BMRB Entry 16005

Name: EphA2 dimeric structure in the lipidic bicelle at pH 5.0
Published: 2010-05-06

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PDB ID: 2k9y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16005
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

EphA2 dimeric structure in the lipidic bicelle at pH 5.0

Deposition date:

2008-10-27

Original release date:

2010-05-06

Authors:

Mayzel, Maxim; Bocharov, Eduard; Areniev, Alexandr

Citation:

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).
PubMed: 20197042

Assembly members:

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

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: PGEMEX1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EphA2_TM: EFQTLSPEGSGNLAVIGGVA VGVVLLLVLAGVGFFIHRRR K

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts

Data type	Count
13C chemical shifts	174
15N chemical shifts	41
1H chemical shifts	290

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EphA2 TM chain 1	1
2	EphA2 TM chain 2	1

Entities:

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

1

GLU

PHE

GLN

THR

LEU

SER

PRO

GLU

GLY

SER

2

GLY

ASN

LEU

ALA

VAL

ILE

GLY

VAL

ALA

3

VAL

GLY

VAL

LEU

VAL

LEU

ALA

4

GLY

VAL

GLY

PHE

ILE

HIS

ARG

5

LYS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	EphA2_TM_15N_homodimer	isotropic	sample_conditions
2D 1H-13C HSQC	EphA2_TM_15N_13C_homodimer	isotropic	sample_conditions
3D HNCO	EphA2_TM_15N_13C_homodimer	isotropic	sample_conditions
3D HNCA	EphA2_TM_15N_13C_homodimer	isotropic	sample_conditions
3D HCCH-TOCSY	EphA2_TM_15N_13C_homodimer	isotropic	sample_conditions
3D 1H-15N NOESY	EphA2_TM_15N_homodimer	isotropic	sample_conditions
3D 1H-15N TOCSY	EphA2_TM_15N_homodimer	isotropic	sample_conditions
3D 1H-13C NOESY	EphA2_TM_15N_13C_homodimer	isotropic	sample_conditions
3D HNHB	EphA2_TM_15N_homodimer	isotropic	sample_conditions
3D HNHA	EphA2_TM_15N_homodimer	isotropic	sample_conditions
2D 1H-1H NOESY	EphA2_TM_15N_homodimer	isotropic	sample_conditions
13C F1-filtered/F3-edited-NOESY	EphA2_TM_15N_13C_heterodimer	isotropic	sample_conditions
15N-T2	EphA2_TM_15N_homodimer	isotropic	sample_conditions
15N-T1	EphA2_TM_15N_homodimer	isotropic	sample_conditions
15N-NOE	EphA2_TM_15N_homodimer	isotropic	sample_conditions
2D 1H-1H TOCSY	EphA2_TM_15N_homodimer	isotropic	sample_conditions

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

BMRB Entry 16005

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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