BMRB Entry 25426

Name: MBD2 intrinsically disordered region
Published: 2018-02-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25426

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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:

MBD2 intrinsically disordered region

Deposition date:

2015-01-12

Original release date:

2018-02-23

Authors:

Williams, David

Citation:

Citation: Desai, Megha; Webb, Heather; Sinanan, Leander; Scarsdale, Neel; Walavalkar, Ninad; Ginder, Gordon; Williams, David. "An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex" Nucleic Acids Res. 43, 3100-3113 (2015).
PubMed: 25753662

Assembly members:

Assembly members:
MBD2, polymer, 121 residues, Formula weight is not available

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 Vector: pet32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MBD2: GSDLNTTLPIRQTASIFKQP VTKVTNHPSNKVKSDPQRMN EQPRQLFWEKRLQGLSASDV TEQIIKTMELPKGLQGVGPG SNDETLLSAVASALHTSSAP ITGQVSAAVEKNPAVWLNTS Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	331
15N chemical shifts	106
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	MBD2 IDR	1

Entities:

Entity 1, MBD2 IDR 121 residues - Formula weight is not available

Residue 1-2 represent residual from non-native affinity tag.

1

GLY

SER

ASP

LEU

ASN

THR

LEU

PRO

ILE

2

ARG

GLN

THR

ALA

SER

ILE

PHE

LYS

GLN

PRO

3

VAL

THR

LYS

VAL

THR

ASN

HIS

PRO

SER

ASN

4

LYS

VAL

LYS

SER

ASP

PRO

GLN

ARG

MET

ASN

5

GLU

GLN

PRO

ARG

GLN

LEU

PHE

TRP

GLU

LYS

6

ARG

LEU

GLN

GLY

LEU

SER

ALA

SER

ASP

VAL

7

THR

GLU

GLN

ILE

LYS

THR

MET

GLU

LEU

8

PRO

LYS

GLY

LEU

GLN

GLY

VAL

GLY

PRO

GLY

9

SER

ASN

ASP

GLU

THR

LEU

SER

ALA

VAL

10

ALA

SER

ALA

LEU

HIS

THR

SER

ALA

PRO

11

ILE

THR

GLY

GLN

VAL

SER

ALA

VAL

GLU

12

LYS

ASN

PRO

ALA

VAL

TRP

LEU

ASN

THR

SER

13

GLN

Samples:

sample_1: MBD2, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%; NaH2PO4 10 mM; sodium azide 0.02%; DTT 1 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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

Software:

CcpNMR, CCPN - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 700 MHz

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