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 26691

Title: Chemical shift assignment of yeast Bcd1 protein zinc finger   PubMed: 27139642

Deposition date: 2015-10-22 Original release date: 2016-05-23

Authors: Bragantini, Benoit; Quinternet, Marc; Manival, Xavier

Citation: Bragantini, Benoit; Quinternet, Marc; Manival, Xavier; Charpentier, Bruno; Tiotiu, Decebal; Rothe, Benjamin; Saliou, Jean-Michel; Cianferani, Sarah. "Functional and structural insights into the zinc-finger HIT protein family involved in box C/D snoRNP biogenesis"  J. Mol. Biol. 428, 2488-2506 (2016).

Assembly members:
ZnF-Bcd1, polymer, 48 residues, 5341.2 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ZnF-Bcd1: GPHMAVLCGVCGIKEFKYKC PRCLVQTCSLECSKKHKTRD NCSGQTHD

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts84
1H chemical shifts583

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ZnF-Bcd11
2zinc ion, 12
3zinc ion, 22

Entities:

Entity 1, ZnF-Bcd1 48 residues - 5341.2 Da.

Residues 1-3 represent non-native residues from affinity tag

1   GLYPROHISMETALAVALLEUCYSGLYVAL
2   CYSGLYILELYSGLUPHELYSTYRLYSCYS
3   PROARGCYSLEUVALGLNTHRCYSSERLEU
4   GLUCYSSERLYSLYSHISLYSTHRARGASP
5   ASNCYSSERGLYGLNTHRHISASP

Entity 2, zinc ion, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: ZnF-Bcd1, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 150 mM; TCEP 0.5 mM; DTT, [U-2H], 3 mM

sample_conditions_1: ionic strength: 160 mM; pH: 6.4; pressure: 1 atm; temperature: 313 K

sample_conditions_2: ionic strength: 160 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQC long rangesample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz

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