Mass: 28443.596 Da / Num. of mol.: 1 / Mutation: N-TERMINAL HIS-TAGGED Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rous sarcoma virus / Genus: Alpharetrovirus / Strain: SCHMIDT RUPPIN A-2 Description: THE SOURCE OF THE CA_RSV GENE IS PLASMID PSRA-2 OF ATCC 45000, WHICH IS A PLASMID CLONE CONTAINING FULL LENGTH ROUS SARCOMA VIRUS, STRAIN SCHMIDT RUPPIN A-2, DERIVED FROM UNINTEGRATED ...Description: THE SOURCE OF THE CA_RSV GENE IS PLASMID PSRA-2 OF ATCC 45000, WHICH IS A PLASMID CLONE CONTAINING FULL LENGTH ROUS SARCOMA VIRUS, STRAIN SCHMIDT RUPPIN A-2, DERIVED FROM UNINTEGRATED DNA FROM AN ACUTE INFECTION OF QT-6 CELLS Plasmid: PET-16B (NOVAGEN) / Production host: Escherichia coli (E. coli) / Strain (production host): HMS174(DE3) PLYSS / References: UniProt: O92954
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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
4D 13C-SEPARATED NOESY
1
2
1
4D 13C/15N-SEPARATED NOESY
1
3
1
4D 15N-SEPARATED NOESY
1
4
1
3D 15N- SEPARATED NOESY
NMR details
Text: THE 1H, 13C, AND 15N CHEMICAL SHIFT ASSIGNMENTS HAVE BEEN DEPOSITED ATTHE BIOMOLECULAR RESONANCE DATABANK (BMRB ENTRY 4384).
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
~1 MM CA_RSV, 10 MM PHOSPHATE (PH 6.0), 0.2 MM N3NA, 0.1 MM EDTA, 0.1 MM PMSF, 1 MG/L PEPSTATIN A, 5 MM BETA-MERCAPTOETHANOL
90% H2O/10% D2O
2
~1 MM CA_RSV, 10 MM PHOSPHATE (PH 6.0), 0.2 MM N3NA, 0.1 MM EDTA, 0.1 MM PMSF, 1 MG/L PEPSTATIN A, 5 MM BETA-MERCAPTOETHANOL
100% D2O
Sample conditions
Ionic strength: 10 mM PHOSPHATE / pH: 6.00 / Pressure: 1 atm / Temperature: 303.00 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
NMR spectrometer
Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 800 MHz
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Processing
NMR software
Name
Version
Developer
Classification
DYANA
1.5
P.GUNTHER, ETH-ZURICH
refinement
XwinNMR
2.5
structuresolution
NMRPipe
1999
structuresolution
NMRView
3
structuresolution
TALOS
1999.019.15.47
structuresolution
Refinement
Method: TORSION ANGLE DYNAMICS SIMULATED ANNEALING / Software ordinal: 1 Details: 20 CONFORMERS COMPATIBLE WITH THE NMR CONSTRAINTS WERE CALCULATED USING DYANA 1.5 AND THE STANDARD TORSION ANGLE SIMULATED ANHEALING PROTOCOL. PRELIMINARY CALCULATIONS WERE CARRIED OUT ...Details: 20 CONFORMERS COMPATIBLE WITH THE NMR CONSTRAINTS WERE CALCULATED USING DYANA 1.5 AND THE STANDARD TORSION ANGLE SIMULATED ANHEALING PROTOCOL. PRELIMINARY CALCULATIONS WERE CARRIED OUT INDEPENDENTLY FOR EACH OF THE TWO N- AND C- TERMINAL DOMAINS OF THE PROTEIN. INITIALLY ONLY NOE DISTANCE CONSTRAINTS WERE IMPOSED. THE INITIAL STRUCTURES WERE THEN USED TO ASSES THE ACCURACY OF THE TORSION ANGLE CONSTRAINTS GENERATED BY ANALYSIS OF HA, CA, CB, CO AND N CHEMICAL SHIFTS WITH THE PROGRAM TALOS. FINALLY, UPPER AND LOWER LIMIT DISTANCE CONSTRAINTS WERE IMPOSED FOR UNAMBIGUOUS INTRAHELICAL H-BONDS.
NMR ensemble
Conformer selection criteria: target function / Conformers calculated total number: 20 / Conformers submitted total number: 20
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