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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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Old 01-29-2014, 02:37 PM
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Default Postdoctoral fellow position at the NIH

The Structural Biophysics Section of the National Heart, Lung, and Blood Institute (NHLBI) at the NIH seeks postdoctoral candidates with experience in advanced solution NMR techniques who are interested in developing innovative approaches to solving problems in structural biology. Candidates should have a Ph.D. in physics, chemistry, or biochemistry. Previous knowledge in protein expression and purification would be advantageous but not essential. The responsibilities of the fellow include developing alternative NMR methods for structure determination, improving NMR relaxation data analysis, and preparation of proteins for structural studies. The Section has strong research programs in apoptosis, cytoskeleton regulation, as well as retroviral replication.

The Structural Biophysics Section has excellent NMR instrumentations, including dedicated 600 MHz and 800 MHz spectrometers as well as access to a 900 MHz spectrometer, all equipped with cryogenic probes. In addition, there is access to modern core facilities within the NHLBI such as the Biochemistry facility (for protein identification and separation), Biophysics core (characterization of protein and their complexes), Light Microscopy core, and Electron Microscopy core. The large NMR community at the NIH has outstanding research and development programs that provides an excellent training environment for postdoctoral fellows.

Interested candidates can email a cover letter, CV with bibliography and the names of three references to:

Nico Tjandra
Laboratory of Molecular Biophysics
National Heart, Lung, and Blood Institute
National Institutes of Health
50 South Drive, Room 3503
Bethesda, MD 20892
301-402-3029
tjandran@nhlbi.nih.gov
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