BMRB Entry 34181

Title:
Solution structure of the LEDGF/p75 IBD - MLL1 (aa 111-160) complex
Deposition date:
2017-10-03
Original release date:
2018-07-20
Authors:
Veverka, V.
Citation:

Citation: Sharma, S.; Cermakova, K.; De Rijck, J.; Demeulemeester, J.; Fabry, M.; El Ashkar, S.; Van Belle, S.; Lepsik, M.; Tesina, P.; Duchoslav, V.; Novak, P.; Hubalek, M.; Srb, P.; Christ, F.; Rezacova, P.; Hodges, H.; Debyser, Z.; Veverka, V.. "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation."  Proc. Natl. Acad. Sci. U.S.A. 115, E7053-E7062 (2018).
PubMed: 29997176

Assembly members:

Assembly members:
entity_1, polymer, 165 residues, 17963.201 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
13C chemical shifts627
15N chemical shifts159
1H chemical shifts1051

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 165 residues - 17963.201 Da.

1   SERASNALAALASERTRPGLUTHRSERMET
2   ASPSERARGLEUGLNARGILEHISALAGLU
3   ILELYSASNSERLEULYSILEASPASNLEU
4   ASPVALASNARGCYSILEGLUALALEUASP
5   GLULEUALASERLEUGLNVALTHRMETGLN
6   GLNALAGLNLYSHISTHRGLUMETILETHR
7   THRLEULYSLYSILEARGARGPHELYSVAL
8   SERGLNVALILEMETGLULYSSERTHRMET
9   LEUTYRASNLYSPHELYSASNMETPHELEU
10   VALGLYGLUGLYASPSERVALILETHRGLN
11   VALLEUASNLYSSERGLYGLYSERGLYSER
12   GLYSERGLYSERSERGLYPHEASPALAALA
13   LEUGLNVALSERALAALAILEGLYTHRASN
14   LEUARGARGPHEARGALAVALPHEGLYGLU
15   SERGLYGLYGLYGLYGLYSERGLYGLUASP
16   GLUGLNPHELEUGLYPHEGLYSERASPGLU
17   GLUVALARGVALARG

Samples:

sample_1: LEDGF/p75 IBD-MLL1, [U-13C; U-15N], 0.5 mM; TRIS 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

YASARA, KRIEGER - refinement

TOPSPIN - structure solution

SPARKY - structure solution

CYANA - structure solution

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

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