BMRB Entry 51007

Name: Assignment of the full length Q216R mouse prion protein
Published: 2021-11-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51007

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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:

Assignment of the full length Q216R mouse prion protein

Deposition date:

2021-07-06

Original release date:

2021-11-10

Authors:

Bhate, Suhas; Udgaonkar, Jayant; Das, Ranabir

Citation:

Citation: Bhate, Suhas; Udgaonkar, Jayant; Das, Ranabir. "Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization" Protein Sci. 30, 2258-2271 (2021).
PubMed: 34558139

Assembly members:

Assembly members:
entity_1, polymer, 211 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: pET-17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKKRPKPGGWNTGGSRYPGQ GSPGGNRYPPQGGTWGQPHG GGWGQPHGGSWGQPHGGSWG QPHGGGWGQGGGTHNQWNKP SKPKTNLKHVAGAAAAGAVV GGLGGYMLGSAMSRPMIHFG NDWEDRYYRENMYRYPNQVY YRPVDQYSNQNNFVHDCVNI TIKQHTVTTTTKGENFTETD VKMMERVVEQMCVTRYQKES QAYYDGRRSSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	267
15N chemical shifts	155
1H chemical shifts	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Q216R mo PrP	1

Entities:

Entity 1, Q216R mo PrP 211 residues - Formula weight is not available

1

MET

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

THR

TRP

GLY

GLN

PRO

HIS

GLY

5

GLY

TRP

GLY

GLN

PRO

HIS

GLY

SER

6

TRP

GLY

GLN

PRO

HIS

GLY

SER

TRP

GLY

7

GLN

PRO

HIS

GLY

TRP

GLY

GLN

GLY

8

GLY

THR

HIS

ASN

GLN

TRP

ASN

LYS

PRO

9

SER

LYS

PRO

LYS

THR

ASN

LEU

LYS

HIS

VAL

10

ALA

GLY

ALA

GLY

ALA

VAL

11

GLY

LEU

GLY

TYR

MET

LEU

GLY

SER

12

ALA

MET

SER

ARG

PRO

MET

ILE

HIS

PHE

GLY

13

ASN

ASP

TRP

GLU

ASP

ARG

TYR

ARG

GLU

14

ASN

MET

TYR

ARG

TYR

PRO

ASN

GLN

VAL

TYR

15

TYR

ARG

PRO

VAL

ASP

GLN

TYR

SER

ASN

GLN

16

ASN

PHE

VAL

HIS

ASP

CYS

VAL

ASN

ILE

17

THR

ILE

LYS

GLN

HIS

THR

VAL

THR

18

THR

LYS

GLY

GLU

ASN

PHE

THR

GLU

THR

ASP

19

VAL

LYS

MET

GLU

ARG

VAL

GLU

GLN

20

MET

CYS

VAL

THR

ARG

TYR

GLN

LYS

GLU

SER

21

GLN

ALA

TYR

ASP

GLY

ARG

SER

22

SER

Samples:

sample_1: Q216R mouse prion protein, [U-99% 13C; U-99% 15N], 500 uM; Sodium Acetate 10 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 4; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks