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Yorodumi- PDB-1gq0: Solution structure of Antiamoebin I, a membrane channel-forming p... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gq0 | ||||||
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Title | Solution structure of Antiamoebin I, a membrane channel-forming polypeptide; NMR, 20 structures | ||||||
Components | ANTIAMOEBIN I | ||||||
Keywords | ANTIBIOTIC / ANTIAMOEBIN I / PEPTAIBOL / ANTIBACTERIAL / ANTIFUNGAL | ||||||
Function / homology | Antiamoebin 1 / : Function and homology information | ||||||
Biological species | EMERICELLOPSIS SP. 2723 (fungus) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Galbraith, T.P. / Harris, R. / Driscoll, P.C. / Wallace, B.A. | ||||||
Citation | Journal: Biophys. J. / Year: 2003 Title: Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide. Authors: Galbraith, T.P. / Harris, R. / Driscoll, P.C. / Wallace, B.A. #1: Journal: Structure / Year: 1998 Title: The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide. Authors: Snook, C.F. / Woolley, G.A. / Oliva, G. / Pattabhi, V. / Wood, S.F. / Blundell, T.L. / Wallace, B.A. #2: Journal: Biochim. Biophys. Acta / Year: 1998 Title: Antiamoebin can function as a carrier or as a pore-forming peptaibol. Authors: Duclohier, H. / Snook, C.F. / Wallace, B.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gq0.cif.gz | 90.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gq0.ent.gz | 69.9 KB | Display | PDB format |
PDBx/mmJSON format | 1gq0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gq0_validation.pdf.gz | 354.4 KB | Display | wwPDB validaton report |
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Full document | 1gq0_full_validation.pdf.gz | 473 KB | Display | |
Data in XML | 1gq0_validation.xml.gz | 15.8 KB | Display | |
Data in CIF | 1gq0_validation.cif.gz | 20.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gq/1gq0 ftp://data.pdbj.org/pub/pdb/validation_reports/gq/1gq0 | 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
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 7 / Pressure: 1 atm / 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: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: 246 ATOMS USED IN SIMULATED ANNEALING (INCLUDING HYDROGENS) RMSD VALUES FROM IDEAL GEOMETRY FOR 20 MODELS: BOND DISTANCES 0.013 ANGSTROMS, STANDARD DEVIATION 0.0001 BOND ANGLES 2.92 DEGREES, ...Details: 246 ATOMS USED IN SIMULATED ANNEALING (INCLUDING HYDROGENS) RMSD VALUES FROM IDEAL GEOMETRY FOR 20 MODELS: BOND DISTANCES 0.013 ANGSTROMS, STANDARD DEVIATION 0.0001 BOND ANGLES 2.92 DEGREES, STANDARD DEVIATION 0.017 IMPROPER ANGLES 6.62 DEGREES, STANDARD DEVIATION 0.028 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 20 |