BMRB Entry 51810

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51810

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Title:
Backbone chemical shifts for the Drosophila melanogaster Deltex WWE2 domain
Deposition date:
2023-01-25
Original release date:
2023-06-19
Authors:
Carter, Andrea; Majumdar, Ananya; Barrick, Doug
Citation:

Citation: Carter, Andrea; Ramsey, Kristen; Hatem, Christine; Sherry, Kathryn; Majumdar, Ananya; Barrick, Doug. "Structural features of the Notch ankyrin domain-Deltex WWE2 domain heterodimer determined by NMR spectroscopy and functional implications"  Structure 31, 584-594 (2023).
PubMed: 36977409

Assembly members:

Assembly members:
entity_1, polymer, 236 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATMALSTAGSGGPPVNHAHA VSVWEFESRGKWLPYSPAVS QHLERAHAKKLTRVMLSDAD PSLEQYYVNVRTMTQESEAE TAGSGLLTIGVRRMFYAPSS PAGKGTKWEWSGGSADSNND WRPYNMHVQSIIEDAWARGE QTLDLSNTHIGLPYTINFSN LTQLRQPSGPMRSIRRTQQA PYPLVKLTPQQANQLKSNSA SVSSQYNTLPKLGDTKSLHR VPMTRQQHPLPTSHQV

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts169
1H chemical shifts169

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Deltex1

Entities:

Entity 1, Deltex 236 residues - Formula weight is not available

The first residue (A) is residue 26 of Drosophila Deltex. The last residue (V) is residue 261. Four surface-exposed Cysteine residues in Drosophila Deltex were substituted with Serine residues.

1   ALATHRMETALALEUSERTHRALAGLYSER
2   GLYGLYPROPROVALASNHISALAHISALA
3   VALSERVALTRPGLUPHEGLUSERARGGLY
4   LYSTRPLEUPROTYRSERPROALAVALSER
5   GLNHISLEUGLUARGALAHISALALYSLYS
6   LEUTHRARGVALMETLEUSERASPALAASP
7   PROSERLEUGLUGLNTYRTYRVALASNVAL
8   ARGTHRMETTHRGLNGLUSERGLUALAGLU
9   THRALAGLYSERGLYLEULEUTHRILEGLY
10   VALARGARGMETPHETYRALAPROSERSER
11   PROALAGLYLYSGLYTHRLYSTRPGLUTRP
12   SERGLYGLYSERALAASPSERASNASNASP
13   TRPARGPROTYRASNMETHISVALGLNSER
14   ILEILEGLUASPALATRPALAARGGLYGLU
15   GLNTHRLEUASPLEUSERASNTHRHISILE
16   GLYLEUPROTYRTHRILEASNPHESERASN
17   LEUTHRGLNLEUARGGLNPROSERGLYPRO
18   METARGSERILEARGARGTHRGLNGLNALA
19   PROTYRPROLEUVALLYSLEUTHRPROGLN
20   GLNALAASNGLNLEULYSSERASNSERALA
21   SERVALSERSERGLNTYRASNTHRLEUPRO
22   LYSLEUGLYASPTHRLYSSERLEUHISARG
23   VALPROMETTHRARGGLNGLNHISPROLEU
24   PROTHRSERHISGLNVAL

Samples:

sample_1: Deltex WWE2 domain, [U-100% 2H; U-100% 13C; U-100% 15N], 500 uM; sodium chloride 300 mM; sodium phosphate 25 mM

sample_2: Deltex WWE2 domain, [U-100% 2H; U-100% 15N], 500 uM; sodium chloride 300 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 25 K

sample_conditions_2: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 25 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_2isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
HN(CA)Nsample_1isotropicsample_conditions_1
HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

CARA - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance II 600 MHz

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