BMRB Entry 19412

Title:
K11-linked Diubiquitin average solution structure at pH 6.8, 150 mM NaCl
Deposition date:
2013-08-03
Original release date:
2013-09-03
Authors:
Castaneda, Carlos; Fushman, David
Citation:

Citation: Castaneda, Carlos; Kashyap, Tanuja; Nakasone, Mark; Krueger, Susan; Fushman, David. "Unique structural, dynamical, and functional properties of K11-linked polyubiquitin chains"  Structure 21, 1168-1181 (2013).
PubMed: 23823328

Assembly members:

Assembly members:
entity, polymer, 152 residues, 8576.914 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   Vector: pet3a

Data sets:
Data typeCount
15N chemical shifts138
1H chemical shifts138

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1K11-linked Diubiquitin_11
2K11-linked Diubiquitin_21

Entities:

Entity 1, K11-linked Diubiquitin_1 152 residues - 8576.914 Da.

Residues 1-76 chain A are distal Ub residues, while residues 1-76 chain B are proximal Ub residues. K11 linkage occurs between K11 of chain B and G76 of chain A.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLYMETGLNILEPHE
9   VALLYSTHRLEUTHRGLYLYSTHRILETHR
10   LEUGLUVALGLUPROSERASPTHRILEGLU
11   ASNVALLYSALALYSILEGLNASPLYSGLU
12   GLYILEPROPROASPGLNGLNARGLEUILE
13   PHEALAGLYLYSGLNLEUGLUASPGLYARG
14   THRLEUSERASPTYRASNILEGLNLYSGLU
15   SERTHRLEUHISLEUVALLEUARGLEUARG
16   GLYGLY

Samples:

sample_1: entity, [U-99% 15N], 75 uM; sodium phosphate 20 mM; D2O 7%; H2O 93%; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_1anisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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