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- PDB-1rnt: RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF T... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rnt | ||||||
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Title | RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF THE RIBONUCLEASE T1(ASTERISK)2(PRIME)-GUANYLIC ACID COMPLEX AT 1.9 ANGSTROMS RESOLUTION | ||||||
![]() | RIBONUCLEASE T1 ISOZYME | ||||||
![]() | HYDROLASE(ENDORIBONUCLEASE) | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Saenger, W. / Arni, R. / Heinemann, U. / Tokuoka, R. | ||||||
![]() | Journal: Acta Crystallogr.,Sect.B / Year: 1987 Title: Restrained Least-Squares Refinement of the Crystal Structure of the Ribonuclease T1(Asterisk)2(Prime)-Guanylic Acid Complex at 1.9 Angstroms Resolution Authors: Arni, R. / Heinemann, U. / Maslowska, M. / Tokuoka, R. / Saenger, W. #1: ![]() Title: Three-Dimensional Structure of the Ribonuclease T1(Asterisk)2(Prime)-Gmp Complex at 1.9-Angstroms Resolution Authors: Arni, R. / Heinemann, U. / Tokuoka, R. / Saenger, W. #2: ![]() Title: Struktur Und Funktion Des Enzyms Ribonuclease T1 (German) Authors: Arni, R. / Heinemann, U. / Saenger, W. #3: ![]() Title: Mechanism of Guanosine Recognition and RNA Hydrolysis by Ribonuclease T1 Authors: Heinemann, U. / Saenger, W. #4: ![]() Title: The Structural and Sequence Homology of a Family of Microbial Ribonucleases Authors: Hill, C. / Dodson, G. / Heinemann, U. / Saenger, W. / Mitsui, Y. / Nakamura, K. / Borisov, S. / Tischenko, G. / Polyakov, K. / Pavlovsky, S. #5: ![]() Title: Ribonuclease T1. Mechanism of Specific Guanine Recognition and RNA Hydrolysis Authors: Heinemann, U. / Saenger, W. #6: ![]() Title: Crystallographic Study of Mechanism of Ribonuclease T1-Catalysed Specific RNA Hydrolysis Authors: Heinemann, U. / Saenger, W. #7: ![]() Title: Specific Protein-Nucleic Acid Recognition in Ribonuclease T1-2(Prime)-Guanylic Acid Complex. An X-Ray Study Authors: Heinemann, U. / Saenger, W. #8: ![]() Title: Crystallization of a Complex between Ribonuclease T1 and 2(Prime)-Guanylic Acid Authors: Heinemann, U. / Wernitz, M. / Paehler, A. / Saenger, W. / Menke, G. / Rueterjans, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 30.4 KB | Display | ![]() |
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PDB format | ![]() | 23.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 838.9 KB | Display | ![]() |
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Full document | ![]() | 840.5 KB | Display | |
Data in XML | ![]() | 8.1 KB | Display | |
Data in CIF | ![]() | 10.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES 39 AND 55 ARE CIS-PROLINES. |
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Components
#1: Protein | Mass: 11094.694 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-2GP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.43 % |
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Crystal grow | *PLUS Method: other / Details: Heinemann, U., (1980) Eur. J. Biochem., 109, 109. |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 6788 / % possible obs: 93 % / Observed criterion σ(I): 1 / Num. measured all: 23819 / Rmerge(I) obs: 0.088 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→6 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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