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NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default 1 Postdoc and 1 PhD position MPI Göttingen

1 Postdoc and 1 PhD position MPI Göttingen

1 Postdoc and 1 PhD position in Computational NMR at the Max-Planck-Institute for Biophysical Chemistry

are available. The aim of the project is to further develop the PALES method (Zweckstetter, Nature Protocols 2008) to predict residual dipolar couplings from a given 3D structure. The project requires experience in C programming. NMR and/or biochemical knowledge is advantageous.

An excellent environment is available for training in the area of biomolecular NMR spectroscopy. The Max Planck Institute for Biophysical Chemistry, Göttingen, is one of the top research institutes in Germany. The NMR center at the MPI for Biophysical Chemistry houses numerous, state-of-the-art NMR spectrometers from 400 to 900 MHz for both solution and solid-state NMR spectroscopy. In addition, a fully equipped laboratory for production of recombinant proteins is available.

The Ph.D. position (BAT IIa/2) is limited for two years but can be extended for an additional year. The postdoc position (BAT IIa) is available for three years.

Interested applicants should send a CV and contact information for two references to:

Prof. Dr. Markus Zweckstetter
Max Planck Institute for Biophysical Chemistry
Am Fassberg 11, D-37077 Göttingen
Tel.: ++49-551-201-2220
Fax: ++49-551-201-2202
Email: mzwecks@gwdg.de[IMG]https://blog...s.blogspot.com[/IMG]


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