BMRB Entry 15714

Title:
Backbone chemical shift assignements for monomeric apoSOD1 - variant D90A
Deposition date:
2008-04-03
Original release date:
2009-10-01
Authors:
Teilum, Kaare; Akke, Mikael
Citation:

Citation: Teilum, Kaare; Smith, Melanie; Schulz, Eike; Christensen, Lea; Solomentsev, Gleb; Oliveberg, Mikael; Akke, Mikael. "Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization."  Proc. Natl. Acad. Sci. U.S.A. 106, 18273-18278 (2009).
PubMed: 19828437

Assembly members:

Assembly members:
SOD1, polymer, 153 residues, Formula weight is not available

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: N/A

Data sets:
Data typeCount
13C chemical shifts154
15N chemical shifts146
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1chain 1, proline cis conformer1
2chain 2, proline trans conformer1

Entities:

Entity 1, chain 1, proline cis conformer 153 residues - Formula weight is not available

1   ALATHRLYSALAVALALAVALLEULYSGLY
2   ASPGLYPROVALGLNGLYILEILEASNPHE
3   GLUGLNLYSGLUSERASNGLYPROVALLYS
4   VALTRPGLYSERILELYSGLYLEUTHRGLU
5   GLYLEUHISGLYPHEHISVALHISGLUGLU
6   GLUASPASNTHRALAGLYCYSTHRSERALA
7   GLYPROHISPHEASNPROLEUSERARGLYS
8   HISGLYGLYPROLYSASPGLUGLUARGHIS
9   VALGLYASPLEUGLYASNVALTHRALAALA
10   LYSASPGLYVALALAASPVALSERILEGLU
11   ASPSERVALILESERLEUSERGLYASPHIS
12   ALAILEILEGLYARGTHRLEUVALVALHIS
13   GLULYSALAASPASPLEUGLYLYSGLYGLY
14   ASNGLUGLUSERTHRLYSTHRGLYASNALA
15   GLYSERARGLEUALACYSGLYVALILEGLY
16   ILEALAGLN

Samples:

sample_1: SOD1, [U-100% 13C; U-100% 15N], 1 mM; MES 10 mM; EDTA 1 mM; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15711 15712 15713 18509 18708 18968 26570 4202
PDB
GB AAA72747 AAA80237

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