NMR paper Determination of the electron relaxation rates in paramagnetic metal complexes: appli

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[NMR paper] Determination of the electron relaxation rates in paramagnetic metal complexes: appli

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

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11-24-2010, 09:51 PM

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Determination of the electron relaxation rates in paramagnetic metal complexes: appli

Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.

Related Articles Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.

J Magn Reson. 2004 Apr;167(2):169-77

Authors: Jensen MR, Led JJ

Four different approaches for determining the electron relaxation rates in paramagnetic metallo-proteins are investigated, using a paramagnetic Ni2+ complex of a protein as an example. All four approaches rely on the determination of the longitudinal paramagnetic relaxation enhancements, R1p, of the 1H nuclei and the backbone 15N nuclei. Three of the methods utilize the field dependence of the R1p rates. It is found that the applicability of each of these methods depends on whether the fast-motion condition, omegaS2tau2

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