+
Open data
-
Basic information
Entry | Database: PDB / ID: 1fzu | ||||||
---|---|---|---|---|---|---|---|
Title | RNAse T1 V78A mutant | ||||||
![]() | GUANYL-SPECIFIC RIBONUCLEASE T1 | ||||||
![]() | HYDROLASE / ribonuclease | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | De Vos, S. / Loris, R. / Steyaert, J. | ||||||
![]() | ![]() Title: Hydrophobic core manipulations in ribonuclease T1. Authors: De Vos, S. / Backmann, J. / Prevost, M. / Steyaert, J. / Loris, R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 30.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 22.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 794.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 794.6 KB | Display | |
Data in XML | ![]() | 7.3 KB | Display | |
Data in CIF | ![]() | 9.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fysC ![]() 1g02C ![]() 1i2eC ![]() 1i2fC ![]() 1i2gC ![]() 1i3fC ![]() 1i3iC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 11066.641 Da / Num. of mol.: 1 / Mutation: V78A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-2GP / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.47 % | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: MPD, calcium chloride, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 4.2 / Method: vapor diffusion, hanging drop / Details: Zegers, I., (1998) Nat.Struct.Biol., 5, 280. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 17, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→15 Å / Num. all: 9478 / Num. obs: 9478 / % possible obs: 99.1 % / Observed criterion σ(F): -6 / Observed criterion σ(I): -3 / Redundancy: 3.83 % / Biso Wilson estimate: -12.55 Å2 / Rmerge(I) obs: 0.099 / Net I/σ(I): 11.99 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.257 / Num. unique all: 914 / % possible all: 97.6 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.8→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→15 Å
| ||||||||||||||||||||
Refine LS restraints |
|