BMRB Entry 27380

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27380

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Title:
Assignment of the 1H, 13C, and 15N resonances of ataxin-3
Deposition date:
2018-01-23
Original release date:
2018-08-16
Authors:
Sicorello, Alessandro; Kelly, Geoffry; Oregioni, Alain; Novacek, Jiri; Pastore, Annalisa
Citation:

Citation: Sicorello, Alessandro; Kelly, Geoff; Oregioni, Alain; Novacek, Jiri; Sklenar, Vladimir; Pastore, Annalisa. "The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3."  Biophys. J. 115, 59-71 (2018).
PubMed: 29972812

Assembly members:

Assembly members:
ataxin-3, polymer, 362 residues, 41307.09 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: pMht

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ataxin-3: GMESIFHEKQEGSLCAQHCL NNLLQGEYFSPVELSSIAHQ LDEEERMRMAEGGVTSEDYR TFLQQPSGNMDDSGFFSIQV ISNALKVWGLELILFNSPEY QRLRIDPINERSFICNYKEH WFTVRKLGKQWFNLNSLLTG PELISDTYLALFLAQLQQEG YSIFVVKGDLPDCEADQLLQ MIRVQQMHRPKLIGEELAQL KEQRVHKTDLERVLEANDGS GMLDEDEEDLQRALALSRQE IDMEDEEADLRRAIQLSMQG SSRNISQDMTQTSGTNLTSE ELRKRREAYFEKQQQKQQQQ QQQQQQGDLSGQSSHPCERP ATSSGALGSDLGDAMSEEDM LQAAVTMSLETVRNDLKTEG KK

Data sets:
Data typeCount
13C chemical shifts316
15N chemical shifts316
1H chemical shifts316

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ataxin-31

Entities:

Entity 1, ataxin-3 362 residues - 41307.09 Da.

1   GLYMETGLUSERILEPHEHISGLULYSGLN
2   GLUGLYSERLEUCYSALAGLNHISCYSLEU
3   ASNASNLEULEUGLNGLYGLUTYRPHESER
4   PROVALGLULEUSERSERILEALAHISGLN
5   LEUASPGLUGLUGLUARGMETARGMETALA
6   GLUGLYGLYVALTHRSERGLUASPTYRARG
7   THRPHELEUGLNGLNPROSERGLYASNMET
8   ASPASPSERGLYPHEPHESERILEGLNVAL
9   ILESERASNALALEULYSVALTRPGLYLEU
10   GLULEUILELEUPHEASNSERPROGLUTYR
11   GLNARGLEUARGILEASPPROILEASNGLU
12   ARGSERPHEILECYSASNTYRLYSGLUHIS
13   TRPPHETHRVALARGLYSLEUGLYLYSGLN
14   TRPPHEASNLEUASNSERLEULEUTHRGLY
15   PROGLULEUILESERASPTHRTYRLEUALA
16   LEUPHELEUALAGLNLEUGLNGLNGLUGLY
17   TYRSERILEPHEVALVALLYSGLYASPLEU
18   PROASPCYSGLUALAASPGLNLEULEUGLN
19   METILEARGVALGLNGLNMETHISARGPRO
20   LYSLEUILEGLYGLUGLULEUALAGLNLEU
21   LYSGLUGLNARGVALHISLYSTHRASPLEU
22   GLUARGVALLEUGLUALAASNASPGLYSER
23   GLYMETLEUASPGLUASPGLUGLUASPLEU
24   GLNARGALALEUALALEUSERARGGLNGLU
25   ILEASPMETGLUASPGLUGLUALAASPLEU
26   ARGARGALAILEGLNLEUSERMETGLNGLY
27   SERSERARGASNILESERGLNASPMETTHR
28   GLNTHRSERGLYTHRASNLEUTHRSERGLU
29   GLULEUARGLYSARGARGGLUALATYRPHE
30   GLULYSGLNGLNGLNLYSGLNGLNGLNGLN
31   GLNGLNGLNGLNGLNGLNGLYASPLEUSER
32   GLYGLNSERSERHISPROCYSGLUARGPRO
33   ALATHRSERSERGLYALALEUGLYSERASP
34   LEUGLYASPALAMETSERGLUGLUASPMET
35   LEUGLNALAALAVALTHRMETSERLEUGLU
36   THRVALARGASNASPLEULYSTHRGLUGLY
37   LYSLYS

Samples:

sample_1: ataxin-3, [U-100% 13C; U-100% 15N], 0.250 mM; sodium phosphate 20 mM; TCEP 2 mM

sample: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample
3D HNCACBsample_1isotropicsample
5D HNCaCONHsample_1isotropicsample
5D HabCabCONHsample_1isotropicsample
3D HNCOsample_1isotropicsample

Software:

CCPNMR v2.4.2, CCPN - chemical shift assignment, peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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