BMRB Entry 25881

Title:
Chemical shift assignment of yeast Hit1 protein zinc finger
Deposition date:
2015-11-06
Original release date:
2016-05-23
Authors:
Bragantini, Benoit; Quinternet, Marc; Manival, Xavier
Citation:

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).
PubMed: 27139642

Assembly members:

Assembly members:
entity_1, polymer, 49 residues, 5399.411 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pnEA-3cH

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMVSSAVKCGICRGVDGK YKCPKCGVRYCSLKCYKDAA KHVHKESEQ

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts91
1H chemical shifts549

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZN ion, 12
3ZN ion, 22

Entities:

Entity 1, entity_1 49 residues - 5399.411 Da.

1   GLYPROHISMETVALSERSERALAVALLYS
2   CYSGLYILECYSARGGLYVALASPGLYLYS
3   TYRLYSCYSPROLYSCYSGLYVALARGTYR
4   CYSSERLEULYSCYSTYRLYSASPALAALA
5   LYSHISVALHISLYSGLUSERGLUGLN

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

1   ZN

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 2.2 mM; sodium phosphate 10 mM; sodium chloride 150 mM; TCEP 0.5 mM; DTT, [U-2H], 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 160 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 160 mM; pH: 6.4; pressure: 1 atm; temperature: 313 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
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_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-15N HSQC long rangesample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-15N HSQC long rangesample_1isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_2

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz

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