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1TFS
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BU of 1tfs by Molmil
NMR AND RESTRAINED MOLECULAR DYNAMICS STUDY OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF TOXIN FS2, A SPECIFIC BLOCKER OF THE L-TYPE CALCIUM CHANNEL, ISOLATED FROM BLACK MAMBA VENOM
Descriptor: TOXIN FS2
Authors:Albrand, J.-P, Blackledge, M.J, Pascaud, F, Hollecker, M, Marion, D.
Deposit date:1995-01-26
Release date:1995-03-31
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom.
Biochemistry, 34, 1995
1IMT
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BU of 1imt by Molmil
MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES
Descriptor: INTESTINAL TOXIN 1
Authors:Boisbouvier, J, Albrand, J.-P, Blackledge, M, Jaquinod, M, Schweitz, H, Lazdunski, M, Marion, D.
Deposit date:1998-04-14
Release date:1999-04-20
Last modified:2022-02-23
Method:SOLUTION NMR
Cite:A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis.
J.Mol.Biol., 283, 1998
1HRR
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BU of 1hrr by Molmil
THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR
Descriptor: IRON/SULFUR CLUSTER, REDUCED HIGH POTENTIAL IRON SULFUR PROTEIN
Authors:Banci, L, Bertini, I, Dikiy, A, Kastrau, D.H.W, Luchinat, C, Sompornpisut, P.
Deposit date:1995-01-17
Release date:1995-07-31
Last modified:2022-02-23
Method:SOLUTION NMR
Cite:The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Biochemistry, 34, 1995
1HRQ
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BU of 1hrq by Molmil
THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR
Descriptor: HIGH POTENTIAL IRON SULFUR PROTEIN, IRON/SULFUR CLUSTER
Authors:Banci, L, Bertini, I, Dikiy, A, Kastrau, D.H.W, Luchinat, C, Sompornpisut, P.
Deposit date:1995-01-17
Release date:1995-06-03
Last modified:2022-02-23
Method:SOLUTION NMR
Cite:The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Biochemistry, 34, 1995

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