BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25942

Title: Full-length WT SOD1 in DPC MICELLE   PubMed: 27378311

Deposition date: 2016-01-06 Original release date: 2016-12-08

Authors: Lim, Liangzhong; Song, Jianxing

Citation: Lim, Liangzhong; Song, Jianxing. "SALS-linked WT-SOD1 adopts a highly similar helical conformation as FALS-causing L126Z-SOD1 in a membrane environment"  Biochim. Biophys. Acta 1858, 2223-2230 (2016).

Assembly members:
entity, polymer, 161 residues, 15827.688 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity: MGHHHHHHATKAVCVLKGDG PVQGIINFEQKESNGPVKVW GSIKGLTEGLHGFHVHEFGD NTAGCTSAGPHFNPLSRKHG GPKDEERHVGDLGNVTADKD GVADVSIEDSVISLSGDHCI IGRTLVVHEKADDLGKGGNE ESTKTGNAGSRLACGVIGIA Q

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts158
1H chemical shifts721

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 161 residues - 15827.688 Da.

Residue 1-8 are the non-native affinity 6xHis-tag of full-length SOD1

1   METGLYHISHISHISHISHISHISALATHR
2   LYSALAVALCYSVALLEULYSGLYASPGLY
3   PROVALGLNGLYILEILEASNPHEGLUGLN
4   LYSGLUSERASNGLYPROVALLYSVALTRP
5   GLYSERILELYSGLYLEUTHRGLUGLYLEU
6   HISGLYPHEHISVALHISGLUPHEGLYASP
7   ASNTHRALAGLYCYSTHRSERALAGLYPRO
8   HISPHEASNPROLEUSERARGLYSHISGLY
9   GLYPROLYSASPGLUGLUARGHISVALGLY
10   ASPLEUGLYASNVALTHRALAASPLYSASP
11   GLYVALALAASPVALSERILEGLUASPSER
12   VALILESERLEUSERGLYASPHISCYSILE
13   ILEGLYARGTHRLEUVALVALHISGLULYS
14   ALAASPASPLEUGLYLYSGLYGLYASNGLU
15   GLUSERTHRLYSTHRGLYASNALAGLYSER
16   ARGLEUALACYSGLYVALILEGLYILEALA
17   GLN

Samples:

sample_1: DPC 20 mM; entity, [U-13C; U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

Gromacs v4.5.3, David van der Spoel, and Erik Lindahl - refinement

Cyana v2, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

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