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NMR processing:
MDD
NMR assignment:
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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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Old 08-21-2010, 05:14 AM
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Default Academic Positions University of Kent, UK

Academic Positions University of Kent, UK

The School of Biosciences wishes to appoint five Faculty members at any level (Lecturer/Senior Lecturer/Reader/Professor) including two new members of the Protein Science Research Group within the areas of:

Structural Biology Ref: STM0154
and
Chemical Biology/Enzymology Ref: STM0155

In addition to integrating with current strengths in protein science, individuals would also be encouraged to engage with the Centre for Molecular Processing (see above). Following a recent £0.5 M award to upgrade our NMR facility by the Wellcome Trust and we are particularly interested in research scientists who can contribute to the use and development of this facility. The upgrade will provide a new console and cryogenic probe for our existing 600 MHz NMR spectrometer.

More details can be found at the University of Kent website and inserting references: STM0154 or STM0155 as above.

Closing date for applications is Monday 6 September, 2010.

Informal enquiries can be made to Dr. Mark Howard
================================================
Dr. Mark J. Howard CSci CChem MRSC
Senior Lecturer in Biomolecular NMR Spectroscopy
School of Biosciences
University of Kent
Canterbury, Kent, CT2 7NJ, UK.

Tel No: 01227 824730 (office) or 827117 (NMR)
================================================


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