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 25523

Title: NMR structure of Neuromedin C in 60% TFE

Deposition date: 2015-03-05 Original release date: 2015-10-19

Authors: Adrover, Miquel; Sanchis, Pilar; Vilanova, Bartolome; Pauwels, Kris; Martorell, Gabriel; Perez, Juan Jesus

Citation: Adrover, Miquel; Sanchis, Pilar; Vilanova, Bartolome; Pauwels, Kris; Martorell, Gabriel; Perez, Juan Jesus. "Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism"  RSC ADV 5, 83074-83088 (2015).

Assembly members:
Neuromedin_C, polymer, 11 residues, 1123.295 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):

Data sets:
Data typeCount
13C chemical shifts34
15N chemical shifts11
1H chemical shifts68
T1 relaxation values9
T2 relaxation values9
heteronuclear NOE values9

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, entity 11 residues - 1123.295 Da.

2   NH2


sample_1: entity 5.0 ± 0.1 mM; sodium acetate 10 ± 0.1 mM; DSS 1.6 ± 0.1 mM; TFE, [U-99% 2H], 60 ± 0.5 %; D2O, [U-100% 2H], 10 ± 1 %

sample_conditions_1: ionic strength: 0.01 M; pH: 4.0; pressure: 1 atm; temperature: 273 K


NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 15N-T1sample_1isotropicsample_conditions_1
2D 15N-T2sample_1isotropicsample_conditions_1
2D 15N-HET-NOEsample_1isotropicsample_conditions_1


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

XEASY, Bartels et al. - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:


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