BMRB Entry 26697

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26697

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Title:
Denatured CSE4 Protein from Saccharomyces cerevisiae
Deposition date:
2015-10-27
Original release date:
2016-09-09
Authors:
Malik, Nikita; Kumar, Ashutosh
Citation:

Citation: Malik, Nikita; Kumar, Ashutosh. "Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state"  J. Biomol. NMR 66, 21-35 (2016).
PubMed: 27586017

Assembly members:

Assembly members:
CSE4_protein, polymer, 229 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pKS387

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CSE4_protein: MSSKQQWVSSAIQSDSSGRS LSNVNRLAGDQQSINDRALS LLQRTRATKNLFPRREERRR YESSKSDLDIETDYEDQAGN LEIETENEEEAEMETEVPAP VRTHSYALDRYVRQKRREKQ RKQSLKRVEKKYTPSELALY EIRKYQRSTDLLISKIPFAR LVKEVTDEFTTKDQDLRWQS MAIMALQEASEAYLVGLLEH TNLLALHAKRITIMKKDMQL ARRIRGQFI

Data sets:
Data typeCount
13C chemical shifts901
15N chemical shifts218
1H chemical shifts879

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CSE4 protein1

Entities:

Entity 1, CSE4 protein 229 residues - Formula weight is not available

1   METSERSERLYSGLNGLNTRPVALSERSER
2   ALAILEGLNSERASPSERSERGLYARGSER
3   LEUSERASNVALASNARGLEUALAGLYASP
4   GLNGLNSERILEASNASPARGALALEUSER
5   LEULEUGLNARGTHRARGALATHRLYSASN
6   LEUPHEPROARGARGGLUGLUARGARGARG
7   TYRGLUSERSERLYSSERASPLEUASPILE
8   GLUTHRASPTYRGLUASPGLNALAGLYASN
9   LEUGLUILEGLUTHRGLUASNGLUGLUGLU
10   ALAGLUMETGLUTHRGLUVALPROALAPRO
11   VALARGTHRHISSERTYRALALEUASPARG
12   TYRVALARGGLNLYSARGARGGLULYSGLN
13   ARGLYSGLNSERLEULYSARGVALGLULYS
14   LYSTYRTHRPROSERGLULEUALALEUTYR
15   GLUILEARGLYSTYRGLNARGSERTHRASP
16   LEULEUILESERLYSILEPROPHEALAARG
17   LEUVALLYSGLUVALTHRASPGLUPHETHR
18   THRLYSASPGLNASPLEUARGTRPGLNSER
19   METALAILEMETALALEUGLNGLUALASER
20   GLUALATYRLEUVALGLYLEULEUGLUHIS
21   THRASNLEULEUALALEUHISALALYSARG
22   ILETHRILEMETLYSLYSASPMETGLNLEU
23   ALAARGARGILEARGGLYGLNPHEILE

Samples:

sample_1: urea 8 M; sodium acetate 20 mM; sodium chloride 200 mM; EDTA 1 mM; beta-mercaptoethanol 5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CACABsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 750 MHz

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