Lyme disease antigen ospa in complex with neutralizing antibody FAB la-2. Determined by X-ray diffraction at 2.68 Å resolution. Released 11 Oct 2000.
Explore 1FJ1 in 3D Show helices and sheets RCSB PDB PDBe
1FJ1 contains 25 α-helices and 135 β-strands across 6 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 | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-107 | 6 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 5 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 35-39 | 5 | 7 |
| β-strand | 45-51 | 7 | 7 |
| β-strand | 58-60 | 3 | 7 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 6 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 7 |
| β-strand | 102-103 | 2 | 7 |
| β-strand | 107-111 | 5 | 7 |
| β-strand | 117 | 1 | 8 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 9 |
| β-strand | 135-145 | 11 | 9 |
| β-strand | 146 | 1 | 8 |
| β-strand | 151-155 | 5 | 10 |
| β-strand | 162-171 | 10 | 9 |
| β-strand | 174-184 | 11 | 9 |
| β-strand | 194-199 | 6 | 10 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 11 |
| β-strand | 10-14 | 5 | 12 |
| β-strand | 19-25 | 7 | 11 |
| β-strand | 33-38 | 6 | 12 |
| β-strand | 45-49 | 5 | 12 |
| β-strand | 53-54 | 2 | 12 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 11 |
| β-strand | 70-75 | 6 | 11 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 12 |
| β-strand | 97-98 | 2 | 12 |
| β-strand | 102-107 | 6 | 12 |
| β-strand | 111 | 1 | 13 |
| β-strand | 114-118 | 5 | 14 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 14 |
| β-strand | 140 | 1 | 13 |
| β-strand | 145-150 | 6 | 15 |
| β-strand | 153-155 | 3 | 15 |
| β-strand | 159-163 | 5 | 14 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 14 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 15 |
| β-strand | 205-210 | 6 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 16 |
| β-strand | 10-12 | 3 | 17 |
| β-strand | 18-25 | 8 | 16 |
| α-helix | 29-31 | 3 | |
| β-strand | 35-39 | 5 | 17 |
| β-strand | 46-51 | 6 | 17 |
| β-strand | 58-60 | 3 | 17 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 16 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 16 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 17 |
| β-strand | 102-103 | 2 | 17 |
| β-strand | 107-111 | 5 | 17 |
| β-strand | 117 | 1 | 18 |
| β-strand | 120-124 | 5 | 19 |
| β-strand | 133 | 1 | 19 |
| β-strand | 135-145 | 11 | 19 |
| β-strand | 146 | 1 | 18 |
| β-strand | 151-155 | 5 | 20 |
| β-strand | 163-171 | 9 | 19 |
| β-strand | 174-184 | 11 | 19 |
| β-strand | 194-199 | 6 | 20 |
| β-strand | 204-209 | 6 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31-34 | 4 | 21 |
| β-strand | 38-41 | 4 | 21 |
| β-strand | 54 | 1 | 22 |
| β-strand | 55 | 1 | 21 |
| β-strand | 65 | 1 | 22 |
| β-strand | 75-76 | 2 | 23 |
| β-strand | 79 | 1 | 24 |
| β-strand | 85 | 1 | 24 |
| β-strand | 87-89 | 3 | 23 |
| β-strand | 98-102 | 5 | 23 |
| β-strand | 109-115 | 7 | 23 |
| β-strand | 121-126 | 6 | 23 |
| β-strand | 132-138 | 7 | 23 |
| β-strand | 144-148 | 5 | 23 |
| β-strand | 156-162 | 7 | 23 |
| β-strand | 165-171 | 7 | 23 |
| β-strand | 175-182 | 8 | 23 |
| β-strand | 185-192 | 8 | 23 |
| β-strand | 197-203 | 7 | 23 |
| β-strand | 212-217 | 6 | 25 |
| β-strand | 222-227 | 6 | 25 |
| β-strand | 230-237 | 8 | 25 |
| β-strand | 243-247 | 5 | 25 |
| β-strand | 248 | 1 | 26 |
| β-strand | 255 | 1 | 26 |
| β-strand | 260-261 | 2 | 25 |
| α-helix | 265-271 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hybridoma antibody LA2 (light chain) | A, C | protein | 213 | Mus musculus | P01837 (AlphaFold model) |
| Hybridoma antibody LA2 (heavy chain) | B, D | protein | 213 | Mus musculus | P01867 (AlphaFold model) |
| Outer surface protein A | E, F | protein | 257 | Borrelia burgdorferi | P0CL66 (AlphaFold model) |
>1FJ1_1 HYBRIDOMA ANTIBODY LA2 (LIGHT CHAIN) (chains A, C) DIQMTQSPSSLSATLGGKVTITCKASQDINKYIAWYQHKPGKGPRLLIHYTSTLQPGNPS RFSGSGSGRDYSFSISNLEAEDIAIYYCLQYDNLQRTFGGGTKVEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNE
>1FJ1_2 HYBRIDOMA ANTIBODY LA2 (HEAVY CHAIN) (chains B, D) QIQLVQSGPELKKPGETVKISCKASGYTFTDYSMYWVKQAPGKGLKRMGWINTETGEPTY ADDFKGRFALSLDTSASTAYLHISNLKNEDTATYFCARGLDSWGQGTSVTVSSAKTTPPS VYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSS VTVPSSTWPSQTVTCSVAHPASSTTVDKKLEPS
>1FJ1_3 OUTER SURFACE PROTEIN A (chains E, F) AKQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVL EGVKADKCKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKI ITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGE VSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLE GSAVEITKLDEIKNALK
Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA. Ding, W., Huang, X., Yang, X. et al. J Mol Biol (2000) 302:1153-1164. DOI 10.1006/jmbi.2000.4119 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1FJ1 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.