BMRB: 4202

Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase(SOD). Why SOD is a Dimeric Enzyme?

Authors

Banci, L., Benedetto, M., Bertini, I., Del Conte, R., Piccioli, M., Viezzoli, M.SILVIA.

Assembly

Superoxide Dismutase

Entity

1. Superoxide Dismutase (polymer, Thiol state: all disulfide bound), 153 monomers, 15809.25 Da Detail

ATKAVAVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEE EDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH SIIGRTLVVH EKADDLGKGG NEQSTKTGNA GSRLACGVIG IAQ

2. COPPER (II) ION (non-polymer), 63.546 Da
3. ZINC ION (non-polymer), 65.409 Da

Total weight

15938.205 Da

Max. entity weight

15809.25 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

TORTION ANGLES DYNAMIC (DYANA)

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.7 %, Completeness: 91.9 %, Completeness (bb): 96.1 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	91.9 % (1491 of 1622)	92.9 % (776 of 835)	90.9 % (570 of 627)	90.6 % (145 of 160)
Backbone	96.1 % (873 of 908)	96.3 % (313 of 325)	96.8 % (421 of 435)	93.9 % (139 of 148)
Sidechain	88.0 % (742 of 843)	90.8 % (463 of 510)	85.0 % (273 of 321)	50.0 % (6 of 12)
Aromatic	36.5 % (27 of 74)	73.0 % (27 of 37)	0.0 % (0 of 36)	0.0 % (0 of 1)
Methyl	95.2 % (158 of 166)	95.2 % (79 of 83)	95.2 % (79 of 83)

1. Superoxide Dismutase

ATKAVAVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEE EDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH SIIGRTLVVH EKADDLGKGG NEQSTKTGNA GSRLACGVIG IAQ

Show sample condition

Sample

Temperature 298 (±0.2) K, pH 5.0 (±0.01)

#	Name	Isotope labeling	Type	Concentration
1	Superoxide Dismutase	[U-13C; U-15N]		2.0 ~ 3.0 mM

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LACS Plot; CA

Referencing offset: -0.02 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	external	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	external	direct	0.0
15N	DSS	methyl protons	0.0 ppm	external	indirect	0.101329

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LACS Plot; CB

Referencing offset: -0.02 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	external	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	external	direct	0.0
15N	DSS	methyl protons	0.0 ppm	external	indirect	0.101329

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LACS Plot; HA

Referencing offset: -0.06 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	external	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	external	direct	0.0
15N	DSS	methyl protons	0.0 ppm	external	indirect	0.101329

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LACS Plot; CO

Referencing offset: 0.65 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	external	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	external	direct	0.0
15N	DSS	methyl protons	0.0 ppm	external	indirect	0.101329

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Protein Blocks Logo

Calculated from 36 models in PDB: 1BA9, Strand ID: A Detail

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Release date

2000-04-03

Citation

Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?
Banci, L., Benedetto, M., Bertini, I., Del Conte, R., Piccioli, M., Viezzoli, M.SILVIA.
Biochemistry (1998), 37, 11780-11791, PubMed 9718300 , DOI 10.1021/bi9803473 , Abstract

Related entities 1. Superoxide Dismutase, : 1 : 3 : 1 : 244 entities Detail

Interaction partners 1. Superoxide Dismutase, : 26 interactors Detail

Experiments performed 1 experiments Detail