BMRB Entry 50745

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50745

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Title:
NMR backbone resonance assignment of the selenoprotein SelW1 (reduced) from Chlamydomonas reinhardtii.
Deposition date:
2021-02-02
Original release date:
2021-07-11
Authors:
Seeger, Karsten; Schmidt, Christian
Citation:

Citation: Schmidt, Christian; Daberger, Jan; Sobek, Michael; Seeger, Karsten. "Structural and biophysical characterization of the selenoprotein SelW1 from Chlamydomonas reinhardtii."  Biochim. Biophys. Acta Proteins Proteom. 1869, 140685-140685 (2021).
PubMed: 34216797

Assembly members:

Assembly members:
Selenoprotein W1, polymer, 88 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: green algae   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Selenoprotein W1: MAPVQVHVLYCGGCGYGSRY RSLENAIRMKFPNADIKFSF EATPQATGFFEVEVNGELVH SKKNGGGHVDNQEKVERIFA KIGEALAK

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts133
1H chemical shifts560
T1 relaxation values118
T2 relaxation values120
heteronuclear NOE values120

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SelW1, conformer 11
2SelW1, conformer 21
3SelW1, conformer 31

Entities:

Entity 1, SelW1, conformer 1 88 residues - Formula weight is not available

The U14C mutant Selenoprotein W1 (provided amino acid sequence) is investigated. In the wildtype selenoprotein W1 from Chlamydomonas position 14 is selenocystein.

1   METALAPROVALGLNVALHISVALLEUTYR
2   CYSGLYGLYCYSGLYTYRGLYSERARGTYR
3   ARGSERLEUGLUASNALAILEARGMETLYS
4   PHEPROASNALAASPILELYSPHESERPHE
5   GLUALATHRPROGLNALATHRGLYPHEPHE
6   GLUVALGLUVALASNGLYGLULEUVALHIS
7   SERLYSLYSASNGLYGLYGLYHISVALASP
8   ASNGLNGLULYSVALGLUARGILEPHEALA
9   LYSILEGLYGLUALALEUALALYS

Samples:

sample_1: Selenoprotein W1, [U-15N], 0.89 mM; sodium chloride 25 mM; sodium phosphate 25 mM; TSP 0.1 mM; TCEP, [U-2H], 2 mM

sample_2: Selenoprotein W1, [U-13C; U-15N], 1.0 mM; sodium chloride 25 mM; sodium phosphate 25 mM; TSP 0.1 mM; TCEP, [U-2H], 4 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
15N-(1H) NOEsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis

TOPSPIN v3.2 and higher - collection, processing

NMR spectrometers:

  • Bruker AVANCE III 500 MHz

Related Database Links:

NCBI XP_001693901

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