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- PDB-1atd: HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTIO... -
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Basic information
Entry | Database: PDB / ID: 1atd | ||||||
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Title | HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE | ||||||
![]() | ASCARIS TRYPSIN INHIBITOR | ||||||
![]() | PROTEINASE INHIBITOR(TRYPSIN) | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Clore, G.M. / Grasberger, B.L. / Gronenborn, A.M. | ||||||
![]() | ![]() Title: High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Authors: Grasberger, B.L. / Clore, G.M. / Gronenborn, A.M. #1: ![]() Title: Sequential Resonance Assignment and Secondary Structure Determination of the Ascaris Trypsin Inhibitor, a Member of a Novel Class of Proteinase Inhibitors Authors: Gronenborn, A.M. / Nilges, M. / Peanasky, R.J. / Clore, G.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 564.1 KB | Display | ![]() |
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PDB format | ![]() | 490.6 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6807.853 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: ![]() |
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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 STRUCTURE OF THE PH 4.75 FORM OF THE ASCARIS TRYPSIN INHIBITOR IN SOLUTION BY NMR IS BASED ON 1078 EXPERIMENTAL RESTRAINTS COMPRISING: 43 SHORT RANGE (1 < |I-J| 5) INTERRESIDUE ...Details: THE 3D STRUCTURE OF THE PH 4.75 FORM OF THE ASCARIS TRYPSIN INHIBITOR IN SOLUTION BY NMR IS BASED ON 1078 EXPERIMENTAL RESTRAINTS COMPRISING: 43 SHORT RANGE (1 < |I-J| <=5) AND 218 LONG RANGE (|I-J|>5) INTERRESIDUE INTERPROTON DISTANCE RESTRAINTS, 320 INTRARESIDUE INTERPROTON DISTANCE RESTRAINTS, 48 DISTANCE RESTRAINTS FOR 4 HYDROGEN BONDS, AND 59 PHI, 49 PSI AND 41 CHI1 TORSION ANGLE RESTRAINTS. A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS HAS 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 29, 317-324 ALL STRUCTURAL STATISTICS ARE GIVEN IN REFERENCE 1. THE RESTRAINED MINIMIZED AVERAGE STRUCTURE (SA)R IS PRESENTED IN PROTEIN DATA BANK ENTRY 1ATA. THIS IS OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 32 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 5 - 60, AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 IN ENTRY 1ATA (THE B VALUE FIELD IN X-RAY STRUCTURES) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE QUANTITIES IN THIS FIELD OF THE INDIVIDUAL STRUCTURES IN THIS ENTRY HAVE NO MEANING. |
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NMR ensemble | Conformers submitted total number: 32 |