BMRB Entry 6821

Title:
Human SOD before harboring the catalytic metal: Solution structure of copper depleted, disulfide reduced form
Deposition date:
2005-09-09
Original release date:
2007-01-29
Authors:
Banci, L.; Bertini, I.; Cantini, F.; D'Amelio, N.; Gaggelli, E.
Citation:

Citation: Banci, L.; Bertini, I.; Cantini, F.; D'Amelio, N.; Gaggelli, E.. "Human SOD1 before harboring the catalytic metal: Solution structure of copper depleted, disulfide reduced form"  J. Biol. Chem. 281, 2333-2337 (2006).
PubMed: 16291742

Assembly members:

Assembly members:
Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1), polymer, 153 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: PBR322

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts158
1H chemical shifts987

Additional metadata:

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  • Samples and Experiments
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  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Superoxide dismutase [Cu-Zn], chain A1
2Superoxide dismutase [Cu-Zn], chain B1
3ZINC ION, 12
4ZINC ION, 22

Entities:

Entity 1, Superoxide dismutase [Cu-Zn], chain A 153 residues - Formula weight is not available

1   ALATHRLYSALAVALALAVALLEULYSGLY
2   ASPGLYPROVALGLNGLYILEILEASNPHE
3   GLUGLNLYSGLUSERASNGLYPROVALLYS
4   VALTRPGLYSERILELYSGLYLEUTHRGLU
5   GLYLEUHISGLYPHEHISVALHISGLUPHE
6   GLYASPASNTHRALAGLYCYSTHRSERALA
7   GLYPROHISPHEASNPROLEUSERARGLYS
8   HISGLYGLYPROLYSASPGLUGLUARGHIS
9   VALGLYASPLEUGLYASNVALTHRALAASP
10   LYSASPGLYVALALAASPVALSERILEGLU
11   ASPSERVALILESERLEUSERGLYASPHIS
12   SERILEILEGLYARGTHRLEUVALVALHIS
13   GLULYSALAASPASPLEUGLYLYSGLYGLY
14   ASNGLUGLUSERTHRLYSTHRGLYASNALA
15   GLYSERARGLEUALACYSGLYVALILEGLY
16   ILEALAGLN

Entity 2, ZINC ION, 1 - Zn - 65.409 Da.

1   ZN

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