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 17556

Title: 1H, 13C, and 15N Chemical Shift Assignments of the yPEPmin fragment of Rsa1p   PubMed: 24234454

Deposition date: 2011-03-30 Original release date: 2014-04-23

Authors: Quinternet, Marc; Back, Regis; Branlant, Christiane; Manival, Xavier

Citation: Rothe, Benjamin; Back, Regis; Quinternet, Marc; Bizarro, Jonathan; Robert, Marie-Cecile; Blaud, Magali; Romier, Christophe; Manival, Xavier; Charpentier, Bruno; Bertrand, Edouard; Branlant, Christiane. "Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly."  Nucleic Acids Res. 42, 2015-2036 (2014).

Assembly members:
yPEPmin_of_Rsa1p, polymer, 15 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
yPEPmin_of_Rsa1p: TDEDVKKWREERKKM

Data sets:
Data typeCount
13C chemical shifts56
15N chemical shifts14
1H chemical shifts116

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1yPEPmin1

Entities:

Entity 1, yPEPmin 15 residues - Formula weight is not available

1   THRASPGLUASPVALLYSLYSTRPARGGLU
2   GLUARGLYSLYSMET

Samples:

sample_1: yPEPmin of Rsa1p 3 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18959
PDB

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