BMRB Entry 27300

Title:
Backbone HN, N, CA, and CB assignment of human UBC9_P123L
Deposition date:
2017-11-02
Original release date:
2019-01-10
Authors:
Placzek, William
Citation:

Citation: Wright, Christine; Whitaker, Robert; Onuiri, Joshua; Blackburn, Tessa; McGarity, Sierra; Bjornsti, Mary-Ann; Placzek, William. "UBC9 mutant reveals the impact of protein dynamics on substrate selectivity and SUMO chain linkages"  Biochemistry 58, 621-632 (2019).
PubMed: 30574775

Assembly members:

Assembly members:
UBC9(P123L), polymer, 178 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: pET28b

Data sets:
Data typeCount
13C chemical shifts295
15N chemical shifts129
1H chemical shifts129

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBC9_P123L monomer1

Entities:

Entity 1, UBC9_P123L monomer 178 residues - Formula weight is not available

Residues -19 to 0 are part of the His tag and were not assigned, 1 corresponds with the native residue M1.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERGLYILEALALEUSERARGLEUALA
4   GLNGLUARGLYSALATRPARGLYSASPHIS
5   PROPHEGLYPHEVALALAVALPROTHRLYS
6   ASNPROASPGLYTHRMETASNLEUMETASN
7   TRPGLUCYSALAILEPROGLYLYSLYSGLY
8   THRPROTRPGLUGLYGLYLEUPHELYSLEU
9   ARGMETLEUPHELYSASPASPTYRPROSER
10   SERPROPROLYSCYSLYSPHEGLUPROPRO
11   LEUPHEHISPROASNVALTYRPROSERGLY
12   THRVALCYSLEUSERILELEUGLUGLUASP
13   LYSASPTRPARGPROALAILETHRILELYS
14   GLNILELEULEUGLYILEGLNGLULEULEU
15   ASNGLULEUASNILEGLNASPPROALAGLN
16   ALAGLUALATYRTHRILETYRCYSGLNASN
17   ARGVALGLUTYRGLULYSARGVALARGALA
18   GLNALALYSLYSPHEALAPROSER

Samples:

sample_1: UBC9(P123L), [U-99% 13C; U-99% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 120 mM; D2O 5%; Glutamic acid 10 mM

sample_conditions_1: ionic strength: 0.14 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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