BMRB Entry 7383

Title:
NMR Structure of RRM-1 of Yeast NPL3 Protein
Deposition date:
2007-03-21
Original release date:
2008-05-06
Authors:
Deka, P.; Bucheli, M.; Skrisovska, L.; Allain, F.; Moore, C.; Buratowski, S.; Varani, G.
Citation:

Citation: Deka, P.; Bucheli, M.; Moore, C.; Buratowski, S.; Varani, G.. "Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals"  J. Mol. Biol. 375, 136-150 (2008).
PubMed: 18022637

Assembly members:

Assembly members:
Nucleolar_protein_3, polymer, 74 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts258
15N chemical shifts75
1H chemical shifts476

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nucleolar_protein_31

Entities:

Entity 1, Nucleolar_protein_3 74 residues - Formula weight is not available

1   GLULEUSERASNTHRARGLEUPHEVALARG
2   PROPHEPROLEUASPVALGLNGLUSERGLU
3   LEUASNGLUILEPHEGLYPROPHEGLYPRO
4   METLYSGLUVALLYSILELEUASNGLYPHE
5   ALAPHEVALGLUPHEGLUGLUALAGLUSER
6   ALAALALYSALAILEGLUGLUVALHISGLY
7   LYSSERPHEALAASNGLNPROLEUGLUVAL
8   VALTYRSERLYS

Samples:

sample_1: Nucleolar_protein_3, [U-99% 13C; U-99%15N], 1.0 ± 0.05 mM; Potassium phosphate 20 mM; potassium chloride 20 mM

sample_conditions_1: ionic strength: . .; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, GUNTERT, P. ET AL. - refinement

CYANA v2.1, GUNTERT, P. ET AL. - structure solution

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Varian INOVA 800 MHz
  • Bruker AVANCE 750 MHz

Related Database Links:

BMRB 15485
PDB
DBJ GAA22648
EMBL CAA46817 CAA50291 CAY78932
GB AAA34818 AAB64865 AHY75384 EDN60757 EDV07905
REF NP_010720
SP Q01560
TPG DAA12270
AlphaFold Q01560

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