BMRB Entry 36075
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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/BMR36075
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Title: The PHD finger of human Kiaa1045 protein PubMed: 29430827
Deposition date: 2017-04-24 Original release date: 2018-04-30
Authors: Miyamoto, K.
Citation: Miyamoto, Kazuhide; Yamashita, Ayumi; Saito, Kazuki. "Solution structure of the PHD finger from the human KIAA1045 protein" Protein Sci. 27, 987-992 (2018).
Assembly members:
PHD finger protein 24, polymer, 60 residues, 6858.710 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
PHD finger protein 24: EMCDVCEVWTAESLFPCRVC
TRVFHDGCLRRMGYIQGDSA
AEVTEMAHTETGWSCHYCDN
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 246 |
15N chemical shifts | 55 |
1H chemical shifts | 371 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_ZN_1 | 2 |
3 | entity_ZN_2 | 2 |
Entities:
Entity 1, entity_1 60 residues - 6858.710 Da.
1 | GLU | MET | CYS | ASP | VAL | CYS | GLU | VAL | TRP | THR | |
2 | ALA | GLU | SER | LEU | PHE | PRO | CYS | ARG | VAL | CYS | |
3 | THR | ARG | VAL | PHE | HIS | ASP | GLY | CYS | LEU | ARG | |
4 | ARG | MET | GLY | TYR | ILE | GLN | GLY | ASP | SER | ALA | |
5 | ALA | GLU | VAL | THR | GLU | MET | ALA | HIS | THR | GLU | |
6 | THR | GLY | TRP | SER | CYS | HIS | TYR | CYS | ASP | ASN |
Entity 2, entity_ZN_1 - Zn 2 - 65.409 Da.
1 | ZN |
Samples:
sample_1: PHD finger, [U-13C; U-15N], 1 mM; Tris-HCl 20 mM; NaCl 50 mM; dithiothreitol 1 mM; ZnCl2 50 uM; H2O 90%; D2O, U-2H, 10%
sample_conditions_1: ionic strength: 70 mM; pH: 6.9; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - refinement
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts