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- PDB-1trp: X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1trp | ||||||
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Title | X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1 | ||||||
![]() | 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 | ![]() | ||||||
![]() | Schluckebier, G. / Saenger, W. | ||||||
![]() | ![]() Title: X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. Authors: Schubert, W.D. / Schluckebier, G. / Backmann, J. / Granzin, J. / Kisker, C. / Choe, H.W. / Hahn, U. / Pfeil, W. / 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 | ![]() | 50.3 KB | Display | ![]() |
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PDB format | ![]() | 39.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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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Atom site foot note | 1: CIS PROLINE - PRO A 39 / 2: CIS PROLINE - PRO A 55 / 3: CIS PROLINE - PRO B 239 / 4: CIS PROLINE - PRO B 255 |
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Components
#1: Protein | Mass: 11094.694 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #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: 2.14 Å3/Da / Density % sol: 42.53 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, sitting drop / pH: 4.2 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 6347 / % possible obs: 84 % / Observed criterion σ(F): 1 / Num. measured all: 10071 / Rmerge F obs: 0.054 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.4→10 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.16 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 1.24 |