#1: Journal: J.Mol.Biol. / Year: 2004 Title: Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions. Authors: Li, H. / Byeon, I.-J.L. / Ju, Y. / Tsai, M.-D.
structures with the least restraint violations,structures with the lowest energy
Representative
Model #1
closest to the average
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Components
#1: Protein
AntigenKI-67
Mass: 13826.766 Da / Num. of mol.: 1 / Fragment: FHA domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Genus: Escherichia / Gene: MKI67 / Plasmid: PEG / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P46013
#2: Protein/peptide
MKI67FHAdomaininteractingnucleolarphosphoprotein / Nucleolar protein interacting with the FHA domain of pKI-67 / hNIFK / Nucleolar phosphoprotein Nopp34
Mass: 5197.442 Da / Num. of mol.: 1 / Fragment: residues 226-269 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Genus: Escherichia / Gene: MKI67IP / Plasmid: pEG / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9BYG3
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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
3D 13C-separated NOESY
1
2
1
3D 15N-separated NOESY
1
3
3
3D 13C-separated NOESY
1
4
3
3D 15N-separated NOESY
1
5
1
3D 12C/14N-filtered 13C separated NOESY
1
6
3
3D 12C/14N-filtered 13C separated NOESY
NMR details
Text: The structure was determined using triple-resonance NMR spectroscopy
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
93% H2O/7% D2O
2
0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
100% D2O
3
1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
93% H2O/7% D2O
4
1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
100% D2O
Sample conditions
Ionic strength: 150 mM NaCl / pH: 7.4 / Pressure: ambient / Temperature: 293 K
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker AVANCE
Bruker
AVANCE
800
1
Bruker DMX
Bruker
DMX
750
2
Bruker AVANCE
Bruker
AVANCE
600
3
Bruker DMX
Bruker
DMX
500
4
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Processing
NMR software
Name
Version
Developer
Classification
X-PLOR
NIHversion
Brunger
structuresolution
X-PLOR
NIHversion
Brunger
refinement
Refinement
Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 3476 constraints, 3141 are distance, 215 dihedral angle, and 120 N-H residual dipolar coupling constraints
NMR representative
Selection criteria: closest to the average
NMR ensemble
Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 512 / Conformers submitted total number: 100
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