BMRB Entry 11309

Title:
Solution structure of the N-terminal zinc finger domain of mouse cell growth regulating nucleolar protein LYAR
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Muto, Y.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Muto, Y.; Yokoyama, S.. "Solution structure of the N-terminal zinc finger domain of mouse cell growth regulating nucleolar protein LYAR"  .

Assembly members:

Assembly members:
Zinc finger DNA binding domain, polymer, 79 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P030421-25

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Zinc finger DNA binding domain: GSSGSSGMVFFTCNACGESV KKIQVEKHVSNCRNCECLSC IDCGKDFWGDDYKSHVKCIS EGQKYGGKGYEAKSGPSSG

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts72
1H chemical shifts452

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Zinc finger DNA binding domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, Zinc finger DNA binding domain 79 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETVALPHE
2   PHETHRCYSASNALACYSGLYGLUSERVAL
3   LYSLYSILEGLNVALGLULYSHISVALSER
4   ASNCYSARGASNCYSGLUCYSLEUSERCYS
5   ILEASPCYSGLYLYSASPPHETRPGLYASP
6   ASPTYRLYSSERHISVALLYSCYSILESER
7   GLUGLYGLNLYSTYRGLYGLYLYSGLYTYR
8   GLUALALYSSERGLYPROSERSERGLY

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc finger DNA binding domain, [U-13C; U-15N], 1 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 100 uM; H2O 90%; D2O 10%

condition_1: ionic strength: 220 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 v2.6, Bruker - collection

NMRPipe v20020425, Delagio, F. - processing

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

Kujira v0.896, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB24554 BAC36458
GB AAB26644 AAI16924 AAI16928 EDL37545 EDL37546
REF NP_079557 XP_006503822 XP_006503823 XP_006503824 XP_006503825
SP Q08288
AlphaFold Q08288

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