BMRB Entry 15845

Name: Mouse Prion Protein (121-231) with Mutation S170N
Published: 2008-09-12

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PDB ID: 2k5o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15845
MolProbity Validation Chart

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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:

Mouse Prion Protein (121-231) with Mutation S170N

Deposition date:

2008-06-30

Original release date:

2008-09-12

Authors:

Perez, Daniel; 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, 114 residues, Formula weight is not available

Natural source:

Natural source: Common Name: house 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: pRSETA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prion_Protein: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQYNNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAYYDGRRSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	135
1H chemical shifts	396

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 114 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

TYR

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

ASP

GLY

12

ARG

SER

Samples:

13C_15N: Prion Protein, [U-99% 13C; U-99% 15N], 0.4 mM; D2O 10%; H2O 90%; sodium acetate, [U-2H], 10 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

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

Software:

xwinnmr, Bruker Biospin - collection

CARA, Keller, Rochus - 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

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

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

NMR spectrometers:

Bruker DRX 750 MHz

BMRB	15824 16071 16075 16076 16077 16078 16079 16080 16184 16185 16722 16723 17081 17082 17084 17174 17213 17758 17759
PDB	1AG2 1XYX 1Y15 1Y16 2K56 2K5O 2KFM 2KFO 2KU5 2KU6 2L1D 2L1E 2L1H 2L39 2L40 4H88 4MA7 4MA8
DBJ	BAA08790 BAE28320 BAE28693 BAE29994 BAE34221
EMBL	CAJ18553
GB	AAA37013 AAA37014 AAA39996 AAA39997 AAA39998
PIR	B34759
REF	NP_001265185 NP_035300 NP_036763 XP_003499061 XP_006235124
SP	P04925 P13852 Q60468 Q60506 Q9Z0T3
AlphaFold	P04925 P13852 Q60468 Q60506 Q9Z0T3