BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18874

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

Data sets:
Data typeCount
15N chemical shifts61
1H chemical shifts368

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ING4 PHD mutant N214D1
2Zn ion, 12
3Zn ion, 22

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   METASPMETPROVALASPPROASNGLUPRO
2   THRTYRCYSLEUCYSHISGLNVALSERTYR
3   GLYGLUMETILEGLYCYSASPASPPROASP
4   CYSSERILEGLUTRPPHEHISPHEALACYS
5   VALGLYLEUTHRTHRLYSPROARGGLYLYS
6   TRPPHECYSPROARGCYSSERGLNGLUARG
7   LYSLYSLYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_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

Related Database Links:

UNP Q9UNL4
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts