SAXSdb — 4e2i

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

Large T antigen

Simian virus 40

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 266–627 Chain B； UniProt 266–627 Chain C； UniProt 266–627 Chain D； UniProt 266–627 Chain E； UniProt 266–627 Chain F； UniProt 266–627	Fragment：UNP residues 266-627	DNA polymerase alpha subunit B × 6 （Q14181） ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；0.96 M sodium malonate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 5.00 Å R-free 0.314
2	Protein heterocomplex Heteromer Protein × 11 PDB declaration: undecameric（11） Consistent with protein copy count	Chain G； UniProt 266–627 Chain H； UniProt 266–627 Chain I； UniProt 266–627 Chain J； UniProt 266–627 Chain K； UniProt 266–627 Chain L； UniProt 266–627	Fragment：UNP residues 266-627	DNA polymerase alpha subunit B × 5 （Q14181） ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；0.96 M sodium malonate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 5.00 Å R-free 0.314

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 4E2I	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2H1L The Structure of the Oncoprotein SV40 Large T Antigen and p53 Tumor Suppressor Complex Deposited 2006-05-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain B 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain C 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain D 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain E 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain F 260–627（368 aa） Fragment：Helicase Domain, residues 260-627	Not recorded	ZN ZINC ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；5.4% PEG 4000, 73mM Mops Buffer, 22mM Lithium Sulfate, pH 6.5, VAPOR DIFFUSION, temperature 298K	Resolution 3.16 Å R-free 0.308
2H1L The Structure of the Oncoprotein SV40 Large T Antigen and p53 Tumor Suppressor Complex Deposited 2006-05-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain H 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain I 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain J 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain K 260–627（368 aa） Fragment：Helicase Domain, residues 260-627 Chain L 260–627（368 aa） Fragment：Helicase Domain, residues 260-627	Not recorded	ZN ZINC ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；5.4% PEG 4000, 73mM Mops Buffer, 22mM Lithium Sulfate, pH 6.5, VAPOR DIFFUSION, temperature 298K	Resolution 3.16 Å R-free 0.308
4GDF A Crystal Structure of SV40 Large T Antigen Deposited 2012-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 131–627（497 aa） Fragment：UNP residues 131-627 Chain B 131–627（497 aa） Fragment：UNP residues 131-627	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.75；291 K；100 mM bis-Tris (pH 6.75), 20% (v/v) PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.255
4GDF A Crystal Structure of SV40 Large T Antigen Deposited 2012-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain E 131–627（497 aa） Fragment：UNP residues 131-627 Chain F 131–627（497 aa） Fragment：UNP residues 131-627	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.75；291 K；100 mM bis-Tris (pH 6.75), 20% (v/v) PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.255

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q9DH70_SV40
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–362； UniProt 266–627 Author chain B； PDBConstruct 1–362； UniProt 266–627 Author chain C； PDBConstruct 1–362； UniProt 266–627 Author chain D； PDBConstruct 1–362； UniProt 266–627 Author chain E； PDBConstruct 1–362； UniProt 266–627 Author chain F； PDBConstruct 1–362； UniProt 266–627 Author chain G； PDBConstruct 1–362； UniProt 266–627 Author chain H； PDBConstruct 1–362； UniProt 266–627 Author chain I； PDBConstruct 1–362； UniProt 266–627 Author chain J； PDBConstruct 1–362； UniProt 266–627 Author chain K； PDBConstruct 1–362； UniProt 266–627 Author chain L； PDBConstruct 1–362； UniProt 266–627

DNA polymerase alpha subunit B

Homo sapiens

UniProt Q14181

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain 1； UniProt 1–78 Chain 2； UniProt 1–78 Chain 3； UniProt 1–78 Chain 4； UniProt 1–78 Chain 5； UniProt 1–78 Chain 6； UniProt 1–78	Fragment：UNP residues 1-78	Large T antigen × 6 （Q9DH70） ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；0.96 M sodium malonate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 5.00 Å R-free 0.314
2	Protein heterocomplex Heteromer Protein × 11 PDB declaration: undecameric（11） Consistent with protein copy count	Chain 7； UniProt 1–78 Chain 8； UniProt 1–78 Chain 9； UniProt 1–78 Chain U； UniProt 1–78 Chain W； UniProt 1–78	Fragment：UNP residues 1-78	Large T antigen × 6 （Q9DH70） ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；0.96 M sodium malonate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 5.00 Å R-free 0.314

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 4E2I	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2KEB NMR solution structure of the N-terminal domain of the DNA polymerase alpha p68 subunit Deposited 2009-01-28	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 1–78（78 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.75 mM [U-100% 13C; U-100% 15N] protein, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
4Y97 Crystal Structure of human Pol alpha B-subunit in complex with C-terminal domain of catalytic subunit Deposited 2015-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–598（598 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；The diffraction quality crystals are growing in 2-3 weeks in 100 mM ammonium acetate, 50 mM Na citrate pH 5.6, 10 - 10.4% w/v PEG 4000, 2 mM TCEP and 50 mM guanidine HCl.	Resolution 2.51 Å R-free 0.257
4Y97 Crystal Structure of human Pol alpha B-subunit in complex with C-terminal domain of catalytic subunit Deposited 2015-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–598（598 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；The diffraction quality crystals are growing in 2-3 weeks in 100 mM ammonium acetate, 50 mM Na citrate pH 5.6, 10 - 10.4% w/v PEG 4000, 2 mM TCEP and 50 mM guanidine HCl.	Resolution 2.51 Å R-free 0.257
4Y97 Crystal Structure of human Pol alpha B-subunit in complex with C-terminal domain of catalytic subunit Deposited 2015-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–598（598 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；The diffraction quality crystals are growing in 2-3 weeks in 100 mM ammonium acetate, 50 mM Na citrate pH 5.6, 10 - 10.4% w/v PEG 4000, 2 mM TCEP and 50 mM guanidine HCl.	Resolution 2.51 Å R-free 0.257
4Y97 Crystal Structure of human Pol alpha B-subunit in complex with C-terminal domain of catalytic subunit Deposited 2015-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–598（598 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；The diffraction quality crystals are growing in 2-3 weeks in 100 mM ammonium acetate, 50 mM Na citrate pH 5.6, 10 - 10.4% w/v PEG 4000, 2 mM TCEP and 50 mM guanidine HCl.	Resolution 2.51 Å R-free 0.257
5EXR Crystal structure of human primosome Deposited 2015-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 2–598（597 aa）	Not recorded	ZN ZINC ION × 3 SF4 IRON/SULFUR CLUSTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.2 M lithium sulphate, 50 mM TRIS HCl pH 8.5, 2 mM TCEP pH 7.5, 11.2% w/v PEG 4,000, 3% v/v ethanol, 0.5% v/v polypropylene glycol P400 and 0.2 mM EDTA	Resolution 3.60 Å R-free 0.326
5EXR Crystal structure of human primosome Deposited 2015-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 2–598（597 aa）	Not recorded	ZN ZINC ION × 3 SF4 IRON/SULFUR CLUSTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.2 M lithium sulphate, 50 mM TRIS HCl pH 8.5, 2 mM TCEP pH 7.5, 11.2% w/v PEG 4,000, 3% v/v ethanol, 0.5% v/v polypropylene glycol P400 and 0.2 mM EDTA	Resolution 3.60 Å R-free 0.326
7OPL CryoEM structure of DNA Polymerase alpha - primase bound to SARS CoV nsp1 Deposited 2021-06-01	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 × 5 PDB declaration: pentameric	Chain B 149–598（450 aa）	Not recorded	ZN ZINC ION × 3 SF4 IRON/SULFUR CLUSTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.12 Å
7U5C Cryo-EM structure of human CST bound to DNA polymerase alpha-primase in a recruitment state Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 7 PDB declaration: octameric	Chain D 1–598（598 aa）	Not recorded	ZN ZINC ION × 4 SF4 IRON/SULFUR CLUSTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
8B9D Human replisome bound by Pol Alpha Deposited 2022-10-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 21 PDB declaration: 23-meric	Chain A 1–598（598 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8D0B Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback template Deposited 2022-05-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 7 PDB declaration: octameric	Chain G 143–598（456 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
8D0K Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback template - PRIM2C advanced PIC Deposited 2022-05-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 7 PDB declaration: octameric	Chain G 2–598（597 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.27 Å
8D9D Human DNA polymerase-alpha/primase elongation complex II bound to primer/template Deposited 2022-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric	Chain D 155–598（444 aa）	Not recorded	ZN ZINC ION × 3 SF4 IRON/SULFUR CLUSTER × 1 MG MAGNESIUM ION × 2 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before added to the sample at a final concentration of 4-8 mM immediately before vitrification. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.59 Å
8QJ7 Cryo-EM structure of human DNA polymerase alpha-primase in pre-initiation stage 1 Deposited 2023-09-12	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 × 4 PDB declaration: tetrameric	Chain B 1–598（598 aa）	Not recorded	ZN ZINC ION × 3 MN MANGANESE (II) ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 SF4 IRON/SULFUR CLUSTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
8VY3 Human DNA polymerase alpha/primase - AavLEA1 (1:40 molar ratio) Deposited 2024-02-06	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 × 4 PDB declaration: tetrameric	Chain D 155–598（444 aa）	Not recorded	ZN ZINC ION × 3 SF4 IRON/SULFUR CLUSTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.98 Å
9C8V Human DNA polymerase alpha/primase - CHAPSO (4 mM) Deposited 2024-06-13	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 × 4 PDB declaration: tetrameric	Chain D 155–598（444 aa）	Not recorded	ZN ZINC ION × 3 SF4 IRON/SULFUR CLUSTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.39 Å

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DPOA2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 1； PDBConstruct 1–78； UniProt 1–78 Author chain 2； PDBConstruct 1–78； UniProt 1–78 Author chain 3； PDBConstruct 1–78； UniProt 1–78 Author chain 4； PDBConstruct 1–78； UniProt 1–78 Author chain 5； PDBConstruct 1–78； UniProt 1–78 Author chain 6； PDBConstruct 1–78； UniProt 1–78 Author chain 7； PDBConstruct 1–78； UniProt 1–78 Author chain 8； PDBConstruct 1–78； UniProt 1–78 Author chain 9； PDBConstruct 1–78； UniProt 1–78 Author chain U； PDBConstruct 1–78； UniProt 1–78 Author chain W； PDBConstruct 1–78； UniProt 1–78

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	4e2i
Deposition date deposition_date	2012-03-08
Structure title title	The Complex Structure of the SV40 Helicase Large T Antigen and p68 Subunit of DNA Polymerase Alpha-Primase
Keywords keywords	replication initiation, Hydrolase-DNA binding complex, Hydrolase-DNA binding Protein complex; Hydrolase/DNA 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	75.76 Å
Radius of gyration Rg (electron density) rg_electron	75.77 Å
Forward intensity I(0) i0	4637940000.00
Molecular weight molecular_weight	597280.0 kDa
Excluded volume excluded_volume	754690 Å³
Envelope volume envelope_volume	1203600 Å³
Hydration-shell volume shell_volume	128020 Å³
Envelope diameter envelope_diameter	242.1 Å
Shell Rg shell_rg	83.15 Å
Envelope Rg envelope_rg	72.21 Å
Shape Rg shape_rg	75.77 Å
Total Rg total_rg	75.89 Å
Total atoms total_atoms	41874
Residues n_residues	5202
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	217.0 Å
Rg (real space) rg_real	75.77 Å
Rg uncertainty (real space) rg_real_error	1.34 Å
I(0) (real space) i0_real	4.6330e+09
I(0) uncertainty (real space) i0_real_error	9.8000e+07
Rg (reciprocal space) rg_reciprocal	74.82 Å
I(0) (reciprocal space) i0_reciprocal	4626000000.0000
Solution quality estimate total_estimate	0.8010
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	51.7 Å
Skewness Skewness skewness	0.198
Kurtosis Kurtosis kurtosis	-0.975
Angular range angular_range	— – 0.1050 Å⁻¹
Current regularization parameter α current_alpha	0.0055
Highest regularization parameter α highest_alpha	871600000.0000
Real-space data points n_real_points	22
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.829; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.922; Smooth: 0.000

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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	Large T antigen
Molecular weight formula_weight	41812.7 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	41874

KQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLDRMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDSGKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQGINNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPKDYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLSVYQKMKFNVAMGIGVLD

来源 Source

来源生物 organism	Simian virus 40
通用名 common_name	SV40
NCBI Class编号 ncbi_taxonomy_id	10633
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	DNA polymerase alpha subunit B
Molecular weight formula_weight	8700.9 kDa
Source method src_method	man
Copy count entity_count	11

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2,3,6,U,W,5,7,9,1,4,8

MSASAQQLAEELQIFGLDCEEALIEKLVELCVQYGQNEEGMVGELIAFCTSTHKVGLTSEILNSFEHEFLSKRLSKAR

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	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	12

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8. Citations (1)

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Unit-cell length a length_a	249.098 Å
Unit-cell length b length_b	249.098 Å
Unit-cell length c length_c	387.032 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	96

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	5.000 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.3047
R_work r_work	0.3047
R_free r_free	0.3139

fit	/app/data/saxs_computation/e2/4e2i/4e2i.fit
pddf	/app/data/pr_computation/e2/4e2i/4e2i.pr.out
profile	/app/data/saxs_computation/e2/4e2i/4e2i.dat

The Complex Structure of the SV40 Helicase Large T Antigen and p68 Subunit of DNA Polymerase Alpha-Primase

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

Large T antigen

State in the Current Structure

Other States of the Same Protein in the Database

DNA polymerase alpha subunit B

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 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)