BMRB Entry 25221
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25221
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Title: Solution structure of the PHD domain of Yeast YNG2
Deposition date: 2014-09-12 Original release date: 2014-12-22
Authors: Taeb, Samira; Kaustov, Lilia; Lemak, Alexander; Farhadi, Sahar; Sheng, Yi
Citation: Taeb, Samira; Kaustov, Lilia; Lemak, Alexander; Farhadi, Sahar; Sheng, Yi. "Solution structure of the PHD domain of Yeast YNG2" Not known ., .-..
Assembly members:
entity_1, polymer, 50 residues, 5938.856 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: TLYCFCQRVSFGEMVACDGP
NCKYEWFHYDCVNLKEPPKG
TWYCPECKIE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 340 |
| 13C chemical shifts | 213 |
| 15N chemical shifts | 49 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | ZINC ION_1 | 2 |
| 3 | ZINC ION_2 | 2 |
Entities:
Entity 1, entity_1 50 residues - 5938.856 Da.
| 1 | THR | LEU | TYR | CYS | PHE | CYS | GLN | ARG | VAL | SER | |
| 2 | PHE | GLY | GLU | MET | VAL | ALA | CYS | ASP | GLY | PRO | |
| 3 | ASN | CYS | LYS | TYR | GLU | TRP | PHE | HIS | TYR | ASP | |
| 4 | CYS | VAL | ASN | LEU | LYS | GLU | PRO | PRO | LYS | GLY | |
| 5 | THR | TRP | TYR | CYS | PRO | GLU | CYS | LYS | ILE | GLU |
Entity 2, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: entity_1, [U-13C; U-15N], 0.5 mM; sodium chloride 300 mM; potassium chloride 2.7 mM; potassium phosphate 2 mM; sodium phosphate 10 mM; CHAPS 0.05 mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 273 K; pH: 6.5; pressure: 1 atm; ionic strength: 300 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
FMCGUI, Lemak A., Gutmanas A., Chitayat S., Karra M., Far s C., Sunnerhagen M., and Arrowsmith CH - chemical shift assignment, refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| DBJ | GAA23808 |
| EMBL | CAY80101 |
| GB | AAB68930 AHY77791 AJP39190 AJU16386 AJU16646 |
| REF | NP_011958 |
| SP | P38806 |
| TPG | DAA06786 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts