BMRB Entry 25806
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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/BMR25806
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Title: NMR structure of the prolactin receptor transmembrane domain PubMed: 27174498
Deposition date: 2015-09-11 Original release date: 2016-05-23
Authors: Bugge, Katrine; Kragelund, Birthe
Citation: Bugge, Katrine; Papaleo, Elena; Haxholm, Gitte; Hopper, Jonathan; Dagil, Robert; Robinson, Carol; Olsen, Johan; Lindorff-Larsen, Kresten; Kragelund, Birthe. "A combined computational and structural model of the full-length human prolactin receptor" Nat. Commun. 7, 11578-11578 (2016).
Assembly members:
PRLRTMD, polymer, 37 residues, 3960.773 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):
PRLRTMD: GSFTMNDTTVWISVAVLSAV
ICLIIVWAVALKGYSMV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 161 |
| 15N chemical shifts | 37 |
| 1H chemical shifts | 242 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | prolactin receptor transmembrane domain | 1 |
Entities:
Entity 1, prolactin receptor transmembrane domain 37 residues - 3960.773 Da.
Residues 204-205 represent non-native residues left over from thrombin digestion. This is the transmembrane domain of a receptor
| 1 | GLY | SER | PHE | THR | MET | ASN | ASP | THR | THR | VAL | ||||
| 2 | TRP | ILE | SER | VAL | ALA | VAL | LEU | SER | ALA | VAL | ||||
| 3 | ILE | CYS | LEU | ILE | ILE | VAL | TRP | ALA | VAL | ALA | ||||
| 4 | LEU | LYS | GLY | TYR | SER | MET | VAL |
Samples:
sample_1: PRLRTMD, [U-13C; U-15N], 0.8 mM; DSS 2 mM; sodium azide 0.05%; DHPC 560 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_2: PRLRTMD, [U-13C; U-15N], 1 mM; DSS 2 mM; sodium azide 0.05%; DHPC, [U-2H], 700 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample15N: PRLRTMD, [U-15N], 0.7 mM; DSS 2 mM; sodium azide 0.05%; DHPC 490 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample15N | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample15N | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 750 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts