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Side-chains:
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NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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iCing
RDCs:
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Protein geomtery:
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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PPM
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From sequence:
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Camcoil
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
UPLABEL
Solid-state NMR:
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Default NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.

NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.

Related Articles NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.

Biomol NMR Assign. 2013 Jan 17;

Authors: Vajpai N, Schott AK, Vogtherr M, Breeze AL

Abstract
Members of the fibroblast growth factor receptor tyrosine kinase family (FGFR1-4) play an important role in many signalling cascades. Although tightly regulated, aberrant activity of these enzymes may lead to, or become features of, disease pathologies including cancer. FGFR isoforms have been the subject of drug discovery programmes, with a number of kinase-domain inhibitors in pre-clinical and clinical development. Here, we present the first (83*% complete) backbone resonance assignments of apo-FGFR1 kinase.


PMID: 23325512 [PubMed - as supplied by publisher]



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