BMRB Entry 34001
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34001
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Title: D11 bound [S39_PQ]-IGF-II PubMed: 27510031
Deposition date: 2016-05-23 Original release date: 2016-08-01
Authors: Hexnerova, R.
Citation: Hexnerova, Rozalie; Krizkova, Kvetoslava; Fabry, Milan; Sieglova, Irena; Kedrova, Katerina; Collinsova, Michaela; Ullrichova, Pavlina; Srb, Pavel; Williams, Christopher; Crump, Matthew; Tosner, Zdenek; Jiracek, Jiri; Veverka, Vaclav; Zakova, Lenka. "Probing Receptor Specificity by Sampling the Conformational Space of the Insulin-like Growth Factor II C-domain" J. Biol. Chem. 291, 21234-21245 (2016).
Assembly members:
Insulin-like growth factor II, polymer, 69 residues, 7709.715 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):
Insulin-like growth factor II: AYRPSETLCGGELVDTLQFV
CGDRGFYFSRPASRVSRRSP
QRGIVEECCFRSCDLALLET
YCATPAKSE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 184 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 458 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 69 residues - 7709.715 Da.
| 1 | ALA | TYR | ARG | PRO | SER | GLU | THR | LEU | CYS | GLY | ||||
| 2 | GLY | GLU | LEU | VAL | ASP | THR | LEU | GLN | PHE | VAL | ||||
| 3 | CYS | GLY | ASP | ARG | GLY | PHE | TYR | PHE | SER | ARG | ||||
| 4 | PRO | ALA | SER | ARG | VAL | SER | ARG | ARG | SER | PRO | ||||
| 5 | GLN | ARG | GLY | ILE | VAL | GLU | GLU | CYS | CYS | PHE | ||||
| 6 | ARG | SER | CYS | ASP | LEU | ALA | LEU | LEU | GLU | THR | ||||
| 7 | TYR | CYS | ALA | THR | PRO | ALA | LYS | SER | GLU |
Samples:
sample_1: acetic acid, d4, 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 mM; pH: 4.2; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment
TOPSPIN, Bruker Biospin - collection, processing
YASARA, Hoegenauer, Koraimann, Kungl, Vriend - refinement
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts