BMRB Entry 25079
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25079
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Title: Assignment of the transmembrane domain of the erythropoietin receptor PubMed: 25418301
Deposition date: 2014-07-05 Original release date: 2014-12-08
Authors: Li, Qingxin; Wong, Ying Lei; Huang, Qiwei; Kang, Congbao
Citation: Li, Qingxin; Wong, Ying Lei; Huang, Qiwei; kang, congbao. "Structural insight into the transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles" Biophys. J. 107, 2325-2336 (2014).
Assembly members:
human_EpoR, polymer, 55 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
Entity Sequences (FASTA):
human_EpoR: MSEPVSLLTPSDLDPLILTL
SLILVVILVLLTVLALLSHR
RALKQKIWPHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 90 |
| 1H chemical shifts | 170 |
| 15N chemical shifts | 42 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human Epo | 1 |
Entities:
Entity 1, human Epo 55 residues - Formula weight is not available
| 1 | MET | SER | GLU | PRO | VAL | SER | LEU | LEU | THR | PRO | ||||
| 2 | SER | ASP | LEU | ASP | PRO | LEU | ILE | LEU | THR | LEU | ||||
| 3 | SER | LEU | ILE | LEU | VAL | VAL | ILE | LEU | VAL | LEU | ||||
| 4 | LEU | THR | VAL | LEU | ALA | LEU | LEU | SER | HIS | ARG | ||||
| 5 | ARG | ALA | LEU | LYS | GLN | LYS | ILE | TRP | PRO | HIS | ||||
| 6 | HIS | HIS | HIS | HIS | HIS |
Samples:
15N: human EpoR, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; DPC 200 mM; H20 90%; D20 10%
13C-15N: human EpoR, [U-100% 13C; U-100% 15N], 0.2 – 0.8 mM; sodium phosphate 20 mM; DPC 200 mM; H20 90%; D20 10%
sample_3: human EpoR, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; sodium phosphate 20 mM; DPC 200 mM; H20 90%; D20 10%
sample_conditions_1: temperature: 313 K; pH: 6.5; pressure: 1 atm; ionic strength: 20 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 15N | isotropic | sample_conditions_1 |
| 3D HNCA | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C-15N | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 13C-15N | isotropic | sample_conditions_1 |
| 3D HCACO | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCO | 13C-15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 13C-15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| DBJ | BAG37561 BAI45971 |
| GB | AAA52401 AAA52403 AAB23271 AAI12154 AFM52330 |
| REF | NP_000112 XP_001105833 XP_002828735 XP_003830541 XP_004060086 |
| SP | P19235 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts