BMRB Entry 25519

Title:
NMR structure of Neuromedin C in aqueous solution.
Deposition date:
2015-03-05
Original release date:
2015-10-12
Authors:
Adrover, Miquel; Sanchis, Pilar; Vilanova, Bartolome; Pauwels, Kris; Martorell, Gabriel; Perez, Juan Jesus
Citation:

Citation: Adrover, Miquel; Sanchis, Pilar; Vilanova, Bartolome; Pauwels, Kris; Martorell, Gabriel; Perez, J.. "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:

Assembly members:
Neuromedin_C, polymer, 11 residues, 1123.295 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: obtained from a vendor

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Neuromedin_C: GNHWAVGHLMX

Data sets:
Data typeCount
13C chemical shifts34
15N chemical shifts12
1H chemical shifts69
T1 relaxation values10
T2 relaxation values10
heteronuclear NOE values10

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Neuromedin C1

Entities:

Entity 1, Neuromedin C 11 residues - 1123.295 Da.

1   GLYASNHISTRPALAVALGLYHISLEUMET
2   NH2

Samples:

sample_1: Neuromedin C 5.0 ± 0.1 mM; sodium acetate 10 ± 0.1 mM; DSS 1.6 ± 0.1 mM; H2O 90%; D2O 10%

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

Experiments:

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

Software:

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:

PDB

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