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Open data
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Basic information
Entry | Database: PDB / ID: 1mbh | ||||||
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Title | MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 2 | ||||||
![]() | C-MYB | ||||||
![]() | DNA BINDING PROTEIN / PROTOONCOGENE PRODUCT / DNA-BINDING PROTEIN | ||||||
Function / homology | ![]() positive regulation of testosterone secretion / myeloid cell development / positive regulation of hepatic stellate cell proliferation / positive regulation of hepatic stellate cell activation / positive regulation of transforming growth factor beta production / embryonic digestive tract development / stem cell division / myeloid cell differentiation / cellular response to interleukin-6 / WD40-repeat domain binding ...positive regulation of testosterone secretion / myeloid cell development / positive regulation of hepatic stellate cell proliferation / positive regulation of hepatic stellate cell activation / positive regulation of transforming growth factor beta production / embryonic digestive tract development / stem cell division / myeloid cell differentiation / cellular response to interleukin-6 / WD40-repeat domain binding / homeostasis of number of cells / positive regulation of collagen biosynthetic process / positive regulation of glial cell proliferation / spleen development / B cell differentiation / thymus development / cellular response to leukemia inhibitory factor / positive regulation of smooth muscle cell proliferation / G1/S transition of mitotic cell cycle / RNA polymerase II transcription regulator complex / calcium ion transport / positive regulation of neuron apoptotic process / mitotic cell cycle / regulation of gene expression / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / DNA-binding transcription factor activity, RNA polymerase II-specific / 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 | ||||||
![]() | Ogata, K. / Morikawa, S. / Nakamura, H. / Hojo, H. / Yoshimura, S. / Zhang, R. / Aimoto, S. / Ametani, Y. / Hirata, Z. / Sarai, A. ...Ogata, K. / Morikawa, S. / Nakamura, H. / Hojo, H. / Yoshimura, S. / Zhang, R. / Aimoto, S. / Ametani, Y. / Hirata, Z. / Sarai, A. / Ishii, S. / Nishimura, Y. | ||||||
![]() | ![]() 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. / Ishii, S. / Nishimura, Y. #1: ![]() 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. #2: ![]() 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 | ![]() | 867.2 KB | Display | ![]() |
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PDB format | ![]() | 730.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 340.2 KB | Display | ![]() |
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Full document | ![]() | 560.9 KB | Display | |
Data in XML | ![]() | 35.9 KB | Display | |
Data in CIF | ![]() | 62.9 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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NMR ensembles |
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Components
#1: Protein | Mass: 6300.351 Da / Num. of mol.: 1 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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Sample preparation
Sample conditions | pH: 6.8 / Temperature: 290 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software |
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Refinement | Software ordinal: 1 Details: A TOTAL OF 50 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINTED MINIMIZED AVERAGED STRUCTURE WERE OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES, AND THEN BY ...Details: A TOTAL OF 50 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINTED MINIMIZED AVERAGED STRUCTURE WERE OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES, AND THEN BY SUBJECTING THE RESULTING COORDINATES TO THE RESTRAINED ENERGY MINIZATION BY PRESTO. THE MINIMIZED AVERAGE STRUCTURE IS PRESENTED IN PROTEIN DATA BANK ENTRY 1MBG. | |||||||||
NMR ensemble | Conformers submitted total number: 50 |