Murine alloreactive scFv TCR-peptide-MHC class I molecule complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 11 Mar 2003.
Explore 1NAM in 3D Show helices and sheets RCSB PDB PDBe
1NAM contains 11 α-helices and 51 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 1 |
| β-strand | 9-13 | 5 | 2 |
| β-strand | 18-20 | 3 | 1 |
| β-strand | 23-24 | 2 | 1 |
| β-strand | 31-37 | 7 | 2 |
| β-strand | 43-50 | 8 | 2 |
| β-strand | 58-59 | 2 | 1 |
| β-strand | 62-67 | 6 | 1 |
| α-helix | 68-70 | 3 | |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 2 |
| β-strand | 104-106 | 3 | 2 |
| β-strand | 110-115 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 3 |
| β-strand | 10-13 | 4 | 4 |
| β-strand | 19-25 | 7 | 3 |
| β-strand | 31-37 | 7 | 4 |
| β-strand | 43-49 | 7 | 4 |
| β-strand | 55-60 | 6 | 3 |
| β-strand | 63-69 | 7 | 3 |
| β-strand | 74-80 | 7 | 3 |
| β-strand | 86-95 | 8 | 4 |
| α-helix | 103-106 | 3 | |
| β-strand | 107-108 | 2 | 4 |
| β-strand | 112-116 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 5 |
| β-strand | 21-28 | 8 | 5 |
| β-strand | 31-37 | 7 | 5 |
| β-strand | 46-47 | 2 | 5 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 5 |
| β-strand | 109-118 | 10 | 5 |
| β-strand | 121-126 | 6 | 5 |
| β-strand | 133-135 | 3 | 5 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-179 | 17 | |
| β-strand | 183 | 1 | 6 |
| β-strand | 186-191 | 6 | 7 |
| β-strand | 201-208 | 8 | 7 |
| β-strand | 209 | 1 | 6 |
| β-strand | 214-218 | 5 | 8 |
| β-strand | 223 | 1 | 8 |
| β-strand | 229-230 | 2 | 7 |
| β-strand | 234-235 | 2 | 7 |
| β-strand | 241-247 | 7 | 7 |
| β-strand | 258-262 | 5 | 8 |
| β-strand | 270-272 | 3 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| β-strand | 6-9 | 4 | 9 |
| β-strand | 24-30 | 7 | 9 |
| β-strand | 35-39 | 5 | 10 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 9 |
| β-strand | 62-67 | 6 | 9 |
| β-strand | 79 | 1 | 11 |
| β-strand | 80-84 | 5 | 10 |
| β-strand | 91 | 1 | 10 |
| β-strand | 94 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-7 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BM3.3 T Cell Receptor alpha-Chain | A | protein | 116 | Mus musculus | Q5R1F1 (AlphaFold model) |
| BM3.3 T Cell Receptor beta-Chain | B | protein | 113 | Mus musculus | P04214 (AlphaFold model) |
| H-2 class I histocompatibility antigen, K-B alpha chain precursor | H | protein | 275 | Mus musculus | P01901 (AlphaFold model) |
| Nucleocapsid | P | protein | 8 | P11212 | |
| Beta-2-microglobulin | L | protein | 100 | Mus musculus | P01887 |
>1NAM_1 BM3.3 T Cell Receptor alpha-Chain (chains A) QKVTQTQTSISVMEKTTVTMDCVYETQDSSYFLFWYKQTASGEIVFLIRQDSYKKENATV GHYSLNFQKPKSSIGLIITATQIEDSAVYFCAMRGDYGGSGNKLIFGTGTLLSVKP
>1NAM_2 BM3.3 T Cell Receptor beta-Chain (chains B) VTLLEQNPRWRLVPRGQAVNLRCILKNSQYPWMSWYQQDLQKQLQWLFTLRSPGDKEVKS LPGADYLATRVTDTELRLQVANMSQGRTLYCTCSADRVGNTLYFGEGSRLIVV
>1NAM_3 H-2 class I histocompatibility antigen, K-B alpha chain precursor (chains H) GPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYW ERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDG CDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLL RTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGT FQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWE
>1NAM_4 Nucleocapsid (chains P) RGYVYQGL
>1NAM_5 Beta-2-microglobulin (chains L) MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKD WSFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
CDR3 loop flexibility contributes to the degeneracy of TCR recognition. Reiser, J.-B., Darnault, C., Gregoire, C. et al. Nat Immunol (2003) 4:241-247. DOI 10.1038/ni891 · PubMed
Other PDB entries of the same protein (UniProt Q5R1F1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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