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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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Unread 08-20-2014, 01:45 AM
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Default Position at MIT

From The DNP-NMR Blog:

Position at MIT

From the AMPERE Magnetic Resonance List




MIT-Harvard Center for Magnetic Resonance




JOB DESCRIPTION:


A position is available at the MIT-Harvard Center for Magnetic Research (CMR) located at the Francis Bitter Magnet Laboratory at MIT. Duties require assisting with the management of the day-to-day operations of the CMR, and carries responsibilities for training and advising users. The candidate is expected to improve laboratory operations, evaluate and test new methods of data collection, assist in the administration and maintenance of a cluster of Linux computers, maintain records of laboratory use, and perform routine and non-routine maintenance. In addition, the position requires supervision of the CMR infrastructure that includes compressed air, chilled water, nitrogen purification, and in the near future, a helium recovery and liquefier system. In addition, it is required that the candidate actively participate in the ample research opportunities of the CMR in solution, solid state and DNP NMR and/or high frequency EPR.


Qualifications:


Interested parties are required to have a PhD and established record of accomplishment in magnetic resonance. Experience with custom-built magnetic resonance instruments, NMR probe design, high frequency microwave instrumentation and/or commercial spectrometers would be a distinct advantage.




Please e-mail a resume, list of publications, and the names and e-mail addresses of three references to :


Prof. Robert G. Griffin
Francis Bitter Magnet Laboratory
Mass. Institute of Technology
NW14-3220, 77 Mass. Avenue
Cambridge, MA 02139-4703
USA


Email: rgg@mit.edu
Voice: 617-253-5597
Fax : 617-253-5405


http://web.mit.edu/chemistry/www/faculty/griffin.html
http://web.mit.edu/fbml/cmr/griffin-group/index.html



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Go to The DNP-NMR Blog for more info.
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