Neurabin-2 / Neurabin-II / Neural tissue-specific F-actin binding protein II / Protein phosphatase 1 regulatory ...Neurabin-II / Neural tissue-specific F-actin binding protein II / Protein phosphatase 1 regulatory subunit 9B / Spinophilin / p130 / PP1bp134
Mass: 12135.745 Da / Num. of mol.: 1 / Fragment: PDZ domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ppp1r9b / Plasmid: derivitive of pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) RIL codon plus / References: UniProt: O35274
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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
3D 15N resolved [1H,1H] NOESY
1
2
2
3D 13C resolved [1H,1H] NOESY
1
3
3
2D 1H-1H NOESY
NMR details
Text: The following spectra were used to achieve the sequence-specific backbone and side chain assignments of all aliphatic residues: 2D [1H,15N]-HSQC, 2D [1H,13C]-HSQC, 3D HNCACB, 3D CBCA(CO)NH, 3D ...Text: The following spectra were used to achieve the sequence-specific backbone and side chain assignments of all aliphatic residues: 2D [1H,15N]-HSQC, 2D [1H,13C]-HSQC, 3D HNCACB, 3D CBCA(CO)NH, 3D CC(CO)NH, 3D HNCO, 3D HNCA, 3D HBHA(CO)NH, 3D 15N-resolved [1H,1H]-TOCSY, 3D HC(C)H-TOCSY6. The 2D [1H,1H]-NOESY, 2D [1H,1H]-TOCSY and 2D [1H,1H]-COSY spectra of the Spinophilin493-602 sample in D2O solution after complete H/D exchange of the labile protons were used for the assignment of the aromatic side chains. The NMR spectra were processed with Topspin1.3, and analyzed with the CARA software package. Spectra used for the structure calculation were: 3D 15N-resolved [1H,1H]-NOESY, 3D 13C-resolved [1H,1H]-NOESY (mixing time of 85 ms) and 2D [1H,1H]-NOESY (mixing time 85 ms, D2O solution).
Ionic strength: 20 mM Na phosphate; 50 mM NaCl / pH: 6.5 / Pressure: ambient / Temperature: 298 K
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NMR measurement
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz
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Processing
NMR software
Name
Version
Developer
Classification
TopSpin
1.3
Bruker
processing
CYANA
2
peterguntert
structuresolution
CNS
1.1
Brunger
refinement
atnos/candid
2
TorstenHerrmann
structuresolution
CARA
1.5
RochusKeller
dataanalysis
Refinement
Method: simulated annealing torsion angle dynamics / Software ordinal: 1 Details: The amino acid sequence, the chemical shift assignment, and the NOESY spectra were input for the automated NOESY peak picking and NOE assignment method of ATNOS/CANDID/CYANA. The results of ...Details: The amino acid sequence, the chemical shift assignment, and the NOESY spectra were input for the automated NOESY peak picking and NOE assignment method of ATNOS/CANDID/CYANA. The results of ATNOS/CANDID/CYANA were refined by manual peak adjustment and additional calculations in CYANA. The 20 conformers from the ATNOS/CANDID cycle 7 with the lowest residual CYANA target function values were energy-minimized in a water shell with the program CNS.
NMR representative
Selection criteria: closest to the average
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20
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