{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":1,"total":29,"mapped":1},"pagination":{"has_next":false},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"input":"P02649","source":"P02649|Apolipoprotein E","targets":["1B68|APOLIPOPROTEIN E4 (APOE4), 22K FRAGMENT|X-RAY DIFFRACTION|2|Homo sapiens|0|LIPID TRANSPORT","1BZ4|APOLIPOPROTEIN E3 (APO-E3), TRUNCATION MUTANT 165|X-RAY DIFFRACTION|1.85|Homo sapiens|0|LIPID BINDING PROTEIN","1EA8|Apolipoprotein E3 22kD fragment LYS146GLU mutant|X-RAY DIFFRACTION|1.95|HOMO SAPIENS|0|LIPID BINDING PROTEIN","1GS9|Apolipoprotein E4, 22k domain|X-RAY DIFFRACTION|1.7|HOMO SAPIENS|0|LIPID BINDING PROTEIN","1H7I|Apolipoprotein E3 22kD fragment LYS146GLN mutant|X-RAY DIFFRACTION|1.9|HOMO SAPIENS|0|LIPID BINDING PROTEIN","1LE2|STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E|X-RAY DIFFRACTION|3|Homo sapiens|0|LIPOPROTEIN","1LE4|STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E|X-RAY DIFFRACTION|2.5|Homo sapiens|0|LIPOPROTEIN","1LPE|THREE-DIMENSIONAL STRUCTURE OF THE LDL RECEPTOR-BINDING DOMAIN OF HUMAN APOLIPOPROTEIN E|X-RAY DIFFRACTION|2.25|Homo sapiens|0|LIPOPROTEIN","1NFN|APOLIPOPROTEIN E3 (APOE3)|X-RAY DIFFRACTION|1.8|Homo sapiens|0|LIPID TRANSPORT","1NFO|APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)|X-RAY DIFFRACTION|2|Homo sapiens|0|LIPID TRANSPORT","1OEF|PEPTIDE OF HUMAN APOE RESIDUES 263-286, NMR, 5 STRUCTURES AT PH 4.8, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90|SOLUTION NMR||Homo sapiens|0|APOLIPOPROTEIN","1OEG|PEPTIDE OF HUMAN APOE RESIDUES 267-289, NMR, 5 STRUCTURES AT PH 6.0, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90|SOLUTION NMR||Homo sapiens|0|APOLIPOPROTEIN","1OR2|APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165|X-RAY DIFFRACTION|2.5|Homo sapiens|0|LIPID BINDING PROTEIN","1OR3|APOLIPOPROTEIN E3 (APOE3), TRIGONAL TRUNCATION MUTANT 165|X-RAY DIFFRACTION|1.73|Homo sapiens|0|LIPID BINDING PROTEIN","2KC3|NMR solution structure of complete receptor binding domain of human apolipoprotein E|SOLUTION NMR||Homo sapiens|0|LIPOPROTEIN","2KNY|Fusion construct of CR17 from LRP-1 and ApoE residues 130-149|SOLUTION NMR||Homo sapiens|0|METAL BINDING PROTEIN","2L7B|NMR Structure of full length apoE3|SOLUTION NMR||Homo sapiens|0|LIPID TRANSPORT","6IWB|Crystal structure of a computationally designed protein (LD3) in complex with BCL-2|X-RAY DIFFRACTION|2.5|Homo sapiens|0|APOPTOSIS","6NCN|Fragment-based Discovery of an apoE4 Stabilizer|X-RAY DIFFRACTION|1.82|Homo sapiens|0|LIPID TRANSPORT","6NCO|Fragment-based Discovery of an apoE4 Stabilizer|X-RAY DIFFRACTION|1.707|Homo sapiens|0|LIPID TRANSPORT","6V7M|Crystal structure of a proteolytically cleaved, amino terminal domain of apolipoprotein E3|X-RAY DIFFRACTION|2|Homo sapiens|0|LIPID TRANSPORT","7FCR|Crystal structure of the N-terminal domain of mutants of Human Apolipoprotein-E (ApoE)|X-RAY DIFFRACTION|1.4|Homo sapiens|0|LIPID TRANSPORT","7FCS|Crystal structure of the N-terminal domain of mutants of Human Apolipoprotein-E (ApoE)|X-RAY DIFFRACTION|1.6|Homo sapiens|0|LIPID TRANSPORT","7UVJ|Rationally Designed ED1 Epitope-Scaffold Immunogen for SARS-CoV-2|X-RAY DIFFRACTION|1.99|Escherichia coli|0|DE NOVO PROTEIN","8AX8|Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P3121)|X-RAY DIFFRACTION|1.551|Homo sapiens|0|LIPID BINDING PROTEIN","8AX9|Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P212121)|X-RAY DIFFRACTION|1.549|Homo sapiens|0|LIPID BINDING PROTEIN","8CDY|N-terminal domain of human apolipoprotein E|X-RAY DIFFRACTION|1.9|Escherichia coli; Homo sapiens|0|LIPID TRANSPORT","8CE0|N-terminal domain of human apolipoprotein E|X-RAY DIFFRACTION|1.75|Escherichia coli; Homo sapiens|0|LIPID TRANSPORT","8GRX|APOE4 receptor in complex with APOE4 NTD|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|IMMUNE SYSTEM"]}]}