9e7m

In situ cryoEM structure of bacteriophage Ur-lambda tail tip complex

Method: ELECTRON MICROSCOPY Dmax: 231.0 Å Quality: GOOD

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

Tape measure protein

Escherichia phage Lambda

UniProt P03736

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain Ha; UniProt 818–849 Chain Hb; UniProt 818–849 Chain Hc; UniProt 818–849 Not recorded Tail tip assembly protein I × 2 (P03730) Tail tip assembly protein I × 1 (P03730) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tail fiber protein × 12 (P03764) Tail tip protein M × 6 (P03737) Tail tube protein × 6 (P03733) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

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

View Construct and Data Evidence
UniProt name TMP_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain Ha; PDBConstruct 1–32; UniProt 818–849 Author chain Hb; PDBConstruct 1–32; UniProt 818–849 Author chain Hc; PDBConstruct 1–32; UniProt 818–849

Tail tip assembly protein I

Escherichia phage Lambda

UniProt P03730

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain Ia; UniProt 133–222 Chain Ib; UniProt 133–222 Chain Ic; UniProt 133–222 Not recorded Tape measure protein × 3 (P03736) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tail fiber protein × 12 (P03764) Tail tip protein M × 6 (P03737) Tail tube protein × 6 (P03733) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

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

View Construct and Data Evidence
UniProt name TIPI_LAMBD
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain Ia; PDBConstruct 1–90; UniProt 133–222 Author chain Ib; PDBConstruct 1–90; UniProt 133–222 Author chain Ic; PDBConstruct 1–90; UniProt 133–222

Tip attachment protein J

Escherichia phage Lambda

UniProt P03749

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain Ja; UniProt 1–835 Chain Jb; UniProt 1–835 Chain Jc; UniProt 1–835 Not recorded Tape measure protein × 3 (P03736) Tail tip assembly protein I × 2 (P03730) Tail tip assembly protein I × 1 (P03730) Tail tip protein L × 3 (P03738) Tail fiber protein × 12 (P03764) Tail tip protein M × 6 (P03737) Tail tube protein × 6 (P03733) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIPJ_LAMBD
Isoform
PDB entities 4
Chains and sequence ranges Author chain Ja; PDBConstruct 1–835; UniProt 1–835 Author chain Jb; PDBConstruct 1–835; UniProt 1–835 Author chain Jc; PDBConstruct 1–835; UniProt 1–835

Tail tip protein L

Escherichia phage Lambda

UniProt P03738

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain La; UniProt 1–232 Chain Lb; UniProt 1–232 Chain Lc; UniProt 1–232 Not recorded Tape measure protein × 3 (P03736) Tail tip assembly protein I × 2 (P03730) Tail tip assembly protein I × 1 (P03730) Tip attachment protein J × 3 (P03749) Tail fiber protein × 12 (P03764) Tail tip protein M × 6 (P03737) Tail tube protein × 6 (P03733) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

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

View Construct and Data Evidence
UniProt name TIPL_LAMBD
Isoform
PDB entities 5
Chains and sequence ranges Author chain La; PDBConstruct 1–232; UniProt 1–232 Author chain Lb; PDBConstruct 1–232; UniProt 1–232 Author chain Lc; PDBConstruct 1–232; UniProt 1–232

Tail fiber protein

Escherichia phage Lambda

UniProt P03764

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain Ta; UniProt 1–94 Chain Tb; UniProt 1–94 Chain Tc; UniProt 1–94 Chain Td; UniProt 1–94 Chain Te; UniProt 1–94 Chain Tf; UniProt 1–94 Chain Tg; UniProt 1–94 Chain Th; UniProt 1–94 Chain Ti; UniProt 1–94 Chain Tj; UniProt 1–94 Chain Tk; UniProt 1–94 Chain Tl; UniProt 1–94 Not recorded Tape measure protein × 3 (P03736) Tail tip assembly protein I × 2 (P03730) Tail tip assembly protein I × 1 (P03730) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tail tip protein M × 6 (P03737) Tail tube protein × 6 (P03733) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBER_LAMBD
Isoform
PDB entities 6
Chains and sequence ranges Author chain Ta; PDBConstruct 1–94; UniProt 1–94 Author chain Tb; PDBConstruct 1–94; UniProt 1–94 Author chain Tc; PDBConstruct 1–94; UniProt 1–94 Author chain Td; PDBConstruct 1–94; UniProt 1–94 Author chain Te; PDBConstruct 1–94; UniProt 1–94 Author chain Tf; PDBConstruct 1–94; UniProt 1–94 Author chain Tg; PDBConstruct 1–94; UniProt 1–94 Author chain Th; PDBConstruct 1–94; UniProt 1–94 Author chain Ti; PDBConstruct 1–94; UniProt 1–94 Author chain Tj; PDBConstruct 1–94; UniProt 1–94 Author chain Tk; PDBConstruct 1–94; UniProt 1–94 Author chain Tl; PDBConstruct 1–94; UniProt 1–94

Tail tip protein M

Escherichia phage Lambda

UniProt P03737

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain Ma; UniProt 1–109 Chain Mb; UniProt 1–109 Chain Mc; UniProt 1–109 Chain Md; UniProt 1–109 Chain Me; UniProt 1–109 Chain Mf; UniProt 1–109 Not recorded Tape measure protein × 3 (P03736) Tail tip assembly protein I × 2 (P03730) Tail tip assembly protein I × 1 (P03730) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tail fiber protein × 12 (P03764) Tail tube protein × 6 (P03733) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

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

View Construct and Data Evidence
UniProt name TIPM_LAMBD
Isoform
PDB entities 7
Chains and sequence ranges Author chain Ma; PDBConstruct 1–109; UniProt 1–109 Author chain Mb; PDBConstruct 1–109; UniProt 1–109 Author chain Mc; PDBConstruct 1–109; UniProt 1–109 Author chain Md; PDBConstruct 1–109; UniProt 1–109 Author chain Me; PDBConstruct 1–109; UniProt 1–109 Author chain Mf; PDBConstruct 1–109; UniProt 1–109

Tail tube protein

Escherichia phage Lambda

UniProt P03733

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain Va; UniProt 3–157 Chain Vb; UniProt 3–157 Chain Vc; UniProt 3–157 Chain Vd; UniProt 3–157 Chain Ve; UniProt 3–157 Chain Vf; UniProt 3–157 Not recorded Tape measure protein × 3 (P03736) Tail tip assembly protein I × 2 (P03730) Tail tip assembly protein I × 1 (P03730) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tail fiber protein × 12 (P03764) Tail tip protein M × 6 (P03737) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

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

View Construct and Data Evidence
UniProt name TUBE_LAMBD
Isoform
PDB entities 8
Chains and sequence ranges Author chain Va; PDBConstruct 1–152; UniProt 3–157 Author chain Vb; PDBConstruct 1–152; UniProt 3–157 Author chain Vc; PDBConstruct 1–152; UniProt 3–157 Author chain Vd; PDBConstruct 1–152; UniProt 3–157 Author chain Ve; PDBConstruct 1–152; UniProt 3–157 Author chain Vf; PDBConstruct 1–152; UniProt 3–157

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9e7m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e7m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e7m
Deposition date deposition_date2024-11-03
Structure title titleIn situ cryoEM structure of bacteriophage Ur-lambda tail tip complex
Keywords keywordsbacteriophage, tail tip complex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.64
Radius of gyration Rg (electron density) rg_electron69.55
Forward intensity I(0) i06924270000.00
Molecular weight molecular_weight686500.0 kDa
Excluded volume excluded_volume851970 ų
Envelope volume envelope_volume1322900 ų
Hydration-shell volume shell_volume162410 ų
Envelope diameter envelope_diameter269.2
Shell Rg shell_rg66.91
Envelope Rg envelope_rg69.01
Shape Rg shape_rg69.58
Total Rg total_rg69.38
Total atoms total_atoms48257
Residues n_residues6260
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax231.0
Rg (real space) rg_real68.61
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real6.9100e+09
I(0) uncertainty (real space) i0_real_error1.5070e+08
Rg (reciprocal space) rg_reciprocal67.55
I(0) (reciprocal space) i0_reciprocal6906000000.0000
Solution quality estimate total_estimate0.8215
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.3
Skewness Skewness skewness0.639
Kurtosis Kurtosis kurtosis0.117
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0306
Highest regularization parameter α highest_alpha842800000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.740; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.453

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)