BMRB Entry 11389

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11389

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Title:
Solution structure of the ARID domain of JARID1D protein
Deposition date:
2010-09-08
Original release date:
2011-09-07
Authors:
Tanabe, W.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.
Citation:

Citation: Tanabe, W.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the ARID domain of JARID1D protein"  .

Assembly members:

Assembly members:
ARID domain, polymer, 100 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   Vector: P060731-15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ARID domain: GSSGSSGTRVKLNYLDQIAK FWEIQGSSLKIPNVERKILD LYSLSKIVIEEGGYEAICKD RRWARVAQRLHYPPGKNIGS LLRSHYERIIYPYEMFQSGA

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts95
1H chemical shifts702

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ARID domain1

Entities:

Entity 1, ARID domain 100 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRARGVAL
2   LYSLEUASNTYRLEUASPGLNILEALALYS
3   PHETRPGLUILEGLNGLYSERSERLEULYS
4   ILEPROASNVALGLUARGLYSILELEUASP
5   LEUTYRSERLEUSERLYSILEVALILEGLU
6   GLUGLYGLYTYRGLUALAILECYSLYSASP
7   ARGARGTRPALAARGVALALAGLNARGLEU
8   HISTYRPROPROGLYLYSASNILEGLYSER
9   LEULEUARGSERHISTYRGLUARGILEILE
10   TYRPROTYRGLUMETPHEGLNSERGLYALA

Samples:

sample_1: ARID domain mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20060702, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A - data analysis

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.1, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAG64942
EMBL CAH90475
GB AAC48699 AAC50806 AAC51135 AAG00951 AAI32722
REF NP_001008975 NP_001140177 NP_004644 XP_005262617 XP_005262618
SP Q5XUN4 Q9BY66
AlphaFold Q5XUN4 Q9BY66

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