BMRB Entry 17756

Name: Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its oxidized state
Published: 2011-07-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17756

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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 and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its oxidized state

Deposition date:

2011-07-05

Original release date:

2011-07-18

Authors:

Schwalbe, Harald

Citation:

Citation: Gerum, Christian; Silvers, Robert; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Unfolded-State Structure and Dynamics Influence the Fibril Formation of Human Prion Protein" Angew. Chem. Int. Ed. 48, 9452-9456 (2009).
PubMed: 19882604

Assembly members:

Assembly members:
hPrP(121-230), polymer, 113 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: pJC40(TEV)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hPrP(121-230): GHMVVGGLGGYMLGSAMSRP IIHFGSDYEDRYYRENMHRY PNQVYYRPMDEYSNQNNFVH DCVNITIKQHTVTTTTKGEN FTETDVKMMERVVEQMCITQ YERESQAYYQRGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	254
1H chemical shifts	177

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human prion protein (residues 121-230)	1

Entities:

Entity 1, human prion protein (residues 121-230) 113 residues - Formula weight is not available

Construct constitutes C-terminal domain (residues 121-230). First three residues are a remnant of the N-terminal (his)6 tag.

1

GLY

HIS

MET

VAL

GLY

LEU

GLY

2

TYR

MET

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

3

ILE

HIS

PHE

GLY

SER

ASP

TYR

GLU

ASP

4

ARG

TYR

ARG

GLU

ASN

MET

HIS

ARG

TYR

5

PRO

ASN

GLN

VAL

TYR

ARG

PRO

MET

ASP

6

GLU

TYR

SER

ASN

GLN

ASN

PHE

VAL

HIS

7

ASP

CYS

VAL

ASN

ILE

THR

ILE

LYS

GLN

HIS

8

THR

VAL

THR

LYS

GLY

GLU

ASN

9

PHE

THR

GLU

THR

ASP

VAL

LYS

MET

GLU

10

ARG

VAL

GLU

GLN

MET

CYS

ILE

THR

GLN

11

TYR

GLU

ARG

GLU

SER

GLN

ALA

TYR

GLN

12

ARG

GLY

SER

Samples:

sample_1: hPrP(121-230), [U-13C; U-15N], 0.2 – 0.5 mM; TSP 1 mM; urea 8 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 2.0; pressure: 1 atm; temperature: 298 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 600 MHz
Bruker Avance 700 MHz
Bruker Avance 800 MHz

BMRB	15676 16743 16757 17714 17757 17780 18426 18550 19268 4379 4402 4434 4620 4641 4736
PDB	1E1G 1E1J 1E1P 1E1S 1E1U 1E1W 1FKC 1FO7 1H0L 1HJM 1HJN 1I4M 1QLX 1QLZ 1QM0 1QM1 1QM2 1QM3 2K1D 2KUN 2LEJ 2LFT 2LSB 2LV1 2M8T 2W9E 3HAF 3HAK 3HEQ 3HER 3HES 3HJ5 3HJX 4DGI 4KML 4N9O
DBJ	BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL	CAA58442 CAG46836 CAG46869
GB	AAA19664 AAA60182 AAA68632 AAA68633 AAB59442
REF	NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP	P04156 P40252 P61766 P61767 P61768
AlphaFold	P04156 P40252 P61766 P61767 P61768