1noh

The structure of bacteriophage phi29 scaffolding protein gp7 after prohead assembly

Method: X-RAY DIFFRACTION Dmax: 96.8 Å Quality: GOOD

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

HEAD MORPHOGENESIS PROTEIN

Bacillus phage phi29

UniProt P13848

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–97 Chain B; UniProt 1–97 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;14.4 % Peg 8000, 0.08 M sodium cacodylate, 0.16 M calcium acetate, 20 % glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.80 Å R-free 0.290
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–97 Chain D; UniProt 1–97 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;14.4 % Peg 8000, 0.08 M sodium cacodylate, 0.16 M calcium acetate, 20 % glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.80 Å R-free 0.290
3 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–97 Chain B; UniProt 1–97 Chain C; UniProt 1–97 Chain D; UniProt 1–97 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;14.4 % Peg 8000, 0.08 M sodium cacodylate, 0.16 M calcium acetate, 20 % glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.80 Å R-free 0.290

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VG7_BPPH2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 1–97 Author chain B; PDBConstruct 1–97; UniProt 1–97 Author chain C; PDBConstruct 1–97; UniProt 1–97 Author chain D; PDBConstruct 1–97; UniProt 1–97

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 1noh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1noh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1noh
Deposition date deposition_date2003-01-16
Structure title titleThe structure of bacteriophage phi29 scaffolding protein gp7 after prohead assembly
Keywords keywordscoiled-coil, Viral protein; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.51
Radius of gyration Rg (electron density) rg_electron30.95
Forward intensity I(0) i018438300.00
Molecular weight molecular_weight33381.0 kDa
Excluded volume excluded_volume41778 ų
Envelope volume envelope_volume58309 ų
Hydration-shell volume shell_volume16840 ų
Envelope diameter envelope_diameter97.5
Shell Rg shell_rg35.87
Envelope Rg envelope_rg29.84
Shape Rg shape_rg30.93
Total Rg total_rg31.52
Total atoms total_atoms2356
Residues n_residues292
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 dmax96.8
Rg (real space) rg_real31.59
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.8440e+07
I(0) uncertainty (real space) i0_real_error2.5960e+05
Rg (reciprocal space) rg_reciprocal31.56
I(0) (reciprocal space) i0_reciprocal18440000.0000
Solution quality estimate total_estimate0.7826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.058
Kurtosis Kurtosis kurtosis-1.083
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha983400.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.559; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.582; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1noha_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.24 — Head morphogenesis protein gp7
Family Family familyh.1.24.1 — Head morphogenesis protein gp7
Domain ID domain_idd1nohb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.24 — Head morphogenesis protein gp7
Family Family familyh.1.24.1 — Head morphogenesis protein gp7
Domain ID domain_idd1nohc_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.24 — Head morphogenesis protein gp7
Family Family familyh.1.24.1 — Head morphogenesis protein gp7
Domain ID domain_idd1nohd_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.24 — Head morphogenesis protein gp7
Family Family familyh.1.24.1 — Head morphogenesis protein gp7

CATH v4.4 (4 domains)

Domain ID domain_id1nohA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily400
Domain ID domain_id1nohB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily400
Domain ID domain_id1nohC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily400
Domain ID domain_id1nohD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily400

8. Citations (1)

9. Files and Curves (10)