BMRB Entry 30705
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30705
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Title: Solution structure of the PHD of mouse UHRF1 (NP95)
Deposition date: 2020-01-06 Original release date: 2020-06-11
Authors: Lemak, A.; Houliston, S.; Duan, S.; Arrowsmith, C.
Citation: Lemak, A.; Houliston, S.; Duan, S.; Arrowsmith, C.. "Solution structure of the PHD of mouse UHRF1 (NP95)" To be published ., .-..
Assembly members:
entity_1, polymer, 78 residues, 8693.900 Da.
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: SGPSCRFCKDDENKPCRKCA
CHVCGGREAPEKQLLCDECD
MAFHLYCLKPPLTSVPPEPE
WYCPSCRTDSSEVVQAGE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 303 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 486 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | ZN ion, 1 | 2 |
| 3 | ZN ion, 2 | 2 |
| 4 | ZN ion, 3 | 2 |
Entities:
Entity 1, unit_1 78 residues - 8693.900 Da.
| 1 | SER | GLY | PRO | SER | CYS | ARG | PHE | CYS | LYS | ASP | ||||
| 2 | ASP | GLU | ASN | LYS | PRO | CYS | ARG | LYS | CYS | ALA | ||||
| 3 | CYS | HIS | VAL | CYS | GLY | GLY | ARG | GLU | ALA | PRO | ||||
| 4 | GLU | LYS | GLN | LEU | LEU | CYS | ASP | GLU | CYS | ASP | ||||
| 5 | MET | ALA | PHE | HIS | LEU | TYR | CYS | LEU | LYS | PRO | ||||
| 6 | PRO | LEU | THR | SER | VAL | PRO | PRO | GLU | PRO | GLU | ||||
| 7 | TRP | TYR | CYS | PRO | SER | CYS | ARG | THR | ASP | SER | ||||
| 8 | SER | GLU | VAL | VAL | GLN | ALA | GLY | GLU |
Entity 2, ZN ion, 1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: PHD, [U-99% 13C; U-99% 15N], 200 uM; DTT 5 mM; beta-mercaptoethanol 2 mM; TCEP 5 mM; sodium chloride 150 mM; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 290 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
ABACUS, Lemak and Arrowsmith - chemical shift assignment
Sparky, Goddard - peak picking
NMR spectrometers:
- Bruker AVANCE II 800 MHz
- Bruker AVANCE III 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts