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- PDB-2cbt: Crystal structure of the neocarzinostatin 4Tes1 mutant bound test... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cbt | ||||||
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Title | Crystal structure of the neocarzinostatin 4Tes1 mutant bound testosterone hemisuccinate. | ||||||
![]() | NEOCARZINOSTATIN | ||||||
![]() | ANTIBIOTIC / PHAGE-DISPLAY / HAPTEN BINDING / NEOCARZINOSTATIN / ANTIMICROBIAL / DNA-BINDING | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Drevelle, A. / Graille, M. / Heyd, B. / Sorel, I. / Ulryck, N. / Pecorari, F. / Desmadril, M. / Van Tilbeurgh, H. / Minard, P. | ||||||
![]() | ![]() Title: Structures of in Vitro Evolved Binding Sites on Neocarzinostatin Scaffold Reveal Unanticipated Evolutionary Pathways. Authors: Drevelle, A. / Graille, M. / Heyd, B. / Sorel, I. / Ulryck, N. / Pecorari, F. / Desmadril, M. / Van Tilbeurgh, H. / Minard, P. #1: Journal: Biochemistry / Year: 2003 Title: In Vitro Evolution of the Binding Specificity of Neocarzinostatin, an Enediyne-Binding Chromoprotein. Authors: Heyd, B. / Pecorari, F. / Collinet, B. / Adjadj, E. / Desmadril, M. / Minard, P. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.2 KB | Display | ![]() |
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PDB format | ![]() | 39.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 954.7 KB | Display | ![]() |
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Full document | ![]() | 974.3 KB | Display | |
Data in XML | ![]() | 13.8 KB | Display | |
Data in CIF | ![]() | 17.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2cbmC ![]() 2cboC ![]() 2cbqC ![]() 1ncoS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 11290.296 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, ASP 67 TO TRP ENGINEERED RESIDUE IN CHAIN A, GLY 69 TO ALA ...ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43.71 % |
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Crystal grow | Details: 0.9 M SODIUM CITRATE, 0.1 M HEPES PH 7.5 AND 3% ETHANOL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 9943 / % possible obs: 98.9 % / Observed criterion σ(I): 2 / Redundancy: 11 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 18.3 |
Reflection shell | Resolution: 2.2→2.26 Å / Redundancy: 11 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2.9 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1NCO Resolution: 2.2→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Details: TWINNING FRACTION 0.42
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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