BMRB Entry 26529

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26529

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
WHB in complex with UBCH10
Deposition date:
2015-03-03
Original release date:
2015-06-17
Authors:
Royappa, Grace; Brown, Nicholas
Citation:

Citation: Brown, Nicholas; VanderLinden, Ryan; Watson, Edmond; Qiao, Renping; Grace, Christy; Yamaguchi, Masaya; Weissmann, Florian; Frye, Jeremiah; Dube, Prakash; Cho, Shein; Actis, Marcelo; Rodrigues, Patrick; Fujii, Naoaki; Peters, Jan-Michael; Stark, Holger; Schulman, Brenda. "RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex"  Proc. Natl. Acad. Sci. U. S. A. 17, 5272-5279 (2015).
PubMed: 25825779

Assembly members:

Assembly members:
Molecule_4, polymer, 90 residues, Formula weight is not available
Molecule_5, polymer, 187 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PRSF1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Molecule_4: GSESDSGMASQADQKEEELL LFWTYIQAMLTNLESLSLDR IYNMLRMFVVTGPALAEIDL QELQGYLQKKVRDQQLVYSA GVYRLPKNCS
Molecule_5: MASQNRDPAATSVAAARKGA EPSGGGARGPVGKRLQQELM TLMMSGDKGISAFPESDNLF KWVGTIHGAAGTVYEDLRYK LSLEFPSGYPYNAPTVKFLT PCYHPNVDTQGNISLDILKE KWSALYDVRTILLSIQSLLG EPNIDSPLNTHAAELWKNPT AFKKYLQETYSKQVTSQEPG SHHHHHH

Data sets:
Data typeCount
13C chemical shifts227
15N chemical shifts85
1H chemical shifts85

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Molecule_41
2UB2

Entities:

Entity 1, Molecule_4 90 residues - Formula weight is not available

1   GLYSERGLUSERASPSERGLYMETALASER
2   GLNALAASPGLNLYSGLUGLUGLULEULEU
3   LEUPHETRPTHRTYRILEGLNALAMETLEU
4   THRASNLEUGLUSERLEUSERLEUASPARG
5   ILETYRASNMETLEUARGMETPHEVALVAL
6   THRGLYPROALALEUALAGLUILEASPLEU
7   GLNGLULEUGLNGLYTYRLEUGLNLYSLYS
8   VALARGASPGLNGLNLEUVALTYRSERALA
9   GLYVALTYRARGLEUPROLYSASNCYSSER

Entity 2, UB 187 residues - Formula weight is not available

1   METALASERGLNASNARGASPPROALAALA
2   THRSERVALALAALAALAARGLYSGLYALA
3   GLUPROSERGLYGLYGLYALAARGGLYPRO
4   VALGLYLYSARGLEUGLNGLNGLULEUMET
5   THRLEUMETMETSERGLYASPLYSGLYILE
6   SERALAPHEPROGLUSERASPASNLEUPHE
7   LYSTRPVALGLYTHRILEHISGLYALAALA
8   GLYTHRVALTYRGLUASPLEUARGTYRLYS
9   LEUSERLEUGLUPHEPROSERGLYTYRPRO
10   TYRASNALAPROTHRVALLYSPHELEUTHR
11   PROCYSTYRHISPROASNVALASPTHRGLN
12   GLYASNILESERLEUASPILELEULYSGLU
13   LYSTRPSERALALEUTYRASPVALARGTHR
14   ILELEULEUSERILEGLNSERLEULEUGLY
15   GLUPROASNILEASPSERPROLEUASNTHR
16   HISALAALAGLULEUTRPLYSASNPROTHR
17   ALAPHELYSLYSTYRLEUGLNGLUTHRTYR
18   SERLYSGLNVALTHRSERGLNGLUPROGLY
19   SERHISHISHISHISHISHIS

Samples:

sample_1: Molecule_4, [U-100% 13C; U-100% 15N], 0.5 mM; Molecule_5 0.6 mM; DTT 0.01 mM; sodium chloride 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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