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 15728

Title: NMR structures of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 in lipid bicelles at pH 4.3   PubMed: 18728013

Deposition date: 2008-04-15 Original release date: 2008-09-02

Authors: Mayzel, Maxim; Bocharov, Eduard; Arseniev, Alexander; Goncharuk, Marina

Citation: Bocharov, Eduard; Mayzel, Maxim; Volynsky, Pavel; Goncharuk, Marina; Ermolyuk, Yaroslav; Schulga, Alexey; Artemenko, Elena; Efremov, Roman; Arseniev, Alexander. "Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1"  J. Biol. Chem. 283, 29385-29395 (2008).

Assembly members:
EphA1_TM, polymer, 38 residues, 3890.7 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: PGEMEX1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts35
1H chemical shifts276
coupling constants56
heteronuclear NOE values30
T1 relaxation values35
T2 relaxation values34

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1EphA1 TM chain A1
2EphA1 TM chain B1


Entity 1, EphA1 TM chain A 38 residues - 3890.7 Da.



EphA1_TM_15N_13C_homodimer: EphA1_TM 15N,13C, [U-15N; U-13C], 3 mM; DHPC, 2H, 96 mM; DMPC, 2H, 24 mM; NaN3 1.5 mkM; EDTA 1 mM; phosphate buffer 10 mM; D2O 100%

EphA1_TM_15N_homodimer: EphA1_TM 15N, [U-15N; U-13C], 3 mM; DHPC, 2H, 96 mM; DMPC, 2H, 24 mM; NaN3 1.5 mkM; EDTA 1 mM; phosphate buffer 10 mM; D2O 5%; H2O 95%

EphA1_TM_15N_13C_heterodimer: EphA1_TM 15N,13C, [U-15N; U-13C], 1.5 mM; DHPC, 2H, 96 mM; DMPC, 2H, 24 mM; NaN3 1.5 mkM; EDTA 1 mM; phosphate buffer 10 mM; EphA1_TM 1.5 mM; D2O 100%

pH_4.3: pH: 4.3; temperature: 313 K

pH_6.3: pH: 6.3; temperature: 313 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCEphA1_TM_15N_homodimerisotropicpH_4.3
2D 1H-13C HSQCEphA1_TM_15N_13C_homodimerisotropicpH_4.3
3D HNCOEphA1_TM_15N_13C_homodimerisotropicpH_4.3
3D HNCAEphA1_TM_15N_13C_homodimerisotropicpH_4.3
3D HN(CO)CAEphA1_TM_15N_13C_homodimerisotropicpH_4.3
3D HCCH-TOCSYEphA1_TM_15N_13C_homodimerisotropicpH_4.3
3D HNHAEphA1_TM_15N_homodimerisotropicpH_4.3
3D HNHBEphA1_TM_15N_homodimerisotropicpH_4.3
3D 1H-15N NOESYEphA1_TM_15N_homodimerisotropicpH_4.3
3D 1H-15N TOCSYEphA1_TM_15N_homodimerisotropicpH_4.3
3D 1H-13C NOESYEphA1_TM_15N_13C_homodimerisotropicpH_4.3
13C F1-filtered/F3-edited-NOESYEphA1_TM_15N_13C_heterodimerisotropicpH_4.3
2D 1H-15N HSQCEphA1_TM_15N_homodimerisotropicpH_6.3


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

CARA v1.5.5, 1.8, Keller and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Unity 600 600 MHz MHz

Related Database Links:

DBJ BAF83040
GB AAA36747 AAD43440 AAI30292 AAS07458 AIC54347
REF NP_005223 XP_002751927 XP_003270912 XP_003791590 XP_003820582
SP P21709
AlphaFold P21709

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