Mass: 8026.125 Da / Num. of mol.: 1 / Fragment: SH3 DOMAIN RESIDUES 5601-5668 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MUSCLE / Cell: MYOCYTE / Organ: HEART / Plasmid: PET8C / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q96AA2, UniProt: Q5VST9*PLUS
Sequence details
THE FIRST THREE RESIDUES IN THE SEQRES RECORDS BELOW ARE THE REMANENTS OF A TEV CLEAVED HIS TAG AND ...THE FIRST THREE RESIDUES IN THE SEQRES RECORDS BELOW ARE THE REMANENTS OF A TEV CLEAVED HIS TAG AND DO NOT FORM PART OF THE OBSCURIN SH3 DOMAIN
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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 NOESY-HSQC
1
2
1
3D 13C RESOLVED NOESY-HSQC
NMR details
Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED OBSH3
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Sample preparation
Sample conditions
Ionic strength: 200 mM / pH: 5.76 / Pressure: 1 atm / Temperature: 298 K
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NMR measurement
NMR spectrometer
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz
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Processing
NMR software
Name
Version
Developer
Classification
CNS
1.1
BRUNGERET.AL.
refinement
CNS/ARIA
structuresolution
Refinement
Method: simulated annealing / Software ordinal: 1 Details: STANDARD ARIA SIMULATED ANNEALING PROTOCOL ACCORDING TO NILGES. ALL DEFAULT PARAMETERS COMING WITH VERSION 1.2 WERE USED APART FROM A NUMBER OF 200 STRUCTURES CALCULATED IN ITERATION 8 OF ...Details: STANDARD ARIA SIMULATED ANNEALING PROTOCOL ACCORDING TO NILGES. ALL DEFAULT PARAMETERS COMING WITH VERSION 1.2 WERE USED APART FROM A NUMBER OF 200 STRUCTURES CALCULATED IN ITERATION 8 OF WHICH 20 WHERE SELECTED. NO WATER REFINEMENT WAS USED.
NMR ensemble
Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 200 / Conformers submitted total number: 20
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