BMRB Entry 31192

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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/BMR31192
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
SET Domain of Histone-Lysine N-Methyltransferase NSD2 in Complex with Selective Inhibitor
Deposition date:
2024-07-29
Original release date:
2025-05-08
Authors:
Szczepski, K.; Jaremko, L.
Citation:

Citation: Szczepski, K.; Jaremko, L.. "Selective NSD2 Inhibition Reveals an Epigenetic Dependency of KRAS-Driven Cancers"  .

Assembly members:

Assembly members:
entity_1, polymer, 220 residues, 24987.518 Da.
entity_ZN, non-polymer, 65.409 Da.
entity_3, non-polymer, 513.545 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SERKPPPYKHIKVNKPYGKV QIYTADISEIPKCNCKPTDE NPCGFDSECLNRMLMFECHP QVCPAGEFCQNQCFTKRQYP ETKIIKTDGKGWGLVAKRDI RKGEFVNEYVGELIDEEECM ARIKHAHENDITHFYMLTID KDRIIDAGPKGNYSRFMNHS CQPNCETLKWTVNGDTRVGL FAVCDIPAGTELTFNYNLDC LGNEKTVCRCGASNCSGFLG

Data sets:
Data typeCount
13C chemical shifts410
15N chemical shifts189
1H chemical shifts189

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22
3unit_32
4unit_42
5unit_53

Entities:

Entity 1, unit_1 220 residues - 24987.518 Da.

1   SERGLUARGLYSPROPROPROTYRLYSHIS
2   ILELYSVALASNLYSPROTYRGLYLYSVAL
3   GLNILETYRTHRALAASPILESERGLUILE
4   PROLYSCYSASNCYSLYSPROTHRASPGLU
5   ASNPROCYSGLYPHEASPSERGLUCYSLEU
6   ASNARGMETLEUMETPHEGLUCYSHISPRO
7   GLNVALCYSPROALAGLYGLUPHECYSGLN
8   ASNGLNCYSPHETHRLYSARGGLNTYRPRO
9   GLUTHRLYSILEILELYSTHRASPGLYLYS
10   GLYTRPGLYLEUVALALALYSARGASPILE
11   ARGLYSGLYGLUPHEVALASNGLUTYRVAL
12   GLYGLULEUILEASPGLUGLUGLUCYSMET
13   ALAARGILELYSHISALAHISGLUASNASP
14   ILETHRHISPHETYRMETLEUTHRILEASP
15   LYSASPARGILEILEASPALAGLYPROLYS
16   GLYASNTYRSERARGPHEMETASNHISSER
17   CYSGLNPROASNCYSGLUTHRLEULYSTRP
18   THRVALASNGLYASPTHRARGVALGLYLEU
19   PHEALAVALCYSASPILEPROALAGLYTHR
20   GLULEUTHRPHEASNTYRASNLEUASPCYS
21   LEUGLYASNGLULYSTHRVALCYSARGCYS
22   GLYALASERASNCYSSERGLYPHELEUGLY

Entity 2, unit_2 - Zn - 65.409 Da.

1   ZN

Entity 3, unit_5 - 513.545 Da.

1   A1A0M

Samples:

sample_1: NSD2 SET domain, [U-2H; U-13C; U-15N; CH3 ILV], 200 uM; TRIS 50 mM; sodium chloride 150 mM; TCEP 1 mM; 17596 1 mM

sample_2: NSD2 SET domain, [U-13C; U-15N], 200 uM; TRIS 50 mM; sodium chloride 150 mM; TCEP 1 mM; 17596 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY filteredsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

Sparky, Goddard - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

HADDOCK, Bonvin - refinement

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz
  • Bruker AVANCE NEO 950 MHz

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