2H3O
| Structure of MERFT, a membrane protein with two trans-membrane helices | Descriptor: | MerF | Authors: | Opella, S.J, De Angelis, A.A, Howell, S.C, Nevzorov, A.A. | Deposit date: | 2006-05-22 | Release date: | 2006-10-03 | Last modified: | 2024-05-29 | Method: | SOLID-STATE NMR | Cite: | Structure Determination of a Membrane Protein with Two Trans-membrane Helices in Aligned Phospholipid Bicelles by Solid-State NMR Spectroscopy. J.Am.Chem.Soc., 128, 2006
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1CEK
| THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY | Descriptor: | PROTEIN (ACETYLCHOLINE RECEPTOR M2) | Authors: | Marassi, F.M, Gesell, J.J, Kim, Y, Valente, A.P, Oblatt-Montal, M, Montal, M, Opella, S.J. | Deposit date: | 1999-03-09 | Release date: | 1999-03-11 | Last modified: | 2023-12-27 | Method: | SOLID-STATE NMR | Cite: | Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat.Struct.Biol., 6, 1999
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5WDZ
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1ZN5
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1EQ8
| THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT | Descriptor: | ACETYLCHOLINE RECEPTOR PROTEIN | Authors: | Marassi, F.M, Gesell, J.J, Kim, Y, Valente, A.P, Oblatt-Montal, M, Montal, M, Opella, S.J. | Deposit date: | 2000-04-03 | Release date: | 2000-04-26 | Last modified: | 2024-09-25 | Method: | SOLID-STATE NMR | Cite: | Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat.Struct.Biol., 6, 1999
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1WAZ
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1DVW
| NMR structure of 18 residue peptide from merp protein | Descriptor: | 18 RESIDUE PEPTIDE FROM MERP PROTEIN, MERCURY (II) ION | Authors: | Veglia, G, Porcelli, F, De Silva, T.M, Prantner, A.M, Opella, S.J. | Deposit date: | 2000-01-22 | Release date: | 2003-12-23 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | The Structure of the Metal-Binding Motif
GMTCAAC Is Similar in an 18-Residue Linear
Peptide and the Mercury Binding Protein MerP J.Am.Chem.Soc., 122, 2000
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1FDM
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1MZT
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2GOH
| Three-dimensional Structure of the Trans-membrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles | Descriptor: | VPU protein | Authors: | Park, S.H, De Angelis, A.A, Nevzorov, A.A, Wu, C.H, Opella, S.J. | Deposit date: | 2006-04-12 | Release date: | 2006-08-08 | Last modified: | 2024-05-29 | Method: | SOLUTION NMR | Cite: | Three-Dimensional Structure of the Transmembrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles. Biophys.J., 91, 2006
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2GOF
| Three-dimensional structure of the trans-membrane domain of Vpu from HIV-1 in aligned phospholipid bicelles | Descriptor: | VPU protein | Authors: | Park, S.H, De Angelis, A.A, Nevzorov, A.A, Wu, C.H, Opella, S.J. | Deposit date: | 2006-04-12 | Release date: | 2006-08-08 | Last modified: | 2024-05-29 | Method: | SOLUTION NMR | Cite: | Three-Dimensional Structure of the Transmembrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles. Biophys.J., 91, 2006
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2JPX
| A18H Vpu TM structure in lipid bilayers | Descriptor: | Vpu protein | Authors: | Park, S, Opella, S.J. | Deposit date: | 2007-05-25 | Release date: | 2007-11-13 | Last modified: | 2023-12-20 | Method: | SOLUTION NMR | Cite: | Conformational changes induced by a single amino acid substitution in the trans-membrane domain of Vpu: implications for HIV-1 susceptibility to channel blocking drugs Protein Sci., 16, 2007
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1PJD
| Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers | Descriptor: | Pheromone alpha factor receptor | Authors: | Valentine, K.G, Liu, S.-F, Marassi, F.M, Veglia, G, Nevzorov, A.A, Opella, S.J, Ding, F.-X, Wang, S.-H, Arshava, B, Becker, J.M, Naider, F. | Deposit date: | 2003-06-02 | Release date: | 2003-09-16 | Last modified: | 2024-05-22 | Method: | SOLID-STATE NMR | Cite: | Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers Biopolymers, 59, 2001
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1PJE
| Structure of the channel-forming trans-membrane domain of Virus protein "u"(Vpu) from HIV-1 | Descriptor: | VPU protein | Authors: | Park, S.H, Mrse, A.A, Nevzorov, A.A, Mesleh, M.F, Oblatt-Montal, M, Montal, M, Opella, S.J. | Deposit date: | 2003-06-02 | Release date: | 2003-10-14 | Last modified: | 2024-05-22 | Method: | SOLID-STATE NMR | Cite: | Three-dimensional structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1 J.Mol.Biol., 333, 2003
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1PI7
| Structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1 | Descriptor: | VPU protein | Authors: | Park, S.H, Mrse, A.A, Nevzorov, A.A, Mesleh, M.F, Oblatt-Montal, M, Montal, M, Opella, S.J. | Deposit date: | 2003-05-29 | Release date: | 2003-11-11 | Last modified: | 2024-05-22 | Method: | SOLID-STATE NMR | Cite: | Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1 J.Mol.Biol., 333, 2003
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1PI8
| Structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1 | Descriptor: | VPU protein | Authors: | Park, S.H, Mrse, A.A, Nevzorov, A.A, Mesleh, M.F, Oblatt-Montal, M, Montal, M, Opella, S.J. | Deposit date: | 2003-05-29 | Release date: | 2003-11-11 | Last modified: | 2024-05-22 | Method: | SOLID-STATE NMR | Cite: | Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1 J.Mol.Biol., 333, 2003
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1PJF
| Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage | Descriptor: | COAT PROTEIN B | Authors: | Thiriot, D.S, Nevzorov, A.A, Zagyanskiy, L, Wu, C.H, Opella, S.J. | Deposit date: | 2003-06-02 | Release date: | 2004-08-10 | Last modified: | 2024-05-01 | Method: | SOLID-STATE NMR | Cite: | Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy. J.Mol.Biol., 341, 2004
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1KVJ
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1NH4
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1KVI
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1A11
| NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES | Descriptor: | ACETYLCHOLINE RECEPTOR M2 | Authors: | Gesell, J.J, Sun, W, Montal, M, Opella, S.J. | Deposit date: | 1997-12-19 | Release date: | 1998-04-08 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat.Struct.Biol., 6, 1999
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1AFI
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1AFJ
| STRUCTURE OF THE MERCURY-BOUND FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES | Descriptor: | MERCURY (II) ION, MERP | Authors: | Steele, R.A, Opella, S.J. | Deposit date: | 1997-03-07 | Release date: | 1997-07-23 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. Biochemistry, 36, 1997
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1A1U
| SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE | Descriptor: | P53 | Authors: | Mccoy, M.A, Stavridi, E.S, Waterman, J.L.F, Wieczorek, A, Opella, S.J, Halezonetis, T.D. | Deposit date: | 1997-12-16 | Release date: | 1998-04-08 | Last modified: | 2024-05-22 | Method: | SOLUTION NMR | Cite: | Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain. EMBO J., 16, 1997
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1BZB
| GLYCOSYLATED EEL CALCITONIN | Descriptor: | PROTEIN (CALCITONIN), alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Authors: | Hashimoto, Y, Toma, K, Nishikido, J, Yamamoto, K, Haneda, K, Inazu, T, Valentine, K, Opella, S.J. | Deposit date: | 1998-10-27 | Release date: | 1998-11-11 | Last modified: | 2024-10-16 | Method: | SOLUTION NMR | Cite: | Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy. Biochemistry, 38, 1999
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