Mass: 21106.293 Da / Num. of mol.: 1 / Fragment: RRM1 and RRM2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CUGBP1 (AMINO ACIDS 1 - 187) / Plasmid: pET15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q92879
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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 NOESY
1
2
1
2D HSQC
1
3
1
3D HNCO
1
4
1
3D HNCA
1
5
1
3DHN(CO)CA
1
6
1
3D HN(CA)CB
1
7
1
3DCBCA(CO)NH
1
8
1
3DHBHANH
1
9
1
3DHBHA(CO)NH
1
10
1
3D 15N-separated NOESY
1
11
1
3D 13C-separated NOESY
1
12
1
4D 13C-separated NOESY
1
13
1
4D 13C/15N-separated NOESY
1
14
1
HNHA
NMR details
Text: The structure was determined using triple-resonance NMR spectroscopy. The both two domains RRM1 (RNA recognition motif) and RRM2 contain the same beta-alpha-beta-beta-alpha-beta topology as ...Text: The structure was determined using triple-resonance NMR spectroscopy. The both two domains RRM1 (RNA recognition motif) and RRM2 contain the same beta-alpha-beta-beta-alpha-beta topology as expected for RNA-recognition motif. The four beta strands form an anti parallel beta sheet. The two alpha helices are packed against the beta sheet. Other NMR experiments including 15N T1 and T2 and {1H}-15N steady state NOE, and titration with DNA and RNA, were carried out. the RRM1 shows more conformat on exchange than RRM2. The N-terminal region and the linker between the RRM1 and RRM2 show more flexibility than other regions. In addition, two loops L3 and L5 in RRM1 also demonstrate considerable flexibility and conformation exchange. The conformation exchange and flexibility in the RRM1 may be utilized in the recognition process by allowing different conformational states to be accessed and facilitating induced fit for complex forming. From the titration experiments,we found that the (GTC)3 and (GUCU)3 mainly bind the two central beta strands of the RRM1 and the linker of the RRM1 and RRM2 domains.
Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: The protein CUGBP1ab has total 187 residues (residues 1-187 of CUGBP1) including an N-terminus Histag-thrombin site (21 amino acids) and 20 amino acids in the C-terminus which is from the ...Details: The protein CUGBP1ab has total 187 residues (residues 1-187 of CUGBP1) including an N-terminus Histag-thrombin site (21 amino acids) and 20 amino acids in the C-terminus which is from the plasmid. The molecular weight of the CUGBP1ab is 25.4 kDa. The structures are based on a total of 4228 restraints, 3776 are NOE-derived distance donstraints, 324 dihedral angle restraints,128 distance restraints from hydrogen bonds.
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 7
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