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Yorodumi- PDB-2jrw: Solution structure of Cyclic extended Pep1(Cyc.ext.Pep.1) for aut... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2jrw | ||||||
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Title | Solution structure of Cyclic extended Pep1(Cyc.ext.Pep.1) for autoimmune myasthenia gravis | ||||||
Components | Cyclic extended Pep.1 | ||||||
Keywords | IMMUNE SYSTEM / acetylcholine receptor / phage display / peptide cyclization | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Authors | Jung, H.H. / Yi, H.J. / Lee, S.K. / Lee, J.Y. / Jung, H.J. / Yang, S.T. / Eu, Y.-J. / Im, S.-H. / Kim, J.I. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: Structural analysis of immunotherapeutic peptides for autoimmune Myasthenia gravis Authors: Jung, H.H. / Yi, H.J. / Lee, S.K. / Lee, J.Y. / Jung, H.J. / Yang, S.T. / Eu, Y.-J. / Im, S.-H. / Kim, J.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jrw.cif.gz | 104.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jrw.ent.gz | 83.6 KB | Display | PDB format |
PDBx/mmJSON format | 2jrw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jr/2jrw ftp://data.pdbj.org/pub/pdb/validation_reports/jr/2jrw | 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: 2678.023 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Solid Phase Peptide Synthesis |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1mM protein; 90% H2O, 10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: protein |
Sample conditions | pH: 3.1 / Pressure: ambient / Temperature: 288 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 16 / Conformers submitted total number: 16 / Maximum lower distance constraint violation: 1.8 Å / Maximum upper distance constraint violation: 6 Å / Torsion angle constraint violation method: PROCHECK_NMR |