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 10125

Title: Solution structure of the dsRBD from hypothetical protein BAB26260

Deposition date: 2007-04-02 Original release date: 2008-09-02

Authors: Nagata, T.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.

Citation: Nagata, T.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the dsRBD from hypothetical protein BAB26260"  .

Assembly members:
double-stranded RNA binding domain, polymer, 128 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: P021209-40

Entity Sequences (FASTA):
double-stranded RNA binding domain: GSSGSSGSGIIKMAIRFDRR AYPPQITPKMCLLEWCRREK LPQPVYETVQRTIDRMFCSV VTVAEQKYQSTLWDKSKKLA EQTAAIVCLRSQGLPEGRLG EESPSLNKRKREAPDQDPGG PRSGPSSG

Data sets:
Data typeCount
13C chemical shifts547
15N chemical shifts124
1H chemical shifts857

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein RIKEN cDNA 2310016K041

Entities:

Entity 1, hypothetical protein RIKEN cDNA 2310016K04 128 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERGLYILE
2   ILELYSMETALAILEARGPHEASPARGARG
3   ALATYRPROPROGLNILETHRPROLYSMET
4   CYSLEULEUGLUTRPCYSARGARGGLULYS
5   LEUPROGLNPROVALTYRGLUTHRVALGLN
6   ARGTHRILEASPARGMETPHECYSSERVAL
7   VALTHRVALALAGLUGLNLYSTYRGLNSER
8   THRLEUTRPASPLYSSERLYSLYSLEUALA
9   GLUGLNTHRALAALAILEVALCYSLEUARG
10   SERGLNGLYLEUPROGLUGLYARGLEUGLY
11   GLUGLUSERPROSERLEUASNLYSARGLYS
12   ARGGLUALAPROASPGLNASPPROGLYGLY
13   PROARGSERGLYPROSERSERGLY

Samples:

sample_1: double-stranded RNA binding domain, [U-13C; U-15N], 1.28 mM; phosphate 20 mM; NaCl 100 mM; DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRView v5.0.4, Johnson - data analysis

CYANA v2.0, Guntert, P. - refinement, structure solution

NMRPipe v2.3, Delaglio, F. - processing

Kujira v0.901, Kobayashi, N. - data analysis

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB26260
GB AAH58431 AAI16935 AAI16937 EDL11340 EDL11341
REF NP_001288105 NP_079794 XP_006531341 XP_006986898
SP Q9D7B1
AlphaFold Q9D7B1

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