BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50612

Title: NMR assignments of ARID4B Tudor domain   PubMed: 33675746

Deposition date: 2020-12-01 Original release date: 2021-05-28

Authors: Ren, Jie; Yao, Hongwei; Hu, Wanhui; Feng, Yingang; Perrett, Sarah; Gong, Weibin

Citation: Ren, Jie; Yao, Hongwei; Hu, Wanhui; Perrett, Sarah; Gong, Weibin; Feng, Yingang. "Structural basis for the DNA-binding activity of human ARID4B Tudor domain."  J. Biol. Chem. 296, 100506-100506 (2021).

Assembly members:
entity_1, polymer, 151 residues, 16880 Da.

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   Vector: pET28a

Entity Sequences (FASTA):
entity_1: MKALDEPPYLTVGTDVSAKY RGAFCEAKIKTAKRLVKVKV TFRHDSSTVEVQDDHIKGPL KVGAIVEVKNLDGAYQEAVI NKLTDASWYTVVFDDGDEKT LRRSSLCLKGERHFAESETL DQLPLTNPEHFGTPVIGKKT NRGRRSNHIPE

Data sets:
Data typeCount
13C chemical shifts629
15N chemical shifts150
1H chemical shifts995

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ARID4B Tudor domain1

Entities:

Entity 1, ARID4B Tudor domain 151 residues - 16880 Da.

Tudor domain and C-terminal extended disordered region of ARID4B

1   METLYSALALEUASPGLUPROPROTYRLEU
2   THRVALGLYTHRASPVALSERALALYSTYR
3   ARGGLYALAPHECYSGLUALALYSILELYS
4   THRALALYSARGLEUVALLYSVALLYSVAL
5   THRPHEARGHISASPSERSERTHRVALGLU
6   VALGLNASPASPHISILELYSGLYPROLEU
7   LYSVALGLYALAILEVALGLUVALLYSASN
8   LEUASPGLYALATYRGLNGLUALAVALILE
9   ASNLYSLEUTHRASPALASERTRPTYRTHR
10   VALVALPHEASPASPGLYASPGLULYSTHR
11   LEUARGARGSERSERLEUCYSLEULYSGLY
12   GLUARGHISPHEALAGLUSERGLUTHRLEU
13   ASPGLNLEUPROLEUTHRASNPROGLUHIS
14   PHEGLYTHRPROVALILEGLYLYSLYSTHR
15   ASNARGGLYARGARGSERASNHISILEPRO
16   GLU

Samples:

sample_1: ARID4B Tudor domain, [U-99% 13C; U-99% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; DTT 2 mM; EDTA 2 mM; DSS 0.02%; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.14 M; pH: 7; pressure: 1 atm; temperature: 302 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRViewJ - chemical shift assignment, data analysis

CYANA - structure solution

CNS - refinement

SANE - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP Q4LE39

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