BMRB Entry 51699

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51699

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NMR-STAR v3 text file.
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Title:
1H, 13C, 15N resonance assignments for the EGF20 to EGF23 domains of human Notch 1
Deposition date:
2022-11-20
Original release date:
2024-10-25
Authors:
Hill, Johan; Handford, Penny; Redfield, Christina
Citation:

Citation: Bo, Zhihan; Rowntree, Thomas; Suckling, Richard; Hill, Johan; Korona, Bogusia; Boyce, Abi; Weisshuhn, Philip; Sheppard, Devon; Meng, Yao; Liang, Shaoyang; Barber, Lucy; Lea, Susan; Redfield, Christina; Handford, Penny. "Structural and functional studies of the EGF20-27 region reveal new features of the human Notch receptor important for optimal activation"  Structure ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 157 residues, Formula weight is not available
entity_CA, 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SAINNNECESNPCVNGGTCK DMTSGYVCTCREGFSGPNCQ TNINECASNPCLNQGTCIDD VAGYKCNCLLPYTGATCEVV LAPCAPSPCRNGGECRQSED YESFSCVCPTGWQGQTCEVD INECVLSPCRHGASCQNTHG GYRCHCQAGYSGRNCET

Data sets:
Data typeCount
13C chemical shifts465
15N chemical shifts122
1H chemical shifts589

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Notch20-231
2Ca-12
3Ca-22
4Ca-32

Entities:

Entity 1, Notch20-23 157 residues - Formula weight is not available

1   SERALAILEASNASNASNGLUCYSGLUSER
2   ASNPROCYSVALASNGLYGLYTHRCYSLYS
3   ASPMETTHRSERGLYTYRVALCYSTHRCYS
4   ARGGLUGLYPHESERGLYPROASNCYSGLN
5   THRASNILEASNGLUCYSALASERASNPRO
6   CYSLEUASNGLNGLYTHRCYSILEASPASP
7   VALALAGLYTYRLYSCYSASNCYSLEULEU
8   PROTYRTHRGLYALATHRCYSGLUVALVAL
9   LEUALAPROCYSALAPROSERPROCYSARG
10   ASNGLYGLYGLUCYSARGGLNSERGLUASP
11   TYRGLUSERPHESERCYSVALCYSPROTHR
12   GLYTRPGLNGLYGLNTHRCYSGLUVALASP
13   ILEASNGLUCYSVALLEUSERPROCYSARG
14   HISGLYALASERCYSGLNASNTHRHISGLY
15   GLYTYRARGCYSHISCYSGLNALAGLYTYR
16   SERGLYARGASNCYSGLUTHR

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

1   CA

Samples:

sample_1: Notch1 20-23, [U-98% 13C; U-98% 15N], 0.8 mM; calcium ion 10 mM; TRIS 5 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.18 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CCCONHsample_1isotropicsample_conditions_1
3D HCCCONHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2 - collection

NMRPipe - processing

CcpNMR v2.4/2.5 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 750 MHz

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