BMRB Entry 30703
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30703
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Title: Solution structure of the TTD and linker region of UHRF1
Deposition date: 2019-12-31 Original release date: 2020-06-11
Authors: Lemak, A.; Houliston, S.; Duan, S.; Ong, M.; Arrowsmith, C.
Citation: Lemak, A.; Houliston, S.; Duan, S.; Ong, M.; Arrowsmith, C.. "Solution structure of the TTD and linker region of UHRF1" To be published ., .-..
Assembly members:
entity_1, polymer, 168 residues, 19475.812 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GLYKVNEYVDARDTNMGAWF
EAQVVRVTRKAPSRDEPCSS
TSRPALEEDVIYHVKYDDYP
ENGVVQMNSRDVRARARTII
KWQDLEVGQVVMLNYNPDNP
KERGFWYDAEISRKRETRTA
RELYANVVLGDDSLNDCRII
FVDEVFKIERPGEGSPMVDN
PMRRKSGP
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 616 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 1027 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 168 residues - 19475.812 Da.
| 1 | GLY | LEU | TYR | LYS | VAL | ASN | GLU | TYR | VAL | ASP | ||||
| 2 | ALA | ARG | ASP | THR | ASN | MET | GLY | ALA | TRP | PHE | ||||
| 3 | GLU | ALA | GLN | VAL | VAL | ARG | VAL | THR | ARG | LYS | ||||
| 4 | ALA | PRO | SER | ARG | ASP | GLU | PRO | CYS | SER | SER | ||||
| 5 | THR | SER | ARG | PRO | ALA | LEU | GLU | GLU | ASP | VAL | ||||
| 6 | ILE | TYR | HIS | VAL | LYS | TYR | ASP | ASP | TYR | PRO | ||||
| 7 | GLU | ASN | GLY | VAL | VAL | GLN | MET | ASN | SER | ARG | ||||
| 8 | ASP | VAL | ARG | ALA | ARG | ALA | ARG | THR | ILE | ILE | ||||
| 9 | LYS | TRP | GLN | ASP | LEU | GLU | VAL | GLY | GLN | VAL | ||||
| 10 | VAL | MET | LEU | ASN | TYR | ASN | PRO | ASP | ASN | PRO | ||||
| 11 | LYS | GLU | ARG | GLY | PHE | TRP | TYR | ASP | ALA | GLU | ||||
| 12 | ILE | SER | ARG | LYS | ARG | GLU | THR | ARG | THR | ALA | ||||
| 13 | ARG | GLU | LEU | TYR | ALA | ASN | VAL | VAL | LEU | GLY | ||||
| 14 | ASP | ASP | SER | LEU | ASN | ASP | CYS | ARG | ILE | ILE | ||||
| 15 | PHE | VAL | ASP | GLU | VAL | PHE | LYS | ILE | GLU | ARG | ||||
| 16 | PRO | GLY | GLU | GLY | SER | PRO | MET | VAL | ASP | ASN | ||||
| 17 | PRO | MET | ARG | ARG | LYS | SER | GLY | PRO |
Samples:
sample_1: TTD-linker, [U-99% 13C; U-99% 15N], 250 uM; sodium chloride 150 mM; sodium phosphate 25 mM; DTT 5 mM; beta-mercaptoethanol 2 mM; TCEP 2 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 303 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
ABACUS, Lemak and Arrowsmith - chemical shift assignment
Sparky, Goddard - peak picking
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE II 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts