positive regulation of potassium ion transport / negative regulation of lipid transport / negative regulation of macrophage derived foam cell differentiation / negative regulation of reactive oxygen species biosynthetic process / Wnt signaling pathway / DNA-binding transcription repressor activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II ...positive regulation of potassium ion transport / negative regulation of lipid transport / negative regulation of macrophage derived foam cell differentiation / negative regulation of reactive oxygen species biosynthetic process / Wnt signaling pathway / DNA-binding transcription repressor activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / RNA binding / nucleus Similarity search - Function
HMG box-containing protein 1 / Ataxin, AXH domain / Ataxin, AXH domain superfamily / Ataxin-1 and HBP1 module (AXH) / AXH domain profile. / domain in Ataxins and HMG containing proteins / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily Similarity search - Domain/homology
#1: Journal: J.Biomol.NMR / Year: 2004 Title: Assignment of the 1H,13C, and 15N Resonances of the Axh Domain of the Transcription Factor Hbp1 Authors: De Chiara, C. / Kelly, G. / Frankiel, T.A. / Pastore, A.
HMGBOX-CONTAININGPROTEIN1 / HBP1 / HMG-BOX CONTAINING PROTEIN-1 / HMG BOX TRANSCRIPTION FACTOR 1 / HIGH MOBILITY GROUP BOX ...HBP1 / HMG-BOX CONTAINING PROTEIN-1 / HMG BOX TRANSCRIPTION FACTOR 1 / HIGH MOBILITY GROUP BOX TRANSCRIPTION FACTOR 1
Mass: 15775.749 Da / Num. of mol.: 1 / Fragment: AXH DOMAIN, RESIDUES 208-345 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PET24D / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8R316
Sequence details
THE FOLLOWING N-TERMINAL RESIDUES FROM THE EXPRESSION SYSTEM TAG WERE NOT LOCATED IN THE EXPERIMENT: ...THE FOLLOWING N-TERMINAL RESIDUES FROM THE EXPRESSION SYSTEM TAG WERE NOT LOCATED IN THE EXPERIMENT: GLY ALA MET ALA
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
TRIPLERESONANCE
1
2
1
NOESY
NMR details
Text: STRUCTURAL RESTRAINTS WERE DERIVED FROM 13C- AND 15N-EDITED NOESY EXPERIMENTS AND J-COUPLINGS
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Sample preparation
Details
Contents: 0.7 MM 15N- OR 15N, 13C-LABELED PROTEIN, 20 MM TRIS-HCL, 10 MM NACL, 2 MM BETA-MERCAPTOETHANOL, 10% WATER/90% D2O
Sample conditions
Ionic strength: 10 MM NACL / pH: 7 / Pressure: 1 atm / Temperature: 303 K
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Varian INOVA
Varian
INOVA
600
1
Varian INOVA
Varian
INOVA
800
2
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Processing
NMR software
Name
Version
Developer
Classification
ARIA 1.2, CNS
1.1
NILGES, BRUNGERETAL.
refinement
NMRPipe
1.7
structuresolution
XEASY
1.2
structuresolution
ARIA
1.2
structuresolution
Refinement
Method: simulated annealing / Software ordinal: 1 Details: THE EXPERIMENTALLY DETERMINED DISTANCE AND DIHEDRAL ANGLE RESTRAINTS WERE APPLIED IN A MIXED TORSION AND CARTESIAN DYNAMICS SIMULATED ANNEALING PROTOCOL. THE FINAL STRUCTURE ENSEMBLE WAS ...Details: THE EXPERIMENTALLY DETERMINED DISTANCE AND DIHEDRAL ANGLE RESTRAINTS WERE APPLIED IN A MIXED TORSION AND CARTESIAN DYNAMICS SIMULATED ANNEALING PROTOCOL. THE FINAL STRUCTURE ENSEMBLE WAS REFINED IN A SHELL OF WATER MOLECULES
NMR ensemble
Conformer selection criteria: LOWEST ENERGIES / Conformers calculated total number: 100 / Conformers submitted total number: 20
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