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Open data
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Basic information
Entry | Database: PDB / ID: 1de3 | ||||||
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Title | SOLUTION STRUCTURE OF THE CYTOTOXIC RIBONUCLEASE ALPHA-SARCIN | ||||||
![]() | RIBONUCLEASE ALPHA-SARCIN | ||||||
![]() | HYDROLASE / ALPHA-BETA PROTEIN | ||||||
Function / homology | ![]() ribotoxin / rRNA endonuclease activity / negative regulation of cytoplasmic translation / RNA endonuclease activity / lyase activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Perez-Canadillas, J.M. / Campos-Olivas, R. / Santoro, J. / Lacadena, J. / Martinez del Pozo, A. / Gavilanes, J.G. / Rico, M. / Bruix, M. | ||||||
![]() | ![]() Title: The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity. Authors: Perez-Canadillas, J.M. / Santoro, J. / Campos-Olivas, R. / Lacadena, J. / Martinez del Pozo, A. / Gavilanes, J.G. / Rico, M. / Bruix, M. #1: ![]() Title: Characterization of pKa Values and Titration Shifts in the Cytotoxic Ribonuclease alpha-Sarcin by NMR. Relationship Between Electrostatic Interactions, Structure, and Catalytic Function. Authors: Perez-Canadillas, J.M. / Campos-Olivas, R. / Lacadena, J. / Martinez del Pozo, A. / Gavilanes, J.G. / Santoro, J. / Rico, M. / Bruix, M. #2: ![]() Title: Structural Basis for the Catalytic Mechanism and Substrate Specificity of the Ribonuclease alpha-Sarcin. Authors: Campos-Olivas, R. / Bruix, M. / Santoro, J. / Martinez del Pozo, A. / Lacadena, J. / Gavilanes, J.G. / Rico, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 909.3 KB | Display | ![]() |
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PDB format | ![]() | 789 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 356.2 KB | Display | ![]() |
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Full document | ![]() | 513.2 KB | Display | |
Data in XML | ![]() | 62.5 KB | Display | |
Data in CIF | ![]() | 80.8 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: 17012.998 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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NMR experiment |
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NMR details | Text: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR TECHNIQUES. |
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Sample preparation
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2777 RESTRAINTS, 2658 ARE NOE-DERIVED DISTANCE CONSTRAINTS AND 119 DIHEDRAL PHI ANGLE RESTRAINTS. THE STRUCTURES WERE ENERGY MINIMISED WITH THE GROMOS FORCE FIELD. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 47 / Conformers submitted total number: 20 |