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 4641

Title: Human Prion Protein Mutant E200K Fragment 90-231

Authors: Zhang, Y.; Swietnicki, W.; Zagorski, M.; Surewicz, W.; Soennichsen, F.

Citation: Zhang, Y.; Swietnicki, W.; Zagorski, M.; Surewicz, W.; Soennichsen, F.. "Solution structure of Human Prion Protein Mutant E200K Fragment 90-231"  J. Biol. Chem. 275, 33650-33654 (2000).

Assembly members:
PRION PROTEIN, polymer, 146 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):
PRION PROTEIN: GSDPGQGGGTHSQWNKPSKP KTNMKHMAGAAAAGAVVGGL GGYMLGSAMSRPIIHFGSDY EDRYYRENMHRYPNQVYYRP MDEYSNQNNFVHDCVNITIK QHTVTTTTKGENFTKTDVKM MERVVEQMCITQYERESQAY YQRGSS

Data sets:
Data typeCount
13C chemical shifts593
1H chemical shifts929
15N chemical shifts162
coupling constants44

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PRION PROTEIN1

Entities:

Entity 1, PRION PROTEIN 146 residues - Formula weight is not available

1   GLYSERASPPROGLYGLNGLYGLYGLYTHR
2   HISSERGLNTRPASNLYSPROSERLYSPRO
3   LYSTHRASNMETLYSHISMETALAGLYALA
4   ALAALAALAGLYALAVALVALGLYGLYLEU
5   GLYGLYTYRMETLEUGLYSERALAMETSER
6   ARGPROILEILEHISPHEGLYSERASPTYR
7   GLUASPARGTYRTYRARGGLUASNMETHIS
8   ARGTYRPROASNGLNVALTYRTYRARGPRO
9   METASPGLUTYRSERASNGLNASNASNPHE
10   VALHISASPCYSVALASNILETHRILELYS
11   GLNHISTHRVALTHRTHRTHRTHRLYSGLY
12   GLUASNPHETHRLYSTHRASPVALLYSMET
13   METGLUARGVALVALGLUGLNMETCYSILE
14   THRGLNTYRGLUARGGLUSERGLNALATYR
15   TYRGLNARGGLYSERSER

Samples:

sample_1: PRION PROTEIN, [U-15N; U-13C], 0.8 mM; acetate buffer 10 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 4.6; temperature: 299 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablesample_cond_1
3D 15N-separated NOESYsample_1not availablesample_cond_1
2D NOESYsample_1not availablesample_cond_1
HNHAsample_1not availablesample_cond_1

Software:

NMRPipe vsgi6x.m4 - processing

FELIX v98 - processing

PIPP v4.24 - data analysis

ARIA v0.9 - structure solution

CNS v0.9 - structure solution, refinement

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

BMRB 15676 16743 16757 17714 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4736
PDB
DBJ BAF62360 BAG32276 BAG32278 BAG52189 BAG56832
EMBL CAA58442 CAG46836
GB AAA60182 AAA68632 AAB59442 AAB59443 AAC05365
REF NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP P04156 P61766 P61767 P61768