Search Count: 7
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Different Thermodynamic Binding Mechanisms And Peptide Fine Specificities Associated With A Panel Of Structurally Similar High-Affinity T Cell Receptors
Organism: Homo sapiens
Method: X-RAY DIFFRACTION Resolution:1.95 Å Release Date: 2008-11-25 Classification: IMMUNE SYSTEM |
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Release Date: 2008-11-25
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Crystal Structure Of A Surrogate Light Chain (Lambda5 And Vpreb) Homodimer
Organism: Homo sapiens
Method: X-RAY DIFFRACTION Resolution:2.30 Å Release Date: 2007-05-08 Classification: IMMUNE SYSTEM |
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Release Date: 2007-05-08
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Structure Of A High-Affinity Mutant Of The 2C Tcr In Complex With Ld/Ql9
Organism: Mus musculus
Method: X-RAY DIFFRACTION Resolution:2.50 Å Release Date: 2007-04-24 Classification: IMMUNE SYSTEM |
Organism: Mus musculus
Method: X-RAY DIFFRACTION
Release Date: 2007-04-24
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Crystal Structure Of The Pre-B Cell Receptor
Organism: Homo sapiens
Method: X-RAY DIFFRACTION Resolution:2.70 Å Release Date: 2007-04-24 Classification: IMMUNE SYSTEM Ligands: ZN |
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Release Date: 2007-04-24
Ligands: ZN
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Structure Of The 2C/Ld/Ql9 Allogeneic Complex
Organism: Mus musculus
Method: X-RAY DIFFRACTION Resolution:2.35 Å Release Date: 2007-04-24 Classification: IMMUNE SYSTEM |
Organism: Mus musculus
Method: X-RAY DIFFRACTION
Release Date: 2007-04-24
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Structure Of A Human A-Type Potassium Channel Accelerating Factor Dppx, A Member Of The Dipeptidyl Aminopeptidase Family
Organism: Homo sapiens
Method: X-RAY DIFFRACTION Resolution:3.00 Å Release Date: 2004-10-26 Classification: MEMBRANE PROTEIN |
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Release Date: 2004-10-26
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Crystal Structure Of Leukemia Inhibitory Factor In Complex With Gp130
Organism: Homo sapiens
Method: X-RAY DIFFRACTION Resolution:2.50 Å Release Date: 2003-10-14 Classification: signaling protein/cytokine Ligands: IOD |
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Release Date: 2003-10-14
Ligands: IOD
