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- PDB-1hcr: HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hcr | ||||||
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Title | HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS | ||||||
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![]() | DNA BINDING PROTEIN/DNA / ![]() | ||||||
Function / homology | ![]() DNA strand exchange activity / DNA integration / DNA recombination / ![]() Similarity search - Function | ||||||
Method | ![]() | ||||||
![]() | Feng, J.-A. / Johnson, R.C. / Dickerson, R.E. | ||||||
![]() | ![]() Title: Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions. Authors: Feng, J.A. / Johnson, R.C. / Dickerson, R.E. #1: ![]() Title: Crystallization and Prelimanary X-Ray Analysis of the DNA Binding Domain of the Hin Recombinase with its DNA Binding Site Authors: Feng, J.-A. / Simon, M. / Mack, D.P. / Dervan, P.B. / Johnson, R.C. / Dickerson, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 40.1 KB | Display | ![]() |
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PDB format | ![]() | 24.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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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Atom site foot note | 1: LYS A 186 - LYS A 187 OMEGA =148.79 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: DNA chain | Mass: 4324.836 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
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#2: DNA chain | Mass: 3918.599 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
#3: Protein | Mass: 6047.051 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P03013 |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 53.79 % | ||||||||||||
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Crystal grow![]() | Method: vapor diffusion / Details: VAPOR DIFFUSION | ||||||||||||
Components of the solutions |
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-Data collection
Diffraction | Mean temperature: 123 K |
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Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 2.3 Å / Num. all: 17839 / Num. obs: 5346 / Observed criterion σ(F): 2 |
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Processing
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Refinement | Resolution: 2.3→8 Å / σ(F): 2 Details: THIS COORDINATE SET IS PRELIMINARY. REFINEMENT IS STILL IN PROGRESS. RESIDUES SER 183 AND SER 184 ARE POORLY DEFINED IN THE ELECTRON DENSITY MAP.
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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