BMRB Entry 26691
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26691
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 369 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 583 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ZnF-Bcd1 | 1 |
| 2 | zinc ion, 1 | 2 |
| 3 | zinc ion, 2 | 2 |
Entities:
Entity 1, ZnF-Bcd1 48 residues - 5341.2 Da.
Residues 1-3 represent non-native residues from affinity tag
| 1 | GLY | PRO | HIS | MET | ALA | VAL | LEU | CYS | GLY | VAL | ||||
| 2 | CYS | GLY | ILE | LYS | GLU | PHE | LYS | TYR | LYS | CYS | ||||
| 3 | PRO | ARG | CYS | LEU | VAL | GLN | THR | CYS | SER | LEU | ||||
| 4 | GLU | CYS | SER | LYS | LYS | HIS | LYS | THR | ARG | ASP | ||||
| 5 | ASN | CYS | SER | GLY | GLN | THR | HIS | ASP |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC long range | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_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