BMRB Entry 26768

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26768

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Title:
1H, 15N and 13C backbone assignments of the catalytic domain of human NSD2
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:
NSD2, polymer, 235 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):
NSD2: GSHMKLQREARETQESERKP PPYKHIKVNKPYGKVQIYTA DISEIPKCNCKPTDENPCGF DSECLNRMLMFECHPQVCPA GEFCQNQCFTKRQYPETKII KTDGKGWGLVAKRDIRKGEF VNEYVGELIDEEECMARIKH AHENDITHFYMLTIDKDRII DAGPKGNYSRFMNHSCQPNC ETLKWTVNGDTRVGLFAVCD IPAGTELTFNYNLDCLGNEK TVCRCGASNCSGFLG

Data sets:
Data typeCount
13C chemical shifts629
15N chemical shifts206
1H chemical shifts206

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NSD21

Entities:

Entity 1, NSD2 235 residues - Formula weight is not available

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

Samples:

sample_1: NSD2, [U-98% 13C; U-98% 15N], 0.2 mM; potassium phosphate 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: 7; pressure: 1 atm; temperature: 310 K

Experiments:

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