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 17473

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17473

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Title: Backbone 1H and 15N Chemical Shift Assignments for chimeric fusion of S. cerevisiae and C. albicans Sup35   PubMed: 21333653

Deposition date: 2011-02-16 Original release date: 2011-03-07

Authors: Foo, Catherine; Kelly, Mark; Jonathan, Weissman

Citation: Foo, Catherine; Ohhashi, Yumiko; Kelly, Mark; Tanaka, Motomasa; Weissman, Jonathan. "Radically different amyloid conformations dictate the seeding specificity of a chimeric sup35 prion."  J. Mol. Biol. 408, 1-8 (2011).

Assembly members:
SC/CA_Sup35_chimera, polymer, 274 residues, Formula weight is not available

Natural source:   Common Name: yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
SC/CA_Sup35_chimera: MSDSNQGNNQQNYQQYSQNG NQQQGNNRYQGYQAYNAQAQ SFVPQGGYQQFQQFQPQQQQ QQYGGYNQYNQYQGGYQQNY NNRGGYQQGYNNRGGYQQNY NNRGGYQGYNQNQQYGGYQQ YNSQPQQQQQQQSQGMSLND FQKQQKQAAPKPKKTLKLVS SSGIKLANATKKVGTKPAES DKKEEEKSAETKEPTKEPTK VEEPVKKEEKPVQTEEKTEE KSELPKVEDLKISESTHNTN NANVTSADALIKEQEEEVDD EVVNDHHHHHHHHH

Data sets:
Data typeCount
15N chemical shifts146
1H chemical shifts140

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Chimera monomer1

Entities:

Entity 1, Chimera monomer 274 residues - Formula weight is not available

1   METSERASPSERASNGLNGLYASNASNGLN
2   GLNASNTYRGLNGLNTYRSERGLNASNGLY
3   ASNGLNGLNGLNGLYASNASNARGTYRGLN
4   GLYTYRGLNALATYRASNALAGLNALAGLN
5   SERPHEVALPROGLNGLYGLYTYRGLNGLN
6   PHEGLNGLNPHEGLNPROGLNGLNGLNGLN
7   GLNGLNTYRGLYGLYTYRASNGLNTYRASN
8   GLNTYRGLNGLYGLYTYRGLNGLNASNTYR
9   ASNASNARGGLYGLYTYRGLNGLNGLYTYR
10   ASNASNARGGLYGLYTYRGLNGLNASNTYR
11   ASNASNARGGLYGLYTYRGLNGLYTYRASN
12   GLNASNGLNGLNTYRGLYGLYTYRGLNGLN
13   TYRASNSERGLNPROGLNGLNGLNGLNGLN
14   GLNGLNSERGLNGLYMETSERLEUASNASP
15   PHEGLNLYSGLNGLNLYSGLNALAALAPRO
16   LYSPROLYSLYSTHRLEULYSLEUVALSER
17   SERSERGLYILELYSLEUALAASNALATHR
18   LYSLYSVALGLYTHRLYSPROALAGLUSER
19   ASPLYSLYSGLUGLUGLULYSSERALAGLU
20   THRLYSGLUPROTHRLYSGLUPROTHRLYS
21   VALGLUGLUPROVALLYSLYSGLUGLULYS
22   PROVALGLNTHRGLUGLULYSTHRGLUGLU
23   LYSSERGLULEUPROLYSVALGLUASPLEU
24   LYSILESERGLUSERTHRHISASNTHRASN
25   ASNALAASNVALTHRSERALAASPALALEU
26   ILELYSGLUGLNGLUGLUGLUVALASPASP
27   GLUVALVALASNASPHISHISHISHISHIS
28   HISHISHISHIS

Samples:

sample_1: SC/CA Sup35 chimera, [U-99% 13C; U-99% 15N], .135 nM; DMSO 100%

sample_conditions_1: pH: 5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 500 MHz

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