Cyclin-dependentkinase2-associatedprotein2 / CDK2-associated protein 2 / DOC-1-related protein / DOC-1R
Mass: 7644.793 Da / Num. of mol.: 2 / Fragment: UNP residues 61-126 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CDK2AP2, DOC1R / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pMgK / References: UniProt: O75956
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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
1
2D 1H-13C HSQC
1
3
1
3D HNCO
1
4
1
3DCBCA(CO)NH
1
5
1
3D HN(CA)CB
1
6
1
3DCBCA(CO)NH
1
7
1
3DHBHA(CO)NH
1
8
1
3DHN(CA)CO
1
9
1
3D 1H-13C NOESY aliphatic
1
10
1
3D 1H-15N NOESY
1
11
2
3D 13C-filtered NOESY aliphatic
1
12
2
2D 13C-filtered NOESY aromatic
1
13
4
2D 1H-13C high res (L/V methyl stereospecific assignment)
1
14
1
3D (H)CCH-TOCSY
1
15
1
3D (H)CCH-COSY
1
16
1
3D (H)CCH-TOCSY
1
17
1
3D 1H-13C NOESY aromatic
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
5.0 mg/mL [U-100% 13C; U-100% 15N] HR8910C.003, 1 x Proteinase Inhibitors, 0.02 % NaN3, 10 mM DTT, 5 mM CaCL2, 200 mM NaCL, 20 mM MES pH 6.5, 5 % D2O, 95% H2O/5% D2O
95% H2O/5% D2O
2
5.0 mg/mL [U-100% 13C; U-100% 15N] HR8910C, 15.0 mg/mL HR8910C, 0.02 % NaN3, 10 mM DTT, 5 mM CaCL2, 200 mM NaCL, 20 mM MES pH 6.5, 5 % D2O, 1 x Proteinase Inhibitors, 95% H2O/5% D2O
95% H2O/5% D2O
3
0.3 mM [U-100% 15N] HR8910C, 0.02 % NaN3, 10 mM DTT, 5 mM CaCL2, 200 mM NaCL, 20 mM MES pH 6.5, 5 % D2O, 1 x Proteinase Inhibitors, 4.2 % PEG, 95% H2O/5% D2O
95% H2O/5% D2O
4
5.0 mg/mL [U-5% 13C; U-100% 15N] HR8910C.005, 1 x Proteinase Inhibitors, 0.02 % NaN3, 10 mM DTT, 5 mM CaCL2, 200 mM NaCL, 20 mM MES pH 6.5, 5 % D2O, 95% H2O/5% D2O
95% H2O/5% D2O
Sample
Conc. (mg/ml)
Component
Isotopic labeling
Solution-ID
5.0mg/mL
HR8910C.003-1
[U-100% 13C; U-100% 15N]
1
1 %
Proteinase Inhibitors-2
1
0.02 %
NaN3-3
1
10mM
DTT-4
1
5mM
CaCL2-5
1
200mM
NaCL-6
1
20mM
MES pH 6.5-7
1
5 %
D2O-8
1
5.0mg/mL
HR8910C-9
[U-100% 13C; U-100% 15N]
2
15.0mg/mL
HR8910C-10
2
0.02 %
NaN3-11
2
10mM
DTT-12
2
5mM
CaCL2-13
2
200mM
NaCL-14
2
20mM
MES pH 6.5-15
2
5 %
D2O-16
2
1 %
Proteinase Inhibitors-17
2
0.3mM
HR8910C-18
[U-100% 15N]
3
0.02 %
NaN3-19
3
10mM
DTT-20
3
5mM
CaCL2-21
3
200mM
NaCL-22
3
20mM
MES pH 6.5-23
3
5 %
D2O-24
3
1 %
Proteinase Inhibitors-25
3
4.2 %
PEG-26
3
5.0mg/mL
HR8910C.005-27
[U-5% 13C; U-100% 15N]
4
1 %
Proteinase Inhibitors-28
4
0.02 %
NaN3-29
4
10mM
DTT-30
4
5mM
CaCL2-31
4
200mM
NaCL-32
4
20mM
MES pH 6.5-33
4
5 %
D2O-34
4
Sample conditions
pH: 6.5 / Pressure: ambient / Temperature: 298 K
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NMR measurement
NMR spectrometer
Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz
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Processing
NMR software
Name
Version
Developer
Classification
CNS
1.3
Brunger, Adams, Clore, Gros, NilgesandRead
refinement,structuresolution,geometryoptimization
CYANA
3.02
Guntert, MumenthalerandWuthrich
refinement,geometryoptimization,structuresolution
AutoAssign
2.1
Zimmerman, Moseley, KulikowskiandMontelione
dataanalysis,chemicalshiftassignment
NMRPipe
2
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
TopSpin
2.1
BrukerBiospin
collection
PINE
1
Bahrami, Markley, Assadi, andEghbalnia
chemicalshiftassignment
Sparky
3.112
Goddard
dataanalysis
TALOS+
Shen, Cornilescu, DelaglioandBax
geometryoptimization
PALES
PALES (Zweckstetter, Bax)
geometryoptimization
PSVS
1.4
Bhattacharya, Montelione
structurevalidation
CNS
1.3
Brunger, Adams, Clore, Gros, NilgesandRead
refinement
Refinement
Method: simulated annealing / Software ordinal: 1 Details: Structure determination of this symmetric homodimer was performed iteratively using CYANA 3.02. The 20 structures out of 100 with lowest target function were further refined by restrained ...Details: Structure determination of this symmetric homodimer was performed iteratively using CYANA 3.02. The 20 structures out of 100 with lowest target function were further refined by restrained molecular dynamics/energy minimization in explicit water using CNS 1.3. Residual dipolar couplings and backbone dihedral angle constraints for the ordered regions were applied at all stages of the structure determination
NMR constraints
NOE constraints total: 1914 / NOE intraresidue total count: 437 / NOE long range total count: 476 / NOE medium range total count: 523 / NOE sequential total count: 478 / Protein phi angle constraints total count: 50 / Protein psi angle constraints total count: 51
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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