3g26

Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Mutant A184C

Method: X-RAY DIFFRACTION D_max: 42.3 Å Quality: GOOD

▼

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

Gag polyprotein

Rous sarcoma virus

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 389–465	Fragment：C-terminal domain, UNP residues 389-465 Mutation：A184C	MLA MALONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 3.7；291 K；0.1M Malic acid/KOH, pH3.7, 1.4 M Malonic acid/KOH, pH3.7, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.55 Å R-free 0.214

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 3G26	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A6S M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 STRUCTURES Deposited 1998-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–87（86 aa） Fragment：M-DOMAIN	Mutation：M1G	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；308 K；Ionic strength (raw mmCIF value) 100 mM；Pressure 1 NMR sample composition H20	Resolution not provided
1EM9 ROUS SARCOMA VIRUS CAPSID PROTEIN: N-TERMINAL DOMAIN Deposited 2000-03-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 240–393（154 aa） Fragment：N-TERMINAL DOMAIN	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 9.1；277 K；Boric acid/Potassium Hydroxide, PEG 6000, Magnesium Nitrate, pH 9.1, VAPOR DIFFUSION, temperature 277K	Resolution 2.05 Å R-free 0.271
1EM9 ROUS SARCOMA VIRUS CAPSID PROTEIN: N-TERMINAL DOMAIN Deposited 2000-03-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 240–393（154 aa） Fragment：N-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 9.1；277 K；Boric acid/Potassium Hydroxide, PEG 6000, Magnesium Nitrate, pH 9.1, VAPOR DIFFUSION, temperature 277K	Resolution 2.05 Å R-free 0.271
1EOQ ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN Deposited 2000-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 394–488（95 aa） Fragment：C-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.9；298 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure ambient NMR measurement conditions pH 4.9；298 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure ambient NMR measurement conditions pH 4.9；298 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure ambient NMR sample composition U-15N RSV CA(155-249) (used for the 3D_15N-SEPARATED_NOESY, HNHA, HNHB expts) and U-15N/U-13C RSV CA(155-249) (used for the 3D_13C-SEPARATED_NOESY expt) both suspended in the same buffer (50 mM Sodium phosphate pH 4.9 50 mM NaCl 1 mM EDTA 1 mM DTT) \| 90% H20, 10%D20 NMR sample composition U-15N RSV CA(155-249) 50 mM Sodium phosphate pH 4.9 50 mM NaCl 1 mM EDTA 1 mM DTT \| 90% H20, 10%D20 NMR sample composition U-15N,13C RSV CA(155-249) 50 mM Sodium phosphate pH 4.9 50 mM NaCl 1 mM EDTA 1 mM DTT \| 90% H20, 10%D20	Resolution not provided
1P7N Dimeric Rous Sarcoma virus Capsid protein structure with an upstream 25-amino acid residue extension of C-terminal of Gag p10 protein Deposited 2003-05-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 215–386（172 aa） Fragment：N-terminal domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；10 mM HEPES-sodium buffer and 0.8M potassium sodium tartrate tetrahydrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.60 Å R-free 0.298
2IHX Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:uPsi RNA Packaging Signal Complex Deposited 2006-09-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 503–563（61 aa） Fragment：Nucleocapsid domain (residues 503-563)	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7；308 K；Ionic strength (raw mmCIF value) 5 mM NaCl, 0.1 mM ZnCl2；Pressure ambient NMR sample composition 1.0 mM unlabeled nucleocapsid protein, 1.0 mM A-selectively-protonated uPsi RNA, 5 mM Tris-d11-HCl buffer, pH 7.0, 5mM NaCl, 0.1 mM ZnCl2, 100% D2O \| 100% D2O NMR sample composition 1.2 mM unlabeled nucleocapsid protein, 1.2 mM G-selectively-protonated uPsi RNA, 5 mM Tris-d11-HCl buffer, pH 7.0, 5mM NaCl, 0.1 mM ZnCl2, 100% D2O \| 100% D2O NMR sample composition 0.8 mM unlabeled nucleocapsid protein, 0.8 mM U-selectively-protonated uPsi RNA, 5 mM Tris-d11-HCl buffer, pH 7.0, 5mM NaCl, 0.1 mM ZnCl2, 100% D2O \| 100% D2O NMR sample composition 0.8 mM unlabeled nucleocapsid protein, 0.8 mM C-selectively-protonated uPsi RNA, 5 mM Tris-d11-HCl buffer, pH 7.0, 5mM NaCl, 0.1 mM ZnCl2, 100% D2O \| 100% D2O NMR sample composition 1.2 mM unlabeled nucleocapsid protein, 1.2 mM unlabeled uPsi RNA, 5 mM Tris-d11-HCl buffer, pH 7.0, 5mM NaCl, 0.1 mM ZnCl2, 100% D2O \| 100% D2O NMR sample composition 1.2 mM 15N, 13C-labeled nucleocapsid protein, 1.2 mM unlabeled uPsi RNA, 5 mM Tris-d11-HCl buffer, pH 7.0; 5mM NaCl, 0.1 mM ZnCl2, 100% D2O \| 100% D2O	Resolution not provided
2RSP STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION Deposited 1989-10-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 578–701（124 aa） Chain B 578–701（124 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
2X8Q Cryo-EM 3D model of the icosahedral particle composed of Rous sarcoma virus capsid protein pentamers Deposited 2010-03-11	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 × 60 PDB declaration: 60-MERIC	Chain A 240–465（226 aa） Fragment：RESIDUES 240-465	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL；pH 5；0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 85, INSTRUMENT- VITROBOT MARK IV, METHOD- BLOT FOR 5 SECONDS BEFORE PLUNGING,	Resolution 18.30 Å
2X8Q Cryo-EM 3D model of the icosahedral particle composed of Rous sarcoma virus capsid protein pentamers Deposited 2010-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 240–465（226 aa） Fragment：RESIDUES 240-465	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL；pH 5；0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 85, INSTRUMENT- VITROBOT MARK IV, METHOD- BLOT FOR 5 SECONDS BEFORE PLUNGING,	Resolution 18.30 Å
2X8Q Cryo-EM 3D model of the icosahedral particle composed of Rous sarcoma virus capsid protein pentamers Deposited 2010-03-11	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 × 5 PDB declaration: pentameric	Chain A 240–465（226 aa） Fragment：RESIDUES 240-465	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL；pH 5；0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 85, INSTRUMENT- VITROBOT MARK IV, METHOD- BLOT FOR 5 SECONDS BEFORE PLUNGING,	Resolution 18.30 Å
2X8Q Cryo-EM 3D model of the icosahedral particle composed of Rous sarcoma virus capsid protein pentamers Deposited 2010-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 240–465（226 aa） Fragment：RESIDUES 240-465	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL；pH 5；0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 85, INSTRUMENT- VITROBOT MARK IV, METHOD- BLOT FOR 5 SECONDS BEFORE PLUNGING,	Resolution 18.30 Å
2X8Q Cryo-EM 3D model of the icosahedral particle composed of Rous sarcoma virus capsid protein pentamers Deposited 2010-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 240–465（226 aa） Fragment：RESIDUES 240-465	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL；pH 5；0.1M CITRIC ACID, 5MM MOPS/KOH, 725MM NACL, 0.25MM NA AZIDE, 0.125MM TCEP-HCL cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 85, INSTRUMENT- VITROBOT MARK IV, METHOD- BLOT FOR 5 SECONDS BEFORE PLUNGING,	Resolution 18.30 Å
3G0V Crystal structure of the C-terminal domain from the Rous Sarcoma Virus capsid protein: mutant D179A Deposited 2009-01-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465	Mutation：D179A	NO3 NITRATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.3；291 K；0.2M Succinic acid/KOH, pH4.3, 24% PEG8000, 1M Sodium Nitrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.00 Å R-free 0.228
3G1G Crystal structure of the C-terminal domain from the Rous Sarcoma Virus capsid protein: High pH Deposited 2009-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 390–476（87 aa） Fragment：C-terminal domain, UNP residues 390-476 Chain B 390–476（87 aa） Fragment：C-terminal domain, UNP residues 390-476	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 10.3；291 K；0.2M Beta-Alanine/KOH, pH10.3, 10-25% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.01 Å R-free 0.257
3G1G Crystal structure of the C-terminal domain from the Rous Sarcoma Virus capsid protein: High pH Deposited 2009-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 390–476（87 aa） Fragment：C-terminal domain, UNP residues 390-476 Chain B 390–476（87 aa） Fragment：C-terminal domain, UNP residues 390-476	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 10.3；291 K；0.2M Beta-Alanine/KOH, pH10.3, 10-25% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.01 Å R-free 0.257
3G1I Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Intermediate pH Deposited 2009-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465 Chain B 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；0.2M Bis-tris propane/HCl, pH8.5, 0.75-1.85M Ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.10 Å R-free 0.245
3G21 Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Low pH Deposited 2009-01-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465	Not recorded	NO3 NITRATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.3；291 K；0.20M Succinic acid/KOH, pH4.3, 13-18% PEG8000, 0.75M Magnesium Nitrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 0.90 Å R-free 0.142
3G28 Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: mutant D179N, low pH Deposited 2009-01-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465	Mutation：D179N	NO3 NITRATE ION × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 3.7；291 K；0.2M Formic acid/KOH, pH3.7, 12% PEG8000, 0.25M Ammonium Nitrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.64 Å R-free 0.200
3G29 Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: D179N mutant, neutral pH Deposited 2009-01-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465	Mutation：D179N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.9；291 K；0.20M Tris/HCl, pH7.9, 1.5M Ammonium Citrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.50 Å R-free 0.322
3G29 Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: D179N mutant, neutral pH Deposited 2009-01-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 389–465（77 aa） Fragment：C-terminal domain, UNP residues 389-465	Mutation：D179N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.9；291 K；0.20M Tris/HCl, pH7.9, 1.5M Ammonium Citrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.50 Å R-free 0.322
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	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 × 6 PDB declaration: hexameric	Chain A 84–577（494 aa） Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain F 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	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 × 6 PDB declaration: hexameric	Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain K 84–577（494 aa） Chain R 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	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 × 6 PDB declaration: hexameric	Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain L 84–577（494 aa） Chain M 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain G 84–577（494 aa） Chain N 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain H 84–577（494 aa） Chain O 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain I 84–577（494 aa） Chain P 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
5A9E Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles Deposited 2015-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain B 84–577（494 aa） Chain C 84–577（494 aa） Chain D 84–577（494 aa） Chain E 84–577（494 aa） Chain J 84–577（494 aa） Chain Q 84–577（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP；pH 6.5；MES PH6.5, 100MM NACL, 2UM ZNCL2, 2MM TCEP cryo-EM vitrification conditions Cryogen ETHANE；DEGASSED C-FLAT 2 2-3C GRIDS WERE GLOW DISCHARGED FOR 30 SECONDS AT 20 MA. VIRUS SOLUTION WAS DILUTED IN OBS CONTAINING 10NM COLLOIDAL GOLD. 2.5UL OF THIS MIXTURE WAS APPLIED TO A GRID. BLOTTING TIME 2.5 SECONDS.	Resolution 7.70 Å
7NO0 Structure of the mature RSV CA lattice: T=1 CA icosahedron Deposited 2021-02-25	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 × 60 PDB declaration: 60-meric	Chain A 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot time= 2.5 s blot force= 0	Resolution 3.10 Å
7NO1 Structure of the mature RSV CA lattice: T=3 CA icosahedron Deposited 2021-02-25	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 × 180 PDB declaration: 180-meric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot time = 2.5s blot force = 0	Resolution 7.60 Å
7NO2 Structure of the mature RSV CA lattice: hexamer derived from tubes (C2-symmetric) Deposited 2021-02-25	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 × 6 PDB declaration: hexameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 4.30 Å
7NO3 Structure of the mature RSV CA lattice: pentamer derived from polyhedral VLPs Deposited 2021-02-25	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 × 5 PDB declaration: pentameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 5.80 Å
7NO4 Structure of the mature RSV CA lattice: hexamer with 3 adjacent pentamers (C3 symmetric) Deposited 2021-02-25	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 × 6 PDB declaration: hexameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.50 Å
7NO5 Structure of the mature RSV CA lattice: hexamer with 2 adjacent pentamers (C2 symmetric) Deposited 2021-02-25	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 × 6 PDB declaration: hexameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.40 Å
7NO6 Structure of the mature RSV CA lattice: Group I, pentamer-hexamer interface, class 1 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.00 Å
7NO7 Structure of the mature RSV CA lattice: Group I, pentamer-hexamer interface, class 1"2 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.50 Å
7NO8 Structure of the mature RSV CA lattice: Group I, pentamer-hexamer interface, class 1"6 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.90 Å
7NO9 Structure of the mature RSV CA lattice: Group I, pentamer-pentamer interface, class 1'1 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.60 Å
7NOA Structure of the mature RSV CA lattice: Group II, hexamer-hexamer interface, class 6 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.40 Å
7NOB Structure of the mature RSV CA lattice: Group II, hexamer-hexamer interface, class 2'6 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.70 Å
7NOC Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 3'3 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.80 Å
7NOD Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 3'4 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.80 Å
7NOE Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 3'5 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.50 Å
7NOF Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 4'4 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.60 Å
7NOG Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 4'5 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.80 Å
7NOH Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 5'5 Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.10 Å
7NOI Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 3'Alpha Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.20 Å
7NOJ Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 3'Beta Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.70 Å
7NOK Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 3'Gamma Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 9.10 Å
7NOL Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 4'Alpha Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 8.20 Å
7NOM Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 4'Beta Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.70 Å
7NON Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 4'Gamma Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.80 Å
7NOO Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 5'Alpha Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.90 Å
7NOP Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 5'Beta Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 7.80 Å
7NOQ Structure of the mature RSV CA lattice: Group IV, hexamer-hexamer interface, class 5'Gamma Deposited 2021-02-25	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 × 10 PDB declaration: decameric	Chain A 240–468（229 aa） Chain B 240–468（229 aa） Chain C 240–468（229 aa） Chain D 240–468（229 aa） Chain E 240–468（229 aa） Chain F 240–468（229 aa） Chain G 240–468（229 aa） Chain H 240–468（229 aa） Chain I 240–468（229 aa） Chain J 240–468（229 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.2 cryo-EM vitrification conditions Cryogen ETHANE；2.5 seconds blotting time	Resolution 6.50 Å

41 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GAG_RSVP
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–77； UniProt 389–465

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	3g26
Deposition date deposition_date	2009-01-30
Structure title title	Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Mutant A184C
Keywords keywords	ALPHA-HELICAL BUNDLE, CAPSID PROTEIN, VIRION, VIRAL PROTEIN, RETROVIRUS; 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	13.43 Å
Radius of gyration Rg (electron density) rg_electron	11.94 Å
Forward intensity I(0) i0	1650450.00
Molecular weight molecular_weight	8602.0 kDa
Excluded volume excluded_volume	10766 Å³
Envelope volume envelope_volume	11850 Å³
Hydration-shell volume shell_volume	8791 Å³
Envelope diameter envelope_diameter	38.9 Å
Shell Rg shell_rg	17.16 Å
Envelope Rg envelope_rg	12.22 Å
Shape Rg shape_rg	11.90 Å
Total Rg total_rg	13.35 Å
Total atoms total_atoms	604
Residues n_residues	77
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	42.3 Å
Rg (real space) rg_real	13.36 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	1.6500e+06
I(0) uncertainty (real space) i0_real_error	1.6680e+04
Rg (reciprocal space) rg_reciprocal	13.36 Å
I(0) (reciprocal space) i0_reciprocal	1650000.0000
Solution quality estimate total_estimate	0.8966
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.6 Å
Skewness Skewness skewness	0.134
Kurtosis Kurtosis kurtosis	-0.384
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	215900.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.987

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Gag polyprotein
Molecular weight formula_weight	8506.7 kDa
EC 编号 ec_number	3.4.23.-
Mutation mutation	A184C
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	719

AGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSCRAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQ

来源 Source

来源生物 organism	Rous sarcoma virus
通用名 common_name	RSV-PrC
NCBI Class编号 ncbi_taxonomy_id	11888
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MALONIC ACID
Molecular weight formula_weight	104.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	81

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3g26a_
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.28.3.1 — Retrovirus capsid protein C-terminal domain

CATH v4.4 (1 domains)

Domain ID domain_id	3g26A00
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	32.243 Å
Unit-cell length b length_b	32.243 Å
Unit-cell length c length_c	113.993 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 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	1.550 Å
Low-resolution limit resolution_low	27.920 Å
R factor r_factor	0.1880
R_work r_work	0.1866
R_free r_free	0.2137

fit	/app/data/saxs_computation/g2/3g26/3g26.fit
pddf	/app/data/pr_computation/g2/3g26/3g26.pr.out
profile	/app/data/saxs_computation/g2/3g26/3g26.dat