BMRB Entry 17757

Name: Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its reduced state
Published: 2011-07-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17757

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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 reduced state

Deposition date:

2011-07-05

Original release date:

2011-07-14

Authors:

Schwalbe, Harald; Schlepckow, Kai

Citation:

Citation: Gerum, Christian; Silvers, Robert; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Unfolded-state Structure and Dynamics Influence 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 DXVNITIKQHTVTTTTKGEN FTETDVKMMERVVEQMXITQ YERESQAYYQRGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	257
1H chemical shifts	174

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

SMC

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

SMC

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

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