+Open data
-Basic information
Entry | Database: PDB / ID: 2rvd | ||||||
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Title | NMR STRUCTURE of A MUTANT OF CHIGNOLIN, CLN025 | ||||||
Components | CLN025 | ||||||
Keywords | DE NOVO PROTEIN / BETA-HAIRPIN / MINI-PROTEIN / CHIGNOLIN | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Kato, Y. / Ishimura, M. / Honda, S. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2008 Title: Crystal structure of a ten-amino acid protein Authors: Honda, S. / Akiba, T. / Kato, Y.S. / Sawada, Y. / Sekijima, M. / Ishimura, M. / Ooishi, A. / Watanabe, H. / Odahara, T. / Harata, K. #2: Journal: Structure / Year: 2004 Title: 10 Residue folded peptide designed by segment statistics Authors: Honda, S. / Yamasaki, K. / Sawada, Y. / Morii, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rvd.cif.gz | 69.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rvd.ent.gz | 50.6 KB | Display | PDB format |
PDBx/mmJSON format | 2rvd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rvd_validation.pdf.gz | 417.7 KB | Display | wwPDB validaton report |
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Full document | 2rvd_full_validation.pdf.gz | 490.4 KB | Display | |
Data in XML | 2rvd_validation.xml.gz | 6.6 KB | Display | |
Data in CIF | 2rvd_validation.cif.gz | 9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rv/2rvd ftp://data.pdbj.org/pub/pdb/validation_reports/rv/2rvd | HTTPS FTP |
-Related structure data
Related structure data | 5awlC C: citing same article (ref.) |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1294.322 Da / Num. of mol.: 1 / Mutation: G1Y/G10Y / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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Sequence details | THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEBASE DATABASE (UNIPROTKB) AT ...THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEB |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||||||||||
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Sample |
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Sample conditions | pH: 5.7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / 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 constraints | NOE constraints total: 80 / NOE intraresidue total count: 26 / NOE long range total count: 15 / NOE medium range total count: 22 / NOE sequential total count: 17 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |