BMRB Entry 28116

Name: Sequence-specific Backbone Resonance Assignments of Human PrP(23-144) at pH 7.0
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28116

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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:

Sequence-specific Backbone Resonance Assignments of Human PrP(23-144) at pH 7.0

Deposition date:

2020-04-16

Original release date:

2021-07-16

Authors:

Flender, Daniel; Roesener, Nadine; Gremer, Lothar; Heise, Henrike; Willbold, Dieter; Neudecker, Philipp

Citation:

Citation: Konig, Anna; Rosener, Nadine; Gremer, Lothar; Tusche, Markus; Flender, Daniel; Reinartz, Elke; Hoyer, Wolfgang; Neudecker, Philipp; Willbold, Dieter; Heise, Henrike. "Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy" J. Biol. Chem. 296, 100499-100499 (2021).
PubMed: 33667547

Assembly members:

Assembly members:
huPrP(23-144), polymer, 123 residues, 12224.5 Da.

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: pET302/NT-His

Entity Sequences (FASTA):

Entity Sequences (FASTA):
huPrP(23-144): GKKRPKPGGWNTGGSRYPGQ GSPGGNRYPPQGGGGWGQPH GGGWGQPHGGGWGQPHGGGW GQPHGGGWGQGGGTHSQWNK PSKPKTNMKHMAGAAAAGAV VGGLGGYMLGSAMSRPIIHF GSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_HEPES

Data type	Count
13C chemical shifts	326
15N chemical shifts	126
1H chemical shifts	138

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	huPrP(23-144)	1

Entities:

Entity 1, huPrP(23-144) 123 residues - 12224.5 Da.

The 22-residue N-terminal signal peptide is not included. Instead, the sequence has a short N-terminal cloning artifact consisting of a single glycine residue.

1

GLY

LYS

ARG

PRO

LYS

PRO

GLY

TRP

2

ASN

THR

GLY

SER

ARG

TYR

PRO

GLY

GLN

3

GLY

SER

PRO

GLY

ASN

ARG

TYR

PRO

4

GLN

GLY

TRP

GLY

GLN

PRO

HIS

5

GLY

TRP

GLY

GLN

PRO

HIS

GLY

6

GLY

TRP

GLY

GLN

PRO

HIS

GLY

TRP

7

GLY

GLN

PRO

HIS

GLY

TRP

GLY

GLN

8

GLY

THR

HIS

SER

GLN

TRP

ASN

LYS

9

PRO

SER

LYS

PRO

LYS

THR

ASN

MET

LYS

HIS

10

MET

ALA

GLY

ALA

GLY

ALA

VAL

11

VAL

GLY

LEU

GLY

TYR

MET

LEU

GLY

12

SER

ALA

MET

SER

ARG

PRO

ILE

HIS

PHE

13

GLY

SER

ASP

Samples:

sample_13C15N_HEPES: huPrP(23-144), [U-13C; U-15N], 0.30 mM; HEPES 50 mM; H2O 90%; D2O 10%

sample_conditions_HEPES: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 278.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_13C15N_HEPES	isotropic	sample_conditions_HEPES
3D HNCO	sample_13C15N_HEPES	isotropic	sample_conditions_HEPES
3D HNCACB	sample_13C15N_HEPES	isotropic	sample_conditions_HEPES
3D BEST-TROSY-(H)N(COCA)NH	sample_13C15N_HEPES	isotropic	sample_conditions_HEPES

Software:

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

NMRViewJ v8.0.3, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Varian VNMRS 800 MHz

UNP	P04156
AlphaFold	Q9UP19