DNA/RNA-bindingproteinKIN17 / Binding to curved DNA / KIN / antigenic determinant of recA protein homolog
Mass: 14348.669 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIN, BTCD, KIN17 / Production host: Escherichia coli (E. coli) / References: UniProt: O60870
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Sample state
Spectrometer-ID
Type
1
1
1
isotropic
1
3D 1H-13C NOESY aliphatic
1
2
1
isotropic
1
3D 1H-13C NOESY aromatic
1
3
1
isotropic
1
3D 1H-15N NOESY
1
4
1
isotropic
1
2D 1H-15N HSQC
1
5
1
isotropic
1
2D 1H-13C HSQC aliphatic
1
6
1
isotropic
1
2D 1H-13C HSQC aromatic
1
7
1
isotropic
1
3D HNCO
1
8
1
isotropic
1
3D HNCA
1
9
1
isotropic
1
3D HN(CA)CB
1
10
1
isotropic
1
3DCBCA(CO)NH
1
11
1
isotropic
1
3DC(CO)NH
1
12
1
isotropic
1
3DH(CCO)NH
1
13
1
isotropic
1
3D (H)CCH-TOCSY
1
14
1
isotropic
1
3D (H)CCH-TOCSY
1
15
1
isotropic
1
2D (HB)CB(CGCD)HD
1
16
1
isotropic
1
2D (HB)CB(CGCDCE)HE
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Sample preparation
Details
Type: solution Contents: 500 uM [U-13C; U-15N] SH3-like tandem domain of human KIN protein, 0.5 mM PMSF, 3 mM EDTA, 0.02 % v/v sodium azide, 0.33 mM 98% 2H DSS, 95% H2O/5% D2O Label: 15N_13C_sample / Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)
Component
Isotopic labeling
Solution-ID
500uM
SH3-like tandem domain of human KIN protein
[U-13C; U-15N]
1
0.5mM
PMSF
naturalabundance
1
3mM
EDTA
naturalabundance
1
0.02 % v/v
sodiumazide
naturalabundance
1
0.33mM
DSS
98% 2H
1
Sample conditions
Ionic strength: 50 mM NaPi, 100 mM NaCl mM / Label: conditions_1 / pH: 6.5 / Pressure: 1 atm / Temperature: 298.4 K
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NMR measurement
NMR spectrometer
Type: Bruker AVANCE III HD / Manufacturer: Bruker / Model: AVANCE III HD / Field strength: 600 MHz
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Processing
NMR software
Name
Version
Developer
Classification
CcpNmr Analysis
CCPN
chemicalshiftassignment
ARIA
2.3.2
Linge, O'DonoghueandNilges
refinement
CNS
Brunger, Adams, Clore, Gros, NilgesandRead
structurecalculation
CcpNmr Analysis
CCPN
peakpicking
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
CNS
Brunger, Adams, Clore, Gros, NilgesandRead
refinement
ARIA
2.3.2
Linge, O'DonoghueandNilges
refinement
Refinement
Method: distance geometry / Software ordinal: 2 Details: The structures are based on a total of 5751 restraints, 4523 are NOE-derived distance constraints, and 1228 ambiguous restraints.
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 200 / Conformers submitted total number: 10
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