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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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  #1  
Old 05-19-2008, 09:15 AM
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Default PhD position, Max Planck Institute Tübingen, Germany

Applications are invited for

Diploma / Master and PhD positions

in the newly established research group of Dr. Silke Wiesner at the Max Planck Institute for Developmental Biology in Tübingen, Germany.

The group is interested in the Ubiquitin-dependent regulation of cell polarity. As part of this focus, we wish to describe the protein ubiquitination reaction at atomic resolution. The attachment of ubiquitin to proteins is one of the most abundant post-translational modifications. Deregulation of the ubiquitination reaction is the cause of various diseases, including cancer. Yet, the exact mechanisms underlying protein ubiquitination and its regulation are still unknown.

The project aims at identifying and characterizing binding surfaces and conformational changes in HECT-type ubiquitin ligases at different steps of the ubiquitination reaction using biomolecular NMR spectroscopy in combination with other biophysical and biochemical methods. The interdisciplinary character of the project offers the opportunity to learn and apply a variety of techniques in a team-oriented, collaborative environment. The institute is equipped with state-of-the-art facilities (e.g. a 600 and an 800 MHz NMR spectrometer installed in May 2008) and offers an international PhD program.

The positions are available as of July 01, 2008.

Motivated and creative students with strong interests in structural biology are encouraged to apply. Applications should include a letter stating research interests / experience and a CV. Please send your application in PDF format to: silke.wiesner[at]tuebingen.mpg.de.

Applicants for PhD positions must hold a Diploma or Master degree in Chemistry or Biochemistry by the time they start their PhD studies.
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