TCR156 S32Halpha bound to HLA A*02:01-PAP. Determined by X-ray diffraction at 1.97 Å resolution. Released 18 Mar 2026.
Explore 9NMV in 3D Show helices and sheets RCSB PDB PDBe
9NMV contains 27 α-helices and 72 β-strands across 4 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 | 3-12 | 10 | 1 |
| α-helix | 18-20 | 3 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-192 | 7 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222 | 1 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 253-256 | 4 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-273 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 8 |
| β-strand | 11-14 | 4 | 9 |
| β-strand | 19-25 | 7 | 8 |
| β-strand | 32-38 | 7 | 9 |
| β-strand | 45-50 | 6 | 9 |
| β-strand | 54-58 | 5 | 8 |
| β-strand | 61-66 | 6 | 8 |
| β-strand | 71-76 | 6 | 8 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-92 | 8 | 9 |
| β-strand | 96-98 | 3 | 9 |
| β-strand | 102-107 | 6 | 9 |
| α-helix | 108 | 1 | |
| β-strand | 116-121 | 6 | 10 |
| β-strand | 122 | 1 | 11 |
| β-strand | 129-134 | 6 | 10 |
| β-strand | 151-152 | 2 | 10 |
| α-helix | 153-155 | 3 | |
| β-strand | 156-160 | 5 | 10 |
| β-strand | 165-173 | 9 | 10 |
| β-strand | 195 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 12 |
| β-strand | 10-14 | 5 | 13 |
| β-strand | 19-24 | 6 | 12 |
| α-helix | 25-26 | 2 | |
| β-strand | 31-37 | 7 | 13 |
| β-strand | 43-50 | 8 | 13 |
| β-strand | 53-57 | 5 | 13 |
| β-strand | 64-68 | 5 | 12 |
| β-strand | 74-78 | 5 | 12 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-94 | 8 | 13 |
| α-helix | 100-101 | 2 | |
| β-strand | 102-103 | 2 | 13 |
| β-strand | 107-112 | 6 | 13 |
| α-helix | 115-117 | 3 | |
| β-strand | 119 | 1 | 14 |
| α-helix | 120-121 | 2 | |
| β-strand | 122-126 | 5 | 11 |
| α-helix | 127-129 | 3 | |
| α-helix | 130-136 | 7 | |
| β-strand | 138-148 | 11 | 11 |
| β-strand | 149 | 1 | 14 |
| β-strand | 153-159 | 7 | 15 |
| β-strand | 162-164 | 3 | 15 |
| β-strand | 168-170 | 3 | 11 |
| α-helix | 174 | 1 | |
| β-strand | 175-176 | 2 | 11 |
| β-strand | 186-195 | 10 | 11 |
| α-helix | 196-199 | 4 | |
| β-strand | 205-212 | 8 | 15 |
| β-strand | 215 | 1 | 16 |
| α-helix | 226-227 | 2 | |
| β-strand | 229 | 1 | 16 |
| β-strand | 231-238 | 8 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class I histocompatibility antigen, A alpha chain | A | protein | 279 | Homo sapiens | A5I8L1 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Prostatic acid phosphatase | C | protein | 9 | Homo sapiens | P15309 (AlphaFold model) |
| TCR156 alpha chain S32H variant | D | protein | 255 | Homo sapiens | |
| TCR156 beta chain | E | protein | 307 | Homo sapiens |
>9NMV_1 HLA class I histocompatibility antigen, A alpha chain (chains A) MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEY WDGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD GKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETL QRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG TFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEPSS
>9NMV_2 Beta-2-microglobulin (chains B) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>9NMV_3 Prostatic acid phosphatase (chains C) TLMSAMTNL
>9NMV_4 TCR156 alpha chain S32H variant (chains D) QQKEVEQNSGPLSVPEGAIASLNCTYSDRGSQHFFWYRQYSGKSPELIMFIYSNGDKEDG RFTAQLNKASQYVSLLIRDSQPSDSATYLCAVNNARLMFGDGTQLVVKPNIQNPDPAVYQ LRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSDF ACANAFNNSIIPEDTFFPSPESSSRGGLEVLFQGPEFGGSTTAPSAQLKKKLQALKKKNA QLKWKLQALKKKLAQ
>9NMV_5 TCR156 beta chain (chains E) GVTQTPKHLITATGQRVTLRCSPRSGDLSVYWYQQSLDQGLQFLIQYYNGEERAKGNILE RFSAQQFPDLHSELNLSSLELGDSALYFCASSVAGSPEAFFGQGTRLTVVEDLKNVFPPE VAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPALN DSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRAD SRGGLEVLFQGPEFGGSTTAPSAQLEKELQALEKENAQLEWELQALEKELAQGLNDIFEA QKIEWHE
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (GOL) are not listed.
Overcoming T cell tolerance to tumor self-antigens through catch-bond engineering. Chen, X., Mao, Z., Kolawole, E.M. et al. Science (2026) 391:eadx3162-eadx3162. DOI 10.1126/science.adx3162 · PubMed
Other PDB entries of the same protein (UniProt A5I8L1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9NMV directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.