8iyk

Tail tip conformation 1 of phage lambda tail

Method: ELECTRON MICROSCOPY Dmax: 287.9 Å Quality: GOOD

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

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain A; UniProt 1–246 Chain B; UniProt 1–246 Chain C; UniProt 1–246 Chain D; UniProt 1–246 Chain G; UniProt 1–246 Chain Q; UniProt 1–246 Chain R; UniProt 1–246 Chain S; UniProt 1–246 Chain T; UniProt 1–246 Chain U; UniProt 1–246 Chain V; UniProt 1–246 Chain W; UniProt 1–246 Chain X; UniProt 1–246 Chain a; UniProt 1–246 Chain b; UniProt 1–246 Chain c; UniProt 1–246 Chain d; UniProt 1–246 Chain i; UniProt 1–246 Chain j; UniProt 1–246 Chain k; UniProt 1–246 Chain l; UniProt 1–246 Chain n; UniProt 1–246 Chain o; UniProt 1–246 Chain v; UniProt 1–246 Not recorded Tail tip protein M × 6 (P03737) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tape measure protein × 3 (P03736) Tail tip assembly protein I × 3 (P03730) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.95 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–246; UniProt 1–246 Author chain B; PDBConstruct 1–246; UniProt 1–246 Author chain C; PDBConstruct 1–246; UniProt 1–246 Author chain D; PDBConstruct 1–246; UniProt 1–246 Author chain G; PDBConstruct 1–246; UniProt 1–246 Author chain Q; PDBConstruct 1–246; UniProt 1–246 Author chain R; PDBConstruct 1–246; UniProt 1–246 Author chain S; PDBConstruct 1–246; UniProt 1–246 Author chain T; PDBConstruct 1–246; UniProt 1–246 Author chain U; PDBConstruct 1–246; UniProt 1–246 Author chain V; PDBConstruct 1–246; UniProt 1–246 Author chain W; PDBConstruct 1–246; UniProt 1–246 Author chain X; PDBConstruct 1–246; UniProt 1–246 Author chain a; PDBConstruct 1–246; UniProt 1–246 Author chain b; PDBConstruct 1–246; UniProt 1–246 Author chain c; PDBConstruct 1–246; UniProt 1–246 Author chain d; PDBConstruct 1–246; UniProt 1–246 Author chain i; PDBConstruct 1–246; UniProt 1–246 Author chain j; PDBConstruct 1–246; UniProt 1–246 Author chain k; PDBConstruct 1–246; UniProt 1–246 Author chain l; PDBConstruct 1–246; UniProt 1–246 Author chain n; PDBConstruct 1–246; UniProt 1–246 Author chain o; PDBConstruct 1–246; UniProt 1–246 Author chain v; PDBConstruct 1–246; UniProt 1–246

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain E; UniProt 1–109 Chain K; UniProt 1–109 Chain M; UniProt 1–109 Chain Y; UniProt 1–109 Chain e; UniProt 1–109 Chain m; UniProt 1–109 Not recorded Tail tube protein × 24 (P03733) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tape measure protein × 3 (P03736) Tail tip assembly protein I × 3 (P03730) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.95 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 2
Chains and sequence ranges Author chain E; PDBConstruct 1–109; UniProt 1–109 Author chain K; PDBConstruct 1–109; UniProt 1–109 Author chain M; PDBConstruct 1–109; UniProt 1–109 Author chain Y; PDBConstruct 1–109; UniProt 1–109 Author chain e; PDBConstruct 1–109; UniProt 1–109 Author chain m; PDBConstruct 1–109; UniProt 1–109

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain F; UniProt 1–1132 Chain J; UniProt 1–1132 Chain Z; UniProt 1–1132 Not recorded Tail tube protein × 24 (P03733) Tail tip protein M × 6 (P03737) Tail tip protein L × 3 (P03738) Tape measure protein × 3 (P03736) Tail tip assembly protein I × 3 (P03730) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.95 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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–1132; UniProt 1–1132 Author chain J; PDBConstruct 1–1132; UniProt 1–1132 Author chain Z; PDBConstruct 1–1132; UniProt 1–1132

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain L; UniProt 1–232 Chain N; UniProt 1–232 Chain f; UniProt 1–232 Not recorded Tail tube protein × 24 (P03733) Tail tip protein M × 6 (P03737) Tip attachment protein J × 3 (P03749) Tape measure protein × 3 (P03736) Tail tip assembly protein I × 3 (P03730) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.95 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 4
Chains and sequence ranges Author chain L; PDBConstruct 1–232; UniProt 1–232 Author chain N; PDBConstruct 1–232; UniProt 1–232 Author chain f; PDBConstruct 1–232; UniProt 1–232

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain H; UniProt 1–853 Chain O; UniProt 1–853 Chain g; UniProt 1–853 Not recorded Tail tube protein × 24 (P03733) Tail tip protein M × 6 (P03737) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tail tip assembly protein I × 3 (P03730) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.95 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 5
Chains and sequence ranges Author chain H; PDBConstruct 1–853; UniProt 1–853 Author chain O; PDBConstruct 1–853; UniProt 1–853 Author chain g; PDBConstruct 1–853; UniProt 1–853

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain I; UniProt 1–223 Chain P; UniProt 1–223 Chain h; UniProt 1–223 Not recorded Tail tube protein × 24 (P03733) Tail tip protein M × 6 (P03737) Tip attachment protein J × 3 (P03749) Tail tip protein L × 3 (P03738) Tape measure protein × 3 (P03736) SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.95 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 6
Chains and sequence ranges Author chain I; PDBConstruct 1–223; UniProt 1–223 Author chain P; PDBConstruct 1–223; UniProt 1–223 Author chain h; PDBConstruct 1–223; UniProt 1–223

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 8iyk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8iyk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8iyk
Deposition date deposition_date2023-04-05
Structure title titleTail tip conformation 1 of phage lambda tail
Keywords keywords;Bacteriophage, caudovirales, siphoviridae, tail complex, delivery device, macromolecular assembly, phage lambda, cryo-EM, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron105.90
Forward intensity I(0) i017298300000.00
Molecular weight molecular_weight1099800.0 kDa
Excluded volume excluded_volume1368200 ų
Envelope volume envelope_volume2328400 ų
Hydration-shell volume shell_volume206650 ų
Envelope diameter envelope_diameter443.4
Shell Rg shell_rg75.89
Envelope Rg envelope_rg105.60
Shape Rg shape_rg105.90
Total Rg total_rg105.60
Total atoms total_atoms77370
Residues n_residues10248
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 dmax287.9
Rg (real space) rg_real96.06
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real1.6520e+10
I(0) uncertainty (real space) i0_real_error3.5250e+08
Rg (reciprocal space) rg_reciprocal92.28
I(0) (reciprocal space) i0_reciprocal16730000000.0000
Solution quality estimate total_estimate0.8932
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.8
Skewness Skewness skewness0.475
Kurtosis Kurtosis kurtosis-0.635
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.8932
Highest regularization parameter α highest_alpha1368000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.893; Stabil: 0.976; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.005

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)