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
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:

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).
PubMed: 19293276

Assembly members:

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:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: modified pET24d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
first PHD finger: GAMAQKNEDECAVCRDGGEL ICCDGCPRAFHLACLSPPLR EIPSGTWRCSSCLQATVQEV QPRAEE
histone H3 tail: ARTKQTARKS

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts64
1H chemical shifts415

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1first PHD finger1
2histone H3 tail2
3ZINC ION_13
4ZINC ION_23

Entities:

Entity 1, first PHD finger 66 residues - 7145.130 Da.

1   GLYALAMETALAGLNLYSASNGLUASPGLU
2   CYSALAVALCYSARGASPGLYGLYGLULEU
3   ILECYSCYSASPGLYCYSPROARGALAPHE
4   HISLEUALACYSLEUSERPROPROLEUARG
5   GLUILEPROSERGLYTHRTRPARGCYSSER
6   SERCYSLEUGLNALATHRVALGLNGLUVAL
7   GLNPROARGALAGLUGLU

Entity 2, histone H3 tail 10 residues - 1150.343 Da.

1   ALAARGTHRLYSGLNTHRALAARGLYSSER

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:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYSample_2isotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA23989 BAA23991
GB AAI37269 AAI37271 AIC54015 EAX09443

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