BMRB Entry 26759

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26759

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Title:
Backbone resonance assignments for the SET domain of the human methyltransferase NSD2
Deposition date:
2016-03-17
Original release date:
2016-07-14
Authors:
Bobby, Romel; Peciak, Karolina; Milbradt, Alexander
Citation:

Citation: Bobby, Romel; Peciak, Karolina; Milbradt, Alexander. "Backbone resonance assignments for the SET domain of the human methyltransferase NSD2"  Biomol. NMR Assign. 10, 307-310 (2016).
PubMed: 27368234

Assembly members:

Assembly members:
NSD2_C16, polymer, 215 residues, 24308.6269 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   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NSD2_C16: GSYKHIKVNKPYGKVQIYTA DISEIPKCNCKPTDENPCGF DSECLNRMLMFECHPQVCPA GEFCQNQCFTKRQYPETKII KTDGKGWGLVAKRDIRKGEF VNEYVGELIDEEECMARIKH AHENDITHFYMLTIDKDRII DAGPKGNYSRFMNHSCQPNC ETLKWTVNGDTRVGLFAVCD IPAGTELTFNYNLDCLGNEK TVCRCGASNCSGFLG

Data sets:
Data typeCount
13C chemical shifts584
15N chemical shifts189
1H chemical shifts189

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NSD2 C161

Entities:

Entity 1, NSD2 C16 215 residues - 24308.6269 Da.

1   GLYSERTYRLYSHISILELYSVALASNLYS
2   PROTYRGLYLYSVALGLNILETYRTHRALA
3   ASPILESERGLUILEPROLYSCYSASNCYS
4   LYSPROTHRASPGLUASNPROCYSGLYPHE
5   ASPSERGLUCYSLEUASNARGMETLEUMET
6   PHEGLUCYSHISPROGLNVALCYSPROALA
7   GLYGLUPHECYSGLNASNGLNCYSPHETHR
8   LYSARGGLNTYRPROGLUTHRLYSILEILE
9   LYSTHRASPGLYLYSGLYTRPGLYLEUVAL
10   ALALYSARGASPILEARGLYSGLYGLUPHE
11   VALASNGLUTYRVALGLYGLULEUILEASP
12   GLUGLUGLUCYSMETALAARGILELYSHIS
13   ALAHISGLUASNASPILETHRHISPHETYR
14   METLEUTHRILEASPLYSASPARGILEILE
15   ASPALAGLYPROLYSGLYASNTYRSERARG
16   PHEMETASNHISSERCYSGLNPROASNCYS
17   GLUTHRLEULYSTRPTHRVALASNGLYASP
18   THRARGVALGLYLEUPHEALAVALCYSASP
19   ILEPROALAGLYTHRGLULEUTHRPHEASN
20   TYRASNLEUASPCYSLEUGLYASNGLULYS
21   THRVALCYSARGCYSGLYALASERASNCYS
22   SERGLYPHELEUGLY

Samples:

sample_1: NSD2_C16, [U-13C; U-15N; U-2H], 0.6 mM; SAM 1.2 mM; NaCl 100.0 mM; TCEP 1.0 mM; NaN3 1.0%

sample_conditions_1: ionic strength: 0.140 M; pH: 7.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
HNCOCACB (H[N[co[{CA|ca[C]}]]])sample_1isotropicsample_conditions_1
HNCOCA (H[N[co[{CA|ca[C]}]]])sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.1, CCPN - Spectrum display, Spectrum analysis

Topspin v3.2.5, Bruker Biospin - Spectrum acquisition, Spectrum display

nmrDraw vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum analysis, Spectrum display

nmrPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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