Second EH domain of Eps15 in complex with the NPF region of Stonin 2

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
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1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex.

Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity.

Residues 6-100 in NMR structure calculations correspond to resiudes 121-215 in the wild-type sequence and pdb file numbering
residues 1-5 (GPLGS) in NMR structure calculations originate from the expression vector

Residues 106-145 in NMR structure calculation correspond to residues 301-340 of the wild-type sequence and pdb file numbering
residues 101-105 in NMR structure calculations originate from the expression vector

Structure Of The Second Eps15 Homology Domain Of Human Eps15, Nmr, 20 Structures

Structure Of The Second Eps15 Homology Domain Of Human Eps15 In Complex With Ptgssstnpfr

Structure Of The Second Eps15 Homology Domain Of Human Eps15 In Complex With Ptgssstnpfl

Structure Of The Eps15-eh2 Stonin2 Complex

Epidermal growth factor receptor substrate 15 [Myotis davidii]

endocytosis protein HSTNB variant [Homo sapiens]

PREDICTED: LOW QUALITY PROTEIN: stonin-2 [Pongo abelii]

PREDICTED: stonin-2 [Chinchilla lanigera]

RecName: Full=Stonin-2; AltName: Full=Stoned B [Homo sapiens]

Structure and Chemical Shift Assignment for the Eps15EH2-Stonin2 complex

Max-Planck-Institute for Medical Research

simulated annealing, torsion angle dynamics

in
10 mM perdeuterated Tris
100 mM NaCl
2 mM CaCl2
1 mM DTT

in
10 mM perdeuterated Tris pH 7
100 mM NaCl
2 mM CaCl2
1 mM DTT

10 mM perdeuterated Tris pH 7
100 mM NaCl
2 mM CaCl2
1 mM DTT

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax

Brunger, Adams, Clore, Gros, Nilges and Read