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 19962

Title: Truncated L126Z-sod1 in DPC micelle

Deposition date: 2015-05-18 Original release date: 2015-05-18

Authors: Lim, Liang Zhong; Song, Jianxing

Citation: Lim, Liangzhong; Lee, Xiaowen; Song, Jianxing. "Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations"  Biochim. Biophys. Acta 1848, 1-7 (2015).

Assembly members:
L126Z-sod1, polymer, 125 residues, 13153.691 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):
L126Z-sod1: ATKAVCVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHCIIGRTLVVH EKADD

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts117
1H chemical shifts252

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Truncated L126Z-sod11

Entities:

Entity 1, Truncated L126Z-sod1 125 residues - 13153.691 Da.

1   ALATHRLYSALAVALCYSVALLEULYSGLY
2   ASPGLYPROVALGLNGLYILEILEASNPHE
3   GLUGLNLYSGLUSERASNGLYPROVALLYS
4   VALTRPGLYSERILELYSGLYLEUTHRGLU
5   GLYLEUHISGLYPHEHISVALHISGLUPHE
6   GLYASPASNTHRALAGLYCYSTHRSERALA
7   GLYPROHISPHEASNPROLEUSERARGLYS
8   HISGLYGLYPROLYSASPGLUGLUARGHIS
9   VALGLYASPLEUGLYASNVALTHRALAASP
10   LYSASPGLYVALALAASPVALSERILEGLU
11   ASPSERVALILESERLEUSERGLYASPHIS
12   CYSILEILEGLYARGTHRLEUVALVALHIS
13   GLULYSALAASPASP

Samples:

sample_1: L126Z-sod1, [U-100% 13C; U-100% 15N], 400 uM; dodecylphosphocholine (DPC) 20 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 313 K

Experiments:

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

Software:

Cyana v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18509 18708 26570
PDB
DBJ BAA14373 BAC20345 BAG35052 BAG73767
EMBL CAA26182 CAG29351 CAG46542
GB AAA72747 AAA80237 AAB05661 AAB05662 AAB27818
REF NP_000445 NP_001009025 XP_003813274 XP_004062735 XP_004062736
SP P00441 P60052

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