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 10287

Title: Solution structure of the second homeobox domain of Zinc fingers and homeoboxes protein 3 (Triple homeobox 1 protein)

Deposition date: 2008-12-17 Original release date: 2009-12-17

Authors: Ohnishi, S.; Kigawa, T.; Saito, K.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation: Ohnishi, S.; Kigawa, T.; Saito, K.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the second homeobox domain of Zinc fingers and homeoboxes protein 3 (Triple homeobox 1 protein)"  .

Assembly members:
The second homeobox domain, polymer, 75 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Vector: P050404-23

Entity Sequences (FASTA):
The second homeobox domain: GSSGSSGPTKYKERAPEQLR ALESSFAQNPLPLDEELDRL RSETKMTRREIDSWFSERRK KVNAEETKKSGPSSG

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts69
1H chemical shifts470

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1The second homeobox domain1

Entities:

Entity 1, The second homeobox domain 75 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROTHRLYS
2   TYRLYSGLUARGALAPROGLUGLNLEUARG
3   ALALEUGLUSERSERPHEALAGLNASNPRO
4   LEUPROLEUASPGLUGLULEUASPARGLEU
5   ARGSERGLUTHRLYSMETTHRARGARGGLU
6   ILEASPSERTRPPHESERGLUARGARGLYS
7   LYSVALASNALAGLUGLUTHRLYSLYSSER
8   GLYPROSERSERGLY

Samples:

sample_1: The second homeobox domain, [U-13C; U-15N], 1.2 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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