+Open data
-Basic information
Entry | Database: PDB / ID: 1abz | ||||||
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Title | ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES | ||||||
Components | ALPHA-T-ALPHA | ||||||
Keywords | DE NOVO DESIGN / HELIX-TURN-HELIX | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY DYNAMICAL SIMULATED ANNEALING | ||||||
Authors | Fezoui, Y. / Connolly, P.J. / Osterhout, J.J. | ||||||
Citation | Journal: Protein Sci. / Year: 1997 Title: Solution structure of alpha t alpha, a helical hairpin peptide of de novo design. Authors: Fezoui, Y. / Connolly, P.J. / Osterhout, J.J. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: De Novo Design and Structural Characterization of an Alpha-Helical Hairpin Peptide: A Model System for the Study of Protein Folding Intermediates Authors: Fezoui, Y. / Weaver, D.L. / Osterhout, J.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1abz.cif.gz | 279.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1abz.ent.gz | 243.3 KB | Display | PDB format |
PDBx/mmJSON format | 1abz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1abz_validation.pdf.gz | 342.9 KB | Display | wwPDB validaton report |
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Full document | 1abz_full_validation.pdf.gz | 496.4 KB | Display | |
Data in XML | 1abz_validation.xml.gz | 18.2 KB | Display | |
Data in CIF | 1abz_validation.cif.gz | 28.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/1abz ftp://data.pdbj.org/pub/pdb/validation_reports/ab/1abz | 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: 4446.004 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: DE NOVO DESIGNED PEPTIDE |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR TWO-DIMENSIONAL NMR SPECTROSCOPY. |
-Sample preparation
Sample conditions | pH: 3.6 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 400 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY DYNAMICAL SIMULATED ANNEALING Software ordinal: 1 Details: THE FAMILY OF 23 STRUCTURES IS SUPERIMPOSED OVER THE WELL-DEFINED HELICAL REGION ENCOMPASSING RESIDUES 4 - 16 AND 24 - 34. THE AVERAGE RMSD'S BETWEEN THE 23 REFINED STRUCTURES AND AVERAGE ...Details: THE FAMILY OF 23 STRUCTURES IS SUPERIMPOSED OVER THE WELL-DEFINED HELICAL REGION ENCOMPASSING RESIDUES 4 - 16 AND 24 - 34. THE AVERAGE RMSD'S BETWEEN THE 23 REFINED STRUCTURES AND AVERAGE STRUCTURE ARE AS FOLLOWS: 0.81 (RESIDUES 4 - 16 AND 24 - 34, BACKBONE ATOMS) 1.48 (RESIDUES 4 - 16 AND 24 - 34, HEAVY ATOMS) 1.08 (ALL BACKBONE ATOMS) 1.77 (ALL HEAVY ATOMS). | ||||||||||||
NMR ensemble | Conformers calculated total number: 100 / Conformers submitted total number: 23 |