+
Open data
-
Basic information
Entry | Database: PDB / ID: 4eba | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the Rna14-Rna15 complex | ||||||
![]() |
| ||||||
![]() | STRUCTURAL PROTEIN/RNA BINDING PROTEIN / HAT domain / HEAT repeat / monkeytail / Clp1 / Pcf11 / STRUCTURAL PROTEIN-RNA BINDING PROTEIN complex | ||||||
Function / homology | ![]() mRNA 3'-end processing / mRNA binding / RNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Paulson, A.R. / Tong, L. | ||||||
![]() | ![]() Title: Crystal structure of the Rna14-Rna15 complex. Authors: Paulson, A.R. / Tong, L. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 733.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 603.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 549.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 800.6 KB | Display | |
Data in XML | ![]() | 150.7 KB | Display | |
Data in CIF | ![]() | 202.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4e6hC ![]() 4e85SC C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | The trimers are formed by two Rna14 and one Rna15. |
-
Components
#1: Protein | Mass: 76161.523 Da / Num. of mol.: 6 / Fragment: UNP residues 18-661 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37 Gene: RNA14, KLLA0F26290g / Production host: ![]() ![]() #2: Protein | Mass: 19549.305 Da / Num. of mol.: 3 / Fragment: UNP residues 105-258 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37 Gene: KLLA0F09383g / Production host: ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.87 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 50 mM HEPES 7.0, 1% tryptone, 13% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 9, 2011 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.075 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→50 Å / Num. all: 79000 / Num. obs: 71640 / % possible obs: 90.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 1.7 % / Rmerge(I) obs: 0.055 / Net I/σ(I): 10.9049 |
Reflection shell | Resolution: 3.3→3.42 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.442 / Mean I/σ(I) obs: 1.242 / % possible all: 71.2 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4E85 Resolution: 3.3→47.79 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 371325.06 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 57.2895 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 100.2 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.3→47.79 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS | NCS model details: CONSTR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.3→3.42 Å / Rfactor Rfree error: 0.027 / Total num. of bins used: 10
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file | Serial no: 1 / Param file: protein_rep.param / Topol file: protein.top |