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Yorodumi- PDB-1n0a: Turn stability in beta-hairpin peptides: 3:5 type I G1 bulge turns -
+Open data
-Basic information
Entry | Database: PDB / ID: 1n0a | ||||||
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Title | Turn stability in beta-hairpin peptides: 3:5 type I G1 bulge turns | ||||||
Components | bhpw_pdg, beta-hairpin peptide | ||||||
Keywords | DE NOVO PROTEIN / beta hairpin / beta-turn / beta-bulge | ||||||
Method | SOLUTION NMR / distance geometry, restrained molecular dynamics | ||||||
Authors | Blandl, T. / Cochran, A.G. / Skelton, N.J. | ||||||
Citation | Journal: PROTEIN SCI. / Year: 2003 Title: Turn stability in beta-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns Authors: Blandl, T. / Cochran, A.G. / Skelton, N.J. | ||||||
History |
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Remark 999 | SEQUENCE There is no sequence database reference since the peptide is a de novo designed sequence. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n0a.cif.gz | 61.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n0a.ent.gz | 48 KB | Display | PDB format |
PDBx/mmJSON format | 1n0a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1n0a_validation.pdf.gz | 330 KB | Display | wwPDB validaton report |
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Full document | 1n0a_full_validation.pdf.gz | 398.6 KB | Display | |
Data in XML | 1n0a_validation.xml.gz | 5.1 KB | Display | |
Data in CIF | 1n0a_validation.cif.gz | 8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n0/1n0a ftp://data.pdbj.org/pub/pdb/validation_reports/n0/1n0a | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar 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: 1277.470 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. |
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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 augmented by loose phi and psi restraints generated from TALOS. MODEL 21 is the average minimized structure. |
-Sample preparation
Details |
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Sample conditions |
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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 DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry, restrained molecular dynamics / Software ordinal: 1 Details: 100 distance geometry structures were calculated. The 80 structures of lowest penalty function were further refined using restrained molecular dynamics. The 20 structures of lowest restraint ...Details: 100 distance geometry structures were calculated. The 80 structures of lowest penalty function were further refined using restrained molecular dynamics. The 20 structures of lowest restraint violation energy were used to describe the structure. 61 distance and 21 dihedral angle restraints were used. The final ensemble has no distance violations greater than 0.1 A and no dihedral angle vioaltions greater than 1 degree. 95% of the residues are in the most favourable region of the Ramachandran plot. The mean backbone atom rmsd to the mean structure is 0.29+/-0.05 A. | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 80 / Conformers submitted total number: 21 |