BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27259

Title: 1H, 15N, 13C resonance assignments for Human prion protein (91-231): mutant V127M129 (scilicet HuPrPG127V)   PubMed: 30181558

Deposition date: 2017-09-20 Original release date: 2017-10-20

Authors: Zheng, Zhen; Lin, Donghai; Feng, Liubin

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts147
1H chemical shifts900

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HuPrPG127V1

Entities:

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

1   METGLNGLYGLYGLYTHRHISSERGLNTRP
2   ASNLYSPROSERLYSPROLYSTHRASNMET
3   LYSHISMETALAGLYALAALAALAALAGLY
4   ALAVALVALGLYGLYLEUGLYVALTYRMET
5   LEUGLYSERALAMETSERARGPROILEILE
6   HISPHEGLYSERASPTYRGLUASPARGTYR
7   TYRARGGLUASNMETHISARGTYRPROASN
8   GLNVALTYRTYRARGPROMETASPGLUTYR
9   SERASNGLNASNASNPHEVALHISASPCYS
10   VALASNILETHRILELYSGLNHISTHRVAL
11   THRTHRTHRTHRLYSGLYGLUASNPHETHR
12   GLUTHRASPVALLYSMETMETGLUARGVAL
13   VALGLUGLNMETCYSILETHRGLNTYRGLU
14   ARGGLUSERGLNALATYRTYRGLNARGGLY
15   SERSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts