BMRB Entry 15676

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15676
MolProbity Validation Chart

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Title:
NMR Studies of a Pathogenic Mutant (D178N) of the Human Prion Protein
Deposition date:
2008-02-29
Original release date:
2009-11-30
Authors:
Mills, Jeffrey; Surewicz, Krystyna; Surewicz, Witold; Sonnichsen, Frank
Citation:

Citation: Mills, Jeffrey; Surewicz, Krystyna; Surewicz, Witold; Sonnichsen, Frank. "Null"  .

Assembly members:

Assembly members:
V129/D178N_prion_protein, polymer, 146 residues, 16471.2 Da.

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: pRSETB

Entity Sequences (FASTA):

Entity Sequences (FASTA):
V129/D178N_prion_protein: GSDPGQGGGTHSQWNKPSKP KTNMKHMAGAAAAGAVVGGL GGYVLGSAMSRPIIHFGSDY EDRYYRENMHRYPNQVYYRP MDEYSNQNNFVHNCVNITIK QHTVTTTTKGENFTETDVKM MERVVEQMCITQYERESQAY YQRGSS

Data sets:
Data typeCount
13C chemical shifts301
15N chemical shifts117
1H chemical shifts635

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1

Entities:

Entity 1, monomer 146 residues - 16471.2 Da.

Expressed protein contained residues 90-231 (plus GSDP cloning artifact), but only residues 125-231 are deposited

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

Samples:

sample_1: V129/D178N prion protein, [U-99% 13C; U-99% 15N], 350 uM; sodium acetate 10 mM; sodium azide 100 uM

sample_conditions_1: ionic strength: 20 mM; pH: 4.6; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich, Herrmann, Guntert and Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

  • BRUKER Avance 600 MHz

Related Database Links:

BMRB 16743 16757 17714 17756 17780 18426 18550 19268 4379 4434 4641
PDB
DBJ BAF62360 BAG32277 BAG32279 BAG35206 BAG52189
EMBL CAG46869
GB AAA68632 AAA68633 AAC50085 AAC50088 AAC50089
REF NP_001009093 NP_001103676 XP_003278028 XP_003278029 XP_003278030
SP P40252 P61766 P61767 P61768
AlphaFold P40252 P61766 P61767 P61768

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