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 25130

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25130
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution structure of LEDGF/p75 IBD in complex with MLL1 peptide (140-160)   PubMed: 25082813

Deposition date: 2014-08-05 Original release date: 2014-08-25

Authors: Cermakova, Katerina; Tesina, Petr; Demeulemeester, Jonas; El Ashkar, Sara; Mereau, Helene; Schwaller, Juerg; Rezacova, Pavlina; Veverka, Vaclav; De Rijck, Jan

Citation: Cermakova, Katerina; Tesina, Petr; Demeulemeester, Jonas; El Ashkar, Sara; Mereau, Helene; Schwaller, Juerg; Rezacova, Pavlina; Veverka, Vaclav; De Rijck, Jan. "Validation and Structural Characterization of the LEDGF/p75-MLL Interface as a New Target for the Treatment of MLL-Dependent Leukemia."  Cancer Res. 74, 5139-5151 (2014).

Assembly members:
MLL1_140-160, polymer, 21 residues, 2272.364 Da.
IBD, polymer, 88 residues, 10260.019 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
MLL1_140-160: GGSGEDEQFLGFGSDEEVRV R
IBD: SNAASRETSMDSRLQRIHAE IKNSLKIDNLDVNRCIEALD ELASLQVTMQQAQKHTEMIT TLKKIRRFKVSQVIMEKSTM LYNKFKNM

Data sets:
Data typeCount
1H chemical shifts734
13C chemical shifts372
15N chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MLL1 peptide (140-160)1
2LEDGF/p75 IBD2

Entities:

Entity 1, MLL1 peptide (140-160) 21 residues - 2272.364 Da.

1   GLYGLYSERGLYGLUASPGLUGLNPHELEU
2   GLYPHEGLYSERASPGLUGLUVALARGVAL
3   ARG

Entity 2, LEDGF/p75 IBD 88 residues - 10260.019 Da.

1   SERASNALAALASERARGGLUTHRSERMET
2   ASPSERARGLEUGLNARGILEHISALAGLU
3   ILELYSASNSERLEULYSILEASPASNLEU
4   ASPVALASNARGCYSILEGLUALALEUASP
5   GLULEUALASERLEUGLNVALTHRMETGLN
6   GLNALAGLNLYSHISTHRGLUMETILETHR
7   THRLEULYSLYSILEARGARGPHELYSVAL
8   SERGLNVALILEMETGLULYSSERTHRMET
9   LEUTYRASNLYSPHELYSASNMET

Samples:

sample_1: MLL1_140-160 0.5 mM; IBD, [U-13C; U-15N], 0.5 mM; HEPES 25 mM; sodium chloride 100 mM; beta-mercaptoethanol 0.05%

sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 125 mM

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-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, YASARA - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA03407 BAJ78791 BAK63380
EMBL CAA93625 CAC34944
GB AAA58669 AAA62593 AAC37520 AAC95283 AAC95284 AAB52589 AAC25167 AAC97946 AAF25870 AAH02260
PIR A48205
PRF 1919460A
REF NP_001074518 NP_001184033 NP_005924 XP_001093874 XP_003253537 NP_001009372 NP_001075982 NP_001121689 NP_001137364 NP_001193405
SP P55200 Q03164 O75475 Q66T72 Q812D1 Q8MJG1 Q99JF8
TPG DAA22311 DAA26946
BMRB 25171

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