NMR paper NMR backbone resonance assignments of the N, P domains of CopA, a copper-transporting ATPase, in the apo and ligand bound states.

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[NMR paper] NMR backbone resonance assignments of the N, P domains of CopA, a copper-transporting ATPase, in the apo and ligand bound states.

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

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Solid-state NMR:

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11-14-2015, 03:37 PM

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NMR backbone resonance assignments of the N, P domains of CopA, a copper-transporting ATPase, in the apo and ligand bound states.

Related Articles NMR backbone resonance assignments of the N, P domains of CopA, a copper-transporting ATPase, in the apo and ligand bound states.

Biomol NMR Assign. 2015 Apr;9(1):129-33

Authors: Meng D, Bruschweiler-Li L, Zhang F, Brüschweiler R

Abstract
Copper-transporting ATPase, a member of P-type ATPase family, plays a key role in the homeostasis of cellular copper levels. Here, the backbone assignments of the directly connected N and P domains (292 residues, 31*kDa) of Cu-transporting ATPase in the ligand free and the AMPPCP-bound states are reported in solution. The NMR assignments pave the way for binding and dynamics studies of this enzyme to better understand its function.

PMID: 24706033 [PubMed - indexed for MEDLINE]

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