BMRB Entry 17758

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

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17758

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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 oxidized 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 CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAYYDGRRSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	283
1H chemical shifts	93

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

CYS

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

CYS

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

BMRB	15845 16071 16075 16076 16077 16078 16079 16080 16184 16185 16722 16723 17081 17082 17084 17087 17174 17213 17759
PDB	1AG2 1XYX 1Y15 1Y16 2K5O 2KFM 2KFO 2KU5 2KU6 2L1D 2L1E 2L1H 2L1K 2L39 2L40 4H88 4MA7 4MA8
DBJ	BAA08790 BAE28320 BAE28693 BAE29994 BAE34221
EMBL	CAJ18553
GB	AAA39996 AAA39997 AAA39998 AAA41947 AAB30728
REF	NP_001265185 NP_035300 NP_036763 XP_006235124 XP_006984054
SP	P04925 P13852 Q9Z0T3
AlphaFold	P04925 P13852 Q9Z0T3