BMRB Entry 31105

Name: Solution structure of TET3/MLL4-PHD6
Published: 2024-06-20

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PDB ID: 8u2y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31105
MolProbity Validation Chart

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

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Title:

Solution structure of TET3/MLL4-PHD6

Deposition date:

2023-09-06

Original release date:

2024-06-20

Authors:

Mohid, S.; Zandian, M.; Zhang, Y.; Kutateladze, T.

Citation:

Citation: Becht, Dustin; Mohid, Sk Abdul; Lee, Ji-Eun; Zandian, Mohamad; Benz, Caroline; Biswas, Soumi; Sinha, Vikrant Kumar; Ivarsson, Ylva; Ge, Kai; Zhang, Yi; Kutateladze, Tatiana. "MLL4 binds TET3" Structure 32, 706-714 (2024).
PubMed: 38579707

Assembly members:

Assembly members:
entity_1, polymer, 9 residues, 864.945 Da.
entity_2, polymer, 60 residues, 6826.676 Da.
entity_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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GVGGSWGVF
entity_2: SLVTCPICHAPYVEEDLLIQ CRHCERWMHAGCESLFTEDD VEQAADEGFDCVSCQPYVVK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	246
15N chemical shifts	68
1H chemical shifts	355

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2
3	unit_3	3
4	unit_4	3

Entities:

Entity 1, unit_1 9 residues - 864.945 Da.

1

GLY

VAL

GLY

SER

TRP

GLY

VAL

PHE

Entity 2, unit_2 60 residues - 6826.676 Da.

1	SER	LEU	VAL	THR	CYS	PRO	ILE	CYS	HIS	ALA
2	PRO	TYR	VAL	GLU	GLU	ASP	LEU	LEU	ILE	GLN
3	CYS	ARG	HIS	CYS	GLU	ARG	TRP	MET	HIS	ALA
4	GLY	CYS	GLU	SER	LEU	PHE	THR	GLU	ASP	ASP
5	VAL	GLU	GLN	ALA	ALA	ASP	GLU	GLY	PHE	ASP
6	CYS	VAL	SER	CYS	GLN	PRO	TYR	VAL	VAL	LYS

Entity 3, unit_3 - Zn - 65.409 Da.

1

ZN

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
1D 1H	sample_1	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 31105

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	SER	LEU	VAL	THR	CYS	PRO	ILE	CYS	HIS	ALA
2	PRO	TYR	VAL	GLU	GLU	ASP	LEU	LEU	ILE	GLN
3	CYS	ARG	HIS	CYS	GLU	ARG	TRP	MET	HIS	ALA
4	GLY	CYS	GLU	SER	LEU	PHE	THR	GLU	ASP	ASP
5	VAL	GLU	GLN	ALA	ALA	ASP	GLU	GLY	PHE	ASP
6	CYS	VAL	SER	CYS	GLN	PRO	TYR	VAL	VAL	LYS

1	SER	LEU	VAL	THR	CYS	PRO	ILE	CYS	HIS	ALA
2	PRO	TYR	VAL	GLU	GLU	ASP	LEU	LEU	ILE	GLN
3	CYS	ARG	HIS	CYS	GLU	ARG	TRP	MET	HIS	ALA
4	GLY	CYS	GLU	SER	LEU	PHE	THR	GLU	ASP	ASP
5	VAL	GLU	GLN	ALA	ALA	ASP	GLU	GLY	PHE	ASP
6	CYS	VAL	SER	CYS	GLN	PRO	TYR	VAL	VAL	LYS

1	SER	LEU	VAL	THR	CYS	PRO	ILE	CYS	HIS	ALA
2	PRO	TYR	VAL	GLU	GLU	ASP	LEU	LEU	ILE	GLN
3	CYS	ARG	HIS	CYS	GLU	ARG	TRP	MET	HIS	ALA
4	GLY	CYS	GLU	SER	LEU	PHE	THR	GLU	ASP	ASP
5	VAL	GLU	GLN	ALA	ALA	ASP	GLU	GLY	PHE	ASP
6	CYS	VAL	SER	CYS	GLN	PRO	TYR	VAL	VAL	LYS