SAXSdb — 9lc0

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

60 kDa protein

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 × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain A； UniProt 1–556 Chain B； UniProt 1–556 Chain C； UniProt 1–556 Chain D； UniProt 1–556 Chain E； UniProt 1–556 Chain F； UniProt 1–556 Chain G； UniProt 1–556 Chain L； UniProt 1–556 Chain Q； UniProt 1–556 Chain V； UniProt 1–556 Chain a； UniProt 1–556 Chain f； UniProt 1–556	Not recorded	Gp64 × 6 （A0MZE6） Non-contractile tail sheath × 6 （A0MZE7） 30 kDa protein × 12 （A0MZE9） Gp54 × 12 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
2	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 1–556 Chain B； UniProt 1–556 Chain C； UniProt 1–556 Chain D； UniProt 1–556 Chain E； UniProt 1–556 Chain F； UniProt 1–556 Chain G； UniProt 1–556 Chain L； UniProt 1–556 Chain Q； UniProt 1–556 Chain V； UniProt 1–556 Chain a； UniProt 1–556 Chain f； UniProt 1–556	Not recorded	Gp64 × 2 （A0MZE6） Non-contractile tail sheath × 2 （A0MZE7） 30 kDa protein × 4 （A0MZE9） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
3	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 1–556 Chain B； UniProt 1–556 Chain C； UniProt 1–556 Chain D； UniProt 1–556 Chain E； UniProt 1–556 Chain F； UniProt 1–556 Chain G； UniProt 1–556 Chain L； UniProt 1–556 Chain Q； UniProt 1–556 Chain V； UniProt 1–556 Chain a； UniProt 1–556 Chain f； UniProt 1–556	Not recorded	Gp64 × 2 （A0MZE6） Non-contractile tail sheath × 2 （A0MZE7） 30 kDa protein × 4 （A0MZE9） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 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 9LC0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YF4 N4 Full Virion C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain XA 1–556（556 aa） Chain XB 1–556（556 aa） Chain XC 1–556（556 aa） Chain XD 1–556（556 aa） Chain XE 1–556（556 aa） Chain XF 1–556（556 aa） Chain XG 1–556（556 aa） Chain XH 1–556（556 aa） Chain XI 1–556（556 aa） Chain XJ 1–556（556 aa） Chain XK 1–556（556 aa） Chain XL 1–556（556 aa） Chain YA 1–556（556 aa） Chain YB 1–556（556 aa） Chain YC 1–556（556 aa） Chain YD 1–556（556 aa） Chain YE 1–556（556 aa） Chain YF 1–556（556 aa） Chain YG 1–556（556 aa） Chain YH 1–556（556 aa） Chain YI 1–556（556 aa） Chain YJ 1–556（556 aa） Chain YK 1–556（556 aa） Chain YL 1–556（556 aa） Chain ZA 1–556（556 aa） Chain ZB 1–556（556 aa） Chain ZC 1–556（556 aa） Chain ZD 1–556（556 aa） Chain ZE 1–556（556 aa） Chain ZF 1–556（556 aa） Chain ZG 1–556（556 aa） Chain ZH 1–556（556 aa） Chain ZI 1–556（556 aa） Chain ZJ 1–556（556 aa） Chain ZK 1–556（556 aa） Chain ZL 1–556（556 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.28 Å
9YF5 N4 Empty Particle C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 84 PDB declaration: 84-meric	Chain XA 1–556（556 aa） Chain XB 1–556（556 aa） Chain XC 1–556（556 aa） Chain XD 1–556（556 aa） Chain XE 1–556（556 aa） Chain XF 1–556（556 aa） Chain XG 1–556（556 aa） Chain XH 1–556（556 aa） Chain XI 1–556（556 aa） Chain XJ 1–556（556 aa） Chain XK 1–556（556 aa） Chain XL 1–556（556 aa） Chain YA 1–556（556 aa） Chain YB 1–556（556 aa） Chain YC 1–556（556 aa） Chain YD 1–556（556 aa） Chain YE 1–556（556 aa） Chain YF 1–556（556 aa） Chain YG 1–556（556 aa） Chain YH 1–556（556 aa） Chain YI 1–556（556 aa） Chain YJ 1–556（556 aa） Chain YK 1–556（556 aa） Chain YL 1–556（556 aa） Chain ZA 1–556（556 aa） Chain ZB 1–556（556 aa） Chain ZC 1–556（556 aa） Chain ZD 1–556（556 aa） Chain ZE 1–556（556 aa） Chain ZF 1–556（556 aa） Chain ZG 1–556（556 aa） Chain ZH 1–556（556 aa） Chain ZI 1–556（556 aa） Chain ZJ 1–556（556 aa） Chain ZK 1–556（556 aa） Chain ZL 1–556（556 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

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

View Construct and Data Evidence

UniProt name	A0MZE8_BPN4
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–556； UniProt 1–556 Author chain B； PDBConstruct 1–556； UniProt 1–556 Author chain C； PDBConstruct 1–556； UniProt 1–556 Author chain D； PDBConstruct 1–556； UniProt 1–556 Author chain E； PDBConstruct 1–556； UniProt 1–556 Author chain F； PDBConstruct 1–556； UniProt 1–556 Author chain G； PDBConstruct 1–556； UniProt 1–556 Author chain L； PDBConstruct 1–556； UniProt 1–556 Author chain Q； PDBConstruct 1–556； UniProt 1–556 Author chain V； PDBConstruct 1–556； UniProt 1–556 Author chain a； PDBConstruct 1–556； UniProt 1–556 Author chain f； PDBConstruct 1–556； UniProt 1–556

Gp64

OrganismNot specified

UniProt A0MZE6

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 × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain M； UniProt 1–417 Chain R； UniProt 1–417	Not recorded	60 kDa protein × 36 （A0MZE8） Non-contractile tail sheath × 6 （A0MZE7） 30 kDa protein × 12 （A0MZE9） Gp54 × 12 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
2	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain M； UniProt 1–417 Chain R； UniProt 1–417	Not recorded	60 kDa protein × 12 （A0MZE8） Non-contractile tail sheath × 2 （A0MZE7） 30 kDa protein × 4 （A0MZE9） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
3	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain M； UniProt 1–417 Chain R； UniProt 1–417	Not recorded	60 kDa protein × 12 （A0MZE8） Non-contractile tail sheath × 2 （A0MZE7） 30 kDa protein × 4 （A0MZE9） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 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 9LC0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YF4 N4 Full Virion C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain SA 1–417（417 aa） Chain SB 1–417（417 aa） Chain SC 1–417（417 aa） Chain SD 1–417（417 aa） Chain SE 1–417（417 aa） Chain SF 1–417（417 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.28 Å
9YF5 N4 Empty Particle C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 84 PDB declaration: 84-meric	Chain SA 1–417（417 aa） Chain SB 1–417（417 aa） Chain SC 1–417（417 aa） Chain SD 1–417（417 aa） Chain SE 1–417（417 aa） Chain SF 1–417（417 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

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

View Construct and Data Evidence

UniProt name	A0MZE6_BPN4
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain M； PDBConstruct 1–417； UniProt 1–417 Author chain R； PDBConstruct 1–417； UniProt 1–417

Non-contractile tail sheath

OrganismNot specified

UniProt A0MZE7

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 × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain I； UniProt 1–1382 Chain N； UniProt 1–1382	Not recorded	60 kDa protein × 36 （A0MZE8） Gp64 × 6 （A0MZE6） 30 kDa protein × 12 （A0MZE9） Gp54 × 12 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
2	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain I； UniProt 1–1382 Chain N； UniProt 1–1382	Not recorded	60 kDa protein × 12 （A0MZE8） Gp64 × 2 （A0MZE6） 30 kDa protein × 4 （A0MZE9） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
3	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain I； UniProt 1–1382 Chain N； UniProt 1–1382	Not recorded	60 kDa protein × 12 （A0MZE8） Gp64 × 2 （A0MZE6） 30 kDa protein × 4 （A0MZE9） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 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 9LC0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YF4 N4 Full Virion C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain LA 1–1382（1382 aa） Chain LB 1–1382（1382 aa） Chain LC 1–1382（1382 aa） Chain LD 1–1382（1382 aa） Chain LE 1–1382（1382 aa） Chain LF 1–1382（1382 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.28 Å
9YF5 N4 Empty Particle C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 84 PDB declaration: 84-meric	Chain LA 1–1382（1382 aa） Chain LB 1–1382（1382 aa） Chain LC 1–1382（1382 aa） Chain LD 1–1382（1382 aa） Chain LE 1–1382（1382 aa） Chain LF 1–1382（1382 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9YFT N4 Bacteriophage Asymmetric Tail Gating Complex Deposited 2025-09-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain LA 1–1382（1382 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.61 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NCTSP_BPN4
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain I； PDBConstruct 1–1382； UniProt 1–1382 Author chain N； PDBConstruct 1–1382； UniProt 1–1382

30 kDa protein

OrganismNot specified

UniProt A0MZE9

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 × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain H； UniProt 1–236 Chain J； UniProt 1–236 Chain O； UniProt 1–236 Chain S； UniProt 1–236	Not recorded	60 kDa protein × 36 （A0MZE8） Gp64 × 6 （A0MZE6） Non-contractile tail sheath × 6 （A0MZE7） Gp54 × 12 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
2	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain H； UniProt 1–236 Chain J； UniProt 1–236 Chain O； UniProt 1–236 Chain S； UniProt 1–236	Not recorded	60 kDa protein × 12 （A0MZE8） Gp64 × 2 （A0MZE6） Non-contractile tail sheath × 2 （A0MZE7） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
3	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain H； UniProt 1–236 Chain J； UniProt 1–236 Chain O； UniProt 1–236 Chain S； UniProt 1–236	Not recorded	60 kDa protein × 12 （A0MZE8） Gp64 × 2 （A0MZE6） Non-contractile tail sheath × 2 （A0MZE7） Gp54 × 4 （Q859Q3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 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 9LC0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YF4 N4 Full Virion C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain AA 1–236（236 aa） Chain AB 1–236（236 aa） Chain AC 1–236（236 aa） Chain AD 1–236（236 aa） Chain AE 1–236（236 aa） Chain AF 1–236（236 aa） Chain AG 1–236（236 aa） Chain AH 1–236（236 aa） Chain AI 1–236（236 aa） Chain AJ 1–236（236 aa） Chain AK 1–236（236 aa） Chain AL 1–236（236 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.28 Å
9YF5 N4 Empty Particle C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 84 PDB declaration: 84-meric	Chain AA 1–236（236 aa） Chain AB 1–236（236 aa） Chain AC 1–236（236 aa） Chain AD 1–236（236 aa） Chain AE 1–236（236 aa） Chain AF 1–236（236 aa） Chain AG 1–236（236 aa） Chain AH 1–236（236 aa） Chain AI 1–236（236 aa） Chain AJ 1–236（236 aa） Chain AK 1–236（236 aa） Chain AL 1–236（236 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

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

View Construct and Data Evidence

UniProt name	A0MZE9_BPN4
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain H； PDBConstruct 1–236； UniProt 1–236 Author chain J； PDBConstruct 1–236； UniProt 1–236 Author chain O； PDBConstruct 1–236； UniProt 1–236 Author chain S； PDBConstruct 1–236； UniProt 1–236

Gp54

OrganismNot specified

UniProt Q859Q3

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 × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain K； UniProt 1–299 Chain P； UniProt 1–299 Chain T； UniProt 1–299 Chain U； UniProt 1–299	Not recorded	60 kDa protein × 36 （A0MZE8） Gp64 × 6 （A0MZE6） Non-contractile tail sheath × 6 （A0MZE7） 30 kDa protein × 12 （A0MZE9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
2	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain K； UniProt 1–299 Chain P； UniProt 1–299 Chain T； UniProt 1–299 Chain U； UniProt 1–299	Not recorded	60 kDa protein × 12 （A0MZE8） Gp64 × 2 （A0MZE6） Non-contractile tail sheath × 2 （A0MZE7） 30 kDa protein × 4 （A0MZE9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 Å
3	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain K； UniProt 1–299 Chain P； UniProt 1–299 Chain T； UniProt 1–299 Chain U； UniProt 1–299	Not recorded	60 kDa protein × 12 （A0MZE8） Gp64 × 2 （A0MZE6） Non-contractile tail sheath × 2 （A0MZE7） 30 kDa protein × 4 （A0MZE9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.20 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 9LC0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YF4 N4 Full Virion C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 96 PDB declaration: 96-meric	Chain TA 1–299（299 aa） Chain TB 1–299（299 aa） Chain TC 1–299（299 aa） Chain TD 1–299（299 aa） Chain TE 1–299（299 aa） Chain TF 1–299（299 aa） Chain TG 1–299（299 aa） Chain TH 1–299（299 aa） Chain TI 1–299（299 aa） Chain TJ 1–299（299 aa） Chain TK 1–299（299 aa） Chain TL 1–299（299 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.28 Å
9YF5 N4 Empty Particle C6 Tail Deposited 2025-09-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 84 PDB declaration: 84-meric	Chain TA 1–299（299 aa） Chain TB 1–299（299 aa） Chain TC 1–299（299 aa） Chain TD 1–299（299 aa） Chain TE 1–299（299 aa） Chain TF 1–299（299 aa） Chain TG 1–299（299 aa） Chain TH 1–299（299 aa） Chain TI 1–299（299 aa） Chain TJ 1–299（299 aa） Chain TK 1–299（299 aa） Chain TL 1–299（299 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9YFT N4 Bacteriophage Asymmetric Tail Gating Complex Deposited 2025-09-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain TA 1–299（299 aa） Chain TB 1–299（299 aa） Chain TC 1–299（299 aa） Chain TD 1–299（299 aa） Chain TE 1–299（299 aa） Chain TF 1–299（299 aa） Chain TG 1–299（299 aa） Chain TH 1–299（299 aa） Chain TI 1–299（299 aa） Chain TJ 1–299（299 aa） Chain TK 1–299（299 aa） Chain TL 1–299（299 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.61 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q859Q3_BPN4
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain K； PDBConstruct 1–299； UniProt 1–299 Author chain P； PDBConstruct 1–299； UniProt 1–299 Author chain T； PDBConstruct 1–299； UniProt 1–299 Author chain U； PDBConstruct 1–299； UniProt 1–299

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	9lc0
Deposition date deposition_date	2025-01-03
Structure title title	tail complex of mature phage N4
Keywords keywords	Complex, VIRAL PROTEIN; VIRAL PROTEIN
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	97.44 Å
Radius of gyration Rg (electron density) rg_electron	99.64 Å
Forward intensity I(0) i0	7418240000.00
Molecular weight molecular_weight	734680.0 kDa
Excluded volume excluded_volume	919820 Å³
Envelope volume envelope_volume	1817900 Å³
Hydration-shell volume shell_volume	169180 Å³
Envelope diameter envelope_diameter	379.0 Å
Shell Rg shell_rg	74.05 Å
Envelope Rg envelope_rg	99.56 Å
Shape Rg shape_rg	99.61 Å
Total Rg total_rg	99.46 Å
Total atoms total_atoms	51753
Residues n_residues	6537
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	273.2 Å
Rg (real space) rg_real	91.49 Å
Rg uncertainty (real space) rg_real_error	1.49 Å
I(0) (real space) i0_real	7.1030e+09
I(0) uncertainty (real space) i0_real_error	1.5620e+08
Rg (reciprocal space) rg_reciprocal	89.36 Å
I(0) (reciprocal space) i0_reciprocal	7228000000.0000
Solution quality estimate total_estimate	0.9011
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	85.4 Å
Skewness Skewness skewness	0.511
Kurtosis Kurtosis kurtosis	-0.507
Angular range angular_range	— – 0.0800 Å⁻¹
Current regularization parameter α current_alpha	0.6322
Highest regularization parameter α highest_alpha	561800000.0000
Real-space data points n_real_points	17
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.011; Oscil: 0.910; Stabil: 0.984; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.037

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	60 kDa protein
Molecular weight formula_weight	58943.9 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,L,Q,V,a,f
Atom count atom_count	51753

MSGHTPFNTIPNEGYCCETLNDPIVDKMIGNAYYVVKFVALRMPFIKNVSDNMTQLLAIHNKLTELSAIYTKLDELQLIHNNLDKLQELYNQLSKLTGLYDNLQALLRVYDNLTPINTVASNIDAVNTVATDIAKVIIVSAQIDKVITVANSITNVNTVAGSIDAVNTVSTNINAIKNVNTNMAALLDLDNHMTELLAVHARLGDLVTIAEQLDTIIADHEKYATAEGAGLIGFNQAQTYAANTVGAMLRQVITMGNDKGGYAVAGKLTSARGVWSLATGSINMNAPTAGAVANLVLNYKAGKVSGLLVAPSQQMALDGLIMGASTADNTATVSVTAPLRFKADLTAKTISGVNTRIMPSSAVTLNVDAYGGITLGYPPSLQTVEPVMTFITPTGKAPLTPRFSSVTAGAAVLVMVGEAEAQLKYSGGGWAAVSDWDSGTYCAFDTVSGELTVYHSTLIKDSTVTFSLLLPTDDTQLTAQLKSHTDSSFVVKIAKPDGSLLDAPLEGMGIMYSRGMHGIYKVPYGSLIVDVGRVQVKFSEFNTTEGISVVGINSNA

Entity 2 Entity 2 polymer

Description description	Gp64
Molecular weight formula_weight	48100.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M,R

MSNAAVVPMPYSPTTVPREQIREIQLQLINEMTDVHMGALTAQYMPDDFTFEPGIGQIHFNVETSRKVCLDLAKSVLRLVPVYPLVSPVKKQHDDYWFVGRLGLDPVSEPEPINMPTMEFYKRFLSLLHERDMKFVNSVAYEILNFFMPDEWKQLNWKGDPALSGWYPPSSFIQPTNKDALDFVSKAQCQILKECQNLGMELYFQIGEPWWWDGSYNTGEGKNAPCIYDPKTMALYKEETGNDVPTPWIKDIFAPVEEHQWPYVDWLCTKLGQSTNYIRDYVKGKFPDAQATLLFFTPQIMSPASELTGRLNFPESEWIFPNYDFVQIEDYDWIIDGRLDLVPLTFDAAVNRLGYPLNVVHYFIGFVLLPEDAKKIWADVDKAWGLALEAGIPHIYPWSYTQVMRDGVIYAVPKVCG

Entity 3 Entity 3 polymer

Description description	Non-contractile tail sheath
Molecular weight formula_weight	154255.1 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,N

MSIEDYLKGKNCLASPNYDPDDQHSSWREDLPQFKKDREHLTLVNTRRNRTYNTKLNRFDPEYWVVDYNALMVATIIPYGSKSFKVPCQWRTNKDFLGVRWMTEDTFDHHLYRYETDPNYLGLILAFRHNPDEPDKFTVTIQTPEKAYTYRLAPYGFNNKTRRWECLDTKYGTKRTYQADIFVATDEDIPESEMTEVYGTKDYIFILDFADLRTGVAFNGVTINPRNITMISFDCTEAHHGLGKDAYIAAMYNNDDGATFQMEIGGIHTNAALAAGDKLQCIWRYLDVNGNAQAAENEFEVVSYEGFGTSNFSVKCKGMLPGKFIGCDAFYGKYLQTDGPIKQVDSVKWFTNLTVSGSGRKQLGQRKYPQVVMGMGMTSGFDDGYNLTPERQVKMAYGLGYRDWWTTYIGMSHYWKGLTAFQDKETGELITEQTVLDYPILFAGESQVAIHFMSGAYPDRGYDVFQKYMTETWGINYAGVHPINGTTGSTAVDRACAVNPNSEVFDPTQSSGAGGLWWWDLEADKPGPALLHCVGQVGKLKPKAIIWGQGDQDATALAYPGDRNPAPSLTRTKQATKKVFEYLRSLYGQIPIFIQELSYAWGITNTDAPNVPIRTGLPSFLAARRNTWGDIEFRWKSYGLDPALAQYRIEIYNPSNLNQILHSFVVSGTQEANGYVYADFTVEDWIPVMMEAVGSPNPWEFMKWRVVCLYQEREIPSAPWSDNIPLDNAGLVKKTILVGINQFGGGHFTDMSDPTATTANGAIGRKDKVSASTLRLTFAEKAGLRPIQVMPVNVAADSAGMTVGTHKWWNTSSNSPGDALLAINDMVKGLGVKPDYFIEANPWETMYMKDVNSSTWPALMTAFESSNKAMLAWMRTNWGNPNLEIWFQGATTVWFGVAPPNDLNSEATVTVRDKQIQMATANIGFKLGSFVPGSNLYTAYRNVESSWIYYTVEAFHATAIELGEALALNINRATNPPDWSYLRPPANLQGRKLATRDIKMTWDNRAGITHWKYANRHVTTGAEISSGILTSPEYVFTLNDQQNAYNGDTLNMSFSVSEYAADSGAVGASSSFVGVVQNGSYMQTPTQLKAAKQLNGDIIFTWVGRPSWQHFWVVNTSVNDSKTVIFSKEWSSESLTWTVAEQNEFYGLEEGGATHVIFMVSEYDPSNGLVSIGAQVTGQAEQPSNPMNPVAGLYAVFTGDPGNSNIKIMWDKPSVGGRDVRIRNMHVTSSATISDQFVSDNNLVFTREEQVAAYGFTASSVSVRAQEHDIESGALGLTTEYVAVPETAGTVGQGFAKKDSVGNCTMSWEVGDAVQWQVEILNAENSTVVKTEIVVAPTITWMAEEITAEYGYLTDHMVWRVRPYRADGASNVAKQFDMTATL

Entity 4 Entity 4 polymer

Description description	30 kDa protein
Molecular weight formula_weight	27192.4 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,O,S,H

MYYIEELFCRLANGVLNNTGIVTDDRGDIEDDSKPFIIVAANEALTRLHGRFNMRNNNVVVEMQEGRTNYPLLAKYAVQSYDPNEVKCPFIMDLAGEKFAEDVIRILEVYDDKGRRRPLNDRNNPCSLFTPRPNVLQNNAPKAWEVLNVMYQAKHPKLSTAEDGYNEIDIPDTLDPALDAYIAYRYYTSLNTPESSAKAAEYLSFYDSICREVVEYDLTSDTEVDTNTLFRKRGWR

Entity 5 Entity 5 polymer

Description description	Gp54
Molecular weight formula_weight	32438.4 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K,P,T,U

MSCGAELEANALLTALVAGEDFTLPDIDMSGSEYDIPGGINSPIYAEIEKITTEQLTTREVGGSGVFDALMQSASNHLLAEFKNNRITGGDYVKAYIATMEACMANAVQFLTTKDQAYWNAVTAQVAAITARANLGIIKANFVTAKIQALATKAEYALTKLKLSNESVTYCTAQYNLSSMLPQQLLMLKNQTTQVAEQTKLTTEQINMTKEQKEAQRAQTSDTRTDGTRVAGSVGKQKELYDQQITSYKRDAEVKAAKLFTDAWVTQKTIDEGLSPPNGFTNSSLDSILTALKNNNALG

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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	3.200 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.20 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	47179

fit	/app/data/saxs_computation/lc/9lc0/9lc0.fit
pddf	/app/data/pr_computation/lc/9lc0/9lc0.pr.out
profile	/app/data/saxs_computation/lc/9lc0/9lc0.dat

tail complex of mature phage N4

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

60 kDa protein

State in the Current Structure

Other States of the Same Protein in the Database

Gp64

State in the Current Structure

Other States of the Same Protein in the Database

Non-contractile tail sheath

State in the Current Structure

Other States of the Same Protein in the Database

30 kDa protein

State in the Current Structure

Other States of the Same Protein in the Database

Gp54

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)