BMRB Entry 16105
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16105
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Title: THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN. PubMed: 19244249
Deposition date: 2009-01-02 Original release date: 2009-03-17
Authors: Patil, Sharadrao; Xu, Shihao; Sheftic, Sarah; Alexandrescu, Andrei
Citation: Patil, Sharadrao; Xu, Shihao; Sheftic, Sarah; Alexandrescu, Andrei. "THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN." J. Biol. Chem. 284, 11982-11991 (2009).
Assembly members:
alpha-helix, polymer, 37 residues, 3909.330 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):
alpha-helix: KCNTATCATQRLANFLVHSS
NNFGAILSSTNVGSNTY
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 44 |
| 1H chemical shifts | 192 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alpha-helix | 1 |
Entities:
Entity 1, alpha-helix 37 residues - 3909.330 Da.
| 1 | LYS | CYS | ASN | THR | ALA | THR | CYS | ALA | THR | GLN | ||||
| 2 | ARG | LEU | ALA | ASN | PHE | LEU | VAL | HIS | SER | SER | ||||
| 3 | ASN | ASN | PHE | GLY | ALA | ILE | LEU | SER | SER | THR | ||||
| 4 | ASN | VAL | GLY | SER | ASN | THR | TYR |
Samples:
sample_2: amylin, [U-100% 15N], 0.5 mM; sodium dodecyl sulfate, [U-99% 2H], 100 mM; acetic acid, [U-99% 2H], 60 mM
sample_1: amylin, [U-99% 15N], 0.5 mM; SDS, [U-2H], 100 mM; acetic acid 60 mM
sample_conditions_1: ionic strength: 60 mM; pH: 4.6; pressure: 1.0 atm; temperature: 310 K
sample_conditions_2: ionic strength: 60 mM; pH*: 4.2; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR v3.851, Brunger - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts