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 11258

Title: Solution Structure of Mouse Hypothetical Protein 2900073H19RIK

Deposition date: 2010-08-09 Original release date: 2011-08-17

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

Citation: Zhao, C.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of Mouse Hypothetical Protein 2900073H19RIK"  .

Assembly members:
ThiS domain, polymer, 114 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 10090   Superkingdom: Metazoa   Kingdom: Mus   Genus/species: musculus not available

Experimental source:   Production method: cell free synthesis' 'E. coli - cell free' 'E. coli

Entity Sequences (FASTA):
ThiS domain: GSSGSSGMAAPLCVKVEFGG GAELLFDGVKKHQVALPGQE EPWDIRNLLVWIKKNLLKER PELFIQGDSVRPGILVLIND ADWELLGELDYQLQDQDSIL FISTLHGGSGPSSG

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts110
1H chemical shifts763

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RIKEN cDNA 2900073H19 protein1

Entities:

Entity 1, RIKEN cDNA 2900073H19 protein 114 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETALAALA
2   PROLEUCYSVALLYSVALGLUPHEGLYGLY
3   GLYALAGLULEULEUPHEASPGLYVALLYS
4   LYSHISGLNVALALALEUPROGLYGLNGLU
5   GLUPROTRPASPILEARGASNLEULEUVAL
6   TRPILELYSLYSASNLEULEULYSGLUARG
7   PROGLULEUPHEILEGLNGLYASPSERVAL
8   ARGPROGLYILELEUVALLEUILEASNASP
9   ALAASPTRPGLULEULEUGLYGLULEUASP
10   TYRGLNLEUGLNASPGLNASPSERILELEU
11   PHEILESERTHRLEUHISGLYGLYSERGLY
12   PROSERSERGLY

Samples:

sample_1: ThiS domain mM; PiNa 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298.0 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, Delaglio, F. - processing

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

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB31673 BAC33621 BAC33956
GB AAH26994 AAI69094 EDL08423
REF NP_001131034 NP_080891 XP_001500842 XP_006154072 XP_006181951
SP Q9D2P4

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