[English] 日本語
![](img/lk-miru.gif)
- PDB-1gto: HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1gto | ||||||
---|---|---|---|---|---|---|---|
Title | HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT | ||||||
![]() | ROP | ||||||
![]() | TRANSCRIPTION REGULATION / TURN / HELIX PACKING / CRYSTAL CONTACTS | ||||||
Function / homology | Helix Hairpins - #230 / Regulatory protein Rop / Rop-like superfamily / Rop protein / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / identical protein binding / Regulatory protein rop![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Agrawal, V. / Predki, P. / Regan, L. / Brunger, A.T. | ||||||
![]() | ![]() Title: Amino-acid substitutions in a surface turn modulate protein stability. Authors: Predki, P.F. / Agrawal, V. / Brunger, A.T. / Regan, L. #1: ![]() Title: Amino-Acid Substitutions in a Surface Turn Modulate Protein Stability Authors: Predki, P.F. / Agrawal, V. / Brunger, A.T. / Regan, L. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 46.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 34.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 441.4 KB | Display | |
Data in XML | ![]() | 9.4 KB | Display | |
Data in CIF | ![]() | 12.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | THREE ROP PROTOMERS ARE IN THE ASYMMETRIC UNIT, TWO OF WHICH ARE RELATED BY A NON-CRYSTALLOGRAPHIC TWO-FOLD RELATIONSHIP FORMING A ROP DIMER (B/C). THE THIRD ROP PROTOMER (A) FORMS ANOTHER ROP DIMER THROUGH A CRYSTALLOGRAPHIC SYMMETRY MATE. |
-
Components
#1: Protein | Mass: 6991.702 Da / Num. of mol.: 3 / Mutation: M1G, D30G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Compound details | THE HYPERSTABLE MUTANT, ROP D30G, SHOWED LITTLE INTRAMOLECULAR CHANGE FROM WILD TYPE. THE R.M.S ...THE HYPERSTABL | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.68 % | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 6.8 / Method: unknown / Details: Banner, D.W., (1987) J. Mol. Biol., 196, 657. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
---|---|
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 15, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Redundancy: 9 % / Biso Wilson estimate: 28.8 Å2 / Rmerge(I) obs: 0.049 |
Reflection | *PLUS Highest resolution: 1.82 Å / Lowest resolution: 20 Å / Num. obs: 17635 / % possible obs: 98.9 % |
Reflection shell | *PLUS Highest resolution: 1.82 Å / Lowest resolution: 1.87 Å / % possible obs: 99.4 % / Rmerge(I) obs: 0.241 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.82→20 Å / Rfactor Rfree error: 0.008 / Cross valid method: THROUGHOUT / σ(F): 2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.2 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.82→20 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.82→1.9 Å / Rfactor Rfree error: 0.024
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|