BMRB Entry 26767

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26767

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Title:
Backbone 1H, 15N and 13C assignments of the catalytic domain of human NSD1
Deposition date:
2016-03-23
Original release date:
2016-04-22
Authors:
Amin, Nader; Nietlispach, Daniel; Coyle, Joe; Williams, Glyn; Chiarparin, Elisabetta
Citation:

Citation: Amin, Nader; Nietlispach, Daniel; Qamar, Seema; Coyle, Joe; Chiarparin, Elisabetta; Williams, Glyn. "NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2"  Biomol. NMR Assign. 10, 315-320 (2016).
PubMed: 27356987

Assembly members:

Assembly members:
NSD1, polymer, 232 residues, Formula weight is not available

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: pET23b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NSD1: MKELRQLQEDRKNDKKPPPY KHIKVNRPIGRVQIFTADLS EIPRCNCKATDENPCGIDSE CINRMLLYECHPTVCPAGGR CQNQCFSKRQYPEVEIFRTL QRGWGLRTKTDIKKGEFVNE YVGELIDEEECRARIRYAQE HDITNFYMLTLDKDRIIDAG PKGNYARFMNHCCQPNCETQ KWSVNGDTRVGLFALSDIKA GTELTFNYNLECLGNGKTVC KCGAPNCSGFLG

Data sets:
Data typeCount
13C chemical shifts612
15N chemical shifts212
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NSD11

Entities:

Entity 1, NSD1 232 residues - Formula weight is not available

1   METLYSGLULEUARGGLNLEUGLNGLUASP
2   ARGLYSASNASPLYSLYSPROPROPROTYR
3   LYSHISILELYSVALASNARGPROILEGLY
4   ARGVALGLNILEPHETHRALAASPLEUSER
5   GLUILEPROARGCYSASNCYSLYSALATHR
6   ASPGLUASNPROCYSGLYILEASPSERGLU
7   CYSILEASNARGMETLEULEUTYRGLUCYS
8   HISPROTHRVALCYSPROALAGLYGLYARG
9   CYSGLNASNGLNCYSPHESERLYSARGGLN
10   TYRPROGLUVALGLUILEPHEARGTHRLEU
11   GLNARGGLYTRPGLYLEUARGTHRLYSTHR
12   ASPILELYSLYSGLYGLUPHEVALASNGLU
13   TYRVALGLYGLULEUILEASPGLUGLUGLU
14   CYSARGALAARGILEARGTYRALAGLNGLU
15   HISASPILETHRASNPHETYRMETLEUTHR
16   LEUASPLYSASPARGILEILEASPALAGLY
17   PROLYSGLYASNTYRALAARGPHEMETASN
18   HISCYSCYSGLNPROASNCYSGLUTHRGLN
19   LYSTRPSERVALASNGLYASPTHRARGVAL
20   GLYLEUPHEALALEUSERASPILELYSALA
21   GLYTHRGLULEUTHRPHEASNTYRASNLEU
22   GLUCYSLEUGLYASNGLYLYSTHRVALCYS
23   LYSCYSGLYALAPROASNCYSSERGLYPHE
24   LEUGLY

Samples:

sample_1: NSD1, [U-98% 13C; U-98% 15N], 0.2 mM; MES 50 mM; sodium chloride 450 mM; TCEP 2 mM; S-adenosyl methionine 2 mM; sodium azide 0.01 % w/v; D2O 10 % v/v

sample_conditions_1: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CCPN_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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