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NMR processing:
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NMR assignment:
Backbone:
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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:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
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RPF scores
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Chemical shifts:
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Vasco
iCing
RDCs:
DC
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Pseudocontact shifts:
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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:
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 07-14-2007, 03:55 AM
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Default NMR post-doc position: NMR-based dynamics study of enzyme mechanism

The following post-doc position in NMR is available in University of Missouri:

Ad text:


"""
We have an opening for a postdoctoral fellow to use NMR to study dynamics of an enzyme while it is carrying on reversible catalysis. The prospects are promising and can be compared with thorough enzymology and crystallography of its ligand-dependent conformational changes (done in our dept.). The enzyme is sizeable enough to be challenging, but we have a battery of excellent 800 MHz spectra of deuterated samples for launching the project. The postdoctoral fellow will be housed in a new building on the same floor with a new 800 MHz facility. In January or February, the new compact Bruker 800 MHz Avance III with TCI cryoprobe will be installed. It joins an existing Inova 600 MHz with cryogenic probe and a Bruker DRX-500 being upgraded with TCI cryoprobe. The fellow will have stimulating interactions with Lesa Beamer’s crystallography group, an enzymologist, and a group simulating enzyme reactions. The abstract for the small, collaborative NIH grant creating the position is at:



http://crisp.cit.nih.gov/crisp/CRISP...11&p_keywords=

Inquiries, applications, or recommendations should be addressed to me and/or Lesa Beamer (beamerl@missouri.edu).


Steven R. Van Doren, Assoc. Prof. &
Director of Graduate Studies
Biochemistry Department, 117 Schweitzer Hall
University of Missouri, Columbia, MO 65211
vandorens@missouri.edu
phone: (573) 882-5113; FAX: (573) 884-4812
"""
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