BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19171

Title: transcriptional repressor domain of methylated DNA binding domain protein 1   PubMed: 24810720

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: 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).

Assembly members:
TRD_of_MBD1, polymer, 117 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
TRD_of_MBD1: MHHHHHHSSGLVPRGSEFDE WTPGTAVLTSPVLVPGCPSK AVDPGLPSVKQEPPDPEEDK EENKDDSASKLAPEEEAGGA GTPVITEIFSLGGTRFRDTA VWLPRSKDLKKPGARKQ

Data sets:
Data typeCount
1H chemical shifts442
13C chemical shifts258
15N chemical shifts91

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1TRD of MBD11

Entities:

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

1   METHISHISHISHISHISHISSERSERGLY
2   LEUVALPROARGGLYSERGLUPHEASPGLU
3   TRPTHRPROGLYTHRALAVALLEUTHRSER
4   PROVALLEUVALPROGLYCYSPROSERLYS
5   ALAVALASPPROGLYLEUPROSERVALLYS
6   GLNGLUPROPROASPPROGLUGLUASPLYS
7   GLUGLUASNLYSASPASPSERALASERLYS
8   LEUALAPROGLUGLUGLUALAGLYGLYALA
9   GLYTHRPROVALILETHRGLUILEPHESER
10   LEUGLYGLYTHRARGPHEARGASPTHRALA
11   VALTRPLEUPROARGSERLYSASPLEULYS
12   LYSPROGLYALAARGLYSGLN

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D MQ-(H)CCH-TOCSYsample_1isotropicsample_conditions_1
4D timeshared 13C/15N NOESYsample_1isotropicsample_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

Related Database Links:

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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts