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 18959

Title: NMR structure of Rsa1p238-259 from S. Cerevisiae   PubMed: 24234454

Deposition date: 2013-01-17 Original release date: 2013-11-26

Authors: Quinternet, Marc; 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:
Rsa1p238-259, polymer, 22 residues, 2840.349 Da.

Natural source:   Common Name: Baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Rsa1p238-259: TDEDVKKWREERKKMWLLKI SN

Data sets:
Data typeCount
13C chemical shifts90
15N chemical shifts26
1H chemical shifts352

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rsa1p238-2591

Entities:

Entity 1, Rsa1p238-259 22 residues - 2840.349 Da.

1   THRASPGLUASPVALLYSLYSTRPARGGLU
2   GLUARGLYSLYSMETTRPLEULEULYSILE
3   SERASN

Samples:

sample_1: Rsa1p238-259 2 mM; potassium phosphate 10 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 3.7; pressure: 1 atm; temperature: 293 K

sample_conditions_2: ionic strength: 150 mM; pH: 3.7; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_2
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_2
2D 1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_2

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CARA, Keller and Wuthrich - chemical shift assignment

PREDITOR, Wishart DS. - structure solution

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ GAA26783
EMBL CAA97906 CAY86767
GB AHY77988 AJP41956 AJU23400 AJU24088 AJU24761
REF NP_015131
SP Q08932
TPG DAA11241

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts