Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
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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
2D 1H-15N HSQC
1
2
3
2D 1H-13C HSQC
1
3
2
3D HNCO
1
4
2
3D HNCA
1
5
2
3D HN(CA)CB
1
6
2
3DCBCA(CO)NH
1
7
2
3DHN(CO)CA
1
8
3
3D (H)CCH-COSY
1
9
3
3DCBCGCD
1
10
1
3D 1H-15N NOESY
1
11
3
3D 1H-13C NOESY
1
12
2
2D 1H-1H NOESY
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
500 uM [U-13C; U-15N] Kaiso, 500 uM Kaiso binding sequence (KBS), 10 mM Tris, 1 mM TCEP, 95% H2O/5% D2O
95% H2O/5% D2O
2
500 uM [U-100% 13C; U-100% 15N; U-80% 2H] Kaiso, 500 uM Kaiso binding sequence (KBS), 10 mM Tris, 1 mM TCEP, 95% H2O/5% D2O
95% H2O/5% D2O
3
500 uM [U-13C; U-15N] Kaiso, 500 uM Kaiso binding sequence (KBS), 10 mM Tris, 1 mM TCEP, 100% D2O
100% D2O
Sample
Conc. (mg/ml)
Component
Isotopic labeling
Solution-ID
500uM
Kaiso-1
[U-13C; U-15N]
1
500uM
Kaiso binding sequence (KBS)-2
1
10mM
Tris-3
1
1mM
TCEP-4
1
500uM
Kaiso-5
[U-100% 13C; U-100% 15N; U-80% 2H]
2
500uM
Kaiso binding sequence (KBS)-6
2
10mM
Tris-7
2
1mM
TCEP-8
2
500uM
Kaiso-9
[U-13C; U-15N]
3
500uM
Kaiso binding sequence (KBS)-10
3
10mM
Tris-11
3
1mM
TCEP-12
3
Sample conditions
pH: 7 / Pressure: ambient / Temperature: 298 K
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker DMX
Bruker
DMX
500
1
Bruker DMX
Bruker
DMX
600
2
Bruker DMX
Bruker
DMX
800
3
Bruker DMX
Bruker
DMX
900
4
Bruker DRX
Bruker
DRX
750
5
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Processing
NMR software
Name
Developer
Classification
Amber
Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... andKollman
refinement
CYANA
Guntert, MumenthalerandWuthrich
peakpicking
NMRView
Johnson, OneMoonScientific
dataanalysis
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
TALOS
Cornilescu, DelaglioandBax
chemicalshiftcalculation
Refinement
Method: molecular dynamics / Software ordinal: 1
NMR constraints
NOE constraints total: 1347 / NOE intraresidue total count: 195 / NOE long range total count: 499 / NOE medium range total count: 258 / NOE sequential total count: 395 / Protein phi angle constraints total count: 131 / Protein psi angle constraints total count: 131
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20
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