BMRB Entry 31105

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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/BMR31105
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of TET3/MLL4-PHD6
Deposition date:
2023-09-06
Original release date:
2024-06-20
Authors:
Mohid, S.; Zandian, M.; Zhang, Y.; Kutateladze, T.
Citation:

Citation: Becht, Dustin; Mohid, Sk Abdul; Lee, Ji-Eun; Zandian, Mohamad; Benz, Caroline; Biswas, Soumi; Sinha, Vikrant Kumar; Ivarsson, Ylva; Ge, Kai; Zhang, Yi; Kutateladze, Tatiana. "MLL4 binds TET3"  Structure 32, 706-714 (2024).
PubMed: 38579707

Assembly members:

Assembly members:
entity_1, polymer, 9 residues, 864.945 Da.
entity_2, polymer, 60 residues, 6826.676 Da.
entity_ZN, non-polymer, 65.409 Da.

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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GVGGSWGVF
entity_2: SLVTCPICHAPYVEEDLLIQ CRHCERWMHAGCESLFTEDD VEQAADEGFDCVSCQPYVVK

Data sets:
Data typeCount
13C chemical shifts246
15N chemical shifts68
1H chemical shifts355

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22
3unit_33
4unit_43

Entities:

Entity 1, unit_1 9 residues - 864.945 Da.

1   GLYVALGLYGLYSERTRPGLYVALPHE

Entity 2, unit_2 60 residues - 6826.676 Da.

1   SERLEUVALTHRCYSPROILECYSHISALA
2   PROTYRVALGLUGLUASPLEULEUILEGLN
3   CYSARGHISCYSGLUARGTRPMETHISALA
4   GLYCYSGLUSERLEUPHETHRGLUASPASP
5   VALGLUGLNALAALAASPGLUGLYPHEASP
6   CYSVALSERCYSGLNPROTYRVALVALLYS

Entity 3, unit_3 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Protein, [U-13C; U-15N], 2.0 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

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