BMRB Entry 16865
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PDB ID: 2kwo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16865
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Title: Solution structure of the double PHD (plant homeodomain) fingers of human transcriptional protein DPF3b bound to a histone H4 peptide containing N-terminal acetylation at serine 1 PubMed: 20613843
Deposition date: 2010-04-14 Original release date: 2010-09-03
Authors: Zeng, Lei; Zhang, Qiang; Li, SiDe; Plotnikov, Alexander; Walsh, Martin; ZHOU, MING-MING
Citation: Zeng, Lei; Zhang, Qiang; Li, SiDe; Plotnikov, Alexander; Walsh, Martin; ZHOU, MING-MING. "Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b" Nature 466, 258-262 (2010).
Assembly members:
histone_H4_acet_serine_1, polymer, 20 residues, 1914.308 Da.
double_PHD_fingers, polymer, 114 residues, 12746.515 Da.
ACS, non-polymer, 395.452 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: chemical synthesis
Entity Sequences (FASTA):
histone_H4_acet_serine_1: XGRGKGGKGLGKGGAKRHRK
double_PHD_fingers: GSYCDFCLGGSNMNKKSGRP
EELVSCADCGRSGHPTCLQF
TLNMTEAVKTYKWQCIECKS
CILCGTSENDDQLLFCDDCD
RGYHMYCLNPPVAEPPEGSW
SCHLCWELLKEKAS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 364 |
15N chemical shifts | 117 |
1H chemical shifts | 801 |
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