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 11420

Title: NMR structure of vasoactive intestinal peptide in DPC Micelle   PubMed: 21439408

Deposition date: 2010-12-21 Original release date: 2011-05-19

Authors: Umetsu, Yoshitaka; Tenno, Takeshi; Goda, Natsuko; Shirakawa, Masahiro; Ikegami, Takahisa; Hiroaki, Hidekazu

Citation: Umetsu, Yoshitaka; Tenno, Takeshi; Goda, Natsuko; Shirakawa, Masahiro; Ikegami, Takahisa; Hiroaki, Hidekazu. "Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments."  Biochim. Biophys. Acta 1814, 724-730 (2011).

Assembly members:
Vasoactive intestinal peptide, polymer, 29 residues, 3389.911 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: PRESAT-vector

Entity Sequences (FASTA):
Vasoactive intestinal peptide: HSDAVFTDNYTRLRKQMAVK KYLNSILNG

Data sets:
Data typeCount
13C chemical shifts127
15N chemical shifts31
1H chemical shifts204

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1Vasoactive intestinal peptide1


Entity 1, Vasoactive intestinal peptide 29 residues - 3389.911 Da.



sample_1: vasoactive intestinal peptide, [U-13C; U-15N], 0.5 mM; DPC 1%; potassium phosphate 50 mM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1


NMRPipe v5.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 11419 1652
DBJ BAB31301 BAF84648 BAP63927 BAP63928 BAP63929
GB AAA61284 AAA61285 AAA61286 AAA61287 AAA61289
PRF 0601216A 0909264A 1007235A 1012267A 1109226A
REF NP_001119840 NP_001182162 NP_001247681 NP_001300898 NP_003372
SP P01282 P01283 P01284 P32648 P32649
TPG DAA26008
AlphaFold P01282 P01283 P01284 P32648 P32649

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