Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin
Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone r...
Ausführliche Beschreibung
Autor*in: |
Brothers, Michael C. [verfasserIn] Geissler, Brett [verfasserIn] Hisao, Grant S. [verfasserIn] Satchell, Karla J. F. [verfasserIn] Wilson, Brenda A. [verfasserIn] Rienstra, Chad M. [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2013 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Biomolecular NMR assignments - Dordrecht [u.a.] : Springer Netherlands, 2007, 8(2013), 1 vom: 14. Juni, Seite 221-224 |
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Übergeordnetes Werk: |
volume:8 ; year:2013 ; number:1 ; day:14 ; month:06 ; pages:221-224 |
Links: |
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DOI / URN: |
10.1007/s12104-013-9487-1 |
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Katalog-ID: |
SPR024329800 |
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100 | 1 | |a Brothers, Michael C. |e verfasserin |4 aut | |
245 | 1 | 0 | |a Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin |
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520 | |a Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. | ||
650 | 4 | |a Membrane localization domain |7 (dpeaa)DE-He213 | |
650 | 4 | |a toxin |7 (dpeaa)DE-He213 | |
650 | 4 | |a Four helical bundle |7 (dpeaa)DE-He213 | |
650 | 4 | |a C1 domain |7 (dpeaa)DE-He213 | |
700 | 1 | |a Geissler, Brett |e verfasserin |4 aut | |
700 | 1 | |a Hisao, Grant S. |e verfasserin |4 aut | |
700 | 1 | |a Satchell, Karla J. F. |e verfasserin |4 aut | |
700 | 1 | |a Wilson, Brenda A. |e verfasserin |4 aut | |
700 | 1 | |a Rienstra, Chad M. |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Biomolecular NMR assignments |d Dordrecht [u.a.] : Springer Netherlands, 2007 |g 8(2013), 1 vom: 14. Juni, Seite 221-224 |w (DE-627)545787599 |w (DE-600)2388861-1 |x 1874-270X |7 nnns |
773 | 1 | 8 | |g volume:8 |g year:2013 |g number:1 |g day:14 |g month:06 |g pages:221-224 |
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10.1007/s12104-013-9487-1 doi (DE-627)SPR024329800 (SPR)s12104-013-9487-1-e DE-627 ger DE-627 rakwb eng 570 ASE Brothers, Michael C. verfasserin aut Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. Membrane localization domain (dpeaa)DE-He213 toxin (dpeaa)DE-He213 Four helical bundle (dpeaa)DE-He213 C1 domain (dpeaa)DE-He213 Geissler, Brett verfasserin aut Hisao, Grant S. verfasserin aut Satchell, Karla J. F. verfasserin aut Wilson, Brenda A. verfasserin aut Rienstra, Chad M. verfasserin aut Enthalten in Biomolecular NMR assignments Dordrecht [u.a.] : Springer Netherlands, 2007 8(2013), 1 vom: 14. Juni, Seite 221-224 (DE-627)545787599 (DE-600)2388861-1 1874-270X nnns volume:8 year:2013 number:1 day:14 month:06 pages:221-224 https://dx.doi.org/10.1007/s12104-013-9487-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2013 1 14 06 221-224 |
spelling |
10.1007/s12104-013-9487-1 doi (DE-627)SPR024329800 (SPR)s12104-013-9487-1-e DE-627 ger DE-627 rakwb eng 570 ASE Brothers, Michael C. verfasserin aut Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. Membrane localization domain (dpeaa)DE-He213 toxin (dpeaa)DE-He213 Four helical bundle (dpeaa)DE-He213 C1 domain (dpeaa)DE-He213 Geissler, Brett verfasserin aut Hisao, Grant S. verfasserin aut Satchell, Karla J. F. verfasserin aut Wilson, Brenda A. verfasserin aut Rienstra, Chad M. verfasserin aut Enthalten in Biomolecular NMR assignments Dordrecht [u.a.] : Springer Netherlands, 2007 8(2013), 1 vom: 14. Juni, Seite 221-224 (DE-627)545787599 (DE-600)2388861-1 1874-270X nnns volume:8 year:2013 number:1 day:14 month:06 pages:221-224 https://dx.doi.org/10.1007/s12104-013-9487-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2013 1 14 06 221-224 |
allfields_unstemmed |
10.1007/s12104-013-9487-1 doi (DE-627)SPR024329800 (SPR)s12104-013-9487-1-e DE-627 ger DE-627 rakwb eng 570 ASE Brothers, Michael C. verfasserin aut Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. Membrane localization domain (dpeaa)DE-He213 toxin (dpeaa)DE-He213 Four helical bundle (dpeaa)DE-He213 C1 domain (dpeaa)DE-He213 Geissler, Brett verfasserin aut Hisao, Grant S. verfasserin aut Satchell, Karla J. F. verfasserin aut Wilson, Brenda A. verfasserin aut Rienstra, Chad M. verfasserin aut Enthalten in Biomolecular NMR assignments Dordrecht [u.a.] : Springer Netherlands, 2007 8(2013), 1 vom: 14. Juni, Seite 221-224 (DE-627)545787599 (DE-600)2388861-1 1874-270X nnns volume:8 year:2013 number:1 day:14 month:06 pages:221-224 https://dx.doi.org/10.1007/s12104-013-9487-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2013 1 14 06 221-224 |
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10.1007/s12104-013-9487-1 doi (DE-627)SPR024329800 (SPR)s12104-013-9487-1-e DE-627 ger DE-627 rakwb eng 570 ASE Brothers, Michael C. verfasserin aut Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. Membrane localization domain (dpeaa)DE-He213 toxin (dpeaa)DE-He213 Four helical bundle (dpeaa)DE-He213 C1 domain (dpeaa)DE-He213 Geissler, Brett verfasserin aut Hisao, Grant S. verfasserin aut Satchell, Karla J. F. verfasserin aut Wilson, Brenda A. verfasserin aut Rienstra, Chad M. verfasserin aut Enthalten in Biomolecular NMR assignments Dordrecht [u.a.] : Springer Netherlands, 2007 8(2013), 1 vom: 14. Juni, Seite 221-224 (DE-627)545787599 (DE-600)2388861-1 1874-270X nnns volume:8 year:2013 number:1 day:14 month:06 pages:221-224 https://dx.doi.org/10.1007/s12104-013-9487-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2013 1 14 06 221-224 |
language |
English |
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Enthalten in Biomolecular NMR assignments 8(2013), 1 vom: 14. Juni, Seite 221-224 volume:8 year:2013 number:1 day:14 month:06 pages:221-224 |
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Enthalten in Biomolecular NMR assignments 8(2013), 1 vom: 14. Juni, Seite 221-224 volume:8 year:2013 number:1 day:14 month:06 pages:221-224 |
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topic_facet |
Membrane localization domain toxin Four helical bundle C1 domain |
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Biomolecular NMR assignments |
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Brothers, Michael C. @@aut@@ Geissler, Brett @@aut@@ Hisao, Grant S. @@aut@@ Satchell, Karla J. F. @@aut@@ Wilson, Brenda A. @@aut@@ Rienstra, Chad M. @@aut@@ |
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570 ASE Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin Membrane localization domain (dpeaa)DE-He213 toxin (dpeaa)DE-He213 Four helical bundle (dpeaa)DE-He213 C1 domain (dpeaa)DE-He213 |
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backbone and side-chain resonance assignments of the membrane localization domain from pasteurellamultocida toxin |
title_auth |
Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin |
abstract |
Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. |
abstractGer |
Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. |
abstract_unstemmed |
Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs. |
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Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin |
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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">SPR024329800</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519134447.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201006s2013 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s12104-013-9487-1</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR024329800</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s12104-013-9487-1-e</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="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">ASE</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Brothers, Michael C.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2013</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99 % of all backbone and side-chain carbon atoms, including 99 % of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Membrane localization domain</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">toxin</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Four helical bundle</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">C1 domain</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Geissler, Brett</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hisao, Grant S.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Satchell, Karla J. 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Juni, Seite 221-224</subfield><subfield code="w">(DE-627)545787599</subfield><subfield code="w">(DE-600)2388861-1</subfield><subfield code="x">1874-270X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:8</subfield><subfield code="g">year:2013</subfield><subfield code="g">number:1</subfield><subfield code="g">day:14</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:221-224</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s12104-013-9487-1</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="912" 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