BMRB Entry 50898

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50898

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Title:
hDVL2 DEP domain (401-510) S418E mutant
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:

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).
PubMed: 34155117

Assembly members:

Assembly members:
entity_1, polymer, 110 residues, 12147 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: pETM-11, EMBL

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts102
1H chemical shifts213
T2 relaxation values97
heteronuclear NOE values101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DVL2 DEP S418E mutant1

Entities:

Entity 1, DVL2 DEP S418E mutant 110 residues - 12147 Da.

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

Samples:

sample_1: DVL2 DEP S418E mutant, [U-100% 13C; U-100% 15N], 350 uM; sodium phosphate 25 mM; sodium chloride 150 mM

sample_2: DVL2 DEP S418E mutant, [U-100% 15N], 330 uM; sodium phosphate 25 mM; sodium chloride 150 mM

sample_3: DVL2 DEP S418E mutant, [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 HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-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+ v3.8 - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE I 600 MHz
  • Bruker AVANCE III 700 MHz

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