- e-NMR aims at deploying and unifying the NMR computational infrastructure in system biology,
a project funded under the
7th framework program of the European Union (Contract no. 213010 - e-NMR).
- NMR plays an important role in life sciences (biomolecular NMR), and structural biology in particular,
at both European and international levels. Our main objective is to optimize and extend the use of the
NMR Research Infrastructures of EU-NMR through the
implementation of an e-Infrastructure in order to provide the biomolecular NMR user community with a
platform integrating and streamlining the computational approaches necessary for NMR data analysis and
structural modelling (e-NMR).
- HADDOCK Biomolecular Docking
HADDOCK (High Ambiguity Driven protein-protein DOCKing) is an
information-driven flexible docking approach for the modeling of biomolecular complexes. HADDOCK distinguishes
itself from ab-initio docking methods in the fact that it encodes information from identified or predicted protein
interfaces in ambiguous interaction restraints (AIRs) to drive the docking process.
HADDOCK can deal with a large
class of modelling problems including protein-protein, protein-nucleic acids and protein-ligand complexes. |
Go to service >>
- Xplor-NIH structure calculations
- This is the eNMR interface to the Xplor-NIH allowing you to run NMR structure calculations
with NOE, dihedral angle and paramagnetic restraints on the eNMR grid infrastructure. |
Go to service >>
- AMBER (restrained) molecular dynamics simulations
- This is the eNMR interface to Amber (acronym to Assisted Model Building with Energy Refinement), 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 information as restraints for MD. the Xplor-NIH allowing you to run NMR structure calculations
with NOE, dihedral angle and paramagnetic restraints on the eNMR grid infrastructure. |
Go to service >>
- CYANA structure calculations
- This is the eNMR interface to CYANA allowing you to run NMR structure calculations
with NOE and dihedral angle restraints on the eNMR grid infrastructure. |
Go to service >>
- CS-ROSETTA structure calculations
- This is the eNMR interface to CS-ROSETTA allowing you to run chemical shift-based structure calculations
with Rosetta. |
Go to service >>
- TALOS+ analysis
- TALOS+ (the improved TALOS) predicts backbone torsion angles using information derived from chemical shift,
amino acid type, and the area of the Ramachandran map where the residue is likely to reside in. This information
is compared to a large database of 200 proteins. |
Go to service >>
- AutoAssign chemical shift assignment
- AutoAssign is a constraint-based expert system for automating the analysis of backbone resonance assignments using triple resonance NMR spectra of small proteins. |
Go to service >>
- MARS chemical shift assignment
- MARS is a program for robust automatic backbone assignment of 13C/15N labeled proteins. |
Go to service >>
- MDD NMR data processing
- MDD NMR allows to process non-uniformly sampled nD spectrum using Multi-Dimensional Decomposition. |
Go to service >>
- CCPNMR FormatConverter
- The CcpNmr FormatConverted is designed to facilitate conversions between any existing NMR data formats and types. The underlying code is based on the existing CcpNmr FormatConverter code written by Wim Vranken, and we provide here a link to the web site developed in a collaborative effort by the team from the CCPN Project, the EBI in Hinxton, and Spronk NMR Consultancy. The FormatConverter webinterface is not designed to provide all NMR format conversion possibilities, but aims to facilitate the most common and simple conversions from format to format, and export of data from existing CCPN projects. |
Go to service >>
