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- PDB-1tnt: A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tnt | ||||||
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Title | A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE | ||||||
![]() | MU-TRANSPOSASE | ||||||
![]() | DNA BINDING PROTEIN / DNA-BINDING PROTEIN | ||||||
Function / homology | ![]() Ligases; Forming phosphoric-ester bonds / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 3'-phosphomonoesters / latency-replication decision / transposase activity / DNA transposition / double-stranded DNA endonuclease activity / viral DNA genome replication / ligase activity / DNA integration / DNA replication ...Ligases; Forming phosphoric-ester bonds / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 3'-phosphomonoesters / latency-replication decision / transposase activity / DNA transposition / double-stranded DNA endonuclease activity / viral DNA genome replication / ligase activity / DNA integration / DNA replication / host cell cytoplasm / DNA repair / DNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Clore, G.M. / Clubb, R.T. / Omichinski, J.G. / Gronenborn, A.M. | ||||||
![]() | ![]() Title: A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase. Authors: Clubb, R.T. / Omichinski, J.G. / Savilahti, H. / Mizuuchi, K. / Gronenborn, A.M. / Clore, G.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 754.1 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 341 KB | Display | ![]() |
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Full document | ![]() | 554.9 KB | Display | |
Data in XML | ![]() | 45 KB | Display | |
Data in CIF | ![]() | 71.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: Protein | Mass: 8268.502 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Refinement | Software ordinal: 1 Details: THE 3D SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF MU TRANSPOSASE (MUA76, RESIDUES 1 - 76) WAS SOLVED BY MULTIDIMENSIONAL HETERONUCLEAR-EDITED NMR EXPERIMENTS AND IS BASED ON 1320 ...Details: THE 3D SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF MU TRANSPOSASE (MUA76, RESIDUES 1 - 76) WAS SOLVED BY MULTIDIMENSIONAL HETERONUCLEAR-EDITED NMR EXPERIMENTS AND IS BASED ON 1320 EXPERIMENTAL RESTRAINTS COMPRISING THE FOLLOWING: (A) 1192 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS (308 SEQUENTIAL, 266 SHORT RANGE 1 , |I-J| <=5, 323 LONG RANGE |I-J|>5, AND 295 INTRARESIDUE (B) 18 DISTANCE RESTRAINTS FOR 9 BACKBONE HYDROGEN BONDS (C) 36 HN-CAH COUPLING CONSTANT RESTRAINTS (D) 74 TORSION ANGLE RESTRAINTS (40 PHI, 23 CHI1 AND 11 CHI2). A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS HAVE BEEN DEPOSITED WITH THE BROOKHAVEN DATA BANK. THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. & GRONENBORN, A.M. (1988) FEBS LETT 229, 317 - 324 ALL STRUCTURAL STATISTICS ARE GIVEN IN REF. 1. PDB ENTRY 1TNS IS THE RESTRAINED MINIMIZED AVERAGE STRUCTURE: (SA)R. THIS IS OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 33 DYNAMICAL SIMULATED ANNEALING (SA) STRUCTURES BEST FITTED TO RESIDUES 3 - 36 AND 45 - 65 AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE LAST NUMBER COLUMN IN THIS SET OF COORDINATES (THE B-FACTOR COLUMN IN X-RAY STRUCTURES) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE NUMBERS IN THE LAST COLUMN OF THE INDIVIDUAL STRUCTURES HAVE NO MEANING. RESIDUES 1 - 2, 66 - 76, AND 37 - 44 ARE DISORDERED IN SOLUTION. THIS ENTRY CONTAINS THE 33 INDIVIDUAL STRUCTURES. |
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NMR ensemble | Conformers submitted total number: 33 |