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Open data
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Basic information
Entry | Database: PDB / ID: 1tig | ||||||
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Title | TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN | ||||||
![]() | TRANSLATION INITIATION FACTOR 3 | ||||||
![]() | RIBOSOME BINDING FACTOR / IF3 C-TERMINAL DOMAIN | ||||||
Function / homology | ![]() ribosome disassembly / translation initiation factor activity / ribosome binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Biou, V. / Shu, F. / Ramakrishnan, V. | ||||||
![]() | ![]() Title: X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. Authors: Biou, V. / Shu, F. / Ramakrishnan, V. #1: ![]() Title: Prokaryotic Translation Initiation Factor If3 is an Elongated Protein Consisting of Two Crystallizable Domains Authors: Kycia, J.H. / Biou, V. / Shu, F. / Gerchman, S.E. / Graziano, V. / Ramakrishnan, V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.6 KB | Display | ![]() |
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PDB format | ![]() | 23.7 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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Unit cell |
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Components
#1: Protein | Mass: 10752.569 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Cell line: B834 / Gene: T7 / Plasmid: T7 VECTOR PET13A / Gene (production host): T7 / Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Nonpolymer details | NOTE THAT SOME SOLVENT MOLECULES HAVE AN OCCUPANCY GREATER THAN 1.0. IF IT IS SIGNIFICANTLY GREATER ...NOTE THAT SOME SOLVENT MOLECULES HAVE AN OCCUPANCY GREATER THAN 1.0. IF IT IS SIGNIFICAN |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.43 % Description: THREE EXPERIMENTS WERE CONDUCTED USING MAD DATA COLLECTED AT THREE WAVELENGTHS ON TWO SELENOMETHIONINE CRYSTALS, USING INVERSE BEAM GEOMETRY: WAVELENGTH DATA REDUNDANCY MERGING R VALUE 0. ...Description: THREE EXPERIMENTS WERE CONDUCTED USING MAD DATA COLLECTED AT THREE WAVELENGTHS ON TWO SELENOMETHIONINE CRYSTALS, USING INVERSE BEAM GEOMETRY: WAVELENGTH DATA REDUNDANCY MERGING R VALUE 0.9802 3.8 (2.9) 4.2 (9.0) 0.9795 3.8 (3.) 4.4 (10.9) 0.930 3.9 (3.9) 4.8 (13.6) |
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Crystal grow | *PLUS pH: 8 / Method: unknown |
Components of the solutions | *PLUS Conc.: 2.4 M / Common name: phosphate |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE AREA DETECTOR / Date: Mar 1, 1994 | |||||||||||||||
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Num. obs: 6402 / % possible obs: 99.9 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.042 | |||||||||||||||
Reflection | *PLUS Rmerge(I) obs: 0.042 |
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Processing
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Refinement | Resolution: 2→6 Å / σ(F): 0
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Displacement parameters | Biso mean: 20.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_dihedral_angle_deg / Dev ideal: 23.8 |