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 / telomerase activity / 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 / telomerase activity / t-circle formation / telomeric D-loop disassembly / shelterin complex / Telomere C-strand synthesis initiation / double-stranded telomeric DNA binding / Telomere C-strand (Lagging Strand) Synthesis / : / positive regulation of telomere maintenance / nuclear telomere cap complex / ankyrin repeat binding / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / telomere capping / DNA binding, bending / negative regulation of telomere maintenance via telomere lengthening / telomeric DNA binding / negative regulation of DNA replication / negative regulation of telomere maintenance via telomerase / 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 / fibrillar center / spindle / microtubule binding / chromosome, telomeric region / nuclear body / cell division / nucleolus / protein homodimerization activity / DNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm Similarity search - Function
Mass: 4102.667 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Human natural telomeric sequence
#2: DNA chain
5'-D(*CP*CP*CP*TP*AP*AP*CP*CP*CP*TP*AP*AP*C)-3'
Mass: 3840.528 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Human natural telomeric sequence
#3: Protein
TELOMERICREPEATBINDINGFACTOR1 / TRF1
Mass: 8598.949 Da / Num. of mol.: 1 / Fragment: DNA-binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TRF1 / Plasmid: pET13A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PLYSS / References: UniProt: P54274
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Type: 3D Sequential assignment protocol; 3D HNHA; 3D 15N separated NOESY, 3D 13C separated NOESY, 2D NOESY, 2D TOCSY and 2D COSY with or without isotope filtering
NMR details
Text: The structures were determined by multi-dimensional heteronuclear -edited and -filtered NMR spectroscopy.
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Sample preparation
Details
Contents: 1.5-2.5mM TRF1-DNA complex; 5mM Phosphate buffer with 10mM NaCl Solvent system: 90% H2O, 10% D2O or 100% D2O
Sample conditions
pH: 6.8 / Pressure: ambient / Temperature: 305 K
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NMR measurement
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker DMX
Bruker
DMX
600
1
Bruker DRX
Bruker
DRX
500
2
Bruker AMX
Bruker
AMX
500
3
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Processing
NMR software
Name
Version
Developer
Classification
EMBOSS
5
Nakai, T, Kidera, A, andNakamura, H.
refinement
EMBOSS
5
Nakai, T, Kidera, A, andNakamura, H.
structuresolution
Refinement
Method: distance geometry, simulated annealing / Software ordinal: 1 Details: The structures were generated by 4-dimensional simulated annealing (4D-SA) with program EMBOSS, based on a total of 1341 experimental restraints, 901 and 356 are the NOE derived distance ...Details: The structures were generated by 4-dimensional simulated annealing (4D-SA) with program EMBOSS, based on a total of 1341 experimental restraints, 901 and 356 are the NOE derived distance restraints for protein and DNA, respectively, 29 are protein dihedral restraints and 55 are protein-DNA intermolecular restrainTs. In addition, 66 hydrogen bond and 221 ring-to-ring restraints are applied through 4D-SA to maintain the DNA base pair planarity.
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20
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