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Open data
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Basic information
Entry | Database: PDB / ID: 1w9g | ||||||
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Title | Structure of ERH (Enhencer of Rudimentary Gene) | ||||||
![]() | ENHANCER OF RUDIMENTARY HOMOLOG | ||||||
![]() | ERH(ENHANCER OF RUDIMENTARY HOMOLOG) / DCOH(DIMERIZATION COFACTOR OF HNF1) | ||||||
Function / homology | ![]() pyrimidine nucleoside metabolic process / methylosome / methyl-CpG binding / nucleobase-containing compound metabolic process / midbody / RNA binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wan, C. / Tempel, W. / Liu, Z. / Wang, B.-C. / Rose, R.B. | ||||||
![]() | ![]() Title: Structure of the Conserved Transcriptional Repressor Enhancer of Rudimentary Homolog Authors: Wan, C. / Tempel, W. / Liu, Z. / Wang, B.-C. / Rose, R.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.2 KB | Display | ![]() |
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PDB format | ![]() | 39.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 371.4 KB | Display | ![]() |
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Full document | ![]() | 378.3 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 9.8 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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Unit cell |
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Components
#1: Protein | Mass: 12273.927 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: MAMMALIAN GENE COLLECTION (MGC) IMAGE NUMBER 3507241 AND GENE BANK IDENTIFIER BC014301 Plasmid: PET24B / Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 51 % |
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Crystal grow | pH: 7.5 Details: 10% ISOPROPANOL, 20% PEG4000, 0.1M HEPES (PH7.5), pH 7.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 17, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2→42.9 Å / Num. obs: 15585 / % possible obs: 95.3 % / Observed criterion σ(I): 2.8 / Redundancy: 2.5 % / Rmerge(I) obs: 0.03 |
Reflection shell | Resolution: 2→2.11 Å / % possible all: 93.9 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2→43.03 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.895 / SU B: 4.878 / SU ML: 0.136 / Cross valid method: THROUGHOUT / ESU R: 0.187 / ESU R Free: 0.18 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 103 AND 104 OF EACH MONOMER ARE DISORDERD. PRO48B, SER49B, ILE50B ARE DISORDERD. THE SIDE CHAINS OF RESIDUES ARG42A AND B, ASN46B, ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 103 AND 104 OF EACH MONOMER ARE DISORDERD. PRO48B, SER49B, ILE50B ARE DISORDERD. THE SIDE CHAINS OF RESIDUES ARG42A AND B, ASN46B, SER49A,ILE50A, THR51B, LYS12A AND B, GLU23B, LYS34B, LYS41A AND B, ASP75B, GLN77A AND B, GLN100A AND B, GLN101A AND B ARE DISORDERED AND OMITED FROM THIS MODEL
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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: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.97 Å2
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Refinement step | Cycle: LAST / Resolution: 2→43.03 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.05 Å / Total num. of bins used: 20 /
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