BMRB Entry 51878

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for apo Vtc2(1-201)
Published: 2023-05-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51878

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for apo Vtc2(1-201)

Deposition date:

2023-03-14

Original release date:

2023-05-08

Authors:

Pipercevic, Joka; Muntener, Thomas; Hiller, Sebastian

Citation:

Citation: Pipercevic, Joka; Kohl, Bastian; Gerasimaite, Ruta; Comte-Miserez, Veronique; Hostachy, Sarah; Muntener, Thomas; Agustoni, Elia; Jessen, Henning Jacob; Fiedler, Dorothea; Mayer, Andreas; Hiller, Sebastian. "Inositol pyrophosphates activate the vacuolar transport chaperone complex in yeast by disrupting a homotypic SPX domain interaction" Nat. Commun. 14, 2645-2645 (2023).
PubMed: 37156835

Assembly members:

Assembly members:
entity_1, polymer, 207 residues, Formula weight is not available

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: modified pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLFGVKLANEVYPPWKGSYI NYEGLKKFLKEDSVKDGSND KKARWDDSDESKFVEELDKE LEKVYGFQLKKYNNLMERLS HLEKQTDTEAAIKALDADAF QRVLEELLSESTELDNFKRL NFTGFAKIVKKHDKLYPKYP SVKSLLEVRLKELPSHSEEY SPLLYRISFLYNILRSNFNT ASEPLASASKFSSIVSNDID MENLYFQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	557
15N chemical shifts	188
1H chemical shifts	188

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Vtc2(1-201)	1

Entities:

Entity 1, Vtc2(1-201) 207 residues - Formula weight is not available

1

MET

LEU

PHE

GLY

VAL

LYS

LEU

ALA

ASN

GLU

2

VAL

TYR

PRO

TRP

LYS

GLY

SER

TYR

ILE

3

ASN

TYR

GLU

GLY

LEU

LYS

PHE

LEU

LYS

4

GLU

ASP

SER

VAL

LYS

ASP

GLY

SER

ASN

ASP

5

LYS

ALA

ARG

TRP

ASP

SER

ASP

GLU

6

SER

LYS

PHE

VAL

GLU

LEU

ASP

LYS

GLU

7

LEU

GLU

LYS

VAL

TYR

GLY

PHE

GLN

LEU

LYS

8

LYS

TYR

ASN

LEU

MET

GLU

ARG

LEU

SER

9

HIS

LEU

GLU

LYS

GLN

THR

ASP

THR

GLU

ALA

10

ALA

ILE

LYS

ALA

LEU

ASP

ALA

ASP

ALA

PHE

11

GLN

ARG

VAL

LEU

GLU

LEU

SER

GLU

12

SER

THR

GLU

LEU

ASP

ASN

PHE

LYS

ARG

LEU

13

ASN

PHE

THR

GLY

PHE

ALA

LYS

ILE

VAL

LYS

14

LYS

HIS

ASP

LYS

LEU

TYR

PRO

LYS

TYR

PRO

15

SER

VAL

LYS

SER

LEU

GLU

VAL

ARG

LEU

16

LYS

GLU

LEU

PRO

SER

HIS

SER

GLU

TYR

17

SER

PRO

LEU

TYR

ARG

ILE

SER

PHE

LEU

18

TYR

ASN

ILE

LEU

ARG

SER

ASN

PHE

ASN

THR

19

ALA

SER

GLU

PRO

LEU

ALA

SER

ALA

SER

LYS

20

PHE

SER

ILE

VAL

SER

ASN

ASP

ILE

ASP

21

MET

GLU

ASN

LEU

TYR

PHE

GLN

Samples:

sample_1: apo-Vtc2(1-201), [U-13C; U-15N; U-2H], 500 uM; D2O 5%; NaCl 250 mM; EDTA 0.5 mM; TCEP 0.5 mM; HEPES 25 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CARA - data analysis

PROSA - processing

XEASY - data analysis

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz

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