BMRB Entry 15728
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15728
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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
Entity Sequences (FASTA):
EphA1_TM: SPPVSRGLTGGEIVAVIFGL
LLGAALLLGILVFRSRRA
- assigned_chemical_shifts
- coupling_constants
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 152 |
| 15N chemical shifts | 35 |
| 1H chemical shifts | 276 |
| coupling constants | 56 |
| heteronuclear NOE values | 30 |
| T1 relaxation values | 35 |
| T2 relaxation values | 34 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EphA1 TM chain A | 1 |
| 2 | EphA1 TM chain B | 1 |
Entities:
Entity 1, EphA1 TM chain A 38 residues - 3890.7 Da.
| 1 | SER | PRO | PRO | VAL | SER | ARG | GLY | LEU | THR | GLY | ||||
| 2 | GLY | GLU | ILE | VAL | ALA | VAL | ILE | PHE | GLY | LEU | ||||
| 3 | LEU | LEU | GLY | ALA | ALA | LEU | LEU | LEU | GLY | ILE | ||||
| 4 | LEU | VAL | PHE | ARG | SER | ARG | ARG | ALA |
Samples:
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
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 2D 1H-13C HSQC | EphA1_TM_15N_13C_homodimer | isotropic | pH_4.3 |
| 3D HNCO | EphA1_TM_15N_13C_homodimer | isotropic | pH_4.3 |
| 3D HNCA | EphA1_TM_15N_13C_homodimer | isotropic | pH_4.3 |
| 3D HN(CO)CA | EphA1_TM_15N_13C_homodimer | isotropic | pH_4.3 |
| 3D HCCH-TOCSY | EphA1_TM_15N_13C_homodimer | isotropic | pH_4.3 |
| 3D HNHA | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 3D HNHB | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 3D 1H-15N NOESY | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 3D 1H-15N TOCSY | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 3D 1H-13C NOESY | EphA1_TM_15N_13C_homodimer | isotropic | pH_4.3 |
| 13C F1-filtered/F3-edited-NOESY | EphA1_TM_15N_13C_heterodimer | isotropic | pH_4.3 |
| 15N-T1 | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 15N-T2 | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 15N-NOE | EphA1_TM_15N_homodimer | isotropic | pH_4.3 |
| 2D 1H-15N HSQC | EphA1_TM_15N_homodimer | isotropic | pH_6.3 |
Software:
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:
| PDB | |
| DBJ | BAF83040 |
| EMBL | CAA81796 |
| GB | AAA36747 AAD43440 AAI30292 AAS07458 AIC54347 |
| REF | NP_005223 XP_002751927 XP_003270912 XP_003791590 XP_003820582 |
| SP | P21709 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts