BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 10294

Title: Solution structure of the homeobox domain of Homeobox protein OTX2

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

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

Citation: Ohnishi, S.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the homeobox domain of Homeobox protein OTX2"  .

Assembly members:
homeobox domain, polymer, 80 residues, Formula weight is not available

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis   Vector: P050711-11

Entity Sequences (FASTA):
homeobox domain: GSSGSSGRRERTTFTRAQLD VLEALFAKTRYPDIFMREEV ALKINLPESRVQVWFKNRRA KCRQQQQQQQNGGQSGPSSG

Data sets:
Data typeCount
13C chemical shifts292
15N chemical shifts66
1H chemical shifts436

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1homeobox domain1

Entities:

Entity 1, homeobox domain 80 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGARGGLU
2   ARGTHRTHRPHETHRARGALAGLNLEUASP
3   VALLEUGLUALALEUPHEALALYSTHRARG
4   TYRPROASPILEPHEMETARGGLUGLUVAL
5   ALALEULYSILEASNLEUPROGLUSERARG
6   VALGLNVALTRPPHELYSASNARGARGALA
7   LYSCYSARGGLNGLNGLNGLNGLNGLNGLN
8   ASNGLYGLYGLNSERGLYPROSERSERGLY

Samples:

sample_1: homeobox domain, [U-13C; U-15N], 1.0 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 v0.965, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA05159 BAB16104 BAB62171 BAC02578 BAC02579
EMBL CAA04396 CAA87093 CAD32962 CAG00311 CAG10588
GB AAA78901 AAA85388 AAB27580 AAB63527 AAD31385
PIR S39407
REF NP_001016021 NP_001016177 NP_001084160 NP_001084955 NP_001094036
SP P32242 P32243 P80206 Q28EM7 Q28FN6
TPG DAA24647 DAA25273 DAA25274
AlphaFold Q28EM7 P32242 P32243 P80206 Q28FN6

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