BMRB Entry 25396
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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/BMR25396
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Title: assignment of the transmembrane domain of the mouse erythropoietin receptor PubMed: 26316120
Deposition date: 2014-12-17 Original release date: 2015-09-21
Authors: Li, Qingxin; Wong, Yinglei; Lee, Michelle; Kang, Congbao
Citation: Li, Qingxin; Wong, Yinglei; Lee, Michelle; Li, Michelle; kang, congbao. "Solution structure of the transmembrane domain of the mouse erythropoietin receptor in detergent micelles" Sci. Rep. 5, 13586-13586 (2015).
Assembly members:
mouse_EpoR, polymer, 55 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mouse_EpoR: MSEPASLLTASDLDPLILTL
SLILVLISLLLTVLALLSHR
RTLQQKIWPHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 136 |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 250 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mouse EpoR | 1 |
Entities:
Entity 1, mouse EpoR 55 residues - Formula weight is not available
| 1 | MET | SER | GLU | PRO | ALA | SER | LEU | LEU | THR | ALA | ||||
| 2 | SER | ASP | LEU | ASP | PRO | LEU | ILE | LEU | THR | LEU | ||||
| 3 | SER | LEU | ILE | LEU | VAL | LEU | ILE | SER | LEU | LEU | ||||
| 4 | LEU | THR | VAL | LEU | ALA | LEU | LEU | SER | HIS | ARG | ||||
| 5 | ARG | THR | LEU | GLN | GLN | LYS | ILE | TRP | PRO | HIS | ||||
| 6 | HIS | HIS | HIS | HIS | HIS |
Samples:
15N_labeled_sample: mouseEpoR, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; DPC 150 mM; H2O 90%; D2O, U-2H, 10%
13C-15N: mouseEpoR, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 20 mM; DPC, [U-100% 2H], 240 mM; H2O 90%; D2O, U-2H, 10%
sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 15N_labeled_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 15N_labeled_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCA | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCO | 13C-15N | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 13C-15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 13C-15N | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 13C-15N | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker DMX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAE23871 |
| EMBL | CAA37248 |
| GB | AAA37571 AAB20029 AAH03953 AAH46282 EDL25236 |
| REF | NP_034279 XP_006510061 |
| SP | P14753 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts