SAXSdb — 4b4n

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

GAG PROTEIN

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 33–178	Fragment：N-TERMINAL DOMAIN, RESIDUES 33-178	CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 6 × 1 （Q16630）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；290 K；17 DEGREES (SITTING DROPS).PROTEIN/ PEPTIDE SOLUTION (0.37 MM HIV-1 CAN AND 4 MM CPSF6313-327 IN 20 MM HEPES PH 7, 50 MM NACL, 1 MM DTT) WAS MIXED WITH RESERVOIR SOLUTION (20% W/V PEG 3350, 0.2 M POTASSIUM PHOSPHATE DIBASIC) IN A 1:1 MIX.	Resolution 1.81 Å R-free 0.273

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A9PKC6_9HIV1
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–146； UniProt 33–178

CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 6

HOMO SAPIENS

UniProt Q16630

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 313–327	Fragment：RESIDUES 313-327	GAG PROTEIN × 1 （A9PKC6）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；290 K；17 DEGREES (SITTING DROPS).PROTEIN/ PEPTIDE SOLUTION (0.37 MM HIV-1 CAN AND 4 MM CPSF6313-327 IN 20 MM HEPES PH 7, 50 MM NACL, 1 MM DTT) WAS MIXED WITH RESERVOIR SOLUTION (20% W/V PEG 3350, 0.2 M POTASSIUM PHOSPHATE DIBASIC) IN A 1:1 MIX.	Resolution 1.81 Å R-free 0.273

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 4B4N	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3P5T CFIm25-CFIm68 complex Deposited 2010-10-11	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 L 80–161（82 aa） Fragment：UNP residues 80-161 Chain M 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；283 K；16% PEG 3350, 5% dioxane, 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 283K	Resolution 2.70 Å R-free 0.265
3P5T CFIm25-CFIm68 complex Deposited 2010-10-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain N 80–161（82 aa） Fragment：UNP residues 80-161 Chain O 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；283 K；16% PEG 3350, 5% dioxane, 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 283K	Resolution 2.70 Å R-free 0.265
3P5T CFIm25-CFIm68 complex Deposited 2010-10-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain P 80–161（82 aa） Fragment：UNP residues 80-161 Chain Q 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；283 K；16% PEG 3350, 5% dioxane, 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 283K	Resolution 2.70 Å R-free 0.265
3P6Y CF Im25-CF Im68-UGUAA complex Deposited 2010-10-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain C 80–161（82 aa） Fragment：UNP residues 80-161 Chain D 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；283 K；15% PEG 3350, 9% dioxane and 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 2.90 Å R-free 0.275
3P6Y CF Im25-CF Im68-UGUAA complex Deposited 2010-10-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain G 80–161（82 aa） Fragment：UNP residues 80-161 Chain H 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；283 K；15% PEG 3350, 9% dioxane and 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 2.90 Å R-free 0.275
3P6Y CF Im25-CF Im68-UGUAA complex Deposited 2010-10-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–RNA Heteromer；Protein × 4 PDB declaration: pentameric	Chain K 80–161（82 aa） Fragment：UNP residues 80-161 Chain L 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；283 K；15% PEG 3350, 9% dioxane and 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 2.90 Å R-free 0.275
3P6Y CF Im25-CF Im68-UGUAA complex Deposited 2010-10-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–RNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain O 80–161（82 aa） Fragment：UNP residues 80-161 Chain P 80–161（82 aa） Fragment：UNP residues 80-161	Mutation：C159S Mutation：C159S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；283 K；15% PEG 3350, 9% dioxane and 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 2.90 Å R-free 0.275
3Q2S Crystal Structure of CFIm68 RRM/CFIm25 complex Deposited 2010-12-20	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 C 13–235（223 aa） Fragment：RRM domain, residues 13-235 Chain D 13–235（223 aa） Fragment：RRM domain, residues 13-235	Mutation：C159V Mutation：C159V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；20% PEG 3350, 0.2M Magnesium Formate, 0.05M HEPES pH 7.0, vapor diffusion, hanging drop, temperature 298K	Resolution 2.90 Å R-free 0.278
3Q2T Crystal Structure of CFIm68 RRM/CFIm25/RNA complex Deposited 2010-12-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain C 13–235（223 aa） Fragment：RRM domain, residues 13-235 Chain D 13–235（223 aa） Fragment：RRM domain, residues 13-235	Mutation：C159V Mutation：C159V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；20% PEG 3350, 0.2M Magnesium Formate, 0.05M HEPES pH 7.0, vapor diffusion, hanging drop, temperature 298K	Resolution 3.06 Å R-free 0.286
4U0A Hexameric HIV-1 CA in complex with CPSF6 peptide, P6 crystal form Deposited 2014-07-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: Dodecameric	Chain B 276–290（15 aa） Fragment：UNP residues 313-327	Not recorded	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 M 276–290（15 aa） Fragment：UNP residues 276-290 Chain N 276–290（15 aa） Fragment：UNP residues 276-290 Chain O 276–290（15 aa） Fragment：UNP residues 276-290 Chain P 276–290（15 aa） Fragment：UNP residues 276-290 Chain Q 276–290（15 aa） Fragment：UNP residues 276-290 Chain R 276–290（15 aa） Fragment：UNP residues 276-290	Not recorded	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 S 276–290（15 aa） Fragment：UNP residues 276-290 Chain T 276–290（15 aa） Fragment：UNP residues 276-290 Chain U 276–290（15 aa） Fragment：UNP residues 276-290 Chain V 276–290（15 aa） Fragment：UNP residues 276-290 Chain W 276–290（15 aa） Fragment：UNP residues 276-290 Chain X 276–290（15 aa） Fragment：UNP residues 276-290	Not recorded	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
4WYM Structural basis of HIV-1 capsid recognition by CPSF6 Deposited 2014-11-17	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 M 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain N 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain O 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain P 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain Q 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain R 313–327（15 aa） Fragment：UNP RESIDUES 313-327	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；0.1 M sodium formate, ammonium acetate, tri-sodium citrate, sodium/potassium tartrate, sodium oxamate; 0.1 M sodium HEPES, MOPS; 30% glycerol, PEG 4000	Resolution 2.60 Å R-free 0.259
4WYM Structural basis of HIV-1 capsid recognition by CPSF6 Deposited 2014-11-17	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 S 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain T 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain U 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain V 313–327（15 aa） Fragment：UNP RESIDUES 313-327 Chain W 313–327（15 aa） Fragment：UNP RESIDUES 313-327	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；0.1 M sodium formate, ammonium acetate, tri-sodium citrate, sodium/potassium tartrate, sodium oxamate; 0.1 M sodium HEPES, MOPS; 30% glycerol, PEG 4000	Resolution 2.60 Å R-free 0.259
6AY9 Structure of the native full-length HIV-1 capsid protein in complex with CPSF6 peptide Deposited 2017-09-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 276–287（12 aa） Fragment：UNP residues 276-287	Not recorded	IOD IODIDE ION × 36 CL CHLORIDE ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；PEG3350, NaI, Sodium cacodylate, Glycerol	Resolution 2.50 Å R-free 0.273
6GX9 Crystal structure of the TNPO3 - CPSF6 RSLD complex Deposited 2018-06-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 408–477（70 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 2 BCN BICINE × 1 BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；12.8% PEG MME 500, 6.4% PEG 20,000, 4% 1,6-hexandiol, 1.5% benzamidine, 75 mM NaCl, 40 mM MgCl2, 6 mM DTT, 80 mM Tris-bicine, pH 8.0	Resolution 2.70 Å R-free 0.248
6GX9 Crystal structure of the TNPO3 - CPSF6 RSLD complex Deposited 2018-06-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 408–477（70 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 2 BCN BICINE × 1 BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；12.8% PEG MME 500, 6.4% PEG 20,000, 4% 1,6-hexandiol, 1.5% benzamidine, 75 mM NaCl, 40 mM MgCl2, 6 mM DTT, 80 mM Tris-bicine, pH 8.0	Resolution 2.70 Å R-free 0.248
7ZUD Crystal structure of HIV-1 capsid IP6-CPSF6 complex Deposited 2022-05-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain M 276–288（13 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.3M Calcium chloride dihydrate, 0.3 M Magnesium chloride hexahydrate, 0.1 M Tris hydrochloride pH 8.5, 0.1 M Bicine, 20% PEG 4000	Resolution 2.93 Å R-free 0.336
8CL1 HIV-1 mature capsid hexamer from CA-IP6 CLPs, bound to CPSF6 peptide. Deposited 2023-02-16	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 276–290（15 aa） Fragment：UNP residues 313-327	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.35 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 Y 313–327（15 aa） Fragment：UNP residues 313-327 Chain Z 313–327（15 aa） Fragment：UNP residues 313-327	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 Y 313–327（15 aa） Fragment：UNP residues 313-327 Chain Z 313–327（15 aa） Fragment：UNP residues 313-327	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 Y 313–327（15 aa） Fragment：UNP residues 313-327 Chain Z 313–327（15 aa） Fragment：UNP residues 313-327	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
9CNV HIV-2 CA hexamer bound with CPSF6 peptide; assembled via liposome templating Deposited 2024-07-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 313–327（15 aa）	Mutation：Delta(1-312) and Delta(328-358)	IHP INOSITOL HEXAKISPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7；The mixed buffer of storage buffer for the protein and lipid components with IP6 supplemented. cryo-EM vitrification conditions Cryogen ETHANE；Grids were dual-side blotted with blot force 0 for 5.5 sec before plunge freezing in liquid ethane.	Resolution 3.16 Å
9CNV HIV-2 CA hexamer bound with CPSF6 peptide; assembled via liposome templating Deposited 2024-07-15	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 313–327（15 aa）	Mutation：Delta(1-312) and Delta(328-358)	IHP INOSITOL HEXAKISPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7；The mixed buffer of storage buffer for the protein and lipid components with IP6 supplemented. cryo-EM vitrification conditions Cryogen ETHANE；Grids were dual-side blotted with blot force 0 for 5.5 sec before plunge freezing in liquid ethane.	Resolution 3.16 Å

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CPSF6_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–15； UniProt 313–327

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4b4n
Deposition date deposition_date	2012-07-31
Structure title title	CPSF6 defines a conserved capsid interface that modulates HIV-1 replication
Keywords keywords	VIRAL PROTEIN-RNA BINDING PROTEIN COMPLEX, HIV-1, CYCLOPHILIN; VIRAL PROTEIN/RNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	16.65 Å
Radius of gyration Rg (electron density) rg_electron	15.43 Å
Forward intensity I(0) i0	5314720.00
Molecular weight molecular_weight	16742.0 kDa
Excluded volume excluded_volume	21058 Å³
Envelope volume envelope_volume	24137 Å³
Hydration-shell volume shell_volume	13391 Å³
Envelope diameter envelope_diameter	54.8 Å
Shell Rg shell_rg	21.04 Å
Envelope Rg envelope_rg	15.92 Å
Shape Rg shape_rg	15.42 Å
Total Rg total_rg	16.56 Å
Total atoms total_atoms	1178
Residues n_residues	151
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

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

Maximum dimension Dmax dmax	54.5 Å
Rg (real space) rg_real	16.58 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	5.3150e+06
I(0) uncertainty (real space) i0_real_error	6.3460e+04
Rg (reciprocal space) rg_reciprocal	16.59 Å
I(0) (reciprocal space) i0_reciprocal	5315000.0000
Solution quality estimate total_estimate	0.8848
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.8 Å
Skewness Skewness skewness	0.221
Kurtosis Kurtosis kurtosis	-0.364
Angular range angular_range	— – 0.4800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	916000.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.959

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	GAG PROTEIN
Molecular weight formula_weight	16204.6 kDa
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	1285

PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYS

来源 Source

来源生物 organism	HUMAN IMMUNODEFICIENCY VIRUS 1
NCBI Class编号 ncbi_taxonomy_id	11676
宿主生物 host_organism	SACCHAROMYCES CEREVISIAE

Entity 2 Entity 2 polymer

Description description	CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 6
Molecular weight formula_weight	1550.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

PVLFPGQPFGQPPLG

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	SACCHAROMYCES CEREVISIAE

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	99

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d4b4na_
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

CATH v4.4 (1 domains)

Domain ID domain_id	4b4nA00
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

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8. Citations (1)

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Unit-cell length a length_a	40.560 Å
Unit-cell length b length_b	46.360 Å
Unit-cell length c length_c	80.820 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.813 Å
Low-resolution limit resolution_low	36.251 Å
R factor r_factor	0.1910
R_work r_work	0.1867
R_free r_free	0.2729

fit	/app/data/saxs_computation/b4/4b4n/4b4n.fit
pddf	/app/data/pr_computation/b4/4b4n/4b4n.pr.out
profile	/app/data/saxs_computation/b4/4b4n/4b4n.dat

CPSF6 defines a conserved capsid interface that modulates HIV-1 replication

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

GAG PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 6

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)