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- PDB-1idy: STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STR... -
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Basic information
Entry | Database: PDB / ID: 1idy | ||||||
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Title | STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
![]() | MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3 | ||||||
![]() | DNA BINDING PROTEIN / PROTOONCOGENE PRODUCT / DNA-BINDING PROTEIN | ||||||
Function / homology | ![]() myeloid cell development / embryonic digestive tract development / myeloid cell differentiation / stem cell division / cellular response to interleukin-6 / WD40-repeat domain binding / homeostasis of number of cells / spleen development / B cell differentiation / cellular response to leukemia inhibitory factor ...myeloid cell development / embryonic digestive tract development / myeloid cell differentiation / stem cell division / cellular response to interleukin-6 / WD40-repeat domain binding / homeostasis of number of cells / spleen development / B cell differentiation / cellular response to leukemia inhibitory factor / thymus development / G1/S transition of mitotic cell cycle / RNA polymerase II transcription regulator complex / calcium ion transport / regulation of gene expression / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING IN 4D | ||||||
![]() | Furukawa, K. / Oda, M. / Nakamura, H. | ||||||
![]() | ![]() Title: A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy. Authors: Furukawa, K. / Oda, M. / Nakamura, H. #1: ![]() Title: Comparison of the Free and DNA-Complexed Forms of the DNA-Binding Domain from C-Myb Authors: Ogata, K. / Morikawa, S. / Nakamura, H. / Hojo, H. / Yoshimura, S. / Zhang, R. / Aimoto, S. / Ametani, Y. / Hirata, Z. / Sarai, A. / al., et #2: ![]() Title: Solution Structure of a Specific DNA Complex of the Myb DNA-Binding Domain with Cooperative Recognition Helices Authors: Ogata, K. / Morikawa, S. / Nakamura, H. / Sekikawa, A. / Inoue, T. / Kanai, H. / Sarai, A. / Ishii, S. / Nishimura, Y. #3: ![]() Title: Solution Structure of a DNA-Binding Unit of Myb: A Helix-Turn-Helix-Related Motif with Conserved Tryptophans Forming a Hydrophobic Core Authors: Ogata, K. / Hojo, H. / Aimoto, S. / Nakai, T. / Nakamura, H. / Sarai, A. / Ishii, S. / Nishimura, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 28.7 KB | Display | ![]() |
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PDB format | ![]() | 18.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6521.496 Da / Num. of mol.: 1 / Mutation: P140M, I155L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D 1H-1H NOESY |
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Sample preparation
Sample conditions | pH: 5 / Temperature: 283 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600.13 MHz |
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Processing
Software | Name: ![]() | |||||||||
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NMR software |
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Refinement | Method: SIMULATED ANNEALING IN 4D / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: 0.1 ANGSTROM MAXIMUM DISTANCE VIOLATION Conformers calculated total number: 120 / Conformers submitted total number: 1 |