SAXSdb — 9k3m

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

Capsid protein F

OrganismNot specified

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 × 180 PDB declaration: 180-meric（180） Consistent with protein copy count	Chain A； UniProt 1–427 Chain AB； UniProt 1–427 Chain AE； UniProt 1–427 Chain BC； UniProt 1–427 Chain BF； UniProt 1–427 Chain CA； UniProt 1–427 Chain CD； UniProt 1–427 Chain D； UniProt 1–427 Chain DB； UniProt 1–427 Chain DE； UniProt 1–427 Chain EC； UniProt 1–427 Chain EF； UniProt 1–427 Chain F； UniProt 1–427 Chain FA； UniProt 1–427 Chain FD； UniProt 1–427 Chain GB； UniProt 1–427 Chain GE； UniProt 1–427 Chain HC； UniProt 1–427 Chain HF； UniProt 1–427 Chain I； UniProt 1–427 Chain IA； UniProt 1–427 Chain ID； UniProt 1–427 Chain JB； UniProt 1–427 Chain JE； UniProt 1–427 Chain KC； UniProt 1–427 Chain KF； UniProt 1–427 Chain LA； UniProt 1–427 Chain LD； UniProt 1–427 Chain M； UniProt 1–427 Chain MB； UniProt 1–427 Chain ME； UniProt 1–427 Chain NC； UniProt 1–427 Chain NF； UniProt 1–427 Chain OA； UniProt 1–427 Chain OD； UniProt 1–427 Chain P； UniProt 1–427 Chain PB； UniProt 1–427 Chain PE； UniProt 1–427 Chain QC； UniProt 1–427 Chain QF； UniProt 1–427 Chain RA； UniProt 1–427 Chain RD； UniProt 1–427 Chain S； UniProt 1–427 Chain SB； UniProt 1–427 Chain SE； UniProt 1–427 Chain TC； UniProt 1–427 Chain TF； UniProt 1–427 Chain UA； UniProt 1–427 Chain UD； UniProt 1–427 Chain VB； UniProt 1–427 Chain VE； UniProt 1–427 Chain W； UniProt 1–427 Chain WC； UniProt 1–427 Chain WF； UniProt 1–427 Chain XA； UniProt 1–427 Chain XD； UniProt 1–427 Chain YB； UniProt 1–427 Chain YE； UniProt 1–427 Chain Z； UniProt 1–427 Chain ZC； UniProt 1–427	Not recorded	Major spike protein G × 60 （A0A5J6T840） DNA-binding protein J × 60 （P69592）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；pH 7.2~7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.68 Å

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	Q2LLZ1_BPPHX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–427； UniProt 1–427 Author chain AB； PDBConstruct 1–427； UniProt 1–427 Author chain AE； PDBConstruct 1–427； UniProt 1–427 Author chain BC； PDBConstruct 1–427； UniProt 1–427 Author chain BF； PDBConstruct 1–427； UniProt 1–427 Author chain CA； PDBConstruct 1–427； UniProt 1–427 Author chain CD； PDBConstruct 1–427； UniProt 1–427 Author chain D； PDBConstruct 1–427； UniProt 1–427 Author chain DB； PDBConstruct 1–427； UniProt 1–427 Author chain DE； PDBConstruct 1–427； UniProt 1–427 Author chain EC； PDBConstruct 1–427； UniProt 1–427 Author chain EF； PDBConstruct 1–427； UniProt 1–427 Author chain F； PDBConstruct 1–427； UniProt 1–427 Author chain FA； PDBConstruct 1–427； UniProt 1–427 Author chain FD； PDBConstruct 1–427； UniProt 1–427 Author chain GB； PDBConstruct 1–427； UniProt 1–427 Author chain GE； PDBConstruct 1–427； UniProt 1–427 Author chain HC； PDBConstruct 1–427； UniProt 1–427 Author chain HF； PDBConstruct 1–427； UniProt 1–427 Author chain I； PDBConstruct 1–427； UniProt 1–427 Author chain IA； PDBConstruct 1–427； UniProt 1–427 Author chain ID； PDBConstruct 1–427； UniProt 1–427 Author chain JB； PDBConstruct 1–427； UniProt 1–427 Author chain JE； PDBConstruct 1–427； UniProt 1–427 Author chain KC； PDBConstruct 1–427； UniProt 1–427 Author chain KF； PDBConstruct 1–427； UniProt 1–427 Author chain LA； PDBConstruct 1–427； UniProt 1–427 Author chain LD； PDBConstruct 1–427； UniProt 1–427 Author chain M； PDBConstruct 1–427； UniProt 1–427 Author chain MB； PDBConstruct 1–427； UniProt 1–427 Author chain ME； PDBConstruct 1–427； UniProt 1–427 Author chain NC； PDBConstruct 1–427； UniProt 1–427 Author chain NF； PDBConstruct 1–427； UniProt 1–427 Author chain OA； PDBConstruct 1–427； UniProt 1–427 Author chain OD； PDBConstruct 1–427； UniProt 1–427 Author chain P； PDBConstruct 1–427； UniProt 1–427 Author chain PB； PDBConstruct 1–427； UniProt 1–427 Author chain PE； PDBConstruct 1–427； UniProt 1–427 Author chain QC； PDBConstruct 1–427； UniProt 1–427 Author chain QF； PDBConstruct 1–427； UniProt 1–427 Author chain RA； PDBConstruct 1–427； UniProt 1–427 Author chain RD； PDBConstruct 1–427； UniProt 1–427 Author chain S； PDBConstruct 1–427； UniProt 1–427 Author chain SB； PDBConstruct 1–427； UniProt 1–427 Author chain SE； PDBConstruct 1–427； UniProt 1–427 Author chain TC； PDBConstruct 1–427； UniProt 1–427 Author chain TF； PDBConstruct 1–427； UniProt 1–427 Author chain UA； PDBConstruct 1–427； UniProt 1–427 Author chain UD； PDBConstruct 1–427； UniProt 1–427 Author chain VB； PDBConstruct 1–427； UniProt 1–427 Author chain VE； PDBConstruct 1–427； UniProt 1–427 Author chain W； PDBConstruct 1–427； UniProt 1–427 Author chain WC； PDBConstruct 1–427； UniProt 1–427 Author chain WF； PDBConstruct 1–427； UniProt 1–427 Author chain XA； PDBConstruct 1–427； UniProt 1–427 Author chain XD； PDBConstruct 1–427； UniProt 1–427 Author chain YB； PDBConstruct 1–427； UniProt 1–427 Author chain YE； PDBConstruct 1–427； UniProt 1–427 Author chain Z； PDBConstruct 1–427； UniProt 1–427 Author chain ZC； PDBConstruct 1–427； UniProt 1–427

Major spike protein G

OrganismNot specified

UniProt A0A5J6T840

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 × 180 PDB declaration: 180-meric（180） Consistent with protein copy count	Chain AA； UniProt 1–175 Chain AD； UniProt 1–175 Chain B； UniProt 1–175 Chain BB； UniProt 1–175 Chain BE； UniProt 1–175 Chain CC； UniProt 1–175 Chain CF； UniProt 1–175 Chain DA； UniProt 1–175 Chain DD； UniProt 1–175 Chain E； UniProt 1–175 Chain EB； UniProt 1–175 Chain EE； UniProt 1–175 Chain FC； UniProt 1–175 Chain FF； UniProt 1–175 Chain G； UniProt 1–175 Chain GA； UniProt 1–175 Chain GD； UniProt 1–175 Chain HB； UniProt 1–175 Chain HE； UniProt 1–175 Chain IC； UniProt 1–175 Chain IF； UniProt 1–175 Chain JA； UniProt 1–175 Chain JD； UniProt 1–175 Chain K； UniProt 1–175 Chain KB； UniProt 1–175 Chain KE； UniProt 1–175 Chain LC； UniProt 1–175 Chain LF； UniProt 1–175 Chain MA； UniProt 1–175 Chain MD； UniProt 1–175 Chain N； UniProt 1–175 Chain NB； UniProt 1–175 Chain NE； UniProt 1–175 Chain OC； UniProt 1–175 Chain OF； UniProt 1–175 Chain PA； UniProt 1–175 Chain PD； UniProt 1–175 Chain Q； UniProt 1–175 Chain QB； UniProt 1–175 Chain QE； UniProt 1–175 Chain RC； UniProt 1–175 Chain RF； UniProt 1–175 Chain SA； UniProt 1–175 Chain SD； UniProt 1–175 Chain T； UniProt 1–175 Chain TB； UniProt 1–175 Chain TE； UniProt 1–175 Chain UC； UniProt 1–175 Chain UF； UniProt 1–175 Chain VA； UniProt 1–175 Chain VD； UniProt 1–175 Chain WB； UniProt 1–175 Chain WE； UniProt 1–175 Chain X； UniProt 1–175 Chain XC； UniProt 1–175 Chain XF； UniProt 1–175 Chain YA； UniProt 1–175 Chain YD； UniProt 1–175 Chain ZB； UniProt 1–175 Chain ZE； UniProt 1–175	Not recorded	Capsid protein F × 60 （Q2LLZ1） DNA-binding protein J × 60 （P69592）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；pH 7.2~7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.68 Å

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	A0A5J6T840_9VIRU
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain AA； PDBConstruct 1–175； UniProt 1–175 Author chain AD； PDBConstruct 1–175； UniProt 1–175 Author chain B； PDBConstruct 1–175； UniProt 1–175 Author chain BB； PDBConstruct 1–175； UniProt 1–175 Author chain BE； PDBConstruct 1–175； UniProt 1–175 Author chain CC； PDBConstruct 1–175； UniProt 1–175 Author chain CF； PDBConstruct 1–175； UniProt 1–175 Author chain DA； PDBConstruct 1–175； UniProt 1–175 Author chain DD； PDBConstruct 1–175； UniProt 1–175 Author chain E； PDBConstruct 1–175； UniProt 1–175 Author chain EB； PDBConstruct 1–175； UniProt 1–175 Author chain EE； PDBConstruct 1–175； UniProt 1–175 Author chain FC； PDBConstruct 1–175； UniProt 1–175 Author chain FF； PDBConstruct 1–175； UniProt 1–175 Author chain G； PDBConstruct 1–175； UniProt 1–175 Author chain GA； PDBConstruct 1–175； UniProt 1–175 Author chain GD； PDBConstruct 1–175； UniProt 1–175 Author chain HB； PDBConstruct 1–175； UniProt 1–175 Author chain HE； PDBConstruct 1–175； UniProt 1–175 Author chain IC； PDBConstruct 1–175； UniProt 1–175 Author chain IF； PDBConstruct 1–175； UniProt 1–175 Author chain JA； PDBConstruct 1–175； UniProt 1–175 Author chain JD； PDBConstruct 1–175； UniProt 1–175 Author chain K； PDBConstruct 1–175； UniProt 1–175 Author chain KB； PDBConstruct 1–175； UniProt 1–175 Author chain KE； PDBConstruct 1–175； UniProt 1–175 Author chain LC； PDBConstruct 1–175； UniProt 1–175 Author chain LF； PDBConstruct 1–175； UniProt 1–175 Author chain MA； PDBConstruct 1–175； UniProt 1–175 Author chain MD； PDBConstruct 1–175； UniProt 1–175 Author chain N； PDBConstruct 1–175； UniProt 1–175 Author chain NB； PDBConstruct 1–175； UniProt 1–175 Author chain NE； PDBConstruct 1–175； UniProt 1–175 Author chain OC； PDBConstruct 1–175； UniProt 1–175 Author chain OF； PDBConstruct 1–175； UniProt 1–175 Author chain PA； PDBConstruct 1–175； UniProt 1–175 Author chain PD； PDBConstruct 1–175； UniProt 1–175 Author chain Q； PDBConstruct 1–175； UniProt 1–175 Author chain QB； PDBConstruct 1–175； UniProt 1–175 Author chain QE； PDBConstruct 1–175； UniProt 1–175 Author chain RC； PDBConstruct 1–175； UniProt 1–175 Author chain RF； PDBConstruct 1–175； UniProt 1–175 Author chain SA； PDBConstruct 1–175； UniProt 1–175 Author chain SD； PDBConstruct 1–175； UniProt 1–175 Author chain T； PDBConstruct 1–175； UniProt 1–175 Author chain TB； PDBConstruct 1–175； UniProt 1–175 Author chain TE； PDBConstruct 1–175； UniProt 1–175 Author chain UC； PDBConstruct 1–175； UniProt 1–175 Author chain UF； PDBConstruct 1–175； UniProt 1–175 Author chain VA； PDBConstruct 1–175； UniProt 1–175 Author chain VD； PDBConstruct 1–175； UniProt 1–175 Author chain WB； PDBConstruct 1–175； UniProt 1–175 Author chain WE； PDBConstruct 1–175； UniProt 1–175 Author chain X； PDBConstruct 1–175； UniProt 1–175 Author chain XC； PDBConstruct 1–175； UniProt 1–175 Author chain XF； PDBConstruct 1–175； UniProt 1–175 Author chain YA； PDBConstruct 1–175； UniProt 1–175 Author chain YD； PDBConstruct 1–175； UniProt 1–175 Author chain ZB； PDBConstruct 1–175； UniProt 1–175 Author chain ZE； PDBConstruct 1–175； UniProt 1–175

DNA-binding protein J

OrganismNot specified

UniProt P69592

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 × 180 PDB declaration: 180-meric（180） Consistent with protein copy count	Chain AC； UniProt 1–38 Chain AF； UniProt 1–38 Chain BA； UniProt 1–38 Chain BD； UniProt 1–38 Chain C； UniProt 1–38 Chain CB； UniProt 1–38 Chain CE； UniProt 1–38 Chain DC； UniProt 1–38 Chain DF； UniProt 1–38 Chain EA； UniProt 1–38 Chain ED； UniProt 1–38 Chain FB； UniProt 1–38 Chain FE； UniProt 1–38 Chain GC； UniProt 1–38 Chain GF； UniProt 1–38 Chain H； UniProt 1–38 Chain HA； UniProt 1–38 Chain HD； UniProt 1–38 Chain IB； UniProt 1–38 Chain IE； UniProt 1–38 Chain J； UniProt 1–38 Chain JC； UniProt 1–38 Chain JF； UniProt 1–38 Chain KA； UniProt 1–38 Chain KD； UniProt 1–38 Chain L； UniProt 1–38 Chain LB； UniProt 1–38 Chain LE； UniProt 1–38 Chain MC； UniProt 1–38 Chain MF； UniProt 1–38 Chain NA； UniProt 1–38 Chain ND； UniProt 1–38 Chain O； UniProt 1–38 Chain OB； UniProt 1–38 Chain OE； UniProt 1–38 Chain PC； UniProt 1–38 Chain PF； UniProt 1–38 Chain QA； UniProt 1–38 Chain QD； UniProt 1–38 Chain R； UniProt 1–38 Chain RB； UniProt 1–38 Chain RE； UniProt 1–38 Chain SC； UniProt 1–38 Chain SF； UniProt 1–38 Chain TA； UniProt 1–38 Chain TD； UniProt 1–38 Chain UB； UniProt 1–38 Chain UE； UniProt 1–38 Chain V； UniProt 1–38 Chain VC； UniProt 1–38 Chain VF； UniProt 1–38 Chain WA； UniProt 1–38 Chain WD； UniProt 1–38 Chain XB； UniProt 1–38 Chain XE； UniProt 1–38 Chain Y； UniProt 1–38 Chain YC； UniProt 1–38 Chain YF； UniProt 1–38 Chain ZA； UniProt 1–38 Chain ZD； UniProt 1–38	Not recorded	Capsid protein F × 60 （Q2LLZ1） Major spike protein G × 60 （A0A5J6T840）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；pH 7.2~7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.68 Å

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 9K3M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03	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 × 180 PDB declaration: 240-MERIC	Chain J 1–37（37 aa）	Not recorded	DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 360	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain J 1–37（37 aa）	Not recorded	DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Heteromer；Protein × 15 PDB declaration: eicosameric	Chain J 1–37（37 aa）	Not recorded	DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Heteromer；Protein × 18 PDB declaration: 24-meric	Chain J 1–37（37 aa）	Not recorded	DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 36	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain J 1–37（37 aa）	Not recorded	DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein–DNA Heteromer；Protein × 60 PDB declaration: 80-meric	Chain J 1–37（37 aa）	Not recorded	DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 120	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.50 Å R-free 0.236
2BPA ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS Deposited 1991-12-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-MERIC	Chain 3 2–38（37 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å
2BPA ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS Deposited 1991-12-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain 3 2–38（37 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å
2BPA ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS Deposited 1991-12-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Heteromer；Protein × 15 PDB declaration: eicosameric	Chain 3 2–38（37 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å
2BPA ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS Deposited 1991-12-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Heteromer；Protein × 18 PDB declaration: 24-meric	Chain 3 2–38（37 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å
2BPA ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS Deposited 1991-12-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain 3 2–38（37 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å

2 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	J_BPPHS
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain AC； PDBConstruct 1–38； UniProt 1–38 Author chain AF； PDBConstruct 1–38； UniProt 1–38 Author chain BA； PDBConstruct 1–38； UniProt 1–38 Author chain BD； PDBConstruct 1–38； UniProt 1–38 Author chain C； PDBConstruct 1–38； UniProt 1–38 Author chain CB； PDBConstruct 1–38； UniProt 1–38 Author chain CE； PDBConstruct 1–38； UniProt 1–38 Author chain DC； PDBConstruct 1–38； UniProt 1–38 Author chain DF； PDBConstruct 1–38； UniProt 1–38 Author chain EA； PDBConstruct 1–38； UniProt 1–38 Author chain ED； PDBConstruct 1–38； UniProt 1–38 Author chain FB； PDBConstruct 1–38； UniProt 1–38 Author chain FE； PDBConstruct 1–38； UniProt 1–38 Author chain GC； PDBConstruct 1–38； UniProt 1–38 Author chain GF； PDBConstruct 1–38； UniProt 1–38 Author chain H； PDBConstruct 1–38； UniProt 1–38 Author chain HA； PDBConstruct 1–38； UniProt 1–38 Author chain HD； PDBConstruct 1–38； UniProt 1–38 Author chain IB； PDBConstruct 1–38； UniProt 1–38 Author chain IE； PDBConstruct 1–38； UniProt 1–38 Author chain J； PDBConstruct 1–38； UniProt 1–38 Author chain JC； PDBConstruct 1–38； UniProt 1–38 Author chain JF； PDBConstruct 1–38； UniProt 1–38 Author chain KA； PDBConstruct 1–38； UniProt 1–38 Author chain KD； PDBConstruct 1–38； UniProt 1–38 Author chain L； PDBConstruct 1–38； UniProt 1–38 Author chain LB； PDBConstruct 1–38； UniProt 1–38 Author chain LE； PDBConstruct 1–38； UniProt 1–38 Author chain MC； PDBConstruct 1–38； UniProt 1–38 Author chain MF； PDBConstruct 1–38； UniProt 1–38 Author chain NA； PDBConstruct 1–38； UniProt 1–38 Author chain ND； PDBConstruct 1–38； UniProt 1–38 Author chain O； PDBConstruct 1–38； UniProt 1–38 Author chain OB； PDBConstruct 1–38； UniProt 1–38 Author chain OE； PDBConstruct 1–38； UniProt 1–38 Author chain PC； PDBConstruct 1–38； UniProt 1–38 Author chain PF； PDBConstruct 1–38； UniProt 1–38 Author chain QA； PDBConstruct 1–38； UniProt 1–38 Author chain QD； PDBConstruct 1–38； UniProt 1–38 Author chain R； PDBConstruct 1–38； UniProt 1–38 Author chain RB； PDBConstruct 1–38； UniProt 1–38 Author chain RE； PDBConstruct 1–38； UniProt 1–38 Author chain SC； PDBConstruct 1–38； UniProt 1–38 Author chain SF； PDBConstruct 1–38； UniProt 1–38 Author chain TA； PDBConstruct 1–38； UniProt 1–38 Author chain TD； PDBConstruct 1–38； UniProt 1–38 Author chain UB； PDBConstruct 1–38； UniProt 1–38 Author chain UE； PDBConstruct 1–38； UniProt 1–38 Author chain V； PDBConstruct 1–38； UniProt 1–38 Author chain VC； PDBConstruct 1–38； UniProt 1–38 Author chain VF； PDBConstruct 1–38； UniProt 1–38 Author chain WA； PDBConstruct 1–38； UniProt 1–38 Author chain WD； PDBConstruct 1–38； UniProt 1–38 Author chain XB； PDBConstruct 1–38； UniProt 1–38 Author chain XE； PDBConstruct 1–38； UniProt 1–38 Author chain Y； PDBConstruct 1–38； UniProt 1–38 Author chain YC； PDBConstruct 1–38； UniProt 1–38 Author chain YF； PDBConstruct 1–38； UniProt 1–38 Author chain ZA； PDBConstruct 1–38； UniProt 1–38 Author chain ZD； PDBConstruct 1–38； UniProt 1–38

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	9k3m
Deposition date deposition_date	2024-10-19
Structure title title	The structure of Microviridae PJNS001
Keywords keywords	structual proteins, VIRUS; VIRUS
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	— Å
Radius of gyration Rg (electron density) rg_electron	129.80 Å
Forward intensity I(0) i0	248974000000.00
Molecular weight molecular_weight	4280900.0 kDa
Excluded volume excluded_volume	5351200 Å³
Envelope volume envelope_volume	11745000 Å³
Hydration-shell volume shell_volume	756830 Å³
Envelope diameter envelope_diameter	353.3 Å
Shell Rg shell_rg	142.70 Å
Envelope Rg envelope_rg	112.70 Å
Shape Rg shape_rg	129.80 Å
Total Rg total_rg	129.90 Å
Total atoms total_atoms	302160
Residues n_residues	38280
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	322.4 Å
Rg (real space) rg_real	129.60 Å
Rg uncertainty (real space) rg_real_error	0.45 Å
I(0) (real space) i0_real	2.4180e+11
I(0) uncertainty (real space) i0_real_error	4.2510e+09
Rg (reciprocal space) rg_reciprocal	151.00 Å
I(0) (reciprocal space) i0_reciprocal	272600000000.0000
Solution quality estimate total_estimate	0.8938
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	214.9 Å
Skewness Skewness skewness	-0.369
Kurtosis Kurtosis kurtosis	-0.576
Angular range angular_range	— – 0.0600 Å⁻¹
Current regularization parameter α current_alpha	2.4090
Highest regularization parameter α highest_alpha	45880000000000.0000
Real-space data points n_real_points	13
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.953; Stabil: 0.956; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; 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	Capsid protein F
Molecular weight formula_weight	48500.5 kDa
Source method src_method	nat
Copy count entity_count	60

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;F,A,D,I,M,P,S,W,Z,CA,FA,IA,LA,OA,RA,UA,XA,AB,DB,GB,JB,MB,PB,SB,VB,YB,BC,EC,HC,KC,NC,QC,TC,WC,ZC,CD,FD,ID,LD,OD,RD,UD,XD,AE,DE,GE,JE,ME,PE,SE,VE,YE,BF,EF,HF,KF,NF,QF,TF,WF ;
Atom count atom_count	302160

MSNVQTGAERMPHDLSHLGFLAGQIGRLITISTTPVIAGDSFEMDAVGALRLSPLRRGLAIDSTVDIFTFYVPHRHVYGEQWIKFMKDGVNAAPLPTVNTTGYIDHAAFLGTINPDTNKIPKHLFQGYLNIYNNYFKAPWMPDRTEANPNQLNEDDARYGFRCCHLKNIWTAPLPPETELSRQMTTSTTSIDIMGLQAAYANLHTDQERDYFMQRYRDVISSFGGKTSYDADNRPLLVMRSNFWASGYDVDGTDQTSLGQFSGRVQQTYKHSVPRFFVPEHGTMFTLALVRFPPTATKEIQYLNAKGALTYTDIAGDPALYGNLPPREISMKDVFRSGDASKKFKIAEGQWYRYAPSYVSPAYHLLEGFPFIQEPPSGDLQERVLIRHHDYDQCFQSVQLLQWNSQVKFNVTVYRNLPTTRDSIMTS

Entity 2 Entity 2 polymer

Description description	Major spike protein G
Molecular weight formula_weight	19112.7 kDa
Source method src_method	nat
Copy count entity_count	60

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;G,B,E,K,N,Q,T,X,AA,DA,GA,JA,MA,PA,SA,VA,YA,BB,EB,HB,KB,NB,QB,TB,WB,ZB,CC,FC,IC,LC,OC,RC,UC,XC,AD,DD,GD,JD,MD,PD,SD,VD,YD,BE,EE,HE,KE,NE,QE,TE,WE,ZE,CF,FF,IF,LF,OF,RF,UF,XF ;

MFQTFISRHNSNFFSDKLVATSVTPASLAPVLQTPKAASSTLYFNQLTVNAGNGGFLHCIQMDTSVNAANQVVSVGADIAFDADPKFFACLVRFESASVPTTLPTDYDVYPLDGRHDGGYYTVKDCVTIDVLPREPGNNVYVGFMVWSNFTATKCRGLVSLNQVIKEIICLQPLK

Entity 3 Entity 3 polymer

Description description	DNA-binding protein J
Molecular weight formula_weight	4239.0 kDa
Source method src_method	nat
Copy count entity_count	60

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;J,C,H,L,O,R,V,Y,BA,EA,HA,KA,NA,QA,TA,WA,ZA,CB,FB,IB,LB,OB,RB,UB,XB,AC,DC,GC,JC,MC,PC,SC,VC,YC,BD,ED,HD,KD,ND,QD,TD,WD,ZD,CE,FE,IE,LE,OE,RE,UE,XE,AF,DF,GF,JF,MF,PF,SF,VF,YF ;

MSKGKKRSGARPGRPQPLRGTKGKRKGARLWYVGGQQF

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.68 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	16905

fit	/app/data/saxs_computation/k3/9k3m/9k3m.fit
pddf	/app/data/pr_computation/k3/9k3m/9k3m.pr.out
profile	/app/data/saxs_computation/k3/9k3m/9k3m.dat

The structure of Microviridae PJNS001

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

Capsid protein F

State in the Current Structure

Other States of the Same Protein in the Database

Major spike protein G

State in the Current Structure

Other States of the Same Protein in the Database

DNA-binding protein J

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)