BMRB Entry 16861

Name: Solution structure of the double PHD (plant homeodomain) fingers of human transcriptional protein DPF3b bound to a histone H4 peptide containing acetylation at lysine 16
Published: 2010-09-03

Click here to enlarge.

PDB ID: 2kwn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16861
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Solution structure of the double PHD (plant homeodomain) fingers of human transcriptional protein DPF3b bound to a histone H4 peptide containing acetylation at lysine 16 PubMed: 20613843

Deposition date: 2010-04-13 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_lys_16, polymer, 15 residues, 1681.058 Da.
double_PHD_fingers, polymer, 114 residues, 12746.515 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_lys_16: GLGKGGAXRHRKVLR
double_PHD_fingers: GSYCDFCLGGSNMNKKSGRP EELVSCADCGRSGHPTCLQF TLNMTEAVKTYKWQCIECKS CILCGTSENDDQLLFCDDCD RGYHMYCLNPPVAEPPEGSW SCHLCWELLKEKAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	364
15N chemical shifts	117
1H chemical shifts	798

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Entity Assembly ID	Entity Name	Entity ID
1	histone_H4_acet_lys_16	1
2	double_PHD_fingers	2
3	ZINC ION_1	3
4	ZINC ION_2	3
5	ZINC ION_3	3
6	ZINC ION_4	3

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-Edited_13C/15N-filtered NOESY	sample_1	isotropic	sample_conditions_1

BMRB	16858 16859 16865
PDB	2KWJ 2KWK 2KWN 2KWO
DBJ	BAC30204
GB	AAX20019 EDL02734 EGV99590 EHH28015 EHH63746
REF	NP_001254554 NP_001267471 XP_001140541 XP_001254780 XP_001375927
SP	P58269 Q92784
TPG	DAA25179

Biological Magnetic Resonance Data Bank

BMRB Entry 16861

Title: Solution structure of the double PHD (plant homeodomain) fingers of human transcriptional protein DPF3b bound to a histone H4 peptide containing acetylation at lysine 16 PubMed: 20613843

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: