+Open data
-Basic information
Entry | Database: PDB / ID: 1de3 | ||||||
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Title | SOLUTION STRUCTURE OF THE CYTOTOXIC RIBONUCLEASE ALPHA-SARCIN | ||||||
Components | RIBONUCLEASE ALPHA-SARCIN | ||||||
Keywords | HYDROLASE / ALPHA-BETA PROTEIN | ||||||
Function / homology | Function and homology information ribotoxin / rRNA endonuclease activity / negative regulation of cytoplasmic translation / RNA endonuclease activity / lyase activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | Aspergillus giganteus (mold) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Perez-Canadillas, J.M. / Campos-Olivas, R. / Santoro, J. / Lacadena, J. / Martinez del Pozo, A. / Gavilanes, J.G. / Rico, M. / Bruix, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 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: Journal: Biochemistry / Year: 1998 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: Journal: FEBS Lett. / Year: 1996 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1de3.cif.gz | 909.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1de3.ent.gz | 789 KB | Display | PDB format |
PDBx/mmJSON format | 1de3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1de3_validation.pdf.gz | 356.2 KB | Display | wwPDB validaton report |
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Full document | 1de3_full_validation.pdf.gz | 513.2 KB | Display | |
Data in XML | 1de3_validation.xml.gz | 62.5 KB | Display | |
Data in CIF | 1de3_validation.cif.gz | 80.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/de/1de3 ftp://data.pdbj.org/pub/pdb/validation_reports/de/1de3 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Aspergillus giganteus (mold) / Strain: MDH 18894 / Plasmid: PINPGAS / Production host: Escherichia coli (E. coli) / References: UniProt: P00655, EC: 3.1.27.10 |
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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. |
-Sample preparation
Details |
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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 |