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Open data
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Basic information
Entry | Database: PDB / ID: 1bir | ||||||
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Title | RIBONUCLEASE T1, PHE 100 TO ALA MUTANT COMPLEXED WITH 2' GMP | ||||||
![]() | RIBONUCLEASE T1 | ||||||
![]() | ENDORIBONUCLEASE / HYDROLASE / NUCLEASE | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Doumen, J. / Gonciarz, M. / Zegers, I. / Loris, R. / Wyns, L. / Steyaert, J. | ||||||
![]() | ![]() Title: A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1. Authors: Doumen, J. / Gonciarz, M. / Zegers, I. / Loris, R. / Wyns, L. / Steyaert, J. #1: ![]() Title: Role of Histidine-40 in Ribonuclease T1 Catalysis: Three-Dimensional Structures of the Partially Active His40Lys Mutant Authors: Zegers, I. / Verhelst, P. / Choe, H.W. / Steyaert, J. / Heinemann, U. / Saenger, W. / Wyns, L. #2: ![]() Title: Three-Dimensional Structure of the Ribonuclease T1 2'-Gmp Complex at 1.9-A Resolution Authors: Arni, R. / Heinemann, U. / Tokuoka, R. / Saenger, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 52 KB | Display | ![]() |
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PDB format | ![]() | 40.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 16.5 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.9963, 0.0852, -0.0065), Vector: |
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Components
#1: Protein | Mass: 11018.598 Da / Num. of mol.: 2 / Mutation: F100A Source method: isolated from a genetically manipulated source Details: COMPLEX WITH 2'-GMP / Source: (gene. exp.) ![]() ![]() Description: STEYAERT ET AL. (1990) BIOCHEMISTRY 29, 9064-9072 Gene: SYNTHETIC GENE / Plasmid: PMC5-RT1 / Gene (production host): SYNTHETIC GENE / Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.04 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.2 / Method: vapor diffusion, sitting drop / Details: used to seeding | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→10 Å / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.056 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 17890 / % possible obs: 99.7 % / Rmerge(I) obs: 0.047 |
Reflection shell | *PLUS Highest resolution: 1.82 Å / Lowest resolution: 1.9 Å / % possible obs: 100 % / Rmerge(I) obs: 0.056 |
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Processing
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Refinement | Resolution: 1.8→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 14.84 Å2 | ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.24 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
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