back calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy
Representative
-
Components
#1: Protein
P47
Mass: 9901.343 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN(RESIDUES 282-370) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: PPRO-EX HTB / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: O35987
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Experimental details
-
Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
HNCA, HN(CO)CA, CBCA(CO)NH, HBHA(CO)NH, 15N-NOESY
2
2
2
IPAP-HSQC
3
3
3
2D NOESY
-
Sample preparation
Details
Solution-ID
Contents
Solvent system
1
1mM 13C, 15N-labelled p47 C domain sample
20mMNaAcbufferpH5.2; 90% H2O, 10% D2O
2
1mM15Np47Cdomainsample
3% C12E5/hexanol (r=0.96)
3
1mMp47Cdomainsample
99.9% D2O, pH5.2
Sample conditions
Conditions-ID
pH
Pressure (kPa)
Temperature (K)
1
5.2
1atm
302K
2
5.2
1atm
302K
3
5.2
1atm
302K
Crystal grow
*PLUS
Method: other / Details: NMR
-
NMR measurement
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz
Conformer selection criteria: back calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the ...Conformer selection criteria: back calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10
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