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Open data
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Basic information
Entry | Database: PDB / ID: 2wcc | ||||||
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Title | phage lambda IntDBD1-64 complex with p prime 2 DNA | ||||||
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![]() | PROTEIN/DNA / DNA INTEGRATION / DNA RECOMBINATION / EXCISION / INTEGRATION / PHAGE LAMBDA / RECOMBINATION / PROTEIN DNA COMPLEX / PROTEIN-DNA complex | ||||||
Function / homology | ![]() provirus excision / integrase activity / DNA integration / viral genome integration into host DNA / establishment of integrated proviral latency / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / transferase activity / DNA recombination / Hydrolases; Acting on ester bonds / hydrolase activity ...provirus excision / integrase activity / DNA integration / viral genome integration into host DNA / establishment of integrated proviral latency / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / transferase activity / DNA recombination / Hydrolases; Acting on ester bonds / hydrolase activity / symbiont entry into host cell / DNA binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / MARS, QUEEN, ATNOS CANDID | ||||||
![]() | Fadeev, E.A. / Sam, M.D. / Clubb, R.T. | ||||||
![]() | ![]() Title: NMR Structure of the Amino-Terminal Domain of the Lambda Integrase Protein in Complex with DNA: Immobilization of a Flexible Tail Facilitates Beta- Sheet Recognition of the Major Groove. Authors: Fadeev, E.A. / Sam, M.D. / Clubb, R.T. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 715.9 KB | Display | ![]() |
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PDB format | ![]() | 602.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: DNA chain | Mass: 3655.419 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: INTN(1-64) COMPLEX WITH 12 MER DOUBLE STRANDED P'2 DNA Source: (synth.) ![]() |
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#2: DNA chain | Mass: 3668.401 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: INTN(1-64) COMPLEX WITH 12 MER DOUBLE STRANDED P'2 DNA Source: (synth.) ![]() |
#3: Protein | Mass: 7628.709 Da / Num. of mol.: 1 / Fragment: P'2 DNA BINDING DOMAIN, RESIDUES 1-64 Source method: isolated from a genetically manipulated source Details: INTN(1-64) COMPLEX WITH 12 MER DOUBLE STRANDED P'2 DNA Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR EXPERIMENTS ON 13C 15N LABELED PROTEIN, UNLABELED DNA. INTERMOLECULAR NOES WERE MEASURED USING 13C FILTERED 2D NOESY ,13C-EDITED 3D NOESY AND ...Text: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR EXPERIMENTS ON 13C 15N LABELED PROTEIN, UNLABELED DNA. INTERMOLECULAR NOES WERE MEASURED USING 13C FILTERED 2D NOESY ,13C-EDITED 3D NOESY AND 15N-EDITED 3D NOESY EXPERIMENTS |
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Sample preparation
Details | Contents: 7% D2O 93% WATER |
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Sample conditions | Ionic strength: 40 mM / pH: 7 / Pressure: 1.0 atm / Temperature: 310.15 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: MARS, QUEEN, ATNOS CANDID / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 200 / Conformers submitted total number: 20 |