BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16314

Title: Three-Dimensional NMR Structure of Rat Islet Amyloid Polypeptide in DPC micelles.   PubMed: 19456151

Authors: Nanga, Ravi P R; Jeffrey, Brender; Xu, Jiadi; Hartman, Kevin; Subramanian, Vivekanandan; Ramamoorthy, Ayyalusamy

Citation: Nanga, Ravi P. R.; Jeffrey, Brender; Xu, Jiadi; Hartman, Kevin; Subramanian, Vivekanandan; Ramamoorthy, Ayyalusamy. "Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy."  J. Am. Chem. Soc. 131, 8252-8261 (2009).

Assembly members:
IAPP, polymer, 37 residues, 3926.447 Da.

Natural source:   Common Name: Norway Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
IAPP: KCNTATCATQRLANFLVRSS NNLGPVLPPTNVGSNTY

Data sets:
Data typeCount
1H chemical shifts212

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1IAPP1

Entities:

Entity 1, IAPP 37 residues - 3926.447 Da.

1   LYSCYSASNTHRALATHRCYSALATHRGLN
2   ARGLEUALAASNPHELEUVALARGSERSER
3   ASNASNLEUGLYPROVALLEUPROPROTHR
4   ASNVALGLYSERASNTHRTYR

Samples:

sample_1: sodium phosphate 20 mM; sodium azide 0.02%; sodium chloride 120 mM; D2O, 99.9%, 10%; DPC, 98% deuterated, 200 mM; entity 2.5 mM; H2O 90%

sample_conditions_1: ionic strength: 120 mM; pH: 7.3; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

BMRB 20046
PDB
DBJ BAA22051
EMBL CAA37003
GB AAA37874 AAA40730 AAA41359 AAH27527 EDL10633
REF NP_034621 NP_036718 XP_006155144 XP_006155145 XP_006237676
SP P12968 P12969