQC CNsample_1isotropicsample_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

Related Database Links:

UNP P00533
AlphaFold Q9UMG5

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