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Open data
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Basic information
Entry | Database: PDB / ID: 2xjz | ||||||
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Title | Crystal structure of the LMO2:LDB1-LID complex, C2 crystal form | ||||||
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![]() | ONCOPROTEIN / T-CELL LEUKEMIA / PROTO-ONCOGENE / TRANSCRIPTION / DEVELOPMENTAL PROTEIN | ||||||
Function / homology | ![]() Expression and translocation of olfactory receptors / regulation of kinase activity / cellular component assembly / negative regulation of erythrocyte differentiation / positive regulation of hemoglobin biosynthetic process / cerebellar Purkinje cell differentiation / epithelial structure maintenance / bHLH transcription factor binding / beta-catenin-TCF complex / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery ...Expression and translocation of olfactory receptors / regulation of kinase activity / cellular component assembly / negative regulation of erythrocyte differentiation / positive regulation of hemoglobin biosynthetic process / cerebellar Purkinje cell differentiation / epithelial structure maintenance / bHLH transcription factor binding / beta-catenin-TCF complex / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / LIM domain binding / gastrulation with mouth forming second / Cardiogenesis / anterior/posterior axis specification / regulation of focal adhesion assembly / cell leading edge / somatic stem cell population maintenance / positive regulation of cell adhesion / hair follicle development / regulation of cell migration / transcription coregulator binding / positive regulation of transcription elongation by RNA polymerase II / neuron differentiation / Wnt signaling pathway / Regulation of expression of SLITs and ROBOs / : / RUNX1 regulates transcription of genes involved in differentiation of HSCs / nervous system development / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription regulator complex / transcription by RNA polymerase II / transcription coactivator activity / cell adhesion / negative regulation of DNA-templated transcription / chromatin binding / chromatin / enzyme binding / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / identical protein binding / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | El Omari, K. / Karia, D. / Porcher, C. / Mancini, E.J. | ||||||
![]() | ![]() Title: Structure of the Leukemia Oncogene Lmo2: Implications for the Assembly of a Hematopoietic Transcription Factor Complex. Authors: El Omari, K. / Hoosdally, S.J. / Tuladhar, K. / Karia, D. / Vyas, P. / Patient, R. / Porcher, C. / Mancini, E.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 327.4 KB | Display | ![]() |
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PDB format | ![]() | 270.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 506.8 KB | Display | ![]() |
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Full document | ![]() | 520.5 KB | Display | |
Data in XML | ![]() | 28.5 KB | Display | |
Data in CIF | ![]() | 39 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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4 | ![]()
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5 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15388.909 Da / Num. of mol.: 5 / Fragment: RESIDUES 26-156 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 3970.351 Da / Num. of mol.: 5 / Fragment: RESIDUES 334-368 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-ZN / #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49 % / Description: NONE |
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Crystal grow | pH: 5 / Details: 1.6 M NACL, 100 MM MES PH5 AND 1 MM DTT |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 15, 2009 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.28226 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. obs: 27216 / % possible obs: 96.7 % / Observed criterion σ(I): 1.8 / Redundancy: 7.3 % / Biso Wilson estimate: 80.34 Å2 / Rmerge(I) obs: 0.14 / Net I/σ(I): 18.8 |
Reflection shell | Resolution: 2.8→2.85 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.84 / Mean I/σ(I) obs: 1.8 / % possible all: 73.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.8→48.32 Å / Cor.coef. Fo:Fc: 0.8949 / Cor.coef. Fo:Fc free: 0.8872 / Cross valid method: THROUGHOUT / σ(F): 0 Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=ZN CL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=6144. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. ...Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=ZN CL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=6144. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=22.
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Displacement parameters | Biso mean: 87.85 Å2
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Refine analyze | Luzzati coordinate error obs: 0.518 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→48.32 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.91 Å / Total num. of bins used: 14
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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