Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53716

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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:

1H, 13C, and 15N backbone resonance assignments of the N-terminal intrinsically disordered region and folded domain of the prion protein segment 90-231 of Bank Vole (BV-PrPC)

Deposition date:

2026-04-11

Original release date:

2026-05-05

Authors:

Sanchez-Pedregal, Victor; Martin-Pastor, Manuel; Requena, Jesus

Citation:

Citation: Sanchez-Pedregal, Victor; Martin-Pastor, Manuel; Requena, Jesus. "1H, 13C, and 15N backbone resonance assignments of the N-terminal intrinsically disordered region and folded domain of the prion protein segment 90-231 of Bank Vole (BV-PrPC)" .
PubMed: 2529837123

Assembly members:

Assembly members:
entity_1, polymer, 143 residues, 16259.05 Da.

Natural source:

Natural source: Common Name: Bank vole Taxonomy ID: 447135 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Myodes glareolus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Myodes glareolus Vector: pOPIN E

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HGQGGGTHNQWNKPSKPKTN IKHVAGAAAAGAVVGGLGGY MLGSAMSRPMIHFGNDWEDR YYRENMNRYPNQVYYRPVDQ YNNQNNFVHDCVNITIKQHT VTTTTKGENFTETDVKMMER VVEQMCVTQYQKESQAYYEG RSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	306
15N chemical shifts	137
1H chemical shifts	665

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Free Bank Vole Prion protein (90-231) natively folded	1

Entities:

Entity 1, Free Bank Vole Prion protein (90-231) natively folded 143 residues - 16259.05 Da.

Bank Vole prion protein residues 90 to 231

1

HIS

GLY

GLN

GLY

THR

HIS

ASN

GLN

2

TRP

ASN

LYS

PRO

SER

LYS

PRO

LYS

THR

ASN

3

ILE

LYS

HIS

VAL

ALA

GLY

ALA

4

GLY

ALA

VAL

GLY

LEU

GLY

TYR

5

MET

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

MET

6

ILE

HIS

PHE

GLY

ASN

ASP

TRP

GLU

ASP

ARG

7

TYR

ARG

GLU

ASN

MET

ASN

ARG

TYR

PRO

8

ASN

GLN

VAL

TYR

ARG

PRO

VAL

ASP

GLN

9

TYR

ASN

GLN

ASN

PHE

VAL

HIS

ASP

10

CYS

VAL

ASN

ILE

THR

ILE

LYS

GLN

HIS

THR

11

VAL

THR

LYS

GLY

GLU

ASN

PHE

12

THR

GLU

THR

ASP

VAL

LYS

MET

GLU

ARG

13

VAL

GLU

GLN

MET

CYS

VAL

THR

GLN

TYR

14

GLN

LYS

GLU

SER

GLN

ALA

TYR

GLU

GLY

15

ARG

SER

Samples:

sample_1: Free Bank Vole Prion protein (90-231) natively folded, [U-100% 13C; U-100% 15N], 6.5 ± 0.5 mg/mL

sample_conditions_1: ionic strength: 0.005 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v3.3.4.1 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 750 MHz

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

BMRB Entry 53716