+Open data
-Basic information
Entry | Database: PDB / ID: 2yfw | ||||||
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Title | Heterotetramer structure of Kluyveromyces lactis Cse4,H4 | ||||||
Components |
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Keywords | CELL CYCLE / KINETOCHORE / CENTROMERE / HISTONE CHAPERONE / BUDDING YEAST | ||||||
Function / homology | Function and homology information CENP-A containing nucleosome / structural constituent of chromatin / protein heterodimerization activity / DNA binding / nucleus Similarity search - Function | ||||||
Biological species | KLUYVEROMYCES LACTIS NRRL Y-1140 (yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Cho, U.S. / Harrison, S.C. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Recognition of the Centromere-Specific Histone Cse4 by the Chaperone Scm3. Authors: Cho, U.S. / Harrison, S.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2yfw.cif.gz | 247.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2yfw.ent.gz | 202.7 KB | Display | PDB format |
PDBx/mmJSON format | 2yfw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yf/2yfw ftp://data.pdbj.org/pub/pdb/validation_reports/yf/2yfw | HTTPS FTP |
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-Related structure data
Related structure data | 2yfvC 1eqzS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 10746.627 Da / Num. of mol.: 4 / Fragment: HISTONE-FOLD DOMAIN, RESIDUES 93-184 Source method: isolated from a genetically manipulated source Source: (gene. exp.) KLUYVEROMYCES LACTIS NRRL Y-1140 (yeast) Plasmid: PET3A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q6CTI2 #2: Protein | Mass: 11436.441 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) KLUYVEROMYCES LACTIS NRRL Y-1140 (yeast) Plasmid: PET3A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q6CMU6 #3: 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: 2.56 Å3/Da / Density % sol: 52 % / Description: NONE |
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Crystal grow | pH: 8.5 Details: 0.1 M TRIS-HCL, PH8.5, 0.2 M NACL, AND 25% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97914 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 15, 2010 / Details: MIRRORS |
Radiation | Monochromator: CHOZU HLD8-24 MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97914 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→50 Å / Num. obs: 26486 / % possible obs: 99.9 % / Observed criterion σ(I): 1.3 / Redundancy: 3.8 % / Biso Wilson estimate: 61.5 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 1.3 / % possible all: 98.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EQZ Resolution: 2.6→50 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.881 / SU B: 27.088 / SU ML: 0.261 / Cross valid method: THROUGHOUT / ESU R: 0.518 / ESU R Free: 0.319 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 93-104, 128,184 FOR CHAIN A, RESIDUES 1-28,95-103 FOR CHAIN B, RESIDUES 93-103, 123-130, 182-184 FOR CHAIN C, RESIDUES 1-23, 95- ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 93-104, 128,184 FOR CHAIN A, RESIDUES 1-28,95-103 FOR CHAIN B, RESIDUES 93-103, 123-130, 182-184 FOR CHAIN C, RESIDUES 1-23, 95-103 FOR CHAIN D, RESIDUES 126-129 FOR CHAIN E, RESIDUES 1-22, 95-103 FOR CHAIN F, RESIDUES 93-103, 182-184 FOR CHAIN G, RESIDUES 1-22,103 FOR CHAIN H ARE DISORDERED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.266 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→50 Å
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