BMRB Entry 26528

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26528

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Title:
UBCH10 in complex with WHB
Deposition date:
2015-03-02
Original release date:
2015-06-17
Authors:
Grace, Christy; 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_3, polymer, 187 residues, Formula weight is not available
Molecule_1, polymer, 90 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_3: MASQNRDPAATSVAAARKGA EPSGGGARGPVGKRLQQELM TLMMSGDKGISAFPESDNLF KWVGTIHGAAGTVYEDLRYK LSLEFPSGYPYNAPTVKFLT PCYHPNVDTQGNISLDILKE KWSALYDVRTILLSIQSLLG EPNIDSPLNTHAAELWKNPT AFKKYLQETYSKQVTSQEPG SHHHHHH
Molecule_1: GSESDSGMASQADQKEEELL LFWTYIQAMLTNLESLSLDR IYNMLRMFVVTGPALAEIDL QELQGYLQKKVRDQQLVYSA GVYRLPKNCS

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts136
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Molecule_31
2WHB2

Entities:

Entity 1, Molecule_3 187 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

Entity 2, WHB 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

Samples:

sample_1: Molecule_3, [U-13C; U-15N; U-2H], 0.5 mM; Molecule_1 0.6 mM; DTT 0.01 mM; sodium chloride 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_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