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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16005
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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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:
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):
EphA2_TM: EFQTLSPEGSGNLAVIGGVA
VGVVLLLVLAGVGFFIHRRR
K
Data type | Count |
13C chemical shifts | 174 |
15N chemical shifts | 41 |
1H chemical shifts | 290 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EphA2 TM chain 1 | 1 |
2 | EphA2 TM chain 2 | 1 |
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 | GLY | VAL | ALA | ||||
3 | VAL | GLY | VAL | VAL | LEU | LEU | LEU | VAL | LEU | ALA | ||||
4 | GLY | VAL | GLY | PHE | PHE | ILE | HIS | ARG | ARG | ARG | ||||
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
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 |
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
DBJ | BAG59366 |
GB | AAA53375 AAH37166 AAX36099 AAX42531 ABM86157 |
REF | NP_004422 XP_003279982 XP_003780411 XP_003806286 XP_004024797 |
SP | P29317 |
AlphaFold | P29317 |
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