BMRB Entry 19171

Name: transcriptional repressor domain of methylated DNA binding domain protein 1
Published: 2014-09-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19171

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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:

transcriptional repressor domain of methylated DNA binding domain protein 1

Deposition date:

2013-04-16

Original release date:

2014-09-19

Authors:

Lim, Jackwee; Shahul Hameed, Umar Farook; Yang, Daiwen; Kunchithapadam, Swaminathan; Wasik, Mariusz

Citation:

Citation: Hameed, Umar Farook Shahul; Lim, Jackwee; Zhang, Qian; Wasik, Mariusz; Yang, Daiwen; Swaminathan, Kunchithapadam. "Transcriptional repressor domain of MBD1 is intrinsically disordered and interacts with its binding partners in a selective manner." Sci. Rep. 4, 4896-4896 (2014).
PubMed: 24810720

Assembly members:

Assembly members:
TRD_of_MBD1, polymer, 117 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):
TRD_of_MBD1: MHHHHHHSSGLVPRGSEFDE WTPGTAVLTSPVLVPGCPSK AVDPGLPSVKQEPPDPEEDK EENKDDSASKLAPEEEAGGA GTPVITEIFSLGGTRFRDTA VWLPRSKDLKKPGARKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	442
13C chemical shifts	258
15N chemical shifts	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRD of MBD1	1

Entities:

Entity 1, TRD of MBD1 117 residues - Formula weight is not available

1

MET

HIS

SER

GLY

2

LEU

VAL

PRO

ARG

GLY

SER

GLU

PHE

ASP

GLU

3

TRP

THR

PRO

GLY

THR

ALA

VAL

LEU

THR

SER

4

PRO

VAL

LEU

VAL

PRO

GLY

CYS

PRO

SER

LYS

5

ALA

VAL

ASP

PRO

GLY

LEU

PRO

SER

VAL

LYS

6

GLN

GLU

PRO

ASP

PRO

GLU

ASP

LYS

7

GLU

ASN

LYS

ASP

SER

ALA

SER

LYS

8

LEU

ALA

PRO

GLU

ALA

GLY

ALA

9

GLY

THR

PRO

VAL

ILE

THR

GLU

ILE

PHE

SER

10

LEU

GLY

THR

ARG

PHE

ARG

ASP

THR

ALA

11

VAL

TRP

LEU

PRO

ARG

SER

LYS

ASP

LEU

LYS

12

LYS

PRO

GLY

ALA

ARG

LYS

GLN

Samples:

sample_1: TRD of MBD1, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 20 mM; sodium azide 0.1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.02 M; 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D MQ-(H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
4D timeshared 13C/15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRspy, Yang Daiwen, Zheng Yu - chemical shift assignment

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

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

NMR spectrometers:

Bruker Avance 800 MHz

DBJ	BAE02268 BAF84208 BAG58353 BAG63407 BAI45833
EMBL	CAA71735 CAH90629
GB	AAD50371 AAD51442 AAD51444 AAH33242 ABM47767
REF	NP_001191065 NP_001191066 NP_001191067 NP_001191068 NP_001191069
SP	Q9UIS9
AlphaFold	Q9UIS9