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5NHX
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BU of 5nhx by Molmil
Periplasmic domain of Outer Membrane Protein A from Klebsiella pneumoniae
分子名称: CITRIC ACID, Outer membrane protein A
著者Demange, P, Tranier, S, Nars, G, Iordanov, I, Mourey, L, Saurel, O, Milon, A.
登録日2017-03-22
公開日2018-05-16
最終更新日2024-01-17
実験手法X-RAY DIFFRACTION (1.95 Å)
主引用文献Structure and dynamics of the C-terminal domain of OmpA from Klebsiella pneumonia
To Be Published
6H3E
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BU of 6h3e by Molmil
Receptor-bound Ghrelin conformation
分子名称: Appetite-regulating hormone, octan-1-amine
著者Ferre, G, Damian, M, M'Kadmi, C, Saurel, O, Czaplicki, G, Demange, P, Marie, J, Fehrentz, J.A, Baneres, J.L, Milon, A.
登録日2018-07-18
公開日2019-07-24
最終更新日2023-06-14
実験手法SOLUTION NMR
主引用文献Structure and dynamics of G protein-coupled receptor-bound ghrelin reveal the critical role of the octanoyl chain.
Proc.Natl.Acad.Sci.USA, 116, 2019
1TOR
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BU of 1tor by Molmil
MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE
分子名称: ACETYLCHOLINE RECEPTOR, MAIN IMMUNOGENIC REGION
著者Orlewski, P, Tsikaris, V, Sakarellos, C, Sakarellos-Daistiotis, M, Vatzaki, E, Tzartos, S.J, Marraud, M, Cung, M.T.
登録日1995-10-11
公開日1996-03-08
最終更新日2024-05-01
実験手法SOLUTION NMR
主引用文献Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data.
Biopolymers, 40, 1996
1TOS
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BU of 1tos by Molmil
TORPEDO CALIFORNICA ACHR RECEPTOR [ALA76] ANALOGUE COMPLEXED WITH THE ANTI-ACETYLCHOLINE MAB6 MONOCLONAL ANTIBODY
分子名称: ACETYLCHOLINE RECEPTOR [ALA76] MIR ANALOGUE
著者Orlewski, P, Tsikaris, V, Sakarellos, C, Sakarellos-Daistiotis, M, Vatzaki, E, Tzartos, S.J, Marraud, M, Cung, M.T.
登録日1995-10-11
公開日1996-03-08
最終更新日2024-05-01
実験手法SOLUTION NMR
主引用文献Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data.
Biopolymers, 40, 1996
1M9I
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BU of 1m9i by Molmil
Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI
分子名称: Annexin VI, CALCIUM ION
著者Freye-Minks, C, Kretsinger, R.H, Creutz, C.E.
登録日2002-07-29
公開日2002-08-07
最終更新日2024-04-03
実験手法X-RAY DIFFRACTION (2.65 Å)
主引用文献Structural and Dynamic Changes in Human Annexin VI Induced by a Phosphorylation-Mimicking Mutation, T356D
Biochemistry, 42, 2003
2JTG
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BU of 2jtg by Molmil
Solution structure of the THAP-zinc finger of THAP1
分子名称: THAP domain-containing protein 1, ZINC ION
著者Bessiere, D, Campagne, S, Milon, A, Gervais, V.
登録日2007-07-31
公開日2007-12-11
最終更新日2022-03-16
実験手法SOLUTION NMR
主引用文献Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways
J.Biol.Chem., 283, 2008
2K0L
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BU of 2k0l by Molmil
NMR structure of the transmembrane domain of the Outer Membrane Protein A from Klebsiella pneumoniae in DHPC micelles.
分子名称: Outer membrane protein A
著者Renault, M, Saurel, O, Gervais, V, Lohr, F, Reat, V, Piotto, M, Milon, A.
登録日2008-02-04
公開日2008-12-23
最終更新日2022-03-16
実験手法SOLUTION NMR
主引用文献Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications.
J.Mol.Biol., 385, 2009
1HVD
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BU of 1hvd by Molmil
STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER
分子名称: ANNEXIN V, CALCIUM ION
著者Burger, A, Huber, R.
登録日1994-06-29
公開日1995-03-31
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter
J.Mol.Biol., 237, 1994
1HVF
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BU of 1hvf by Molmil
STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER
分子名称: ANNEXIN V, CALCIUM ION, SULFATE ION
著者Burger, A, Huber, R.
登録日1994-06-29
公開日1995-03-31
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter
J.Mol.Biol., 237, 1994
1HVG
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BU of 1hvg by Molmil
STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER
分子名称: ANNEXIN V
著者Burger, A, Huber, R.
登録日1994-06-29
公開日1995-03-31
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (3 Å)
主引用文献Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter
J.Mol.Biol., 237, 1994
1HVE
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BU of 1hve by Molmil
STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER
分子名称: ANNEXIN V, CALCIUM ION, SULFATE ION
著者Burger, A, Huber, R.
登録日1994-06-29
公開日1995-03-31
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.3 Å)
主引用文献Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter
J.Mol.Biol., 237, 1994

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