1TCE
| SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE | Descriptor: | PHOSPHOPEPTIDE OF THE ZETA CHAIN OF T CELL RECEPTOR, SHC | Authors: | Zhou, M.-M, Meadows, R.P, Logan, T.M, Yoon, H.S, Wade, W.R, Ravichandran, K.S, Burakoff, S.J, Feisk, S.W. | Deposit date: | 1996-03-27 | Release date: | 1997-05-15 | Last modified: | 2024-10-30 | Method: | SOLUTION NMR | Cite: | Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proc.Natl.Acad.Sci.USA, 92, 1995
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1HCS
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1HCT
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8T6I
| Structure of VHH-Fab complex with engineered Crystal Kappa region | Descriptor: | Fab heavy chain, Fab light chain, GLYCEROL, ... | Authors: | Filippova, E.V, Thompson, I, Kossiakoff, A.A. | Deposit date: | 2023-06-16 | Release date: | 2023-11-29 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (2.55 Å) | Cite: | Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes. Protein Sci., 33, 2024
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8T58
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8T8I
| Structure of VHH-Fab complex with engineered Elbow FNQIKG, Crystal Kappa and SER substitutions | Descriptor: | CHLORIDE ION, DI(HYDROXYETHYL)ETHER, Fab heavy chain, ... | Authors: | Filippova, E.V, Thompson, I, Kossiakoff, A.A. | Deposit date: | 2023-06-22 | Release date: | 2023-11-29 | Last modified: | 2024-10-09 | Method: | X-RAY DIFFRACTION (2.52 Å) | Cite: | Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes. Protein Sci., 33, 2024
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8T9Y
| Structure of VHH-Fab complex with engineered Elbow FNQIKG and Crystal Kappa regions | Descriptor: | DI(HYDROXYETHYL)ETHER, Fab heavy chain, Fab light chain, ... | Authors: | Filippova, E.V, Thompson, I, Kossiakoff, A.A. | Deposit date: | 2023-06-26 | Release date: | 2023-11-29 | Last modified: | 2024-10-23 | Method: | X-RAY DIFFRACTION (2.52 Å) | Cite: | Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes. Protein Sci., 33, 2024
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