BMRB Entry 17394
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17394
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR structure of human amylin in SDS micelles at pH 7.3 PubMed: 21723249
Deposition date: 2011-01-04 Original release date: 2012-06-19
Authors: Nanga, Ravi Prakash Reddy; Brender, Jeffrey; Vivekanandan, Subramanian; Ramamoorthy, Ayyalusamy
Citation: Nanga, Ravi Prakash Reddy; Brender, Jeffrey; Vivekanandan, Subramanian; Ramamoorthy, Ayyalusamy. "Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment." Biochim. Biophys. Acta 1808, 2337-2342 (2011).
Assembly members:
entity, 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: obtained from a vendor
Entity Sequences (FASTA):
entity: KCNTATCATQRLANFLVHSS
NNFGAILSSTNVGSNTY
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 228 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | amidated IAPP | 1 |
Entities:
Entity 1, amidated IAPP 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_1: amidated IAPP 2.5 mM; sodium phosphate 20 mM; sodium chloride 120 mM; D2O, [U-99% 2H], 10%; H2O 90%; SDS, [U-99% 2H], 200 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis, structure solution
ProcheckNMR, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Bruker Avance 900 MHz