BMRB Entry 51020

Name: 1H, 13C and 15N NMR assignments of an engineered Methyl CpG binding domain (MBD) protein
Published: 2023-02-17

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PDB ID: 8ajr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51020
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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:

1H, 13C and 15N NMR assignments of an engineered Methyl CpG binding domain (MBD) protein

Deposition date:

2021-07-15

Original release date:

2023-02-17

Authors:

Singh, Himanshu; Linser, Rasmus

Citation:

Citation: Singh, Himanshu; Das, Chandan; Buchmuller, Benjamin; Schafer, Lars; Summerer, Daniel; Linser, Rasmus. "Epigenetic CpG duplex marks probed by an evolved DNA reader via a well-tempered conformational plasticity" Nucleic Acids Res. 51, 6495-6506 (2023).
PubMed: 36919612

Assembly members:

Assembly members:
entity_1, polymer, 104 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: pBR322

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SLEDRGPMYDDPTLPEGWTR KLTQRKSGRSAGKYDAYLIN PQGKAFRNKVELIAYFEKVG DTSLDPNDFDFTVTGRGSPS RREQKPPKKPKSPKATSHHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	284
15N chemical shifts	79
1H chemical shifts	437

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MeCP2	1

Entities:

Entity 1, MeCP2 104 residues - Formula weight is not available

1

SER

LEU

GLU

ASP

ARG

GLY

PRO

MET

TYR

ASP

2

ASP

PRO

THR

LEU

PRO

GLU

GLY

TRP

THR

ARG

3

LYS

LEU

THR

GLN

ARG

LYS

SER

GLY

ARG

SER

4

ALA

GLY

LYS

TYR

ASP

ALA

TYR

LEU

ILE

ASN

5

PRO

GLN

GLY

LYS

ALA

PHE

ARG

ASN

LYS

VAL

6

GLU

LEU

ILE

ALA

TYR

PHE

GLU

LYS

VAL

GLY

7

ASP

THR

SER

LEU

ASP

PRO

ASN

ASP

PHE

ASP

8

PHE

THR

VAL

THR

GLY

ARG

GLY

SER

PRO

SER

9

ARG

GLU

GLN

LYS

PRO

LYS

PRO

10

LYS

SER

PRO

LYS

ALA

THR

SER

HIS

11

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

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SPARKY: Backbone or all simulated peaks

BMRB Entry 51020

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: