BMRB Entry 30179

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30179
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Title:
The Solution Structure of the Magnesium-bound Conantokin-R1B Mutant
Deposition date:
2016-09-12
Original release date:
2017-06-23
Authors:
Castellino, F.; Yuan, Y.
Citation:

Citation: Yuan, Yue; Balsara, Rashna; Zajicek, Jaroslav; Kunda, Shailaja; Castellino, Francis. "Discerning the Role of the Hydroxyproline Residue in the Structure of Conantokin Rl-B and Its Role in GluN2B Subunit-Selective Antagonistic Activity toward N-Methyl-d-Aspartate Receptors."  Biochemistry 55, 7112-7122 (2016).
PubMed: 27981829

Assembly members:

Assembly members:
entity_1, polymer, 20 residues, 2360.336 Da.

Natural source:

Natural source:   Common Name: Conus rolani   Taxonomy ID: 745791   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Conus rolani

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEXXLAXKAAXFARXLANYX

Data sets:
Data typeCount
13C chemical shifts61
15N chemical shifts19
1H chemical shifts109

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 20 residues - 2360.336 Da.

1   GLYGLUCGUCGULEUALACGULYSALAALA
2   CGUPHEALAARGCGULEUALAASNTYRNH2

Samples:

sample_1: entity_1 mM; HEPES, [U-2H], 20 mM; Magnesium Chloride 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

TOPSPIN, Bruker Biospin - chemical shift assignment, collection, processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AvanceII 800 MHz

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