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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 08-21-2010, 05:17 AM
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Default postdoctoral position in macromolecular NMR

postdoctoral position in macromolecular NMR

There is an opening for a postdoctoral position in macromolecular NMR
and structural biology at the Structural Biophysics Laboratory, National
Cancer Institute, Frederick, MD.

A highly motivated individual is sought to conduct studies in NMR, dynamics,
and integrated structural and functional understanding of proteins and complexes
in the ubiquitination pathway. For an example of the type of work please see
Mol. Cell 34(6):674 [2009]. Individuals interested in spectroscopy, new methods, and/or
biological applications with a commitment to a research career are encouraged to apply.

The position is fully funded and the initial appointment can be extended. Resources
include a wide range of biophysical equipment and NMR spectrometers.

For further information, please contact R. Andrew Byrd via email at byrdra@mail.nih.gov

===============================================
R. Andrew Byrd 301-846-1407
Dir., Molecular Discovery Program
Chief, Structural Biophysics Laboratory FAX 301-846-6231
Macromolecular NMR byrdra@mail.nih.gov
http://ccr.cancer.gov/resources/sbl/

Center for Cancer Research
National Cancer Institute-Frederick
P.O. Box B, Bldg. 538
Frederick, MD 21702-1201
===============================================


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