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- PDB-1vmo: CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vmo | ||||||
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Title | CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRY | ||||||
![]() | VITELLINE MEMBRANE OUTER LAYER PROTEIN I | ||||||
![]() | MEMBRANE PROTEIN | ||||||
Function / homology | Vitelline membrane outer layer protein I (VOMI) / Vitelline membrane outer layer protein I (VOMI) / Vitelline membrane outer layer protein I (VOMI) superfamily / Vitelline membrane outer layer protein I (VOMI) / Aligned Prism / Vitelline Membrane Outer Layer Protein I, subunit A / extracellular space / Mainly Beta / Vitelline membrane outer layer protein 1![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Shimizu, T. / Vassylyev, D.G. / Kido, S. / Doi, Y. / Morikawa, K. | ||||||
![]() | ![]() Title: Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry. Authors: Shimizu, T. / Vassylyev, D.G. / Kido, S. / Doi, Y. / Morikawa, K. #1: ![]() Title: Crystallization and Preliminary Crystallographic Data of Vitelline Membrane Outer Layer Protein 1 Vmo1 Authors: Shimizu, T. / Morikawa, K. / Kido, S. / Doi, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.4 KB | Display | ![]() |
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PDB format | ![]() | 57.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.2 KB | Display | ![]() |
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Full document | ![]() | 377.7 KB | Display | |
Data in XML | ![]() | 8.7 KB | Display | |
Data in CIF | ![]() | 13.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.9941, 0.10496, 0.02729), Vector: |
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Components
#1: Protein | Mass: 18000.307 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE HAS NOT BEEN REPORTED. A PAPER DESCRIBING | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.82 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 4.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.2 Å / Num. obs: 13489 / % possible obs: 83.4 % / Rmerge(I) obs: 0.0459 |
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Processing
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Refinement | Resolution: 2.2→6 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.188 / Rfactor Rwork: 0.188 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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