[English] 日本語
![](img/lk-miru.gif)
- PDB-1gff: THE ATOMIC STRUCTURE OF THE DEGRADED PROCAPSID PARTICLE OF THE BA... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1gff | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | THE ATOMIC STRUCTURE OF THE DEGRADED PROCAPSID PARTICLE OF THE BACTERIOPHAGE G4: INDUCED STRUCTURAL CHANGES IN THE PRESENCE OF CALCIUM IONS AND FUNCTIONAL IMPLICATIONS | |||||||||
![]() | (BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ) x 3 | |||||||||
![]() | VIRUS / COAT PROTEIN / Icosahedral virus | |||||||||
Function / homology | ![]() modulation by virus of host process / T=1 icosahedral viral capsid / viral capsid / host cell cytoplasm / symbiont entry into host cell / virion attachment to host cell / structural molecule activity / DNA binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Rossmann, M.G. | |||||||||
![]() | ![]() Title: Atomic structure of the degraded procapsid particle of the bacteriophage G4: induced structural changes in the presence of calcium ions and functional implications. Authors: McKenna, R. / Bowman, B.R. / Ilag, L.L. / Rossmann, M.G. / Fane, B.A. #1: ![]() Title: Analysis of the Single-Stranded DNA Bacteriophage PhiX174 Refined at a Resolution of 3.0 Angstroms Authors: McKenna, R. / Ilag, L.L. / Rossmann, M.G. #2: ![]() Title: Atomic Structure of Single-Stranded DNA Bacteriophage PhiX174 and its Functional Implications Authors: McKenna, R. / Xia, D. / Willingmann, P. / Ilag, L.L. / Krishnaswamy, S. / Rossmann, M.G. / Olson, N.H. / Baker, T.S. / Incardona, N.L. #3: ![]() Title: Biology of the Bacteriophage PhiX174 Authors: Hayashi, M. / Aoyama, A. / Delwood, L. / Richardson, D.L. / Hayashi, M.N. #4: ![]() Title: Comparative DNA Sequence Analysis of the G4 and PhiX174 Genomes Authors: Godson, G.N. / Fiddles, J.C. / Barrell, B.G. / Sanger, F. | |||||||||
History |
| |||||||||
Remark 700 | SHEET STRAND 4 OF SHEET G2 IS BIFURCATED. SHEET G2 IS REPRESENTED BY TWO SHEETS G2A AND G2B WHICH ...SHEET STRAND 4 OF SHEET G2 IS BIFURCATED. SHEET G2 IS REPRESENTED BY TWO SHEETS G2A AND G2B WHICH DIFFER ONLY IN STRAND 4. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 118.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 87.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 382.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 467.9 KB | Display | |
Data in XML | ![]() | 25.4 KB | Display | |
Data in CIF | ![]() | 35.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| x 60||||||||||||||||||||||||||||||||||||||||||||
2 |
| ||||||||||||||||||||||||||||||||||||||||||||
3 | ![]()
| x 5||||||||||||||||||||||||||||||||||||||||||||
4 | ![]()
| x 6||||||||||||||||||||||||||||||||||||||||||||
5 | ![]()
| ||||||||||||||||||||||||||||||||||||||||||||
6 | ![]()
| x 20||||||||||||||||||||||||||||||||||||||||||||
Unit cell |
| ||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | ||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-
Components
#1: Protein | Mass: 48611.625 Da / Num. of mol.: 1 / Mutation: AM(E)W4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 18837.395 Da / Num. of mol.: 1 / Mutation: AM(E)W4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein/peptide | Mass: 2822.318 Da / Num. of mol.: 1 / Mutation: AM(E)W4 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal grow | *PLUS pH: 6.8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
-
Processing
Refinement | Resolution: 3→6 Å / Rfactor Rwork: 0.352 / σ(F): 3 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement step | Cycle: LAST / Resolution: 3→6 Å
| ||||||||||||
Refinement | *PLUS Rfactor obs: 0.352 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: o_bond_d / Dev ideal: 0.031 |