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Yorodumi- PDB-1zxf: Solution structure of a self-sacrificing resistance protein, CalC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zxf | ||||||
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Title | Solution structure of a self-sacrificing resistance protein, CalC from Micromonospora echinospora | ||||||
Components | CalC | ||||||
Keywords | TOXIN / Self-Sacrificing Resistance Protein / Structural Genomics / PSI / Protein Structure Initiative / Center for Eukaryotic Structural Genomics / CESG | ||||||
Function / homology | Activator of Hsp90 ATPase homologue 1-like / Activator of Hsp90 ATPase homolog 1-like protein / START domain / Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4 / START-like domain superfamily / 2-Layer Sandwich / Alpha Beta / CalC Function and homology information | ||||||
Biological species | Micromonospora echinospora (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Singh, S. / Hager, M.H. / Zhang, C. / Griffith, B.R. / Lee, M.S. / Hallenga, K. / Markley, J.L. / Thorson, J.S. / Center for Eukaryotic Structural Genomics (CESG) | ||||||
Citation | Journal: Acs Chem.Biol. / Year: 2006 Title: Structural insight into the self-sacrifice mechanism of enediyne resistance. Authors: Singh, S. / Hager, M.H. / Zhang, C. / Griffith, B.R. / Lee, M.S. / Hallenga, K. / Markley, J.L. / Thorson, J.S. #1: Journal: Science / Year: 2003 Title: Resistance to enediyne antitumor antibiotics by CalC self-sacrifice. Authors: Biggins, J.B. / Onwueme, K.C. / Thorson, J.S. #2: Journal: Science / Year: 2002 Title: The calicheamicin gene cluster and its iterative type I enediyne PKS. Authors: Ahlert, J. / Shepard, E. / Lomovskaya, N. / Zazopoulos, E. / Staffa, A. / Bachmann, B.O. / Huang, K. / Fonstein, L. / Czisny, A. / Whitwam, R.E. / Farnet, C.M. / Thorson, J.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zxf.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1zxf.ent.gz | 910.1 KB | Display | PDB format |
PDBx/mmJSON format | 1zxf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1zxf_validation.pdf.gz | 345.8 KB | Display | wwPDB validaton report |
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Full document | 1zxf_full_validation.pdf.gz | 539.2 KB | Display | |
Data in XML | 1zxf_validation.xml.gz | 74.6 KB | Display | |
Data in CIF | 1zxf_validation.cif.gz | 97.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zx/1zxf ftp://data.pdbj.org/pub/pdb/validation_reports/zx/1zxf | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17915.072 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Micromonospora echinospora (bacteria) / Gene: CalC / Plasmid: pET11b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)GOLD / Keywords: AAM70338 / References: UniProt: Q8KNF0 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: NOESY mixing time = 100 ms |
-Sample preparation
Details | Contents: 1mM CalC U-15N,13C; 10mM phosphate buffer, 150 mM NaCl, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O | |||||||||||||||
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: The structures are based on a total of 3042 restraints, 2766 are NOE-derived distance constraints, 176 dihedral angle restraints,100 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |