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 11319

Title: Solution Structure of the zinc finger BED domain of the zinc finger BED domain containing protein 1

Deposition date: 2010-08-10 Original release date: 2011-08-19

Authors: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the zinc finger BED domain of the zinc finger BED domain containing protein 1"  .

Assembly members:
zinc finger BED domain, polymer, 73 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040308-29

Entity Sequences (FASTA):
zinc finger BED domain: GSSGSSGSKVWKYFGFDTNA EGCILQWKKIYCRICMAQIA YSGNTSNLSYHLEKNHPEEF CEFVKSNSGPSSG

Data sets:
Data typeCount
13C chemical shifts290
15N chemical shifts66
1H chemical shifts433

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc finger BED domain1
2ZINC ION2

Entities:

Entity 1, zinc finger BED domain 73 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERLYSVAL
2   TRPLYSTYRPHEGLYPHEASPTHRASNALA
3   GLUGLYCYSILELEUGLNTRPLYSLYSILE
4   TYRCYSARGILECYSMETALAGLNILEALA
5   TYRSERGLYASNTHRSERASNLEUSERTYR
6   HISLEUGLULYSASNHISPROGLUGLUPHE
7   CYSGLUPHEVALLYSSERASNSERGLYPRO
8   SERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc finger BED domain, [U-13C; U-15N], 1.09 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.01 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.925, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA34505 BAG09847
EMBL CAA76545 CAA76660
GB AAH15030 ABM84566 ABM86530 AIC55542 EAW98691
REF NP_001164606 NP_001164607 NP_001253637 NP_004720 XP_002831388
SP O96006
AlphaFold O96006

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