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- PDB-1d6x: THE STRUCTURE OF THE ANTIMICROBIAL PEPTIDE TRITRPTICIN BOUND TO M... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1d6x | ||||||
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Title | THE STRUCTURE OF THE ANTIMICROBIAL PEPTIDE TRITRPTICIN BOUND TO MICELLES-A DISTINCT MEMBRANE-BOUND PEPTIDE FOLD | ||||||
![]() | ANTIMICROBIAL PEPTIDE, TRITRPTICIN | ||||||
![]() | IMMUNE SYSTEM / TYPE IV TURN-TYPE III TURN | ||||||
Method | SOLUTION NMR / RESTRAINED SIMULATED ANNEALING, MOLECULAR DYNAMICS | ||||||
Model type details | minimized average | ||||||
![]() | Schibli, D.J. / Hwang, P.M. / Vogel, H.J. | ||||||
![]() | ![]() Title: Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold. Authors: Schibli, D.J. / Hwang, P.M. / Vogel, H.J. #1: ![]() Title: Antimicrobial Activity of a 13 Amino Acid Tryptophan-Rich Peptide Derived From a Putative Porcine Precursor Protein of a Novel Family of Antibacterial Peptides Authors: Lawyer, C. / Pai, S. / Watabe, M. / Borgia, P. / Mashimo, T. / Eagleton, L. / Watabe, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.1 KB | Display | ![]() |
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PDB format | ![]() | 68 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 335.8 KB | Display | ![]() |
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Full document | ![]() | 444.6 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 11.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 1906.286 Da / Num. of mol.: 1 / Fragment: SYNTHETIC CATHELICIDIN FRAGMENT / Source method: obtained synthetically Details: SYNTHETIC PEPTIDE, SEQUENCE FROM A FRAGMENT OF A PORCINE NEUTROPHIL CATHELICIDIN |
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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 |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 400 mM SDS / pH: 4.5 / Pressure: AMBIENT / Temperature: 313 K | ||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: RESTRAINED SIMULATED ANNEALING, MOLECULAR DYNAMICS / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON 163 INTERPROTON RESTRAINTS. OF THESE 47 WERE INTRARESIDUE, 50 SEQUENTIAL, AND 66 SHORT-RANGE | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 97 / Conformers submitted total number: 19 |