BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51794

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51794

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Title: Backbone resonance assignment of the LEDGF/p52 splice variant   PubMed: 37615563

Deposition date: 2023-01-23 Original release date: 2023-12-19

Authors: Koutna, E.; Veverka, V.

Citation: Koutna, Eliska; Lux, Vanda; Kouba, Tomas; Skerlova, Jana; Novacek, Jiri; Srb, Pavel; Hexnerova, Rozalie; Svachova, Hana; Kukacka, Zdenek; Novak, Petr; Fabry, Milan; Poepsel, Simon; Veverka, Vaclav. "Multivalency of nucleosome recognition by LEDGF"  Nucleic Acids Res. 51, 10011-10025 (2023).

Assembly members:
entity_1, polymer, 333 residues, Formula weight is not available

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   Vector: pET28

Entity Sequences (FASTA):
entity_1: MTRDFKPGDLIFAKMKGYPH WPARVDEVPDGAVKPPTNKL PIFFFGTHETAFLGPKDIFP YSENKEKYGKPNKRKGFNEG LWEIDNNPKVKFSSQQAATK QSNASSDVEVEEKETSVSKE DTDHEEKASNEDVTKAVDIT TPKAARRGRKRKAEKQVETE EAGVVTTATASVNLKVSPKR GRPAATEVKIPKPRGRPKMV KQPCPSESDIITEEDKSKKK GQEEKQPKKQPKKDEEGQKE EDKPRKEPDKKEGKKEVESK RKNLAKTGVTSTSDSEEEGD DQEGEKKRKGGRNFQTAHRR NMLKGQHEKEAADRKRKQEE QMETEHQTTCNLQ

Data sets:
Data typeCount
13C chemical shifts883
15N chemical shifts276
1H chemical shifts276

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PC4 and SFRS1-interacting protein1

Entities:

Entity 1, PC4 and SFRS1-interacting protein 333 residues - Formula weight is not available

1   METTHRARGASPPHELYSPROGLYASPLEU
2   ILEPHEALALYSMETLYSGLYTYRPROHIS
3   TRPPROALAARGVALASPGLUVALPROASP
4   GLYALAVALLYSPROPROTHRASNLYSLEU
5   PROILEPHEPHEPHEGLYTHRHISGLUTHR
6   ALAPHELEUGLYPROLYSASPILEPHEPRO
7   TYRSERGLUASNLYSGLULYSTYRGLYLYS
8   PROASNLYSARGLYSGLYPHEASNGLUGLY
9   LEUTRPGLUILEASPASNASNPROLYSVAL
10   LYSPHESERSERGLNGLNALAALATHRLYS
11   GLNSERASNALASERSERASPVALGLUVAL
12   GLUGLULYSGLUTHRSERVALSERLYSGLU
13   ASPTHRASPHISGLUGLULYSALASERASN
14   GLUASPVALTHRLYSALAVALASPILETHR
15   THRPROLYSALAALAARGARGGLYARGLYS
16   ARGLYSALAGLULYSGLNVALGLUTHRGLU
17   GLUALAGLYVALVALTHRTHRALATHRALA
18   SERVALASNLEULYSVALSERPROLYSARG
19   GLYARGPROALAALATHRGLUVALLYSILE
20   PROLYSPROARGGLYARGPROLYSMETVAL
21   LYSGLNPROCYSPROSERGLUSERASPILE
22   ILETHRGLUGLUASPLYSSERLYSLYSLYS
23   GLYGLNGLUGLULYSGLNPROLYSLYSGLN
24   PROLYSLYSASPGLUGLUGLYGLNLYSGLU
25   GLUASPLYSPROARGLYSGLUPROASPLYS
26   LYSGLUGLYLYSLYSGLUVALGLUSERLYS
27   ARGLYSASNLEUALALYSTHRGLYVALTHR
28   SERTHRSERASPSERGLUGLUGLUGLYASP
29   ASPGLNGLUGLYGLULYSLYSARGLYSGLY
30   GLYARGASNPHEGLNTHRALAHISARGARG
31   ASNMETLEULYSGLYGLNHISGLULYSGLU
32   ALAALAASPARGLYSARGLYSGLNGLUGLU
33   GLNMETGLUTHRGLUHISGLNTHRTHRCYS
34   ASNLEUGLN

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

Software:

SPARKY - data analysis

TOPSPIN - collection, processing

NMR spectrometers:

  • Bruker Avance 850 MHz

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