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NMR processing:
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Side-chains:
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Structure from NMR restraints:
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
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
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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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UNIO Shiftinspector
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iCing
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Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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CH3shift- Methyl
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ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Default NMR secondary structure of the plasminogen activator protein staphylokinase.

NMR secondary structure of the plasminogen activator protein staphylokinase.

Related Articles NMR secondary structure of the plasminogen activator protein staphylokinase.

J Biomol NMR. 1997 Apr;9(3):273-86

Authors: Ohlenschläger O, Ramachandran R, Flemming J, Gührs KH, Schlott B, Brown LR

Staphylokinase (Sak) is a 15.5 kDa protein secreted by several strains of Staphylococcus aureus. Due to its ability to convert plasminogen, the inactive proenzyme of the fibrinolytic system, into plasmin, Sak is presently undergoing clinical trials for blood clot lysis in the treatment of thrombovascular disorders. With a view to developing a better understanding of the mode of action of Sak, we have initiated a structural investigation of Sak via multidimensional heteronuclear NMR spectroscopy employing uniformly 15N- and 15N, 13C-labelled Sak. Sequence-specific resonance assignments have been made employing 15N-edited TOCSY and NOE experiments and from HNCACB, CBCA(CO)NH, HBHA-(CBCACO) NH and CC(CO)NH sets of experiments. From an analysis of the chemical shifts, 3JHNH alpha scalar coupling constants, NOEs and HN exchange data, the secondary structural elements of Sak have been characterized.

PMID: 9204556 [PubMed - indexed for MEDLINE]



Source: PubMed
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