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 6870

Title: Probing the conformation and dynamics of allatostatin neuropeptides: a structural model for functional differences.   PubMed: 18191874

Deposition date: 2005-10-20 Original release date: 2008-09-19

Authors: Meyerowitz, E.; Zubkov, S.; Mohanty, S.

Citation: Banerjee, Monimoy; Meyerowitz, Eric; Huang, Chengdong; Mohanty, Smita. "Probing the conformation and dynamics of allatostatin neuropeptides: a structural model for functional differences."  Peptides 29, 375-385 (2008).

Assembly members:
Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2), polymer, 10 residues, Formula weight is not available

Natural source:   Common Name: Cockroach   Taxonomy ID: 6984   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Diploptera punctata

Experimental source:   Production method: from a vendor

Entity Sequences (FASTA):
Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2): GGSLYSFGLX

Data sets:
Data typeCount
13C chemical shifts27
1H chemical shifts50

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2)1

Entities:

Entity 1, Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2) 10 residues - Formula weight is not available

1   GLYGLYSERLEUTYRSERPHEGLYLEUNH2

Samples:

sample_1: Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2) mM; SDS (sodium dodecyl sulfate), [U-2H], 30 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 30 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1not availablesample_cond_1
2D TOCSYsample_1not availablesample_cond_1
DQF-COSYsample_1not availablesample_cond_1
2D 1H-13C HMQCsample_1not availablesample_cond_1

Software:

DYANA vCYANA 1.0.6 - refinement

NMRPipe v97.027.12.56 - processing

NMR spectrometers:

  • Bruker AVANCE 500 MHz