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 16743

Title: Three dimensional structure of HuPrP(90-231 M129 Q212P)   PubMed: 20661422

Authors: Ilc, Gregor; Giachin, Gabriele; Jaremko, Mariusz; Jaremko, Lukasz; Zhukov, Igor; Plavec, Janez; Legname, Guiseppe

Citation: Ilc, Gregor; Giachin, Gabriele; Jaremko, Mariusz; Jaremko, Lukasz; Benetti, Federico; Plavec, Janez; Zhukov, Igor; Legname, Guiseppe. "NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features"  PLoS One 5, e11715-e11715 (2010).

Assembly members:
HuPrP(90-231 M129 Q212P), polymer, 148 residues, 16966.982 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(90-231 M129 Q212P): GQGGGTHSQWNKPSKPKTNM KHMAGAAAAGAVVGGLGGYM LGSAMSRPIIHFGSDYEDRY YRENMHRYPNQVYYRPMDEY SNQNNFVHDCVNITIKQHTV TTTTKGENFTETDVKMMERV VEPMCITQYERESQAYYQRG SSHHHHHH

Data sets:
Data typeCount
13C chemical shifts610
15N chemical shifts147
1H chemical shifts942

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HuPrP(90-231 M129 Q212P)1

Entities:

Entity 1, HuPrP(90-231 M129 Q212P) 148 residues - 16966.982 Da.

His-Tag6 on C-terminus

1   GLYGLNGLYGLYGLYTHRHISSERGLNTRP
2   ASNLYSPROSERLYSPROLYSTHRASNMET
3   LYSHISMETALAGLYALAALAALAALAGLY
4   ALAVALVALGLYGLYLEUGLYGLYTYRMET
5   LEUGLYSERALAMETSERARGPROILEILE
6   HISPHEGLYSERASPTYRGLUASPARGTYR
7   TYRARGGLUASNMETHISARGTYRPROASN
8   GLNVALTYRTYRARGPROMETASPGLUTYR
9   SERASNGLNASNASNPHEVALHISASPCYS
10   VALASNILETHRILELYSGLNHISTHRVAL
11   THRTHRTHRTHRLYSGLYGLUASNPHETHR
12   GLUTHRASPVALLYSMETMETGLUARGVAL
13   VALGLUPROMETCYSILETHRGLNTYRGLU
14   ARGGLUSERGLNALATYRTYRGLNARGGLY
15   SERSERHISHISHISHISHISHIS

Samples:

sample_1: PrP(Q212P), [U-98% 13C; U-98% 15N], 1.0 mM; H2O 90%; D2O 10%; NaCl 150 mM

sample_2: PrP(Q212P), [U-98% 13C; U-98% 15N], 1.0 mM; D2O 100%; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 5.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
3D CCH-TOCSYsample_2isotropicsample_conditions_2

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz
  • Varian Uniform NMR System 700 MHz

Related Database Links:

BMRB 15676 16757 17714 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