BMRB Entry 50734

Name: NMR backbone resonance assignment of the selenoprotein SelW1 (oxidized) from Chlamydomonas reinhardtii.
Published: 2021-07-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50734

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR backbone resonance assignment of the selenoprotein SelW1 (oxidized) from Chlamydomonas reinhardtii.

Deposition date:

2021-01-25

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:
entity_1, 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):
entity_1: MAPVQVHVLYCGGCGYGSRY RSLENAIRMKFPNADIKFSF EATPQATGFFEVEVNGELVH SKKNGGGHVDNQEKVERIFA KIGEALAK

Data sets:

assigned_chemical_shifts
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	370
15N chemical shifts	122
1H chemical shifts	543
T1 relaxation values	109
T2 relaxation values	109
heteronuclear NOE values	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SelW1, conformer 1	1
2	SelW1, conformer 2	1
3	SelW1, conformer 3	1

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

MET

ALA

PRO

VAL

GLN

VAL

HIS

VAL

LEU

TYR

2

CYS

GLY

CYS

GLY

TYR

GLY

SER

ARG

TYR

3

ARG

SER

LEU

GLU

ASN

ALA

ILE

ARG

MET

LYS

4

PHE

PRO

ASN

ALA

ASP

ILE

LYS

PHE

SER

PHE

5

GLU

ALA

THR

PRO

GLN

ALA

THR

GLY

PHE

6

GLU

VAL

GLU

VAL

ASN

GLY

GLU

LEU

VAL

HIS

7

SER

LYS

ASN

GLY

HIS

VAL

ASP

8

ASN

GLN

GLU

LYS

VAL

GLU

ARG

ILE

PHE

ALA

9

LYS

ILE

GLY

GLU

ALA

LEU

ALA

LYS

Samples:

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

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

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

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
15N-(1H) NOE	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis

TOPSPIN v3.2 and higher - collection, processing

NMR spectrometers:

Bruker AVANCE III 500 MHz