BMRB Entry 17759

Name: Backbone 1H and 13C Chemical Shift Assignments of murine prion protein (residues 121-232) in its reduced state
Published: 2011-07-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17759

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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 murine prion protein (residues 121-232) in its reduced state

Deposition date:

2011-07-05

Original release date:

2011-07-14

Authors:

Schwalbe, Harald; Schlepckow, Kai

Citation:

Citation: Gerum, Christian; Schlepckow, Kai; Schwalbe, Harald. "The unfolded state of the murine prion protein and properties of single-point mutants related to human prion diseases" J. Mol. Biol. 401, 7-12 (2010).
PubMed: 20541558

Assembly members:

Assembly members:
mPrP(121-232), polymer, 114 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mPrP(121-232): GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQYSNQNNFVHD XVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMXVTQY QKESQAYYDGRRSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	301
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	murine prion protein (residues 121-232)	1

Entities:

Entity 1, murine prion protein (residues 121-232) 114 residues - Formula weight is not available

Construct constitutes C-terminal domain (residues 121-232). First two residues are a remnant of the N-terminal (his)6 tag.

1

GLY

SER

VAL

GLY

LEU

GLY

TYR

2

MET

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

MET

3

ILE

HIS

PHE

GLY

ASN

ASP

TRP

GLU

ASP

ARG

4

TYR

ARG

GLU

ASN

MET

TYR

ARG

TYR

PRO

5

ASN

GLN

VAL

TYR

ARG

PRO

VAL

ASP

GLN

6

TYR

SER

ASN

GLN

ASN

PHE

VAL

HIS

ASP

7

SMC

VAL

ASN

ILE

THR

ILE

LYS

GLN

HIS

THR

8

VAL

THR

LYS

GLY

GLU

ASN

PHE

9

THR

GLU

THR

ASP

VAL

LYS

MET

GLU

ARG

10

VAL

GLU

GLN

MET

SMC

VAL

THR

GLN

TYR

11

GLN

LYS

GLU

SER

GLN

ALA

TYR

ASP

GLY

12

ARG

SER

Samples:

sample_1: mPrP(121-232), [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