+Open data
-Basic information
Entry | Database: PDB / ID: 2kfq | ||||||
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Title | NMR Structure of FP1 | ||||||
Components | FP1 | ||||||
Keywords | DE NOVO PROTEIN / protein | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Araki, M. / Tamura, A. | ||||||
Citation | Journal: Febs J. / Year: 2009 Title: Solubility-dependent structural formation of a 25-residue, natively unfolded protein, induced by addition of a seven-residue peptide fragment Authors: Araki, M. / Tamura, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kfq.cif.gz | 104.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kfq.ent.gz | 83.9 KB | Display | PDB format |
PDBx/mmJSON format | 2kfq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2kfq_validation.pdf.gz | 339.1 KB | Display | wwPDB validaton report |
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Full document | 2kfq_full_validation.pdf.gz | 410 KB | Display | |
Data in XML | 2kfq_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 2kfq_validation.cif.gz | 15 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kf/2kfq ftp://data.pdbj.org/pub/pdb/validation_reports/kf/2kfq | HTTPS FTP |
-Related structure data
Similar structure data |
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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: 3519.254 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: 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: 25mM [U-100% 2H] acetic acid-1, 50mM sodium chloride-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 3 / Pressure: ambient / Temperature: 293.15 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 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: 50 / Conformers submitted total number: 10 / Representative conformer: 1 |