BMRB Entry 34475

Title:
LEDGF/p75 dimer (residues 345-467)
Deposition date:
2020-01-10
Original release date:
2020-09-07
Authors:
Lux, V.; Veverka, V.
Citation:

Citation: Lux, Vanda; Brouns, Tine; Cermakova, Katerina; Srb, Pavel; Fabry, Milan; Madlikova, Marcela; Horejsi, Magdalena; Kukacka, Zdenek; Novak, Petr; Kugler, Michael; Brynda, Jiri; DeRijck, Jan; Christ, Frauke; Debyser, Zeger; Veverka, Vaclav. "Molecular Mechanism of LEDGF/p75 Dimerization"  Structure ., .-. (2020).
PubMed: 32946742

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, 14644.854 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 shifts549
15N chemical shifts130
1H chemical shifts882

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21

Entities:

Entity 1, unit_1 128 residues - 14644.854 Da.

1   SERASNALAALASERGLUTHRSERMETASP
2   SERARGLEUGLNARGILEHISALAGLUILE
3   LYSASNSERLEULYSILEASPASNLEUASP
4   VALASNARGCYSILEGLUALALEUASPGLU
5   LEUALASERLEUGLNVALTHRMETGLNGLN
6   ALAGLNLYSHISTHRGLUMETILETHRTHR
7   LEULYSLYSILEARGARGPHELYSVALSER
8   GLNVALILEMETGLULYSSERTHRMETLEU
9   TYRASNLYSPHELYSASNMETPHELEUVAL
10   GLYGLUGLYASPSERVALILETHRGLNVAL
11   LEUASNLYSSERLEUALAGLUGLNARGGLN
12   HISGLUGLUALAASNLYSTHRLYSASPGLN
13   GLYLYSLYSGLYPROASNLYSLYS

Samples:

sample_1: LEDGF, [U-13C; U-15N], 0.5 mM; HEPES 20 mM; sodium chloride 100 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

Sparky, Goddard - data analysis

TopSpin, Bruker Biospin - collection, processing

NMR spectrometers:

  • 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