NMR paper Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou

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[NMR paper] Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou

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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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08-22-2010, 03:41 AM

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Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou

Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.

Related Articles Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.

FEBS Lett. 1995 Apr 10;362(3):333-6

Authors: Bycroft M, Proctor M, Freund SM, St Johnston D

NMR spectroscopy has been used to determine the secondary structure of one of the double-stranded RNA binding domains from the Drosophila protein staufen. The domain has an alpha beta beta beta alpha arrangement of secondary structure, with the beta strands forming an antiparallel beta sheet. The secondary structure differs from that found in the RNP RNA binding domain.

PMID: 7729524 [PubMed - indexed for MEDLINE]

Source: PubMed

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