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Side-chains:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
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UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
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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:
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MICS caps, β-turns
d2D
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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NMR model quality:
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Chemical shifts:
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V-NMR
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Methyl S2
B-factor
Molecular dynamics:
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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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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:
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ccSOL
Camfold
camGroEL
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Isotope labeling:
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Solid-state NMR:
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Old 01-03-2016, 01:25 AM
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Default NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.

NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.

Related Articles NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.

Biomol NMR Assign. 2015 Dec 31;

Authors: Polshakov VI, Petrova OA, Parfenova YY, Efimov SV, Klochkov VV, Zvereva MI, Dontsova OA

Abstract
Telomerase is a ribonucleoprotein enzyme that adds telomeric DNA fragments to the ends of chromosomes. This enzyme is the focus of substantial attention, both because its structure and mechanism of action are still poorly studied, and because of its pivotal roles in aging and cellular proliferation. The use of telomerase as a potential target for the design of new anticancer drugs is also of great interest. The catalytic protein subunit of telomerase (TERT) contains an N-terminal domain (TEN) that is essential for activity and processivity. Elucidation of the structure and dynamics of TEN in solution is important for understanding the molecular mechanism of telomerase activity and for the design of new telomerase inhibitors. To approach this problem, in this study we report the (1)H, (13)C, and (15)N chemical shift assignments of TEN from Ogataea polymorpha. Analysis of the assigned chemical shifts allowed us to identify secondary structures and protein regions potentially involved in interaction with other participants of the telomerase catalytic cycle.


PMID: 26721464 [PubMed - as supplied by publisher]



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