BMRB Entry 50649

Name: 1H, 13C, and 15N backbone chemical shift assignments of yeast sulfhydryl oxidase Erv1
Published: 2021-05-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50649

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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:

1H, 13C, and 15N backbone chemical shift assignments of yeast sulfhydryl oxidase Erv1

Deposition date:

2020-12-15

Original release date:

2021-05-21

Authors:

Volkov, Alexander; Peker, Esra; Riemer, Jan

Citation:

Citation: Peker, Esra; Erdogan, Alican; Volkov, Alexander; Riemer, Jan. "Erv1 and cytochrome c mediate rapid electron transfer via a collision-type interaction" J. Mol. Biol. ., .-. (2021).
PubMed: 33971209

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, Formula weight is not available
entity_FAD, non-polymer, 785.550 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPPDVEQLGRSSWTLLHSVA ASYPAQPTDQQKGEMKQFLN IFSHIYPCNWCAKDFEKYIR ENAPQVESREELGRWMCEAH NKVNKKLRKPKFDCNFWEKR WKDGWDELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	265
15N chemical shifts	84
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Erv1	1
2	FAD	2

Entities:

Entity 1, Erv1 115 residues - Formula weight is not available

1

MET

PRO

ASP

VAL

GLU

GLN

LEU

GLY

ARG

2

SER

TRP

THR

LEU

HIS

SER

VAL

ALA

3

ALA

SER

TYR

PRO

ALA

GLN

PRO

THR

ASP

GLN

4

GLN

LYS

GLY

GLU

MET

LYS

GLN

PHE

LEU

ASN

5

ILE

PHE

SER

HIS

ILE

TYR

PRO

CYS

ASN

TRP

6

CYS

ALA

LYS

ASP

PHE

GLU

LYS

TYR

ILE

ARG

7

GLU

ASN

ALA

PRO

GLN

VAL

GLU

SER

ARG

GLU

8

GLU

LEU

GLY

ARG

TRP

MET

CYS

GLU

ALA

HIS

9

ASN

LYS

VAL

ASN

LYS

LEU

ARG

LYS

PRO

10

LYS

PHE

ASP

CYS

ASN

PHE

TRP

GLU

LYS

ARG

11

TRP

LYS

ASP

GLY

TRP

ASP

GLU

LEU

GLU

HIS

12

HIS

Entity 2, FAD - C27 H33 N9 O15 P2 - 785.550 Da.

1

FAD

Samples:

sample_1: Erv1, [U-100% 13C; U-100% 15N; U-95% 2H], 0.7 mM; sodium phosphate 20 mM; sodium chloride 10 mM

sample_conditions_1: ionic strength: 28 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

NMRPipe - processing

CcpNMR - chemical shift assignment, data analysis

qMDD - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

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