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 30697

Title: Solution Structure of the Tau pre-mRNA Exon 10 Splicing Regulatory Element   PubMed: 32364710

Deposition date: 2019-12-16 Original release date: 2020-05-15

Authors: Chen, J.; Fountain, M.; Disney, M.

Citation: Chen, Jonathan; Zhang, Peiyuan; Abe, Masahito; Aikawa, Haruo; Zhang, Liying; Frank, Alexander; Zembryski, Timothy; Hubbs, Christopher; Park, HaJeung; Withka, Jane; Steppan, Claire; Rogers, Lucy; Cabral, Shawn; Pettersson, Martin; Wager, Travis; Fountain, Matthew; Rumbaugh, Gavin; Childs-Disney, Jessica; Disney, Matthew. "Design, Optimization, and Study of Small Molecules That Target Tau Pre-mRNA and Affect Splicing"  J. Am. Chem. Soc. 142, 8706-8727 (2020).

Assembly members:
entity_1, polymer, 11 residues, 3538.154 Da.
entity_2, polymer, 10 residues, 3175.964 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: CCGGCAGUGUG
entity_2: CACACGUCGG

Data sets:
Data typeCount
1H chemical shifts118

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 11 residues - 3538.154 Da.

1   CCGGCAGUGU
2   G

Entity 2, entity_2 10 residues - 3175.964 Da.

1   CACACGUCGG

Samples:

sample_1: WT Tau RNA 0.7 mM; WT Tau RNA 0.7 mM; KH2PO4/K2HPO4 10 mM; EDTA 0.05 mM

sample_2: WT Tau RNA 0.7 mM; WT Tau RNA 0.7 mM; KH2PO4/K2HPO4 10 mM; EDTA 0.05 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 281.5 K

Experiments:

NameSampleSample stateSample conditions
D2O 2D 1H-1H NOESYsample_1isotropicsample_conditions_1
H2O 2D 1H-1H NOESYsample_2isotropicsample_conditions_2
D2O 2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

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

TopSpin, Bruker Biospin - processing

Sparky, Goddard - chemical shift assignment

Amber v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III 700 MHz