BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50897

Title: hDVL2 DEP (401-510)   PubMed: 34155117

Deposition date: 2021-04-15 Original release date: 2021-06-25

Authors: Beitia, Gonzalo; Rutherford, Trevor; Freund, Stefan; Pelham, Hugh; Bienz, Mariann; Gammons, Melissa

Citation: Beitia, Gonzalo; Rutherford, Trevor; Freund, Stefan; Pelham, Hugh; Bienz, Mariann; Gammons, Melissa. "Regulation of Dishevelled DEP domain swapping by conserved phosphorylation sites."  Proc. Natl. Acad. Sci. U. S. A. 118, e2103258118-e2103258118 (2021).

Assembly members:
entity_1, polymer, 110 residues, 12105 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11, EMBL

Entity Sequences (FASTA):
entity_1: SITSGSSLPDGCEGRGLSVH TDMASVTKAMAAPESGLEVR DRMWLKITIPNAFLGSDVVD WLYHHVEGFPERREARKYAS GLLKAGLIRHTVNKITFSEQ CYYVFGDLSG

Data sets:
Data typeCount
13C chemical shifts305
15N chemical shifts102
1H chemical shifts209
T2 relaxation values98
heteronuclear NOE values98

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DVL2 DEP1

Entities:

Entity 1, DVL2 DEP 110 residues - 12105 Da.

1   SERILETHRSERGLYSERSERLEUPROASP
2   GLYCYSGLUGLYARGGLYLEUSERVALHIS
3   THRASPMETALASERVALTHRLYSALAMET
4   ALAALAPROGLUSERGLYLEUGLUVALARG
5   ASPARGMETTRPLEULYSILETHRILEPRO
6   ASNALAPHELEUGLYSERASPVALVALASP
7   TRPLEUTYRHISHISVALGLUGLYPHEPRO
8   GLUARGARGGLUALAARGLYSTYRALASER
9   GLYLEULEULYSALAGLYLEUILEARGHIS
10   THRVALASNLYSILETHRPHESERGLUGLN
11   CYSTYRTYRVALPHEGLYASPLEUSERGLY

Samples:

sample_1: DVL2 DEP, [U-100% 13C; U-100% 15N], 350 uM; sodium phosphate 25 mM; sodium chloride 150 mM

sample_2: DVL2 DEP, [U-100% 15N], 330 uM; sodium phosphate 25 mM; sodium chloride 150 mM

sample_3: DVL2 DEP, [U-100% 15N], 400 uM; sodium phosphate 25 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.7; pressure: 1 atm; temperature: 283 K

sample_conditions_2: ionic strength: 200 mM; pH: 6.7; pressure: 1 atm; temperature: 283 K

sample_conditions_3: ionic strength: 200 mM; pH: 6.7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_2
T2/R2 relaxationsample_3isotropicsample_conditions_3

Software:

TOPSPIN v3 - collection, processing

NMRFAM-SPARKY v1.3 - data analysis, peak picking

MARS v1.1 - chemical shift assignment

TALOS+ v3.80 - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE I 600 MHz

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