BMRB Entry 25325

Name: NMR Chemical Shifts of the hybrid protein Beta-Synuclien HC
Published: 2015-09-03

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25325

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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 Chemical Shifts of the hybrid protein Beta-Synuclien HC

Deposition date:

2014-11-10

Original release date:

2015-09-03

Authors:

Allison, Jane; Rivers, Robert; Christodoulou, John; Vendruscolo, Michele; Dobson, Christopher

Citation:

Citation: Allison, Jane; Rivers, Robert; Christodoulou, John; Vendruscolo, Michele; Dobson, Christopher. "A relationship between the transient structure in the monomeric state and the aggregation propensities" Biochemistry ., .-..

Assembly members:

Assembly members:
beta-synuclein_HC, polymer, 145 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: T9

Entity Sequences (FASTA):

Entity Sequences (FASTA):
beta-synuclein_HC: MDVFMKGLSMAKEGVVAAAE KTKQGVTEAAEKTKEGVLYV GSKTREGVVQGVASVAEKTK EQASHLGGAVFSGVTAVAQK TVEGAGNIAAATGLVKREEF PTDLKPEEVAQEAAEEPLIE PLMEPEGESYEDPPQEEYQE YEPEA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	260
15N chemical shifts	133
1H chemical shifts	133

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Beta-synuclein HC	1

Entities:

Entity 1, Beta-synuclein HC 145 residues - Formula weight is not available

1

MET

ASP

VAL

PHE

MET

LYS

GLY

LEU

SER

MET

2

ALA

LYS

GLU

GLY

VAL

ALA

GLU

3

LYS

THR

LYS

GLN

GLY

VAL

THR

GLU

ALA

4

GLU

LYS

THR

LYS

GLU

GLY

VAL

LEU

TYR

VAL

5

GLY

SER

LYS

THR

ARG

GLU

GLY

VAL

GLN

6

GLY

VAL

ALA

SER

VAL

ALA

GLU

LYS

THR

LYS

7

GLU

GLN

ALA

SER

HIS

LEU

GLY

ALA

VAL

8

PHE

SER

GLY

VAL

THR

ALA

VAL

ALA

GLN

LYS

9

THR

VAL

GLU

GLY

ALA

GLY

ASN

ILE

ALA

10

ALA

THR

GLY

LEU

VAL

LYS

ARG

GLU

PHE

11

PRO

THR

ASP

LEU

LYS

PRO

GLU

VAL

ALA

12

GLN

GLU

ALA

GLU

PRO

LEU

ILE

GLU

13

PRO

LEU

MET

GLU

PRO

GLU

GLY

GLU

SER

TYR

14

GLU

ASP

PRO

GLN

GLU

TYR

GLN

GLU

15

TYR

GLU

PRO

GLU

ALA

Samples:

sample: beta-synuclein HC, [U-99% 13C; U-99% 15N], 150 uM; NaCl 100 mM; Phosphate Buffer 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

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

Software:

SPARKY v3.114, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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