BMRB Entry 27027

Name: N-terminally acetylated beta-Synuclein
Published: 2017-08-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27027

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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:

N-terminally acetylated beta-Synuclein

Deposition date:

2017-02-06

Original release date:

2017-08-23

Authors:

Miotto, Marco; Pavese, Mayra; Quintanar, Liliana; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio

Citation:

Citation: Miotto, Marco; Pavese, Mayra; Quintanar, Liliana; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio. "Bioinorganic Chemistry of Parkinson's Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length beta-Synuclein Protein" Inorg. Chem. 56, 10387-10395 (2017).
PubMed: 28820253

Assembly members:

Assembly members:
AcBS, polymer, 135 residues, Formula weight is not available

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: pT7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AcBS: XMDVFMKGLSMAKEGVVAAA EKTKQGVTEAAEKTKEGVLY VGSKTREGVVQGVASVAEKT KEQASHLGGAVFSGAGNIAA ATGLVKREEFPTDLKPEEVA QEAAEEPLIEPLMEPEGESY EDPPQEEYQEYEPEA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	126
1H chemical shifts	255

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AcBS	1

Entities:

Entity 1, AcBS 135 residues - Formula weight is not available

1

ACE

MET

ASP

VAL

PHE

MET

LYS

GLY

LEU

SER

2

MET

ALA

LYS

GLU

GLY

VAL

ALA

3

GLU

LYS

THR

LYS

GLN

GLY

VAL

THR

GLU

ALA

4

ALA

GLU

LYS

THR

LYS

GLU

GLY

VAL

LEU

TYR

5

VAL

GLY

SER

LYS

THR

ARG

GLU

GLY

VAL

6

GLN

GLY

VAL

ALA

SER

VAL

ALA

GLU

LYS

THR

7

LYS

GLU

GLN

ALA

SER

HIS

LEU

GLY

ALA

8

VAL

PHE

SER

GLY

ALA

GLY

ASN

ILE

ALA

9

ALA

THR

GLY

LEU

VAL

LYS

ARG

GLU

PHE

10

PRO

THR

ASP

LEU

LYS

PRO

GLU

VAL

ALA

11

GLN

GLU

ALA

GLU

PRO

LEU

ILE

GLU

12

PRO

LEU

MET

GLU

PRO

GLU

GLY

GLU

SER

TYR

13

GLU

ASP

PRO

GLN

GLU

TYR

GLN

GLU

14

TYR

GLU

PRO

GLU

ALA

Samples:

sample_1: AcBS, [U-100% 13C; U-100% 15N], 0.2 mM; MES 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

Bruker Avance 600 MHz

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