positive regulation of shelterin complex assembly / negative regulation of establishment of protein localization to telomere / negative regulation of establishment of RNA localization to telomere / negative regulation of establishment of protein-containing complex localization to telomere / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / meiotic telomere clustering / telomeric D-loop disassembly / t-circle formation ...positive regulation of shelterin complex assembly / negative regulation of establishment of protein localization to telomere / negative regulation of establishment of RNA localization to telomere / negative regulation of establishment of protein-containing complex localization to telomere / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / meiotic telomere clustering / telomeric D-loop disassembly / t-circle formation / shelterin complex / Telomere C-strand synthesis initiation / double-stranded telomeric DNA binding / Telomere C-strand (Lagging Strand) Synthesis / Processive synthesis on the C-strand of the telomere / nuclear telomere cap complex / G-rich strand telomeric DNA binding / positive regulation of telomere maintenance / Polymerase switching on the C-strand of the telomere / ankyrin repeat binding / Removal of the Flap Intermediate from the C-strand / telomere capping / negative regulation of telomere maintenance via telomerase / DNA binding, bending / negative regulation of telomere maintenance via telomere lengthening / telomeric DNA binding / negative regulation of DNA replication / negative regulation of telomerase activity / Telomere Extension By Telomerase / telomere maintenance via telomerase / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere maintenance / DNA Damage/Telomere Stress Induced Senescence / spindle / fibrillar center / microtubule binding / chromosome, telomeric region / molecular adaptor activity / nuclear body / cell division / nucleolus / protein homodimerization activity / DNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm Similarity search - Function
Mass: 6668.805 Da / Num. of mol.: 1 / Fragment: DNA-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: NUCLEUSCell nucleus / References: UniProt: P54274
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Experimental details
-
Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
COSY
1
2
1
TOCSY
1
3
1
NOESY
NMR details
Text: THE STRUCTURES OF HTRF1 DNA-BINDING DOMAIN WERE DETERMINED BY 2D PROTON NMR SPECTROSCOPY.
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Sample preparation
Details
Contents: H2O
Sample conditions
Ionic strength: 100 mM PHOSPHATE POTASSIU / pH: 6.8 / Pressure: 1 ATMOSPHERE / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR
-
NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker AMX2 500
Bruker
AMX2500
500
1
Bruker DMX600
Bruker
DMX600
600
2
-
Processing
Software
Name: AMBER / Classification: refinement
NMR software
Name
Developer
Classification
EMBOSS
NAKAI,KIDERA,NAKAMURA
refinement
EMBOSS
structuresolution
Refinement
Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 Details: DETAILS OF THE STRUCTURE CALCULATION AND ALL STRUCTURAL STATISTICS WILL BE GIVEN IN THE REFERENCES CITED ABOVE. THE STRUCTURES WERE CONSTRUCTED ON THE BASIS OF 546 INTERPROTON DISTANCE ...Details: DETAILS OF THE STRUCTURE CALCULATION AND ALL STRUCTURAL STATISTICS WILL BE GIVEN IN THE REFERENCES CITED ABOVE. THE STRUCTURES WERE CONSTRUCTED ON THE BASIS OF 546 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOES AND 27 DIHEDRAL ANGLE RESTRAINTS. THE METHOD USED TO DETERMINE THE STRUCTURES IS THE SIMULATED-ANNEALING PROTOCOL IN FOUR-DIMENSIONAL SPACE IMPLEMENTED IN THE EMBOSS PROGRAM [T.NAKAI, A.KIDERA AND H.NAKAMURA, J.BIOMOL.NMR,3,19-40(1993)]. THE STRUCTURES WERE REFINED BY THE RESTRAINED ENERGY MINIMIZATION USING AMBER ALL-ATOM FORCE FIELD.
NMR ensemble
Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 60 / Conformers submitted total number: 18
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