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Yorodumi- PDB-1kwd: SOLUTION STRUCTURE OF THE CENTRAL CONSERVED REGION OF HUMAN RESPI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1kwd | ||||||
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Title | SOLUTION STRUCTURE OF THE CENTRAL CONSERVED REGION OF HUMAN RESPIRATORY SYNCYTIAL VIRUS ATTACHMENT GLYCOPROTEIN G 187 | ||||||
Components | MAJOR SURFACE GLYCOPROTEIN G | ||||||
Keywords | VIRAL PROTEIN / cysteine nose | ||||||
Function / homology | Function and homology information symbiont entry into host cell / virus-mediated perturbation of host defense response / virion attachment to host cell / host cell plasma membrane / virion membrane / extracellular region / membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, restrained molecular dynamics | ||||||
Authors | Sugawara, M. / Czaplicki, J. / Ferrage, J. / Haeuw, J.F. / Power, U.F. / Corvaia, N. / Nguyen, T. / Beck, A. / Milon, A. | ||||||
Citation | Journal: J.Pept.Res. / Year: 2002 Title: Structure-antigenicity relationship studies of the central conserved region of human respiratory syncytial virus protein G. Authors: Sugawara, M. / Czaplicki, J. / Ferrage, J. / Haeuw, J.F. / Power, U.F. / Corvaia, N. / Nguyen, T. / Beck, A. / Milton, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kwd.cif.gz | 66.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kwd.ent.gz | 50 KB | Display | PDB format |
PDBx/mmJSON format | 1kwd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kw/1kwd ftp://data.pdbj.org/pub/pdb/validation_reports/kw/1kwd | HTTPS FTP |
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-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: 1741.064 Da / Num. of mol.: 1 / Fragment: Residues 172-187 / Source method: obtained synthetically Details: Synthesis of the peptide was performed by a solid phase method using FMOC/tBu chemistry. References: UniProt: P20895 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 1 mM G4a(1-4/2-3), 90% H2O, 10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 4.6 / Pressure: ambient / Temperature: 285 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, restrained molecular dynamics / Software ordinal: 1 Details: The structures are based on 76 NOE-derived distance restrains and 5 dihedral angle restrains. | ||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations, lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry, structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 16 |