BMRB Entry 36204

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36204
MolProbity Validation Chart

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Title:
the solution NMR structure of MBD domain
Deposition date:
2018-07-27
Original release date:
2025-09-27
Authors:
Li, S.; Feng, Y.; Zhou, Y.; Ding, Y.; Liu, K.; Nie, Y.; Li, F.; Yang, Y.
Citation:

Citation: Li, S.; Feng, Y.; Zhou, Y.; Ding, Y.; Liu, K.; Nie, Y.; Li, F.; Yang, Y.. "the solution NMR structure of MBD domains"  .

Assembly members:

Assembly members:
Methyl-CpG-binding domain-containing protein 11, polymer, 95 residues, 10687.85 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Methyl-CpG-binding domain-containing protein 11: MHHHHHHSSGRENLYFQGHM ASGSEEEVVSVELPAPSSWK KLFYPNKVGSVKKTEVVFVA PTGEEISNRKQLEQYLKSHP GNPAIAEFDWTTSGT

Data sets:
Data typeCount
13C chemical shifts335
15N chemical shifts69
1H chemical shifts497

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 95 residues - 10687.85 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYHISMET
3   ALASERGLYSERGLUGLUGLUVALVALSER
4   VALGLULEUPROALAPROSERSERTRPLYS
5   LYSLEUPHETYRPROASNLYSVALGLYSER
6   VALLYSLYSTHRGLUVALVALPHEVALALA
7   PROTHRGLYGLUGLUILESERASNARGLYS
8   GLNLEUGLUGLNTYRLEULYSSERHISPRO
9   GLYASNPROALAILEALAGLUPHEASPTRP
10   THRTHRSERGLYTHR

Samples:

CN-sample: Methyl-CpG-binding domain-containing protein 11, [U-13C; U-15N], mM; DTT 1 mM; sodium chloride 150 mM; TRIS 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 8.5; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCN-sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticCN-sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticCN-sampleisotropicsample_conditions_1
3D HNCOCN-sampleisotropicsample_conditions_1
3D HNCACN-sampleisotropicsample_conditions_1
3D C(CO)NHCN-sampleisotropicsample_conditions_1
3D HBHA(CO)NHCN-sampleisotropicsample_conditions_1
3D CBCA(CO)NHCN-sampleisotropicsample_conditions_1
3D HNCACBCN-sampleisotropicsample_conditions_1
3D HN(CO)CACN-sampleisotropicsample_conditions_1
3D 13C_NOESY_aliCN-sampleisotropicsample_conditions_1
3D 15N_NOESYCN-sampleisotropicsample_conditions_1
3D H(CCO)NHCN-sampleisotropicsample_conditions_1
3D 13C_NOESY_aroCN-sampleisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

Sparky, Goddard - peak picking

TopSpin v3.5, Bruker Biospin - collection

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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