BMRB Entry 30585

Name: Solution structure of MLL4 PHD6 domain in complex with histone H4K16ac peptide
Published: 2019-05-17

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PDB ID: 6o7g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30585
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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 MLL4 PHD6 domain in complex with histone H4K16ac peptide

Deposition date:

2019-03-07

Original release date:

2019-05-17

Authors:

Zhang, Y.; Kutateladze, T.

Citation:

Citation: Zhang, Y.; Jang, Y.; Lee, J.; Ahn, J.; Xu, L.; Holden, M.; Cornett, E.; Krajewski, K.; Klein, B.; Wang, S.; Dou, Y.; Roeder, R.; Strahl, B.; Rothbart, S.; Shi, X.; Ge, K.; Kutateladze, T.. "Selective binding of the PHD6 finger of MLL4 to histone H4K16ac links MLL4 and MOF" Nat. Commun. 10, 2314-2314 (2019).
PubMed: 31127101

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7240.149 Da.
entity_2, polymer, 13 residues, 1264.527 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMSLVTCPICHAPYVEED LLIQCRHCERWMHAGCESLF TEDDVEQAADEGFDCVSCQP YVVK
entity_2: XGKGGAXRHRKVX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	58
1H chemical shifts	392

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2
3	entity_3, 1	3
4	entity_3, 2	3

Entities:

Entity 1, entity_1 64 residues - 7240.149 Da.

1

GLY

SER

HIS

MET

SER

LEU

VAL

THR

CYS

PRO

2

ILE

CYS

HIS

ALA

PRO

TYR

VAL

GLU

ASP

3

LEU

ILE

GLN

CYS

ARG

HIS

CYS

GLU

ARG

4

TRP

MET

HIS

ALA

GLY

CYS

GLU

SER

LEU

PHE

5

THR

GLU

ASP

VAL

GLU

GLN

ALA

ASP

6

GLU

GLY

PHE

ASP

CYS

VAL

SER

CYS

GLN

PRO

7

TYR

VAL

LYS

Entity 2, entity_2 13 residues - 1264.527 Da.

1

ACE

GLY

LYS

GLY

ALA

ALY

ARG

HIS

ARG

2

LYS

VAL

NH2

Entity 3, entity_3, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: MLL4 PHD6, [U-13C; U-15N], 2.5 mM; histone H4K16ac (11-21) peptide 7.5 mM; NaCl buffer 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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 C(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
2D filtered TOCSY	sample_1	isotropic	sample_conditions_1
3D filtered NOESY	sample_1	isotropic	sample_conditions_1
3D NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr Analysis, CCPN - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 900 MHz

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