BMRB Entry 16608
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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/BMR16608
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Yang, Yanwu; Hua, Qing-Xin; Liu, Jin; Shimizu, Eri; Choquette, Meredith; Mackin, Robert; Weiss, Michael. "Solution Structure of Proinsulin: CONNECTING DOMAIN FLEXIBILITY AND PROHORMONE PROCESSING." J. Biol. Chem. 285, 7847-7851 (2010).
PubMed: 20106974
Assembly members:
Proinsulin, polymer, 86 residues, 9379.647 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 Vector: pET-9b
Entity Sequences (FASTA):
Proinsulin: FVNQHLCGSDLVEALYLVCG
ERGFFYTKPTRREAEDLQVG
QVELGGGPGAGSLQPLALEG
SLQKRGIVEQCCTSICSLYQ
LENYCN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 271 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 568 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Proinsulin | 1 |
Entities:
Entity 1, Proinsulin 86 residues - 9379.647 Da.
| 1 | PHE | VAL | ASN | GLN | HIS | LEU | CYS | GLY | SER | ASP | ||||
| 2 | LEU | VAL | GLU | ALA | LEU | TYR | LEU | VAL | CYS | GLY | ||||
| 3 | GLU | ARG | GLY | PHE | PHE | TYR | THR | LYS | PRO | THR | ||||
| 4 | ARG | ARG | GLU | ALA | GLU | ASP | LEU | GLN | VAL | GLY | ||||
| 5 | GLN | VAL | GLU | LEU | GLY | GLY | GLY | PRO | GLY | ALA | ||||
| 6 | GLY | SER | LEU | GLN | PRO | LEU | ALA | LEU | GLU | GLY | ||||
| 7 | SER | LEU | GLN | LYS | ARG | GLY | ILE | VAL | GLU | GLN | ||||
| 8 | CYS | CYS | THR | SER | ILE | CYS | SER | LEU | TYR | GLN | ||||
| 9 | LEU | GLU | ASN | TYR | CYS | ASN |
Samples:
sample_1: proinsulin, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP, Garrett - data analysis, peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker MSL 700 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks