BMRB Entry 34656
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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/BMR34656
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Title: Structure of Insulin-like growth factor 1 receptor's transmembrane domain PubMed: 36835322
Deposition date: 2021-08-16 Original release date: 2022-08-22
Authors: Bershatsky, Y.; Nadezhdin, K.; Bocharova, O.; Bocharov, E.
Citation: Bershatsky, Yaroslav; Kuznetsov, Andrey; Idiatullina, Aisha; Bocharova, Olga; Dolotova, Sofya; Gavrilenkova, Alina; Serova, Oxana; Deyev, Igor; Rakitina, Tatiana; Zangieva, Olga; Pavlov, Konstantin; Batishchev, Oleg; Britikov, Vladimir; Usanov, Sergey; Arseniev, Alexander; Efremov, Roman; Bocharov, Eduard. "Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily" Int. J. Mol. Sci. 24, 3906-3906 (2023).
Assembly members:
entity_1, polymer, 31 residues, 3534.460 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: NFIHLIIALPVAVLLIVGGL
VIMLYVFHRKR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 158 |
| 15N chemical shifts | 31 |
| 1H chemical shifts | 265 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 31 residues - 3534.460 Da.
| 1 | ASN | PHE | ILE | HIS | LEU | ILE | ILE | ALA | LEU | PRO | ||||
| 2 | VAL | ALA | VAL | LEU | LEU | ILE | VAL | GLY | GLY | LEU | ||||
| 3 | VAL | ILE | MET | LEU | TYR | VAL | PHE | HIS | ARG | LYS | ||||
| 4 | ARG |
Samples:
sample_1: IGF1Rtm, [U-100% 13C; U-100% 15N], 0.5 mM; DPC, [U-99% 2H], 100 mM; sodium azide 0.3 mM; KH2PO4 30 mM; K2HPO4 20 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.7; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
TopSpin, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - processing
NMR spectrometers:
- Bruker AVANCE 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts