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 20080

Title: Structure and interactions in membranes of human and bovine Catestatin by solution and solid-state NMR spectroscopy   PubMed: 20103720

Authors: Sugewara, Masae; Resende, Jarbas; Moraes, Cleria; Chich, Jean-Francois; Marquette, Arnaud; Metz-Boutigue, Marie-Helene; Bechinger, Burkhard

Citation: Sugawara, Masae; Resende, Jarbas; Moraes, Cleria Mendonca; Marquette, Arnaud; Chich, Jean-Francois; Metz-Boutigue, Marie-Helene; Bechinger, Burkhard. "Membrane structure and interactions of human catestatin by multidimensional solution and solid-state NMR spectroscopy."  FASEB J. 24, 1737-1746 (2010).

Assembly members:
hCGA(G364S), polymer, 21 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
hCGA(G364S): SSMKLSFRARAYSFRGPGPQ L

Data sets:
Data typeCount
1H chemical shifts132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hCGA(G364S)1

Entities:

Entity 1, hCGA(G364S) 21 residues - Formula weight is not available

1   SERSERMETLYSLEUSERPHEARGALAARG
2   ALATYRSERPHEARGGLYPROGLYPROGLN
3   LEU

Samples:

sample_1: hCGA(G364S) 2.0 ± 0.1 mM; DPC-d38, [U-2H], 400 ± 1.0 mM; D2O, [U-2H], 95%; H2O 5.0%; PB 10 mM

sample_conditions_1: pH: 5.5; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

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

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

GB AKI70208