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NMR processing:
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NMR assignment:
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Side-chains:
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NOEs:
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UNIO Candid
ASDP
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
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RDCs:
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Methyl S2
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Molecular dynamics:
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From structure:
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ArShift- Aromatic
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From sequence:
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Camcoil
Poulsen_rc_CS
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:
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Default NMR determination of the secondary structure and the three-dimensional polypeptide ba

NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.

Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.

FEBS Lett. 1993 Nov 29;335(1):18-26

Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, W├╝thrich K

Nuclear magnetic resonance (NMR) spectroscopy was used to determine the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2 (hSCP2), which is a basic protein with 123 residues believed to participate in the intracellular transport of cholesterol and various other lipids. Sequence-specific assignments were obtained for nearly all backbone 1H and 15N resonances, as well as for about two-thirds of the side-chain 1H resonances, using uniform 15N-labeling of the protein combined with homonuclear two-dimensional 1H NMR and three-dimensional 15N-correlated 1H NMR. Three alpha-helices comprising the polypeptide segments of residues 9-22, 25-30 and 78-84 were identified by sequential and medium-range nuclear Overhauser effects (NOE). The analysis of long-range backbone-backbone NOEs showed that hSCP2 further contains a five-stranded beta-sheet including the residues 33-41, 47-54, 60-62, 71-76 and 100-102, which is a central feature of the molecular architecture. The first three strands are arranged in an antiparallel fashion, the polypeptide chain then crosses over this three-stranded sheet in a right-handed sense so that the fourth strand is added parallel to the first one. The fifth strand runs antiparallel to the fourth one, so that the overall topology is +1, +1, -3x, -1. The three-dimensional arrangement of the beta-sheet and the first two helices was determined using an input of 625 NOE upper distance constraints and 95 scalar coupling constants for a preliminary structure calculation with the distance geometry program DIANA.

PMID: 8243660 [PubMed - indexed for MEDLINE]



Source: PubMed
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