BMRB Entry 27259

Name: 1H, 15N, 13C resonance assignments for Human prion protein (91-231): mutant V127M129 (scilicet HuPrPG127V)
Published: 2017-10-20

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27259

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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, 15N, 13C resonance assignments for Human prion protein (91-231): mutant V127M129 (scilicet HuPrPG127V)

Deposition date:

2017-09-20

Original release date:

2017-10-20

Authors:

Zheng, Zhen; Lin, Donghai; Feng, Liubin

Citation:

Citation: Zheng, Zhen; Zhang, Meilan; Wang, Yongheng; Ma, Rongsheng; Guo, Chenyun; Feng, Liubin; Wu, Jihui; Yao, Hongwei; Lin, Donghai. "Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease" Sci. Rep. 8, 13211-13211 (2018).
PubMed: 30181558

Assembly members:

Assembly members:
HuPrPG127V, polymer, 142 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuPrPG127V: MQGGGTHSQWNKPSKPKTNM KHMAGAAAAGAVVGGLGVYM LGSAMSRPIIHFGSDYEDRY YRENMHRYPNQVYYRPMDEY SNQNNFVHDCVNITIKQHTV TTTTKGENFTETDVKMMERV VEQMCITQYERESQAYYQRG SS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	532
15N chemical shifts	147
1H chemical shifts	900

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HuPrPG127V	1

Entities:

Entity 1, HuPrPG127V 142 residues - Formula weight is not available

1

MET

GLN

GLY

THR

HIS

SER

GLN

TRP

2

ASN

LYS

PRO

SER

LYS

PRO

LYS

THR

ASN

MET

3

LYS

HIS

MET

ALA

GLY

ALA

GLY

4

ALA

VAL

GLY

LEU

GLY

VAL

TYR

MET

5

LEU

GLY

SER

ALA

MET

SER

ARG

PRO

ILE

6

HIS

PHE

GLY

SER

ASP

TYR

GLU

ASP

ARG

TYR

7

TYR

ARG

GLU

ASN

MET

HIS

ARG

TYR

PRO

ASN

8

GLN

VAL

TYR

ARG

PRO

MET

ASP

GLU

TYR

9

SER

ASN

GLN

ASN

PHE

VAL

HIS

ASP

CYS

10

VAL

ASN

ILE

THR

ILE

LYS

GLN

HIS

THR

VAL

11

THR

LYS

GLY

GLU

ASN

PHE

THR

12

GLU

THR

ASP

VAL

LYS

MET

GLU

ARG

VAL

13

VAL

GLU

GLN

MET

CYS

ILE

THR

GLN

TYR

GLU

14

ARG

GLU

SER

GLN

ALA

TYR

GLN

ARG

GLY

15

SER

Samples:

sample_1: HuPrPG127V, [U-100% 13C; U-100% 15N], 0.5 mM; NaOAc 20 mM; NaN3 0.2%

sample_conditions_1: ionic strength: 0.02 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 850 MHz

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