BMRB Entry 18874
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18874
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Title: PHD domain of ING4 N214D mutant PubMed: 20705953
Deposition date: 2012-12-04 Original release date: 2012-12-13
Authors: Blanco, Francisco
Citation: Blanco, Francisco; Palmero, Ignacio. "Functional impact of cancer-associated mutations in the tumor suppressor protein ING4" Carinogenesis 31, 1932-1938 (2010).
Assembly members:
ING4_PHD_mutant_N214D, polymer, 63 residues, 7316.4 Da.
entity_ZN, 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: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ING4_PHD_mutant_N214D: MDMPVDPNEPTYCLCHQVSY
GEMIGCDDPDCSIEWFHFAC
VGLTTKPRGKWFCPRCSQER
KKK
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 368 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ING4 PHD mutant N214D | 1 |
| 2 | Zn ion, 1 | 2 |
| 3 | Zn ion, 2 | 2 |
Entities:
Entity 1, ING4 PHD mutant N214D 63 residues - 7316.4 Da.
Residue Met187 is not native. It comes from the cloning of the fragment and expression in E coli
| 1 | MET | ASP | MET | PRO | VAL | ASP | PRO | ASN | GLU | PRO | ||||
| 2 | THR | TYR | CYS | LEU | CYS | HIS | GLN | VAL | SER | TYR | ||||
| 3 | GLY | GLU | MET | ILE | GLY | CYS | ASP | ASP | PRO | ASP | ||||
| 4 | CYS | SER | ILE | GLU | TRP | PHE | HIS | PHE | ALA | CYS | ||||
| 5 | VAL | GLY | LEU | THR | THR | LYS | PRO | ARG | GLY | LYS | ||||
| 6 | TRP | PHE | CYS | PRO | ARG | CYS | SER | GLN | GLU | ARG | ||||
| 7 | LYS | LYS | LYS |
Entity 2, Zn ion, 1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: ING4 PHD mutant N214D, [U-100% 15N], 0.5 ± 0.05 mM; DSS 30 uM; DTT 1 ± 0.1 mM; sodium phosphate 20 ± 2 mM; sodium chloride 50 ± 5 mM
sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts