BMRB Entry 16510
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16510
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Title: The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation PubMed: 19293276
Deposition date: 2009-09-23 Original release date: 2009-10-06
Authors: Chignola, Francesca; Gaetani, Massimiliano; Rebane, Ana; Org, Tonis; Mollica, Luca; Zucchelli, Chiara; Spitaleri, Andrea; Mannella, Valeria; Peterson, Part; Musco, Giovanna
Citation: Chignola, Francesca; Gaetani, Massimiliano; Rebane, Ana; Org, Tonis; Mollica, Luca; Zucchelli, Chiara; Spitaleri, Andrea; Mannella, Valeria; Peterson, Part; Musco, Giovanna. "The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation" Nucleic Acids Res. 37, 2951-2961 (2009).
Assembly members:
first PHD finger, polymer, 66 residues, 7145.130 Da.
histone H3 tail, polymer, 10 residues, 1150.343 Da.
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):
first PHD finger: GAMAQKNEDECAVCRDGGEL
ICCDGCPRAFHLACLSPPLR
EIPSGTWRCSSCLQATVQEV
QPRAEE
histone H3 tail: ARTKQTARKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 251 |
| 15N chemical shifts | 64 |
| 1H chemical shifts | 415 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | first PHD finger | 1 |
| 2 | histone H3 tail | 2 |
| 3 | ZINC ION_1 | 3 |
| 4 | ZINC ION_2 | 3 |
Entities:
Entity 1, first PHD finger 66 residues - 7145.130 Da.
| 1 | GLY | ALA | MET | ALA | GLN | LYS | ASN | GLU | ASP | GLU | ||||
| 2 | CYS | ALA | VAL | CYS | ARG | ASP | GLY | GLY | GLU | LEU | ||||
| 3 | ILE | CYS | CYS | ASP | GLY | CYS | PRO | ARG | ALA | PHE | ||||
| 4 | HIS | LEU | ALA | CYS | LEU | SER | PRO | PRO | LEU | ARG | ||||
| 5 | GLU | ILE | PRO | SER | GLY | THR | TRP | ARG | CYS | SER | ||||
| 6 | SER | CYS | LEU | GLN | ALA | THR | VAL | GLN | GLU | VAL | ||||
| 7 | GLN | PRO | ARG | ALA | GLU | GLU |
Entity 2, histone H3 tail 10 residues - 1150.343 Da.
| 1 | ALA | ARG | THR | LYS | GLN | THR | ALA | ARG | LYS | SER |
Entity 3, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: AIRE-PHD1, [U-99% 13C; U-99% 15N], 0.1 – 0.5 mM; H3K4me00.3 – 1.5 mM; sodium chloride 150 mM; sodium phosphate 20 mM; DTT 5 mM; H2O 90%; D2O 10%
Sample_2: AIRE-PHD1, [U-99% 13C; U-99% 15N], 0.5 mM; H3K4me0 1.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 5 mM; D2O 100%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.3; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | Sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA v2.2, Linge, O, . - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
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