We are glad to officially release version 2.2 of HADDOCK. For general information and the online manual refer to:
The main changes with respect to version 2.1 are:
- Default setup (parameters/topology files) for CNS1.3
- It is now possible to mix molecule types within one molecule as long as there is no overlap in residue numbering. This this enables for example the docking of a protein onto a protein-DNA complex.
- New S3 and C4 symmetry restraints
- Radius of gyration restraint
- Option to automatically define backbone dihedral angle restraints from the input structures
- Pseudo contact shift restraints (CNS must be recompiled with the provided routines)
- Interaction matrix to scale down or turn off interactions between specific molecules
- Water-mediated contact probabilities option based on Kyte-Doolittle hydrophobic scale
- DNA-specific fraction of water to keep for solvated docking
- Fraction of common contact (FCC) clustering option
- Added examples for various docking scenarios (see the example directory)
See further: http://www.bonvinlab.org/software/haddock2.2/changes.html
Users with a local installation of HADDOCK can simply request the software, indicating the name of the PI registered for HADDOCK. New users should fill in a license form. See for this:
HADDOCK2.2 is also available as web portal. Users already having login credentials for the HADDOCK portal can directly start to use it. New users should register for an account. See:
- http://haddock.science.uu.nl/services/HADDOCK2.2
- http://haddock.science.uu.nl/enmr/services/HADDOCK2.2 (grid-enabled version)
Note that the old 2.1 portal remains accessible at its current URL.
In principle, the 2.2 portal should accept old parameter files saved from the 2.1 version (but make sure the run name does not contain any punctuations or spaces).
With best regards
Alexandre & HADDOCK team