BMRB Entry 26925

Name: 13C and 15N Chemical Shift Assignments for human Y145Stop Prion Protein Amyloid Fibrils
Published: 2017-02-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26925

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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:

13C and 15N Chemical Shift Assignments for human Y145Stop Prion Protein Amyloid Fibrils

Deposition date:

2016-10-26

Original release date:

2017-02-15

Authors:

Theint, Theint; Nadaud, Philippe; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher

Citation:

Citation: Theint, Theint; Nadaud, Philippe; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher. "13C and 15N Chemical Shift Assignments of Mammalian Y145Stop Prion Protein Amyloid Fibrils" Biomol. NMR Assign. 11, 75-80 (2017).
PubMed: 28004358

Assembly members:

Assembly members:
huPrP23-144, polymer, 126 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: pRSETB

Entity Sequences (FASTA):

Entity Sequences (FASTA):
huPrP23-144: GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGGGWG QPHGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQGGGTHSQ WNKPSKPKTNMKHMAGAAAA GAVVGGLGGYMLGSAMSRPI IHFGSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	92
15N chemical shifts	28

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	huPrP23-144	1

Entities:

Entity 1, huPrP23-144 126 residues - Formula weight is not available

The four N-terminal residues (GSDP) correspond to non-native thrombin cleavage sites used for protein purification.

1

GLY

SER

ASP

PRO

LYS

ARG

PRO

LYS

PRO

2

GLY

TRP

ASN

THR

GLY

SER

ARG

TYR

3

PRO

GLY

GLN

GLY

SER

PRO

GLY

ASN

ARG

4

TYR

PRO

GLN

GLY

TRP

GLY

5

GLN

PRO

HIS

GLY

TRP

GLY

GLN

PRO

6

HIS

GLY

TRP

GLY

GLN

PRO

HIS

GLY

7

GLY

TRP

GLY

GLN

PRO

HIS

GLY

8

TRP

GLY

GLN

GLY

THR

HIS

SER

GLN

9

TRP

ASN

LYS

PRO

SER

LYS

PRO

LYS

THR

ASN

10

MET

LYS

HIS

MET

ALA

GLY

ALA

11

GLY

ALA

VAL

GLY

LEU

GLY

TYR

12

MET

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

ILE

13

ILE

HIS

PHE

GLY

SER

ASP

Samples:

sample_1: huPrP23-144, [U-100% 13C; U-100% 15N], 20 mg

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 277 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NCA	sample_1	solid	sample_conditions_1
2D NCACX	sample_1	solid	sample_conditions_1
3D NCACX	sample_1	solid	sample_conditions_1
3D NCOCX	sample_1	solid	sample_conditions_1
3D CONCA	sample_1	solid	sample_conditions_1
2D DARR	sample_1	solid	sample_conditions_1

Software:

VNMR, Varian - collection

SPARKY, Goddard - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS-N, Shen and Bax - secondary structure analysis

nmrglue, Helmus, Jaroniec - processing

NMR spectrometers:

Varian VNMRS 500 MHz