BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34069

Title: Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide.   PubMed: 28287098

Deposition date: 2016-11-21 Original release date: 2017-03-23

Authors: Rodriguez Camargo, D.; Tripsianes, K.; Reif, B.

Citation: Rodriguez Camargo, D.; Tripsianes, K.; Buday, K.; Franko, A.; Gobl, C.; Hartlmuller, C.; Sarkar, R.; Aichler, M.; Mettenleiter, G.; Schulz, M.; Boddrich, A.; Erck, C.; Martens, H.; Walch, A.; Madl, T.; Wanker, E.; Conrad, M.; de Angelis, M.; Reif, B.. "The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes."  Sci. Rep. 7, 44041-44041 (2017).

Assembly members:
entity_1, polymer, 37 residues, 3908.319 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: KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTX

Data sets:
Data typeCount
13C chemical shifts56
15N chemical shifts42
1H chemical shifts238

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 37 residues - 3908.319 Da.

1   LYSCYSASNTHRALATHRCYSALATHRGLN
2   ARGLEUALAASNPHELEUVALHISSERSER
3   ASNASNPHEGLYALAILELEUSERSERTHR
4   ASNVALGLYSERASNTHRTYC

Samples:

sample_1: Islet Amyloid Polypeptide (IAPP or Amylin), [U-99% 13C; U-99% 15N], 150 uM

sample_conditions_1: pH: 5.3; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Bruker Avance 500 MHz
  • Bruker Bruker Avance 600 MHz
  • Bruker Bruker Avance 750 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts