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Open data
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Basic information
Entry | Database: PDB / ID: 2v5r | ||||||
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Title | Structural basis for Dscam isoform specificity | ||||||
![]() | DSCAM![]() | ||||||
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Function / homology | ![]() detection of molecule of bacterial origin / mushroom body development / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Meijers, R. / Puettmann-Holgado, R. / Skiniotis, G. / Liu, J.-H. / Walz, T. / Schmucker, D. / Wang, J.-H. | ||||||
![]() | ![]() Title: Structural Basis of Dscam Isoform Specificity Authors: Meijers, R. / Puettmann-Holgado, R. / Skiniotis, G. / Liu, J.-H. / Walz, T. / Wang, J.-H. / Schmucker, D. | ||||||
Validation Report | ![]() ![]() ![]() | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmcif format | ![]() ![]() ![]() |
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PDB format | ![]() ![]() |
PDBML Plus | ![]() |
Others | ![]() |
-Related structure data
Related structure data | ![]() 2v5mSC ![]() 2v5sC S: Starting model for refinement C: citing same article ( |
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Similar-shape strucutres |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell | γ α β
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.863, -0.001, 0.506), Vector: Details | THE DIMERIC STATE DESCRIBED IN REMARK 350 BELOW HASHAS BEEN EXPERIMENTALLY VALIDATED USIING BEAD AGGREGATIONASSAYS. | |
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Components
#1: Protein | ![]() Mass: 43476.008 Da / Num. of mol.: 2 Fragment: N-TERMINAL FOUR DOMAINS (D1, D2, D3 AND D4), RESIDUES 36-423 Source method: isolated from a genetically manipulated source Details: ISOFORM 4.9/6.9 / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Sugar | ChemComp-NAG / ![]() #3: Chemical | ![]() Sequence details | THE CONFLICTS GIVEN IN THE SEQADV RECORDS BELOW ARE AS A RESULT OF A SPLICE VARIANT FORM OF THE ...THE CONFLICTS GIVEN IN THE SEQADV RECORDS BELOW ARE AS A RESULT OF A SPLICE VARIANT FORM OF THE PROTEIN WHERE EXON 4 COVERING RESIDUES 102 TO 156 CONSISTS OF ISOFORM 9 AND EXON 6 COVERING RESIDUES 205 TO 245 CONSISTS OF ISOFORM 9. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.9 Å3/Da / Density % sol: 69 % / Description: NONE |
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Crystal grow![]() | Details: 10 % PEG 8000, 1MM SPERMIDINE, 0.1 M TRISHCL PH 8.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 9, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3→20 Å / Num. obs: 53580 / % possible obs: 86 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 3→3.2 Å / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 1.9 / % possible all: 55.5 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 2V5M Resolution: 3→20 Å Details: B GROUP REFINEMENT NCS REFINEMENT DOMAIN D4 (RESIDUES 309-391) IS LESS WELL DEFINED
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Refinement step | Cycle: LAST / Resolution: 3→20 Å
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