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NMR processing:
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NMR assignment:
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Side-chains:
UNIO ATNOS-Ascan
NOEs:
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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:
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Secondary structure from chemical shifts:
CSI (via RCI server)
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MICS caps, β-turns
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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RefDB
NMR model quality:
NOEs, other restraints:
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RPF scores
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Chemical shifts:
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Vasco
iCing
RDCs:
DC
Anisofit
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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Ramachandran Plot
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ERRAT
Verify_3D
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NMR spectrum prediction:
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Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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CH3shift- Methyl
ArShift- Aromatic
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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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Unread 08-14-2010, 04:19 AM
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Default Automated solvent artifact removal and base plane correction of multidimensional NMR

Abstract Strong solvent signals lead to a disappearance of weak protein signals close to the solvent resonance frequency and to base plane variations all over the spectrum. AUREMOL-SSA provides an automated approach for solvent artifact removal from multidimensional NMR protein spectra. Its core algorithm is based on singular spectrum analysis (SSA) in the time domain and is combined with an automated base plane correction in the frequency domain. The performance of the method has been tested on synthetic and experimental spectra including two-dimensional NOESY and TOCSY spectra and a three-dimensional 1H,13C-HCCH-TOCSY spectrum. It can also be applied to frequency domain spectra since an optional inverse Fourier transformation is included in the algorithm.
  • Content Type Journal Article
  • DOI 10.1007/s10858-010-9414-z
  • Authors
    • Wilhelm M. Malloni, University of Regensburg Institute of Biophysics and Physical Biochemistry 93040 Regensburg Germany
    • Silvia De Sanctis, University of Regensburg Institute of Biophysics and Physical Biochemistry 93040 Regensburg Germany
    • Ana M. Tomé, University of Aveiro Department Electrical Engineering, Telecommunications and Informatics 3100 Aveiro Portugal
    • Elmar W. Lang, University of Regensburg Institute of Biophysics and Physical Biochemistry 93040 Regensburg Germany
    • Claudia E. Munte, University of Regensburg Institute of Biophysics and Physical Biochemistry 93040 Regensburg Germany
    • Klaus Peter Neidig, BioSpin GmbH, Software Department Silberstreifen 4 76287 Rheinstetten Germany
    • Hans Robert Kalbitzer, University of Regensburg Institute of Biophysics and Physical Biochemistry 93040 Regensburg Germany

Source: Journal of Biomolecular NMR
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