BMRB Entry 31200

Name: ETO2 MYND bound to MPPL peptide from GATAD2A
Published: 2024-09-16

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PDB ID: 9de2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31200
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:

ETO2 MYND bound to MPPL peptide from GATAD2A

Deposition date:

2024-08-28

Original release date:

2024-09-16

Authors:

Williams, D.

Citation:

Citation: Dan-Dukor, G.; Shang, S.; Travis, C.; Leighton, G.; Schwochert, T.; Agrawal, P.; Ajasa, O.; Li, T.; Waters, M.; Ginder, G.; Williams, D.. "The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex" .

Assembly members:

Assembly members:
entity_1, polymer, 71 residues, 7696.501 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: GSASSQVVMPPLVRGAQQKN GRGSDSSESCWNCGRKASET CSGCNAARYCGSFCQHRDWE KHHHVCGQSLQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	266
15N chemical shifts	70
1H chemical shifts	366

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	2

Entities:

Entity 1, unit_1 71 residues - 7696.501 Da.

1

GLY

SER

ALA

SER

GLN

VAL

MET

PRO

2

PRO

LEU

VAL

ARG

GLY

ALA

GLN

LYS

ASN

3

GLY

ARG

GLY

SER

ASP

SER

GLU

SER

CYS

4

TRP

ASN

CYS

GLY

ARG

LYS

ALA

SER

GLU

THR

5

CYS

SER

GLY

CYS

ASN

ALA

ARG

TYR

CYS

6

GLY

SER

PHE

CYS

GLN

HIS

ARG

ASP

TRP

GLU

7

LYS

HIS

VAL

CYS

GLY

GLN

SER

LEU

8

GLN

Entity 2, unit_2 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: ETO2-NHR4-MPPLsc, [U-100% 13C; U-100% 15N], 500 uM; BisTris 25 mM; NaCl 100 mM; DTT 1 mM; ZnSO4 50 uM

sample_2: ETO2-NHR4-MPPLsc, [U-100% 13C; U-100% 15N], 500 uM; BisTris 25 mM; NaCl 100 mM; DTT 1 mM; ZnSO4 50 uM; PEG:hexonal (C13:E5 r=0.85) 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
3D HNCO JNH	sample_2	anisotropic	sample_conditions_2

Software:

CcpNmr Analysis v2, CCPN - chemical shift assignment

X-PLOR NIH v3.8, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker AVANCE III 850 MHz

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