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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 | ![]() 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 | ||||||
![]() | 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 | ![]() | 867.5 KB | Display | ![]() |
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PDB format | ![]() | 730.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-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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Has protein modification | Y |
-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 |