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 11306

Title: Solution Structure of the Ring-H2 Finger Domain of Mouse Deltex Protein 2

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

Authors: Miyamoto, K.; Muto, Y.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Miyamoto, K.; Muto, Y.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the Ring-H2 Finger Domain of Mouse Deltex Protein 2"  .

Assembly members:
Ring-H2 Finger Domain, polymer, 114 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P030421-37

Entity Sequences (FASTA):
Ring-H2 Finger Domain: GSSGSSGEPEQVIRKYTEEL KVAPEEDCIICMEKLAVASG YSDMTDSKALGPMVVGRLTK CSHAFHLLCLLAMYCNGNKD GSLQCPSCKTIYGEKTGTQP WGKMEVFRSGPSSG

Data sets:
Data typeCount
13C chemical shifts465
15N chemical shifts107
1H chemical shifts733

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ring-H2 Finger Domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, Ring-H2 Finger Domain 114 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUPROGLU
2   GLNVALILEARGLYSTYRTHRGLUGLULEU
3   LYSVALALAPROGLUGLUASPCYSILEILE
4   CYSMETGLULYSLEUALAVALALASERGLY
5   TYRSERASPMETTHRASPSERLYSALALEU
6   GLYPROMETVALVALGLYARGLEUTHRLYS
7   CYSSERHISALAPHEHISLEULEUCYSLEU
8   LEUALAMETTYRCYSASNGLYASNLYSASP
9   GLYSERLEUGLNCYSPROSERCYSLYSTHR
10   ILETYRGLYGLULYSTHRGLYTHRGLNPRO
11   TRPGLYLYSMETGLUVALPHEARGSERGLY
12   PROSERSERGLY

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

1   ZN

Samples:

sample_1: Ring-H2 Domain, [U-13C; U-15N], 1.05 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.1 mM; 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 v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.880, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB18940 BAB18941 BAB28055 BAC31780 BAC35781
GB AAI66738 EDL19332 EDL19333 EDL19334 EDL19335
REF NP_001100627 NP_001243025 NP_001243026 NP_001243027 NP_076231
SP Q8R3P2

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