BMRB Entry 25533

Title:
1H, 13C and 15N assignments of EGF domains 8 to 11 of human Notch-1
Deposition date:
2015-03-12
Original release date:
2015-06-04
Authors:
Handford, Penny; Redfield, Christina; Weisshuhn, Philip
Citation:

Citation: Weisshuhn, Philip; Handford, Penny; Redfield, Christina. "1H, 13C and 15N assignments of EGF domains 8-11 of human Notch-1"  Biomol. NMR assign. 9, 375-379 (2015).
PubMed: 25930016

Assembly members:

Assembly members:
hN-1_8-11, polymer, 159 residues, Formula weight is not available
CALCIUM ION, non-polymer, 40.078 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: pQE-30

Data sets:
Data typeCount
13C chemical shifts524
15N chemical shifts161
1H chemical shifts794

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hN-1 8-111
2Ca2+, 12
3Ca2+, 22
4Ca2+, 32

Entities:

Entity 1, hN-1 8-11 159 residues - Formula weight is not available

1   SERALAASPVALASPGLUCYSGLNLEUMET
2   PROASNALACYSGLNASNGLYGLYTHRCYS
3   HISASNTHRHISGLYGLYTYRASNCYSVAL
4   CYSVALASNGLYTRPTHRGLYGLUASPCYS
5   SERGLUASNILEASPASPCYSALASERALA
6   ALACYSPHEHISGLYALATHRCYSHISASP
7   ARGVALALASERPHETYRCYSGLUCYSPRO
8   HISGLYARGTHRGLYLEULEUCYSHISLEU
9   ASNASPALACYSILESERASNPROCYSASN
10   GLUGLYSERASNCYSASPTHRASNPROVAL
11   ASNGLYLYSALAILECYSTHRCYSPROSER
12   GLYTYRTHRGLYPROALACYSSERGLNASP
13   VALASPGLUCYSSERLEUGLYALAASNPRO
14   CYSGLUHISALAGLYLYSCYSILEASNTHR
15   LEUGLYSERPHEGLUCYSGLNCYSLEUGLN
16   GLYTYRTHRGLYPROARGCYSGLUILE

Entity 2, Ca2+, 1 - Ca - 40.078 Da.

1   CA

Samples:

8-11_15N: hN-1 8-11, [U-99% 15N], 1 mM; Calcium ion 30 mM; D2O, [U-2H], 5%; H2O 95%

8-11_15N-13C: hN-1 8-11, [U-100% 13C; U-100% 15N], 0.5 mM; Calcium ion 30 mM; D2O, [U-2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 120 mM; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY8-11_15Nisotropicsample_conditions_1
3D 1H-15N TOCSY8-11_15Nisotropicsample_conditions_1
3D 1H-15N NOESY8-11_15Nisotropicsample_conditions_1
2D 1H-15N HSQC8-11_15Nisotropicsample_conditions_1
2D 1H-15N HSQC8-11_15N-13Cisotropicsample_conditions_1
3D HBHA(CO)NH8-11_15N-13Cisotropicsample_conditions_1
3D HNCA8-11_15N-13Cisotropicsample_conditions_1
3D HNCO8-11_15N-13Cisotropicsample_conditions_1
3D HN(CA)CO8-11_15N-13Cisotropicsample_conditions_1
3D CBCA(CO)NH8-11_15N-13Cisotropicsample_conditions_1
3D HCCH-TOCSY8-11_15N-13Cisotropicsample_conditions_1
3D 1H-13C NOESY8-11_15N-13Cisotropicsample_conditions_1
2D 1H-13C HSQC8-11_15N-13Cisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CCPN_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Home-built Omega 600 MHz
  • Home-built Omega 950 MHz

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