5hgn

Hexameric HIV-1 CA, apo form

Method: X-RAY DIFFRACTION D_max: 82.4 Å Quality: REASONABLE

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Capsid protein P24

Human immunodeficiency virus 1

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 133–363	Mutation：C14A, C45E, A184W, A185M	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；PEG550MME (13-14%), KSCN (0.15M), TRIS (0.1M, pH 8.5)	Resolution 1.90 Å R-free 0.223

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 5HGN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GWP STRUCTURE OF THE N-TERMINAL DOMAIN OF THE MATURE HIV-1 CAPSID PROTEIN Deposited 2002-03-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 132–282（151 aa） Fragment：AMINO-TERMINAL CORE DOMAIN RESIDUES 132 - 282	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 10；Pressure 1	Resolution not provided
1HIW TRIMERIC HIV-1 MATRIX PROTEIN Deposited 1996-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–131（131 aa） Fragment：CORE PROTEIN P17, RESIDUES 1 - 131 OF GAG POLYPROTEIN WITH N-TERMINAL HIS AND MET Chain B 1–131（131 aa） Fragment：CORE PROTEIN P17, RESIDUES 1 - 131 OF GAG POLYPROTEIN WITH N-TERMINAL HIS AND MET Chain C 1–131（131 aa） Fragment：CORE PROTEIN P17, RESIDUES 1 - 131 OF GAG POLYPROTEIN WITH N-TERMINAL HIS AND MET	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.332
1HIW TRIMERIC HIV-1 MATRIX PROTEIN Deposited 1996-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain Q 1–131（131 aa） Fragment：CORE PROTEIN P17, RESIDUES 1 - 131 OF GAG POLYPROTEIN WITH N-TERMINAL HIS AND MET Chain R 1–131（131 aa） Fragment：CORE PROTEIN P17, RESIDUES 1 - 131 OF GAG POLYPROTEIN WITH N-TERMINAL HIS AND MET Chain S 1–131（131 aa） Fragment：CORE PROTEIN P17, RESIDUES 1 - 131 OF GAG POLYPROTEIN WITH N-TERMINAL HIS AND MET	Not recorded	SO4 SULFATE ION × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.332
1UPH HIV-1 Myristoylated Matrix Deposited 2003-10-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–131（131 aa） Fragment：RESIDUES 1-131	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 100MM NACL；Pressure 1	Resolution not provided
2C55 Solution Structure of the Human Immunodeficiency Virus Type 1 p6 Protein Deposited 2005-10-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 448–499（52 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；300 K；Pressure 1.0 NMR sample composition 50% WATER/50% TFE-D2	Resolution not provided
2X2D acetyl-CypA:HIV-1 N-term capsid domain complex Deposited 2010-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 133–278（146 aa） Fragment：RESIDUES 133-278	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.95 Å R-free 0.257
2X2D acetyl-CypA:HIV-1 N-term capsid domain complex Deposited 2010-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 133–278（146 aa） Fragment：RESIDUES 133-278	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.95 Å R-free 0.257
3GV2 X-ray Structure of Hexameric HIV-1 CA Deposited 2009-03-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–351（219 aa） Fragment：UNP residues 133-351 of Capsid protein p24, UNP residues 1-109 of CCMK Chain B 133–351（219 aa） Fragment：UNP residues 133-351 of Capsid protein p24, UNP residues 1-109 of CCMK Chain C 133–351（219 aa） Fragment：UNP residues 133-351 of Capsid protein p24, UNP residues 1-109 of CCMK Chain D 133–351（219 aa） Fragment：UNP residues 133-351 of Capsid protein p24, UNP residues 1-109 of CCMK Chain E 133–351（219 aa） Fragment：UNP residues 133-351 of Capsid protein p24, UNP residues 1-109 of CCMK Chain F 133–351（219 aa） Fragment：UNP residues 133-351 of Capsid protein p24, UNP residues 1-109 of CCMK	Mutation：W184A,M185A Mutation：W184A,M185A Mutation：W184A,M185A Mutation：W184A,M185A Mutation：W184A,M185A Mutation：W184A,M185A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M imidazole, pH 6.5, 600 mM sodium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 7.00 Å R-free 0.323
4U0A Hexameric HIV-1 CA in complex with CPSF6 peptide, P6 crystal form Deposited 2014-07-11	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: Dodecameric	Chain A 133–363（231 aa）	Mutation：A14C,E45C,W184A,M185A	CL CHLORIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.6M sodium potassium tartrate tetrahydrate, 0.1M TRIS	Resolution 2.05 Å R-free 0.253
4U0B Hexamer HIV-1 CA in complex with CPSF6 peptide, P212121 crystal form Deposited 2014-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: Dodecameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；20% v/v PEG 300, 10% v/v glycerol, 5% w/v PEG 8K, 0.1 M TRIS	Resolution 2.80 Å R-free 0.262
4U0B Hexamer HIV-1 CA in complex with CPSF6 peptide, P212121 crystal form Deposited 2014-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: Dodecameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；20% v/v PEG 300, 10% v/v glycerol, 5% w/v PEG 8K, 0.1 M TRIS	Resolution 2.80 Å R-free 0.262
4U0C Hexameric HIV-1 CA in complex with Nup153 peptide, P6 crystal form Deposited 2014-07-11	Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: Dodecameric	Chain A 133–363（231 aa）	Mutation：yes	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；290 K；30% v/v PEG 400, 0.1 M CHES	Resolution 1.77 Å R-free 0.211
4U0D Hexameric HIV-1 CA in complex with Nup153 peptide, P212121 crystal form Deposited 2014-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: Nonameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；290 K；10% w/v PEG 8K, 0.1M imidazole	Resolution 3.00 Å R-free 0.267
4U0D Hexameric HIV-1 CA in complex with Nup153 peptide, P212121 crystal form Deposited 2014-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: Nonameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes Mutation：yes	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；290 K；10% w/v PEG 8K, 0.1M imidazole	Resolution 3.00 Å R-free 0.267
4U0E Hexameric HIV-1 CA in complex with PF3450074 Deposited 2014-07-11	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: Hexameric	Chain A 133–363（231 aa）	Mutation：yes	CL CHLORIDE ION × 6 1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N-PHENYL-L-PHENYLALANINAMIDE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.2 M magnesium chloride, 8% w/v PEG 20K, 8% v/v PEG 550 MME, 0.1 M TRIS pH 8.5, 3% w/v 1,5-diaminopentane dihydrochloride	Resolution 2.04 Å R-free 0.239
4U0F Hexameric HIV-1 CA in Complex with BI-2 Deposited 2014-07-11	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: Hexameric	Chain A 133–363（231 aa）	Mutation：yes	EDO 1,2-ETHANEDIOL × 6 3A8 (4S)-4-(4-hydroxyphenyl)-3-phenyl-4,5-dihydropyrrolo[3,4-c]pyrazol-6(1H)-one × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；12% w/v PEG 4K, 0.1 M TRIS pH 8.5, 3% v/v ethylene glycol	Resolution 2.22 Å R-free 0.270
4XFX Structure of the native full-length HIV-1 capsid protein Deposited 2014-12-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	IOD IODIDE ION × 42 CL CHLORIDE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；PEG3350, NaI, MMT	Resolution 2.43 Å R-free 0.249
4XFY Structure of the native full-length dehydrated HIV-1 capsid protein Deposited 2014-12-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 12 1PE PENTAETHYLENE GLYCOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；PEG3350, NaI, Sodium cacodylate	Resolution 2.80 Å R-free 0.250
4XFZ Structure of the native full-length HIV-1 capsid protein in complex with PF-3450074 (PF74) Deposited 2014-12-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	IOD IODIDE ION × 36 CL CHLORIDE ION × 12 1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N-PHENYL-L-PHENYLALANINAMIDE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；PEG3350, NaI, Sodium cacodylate	Resolution 2.70 Å R-free 0.241
4XRO Disulfide stabilized HIV-1 CA hexamer 4mut (S41A, Q67H, V165I, L172I) Deposited 2015-01-21	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：A14C,S41A,E45C,Q67H,V165I,L172I,W184A,M185A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M NaCl, 12% w/v PEG 4K, 0.1 M TRIS pH 8.5, 4% v/v formamide	Resolution 2.01 Å R-free 0.226
4XRQ Disulfide stabilized HIV-1 CA hexamer 4mut (S41A, Q67H, V165I, L172I) in complex with PF-3450074 Deposited 2015-01-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：A14C,S41A,E45C,Q67H,V165I,L172I,W184A,M185A	1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N-PHENYL-L-PHENYLALANINAMIDE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.2 M potassium thiocyanate, 8% w/v PEG 20K, 8% v/v PEG 550 MME, 0.1 M TRIS pH 8.5, 3% 1,4-dioxane	Resolution 1.95 Å R-free 0.221
5HGL Hexameric HIV-1 CA, open conformation Deposited 2016-01-08	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Mutation：C14A, C45E, A184W, A185M Mutation：C14A, C45E, A184W, A185M Mutation：C14A, C45E, A184W, A185M Mutation：C14A, C45E, A184W, A185M Mutation：C14A, C45E, A184W, A185M Mutation：C14A, C45E, A184W, A185M	1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N-PHENYL-L-PHENYLALANINAMIDE × 6 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；PEG550MME (13-14%), KSCN (0.15M), TRIS (0.1M, pH 8.5)	Resolution 3.10 Å R-free 0.282
5HGM Hexameric HIV-1 CA in complex with dATP Deposited 2016-01-08	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：C14A, C45E, A184W, A185M	DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；PEG550MME (13-14%), KSCN (0.15M), TRIS (0.1M, pH 8.5), 10mM dATP	Resolution 2.04 Å R-free 0.263
5HGO Hexameric HIV-1 CA R18G mutant Deposited 2016-01-08	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：C14A, C45E, A184W, A185M, R18G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；PEG550MME (13-14%), KSCN (0.15M), TRIS (0.1M, pH 8.5)	Resolution 2.00 Å R-free 0.221
5HGP Hexameric HIV-1 CA in complex with hexacarboxybenzene Deposited 2016-01-08	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：C14A, C45E, A184W, A185M	BHC BENZENE HEXACARBOXYLIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；PEG550MME (13-14%), KSCN (0.15M), TRIS (0.1M, pH 8.5), Mellitic acid (1mM). Mellitic acid stock was adjusted to pH 8.0 with TRIS prior to setting up trays.	Resolution 1.95 Å R-free 0.221
5IRT Dimerization interface of the noncrystalline HIV-1 capsid protein lattice from solid state NMR spectroscopy of tubular assemblies Deposited 2016-03-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 133–363（231 aa） Chain B 133–363（231 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 8；278 K；Ionic strength (raw mmCIF value) 1；Pressure 1 NMR sample composition 15 mM U-15N,13C-Met and U-15N Capsid protein, water \| water NMR sample composition 15 mM 2-13C-glycerol and U-15N Capsid protein, water \| water NMR sample composition 15 mM 2-13C-glycerol, U-15N, unlabeled Tyr and Phe Capsid protein, water \| water NMR sample composition 7.5 mM Methyl-13C-Met Capsid protein-1, 7.5 mM 15N-indole Capsid protein-2, water \| water NMR sample composition 15 mM Methyl-13C-Met, 2-13C-indole, U-15N Capsid protein, water \| water	Resolution not provided
5JPA Hexameric HIV-1 CA H12Y mutant Deposited 2016-05-03	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：H12Y, A14C, E45C, W184A, M185A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；290 K；PEG 550MME (12% w/v), KSCN (0.15M), 0.1M TRIS	Resolution 1.70 Å R-free 0.232
5L93 An atomic model of HIV-1 CA-SP1 reveals structures regulating assembly and maturation Deposited 2016-06-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 148–371（224 aa） Chain B 148–371（224 aa） Chain C 148–371（224 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Virus-like particles were assembled in the presence of nucleic acid (73mer oligonucleotide, 1:10 molar ratio oligonucleotide:protein). cryo-EM vitrification conditions Cryogen ETHANE；10nM colloidal gold was added to the sample prior to plunge freezing.	Resolution 3.90 Å
5O2U Llama VHH in complex with p24 Deposited 2017-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–500（500 aa） Chain C 1–500（500 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Tris base pH 8.0, Polyethylene glycol (PEG) 6000 25% Ethylene Glycol	Resolution 2.76 Å R-free 0.256
5TSV HIV-1 CA hexamer with NUP153 peptide - R3 crystal form Deposited 2016-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa）	Not recorded	FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.1 M Tris, pH 8.2 12% PEG 8000 2% Tacsimate	Resolution 2.50 Å R-free 0.251
5TSX HIV-1 CA hexamer with NUP153 peptide - P1 crystal form Deposited 2016-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain K 133–363（231 aa）	Not recorded	FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.1 M Tris, pH 9 12% PEG 8000	Resolution 1.90 Å R-free 0.228
5TSX HIV-1 CA hexamer with NUP153 peptide - P1 crystal form Deposited 2016-10-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain F 133–363（231 aa） Chain G 133–363（231 aa） Chain J 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.1 M Tris, pH 9 12% PEG 8000	Resolution 1.90 Å R-free 0.228
5UPW CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations Deposited 2017-02-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–353（221 aa） Fragment：UNP residues 133-353 Chain B 133–353（221 aa） Fragment：UNP residues 133-353 Chain C 133–353（221 aa） Fragment：UNP residues 133-353 Chain D 133–353（221 aa） Fragment：UNP residues 133-353 Chain E 133–353（221 aa） Fragment：UNP residues 133-353 Chain F 133–353（221 aa） Fragment：UNP residues 133-353	Mutation：A92E Mutation：A92E Mutation：A92E Mutation：A92E Mutation：A92E Mutation：A92E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；The assembled sample (1.5 microliter) was applied to the carbon side of a glow discharged perforated Quantifoil grid, followed by application of 3 microliter of low salt buffer (100 milimolar NaCl, 50 milimolar Tris pH 8.0) on the back side of the grid, and blotting, from the back side, with a filter paper, before plunge-freezing in liquid ethane	Resolution 5.00 Å
6AYA Structure of the native full-length HIV-1 capsid protein in complex with Nup153 peptide Deposited 2017-09-07	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 133–363（231 aa）	Not recorded	IOD IODIDE ION × 42 CL CHLORIDE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；PEG3350, NaI, MIB, Glycerol	Resolution 2.40 Å R-free 0.274
6BHS HIV-1 CA hexamer in complex with IP6, hexagonal crystal form Deposited 2017-10-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Mutation：A146C, E177C, W316A, M317A	IHP INOSITOL HEXAKISPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；293 K；10% PEG 8,000, 2% Tacsimate, 0.1 M Tris	Resolution 1.98 Å R-free 0.284
6BHT HIV-1 CA hexamer in complex with IP6, orthorhombic crystal form Deposited 2017-10-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A	IHP INOSITOL HEXAKISPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.2；290 K；8% PEG 8000, 0.1M Tris	Resolution 2.69 Å R-free 0.255
6BHT HIV-1 CA hexamer in complex with IP6, orthorhombic crystal form Deposited 2017-10-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A Mutation：A146C, E177C, W316A, M317A	IHP INOSITOL HEXAKISPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.2；290 K；8% PEG 8000, 0.1M Tris	Resolution 2.69 Å R-free 0.255
6H09 HIV capsid hexamer with IP6 ligand Deposited 2018-07-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–351（219 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions BATCH MODE；293 K；PEG 4K	Resolution 2.00 Å R-free 0.266
6WAP Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR Deposited 2020-03-25	Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–363（231 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 6；277 K；Ionic strength (raw mmCIF value) 2.4；Pressure 1 NMR sample composition 100 % [U-13C; U-15N] HIV-1 capsid protein, solid \| solid NMR sample composition 100 % [1,6-13C]-Glucose,U-15N HIV-1 capsid protein, solid \| solid NMR sample composition 100 % [2-13C]-Glucose,U-15N HIV-1 capsid protein, solid \| solid NMR sample composition 100 % 13C,15N-His HIV-1 capsid protein, solid \| solid NMR sample composition 100 % 13C,15N-Tyr HIV-1 capsid protein, solid \| solid NMR sample composition 50 % 13C,15N-Ala HIV-1 capsid protein, 50 % 13C,15N-Ile HIV-1 capsid protein, solid \| solid NMR sample composition 50 % 13C,15N-Ala HIV-1 capsid protein, 50 % 13C,15N-Val HIV-1 capsid protein, solid \| solid NMR sample composition 86 % HIV-1 capsid protein, 14 % U-13C,15N-CA HIV-1 capsid protein, solid \| solid NMR sample composition 50 % [U-13C] HIV-1 capsid protein, 50 % [U-15N] HIV-1 capsid protein, solid \| solid	Resolution not provided
6X63 Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR Deposited 2020-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 378 PDB declaration: 378-meric	Chain 0 133–363（231 aa） Chain 0A 133–363（231 aa） Chain 0B 133–363（231 aa） Chain 0C 133–363（231 aa） Chain 0D 133–363（231 aa） Chain 0E 133–363（231 aa） Chain 1 133–363（231 aa） Chain 1A 133–363（231 aa） Chain 1B 133–363（231 aa） Chain 1C 133–363（231 aa） Chain 1D 133–363（231 aa） Chain 1E 133–363（231 aa） Chain 2 133–363（231 aa） Chain 2A 133–363（231 aa） Chain 2B 133–363（231 aa） Chain 2C 133–363（231 aa） Chain 2D 133–363（231 aa） Chain 2E 133–363（231 aa） Chain 3 133–363（231 aa） Chain 3A 133–363（231 aa） Chain 3B 133–363（231 aa） Chain 3C 133–363（231 aa） Chain 3D 133–363（231 aa） Chain 3E 133–363（231 aa） Chain 4 133–363（231 aa） Chain 4A 133–363（231 aa） Chain 4B 133–363（231 aa） Chain 4C 133–363（231 aa） Chain 4D 133–363（231 aa） Chain 4E 133–363（231 aa） Chain 5 133–363（231 aa） Chain 5A 133–363（231 aa） Chain 5B 133–363（231 aa） Chain 5C 133–363（231 aa） Chain 5D 133–363（231 aa） Chain 5E 133–363（231 aa） Chain 6 133–363（231 aa） Chain 6A 133–363（231 aa） Chain 6B 133–363（231 aa） Chain 6C 133–363（231 aa） Chain 6D 133–363（231 aa） Chain 6E 133–363（231 aa） Chain 7 133–363（231 aa） Chain 7A 133–363（231 aa） Chain 7B 133–363（231 aa） Chain 7C 133–363（231 aa） Chain 7D 133–363（231 aa） Chain 7E 133–363（231 aa） Chain 8 133–363（231 aa） Chain 8A 133–363（231 aa） Chain 8B 133–363（231 aa） Chain 8C 133–363（231 aa） Chain 8D 133–363（231 aa） Chain 8E 133–363（231 aa） Chain 9 133–363（231 aa） Chain 9A 133–363（231 aa） Chain 9B 133–363（231 aa） Chain 9C 133–363（231 aa） Chain 9D 133–363（231 aa） Chain 9E 133–363（231 aa） Chain A 133–363（231 aa） Chain AA 133–363（231 aa） Chain AB 133–363（231 aa） Chain AC 133–363（231 aa） Chain AD 133–363（231 aa） Chain AE 133–363（231 aa） Chain AF 133–363（231 aa） Chain B 133–363（231 aa） Chain BA 133–363（231 aa） Chain BB 133–363（231 aa） Chain BC 133–363（231 aa） Chain BD 133–363（231 aa） Chain BE 133–363（231 aa） Chain BF 133–363（231 aa） Chain C 133–363（231 aa） Chain CA 133–363（231 aa） Chain CB 133–363（231 aa） Chain CC 133–363（231 aa） Chain CD 133–363（231 aa） Chain CE 133–363（231 aa） Chain CF 133–363（231 aa） Chain D 133–363（231 aa） Chain DA 133–363（231 aa） Chain DB 133–363（231 aa） Chain DC 133–363（231 aa） Chain DD 133–363（231 aa） Chain DE 133–363（231 aa） Chain DF 133–363（231 aa） Chain E 133–363（231 aa） Chain EA 133–363（231 aa） Chain EB 133–363（231 aa） Chain EC 133–363（231 aa） Chain ED 133–363（231 aa） Chain EE 133–363（231 aa） Chain EF 133–363（231 aa） Chain F 133–363（231 aa） Chain FA 133–363（231 aa） Chain FB 133–363（231 aa） Chain FC 133–363（231 aa） Chain FD 133–363（231 aa） Chain FE 133–363（231 aa） Chain FF 133–363（231 aa） Chain G 133–363（231 aa） Chain GA 133–363（231 aa） Chain GB 133–363（231 aa） Chain GC 133–363（231 aa） Chain GD 133–363（231 aa） Chain GE 133–363（231 aa） Chain H 133–363（231 aa） Chain HA 133–363（231 aa） Chain HB 133–363（231 aa） Chain HC 133–363（231 aa） Chain HD 133–363（231 aa） Chain HE 133–363（231 aa） Chain I 133–363（231 aa） Chain IA 133–363（231 aa） Chain IB 133–363（231 aa） Chain IC 133–363（231 aa） Chain ID 133–363（231 aa） Chain IE 133–363（231 aa） Chain J 133–363（231 aa） Chain JA 133–363（231 aa） Chain JB 133–363（231 aa） Chain JC 133–363（231 aa） Chain JD 133–363（231 aa） Chain JE 133–363（231 aa） Chain K 133–363（231 aa） Chain KA 133–363（231 aa） Chain KB 133–363（231 aa） Chain KC 133–363（231 aa） Chain KD 133–363（231 aa） Chain KE 133–363（231 aa） Chain L 133–363（231 aa） Chain LA 133–363（231 aa） Chain LB 133–363（231 aa） Chain LC 133–363（231 aa） Chain LD 133–363（231 aa） Chain LE 133–363（231 aa） Chain M 133–363（231 aa） Chain MA 133–363（231 aa） Chain MB 133–363（231 aa） Chain MC 133–363（231 aa） Chain MD 133–363（231 aa） Chain ME 133–363（231 aa） Chain N 133–363（231 aa） Chain NA 133–363（231 aa） Chain NB 133–363（231 aa） Chain NC 133–363（231 aa） Chain ND 133–363（231 aa） Chain NE 133–363（231 aa） Chain O 133–363（231 aa） Chain OA 133–363（231 aa） Chain OB 133–363（231 aa） Chain OC 133–363（231 aa） Chain OD 133–363（231 aa） Chain OE 133–363（231 aa） Chain P 133–363（231 aa） Chain PA 133–363（231 aa） Chain PB 133–363（231 aa） Chain PC 133–363（231 aa） Chain PD 133–363（231 aa） Chain PE 133–363（231 aa） Chain Q 133–363（231 aa） Chain QA 133–363（231 aa） Chain QB 133–363（231 aa） Chain QC 133–363（231 aa） Chain QD 133–363（231 aa） Chain QE 133–363（231 aa） Chain R 133–363（231 aa） Chain RA 133–363（231 aa） Chain RB 133–363（231 aa） Chain RC 133–363（231 aa） Chain RD 133–363（231 aa） Chain RE 133–363（231 aa） Chain S 133–363（231 aa） Chain SA 133–363（231 aa） Chain SB 133–363（231 aa） Chain SC 133–363（231 aa） Chain SD 133–363（231 aa） Chain SE 133–363（231 aa） Chain T 133–363（231 aa） Chain TA 133–363（231 aa） Chain TB 133–363（231 aa） Chain TC 133–363（231 aa） Chain TD 133–363（231 aa） Chain TE 133–363（231 aa） Chain U 133–363（231 aa） Chain UA 133–363（231 aa） Chain UB 133–363（231 aa） Chain UC 133–363（231 aa） Chain UD 133–363（231 aa） Chain UE 133–363（231 aa） Chain V 133–363（231 aa） Chain VA 133–363（231 aa） Chain VB 133–363（231 aa） Chain VC 133–363（231 aa） Chain VD 133–363（231 aa） Chain VE 133–363（231 aa） Chain W 133–363（231 aa） Chain WA 133–363（231 aa） Chain WB 133–363（231 aa） Chain WC 133–363（231 aa） Chain WD 133–363（231 aa） Chain WE 133–363（231 aa） Chain X 133–363（231 aa） Chain XA 133–363（231 aa） Chain XB 133–363（231 aa） Chain XC 133–363（231 aa） Chain XD 133–363（231 aa） Chain XE 133–363（231 aa） Chain Y 133–363（231 aa） Chain YA 133–363（231 aa） Chain YB 133–363（231 aa） Chain YC 133–363（231 aa） Chain YD 133–363（231 aa） Chain YE 133–363（231 aa） Chain Z 133–363（231 aa） Chain ZA 133–363（231 aa） Chain ZB 133–363（231 aa） Chain ZC 133–363（231 aa） Chain ZD 133–363（231 aa） Chain ZE 133–363（231 aa） Chain a 133–363（231 aa） Chain aA 133–363（231 aa） Chain aB 133–363（231 aa） Chain aC 133–363（231 aa） Chain aD 133–363（231 aa） Chain aE 133–363（231 aa） Chain b 133–363（231 aa） Chain bA 133–363（231 aa） Chain bB 133–363（231 aa） Chain bC 133–363（231 aa） Chain bD 133–363（231 aa） Chain bE 133–363（231 aa） Chain c 133–363（231 aa） Chain cA 133–363（231 aa） Chain cB 133–363（231 aa） Chain cC 133–363（231 aa） Chain cD 133–363（231 aa） Chain cE 133–363（231 aa） Chain d 133–363（231 aa） Chain dA 133–363（231 aa） Chain dB 133–363（231 aa） Chain dC 133–363（231 aa） Chain dD 133–363（231 aa） Chain dE 133–363（231 aa） Chain e 133–363（231 aa） Chain eA 133–363（231 aa） Chain eB 133–363（231 aa） Chain eC 133–363（231 aa） Chain eD 133–363（231 aa） Chain eE 133–363（231 aa） Chain f 133–363（231 aa） Chain fA 133–363（231 aa） Chain fB 133–363（231 aa） Chain fC 133–363（231 aa） Chain fD 133–363（231 aa） Chain fE 133–363（231 aa） Chain g 133–363（231 aa） Chain gA 133–363（231 aa） Chain gB 133–363（231 aa） Chain gC 133–363（231 aa） Chain gD 133–363（231 aa） Chain gE 133–363（231 aa） Chain h 133–363（231 aa） Chain hA 133–363（231 aa） Chain hB 133–363（231 aa） Chain hC 133–363（231 aa） Chain hD 133–363（231 aa） Chain hE 133–363（231 aa） Chain i 133–363（231 aa） Chain iA 133–363（231 aa） Chain iB 133–363（231 aa） Chain iC 133–363（231 aa） Chain iD 133–363（231 aa） Chain iE 133–363（231 aa） Chain j 133–363（231 aa） Chain jA 133–363（231 aa） Chain jB 133–363（231 aa） Chain jC 133–363（231 aa） Chain jD 133–363（231 aa） Chain jE 133–363（231 aa） Chain k 133–363（231 aa） Chain kA 133–363（231 aa） Chain kB 133–363（231 aa） Chain kC 133–363（231 aa） Chain kD 133–363（231 aa） Chain kE 133–363（231 aa） Chain l 133–363（231 aa） Chain lA 133–363（231 aa） Chain lB 133–363（231 aa） Chain lC 133–363（231 aa） Chain lD 133–363（231 aa） Chain lE 133–363（231 aa） Chain m 133–363（231 aa） Chain mA 133–363（231 aa） Chain mB 133–363（231 aa） Chain mC 133–363（231 aa） Chain mD 133–363（231 aa） Chain mE 133–363（231 aa） Chain n 133–363（231 aa） Chain nA 133–363（231 aa） Chain nB 133–363（231 aa） Chain nC 133–363（231 aa） Chain nD 133–363（231 aa） Chain nE 133–363（231 aa） Chain o 133–363（231 aa） Chain oA 133–363（231 aa） Chain oB 133–363（231 aa） Chain oC 133–363（231 aa） Chain oD 133–363（231 aa） Chain oE 133–363（231 aa） Chain p 133–363（231 aa） Chain pA 133–363（231 aa） Chain pB 133–363（231 aa） Chain pC 133–363（231 aa） Chain pD 133–363（231 aa） Chain pE 133–363（231 aa） Chain q 133–363（231 aa） Chain qA 133–363（231 aa） Chain qB 133–363（231 aa） Chain qC 133–363（231 aa） Chain qD 133–363（231 aa） Chain qE 133–363（231 aa） Chain r 133–363（231 aa） Chain rA 133–363（231 aa） Chain rB 133–363（231 aa） Chain rC 133–363（231 aa） Chain rD 133–363（231 aa） Chain rE 133–363（231 aa） Chain s 133–363（231 aa） Chain sA 133–363（231 aa） Chain sB 133–363（231 aa） Chain sC 133–363（231 aa） Chain sD 133–363（231 aa） Chain sE 133–363（231 aa） Chain t 133–363（231 aa） Chain tA 133–363（231 aa） Chain tB 133–363（231 aa） Chain tC 133–363（231 aa） Chain tD 133–363（231 aa） Chain tE 133–363（231 aa） Chain u 133–363（231 aa） Chain uA 133–363（231 aa） Chain uB 133–363（231 aa） Chain uC 133–363（231 aa） Chain uD 133–363（231 aa） Chain uE 133–363（231 aa） Chain v 133–363（231 aa） Chain vA 133–363（231 aa） Chain vB 133–363（231 aa） Chain vC 133–363（231 aa） Chain vD 133–363（231 aa） Chain vE 133–363（231 aa） Chain w 133–363（231 aa） Chain wA 133–363（231 aa） Chain wB 133–363（231 aa） Chain wC 133–363（231 aa） Chain wD 133–363（231 aa） Chain wE 133–363（231 aa） Chain x 133–363（231 aa） Chain xA 133–363（231 aa） Chain xB 133–363（231 aa） Chain xC 133–363（231 aa） Chain xD 133–363（231 aa） Chain xE 133–363（231 aa） Chain y 133–363（231 aa） Chain yA 133–363（231 aa） Chain yB 133–363（231 aa） Chain yC 133–363（231 aa） Chain yD 133–363（231 aa） Chain yE 133–363（231 aa） Chain z 133–363（231 aa） Chain zA 133–363（231 aa） Chain zB 133–363（231 aa） Chain zC 133–363（231 aa） Chain zD 133–363（231 aa） Chain zE 133–363（231 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 6；277 K；Ionic strength (raw mmCIF value) 2.4；Pressure 1 NMR sample composition 100 % [U-13C; U-15N] HIV-1 capsid protein, solid \| solid NMR sample composition 100 % [1,6-13C]-Glucose,U-15N HIV-1 capsid protein, solid \| solid NMR sample composition 100 % [2-13C]-Glucose,U-15N HIV-1 capsid protein, solid \| solid NMR sample composition 100 % 13C,15N-His HIV-1 capsid protein, solid \| solid NMR sample composition 100 % 13C,15N-Tyr HIV-1 capsid protein, solid \| solid NMR sample composition 50 % 13C,15N-Ala HIV-1 capsid protein, 50 % 13C,15N-Ile HIV-1 capsid, solid \| solid NMR sample composition 50 % 13C,15N-Ala HIV-1 capsid protein, 50 % 13C,15N-Val HIV-1 capsid, solid \| solid NMR sample composition 86 % HIV-1 capsid protein, 14 % U-13C,15N-CA HIV-1 capsid, solid \| solid NMR sample composition 50 % [U-13C] HIV-1 capsid protein, 50 % [U-15N] HIV-1 capsid, solid \| solid	Resolution not provided
7M9F Structure of the wild-type native full-length HIV-1 capsid protein in complex with ZW-1261 Deposited 2021-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	YTG N-(4-chlorophenyl)-Nalpha-[(5-hydroxy-1H-indol-3-yl)acetyl]-N-methyl-L-phenylalaninamide × 6 IOD IODIDE ION × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；PEG 3350, NaI, Sodium Cacodylate, Glycerol	Resolution 2.70 Å R-free 0.253
7QDF Hexameric HIV-1 (M-group) CA R120 mutant Deposited 2021-11-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain AAA 133–363（231 aa）	Mutation：R120	IOD IODIDE ION × 12 CL CHLORIDE ION × 30 BME BETA-MERCAPTOETHANOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；9.5% PEG 3350 (v/v), 310 mM NaI, 100 mM Sodium Cacodylate. Crystals grew in 1 uL protein (3 mg/mL) + 1 uL crystallant. Cryoprotected in 20% (v/v) Glycerol.	Resolution 2.30 Å R-free 0.278
7RAO Structure of M66I mutant of disulfide stabilized HIV-1 CA hexamer Deposited 2021-07-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa）	Mutation：A14C, E45C, M66I, W184A, M185A Mutation：A14C, E45C, M66I, W184A, M185A	IOD IODIDE ION × 18 CL CHLORIDE ION × 21	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；0.125-0.35M Sodium Iodide, 2-8% Peg 3350, 6% glycerol, 0.1M sodium cacodylate pH 6.5	Resolution 2.29 Å R-free 0.244
7RAO Structure of M66I mutant of disulfide stabilized HIV-1 CA hexamer Deposited 2021-07-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain C 133–363（231 aa）	Mutation：A14C, E45C, M66I, W184A, M185A	IOD IODIDE ION × 24 CL CHLORIDE ION × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；0.125-0.35M Sodium Iodide, 2-8% Peg 3350, 6% glycerol, 0.1M sodium cacodylate pH 6.5	Resolution 2.29 Å R-free 0.244
7RAR Structure of Q67H mutant of disulfide stabilized HIV-1 CA hexamer Deposited 2021-07-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain C 133–363（231 aa）	Mutation：A14C, E45C, Q67H, W184A, M185A	IOD IODIDE ION × 36 CL CHLORIDE ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；0.425M NaI, 4% peg 3350, 6% glycerol, 0.1M sodium cacodylate trihydrate pH 6.5	Resolution 2.15 Å R-free 0.240
7RHN Co-crystal structure of Q67H mutant of disulfide stabilized HIV-1 CA hexamer and lenacapavir Deposited 2021-07-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain C 133–363（231 aa）	Mutation：A14C, E45C, Q67H, W184A, M185A	QNG Lenacapavir × 6 IOD IODIDE ION × 18 CL CHLORIDE ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；0.35M NaI, 4% peg 3350, 6% glycerol, 0.1M sodium cacodylate trihydrate pH 6.5	Resolution 2.46 Å R-free 0.288
7URN Structure of HIV-1 capsid declination Deposited 2022-04-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric	Chain A 133–363（231 aa） Chain L 133–363（231 aa） Chain M 133–363（231 aa） Chain N 133–363（231 aa） Chain O 133–363（231 aa） Chain P 133–363（231 aa） Chain Q 133–363（231 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE；Manual plunge-freezing	Resolution 3.43 Å
8EJL Structure of HIV-1 capsid declination in complex with CPSF6-FG peptide Deposited 2022-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain A 133–363（231 aa） Chain L 133–363（231 aa） Chain M 133–363（231 aa） Chain N 133–363（231 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE；Manual plunge-freezing	Resolution 3.90 Å
8EJL Structure of HIV-1 capsid declination in complex with CPSF6-FG peptide Deposited 2022-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa） Chain L 133–363（231 aa） Chain M 133–363（231 aa） Chain N 133–363（231 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE；Manual plunge-freezing	Resolution 3.90 Å
8EJL Structure of HIV-1 capsid declination in complex with CPSF6-FG peptide Deposited 2022-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa） Chain L 133–363（231 aa） Chain M 133–363（231 aa） Chain N 133–363（231 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE；Manual plunge-freezing	Resolution 3.90 Å
8QUB Hexameric HIV-1 CA in complex with DDD00074110 Deposited 2023-10-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	WVZ (1~{S})-1-phenyl-2,4-dihydro-1~{H}-isoquinolin-3-one × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.63 Å R-free 0.210
8QUH Hexameric HIV-1 CA in complex with DDD00057456 Deposited 2023-10-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	AJ2 4-methylquinolin-2-ol × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.55 Å R-free 0.195
8QUI Hexameric HIV-1 CA in complex with DDD00024969 Deposited 2023-10-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	XXL ethyl (3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)acetate × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.69 Å R-free 0.216
8QUJ Hexameric HIV-1 CA in complex with DDD00100452 Deposited 2023-10-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 24 WWR 3-(phenylmethyl)-1~{H}-imidazol-2-one × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.63 Å R-free 0.200
8QUK Hexameric HIV-1 CA in complex with DDD00100439 Deposited 2023-10-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 12 WVU (phenylmethyl) 3-oxidanylidenepiperazine-1-carboxylate × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.38 Å R-free 0.203
8QUL Hexameric HIV-1 CA in complex with DDD00100555 Deposited 2023-10-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	3IP 3-(BENZYLOXY)PYRIDIN-2-AMINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.67 Å R-free 0.210
8QUW Hexameric HIV-1 CA in complex with DDD01044153 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	WZR (4~{R})-7-oxidanyl-4-phenyl-3,4-dihydro-1~{H}-quinolin-2-one × 6 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 2.02 Å R-free 0.230
8QUX Hexameric HIV-1 CA in complex with DDD00100333 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 12 S0I 4-benzyl-3,4-dihydroquinoxalin-2(1H)-one × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 2.30 Å R-free 0.276
8QUY Hexameric HIV-1 CA in complex with DDD01728501 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	X0L 4-[(4-methylphenyl)methyl]-1~{H}-quinoxaline-2,3-dione × 6 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.88 Å R-free 0.215
8QV1 Hexameric HIV-1 CA in complex with DDD01728505 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	X0H methyl 2-(2-oxidanylidene-1~{H}-quinolin-4-yl)ethanoate × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 2.20 Å R-free 0.288
8QV4 Hexameric HIV-1 CA in complex with DDD01728503 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 12 WZX ethyl 2-(3-oxidanylidene-2,4-dihydroquinoxalin-1-yl)ethanoate × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 2.70 Å R-free 0.303
8QV9 Hexameric HIV-1 CA in complex with DDD01829021 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	WZL 7-bromanyl-3-(phenylmethyl)-1~{H}-benzimidazol-2-one × 6 EDO 1,2-ETHANEDIOL × 18	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 1.76 Å R-free 0.246
8QVA Hexameric HIV-1 CA in complex with DDD01829894 Deposited 2023-10-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 12 WZ9 7-azanyl-3-(phenylmethyl)-1~{H}-benzimidazol-2-one × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1M Tris buffer, pH 8.0 to 9.0, 10-15% PEG550MME, 0.15M KSCN	Resolution 2.00 Å R-free 0.254
8TY6 Disulfide-stabilized HIV-1 CA hexamer in complex with PQBP1 Nt Deposited 2023-08-24	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Mutation：A14C, E45C, W184A, M185A Mutation：A14C, E45C, W184A, M185A Mutation：A14C, E45C, W184A, M185A Mutation：A14C, E45C, W184A, M185A Mutation：A14C, E45C, W184A, M185A Mutation：A14C, E45C, W184A, M185A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8V17 HIV-CA Disulfide linked Hexamer with inhibitor bound - exploration of a benzothiazole Deposited 2023-11-19	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–361（229 aa）	Mutation：A14C, E45C, W184A, M185A	Y4X N-(1,3-benzothiazol-5-yl)-3,5-difluoro-Nalpha-[(5-hydroxy-1H-indol-3-yl)acetyl]-N-methyl-L-phenylalaninamide × 6 GOL GLYCEROL × 18	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；Morpheus Condition D11	Resolution 1.50 Å R-free 0.171
8VRP HIV-CA Disulfide linked Hexamer bound to 4-Quinazolinone Scaffold inhibitor Deposited 2024-01-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 133–361（229 aa） Chain C 133–361（229 aa）	Mutation：A14C, E45C, W184A, M185A Mutation：A14C, E45C, W184A, M185A	A1ADQ N-[(1S)-1-[(3P,7M)-3-{4-chloro-3-[(ethanesulfonyl)amino]-1-(2,2,2-trifluoroethyl)-1H-indazol-7-yl}-7-(3-fluoro-4-formylphenyl)-4-oxo-3,4-dihydroquinazolin-2-yl]-2-(3,5-difluorophenyl)ethyl]-2-[3-(trifluoromethyl)-5,6-dihydrocyclopenta[c]pyrazol-1(4H)-yl]acetamide × 6 IOD IODIDE ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；Morpheus condition B2	Resolution 1.80 Å R-free 0.226
8VRP HIV-CA Disulfide linked Hexamer bound to 4-Quinazolinone Scaffold inhibitor Deposited 2024-01-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 133–361（229 aa）	Mutation：A14C, E45C, W184A, M185A	A1ADQ N-[(1S)-1-[(3P,7M)-3-{4-chloro-3-[(ethanesulfonyl)amino]-1-(2,2,2-trifluoroethyl)-1H-indazol-7-yl}-7-(3-fluoro-4-formylphenyl)-4-oxo-3,4-dihydroquinazolin-2-yl]-2-(3,5-difluorophenyl)ethyl]-2-[3-(trifluoromethyl)-5,6-dihydrocyclopenta[c]pyrazol-1(4H)-yl]acetamide × 6 IOD IODIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；Morpheus condition B2	Resolution 1.80 Å R-free 0.226
9D6D Gag CA-SP1 immature lattice bound with Lenacapavir from enveloped virus like particles Deposited 2024-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain B 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain C 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain D 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain E 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain F 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain G 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain H 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain I 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain J 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain K 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain L 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain M 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain N 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain O 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain P 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain Q 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain R 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372)	Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I	QNG Lenacapavir × 18 IHP INOSITOL HEXAKISPHOSPHATE × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；This is the final buffer in which the enveloped viral like particle was resuspended. The Gag-CA-SP1 lattice is inside the viral like particle and thus not in the direct environment of this buffer. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.18 Å
9D6E Gag CA-SP1 immature lattice bound with Bevirimat from enveloped virus like particles Deposited 2024-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain B 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain C 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain D 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain E 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain F 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain G 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain H 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain I 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain J 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain K 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain L 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain M 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain N 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain O 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain P 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain Q 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain R 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372)	Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I	IHP INOSITOL HEXAKISPHOSPHATE × 1 2I4 3alpha-[(3-carboxy-3-methylbutanoyl)oxy]-8alpha,9beta,10alpha,13alpha,17alpha,19beta-lup-20(29)-en-28-oic acid × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；This is the final buffer in which the enveloped viral like particle was resuspended. The Gag-CA-SP1 lattice is inside the viral like particle and thus not in the direct environment of this buffer. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
9D88 Gag CA-SP1 immature lattice from enveloped and perforated virus like particles Deposited 2024-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain B 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain C 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain D 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain E 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain F 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain G 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain H 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain I 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain J 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain K 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain L 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain M 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain N 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain O 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain P 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain Q 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372) Chain R 143–371（229 aa） Fragment：CA-SP1 domains (UNP residues 143-372)	Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I Mutation：L231I	IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；This is the final buffer in which the enveloped viral-like particle was resuspended. The Gag-CA-SP1 lattice is inside the virus-like particle and not directly in the buffer environment. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
9EDZ HIV CA - GLFG peptide (4 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4 10% PEG 4,000	Resolution 3.00 Å R-free 0.267
9EDZ HIV CA - GLFG peptide (4 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4 10% PEG 4,000	Resolution 3.00 Å R-free 0.267
9EE0 HIV CA - GLFG peptide (9 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4 10% PEG 4,000	Resolution 3.10 Å R-free 0.255
9EE0 HIV CA - GLFG peptide (9 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4 10% PEG 4,000	Resolution 3.10 Å R-free 0.255
9EE1 HIV CA - GLFG peptide (43 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 3.00 Å R-free 0.261
9EE1 HIV CA - GLFG peptide (43 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 3.00 Å R-free 0.261
9EE2 HIV CA - FSFG peptide (14 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 2.99 Å R-free 0.253
9EE2 HIV CA - FSFG peptide (14 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 2.99 Å R-free 0.253
9EE3 HIV CA - FG peptide (14 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 3.10 Å R-free 0.261
9EE3 HIV CA - FG peptide (14 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 3.10 Å R-free 0.261
9EE4 HIV CA - FG peptide (34 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa） Chain E 133–363（231 aa） Chain F 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 3.10 Å R-free 0.252
9EE4 HIV CA - FG peptide (34 mM) Deposited 2024-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric	Chain G 133–363（231 aa） Chain H 133–363（231 aa） Chain I 133–363（231 aa） Chain J 133–363（231 aa） Chain K 133–363（231 aa） Chain L 133–363（231 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100 mM Hepes, pH 7.4, 10% PEG 4,000	Resolution 3.10 Å R-free 0.252
9H1P Mature HIV-1 matrix from MA-SP1 cleavage mutant Deposited 2024-10-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 2–132（131 aa） Chain B 433–448（16 aa） Chain C 2–132（131 aa） Chain D 433–448（16 aa） Chain E 2–132（131 aa） Chain F 433–448（16 aa） Chain G 2–132（131 aa） Chain H 433–448（16 aa） Chain I 2–132（131 aa） Chain J 433–448（16 aa） Chain K 2–132（131 aa） Chain L 433–448（16 aa） Chain M 2–132（131 aa） Chain N 433–448（16 aa） Chain O 2–132（131 aa） Chain P 433–448（16 aa） Chain Q 2–132（131 aa） Chain R 433–448（16 aa） Chain S 2–132（131 aa） Chain T 433–448（16 aa） Chain U 2–132（131 aa） Chain V 433–448（16 aa） Chain W 2–132（131 aa） Chain X 433–448（16 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å
9MNM SPA of purified HIV-1 CA protein in vitro assembled with IP6 (mature morphology). 500 uM LEN was added post assembly. Deposited 2024-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa）	Not recorded	QNG Lenacapavir × 18 IHP INOSITOL HEXAKISPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2；25 mM MES, 2mM TCEP, 500 uM LEN cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9MNM SPA of purified HIV-1 CA protein in vitro assembled with IP6 (mature morphology). 500 uM LEN was added post assembly. Deposited 2024-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa）	Not recorded	QNG Lenacapavir × 3 IHP INOSITOL HEXAKISPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2；25 mM MES, 2mM TCEP, 500 uM LEN cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9MNM SPA of purified HIV-1 CA protein in vitro assembled with IP6 (mature morphology). 500 uM LEN was added post assembly. Deposited 2024-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 133–363（231 aa） Chain B 133–363（231 aa） Chain C 133–363（231 aa） Chain D 133–363（231 aa）	Not recorded	QNG Lenacapavir × 3 IHP INOSITOL HEXAKISPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2；25 mM MES, 2mM TCEP, 500 uM LEN cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9P9L Gag CA-SP1 immature lattice bound with Lenacapavir from enveloped virus like particles Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric	Chain A 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain B 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain C 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain D 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain E 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain F 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain G 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain H 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain I 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain J 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain K 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain L 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain M 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain N 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain O 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain P 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain Q 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain R 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region	Not recorded	QNG Lenacapavir × 18 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；This is the final buffer in which the enveloped viral like particle was resuspended. The Gag-CA-SP1 lattice is inside the viral like particle and thus not in the direct environment of this buffer. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.28 Å
9P9M CA-SP1 immature lattice assembled in vitro with inhibitor lenacapavir (dialyzed to 50nM) Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric	Chain A 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain B 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain C 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain D 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain E 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain F 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain G 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain H 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain I 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain J 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain K 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain L 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain M 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain N 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain O 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain P 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain Q 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region Chain R 143–371（229 aa） Fragment：Capsid (CA) domain and Spacer Peptide 1 (SP1) region	Not recorded	QNG Lenacapavir × 18 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；the initial Lenacapavir concentration is 180uM and CA-SP1 is 90uM upon particle assembly; the assembled particle is then dialyzed in same buffer, but have final Lenacapavir concentration drop to 50nM. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å

70 other PDB entries and 88 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GAG_HV1N5
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–231； UniProt 133–363

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	5hgn
Deposition date deposition_date	2016-01-08
Structure title title	Hexameric HIV-1 CA, apo form
Keywords keywords	Capsid, Viral Protein; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	23.25 Å
Radius of gyration Rg (electron density) rg_electron	22.53 Å
Forward intensity I(0) i0	9412560.00
Molecular weight molecular_weight	22570.0 kDa
Excluded volume excluded_volume	28154 Å³
Envelope volume envelope_volume	36821 Å³
Hydration-shell volume shell_volume	15082 Å³
Envelope diameter envelope_diameter	82.8 Å
Shell Rg shell_rg	27.25 Å
Envelope Rg envelope_rg	22.76 Å
Shape Rg shape_rg	22.54 Å
Total Rg total_rg	23.22 Å
Total atoms total_atoms	1580
Residues n_residues	205
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	82.4 Å
Rg (real space) rg_real	23.47 Å
Rg uncertainty (real space) rg_real_error	0.79 Å
I(0) (real space) i0_real	9.4130e+06
I(0) uncertainty (real space) i0_real_error	1.2350e+05
Rg (reciprocal space) rg_reciprocal	23.43 Å
I(0) (reciprocal space) i0_reciprocal	9412000.0000
Solution quality estimate total_estimate	0.7240
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.0 Å
Skewness Skewness skewness	0.454
Kurtosis Kurtosis kurtosis	-0.551
Angular range angular_range	— – 0.3400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1530000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.644; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.478; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d5hgna1
Class class	a — All alpha proteins
Fold Fold fold	a.73 — Retrovirus capsid protein, N-terminal core domain
Superfamily Superfamily superfamily	a.73.1 — Retrovirus capsid protein, N-terminal core domain
Family Family family	a.73.1.1 — Retrovirus capsid protein, N-terminal core domain

Domain ID domain_id	d5hgna2
Class class	a — All alpha proteins
Fold Fold fold	a.28 — Acyl carrier protein-like
Superfamily Superfamily superfamily	a.28.3 — Retrovirus capsid dimerization domain-like
Family Family family	a.28.3.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	5hgnA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	375 — Human Immunodeficiency Virus Type 1 Capsid Protein
Homologous superfamily homologous superfamily	10 — Human Immunodeficiency Virus Type 1 Capsid Protein

Domain ID domain_id	5hgnA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1200 — Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A
Homologous superfamily homologous superfamily	30 — Retrovirus capsid C-terminal domain

▶

8. Citations (1)

▶

Unit-cell length a length_a	90.730 Å
Unit-cell length b length_b	90.730 Å
Unit-cell length c length_c	56.751 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 6
Space-group number int_tables_number	168
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	26.690 Å
R factor r_factor	0.2013
R_work r_work	0.2002
R_free r_free	0.2230

Description description	Capsid protein P24
Molecular weight formula_weight	25461.3 kDa
Mutation mutation	C14A, C45E, A184W, A185M
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1747

Hexameric HIV-1 CA, apo form

1. Protein Identity and Related Structures Protein Identity & Related Structures

Capsid protein P24

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Human immunodeficiency virus 1
通用名 common_name	HIV-1
NCBI Class编号 ncbi_taxonomy_id	11676
宿主生物 host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	124

fit	/app/data/saxs_computation/hg/5hgn/5hgn.fit
pddf	/app/data/pr_computation/hg/5hgn/5hgn.pr.out
profile	/app/data/saxs_computation/hg/5hgn/5hgn.dat