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NMR processing:

NMR assignment:

Backbone:

Side-chains:

UNIO ATNOS-Ascan

NOEs:

UNIO ATNOS-Candid

Structure from NMR restraints:

Ab initio:

UNIO ATNOS-Candid

Fragment-based:

BMRB CS-Rosetta

Rosetta-NMR (Robetta)

Template-based:

Refinement:

Structure from chemical shifts:

Fragment-based:

WeNMR CS-Rosetta

BMRB CS-Rosetta

Homology-based:

Torsion angles from chemical shifts:

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

MICS caps, β-turns

Flexibility from chemical shifts:

Interactions from chemical shifts:

Chemical shifts re-referencing:

UNIO Shiftinspector

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

Resolution-by-Proxy

SAVES2 or SAVES4

Ramachandran Plot

Quality Control Check

NMR spectrum prediction:

Flexibility from structure:

Molecular dynamics:

Chemical shifts prediction:

From structure:

CH3shift- Methyl

ArShift- Aromatic

CheShift-2- Cα

From sequence:

Disordered proteins:

Format conversion & validation:

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

Protein solubility:

Isotope labeling:

Solid-state NMR:

Showing results 1 to 2 of 2 Search took 0.00 seconds. Search: Posts From Last Day
		Thread / Thread Starter	Last Post	Replies	Views	Forum
		F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy - ACS Publications F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy - ACS Publications F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy ACS Publications Read here nmrlearner	Today 09:11 AM by nmrlearner	0	8	Online News
		Re-engineering of a carotenoid-binding protein based on NMR structure Re-engineering of a carotenoid-binding protein based on NMR structure Abstract Recently, a number of message passing neural network (MPNN)-based methods have been introduced that, based on backbone atom coordinates, efficiently recover native amino acid sequences of proteins and predict modifications that result in better expressing, more soluble, and stable variants. However, usually, X-ray structures, or artificial structures generated by algorithms trained on X-ray structures, were employed to define target backbone conformations. Here, we show that commonly used algorithms... nmrlearner	Yesterday 03:23 PM by nmrlearner	0	84	Journal club
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