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Human SOD before harboring the catalytic metal: Solution structure of copper depleted, disulfide reduced form
Authors
Banci, L., Bertini, I., Cantini, F., D'Amelio, N., Gaggelli, E.
Assembly
Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)
Entity
1. Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1) (polymer, Thiol state: all free), 153 monomers, 15756.23 × 2 Da Detail

ATKAVAVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEF GDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH SIIGRTLVVH EKADDLGKGG NEESTKTGNA GSRLACGVIG IAQ


2. ZN (non-polymer), 65.409 × 2 Da
Total weight
31643.28 Da
Max. entity weight
15756.23 Da
Entity Connection
disulfide 6 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1disulfidesing1:HIS63:ND12:ZN1:ZN
2disulfidesing1:HIS71:ND12:ZN1:ZN
3disulfidesing1:HIS80:ND12:ZN1:ZN
4disulfidesing1:HIS63:ND12:ZN1:ZN
5disulfidesing1:HIS71:ND12:ZN1:ZN
6disulfidesing1:HIS80:ND12:ZN1:ZN

Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
torsion angle dynamics, sumulated annealing, restrained energy minimization
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 91.9 %, Completeness (bb): 95.0 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All91.9 % (1493 of 1625)96.8 % (806 of 833)84.1 % (529 of 629)96.9 % (158 of 163)
Backbone95.0 % (839 of 883)97.7 % (294 of 301)91.7 % (398 of 434)99.3 % (147 of 148)
Sidechain88.6 % (771 of 870)96.2 % (512 of 532)76.8 % (248 of 323)73.3 % (11 of 15)
Aromatic47.6 % (40 of 84)83.3 % (35 of 42) 9.8 % (4 of 41)100.0 % (1 of 1)
Methyl95.8 % (159 of 166)100.0 % (83 of 83)91.6 % (76 of 83)

1. Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)

ATKAVAVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEF GDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH SIIGRTLVVH EKADDLGKGG NEESTKTGNA GSRLACGVIG IAQ

Sample #1

Pressure 1 atm, Temperature 298 K, pH 5


#NameIsotope labelingTypeConcentration
1Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)[U-15N]1.5 mM
2ZINC (II) ION1.5 mM
3sodium phosphate20 mM
4DTT buffer20 mM
5H2O90 %
6D2O10 %
Sample #2

Pressure 1 atm, Temperature 298 K, pH 5


#NameIsotope labelingTypeConcentration
7Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)[U-13C; U-15N]1 mM
8ZINC (II) ION1 mM
9sodium phosphate20 mM
10DTT buffer20 mM
11H2O90 %
12D2O10 %

LACS Plot; CA
Referencing offset: 2.3 ppm, Outliers: 3 Detail
LACS Plot; CB
Referencing offset: 2.3 ppm, Outliers: 3 Detail
LACS Plot; HA
Referencing offset: -0.05 ppm, Outliers: 4 Detail
LACS Plot; CO
Referencing offset: 2.85 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 30 models in PDB: 2AF2, Strand ID: A, B Detail


Release date
2007-01-28
Citation
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form
Banci, L., Bertini, I., Cantini, F., D'Amelio, N., Gaggelli, E.
J. Biol. Chem. (2006), 281, 2333-2337, PubMed 16291742 , DOI 10.1074/jbc.M506497200 ,
Related entities 1. Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1), : 1 : 4 : 2 : 82 : 111 entities Detail
Interaction partners 1. Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1), : 26 interactors Detail
Experiments performed 11 experiments Detail
Keywords copper depleted protein, disulfide bond reduced, homodimeric protein, Human superoxide dismutase, NMR, Protein Structure Initiative, PSI, solution structure, SPINE, Structural Genomics, Structural Proteomics in Europe