BMRB Entry 11268

Title:
Solution Structure of the N-terminal Ubiquitin-like Domain in Mouse Ubiquitin-like Protein SB132
Deposition date:
2010-08-09
Original release date:
2011-08-18
Authors:
Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Ubiquitin-like Domain in Mouse Ubiquitin-like Protein SB132"  .

Assembly members:

Assembly members:
ubiquitin-like domain, polymer, 107 residues, Formula weight is not available

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: P050111-20

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts461
15N chemical shifts99
1H chemical shifts723

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin-like domain1

Entities:

Entity 1, ubiquitin-like domain 107 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETSERLEU
2   SERASPTRPHISLEUALAVALLYSLEUALA
3   ASPGLNPROLEUALAPROLYSSERILELEU
4   GLNLEUPROGLUTHRGLULEUGLYGLUTYR
5   SERLEUGLYGLYTYRSERILESERPHELEU
6   LYSGLNLEUILEALAGLYLYSLEUGLNGLU
7   SERVALPROASPPROGLULEUILEASPLEU
8   ILETYRCYSGLYARGLYSLEULYSASPASP
9   GLNTHRLEUASPPHETYRGLYILEGLNPRO
10   GLYSERTHRVALHISVALLEUARGLYSSER
11   TRPSERGLYPROSERSERGLY

Samples:

sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.35 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; 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 v0.921, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB26033 BAE32627
GB AAH16456 AAH79221 AAH94047 AAI12530 AAX08728
REF NP_001004247 NP_001015573 NP_001116345 NP_081362 XP_001135544
SP Q2KIS3 Q91W67
TPG DAA17515
AlphaFold Q2KIS3 Q91W67

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