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NMR processing:
MDD
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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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
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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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Default Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York

Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York

A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York Structural Biology Center
and Brookhaven National Laboratory. Varian and Bruker NMR instruments
with 500-700 MHz field strenghts are available on site. As a member of
the New York Structural Biology Center, we have access to 800 MHz and
900 MHz instruments as well as a access to a large pool of NMR
expertise. The location of Stony Brook University within public
transport commuting distance to New York City and the north shore of
Long Island provide a convenient work-life balance and a family
friendly environment.
Interested candidates with a strong background in protein NMR should
email their CV and the names of three references to Markus Seeliger
(markus.seeliger@gmail.com).


1.) Shan, Y., Seeliger, M.A., et al. A conserved
protonation-dependent switch controls drug binding in the Abl kinase.
Proc Natl Acad Sci U S A, 2009. 106(1): p. 139-44.

2.) Seeliger, M.A., et al., Equally potent inhibition of c-Src and Abl
by compounds that recognize inactive kinase conformations. Cancer Res,
2009. 69(6): p. 2384-92.

************************************************** *****
Markus Seelige
Assistant Professor
Department of Pharmacological Sciences
Stony Brook University Medical School, BST 7-125
Stony Brook, NY 11794-8651
phone: (631) 444-3558 fax: (631) 444-9749
http://www.pharm.stonybrook.edu/seeliger
************************************************** *****


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