BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17714

Title: human prion protein mutant HuPrP(90-231, M129, V210I)   PubMed: 21839748

Deposition date: 2011-06-16 Original release date: 2011-08-19

Authors: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Raspadori, Andrea; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe

Citation: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Raspadori, Andrea; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe. "Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation."  J. Mol. Biol. 412, 660-673 (2011).

Assembly members:
HuPrP, polymer, 147 residues, 16654.660 Da.

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):
HuPrP: GAMDPGQGGGTHSQWNKPSK PKTNMKHMAGAAAAGAVVGG LGGYMLGSAMSRPIIHFGSD YEDRYYRENMHRYPNQVYYR PMDEYSNQNNFVHDCVNITI KQHTVTTTTKGENFTETDVK MMERVIEQMCITQYERESQA YYQRGSS

Data sets:
Data typeCount
13C chemical shifts459
15N chemical shifts149
1H chemical shifts928

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HuPrP1

Entities:

Entity 1, HuPrP 147 residues - 16654.660 Da.

Gly85-Pro89 nonnative

1   GLYALAMETASPPROGLYGLNGLYGLYGLY
2   THRHISSERGLNTRPASNLYSPROSERLYS
3   PROLYSTHRASNMETLYSHISMETALAGLY
4   ALAALAALAALAGLYALAVALVALGLYGLY
5   LEUGLYGLYTYRMETLEUGLYSERALAMET
6   SERARGPROILEILEHISPHEGLYSERASP
7   TYRGLUASPARGTYRTYRARGGLUASNMET
8   HISARGTYRPROASNGLNVALTYRTYRARG
9   PROMETASPGLUTYRSERASNGLNASNASN
10   PHEVALHISASPCYSVALASNILETHRILE
11   LYSGLNHISTHRVALTHRTHRTHRTHRLYS
12   GLYGLUASNPHETHRGLUTHRASPVALLYS
13   METMETGLUARGVALILEGLUGLNMETCYS
14   ILETHRGLNTYRGLUARGGLUSERGLNALA
15   TYRTYRGLNARGGLYSERSER

Samples:

sample_1: HuPrP, [U-100% 13C; U-100% 15N], 0.6 mM; sodium acetate 20 mM; H2O 90%; D2O 10%

sample_2: HuPrP, [U-100% 13C; U-100% 15N], 0.6 mM; sodium acetate 20 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pD: 5.9; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.115, Goddard - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA v11.5.22, (YASARA) - refinement

ProcheckNMR, Laskowski and MacArthur - data analysis

WhatIF, Vriend - data analysis

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

Related Database Links:

BMRB 15676 16743 16757 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4641 4736
PDB
DBJ BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL CAA58442 CAG46836 CAG46869
GB AAA19664 AAA60182 AAA68632 AAA68633 AAB59442
REF NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP P04156 P40252 P61766 P61767 P61768

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