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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
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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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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Chemical shifts re-referencing:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
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From sequence:
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Disordered proteins:
MAXOCC
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
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Default 15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9

15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states.

Related Articles 15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states.

FEBS Lett. 1992 Jun 1;303(2-3):136-40

Authors: Skelton NJ, Akke M, Kördel J, Thulin E, Forsén S, Chazin WJ

15N has been uniformly incorporated into the EF-hand Ca(2+)-binding protein calbindin D9k so that heteronuclear experiments can be used to further characterize the structure and dynamics of the apo, (Cd2+)1 and (Ca2+)2 states of the protein. The 15N NMR resonances were assigned by 2D 15N-resolved 1H experiments, which also allowed the identification of a number of sequential and medium-range 1H-1H contacts that are obscured by chemical shift degeneracy in homonuclear experiments. The 15N chemical shifts are analyzed with respect to correlations with protein secondary structure. In addition, the changes in 15N chemical shift found for the apo----(Cd2+)1----(Ca2+)2 binding sequence confirm that the effects on the protein are mainly associated with chelation of the first ion.

PMID: 1607011 [PubMed - indexed for MEDLINE]



Source: PubMed
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