BMRB Entry 27426

Name: Chemical shift assignments for mutant Hs MBD2 intrinsically disordered region
Published: 2018-03-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27426

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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:

Chemical shift assignments for mutant Hs MBD2 intrinsically disordered region

Deposition date:

2018-03-15

Original release date:

2018-03-19

Authors:

Williams, David

Citation:

Citation: Yu, Xiaofei; Azzo, Alexander; Bilinovich, Stephanie; Kurita, Ryo; Nakamura, Yukio; Williams, David; Ginder, Gordon. "Disruption of the MBD2-NuRD complex but not MBD3-NuRD induces high levels of expression in human adult erythroid cells" .

Assembly members:

Assembly members:
MBD2(R286E-L287A), 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: pET32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MBD2(R286E-L287A): GSDLNTTLPIRQTASIFKQP VTKVTNHPSNKVKSDPQRMN EQPRQLFWEKEAQGLSASDV TEQIIKTMELPKGLQGVGPG SNDETLLSAVASALHTSSAP ITGQVSAAVEKNPAVWLNTS Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	335
15N chemical shifts	107
1H chemical shifts	403

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MBD2 mutant IDR	1

Entities:

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

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

GLU

ALA

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 mutant IDR, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 0.03 M; pH: 6.0; 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 HNCA	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

Bruker INOVA 700 MHz

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