BMRB Entry 25639

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25639
MolProbity Validation Chart

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Title:
Solution structure of LEDGF/p75 IBD in complex with POGZ peptide (1389-1404)
Deposition date:
2015-05-26
Original release date:
2015-08-17
Authors:
Tesina, Petr; Cermakova, Katerina; Horejsi, Magdalena; Prochazkova, Katerina; Fabry, Milan; Sharma, Subhalakshmi; Christ, Frauke; Demeulemeester, Jonas; Debyser, Zeger; De Rijck, Jan; Veverka, Vaclav; Rezacova, Pavlina
Citation:

Citation: Tesina, P.; Cermakova, K.; Horejsi, M.; Prochazkova, K.; Fabry, M.; Sharma, S.; Christ, F.; Demeulemeester, J.; Debyser, Z.; Rijck, J.D.; Veverka, V.; Rezacova, P.. "Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif"  Nat. Commun. 6, 7968-7968 (2015).
PubMed: 26245978

Assembly members:

Assembly members:
entity_1, polymer, 16 residues, 1825.766 Da.
entity_2, polymer, 79 residues, 9355.110 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: chemical synthesis   Vector: n/a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: EGESETESFYGFEEAD
entity_2: MDSRLQRIHAEIKNSLKIDN LDVNRCIEALDELASLQVTM QQAQKHTEMITTLKKIRRFK VSQVIMEKSTMLYNKFKNM

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts81
1H chemical shifts610

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 16 residues - 1825.766 Da.

1   GLUGLYGLUSERGLUTHRGLUSERPHETYR
2   GLYPHEGLUGLUALAASP

Entity 2, entity_2 79 residues - 9355.110 Da.

1   METASPSERARGLEUGLNARGILEHISALA
2   GLUILELYSASNSERLEULYSILEASPASN
3   LEUASPVALASNARGCYSILEGLUALALEU
4   ASPGLULEUALASERLEUGLNVALTHRMET
5   GLNGLNALAGLNLYSHISTHRGLUMETILE
6   THRTHRLEULYSLYSILEARGARGPHELYS
7   VALSERGLNVALILEMETGLULYSSERTHR
8   METLEUTYRASNLYSPHELYSASNMET

Samples:

sample_1: entity_1 0.5 mM; entity_2, [U-13C; U-15N], 0.5 mM; HEPES 25 mM; NaCl 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 125 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, YASARA - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA32306 BAC27169 BAC29003 BAC65570 BAE36623
EMBL CAD97850 CAL37797
GB AAH32176 AAH85188 AAH96492 AAI39433 AAI39434
REF NP_001101163 NP_001156662 NP_001159420 NP_001162545 NP_001181866
SP Q7Z3K3 Q8BZH4
TPG DAA31680
AlphaFold Q7Z3K3 Q8BZH4 Q9UER6

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