BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34182

Title: Solution structure of the LEDGF/p75 IBD - IWS1 (aa 446-548) complex   PubMed: 29997176

Deposition date: 2017-10-03 Original release date: 2018-07-20

Authors: Veverka, V.

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).

Assembly members:
entity_1, polymer, 206 residues, 23837.502 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: SNAASWETSMDSRLQRIHAE IKNSLKIDNLDVNRCIEALD ELASLQVTMQQAQKHTEMIT TLKKIRRFKVSQVIMEKSTM LYNKFKNMFLVGEGDSVITQ VLNKELSDKKNEEKDLFGSD SESGNEEENLIADIFGESGD EEEEEFTGFNQEDLEEEKGE TQVKEAEDSDSDDNIKRGKH MDFLSDFEMMLQRKKSMSGK RRRNRD

Data sets:
Data typeCount
13C chemical shifts850
15N chemical shifts214
1H chemical shifts1343

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 206 residues - 23837.502 Da.

1   SERASNALAALASERTRPGLUTHRSERMET
2   ASPSERARGLEUGLNARGILEHISALAGLU
3   ILELYSASNSERLEULYSILEASPASNLEU
4   ASPVALASNARGCYSILEGLUALALEUASP
5   GLULEUALASERLEUGLNVALTHRMETGLN
6   GLNALAGLNLYSHISTHRGLUMETILETHR
7   THRLEULYSLYSILEARGARGPHELYSVAL
8   SERGLNVALILEMETGLULYSSERTHRMET
9   LEUTYRASNLYSPHELYSASNMETPHELEU
10   VALGLYGLUGLYASPSERVALILETHRGLN
11   VALLEUASNLYSGLULEUSERASPLYSLYS
12   ASNGLUGLULYSASPLEUPHEGLYSERASP
13   SERGLUSERGLYASNGLUGLUGLUASNLEU
14   ILEALAASPILEPHEGLYGLUSERGLYASP
15   GLUGLUGLUGLUGLUPHETHRGLYPHEASN
16   GLNGLUASPLEUGLUGLUGLULYSGLYGLU
17   THRGLNVALLYSGLUALAGLUASPSERASP
18   SERASPASPASNILELYSARGGLYLYSHIS
19   METASPPHELEUSERASPPHEGLUMETMET
20   LEUGLNARGLYSLYSSERMETSERGLYLYS
21   ARGARGARGASNARGASP

Samples:

sample_1: LEDGF/p75 IBD-IWS1, [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:

TOPSPIN - refinement

SPARKY - structure solution

CYANA - structure solution

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts