8k37

Structure of the bacteriophage lambda neck

Method: ELECTRON MICROSCOPY Dmax: 134.3 Å Quality: REASONABLE

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

Tail tube protein

OrganismNot specified

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain G; UniProt 1–246 Chain H; UniProt 1–246 Chain I; UniProt 1–246 Chain J; UniProt 1–246 Chain K; UniProt 1–246 Chain L; UniProt 1–246 Not recorded Tail tube terminator protein × 6 (P03732) Head-tail connector protein FII × 6 (P03714) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 G; PDBConstruct 1–246; UniProt 1–246 Author chain H; 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

Tail tube terminator protein

OrganismNot specified

UniProt P03732

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–131 Chain B; UniProt 1–131 Chain C; UniProt 1–131 Chain D; UniProt 1–131 Chain E; UniProt 1–131 Chain F; UniProt 1–131 Not recorded Tail tube protein × 6 (P03733) Head-tail connector protein FII × 6 (P03714) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

7 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TTTP_LAMBD
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–131; UniProt 1–131 Author chain B; PDBConstruct 1–131; UniProt 1–131 Author chain C; PDBConstruct 1–131; UniProt 1–131 Author chain D; PDBConstruct 1–131; UniProt 1–131 Author chain E; PDBConstruct 1–131; UniProt 1–131 Author chain F; PDBConstruct 1–131; UniProt 1–131

Head-tail connector protein FII

OrganismNot specified

UniProt P03714

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain M; UniProt 1–117 Chain N; UniProt 1–117 Chain O; UniProt 1–117 Chain P; UniProt 1–117 Chain Q; UniProt 1–117 Chain R; UniProt 1–117 Not recorded Tail tube protein × 6 (P03733) Tail tube terminator protein × 6 (P03732) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FII_LAMBD
Isoform
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 1–117; UniProt 1–117 Author chain N; PDBConstruct 1–117; UniProt 1–117 Author chain O; PDBConstruct 1–117; UniProt 1–117 Author chain P; PDBConstruct 1–117; UniProt 1–117 Author chain Q; PDBConstruct 1–117; UniProt 1–117 Author chain R; PDBConstruct 1–117; UniProt 1–117

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 8k37

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k37
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k37
Deposition date deposition_date2023-07-14
Structure title titleStructure of the bacteriophage lambda neck
Keywords keywordsComplex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.50
Radius of gyration Rg (electron density) rg_electron44.46
Forward intensity I(0) i01081730000.00
Molecular weight molecular_weight262590.0 kDa
Excluded volume excluded_volume324510 ų
Envelope volume envelope_volume506830 ų
Hydration-shell volume shell_volume92336 ų
Envelope diameter envelope_diameter139.6
Shell Rg shell_rg52.20
Envelope Rg envelope_rg42.57
Shape Rg shape_rg44.47
Total Rg total_rg44.76
Total atoms total_atoms18528
Residues n_residues2394
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 dmax134.3
Rg (real space) rg_real45.14
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.0820e+09
I(0) uncertainty (real space) i0_real_error1.7540e+07
Rg (reciprocal space) rg_reciprocal45.49
I(0) (reciprocal space) i0_reciprocal1082000000.0000
Solution quality estimate total_estimate0.6374
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.4
Skewness Skewness skewness0.046
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha230400000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.959; Smooth: 0.536

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)