BMRB Entry 15394

Name: NMR structure of rabbit prion protein mutation S173N
Published: 2010-11-15

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PDB ID: 2joh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15394
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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:

NMR structure of rabbit prion protein mutation S173N

Deposition date:

2007-07-19

Original release date:

2010-11-15

Authors:

Li, Jun; Lin, Donghai

Citation:

Citation: Wen, Yi; Li, Jun; Yao, Wenming; Xiong, Minqian; Hong, Jing; Peng, Yu; Xiao, Gengfu; Lin, Donghai. "Unique structural characteristics of the rabbit prion protein." J. Biol. Chem. 285, 31682-31693 (2010).
PubMed: 20639199

Assembly members:

Assembly members:
rpp mutation S173N, polymer, 138 residues, 12512.979 Da.

Natural source:

Natural source: Common Name: rabbit Taxonomy ID: 9986 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oryctolagus cuniculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-30a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rpp mutation S173N: QGGTHNQWGKPSKPKTSMKH VAPAAAAGAVVGGLGGYMLG SAMSRPLIHFGNDYEDRYYR ENMYRYPNQVYYRPVDQYSN QNNFVHDCVNITVKQHTVTT TTKGENFTETDIKIMERVVE QMCITQYQQESQAAYQRA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	317
15N chemical shifts	125
1H chemical shifts	715

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	single chain polymers	1

Entities:

Entity 1, single chain polymers 138 residues - 12512.979 Da.

1

GLN

GLY

THR

HIS

ASN

GLN

TRP

GLY

LYS

2

PRO

SER

LYS

PRO

LYS

THR

SER

MET

LYS

HIS

3

VAL

ALA

PRO

ALA

GLY

ALA

VAL

4

VAL

GLY

LEU

GLY

TYR

MET

LEU

GLY

5

SER

ALA

MET

SER

ARG

PRO

LEU

ILE

HIS

PHE

6

GLY

ASN

ASP

TYR

GLU

ASP

ARG

TYR

ARG

7

GLU

ASN

MET

TYR

ARG

TYR

PRO

ASN

GLN

VAL

8

TYR

ARG

PRO

VAL

ASP

GLN

TYR

SER

ASN

9

GLN

ASN

PHE

VAL

HIS

ASP

CYS

VAL

ASN

10

ILE

THR

VAL

LYS

GLN

HIS

THR

VAL

THR

11

THR

LYS

GLY

GLU

ASN

PHE

THR

GLU

THR

12

ASP

ILE

LYS

ILE

MET

GLU

ARG

VAL

GLU

13

GLN

MET

CYS

ILE

THR

GLN

TYR

GLN

GLU

14

SER

GLN

ALA

TYR

GLN

ARG

ALA

Samples:

sample_1: rpp S173N, [U-13C; U-15N], 0.8 – 1 mM; sodium acetate 20 mM

sample_2: rpp S173N, [U-15N], 0.8 – 1 mM; sodium acetate 20 mM

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298.13 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15399 16328 16616
PDB	1TQB 1TQC 2FJ3 2JOH 2JOM 3O79
EMBL	CBK44083
GB	AAC48697 AAD01554 AAQ81748 AAQ81756 ABL75505
REF	NP_001075490 XP_008254357 XP_008254358
SP	Q95211
AlphaFold	Q95211