BMRB Entry 30602

Title:
NMR Structure of Branched K11/K48-Linked Tri-Ubiquitin
Deposition date:
2019-04-25
Original release date:
2019-10-15
Authors:
Boughton, A.; Fushman, D.
Citation:

Citation: Boughton, A.; Krueger, S.; Fushman, D.. "Branching via K11 and K48 Bestows Ubiquitin Chains with a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1"  Structure 28, 29-43 (2020).
PubMed: 31677892

Assembly members:

Assembly members:
entity_1, polymer, 76 residues, 8660.873 Da.
entity_2, polymer, 76 residues, 8604.845 Da.
entity_3, polymer, 77 residues, 8691.918 Da.

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

Data sets:
Data typeCount
15N chemical shifts140
1H chemical shifts140

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_33

Entities:

Entity 1, entity_1 76 residues - 8660.873 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   ARGTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYARGGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNARGGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Entity 2, entity_2 76 residues - 8604.845 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYARGGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Entity 3, entity_3 77 residues - 8691.918 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLYASP

Samples:

sample_1: entity_1, [U-15N-distal11], 120 uM; entity_2, [U-15N-distal11], 120 uM; entity_3, [U-15N-distal11], 120 uM

sample_2: entity_1, [U-15N-distal48], 100 uM; entity_2, [U-15N-distal48], 100 uM; entity_3, [U-15N-distal48], 100 uM

sample_3: entity_1, [U-15N-distal11], 60 uM; entity_2, [U-15N-distal11], 60 uM; entity_3, [U-15N-distal11], 60 uM

sample_4: entity_1, [U-15N-distal48], 110 uM; entity_2, [U-15N-distal48], 110 uM; entity_3, [U-15N-distal48], 110 uM

sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

Sparky, Goddard - peak picking

HADDOCK, Bonvin - refinement, structure calculation

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 600 MHz

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