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- PDB-2cpb: SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cpb | ||||||
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Title | SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN DODECYLPHOSPHOCHOLINE MICELLES, 25 LOWEST ENERGY STRUCTURES | ||||||
![]() | M13 MAJOR COAT PROTEIN | ||||||
![]() | VIRAL PROTEIN / MAJOR COAT PROTEIN / BACTERIOPHAGE M13 / ASSEMBLY / MICELLE / MEMBRANE | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS, SIMULATED ANNEALING, THIS VERSION OF X-PLOR WAS EXTENDED FOR FLOATING CHIRALITY | ||||||
![]() | Papavoine, C.H.M. / Christiaans, B.E.C. / Folmer, R.H.A. / Konings, R.N.H. / Hilbers, C.W. | ||||||
![]() | ![]() Title: Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues. Authors: Papavoine, C.H. / Christiaans, B.E. / Folmer, R.H. / Konings, R.N. / Hilbers, C.W. #1: ![]() Title: Backbone Dynamics of the Major Coat Protein of Bacteriophage M13 in Detergent Micelles by 15N Nuclear Magnetic Resonance Relaxation Measurements Using the Model-Free Approach and Reduced Spectral Density Mapping Authors: Papavoine, C.H. / Remerowski, M.L. / Horstink, L.M. / Konings, R.N. / Hilbers, C.W. / Van De Ven, F.J. #2: ![]() Title: NMR Studies of the Major Coat Protein of Bacteriophage M13. Structural Information of Gviiip in Dodecylphosphocholine Micelles Authors: Papavoine, C.H. / Aelen, J.M. / Konings, R.N. / Hilbers, C.W. / Van De Ven, F.J. #3: ![]() Title: Location of M13 Coat Protein in Sodium Dodecyl Sulfate Micelles as Determined by NMR Authors: Papavoine, C.H. / Konings, R.N. / Hilbers, C.W. / Van De Ven, F.J. #4: ![]() Title: Assignment of 1H, 15N, and Backbone 13C Resonances in Detergent-Solubilized M13 Coat Protein Via Multinuclear Multidimensional NMR: A Model for the Coat Protein Monomer Authors: Van De Ven, F.J. / Van Os, J.W. / Aelen, J.M. / Wymenga, S.S. / Remerowski, M.L. / Konings, R.N. / Hilbers, C.W. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 369.2 KB | Display | ![]() |
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PDB format | ![]() | 311.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 344 KB | Display | ![]() |
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Full document | ![]() | 502.4 KB | Display | |
Data in XML | ![]() | 21.1 KB | Display | |
Data in CIF | ![]() | 33.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 5243.014 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N -LABELED M13 COAT PROTEIN SOLUBILIZED IN DEUTERATED DODECYLPHOSPHOCHOLINE MICELLES (CONCENTRATION COAT/DODPCHO = 1:200) |
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Sample preparation
Details | Contents: H2O |
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Sample conditions | pH: 4.9 / Temperature: 311 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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NMR software |
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Refinement | Method: RESTRAINED MOLECULAR DYNAMICS, SIMULATED ANNEALING, THIS VERSION OF X-PLOR WAS EXTENDED FOR FLOATING CHIRALITY Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY, DISTANCE RESTRAINTS SMALLER THAN 0.5 A, DIHEDRAL VIOLATIONS SMALLER THAN 5 DEGREES Conformers calculated total number: 80 / Conformers submitted total number: 25 |