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- PDB-1k6f: Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1k6f | ||||||
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Title | Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3 | ||||||
![]() | collagen triple helix | ||||||
![]() | STRUCTURAL PROTEIN / collagen stability / puckering / amino acid preferences / triple helix | ||||||
Function / homology | Saimiri transformation-associated protein / extracellular matrix structural constituent conferring tensile strength / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / extracellular matrix organization / extracellular space / membrane / Saimiri transformation-associated protein![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Berisio, R. / Vitagliano, L. / Mazzarella, L. / Zagari, A. | ||||||
![]() | ![]() Title: Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3) Authors: Berisio, R. / Vitagliano, L. / Mazzarella, L. / Zagari, A. #1: ![]() Title: Preferred proline puckering in cis and trans peptide groups: implications for collagen stability Authors: Vitagliano, L. / Berisio, R. / Mastrangelo, A. / Mazzarella, L. / Zagari, A. #2: ![]() Title: Structural Bases of Collagen Stabilization Induced by Proline Hydroxylation Authors: Vitagliano, L. / Berisio, R. / Mazzarella, L. / Zagari, A. #3: ![]() Title: Crystal Structure of a Collagen-Like Polypeptide with Repeating Sequence Pro-Hyp-Gly at 1.4 A Resolution: Implications for Collagen Hydration Authors: Berisio, R. / Vitagliano, L. / Mazzarella, L. / Zagari, A. | ||||||
History |
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Remark 999 | SEQUENCE An appropriate sequence database reference was not available at the time of processing. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.5 KB | Display | ![]() |
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PDB format | ![]() | 60.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 355.7 KB | Display | ![]() |
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Full document | ![]() | 356.1 KB | Display | |
Data in XML | ![]() | 4.1 KB | Display | |
Data in CIF | ![]() | 8.2 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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3 | ![]()
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Unit cell |
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Components
#1: Protein/peptide | Mass: 2530.828 Da / Num. of mol.: 6 / Source method: obtained synthetically / Details: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. / References: UniProt: Q80BK4*PLUS #2: Water | ChemComp-HOH / | |
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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 | Temperature: 294 K Method: microdialysis carried out in microgravity conditions pH: 5.6 Details: HAc/NaAc, pH 5.6, microdialysis carried out in microgravity conditions, temperature 21K | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: microgravity conditions | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE | |||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Num. all: 29431 / Num. obs: 23121 | |||||||||||||||
Reflection | *PLUS Highest resolution: 1.3 Å / Lowest resolution: 15 Å / % possible obs: 88.3 % / Rmerge(I) obs: 0.09 |
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Processing
Software |
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Refinement | Method to determine structure: ARP/WARP / Resolution: 1.3→15 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.3→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.3→1.33 Å
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.3 Å / Lowest resolution: 15 Å / σ(F): 0 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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