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Yorodumi- PDB-2d3h: Crystal structures of collagen model peptides (Pro-Pro-Gly)4-Hyp-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2d3h | ||||||
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Title | Crystal structures of collagen model peptides (Pro-Pro-Gly)4-Hyp-Hyp-Gly-(Pro-Pro-Gly)4 | ||||||
Components | COLLAGEN MODEL PEPTIDES (PRO-PRO-GLY)4-HYP-HYP-GLY-(PRO-PRO-GLY)4 | ||||||
Keywords | STRUCTURAL PROTEIN / COLLAGEN / TRIPLE-HELIX / HYDROXYPROLINE | ||||||
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 Function and homology information | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.22 Å | ||||||
Authors | Wu, G. / Noguchi, K. / Okuyama, K. / Mizuno, K. / Bachinger, H.P. | ||||||
Citation | Journal: Biopolymers / Year: 2009 Title: High-resolution structures of collagen-like peptides [(Pro-Pro-Gly)(4)-Xaa-Yaa-Gly-(Pro-Pro-Gly)(4)]: Implications for triple-helix hydration and Hyp(X) puckering. Authors: Okuyama, K. / Hongo, C. / Wu, G. / Mizuno, K. / Noguchi, K. / Ebisuzaki, S. / Tanaka, Y. / Nishino, N. / Bachinger, H.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2d3h.cif.gz | 63.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2d3h.ent.gz | 51.4 KB | Display | PDB format |
PDBx/mmJSON format | 2d3h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d3/2d3h ftp://data.pdbj.org/pub/pdb/validation_reports/d3/2d3h | HTTPS FTP |
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-Related structure data
Related structure data | 2d3fC 2cuoS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein/peptide | Mass: 2311.547 Da / Num. of mol.: 6 / Source method: obtained synthetically Details: THIS COLLAGEN MODEL TRIPLETT WAS CHEMICALLY SYSTHESIZED. Hyp-Hyp-Gly guest in Pro-Pro-Gly host peptide. References: UniProt: Q80BK4*PLUS #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.83 Å3/Da / Density % sol: 32.6 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: PEG 1000, ACETATE BUFFER, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 0.978 / Wavelength: 0.978 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 30, 2004 / Details: 1.1-M-LONG BENT-PLANE MIRROR |
Radiation | Monochromator: Trianglualr Si(111) with an asymmetric angle of 7.8 Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 1.22→26.61 Å / Num. obs: 32577 / % possible obs: 98.7 % / Observed criterion σ(F): 1 / Redundancy: 3.52 % / Rmerge(I) obs: 0.082 / Net I/σ(I): 4.5 |
Reflection shell | Resolution: 1.22→1.26 Å / Redundancy: 3.79 % / Rmerge(I) obs: 0.287 / Mean I/σ(I) obs: 2.2 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB 2CUO Resolution: 1.22→8 Å / Num. parameters: 10425 / Num. restraintsaints: 12967 / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber Details: THE POLYMER STRUCTURE CAN BE GENERATED FROM THE SUBMITTED ASYMMETRIC UNIT BY APPLYING THE (0 0 1) TRANSLATION USING FRACTIONAL COORDINATES. BOTH UP- AND DOWN- PUCKERINGS WERE OBSERVED FOR ...Details: THE POLYMER STRUCTURE CAN BE GENERATED FROM THE SUBMITTED ASYMMETRIC UNIT BY APPLYING THE (0 0 1) TRANSLATION USING FRACTIONAL COORDINATES. BOTH UP- AND DOWN- PUCKERINGS WERE OBSERVED FOR PROLINE RING AT THE X POSITION OF THE GLY-X-Y SEQUENCE. ANISOTROPIC REFINEMENT REDUCED FREE R.
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Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 823 / Occupancy sum non hydrogen: 1158 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.22→8 Å
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Refine LS restraints |
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