BMRB Entry 19487
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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/BMR19487
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Title: Solution structure of the PP2WW mutant (KPP2WW) of HYPB PubMed: 24412394
Deposition date: 2013-09-10 Original release date: 2014-02-12
Authors: Gao, Yong-Guang; Hu, Hong-Yu
Citation: Gao, Yong-Guang; Yang, Hui; Zhao, Jian; Jiang, Ya-Jun; Hu, Hong-Yu. "Autoinhibitory Structure of the WW Domain of HYPB/SETD2 Regulates Its Interaction with the Proline-Rich Region of Huntingtin." Structure ., .-. (2014).
Assembly members:
KPP2WW, polymer, 56 residues, 6193.844 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):
KPP2WW: GSDLPPPSPPAAATIVLPPN
WKTARDPEGKIYYYHVITRQ
TQWDPPTWESPGDDAS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 174 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 261 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PP2WW mutant (KPP2WW) of HYPB | 1 |
Entities:
Entity 1, PP2WW mutant (KPP2WW) of HYPB 56 residues - 6193.844 Da.
| 1 | GLY | SER | ASP | LEU | PRO | PRO | PRO | SER | PRO | PRO | ||||
| 2 | ALA | ALA | ALA | THR | ILE | VAL | LEU | PRO | PRO | ASN | ||||
| 3 | TRP | LYS | THR | ALA | ARG | ASP | PRO | GLU | GLY | LYS | ||||
| 4 | ILE | TYR | TYR | TYR | HIS | VAL | ILE | THR | ARG | GLN | ||||
| 5 | THR | GLN | TRP | ASP | PRO | PRO | THR | TRP | GLU | SER | ||||
| 6 | PRO | GLY | ASP | ASP | ALA | SER |
Samples:
sample_1: KPP2WW, [U-99% 13C; U-99% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.05 w/v; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.08 M; pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | 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 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
ARIA, Linge, O, . - structure solution
Molmol, Koradi, Billeter and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection
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