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NMR processing:
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NMR assignment:
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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:
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RPF scores
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Chemical shifts:
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Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
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PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
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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:
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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 11-10-2006, 02:06 PM
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Default Postdoctoral Research Position

NMR Postdoctoral Position
Department of Biochemistry and Biophysics
University of North Carolina
Chapel Hill, North Carolina


A postdoctoral position is available in the Campbell laboratory at the University of North Carolina to pursue structural, biophysical and biochemical research efforts on proteins that regulate cellular growth control through modulation of cell signaling and cell adhesion processes. The systems under investigation are of high biomedical relevance, especially in relation to cancer cell biology. Interested candidates will have access to state-of-the-art NMR facilities [Varian Inova 500, 600 MHz, 700 MHz (UNC-CH), 800 MHz (Duke); the 500, 700 and 800 MHz instruments are equipped with cryogenic probes]. Extensive offline SGI workstations and software are available for NMR data processing, analysis and structure calculations.

Minimum qualifications include a Ph.D., D.V.M., M.D. or equivalent in physics, chemistry, molecular biology, biochemistry, microbiology or a related discipline with an emphasis on NMR spectroscopy as it relates to the determination of protein structure. Candidates should have a strong background in modern NMR spectroscopic methods for bio-macromolecular structural analyses.
For additional information, please contact Sharon Campbell by e-mail (campbesl@med.unc.edu). Information regarding the Campbell laboratory can be obtained at the following website: http://www.med.unc.edu/biochem/scampbell/. Interested parties should submit a curriculum vitae along with telephone numbers and email addresses of three references to the address listed below.

Dr. Sharon Campbell
Department of Biochemistry and Biophysics
University of North Carolina
Chapel Hill, NC 27599-7260
(919)-966-7139; e-mail: campbesl@med.unc.edu
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