+Open data
-Basic information
Entry | Database: PDB / ID: 1a1x | ||||||
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Title | CRYSTAL STRUCTURE OF MTCP-1 INVOLVED IN T CELL MALIGNANCIES | ||||||
Components | HMTCP-1 | ||||||
Keywords | PROTO-ONCOGENE / MTCP-1 / ONCOGENE INVOLVED IN T CELL MALIGNANCIES | ||||||
Function / homology | Function and homology information protein serine/threonine kinase activator activity / positive regulation of peptidyl-serine phosphorylation / intracellular signal transduction / protein kinase binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MAD PHASING / Resolution: 2 Å | ||||||
Authors | Fu, Z.Q. / Dubois, G.C. / Song, S.P. / Kulikovskaya, I. / Virgilio, L. / Rothstein, J. / Croce, C.M. / Weber, I.T. / Harrison, R.W. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1998 Title: Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies. Authors: Fu, Z.Q. / Du Bois, G.C. / Song, S.P. / Kulikovskaya, I. / Virgilio, L. / Rothstein, J.L. / Croce, C.M. / Weber, I.T. / Harrison, R.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a1x.cif.gz | 32.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a1x.ent.gz | 22.4 KB | Display | PDB format |
PDBx/mmJSON format | 1a1x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/1a1x ftp://data.pdbj.org/pub/pdb/validation_reports/a1/1a1x | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 12627.200 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P56278 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 37 % | ||||||||||||||||||||
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Crystal grow | pH: 7.8 Details: PROTEIN WAS CRYSTALLIZED FROM 1.5M AMS WITH TRIZMA BUFFER AT PH 7.8 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Sep 1, 1997 |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→21 Å / Num. obs: 7194 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 5.9 % / Rsym value: 0.047 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 5.4 % / Mean I/σ(I) obs: 7.6 / Rsym value: 0.147 / % possible all: 99.3 |
Reflection | *PLUS Rmerge(I) obs: 0.047 |
Reflection shell | *PLUS % possible obs: 99.3 % / Rmerge(I) obs: 0.147 |
-Processing
Software |
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Refinement | Method to determine structure: MAD PHASING / Resolution: 2→6.5 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 22.01 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å / Rfactor Rfree error: 0.031 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.255 |