NMR paper NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer

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[NMR paper] NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer

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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

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SAVES2 or SAVES4

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FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

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Gromacs

Amber

Antechamber

Chemical shifts prediction:

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Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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DisMeta

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11-17-2010, 11:06 PM

nmrlearner

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NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer

NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.

Related Articles NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.

J Biomol NMR. 1998 May;11(4):407-14

Authors: Pham TN, Koide S

The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We have accomplished nearly complete backbone H, C and N and C beta/H beta assignments of OspA (28 kDa) using standard triple resonance techniques without perdeuteration. This was made possible by recording spectra at a high temperature (45 degrees C). The chemical shift index and 15N T1/T2 ratios show that both the secondary structure and the global conformation of OspA in solution are similar to the crystal structure, suggesting that the unique central beta-sheet is fairly rigid.

PMID: 9691284 [PubMed - indexed for MEDLINE]

Source: PubMed

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