BMRB Entry 15824

Name: Bank Vole Prion Protein (121-231)
Published: 2008-09-12

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15824

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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:

Bank Vole Prion Protein (121-231)

Deposition date:

2008-06-25

Original release date:

2008-09-12

Authors:

Christen, Barbara; Hornemann, Simone; Wuthrich, Kurt

Citation:

Citation: Christen, Barbara; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt. "NMR Structure of the Bank Vole Prion Protein at 20 degrees C Contains a Structured Loop of Residues 165-171" J. Mol. Biol. 383, 306-312 (2008).
PubMed: 18773909

Assembly members:

Assembly members:
Prion_Protein, polymer, 113 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prion_Protein: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMNRYP NQVYYRPVDQYNNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAYYEGRSS

Data sets:

assigned_chemical_shifts
- bvPrP-BMRB.prot

Data type	Count
13C chemical shifts	364
15N chemical shifts	135
1H chemical shifts	414

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Prion Protein	1

Entities:

Entity 1, Prion Protein 113 residues - Formula weight is not available

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

ASN

ARG

TYR

PRO

5

ASN

GLN

VAL

TYR

ARG

PRO

VAL

ASP

GLN

6

TYR

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

GLU

GLY

12

ARG

SER

Samples:

15N: Prion Protein, [U-99% 15N], 1 mM; D2O 10%; H2O 90%; sodium acetate, [U-2H], 10 mM; H2O 90%; D2O, [U-100% 2H], 10%

13C_15N: Prion Protein, [U-99% 13C; U-99% 15N], 1 mM; D2O 10%; H2O 90%; sodium acetate, [U-2H], 10 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	15N	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C_15N	isotropic	sample_conditions_1

Software:

OPAL v1.2, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA v1.5.5, Keller, R. - data analysis

ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking

DYANA v1.0.3, Guntert, Braun and Wuthrich - structure solution

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

Bruker DRX 750 MHz
Bruker Avance 900 MHz

BMRB	15845
PDB	1AG2 2K56 2K5O
GB	AAL57231 AAL57232 ABR23642 ACJ06784 ACV85679
REF	XP_005365625 XP_006984054 XP_007609107