Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein
Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an e...
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1997 |
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6 |
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Springer Online Journal Archives 1860-2002 |
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in: JBIC - 1996, 2(1997) vom: Apr., Seite 464-469 |
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volume:2 ; year:1997 ; month:04 ; pages:464-469 ; extent:6 |
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| 245 | 1 | 0 | |a Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein |
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| 520 | |a Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. | ||
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| 700 | 1 | |a Richards, John H. |4 oth | |
| 700 | 1 | |a Rees, D. C. |4 oth | |
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(DE-627)NLEJ206168098 DE-627 ger DE-627 rakwb eng Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein 1997 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. Springer Online Journal Archives 1860-2002 Faham, Salem oth Mizoguchi, Tadashi J. oth Adman, Elinor T. oth Gray, Harry B. oth Richards, John H. oth Rees, D. C. oth in JBIC 1996 2(1997) vom: Apr., Seite 464-469 (DE-627)NLEJ188989765 (DE-600)1464026-0 1432-1327 nnns volume:2 year:1997 month:04 pages:464-469 extent:6 http://dx.doi.org/10.1007/s007750050157 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 2 1997 4 464-469 6 |
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(DE-627)NLEJ206168098 DE-627 ger DE-627 rakwb eng Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein 1997 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. Springer Online Journal Archives 1860-2002 Faham, Salem oth Mizoguchi, Tadashi J. oth Adman, Elinor T. oth Gray, Harry B. oth Richards, John H. oth Rees, D. C. oth in JBIC 1996 2(1997) vom: Apr., Seite 464-469 (DE-627)NLEJ188989765 (DE-600)1464026-0 1432-1327 nnns volume:2 year:1997 month:04 pages:464-469 extent:6 http://dx.doi.org/10.1007/s007750050157 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 2 1997 4 464-469 6 |
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(DE-627)NLEJ206168098 DE-627 ger DE-627 rakwb eng Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein 1997 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. Springer Online Journal Archives 1860-2002 Faham, Salem oth Mizoguchi, Tadashi J. oth Adman, Elinor T. oth Gray, Harry B. oth Richards, John H. oth Rees, D. C. oth in JBIC 1996 2(1997) vom: Apr., Seite 464-469 (DE-627)NLEJ188989765 (DE-600)1464026-0 1432-1327 nnns volume:2 year:1997 month:04 pages:464-469 extent:6 http://dx.doi.org/10.1007/s007750050157 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 2 1997 4 464-469 6 |
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(DE-627)NLEJ206168098 DE-627 ger DE-627 rakwb eng Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein 1997 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. Springer Online Journal Archives 1860-2002 Faham, Salem oth Mizoguchi, Tadashi J. oth Adman, Elinor T. oth Gray, Harry B. oth Richards, John H. oth Rees, D. C. oth in JBIC 1996 2(1997) vom: Apr., Seite 464-469 (DE-627)NLEJ188989765 (DE-600)1464026-0 1432-1327 nnns volume:2 year:1997 month:04 pages:464-469 extent:6 http://dx.doi.org/10.1007/s007750050157 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 2 1997 4 464-469 6 |
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(DE-627)NLEJ206168098 DE-627 ger DE-627 rakwb eng Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein 1997 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. Springer Online Journal Archives 1860-2002 Faham, Salem oth Mizoguchi, Tadashi J. oth Adman, Elinor T. oth Gray, Harry B. oth Richards, John H. oth Rees, D. C. oth in JBIC 1996 2(1997) vom: Apr., Seite 464-469 (DE-627)NLEJ188989765 (DE-600)1464026-0 1432-1327 nnns volume:2 year:1997 month:04 pages:464-469 extent:6 http://dx.doi.org/10.1007/s007750050157 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 2 1997 4 464-469 6 |
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role of the active-site cysteine of pseudomonas aeruginosa azurin. crystal structure analysis of the cuii(cys112asp) protein |
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Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein |
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Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. |
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Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. |
| abstract_unstemmed |
Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ206168098</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706193943.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s1997 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ206168098</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the CuII(Cys112Asp) protein</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1997</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">6</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Replacement of the cysteine at position 112 of Pseudomonas aeruginosa azurin with an aspartic acid residue results in a mutant (Cys112Asp) protein that retains a strong copper-binding site. CuII(Cys112Asp) azurin can be reduced by excess [RuII(NH3)6]2+, resulting in a CuI protein with an electronic absorption spectrum very similar to that of wild-type CuI azurin. Cys112Asp azurin exhibits reversible interprotein electron-transfer reactivity with P. aeruginosa cytochrome c 551 (μ = 0.1 M sodium phosphate (pH 7.0);E°(CuII/I) = 180 mV vs NHE); this redox activity indicates that electrons can still enter and exit the protein through the partially solvent-exposed imidazole ring of His117. The structure of CuII(Cys112Asp) azurin at 2.4-Å resolution shows that the active-site copper is five coordinate: the pseudo-square base of the distorted square-pyramidal structure is defined by the imidazole Nδ atoms of His46 and His117 and the oxygen atoms of an asymmetrically-bound bidentate carboxylate group of Asp112; the apical position is occupied by the oxygen atom of the backbone carbonyl group of Gly45. The CuII–Asp112 interaction is distinguished by an approximately 1.2-Å displacement of the metal center from the plane defined by the Asp112 carboxylate group.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Faham, Salem</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mizoguchi, Tadashi J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Adman, Elinor T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gray, Harry B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Richards, John H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Rees, D. C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">JBIC</subfield><subfield code="d">1996</subfield><subfield code="g">2(1997) vom: Apr., Seite 464-469</subfield><subfield code="w">(DE-627)NLEJ188989765</subfield><subfield code="w">(DE-600)1464026-0</subfield><subfield code="x">1432-1327</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:2</subfield><subfield code="g">year:1997</subfield><subfield code="g">month:04</subfield><subfield code="g">pages:464-469</subfield><subfield code="g">extent:6</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/s007750050157</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">2</subfield><subfield code="j">1997</subfield><subfield code="c">4</subfield><subfield code="h">464-469</subfield><subfield code="g">6</subfield></datafield></record></collection>
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