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 26972

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26972

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Title: Backbone resonance assignments for the SET domain of human methyltransferase NSD3   PubMed: 28808922

Deposition date: 2016-12-15 Original release date: 2017-08-23

Authors: Li, Yan; Ng, Hui Qi; Kang, CongBao

Citation: Li, Yan; Ng, Hui Qi; Ngo, Anna; Liu, Shuang; Tan, Yih Wan; Kwek, Perlyn Zekui; Hung, Alvin; Joy, Joma; Hill, Jeffrey; Keller, Thomas; Kang, CongBao. "Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor"  Biomol. NMR Assign. 11, 225-229 (2017).

Assembly members:
SET_domain_of_human_methyltransferase_NSD3, polymer, 258 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: pET29b

Entity Sequences (FASTA):
SET_domain_of_human_methyltransferase_NSD3: MQELKAQRESKEALEIEKNS RKPPPYKHIKANKVIGKVQI QVADLSEIPRCNCKPADENP CGLESECLNRMLQYECHPQV CPAGDRCQNQCFTKRLYPDA EIIKTERRGWGLRTKRSIKK GEFVNEYVGELIDEEECRLR IKRAHENSVTNFYMLTVTKD RIIDAGPKGNYSRFMNHSCN PNCETQKWTVNGDVRVGLFA LCDIPAGMELTFNYNLDCLG NGRTECHCGADNCSGFLGVR PKSACASTNEEKHHHHHH

Data sets:
Data typeCount
13C chemical shifts691
15N chemical shifts224
1H chemical shifts224

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SET domain of human methyltransferase NSD31

Entities:

Entity 1, SET domain of human methyltransferase NSD3 258 residues - Formula weight is not available

1   METGLNGLULEULYSALAGLNARGGLUSER
2   LYSGLUALALEUGLUILEGLULYSASNSER
3   ARGLYSPROPROPROTYRLYSHISILELYS
4   ALAASNLYSVALILEGLYLYSVALGLNILE
5   GLNVALALAASPLEUSERGLUILEPROARG
6   CYSASNCYSLYSPROALAASPGLUASNPRO
7   CYSGLYLEUGLUSERGLUCYSLEUASNARG
8   METLEUGLNTYRGLUCYSHISPROGLNVAL
9   CYSPROALAGLYASPARGCYSGLNASNGLN
10   CYSPHETHRLYSARGLEUTYRPROASPALA
11   GLUILEILELYSTHRGLUARGARGGLYTRP
12   GLYLEUARGTHRLYSARGSERILELYSLYS
13   GLYGLUPHEVALASNGLUTYRVALGLYGLU
14   LEUILEASPGLUGLUGLUCYSARGLEUARG
15   ILELYSARGALAHISGLUASNSERVALTHR
16   ASNPHETYRMETLEUTHRVALTHRLYSASP
17   ARGILEILEASPALAGLYPROLYSGLYASN
18   TYRSERARGPHEMETASNHISSERCYSASN
19   PROASNCYSGLUTHRGLNLYSTRPTHRVAL
20   ASNGLYASPVALARGVALGLYLEUPHEALA
21   LEUCYSASPILEPROALAGLYMETGLULEU
22   THRPHEASNTYRASNLEUASPCYSLEUGLY
23   ASNGLYARGTHRGLUCYSHISCYSGLYALA
24   ASPASNCYSSERGLYPHELEUGLYVALARG
25   PROLYSSERALACYSALASERTHRASNGLU
26   GLULYSHISHISHISHISHISHIS

Samples:

sample_1: SET domain of human methyltransferase NSD3, [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing

NMR spectrometers:

  • Bruker Avance 700 MHz

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