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Biological Magnetic Resonance Data Bank


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BMRB Entry 34236

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34236
MolProbity Validation Chart

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Title: Solution structure of mule deer prion protein with polymorphism S138

Deposition date: 2018-02-05 Original release date: 2019-08-23

Authors: Slapsak, Urska; Ilc, Gregor; Plavec, Janez

Citation: Slapsak, Urska; Ilc, Gregor; Plavec, Janez. "Solution structure of mule deer prion protein with polymorphism S138"  .

Assembly members:
Major prion protein, polymer, 140 residues, 16008.847 Da.

Natural source:   Common Name: Mule deer   Taxonomy ID: 9872   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Odocoileus hemionus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Major prion protein: GQGGTHSQWNKPSKPKTNMK HVAGAAAAGAVVGGLGGYML GSAMSRPLIHFGNDYEDRYY RENMYRYPNQVYYRPVDQYN NQNTFVHDCVNITVKQHTVT TTTKGENFTETDIKMMERVV EQMCITQYQRESQAYYQRGA

Data sets:
Data typeCount
13C chemical shifts473
15N chemical shifts153
1H chemical shifts951

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 140 residues - 16008.847 Da.

1   GLYGLNGLYGLYTHRHISSERGLNTRPASN
2   LYSPROSERLYSPROLYSTHRASNMETLYS
3   HISVALALAGLYALAALAALAALAGLYALA
4   VALVALGLYGLYLEUGLYGLYTYRMETLEU
5   GLYSERALAMETSERARGPROLEUILEHIS
6   PHEGLYASNASPTYRGLUASPARGTYRTYR
7   ARGGLUASNMETTYRARGTYRPROASNGLN
8   VALTYRTYRARGPROVALASPGLNTYRASN
9   ASNGLNASNTHRPHEVALHISASPCYSVAL
10   ASNILETHRVALLYSGLNHISTHRVALTHR
11   THRTHRTHRLYSGLYGLUASNPHETHRGLU
12   THRASPILELYSMETMETGLUARGVALVAL
13   GLUGLNMETCYSILETHRGLNTYRGLNARG
14   GLUSERGLNALATYRTYRGLNARGGLYALA

Samples:

sample_1: mdPrP(S138), [U-99% 13C; U-99% 15N], 0.48 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0 Not defined; pH: 5.5; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

YASARA NOVA, Krieger, E. et al - refinement

CYANA v3.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.9.1b18, Keller and Wuthrich - chemical shift assignment

SPARKY v3.114, Goddard - peak picking

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

PSVS, Bhattacharya and Montelione - data analysis

Analysis, CCPN - data analysis

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

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