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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 02-13-2012, 02:48 PM
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Default Postdoctoral position in biomolecular NMR

Postdoctoral position in biomolecular NMR

Postdoctoral Research Associate - Biomolecular NMRDepartment of Biochemistry, South Parks Road, OxfordGrade 7: £29,099 - £35,788 p.a.We are seeking to appoint a Postdoctoral Research Associate in Biomolecular NMRto study the structure and interactions of medically or biologically importantmembrane proteins. This position is part of a joint research activity withseveral other European biomolecular NMR groups involved in the Bio-NMRinitiative www.bio-nmr.net. The goal of the project in Oxford is to applymethods developed by other Bio-NMR partners to the study of challengingmembrane proteins.Applicants should possess a PhD (or be expected shortly to attain one) inBiochemistry, Biophysics or Chemistry and are expected to have relevantexperience in solution-state NMR that includes pulse-sequence implementation,NMR data processing and analysis, and computer programming. This full-time post is funded by the European Commission’s FrameworkProgramme 7 (FP7) Bio-NMR initiative www.bio-nmr.net for up to 12 months in thefirst instance and is based at the Biomolecular NMR Centre in the Department ofBiochemistry, South Parks Road, Oxford. The successful candidate will beformally based in the group of Dr Jason Schnell, but will be expected tointeract extensively with other NMR groups in the Centre.Please quote reference number BR/494 when applying and include a cv and asupporting statement. The closing date for applications is midday on Friday 24February 2012, with interviews for shortlisted candidates on Thursday 8 March2012.Contact Person : Margaret Dixon or Rita Emberton Vacancy ID : 102047Contact Phone : 01865 613204 Closing Date : 24-Feb-2012Contact Email : jobs@bioch.ox.ac.uk

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