BMRB Entry 27436

Name: Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana
Published: 2018-11-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27436

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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:

Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana

Deposition date:

2018-03-28

Original release date:

2018-11-16

Authors:

Iwakawa, Naoto; Mahana, Yutaka; Ono, Arina; Ohki, Izuru; Walinda, Erik; Morimoto, Daichi; Sugase, Kenji; Shirakawa, Masahiro

Citation:

Citation: Iwakawa, Naoto; Mahana, Yutaka; Ono, Arina; Ohki, Izuru; Walinda, Erik; Morimoto, Daichi; Sugase, Kenji; Shirakawa, Masahiro. "Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana" Biomol. NMR Assignments 13, 59-62 (2019).
PubMed: 30242623

Assembly members:

Assembly members:
AtMBD6, polymer, 68 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX6p-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AtMBD6: GPLGSDNWLPPGWRVEDKIR TSGATAGSVDKYYYEPNTGR KFRSRTEVLYYLEHGTSKRG TKKAENTY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	305
15N chemical shifts	64
1H chemical shifts	454

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MBD6	1

Entities:

Entity 1, MBD6 68 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

ASP

ASN

TRP

LEU

PRO

2

PRO

GLY

TRP

ARG

VAL

GLU

ASP

LYS

ILE

ARG

3

THR

SER

GLY

ALA

THR

ALA

GLY

SER

VAL

ASP

4

LYS

TYR

GLU

PRO

ASN

THR

GLY

ARG

5

LYS

PHE

ARG

SER

ARG

THR

GLU

VAL

LEU

TYR

6

TYR

LEU

GLU

HIS

GLY

THR

SER

LYS

ARG

GLY

7

THR

LYS

ALA

GLU

ASN

THR

TYR

Samples:

sample_1: AtMBD6, [U-100% 13C; U-100% 15N], 5 mM; D2O, [U-2H], 5%; H2O 95%; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

MagRO, Kobayashi N, Iwahara J, Koshiba S, Tomizawa T, Tochio N, G ntert P, Kigawa T, Yokoyama S - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

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