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Open data
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Basic information
Entry | Database: PDB / ID: 1ig6 | |||||||||
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Title | HUMAN MRF-2 DOMAIN, NMR, 11 STRUCTURES | |||||||||
![]() | MODULATOR RECOGNITION FACTOR 2 | |||||||||
![]() | DNA BINDING PROTEIN / MRF-2 / DNA-BINDING MOTIF / PROTEIN-DNA INTERACTION | |||||||||
Function / homology | ![]() muscle organ morphogenesis / cell development / fibroblast migration / skeletal system morphogenesis / face morphogenesis / fat pad development / adrenal gland development / female gonad development / roof of mouth development / fat cell differentiation ...muscle organ morphogenesis / cell development / fibroblast migration / skeletal system morphogenesis / face morphogenesis / fat pad development / adrenal gland development / female gonad development / roof of mouth development / fat cell differentiation / platelet-derived growth factor receptor signaling pathway / adipose tissue development / post-embryonic development / liver development / cellular response to leukemia inhibitory factor / kidney development / HDMs demethylate histones / multicellular organism growth / positive regulation of DNA-binding transcription factor activity / male gonad development / transcription coactivator activity / transcription cis-regulatory region binding / negative regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / torsion angle dynamics | |||||||||
![]() | Lin, D. / Tsui, V. / Case, D. / Yuan, Y.C. / Chen, Y. | |||||||||
![]() | ![]() Title: HUMAN MRF-2 DOMAIN, NMR, 11 STRUCTURES Authors: Lin, D. / Tsui, V. / Case, D. / Yuan, Y.C. / Chen, Y. #1: ![]() Title: A Novel DNA-Binding Motif Shares Structural Homology to DNA Replication and Repair Nucleases and Polymerases Authors: Yuan, Y.C. / Whitson, R.H. / Liu, Q. / Itakura, K. / Chen, Y. #2: ![]() Title: Resonance Assignments of the MRF-2 DNA-Binding Domain Authors: Yuan, Y.C. / Whitson, R.H. / Itakura, K. / Chen, 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 | ![]() | 392.4 KB | Display | ![]() |
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PDB format | ![]() | 325.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353 KB | Display | ![]() |
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Full document | ![]() | 415.6 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 31 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 12652.646 Da / Num. of mol.: 1 / Fragment: DNA-BINDING DOMAIN 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 |
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NMR details | Text: This structure was determined using the restraints derived from NMR experiments (NOE, dihedral angles, hydrogen bonds, residual dipolar coupling constants, etc.) |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 100 mM Sodium Phosphate / pH: 6.00 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: The structures are based on a total of 2478 restraints, 2290 are NOE-derived distance constraints, 74 dihedral angle restraints, 42 distance restraints from hydrogen bonds, 35 residual ...Details: The structures are based on a total of 2478 restraints, 2290 are NOE-derived distance constraints, 74 dihedral angle restraints, 42 distance restraints from hydrogen bonds, 35 residual dipolar coupling constants. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 11 |