Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16005

Title: EphA2 dimeric structure in the lipidic bicelle at pH 5.0   PubMed: 20197042

Deposition date: 2008-10-27 Original release date: 2010-05-06

Authors: Mayzel, Maxim; Bocharov, Eduard; Areniev, Alexandr

Citation: Bocharov, Eduard; Mayzel, Maxim; Volynsky, Pavel; Mineev, Konstantin; Tkach, Elena; Ermolyuk, Yaroslav; Schulga, Alexey; Efremov, Roman; Arseniev, Alexander. "Left-handed dimer of EphA2 transmembrane domain: Helix packing diversity among receptor tyrosine kinases."  Biophys. J. 98, 881-889 (2010).

Assembly members:
EphA2_TM, polymer, 41 residues, Formula weight is not available

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: PGEMEX1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts174
15N chemical shifts41
1H chemical shifts290

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1EphA2 TM chain 11
2EphA2 TM chain 21


Entity 1, EphA2 TM chain 1 41 residues - Formula weight is not available

5   LYS


EphA2_TM_15N_13C_homodimer: EphA2_TM, [U-95% 13C; U-95% 15N], 3 mM; DHPC, [U-2H], 96 mM; DMPC, [U-2H], 24 mM; NaN3 1.5 mM; EDTA 1 mM; phosphate buffer 10 mM

EphA2_TM_15N_homodimer: EphA2_TM, [U-95% 15N], 3 mM; DHPC, [U-2H], 96 mM; DMPC, [U-2H], 24 mM; NaN3 1.5 mM; EDTA 1 mM; phosphate buffer 10 mM

EphA2_TM_15N_13C_heterodimer: EphA2_TM, [U-95% 13C; U-95% 15N], 1.5 mM; DHPC, [U-2H], 96 mM; DMPC, [U-2H], 24 mM; NaN3 1.5 mM; EDTA 1 mM; phosphate buffer 10 mM; EphA2_TM 1.5 mM

sample_conditions: ionic strength: 10 mM; pH: 5; pressure: 1 atm; temperature: 313 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCEphA2_TM_15N_homodimerisotropicsample_conditions
2D 1H-13C HSQCEphA2_TM_15N_13C_homodimerisotropicsample_conditions
3D HNCOEphA2_TM_15N_13C_homodimerisotropicsample_conditions
3D HNCAEphA2_TM_15N_13C_homodimerisotropicsample_conditions
3D HCCH-TOCSYEphA2_TM_15N_13C_homodimerisotropicsample_conditions
3D 1H-15N NOESYEphA2_TM_15N_homodimerisotropicsample_conditions
3D 1H-15N TOCSYEphA2_TM_15N_homodimerisotropicsample_conditions
3D 1H-13C NOESYEphA2_TM_15N_13C_homodimerisotropicsample_conditions
3D HNHBEphA2_TM_15N_homodimerisotropicsample_conditions
3D HNHAEphA2_TM_15N_homodimerisotropicsample_conditions
2D 1H-1H NOESYEphA2_TM_15N_homodimerisotropicsample_conditions
13C F1-filtered/F3-edited-NOESYEphA2_TM_15N_13C_heterodimerisotropicsample_conditions
2D 1H-1H TOCSYEphA2_TM_15N_homodimerisotropicsample_conditions


NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - spectra processing

CARA v1.5.5, 1.8, Keller and Wuthrich - Assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - Structure calculation

VNMR, Varian - collection

GROMACS v3.3.2, Erik Lindahl - geometry optimization, refinement

NMR spectrometers:

  • Varian Unity 600 MHz

Related Database Links:

DBJ BAG59366
GB AAA53375 AAH37166 AAX36099 AAX42531 ABM86157
REF NP_004422 XP_003279982 XP_003780411 XP_003806286 XP_004024797
SP P29317
AlphaFold P29317

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts