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Yorodumi- PDB-2cpb: SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS ... -
+Open data
-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 | ||||||
Components | M13 MAJOR COAT PROTEIN | ||||||
Keywords | VIRAL PROTEIN / MAJOR COAT PROTEIN / BACTERIOPHAGE M13 / ASSEMBLY / MICELLE / MEMBRANE | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Enterobacteria phage M13 (virus) | ||||||
Method | SOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS, SIMULATED ANNEALING, THIS VERSION OF X-PLOR WAS EXTENDED FOR FLOATING CHIRALITY | ||||||
Authors | Papavoine, C.H.M. / Christiaans, B.E.C. / Folmer, R.H.A. / Konings, R.N.H. / Hilbers, C.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 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: Journal: Biochemistry / Year: 1997 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: Journal: Eur.J.Biochem. / Year: 1995 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: Journal: Biochemistry / Year: 1994 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: Journal: Biochemistry / Year: 1993 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2cpb.cif.gz | 369.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2cpb.ent.gz | 311.1 KB | Display | PDB format |
PDBx/mmJSON format | 2cpb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2cpb_validation.pdf.gz | 344 KB | Display | wwPDB validaton report |
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Full document | 2cpb_full_validation.pdf.gz | 502.4 KB | Display | |
Data in XML | 2cpb_validation.xml.gz | 21.1 KB | Display | |
Data in CIF | 2cpb_validation.cif.gz | 33.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cp/2cpb ftp://data.pdbj.org/pub/pdb/validation_reports/cp/2cpb | HTTPS FTP |
-Related structure data
-Links
-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.) Enterobacteria phage M13 (virus) / Genus: Inovirus / Plasmid: M13 / Production host: Escherichia coli (E. coli) / References: UniProt: P69541 |
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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) |
-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
Software |
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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 |