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Marketplace Services
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700MHz Varian/Agilent Varian NMR Systems
- 16.4 T magnetOxford
- "Direct Drive" console
- four independent RF channels (1H 100 W, BB 400 W, 2 x BB 1000 W), all channels enable for shaped pulses
- 40 shim coils
- 2H lock
- "high band" lock 2H - 1H
- variable temperature unit
- XYZ PFG amplifier
- Show more >
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WeNMR Consortium, Utrecht, Netherlands
SHIFTX2 predicts both the backbone and side chain 1H, 13C and 15N chemical shifts for proteins using their structural (PDB) coordinates as input. SHIFTX2 combines ensemble machine learning methods with sequence alignment-based methods to calculate protein chemical shifts for backbone and side chain Show more >
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WeNMR Consortium, Firenze, Italy
This is the WeNMR interface to the Xplor-NIH allowing you to run NMR structure calculations with NOE, dihedral angle and paramagnetic restraints on the WeNMR grid infrastructure. Show more >
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WeNMR Consortium, Firenze, Italy
The most common use of the Antechamber program suite is to prepare input files for LEaP, starting from a three-dimensional structure, as found in a PDB file. The antechamber suite automates the process of developing a charge distribution and assigning atom types, and partially automates the process Show more >
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WeNMR Consortium, Firenze, Italy
Amber (acronym to Assisted Model Building with Energy Refinement) is a suite of programs that allow users to perform molecular dynamics (MD) simulations on biological systems. This web portal makes available the entire functionality of AMBER, in particular (but not only) using NMR-derived informati Show more >
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WeNMR Consortium, Firenze, Italy
Maximum Occurrence (MaxOcc) refers to a method for making rigorous numerical assessments about the maximum percent of time that a conformer of a flexible macromolecule can exist and still be compatible with the experimental data. Maximum Occurrence of a conformer is defined as the maximum weight tha Show more >
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WeNMR Consortium, Firenze, Italy
Fitting of Pseudocontact Shifts and Residual Dipolar couplings - The program allows users to fit pseudocontact shift and/or residual dipolar couplings measured for a protein against its structure. The calculation exploits the SIMPLEX minimization algorithm. . As extensively documented in the literat Show more >
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