BMRB Entry 17570

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17570

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Title:
Solid-state NMR assignment of the C-terminal domain of the Ure2p prion in its fibrillar form
Deposition date:
2011-04-01
Original release date:
2012-06-19
Authors:
Habenstein, Birgit; Wasmer, Christian; Bousset, Luc; Sourigues, Yannick; Loquet, Antoine; Meier, Beat; Melki, Ronald; Bockmann, Anja
Citation:

Citation: Habenstein, Birgit; Wasmer, Christian; Bousset, Luc; Sourigues, Yannick; Schutz, Anne; Loquet, Antoine; Meier, Beat; Melki, Ronald; Bockmann, Anja. "Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion."  J. Biomol. NMR 51, 235-243 (2011).
PubMed: 21805376

Assembly members:

Assembly members:
Ure2p prion, polymer, 354 residues, 40270.77 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 3A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ure2p prion: MMNNNGNQVSNLSNALRQVN IGNRNSNTTTDQSNINFEFS TGVNNNNNNNSSSNNNNVQN NNSGRNGSQNNDNENNIKNT LEQHRQQQQAFSDMSHVEYS RITKFFQEQPLEGYTLFSHR SAPNGFKVAIVLSELGFHYN TIFLDFNLGEHRAPEFVSVN PNARVPALIDHGMDNLSIWE SGAILLHLVNKYYKETGNPL LWSDDLADQSQINAWLFFQT SGHAPMIGQALHFRYFHSQK IASAVERYTDEVRRVYGVVE MALAERREALVMELDTENAA AYSAGTTPMSQSRFFDYPVW LVGDKLTIADLAFVPWNNVV DRIGINIKIEFPEVYKWTKH MMRRPAVIKALRGE

Data sets:
Data typeCount
13C chemical shifts527
15N chemical shifts167

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ure2p1

Entities:

Entity 1, Ure2p 354 residues - 40270.77 Da.

1   METMETASNASNASNGLYASNGLNVALSER
2   ASNLEUSERASNALALEUARGGLNVALASN
3   ILEGLYASNARGASNSERASNTHRTHRTHR
4   ASPGLNSERASNILEASNPHEGLUPHESER
5   THRGLYVALASNASNASNASNASNASNASN
6   SERSERSERASNASNASNASNVALGLNASN
7   ASNASNSERGLYARGASNGLYSERGLNASN
8   ASNASPASNGLUASNASNILELYSASNTHR
9   LEUGLUGLNHISARGGLNGLNGLNGLNALA
10   PHESERASPMETSERHISVALGLUTYRSER
11   ARGILETHRLYSPHEPHEGLNGLUGLNPRO
12   LEUGLUGLYTYRTHRLEUPHESERHISARG
13   SERALAPROASNGLYPHELYSVALALAILE
14   VALLEUSERGLULEUGLYPHEHISTYRASN
15   THRILEPHELEUASPPHEASNLEUGLYGLU
16   HISARGALAPROGLUPHEVALSERVALASN
17   PROASNALAARGVALPROALALEUILEASP
18   HISGLYMETASPASNLEUSERILETRPGLU
19   SERGLYALAILELEULEUHISLEUVALASN
20   LYSTYRTYRLYSGLUTHRGLYASNPROLEU
21   LEUTRPSERASPASPLEUALAASPGLNSER
22   GLNILEASNALATRPLEUPHEPHEGLNTHR
23   SERGLYHISALAPROMETILEGLYGLNALA
24   LEUHISPHEARGTYRPHEHISSERGLNLYS
25   ILEALASERALAVALGLUARGTYRTHRASP
26   GLUVALARGARGVALTYRGLYVALVALGLU
27   METALALEUALAGLUARGARGGLUALALEU
28   VALMETGLULEUASPTHRGLUASNALAALA
29   ALATYRSERALAGLYTHRTHRPROMETSER
30   GLNSERARGPHEPHEASPTYRPROVALTRP
31   LEUVALGLYASPLYSLEUTHRILEALAASP
32   LEUALAPHEVALPROTRPASNASNVALVAL
33   ASPARGILEGLYILEASNILELYSILEGLU
34   PHEPROGLUVALTYRLYSTRPTHRLYSHIS
35   METMETARGARGPROALAVALILELYSALA
36   LEUARGGLYGLU

Samples:

sample_1: Ure2p, [U-100% 13C; U-100% 15N], 10-30 mg; KCl 75 mM; TRIS 20 mM; EGTA 1 mM; dithiothreitol 1 mM; DSS 0.5 mg; H2O 100%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D NCACB (DREAM)sample_1solidsample_conditions_1
3D CCCsample_1solidsample_conditions_1
3D CAN(CO)CAsample_1solidsample_conditions_1

Software:

ANALYSIS v2.1.1, CCPN - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

BMRB 17499
PDB
DBJ GAA25878
EMBL CAA93369 CAA96134 CAY82378
GB AAA35201 AAK51641 AAM91938 AAM93167 AAM93168
REF NP_014170
SP P23202 Q7LLZ8
TPG DAA10329
AlphaFold P23202 Q7LLZ8